data_8QG4
# 
_entry.id   8QG4 
# 
_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   8QG4         pdb_00008qg4 10.2210/pdb8qg4/pdb 
WWPDB D_1292132967 ?            ?                   
# 
_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                        8QG4 
_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-(3-azanylpropyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
696.717   1   ?        ? ? ? 
4 non-polymer syn GLYCEROL 92.094    1   ?        ? ? ? 
5 water       nat water 18.015    138 ?        ? ? ? 
# 
_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-(3-azanylpropyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
UZ6 
4 GLYCEROL GOL 
5 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  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
UZ6 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-(3-azanylpropyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
?                               'C29 H40 N14 O7' 696.717 
VAL 'L-peptide linking' y VALINE ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ILE 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 LYS 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 LEU 265 265 ?   ?   ?   A . n 
A 1 266 GLU 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 HIS 269 269 ?   ?   ?   A . n 
A 1 270 HIS 270 270 ?   ?   ?   A . n 
A 1 271 HIS 271 271 ?   ?   ?   A . n 
A 1 272 HIS 272 272 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        UZ6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UZ6 
_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 UZ6 1   302 1   UZ6 XXX A . 
D 4 GOL 1   303 266 GOL GOL A . 
E 5 HOH 1   401 103 HOH HOH A . 
E 5 HOH 2   402 87  HOH HOH A . 
E 5 HOH 3   403 81  HOH HOH A . 
E 5 HOH 4   404 8   HOH HOH A . 
E 5 HOH 5   405 49  HOH HOH A . 
E 5 HOH 6   406 5   HOH HOH A . 
E 5 HOH 7   407 59  HOH HOH A . 
E 5 HOH 8   408 42  HOH HOH A . 
E 5 HOH 9   409 72  HOH HOH A . 
E 5 HOH 10  410 20  HOH HOH A . 
E 5 HOH 11  411 66  HOH HOH A . 
E 5 HOH 12  412 19  HOH HOH A . 
E 5 HOH 13  413 114 HOH HOH A . 
E 5 HOH 14  414 36  HOH HOH A . 
E 5 HOH 15  415 106 HOH HOH A . 
E 5 HOH 16  416 95  HOH HOH A . 
E 5 HOH 17  417 93  HOH HOH A . 
E 5 HOH 18  418 94  HOH HOH A . 
E 5 HOH 19  419 15  HOH HOH A . 
E 5 HOH 20  420 130 HOH HOH A . 
E 5 HOH 21  421 18  HOH HOH A . 
E 5 HOH 22  422 31  HOH HOH A . 
E 5 HOH 23  423 13  HOH HOH A . 
E 5 HOH 24  424 24  HOH HOH A . 
E 5 HOH 25  425 4   HOH HOH A . 
E 5 HOH 26  426 112 HOH HOH A . 
E 5 HOH 27  427 56  HOH HOH A . 
E 5 HOH 28  428 63  HOH HOH A . 
E 5 HOH 29  429 2   HOH HOH A . 
E 5 HOH 30  430 1   HOH HOH A . 
E 5 HOH 31  431 102 HOH HOH A . 
E 5 HOH 32  432 69  HOH HOH A . 
E 5 HOH 33  433 34  HOH HOH A . 
E 5 HOH 34  434 7   HOH HOH A . 
E 5 HOH 35  435 23  HOH HOH A . 
E 5 HOH 36  436 45  HOH HOH A . 
E 5 HOH 37  437 27  HOH HOH A . 
E 5 HOH 38  438 25  HOH HOH A . 
E 5 HOH 39  439 147 HOH HOH A . 
E 5 HOH 40  440 143 HOH HOH A . 
E 5 HOH 41  441 21  HOH HOH A . 
E 5 HOH 42  442 71  HOH HOH A . 
E 5 HOH 43  443 136 HOH HOH A . 
E 5 HOH 44  444 29  HOH HOH A . 
E 5 HOH 45  445 47  HOH HOH A . 
E 5 HOH 46  446 109 HOH HOH A . 
E 5 HOH 47  447 11  HOH HOH A . 
E 5 HOH 48  448 30  HOH HOH A . 
E 5 HOH 49  449 54  HOH HOH A . 
E 5 HOH 50  450 79  HOH HOH A . 
E 5 HOH 51  451 33  HOH HOH A . 
E 5 HOH 52  452 46  HOH HOH A . 
E 5 HOH 53  453 107 HOH HOH A . 
E 5 HOH 54  454 3   HOH HOH A . 
E 5 HOH 55  455 88  HOH HOH A . 
E 5 HOH 56  456 90  HOH HOH A . 
E 5 HOH 57  457 6   HOH HOH A . 
E 5 HOH 58  458 37  HOH HOH A . 
E 5 HOH 59  459 104 HOH HOH A . 
E 5 HOH 60  460 14  HOH HOH A . 
E 5 HOH 61  461 77  HOH HOH A . 
E 5 HOH 62  462 141 HOH HOH A . 
E 5 HOH 63  463 48  HOH HOH A . 
E 5 HOH 64  464 10  HOH HOH A . 
E 5 HOH 65  465 105 HOH HOH A . 
E 5 HOH 66  466 35  HOH HOH A . 
E 5 HOH 67  467 85  HOH HOH A . 
E 5 HOH 68  468 51  HOH HOH A . 
E 5 HOH 69  469 96  HOH HOH A . 
E 5 HOH 70  470 55  HOH HOH A . 
E 5 HOH 71  471 139 HOH HOH A . 
E 5 HOH 72  472 70  HOH HOH A . 
E 5 HOH 73  473 91  HOH HOH A . 
E 5 HOH 74  474 124 HOH HOH A . 
E 5 HOH 75  475 115 HOH HOH A . 
E 5 HOH 76  476 60  HOH HOH A . 
E 5 HOH 77  477 125 HOH HOH A . 
E 5 HOH 78  478 82  HOH HOH A . 
E 5 HOH 79  479 142 HOH HOH A . 
E 5 HOH 80  480 43  HOH HOH A . 
E 5 HOH 81  481 44  HOH HOH A . 
E 5 HOH 82  482 41  HOH HOH A . 
E 5 HOH 83  483 12  HOH HOH A . 
E 5 HOH 84  484 39  HOH HOH A . 
E 5 HOH 85  485 40  HOH HOH A . 
E 5 HOH 86  486 126 HOH HOH A . 
E 5 HOH 87  487 57  HOH HOH A . 
E 5 HOH 88  488 108 HOH HOH A . 
E 5 HOH 89  489 84  HOH HOH A . 
E 5 HOH 90  490 127 HOH HOH A . 
E 5 HOH 91  491 129 HOH HOH A . 
E 5 HOH 92  492 9   HOH HOH A . 
E 5 HOH 93  493 28  HOH HOH A . 
E 5 HOH 94  494 151 HOH HOH A . 
E 5 HOH 95  495 22  HOH HOH A . 
E 5 HOH 96  496 67  HOH HOH A . 
E 5 HOH 97  497 75  HOH HOH A . 
E 5 HOH 98  498 76  HOH HOH A . 
E 5 HOH 99  499 131 HOH HOH A . 
E 5 HOH 100 500 32  HOH HOH A . 
E 5 HOH 101 501 50  HOH HOH A . 
E 5 HOH 102 502 140 HOH HOH A . 
E 5 HOH 103 503 146 HOH HOH A . 
E 5 HOH 104 504 110 HOH HOH A . 
E 5 HOH 105 505 86  HOH HOH A . 
E 5 HOH 106 506 97  HOH HOH A . 
E 5 HOH 107 507 135 HOH HOH A . 
E 5 HOH 108 508 113 HOH HOH A . 
E 5 HOH 109 509 92  HOH HOH A . 
E 5 HOH 110 510 111 HOH HOH A . 
E 5 HOH 111 511 116 HOH HOH A . 
E 5 HOH 112 512 121 HOH HOH A . 
E 5 HOH 113 513 148 HOH HOH A . 
E 5 HOH 114 514 152 HOH HOH A . 
E 5 HOH 115 515 64  HOH HOH A . 
E 5 HOH 116 516 83  HOH HOH A . 
E 5 HOH 117 517 132 HOH HOH A . 
E 5 HOH 118 518 138 HOH HOH A . 
E 5 HOH 119 519 118 HOH HOH A . 
E 5 HOH 120 520 78  HOH HOH A . 
E 5 HOH 121 521 98  HOH HOH A . 
E 5 HOH 122 522 133 HOH HOH A . 
E 5 HOH 123 523 38  HOH HOH A . 
E 5 HOH 124 524 149 HOH HOH A . 
E 5 HOH 125 525 26  HOH HOH A . 
E 5 HOH 126 526 155 HOH HOH A . 
E 5 HOH 127 527 58  HOH HOH A . 
E 5 HOH 128 528 53  HOH HOH A . 
E 5 HOH 129 529 156 HOH HOH A . 
E 5 HOH 130 530 65  HOH HOH A . 
E 5 HOH 131 531 89  HOH HOH A . 
E 5 HOH 132 532 123 HOH HOH A . 
E 5 HOH 133 533 100 HOH HOH A . 
E 5 HOH 134 534 119 HOH HOH A . 
E 5 HOH 135 535 74  HOH HOH A . 
E 5 HOH 136 536 80  HOH HOH A . 
E 5 HOH 137 537 154 HOH HOH A . 
E 5 HOH 138 538 68  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 GLU 94  ? CG  ? A GLU 94  CG  
6  1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
7  1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
8  1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
9  1 Y 1 A LYS 114 ? CG  ? A LYS 114 CG  
10 1 Y 1 A LYS 114 ? CD  ? A LYS 114 CD  
11 1 Y 1 A LYS 114 ? CE  ? A LYS 114 CE  
12 1 Y 1 A LYS 114 ? NZ  ? A LYS 114 NZ  
13 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
14 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
15 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
16 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QG4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.291 
_cell.length_a_esd                 ? 
_cell.length_b                     74.997 
_cell.length_b_esd                 ? 
_cell.length_c                     118.587 
_cell.length_c_esd                 ? 
_cell.volume                       562889.220 
_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                         8QG4 
_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                   8QG4 
_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             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.73 
_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         2020-03-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979257 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979257 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          27.81 
_reflns.entry_id                                       8QG4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.69 
_reflns.d_resolution_low                               48.37 
_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                                     30565 
_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                           96.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.38 
_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                                0.04 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.036000000000000004 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.69 1.8   ? ? ? ? ? ? 4275 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.445                ? ? 1 1 0.9359999999999999 ? ? ? ? 0.39 ? ? ? ? ? ? 
? ? ? 
1.80 1.92  ? ? ? ? ? ? 4647 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.265                ? ? 2 1 0.983              ? ? ? ? 
0.23800000000000002  ? ? ? ? ? ? ? ? ? 
1.92 2.07  ? ? ? ? ? ? 4346 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.146                ? ? 3 1 0.9940000000000001 ? ? ? ? 0.134 ? ? ? ? ? 
? ? ? ? 
2.07 2.27  ? ? ? ? ? ? 3973 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.092                ? ? 4 1 0.997              ? ? ? ? 0.083 ? ? ? ? ? 
? ? ? ? 
2.27 2.54  ? ? ? ? ? ? 3698 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.059000000000000004 ? ? 5 1 0.9990000000000001 ? ? ? ? 
0.054000000000000006 ? ? ? ? ? ? ? ? ? 
2.54 2.93  ? ? ? ? ? ? 3312 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.043                ? ? 6 1 0.9990000000000001 ? ? ? ? 0.039 ? ? ? ? ? 
? ? ? ? 
2.93 3.59  ? ? ? ? ? ? 2807 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.033                ? ? 7 1 0.9990000000000001 ? ? ? ? 0.03 ? ? ? ? ? ? 
? ? ? 
3.59 5.06  ? ? ? ? ? ? 2216 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.03                 ? ? 8 1 0.9990000000000001 ? ? ? ? 
0.027999999999999997 ? ? ? ? ? ? ? ? ? 
5.06 48.37 ? ? ? ? ? ? 1291 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.03                 ? ? 9 1 0.9990000000000001 ? ? ? ? 
0.027000000000000003 ? ? ? ? ? ? ? ? ? 
# 
_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                               36.67 
_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                                 8QG4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.69 
_refine.ls_d_res_low                             48.37 
_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                     30506 
_refine.ls_number_reflns_R_free                  1525 
_refine.ls_number_reflns_R_work                  28981 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.00 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1877 
_refine.ls_R_factor_R_free                       0.2152 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1863 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.0378 
_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                            0.2449 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.69 
_refine_hist.d_res_low                        48.37 
_refine_hist.number_atoms_solvent             138 
_refine_hist.number_atoms_total               2281 
_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        2074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         69 
_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' ? 0.0146  ? 2229 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4206  ? 3023 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0903  ? 326  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0119  ? 413  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1504 ? 845  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.69 1.75  . . 113 2125 78.17 . . . . 0.3666 . . . . . . . . . . . 0.3798 
'X-RAY DIFFRACTION' 1.75 1.81  . . 131 2498 93.36 . . . . 0.2737 . . . . . . . . . . . 0.3125 
'X-RAY DIFFRACTION' 1.81 1.88  . . 140 2692 98.64 . . . . 0.2151 . . . . . . . . . . . 0.2467 
'X-RAY DIFFRACTION' 1.88 1.97  . . 134 2528 92.78 . . . . 0.2523 . . . . . . . . . . . 0.3351 
'X-RAY DIFFRACTION' 1.97 2.07  . . 142 2696 99.68 . . . . 0.1813 . . . . . . . . . . . 0.2344 
'X-RAY DIFFRACTION' 2.07 2.20  . . 142 2706 99.48 . . . . 0.1883 . . . . . . . . . . . 0.2203 
'X-RAY DIFFRACTION' 2.20 2.37  . . 135 2580 94.93 . . . . 0.2197 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 2.37 2.61  . . 144 2740 99.90 . . . . 0.1926 . . . . . . . . . . . 0.2314 
'X-RAY DIFFRACTION' 2.61 2.99  . . 146 2758 99.73 . . . . 0.1923 . . . . . . . . . . . 0.2280 
'X-RAY DIFFRACTION' 2.99 3.77  . . 146 2783 99.73 . . . . 0.1695 . . . . . . . . . . . 0.1894 
'X-RAY DIFFRACTION' 3.77 48.37 . . 152 2875 99.25 . . . . 0.1623 . . . . . . . . . . . 0.1755 
# 
_struct.entry_id                     8QG4 
_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        8QG4 
_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 ? 
E N N 5 ? 
# 
_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              8QG4 
_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 8QG4 LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QG4 GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QG4 HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QG4 HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QG4 HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QG4 HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QG4 HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QG4 HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E 
1 2 A,B,C,D,E 
1 3 A,B,C,D,E 
1 4 A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 63.2910000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 63.2910000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P4 AA4 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P5 AA5 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P6 AA6 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P7 AA7 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 8 ? 
AA3 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? 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 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 2 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA2 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA2 7 ALA A 178 ? SER A 186 ? ALA A 178 SER A 186 
AA2 8 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA3 2 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA3 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA3 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA3 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA3 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA3 7 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 8 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 9 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA2 3 4 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA2 6 7 N SER A 155 ? N SER A 155 O GLN A 180 ? O GLN A 180 
AA2 7 8 N MET A 179 ? N MET A 179 O PHE A 201 ? O PHE A 201 
AA3 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA3 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA3 3 4 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA3 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA3 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 6 7 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 7 8 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 8 9 N PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QG4 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    462 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    503 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.09 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              222 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              223 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              223 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                106.60 
_pdbx_validate_rmsd_angle.angle_target_value         121.70 
_pdbx_validate_rmsd_angle.angle_deviation            -15.10 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
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 TYR A 109 ? ? -122.76 -142.15 
2 1 ASN A 122 ? ? -98.13  -67.52  
3 1 SER A 129 ? ? -89.36  32.42   
4 1 ALA A 162 ? ? -107.08 -131.80 
5 1 HIS A 204 ? ? 83.44   -16.04  
6 1 ASN A 213 ? ? -128.31 -76.07  
7 1 ASP A 222 ? ? 56.72   -137.57 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     256 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.077 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 410 ? E HOH . 
2 1 A HOH 538 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 13.1508483455 23.9555686805 19.1482331402  0.290111185959 ? 0.0662020829172 ? 0.0100939776946 ? 
0.263152636653 ? -0.0685408191938 ? 0.270127743068 ? 2.13071673889 ? -0.548512700818   ? -1.65517566563 ? 1.71513611517 ? 
1.28137288105  ? 6.50326408626 ? -0.0175041147807 ? -0.403151051342  ? 0.231216364067  ? 0.185770196027   ? 0.0753740432687 ? 
0.0757187627077 ? -0.378768354988 ? 0.0549421035156 ? -0.00343205793238 ? 
2 'X-RAY DIFFRACTION' ? refined 20.3068236246 12.8551196184 -1.53899650414 0.176738812363 ? 0.0178338300058 ? 0.0128272072849 ? 
0.168648764244 ? 0.00391587371157 ? 0.212834401861 ? 1.52546419299 ? -0.00721016786705 ? 0.399653160749 ? 1.56591361669 ? 
0.433700130447 ? 3.2418286005  ? 0.0231901794897  ? 0.00326520451646 ? 0.0870549538041 ? -0.0466559089454 ? -0.0279697376   ? 
0.162017099517  ? 0.0025857001335 ? -0.27624108792  ? 0.0130306054085   ? 
# 
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 117 A 120 ? ? 
;chain 'A' and (resid    1  through  120 )
;
2 'X-RAY DIFFRACTION' 2 A 118 A 121 ? A 261 A 264 ? ? 
;chain 'A' and (resid  121  through  264 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
GOL C1   C N N 158 
GOL O1   O N N 159 
GOL C2   C N N 160 
GOL O2   O N N 161 
GOL C3   C N N 162 
GOL O3   O N N 163 
GOL H11  H N N 164 
GOL H12  H N N 165 
GOL HO1  H N N 166 
GOL H2   H N N 167 
GOL HO2  H N N 168 
GOL H31  H N N 169 
GOL H32  H N N 170 
GOL HO3  H N N 171 
HIS N    N N N 172 
HIS CA   C N S 173 
HIS C    C N N 174 
HIS O    O N N 175 
HIS CB   C N N 176 
HIS CG   C Y N 177 
HIS ND1  N Y N 178 
HIS CD2  C Y N 179 
HIS CE1  C Y N 180 
HIS NE2  N Y N 181 
HIS OXT  O N N 182 
HIS H    H N N 183 
HIS H2   H N N 184 
HIS HA   H N N 185 
HIS HB2  H N N 186 
HIS HB3  H N N 187 
HIS HD1  H N N 188 
HIS HD2  H N N 189 
HIS HE1  H N N 190 
HIS HE2  H N N 191 
HIS HXT  H N N 192 
HOH O    O N N 193 
HOH H1   H N N 194 
HOH H2   H N N 195 
ILE N    N N N 196 
ILE CA   C N S 197 
ILE C    C N N 198 
ILE O    O N N 199 
ILE CB   C N S 200 
ILE CG1  C N N 201 
ILE CG2  C N N 202 
ILE CD1  C N N 203 
ILE OXT  O N N 204 
ILE H    H N N 205 
ILE H2   H N N 206 
ILE HA   H N N 207 
ILE HB   H N N 208 
ILE HG12 H N N 209 
ILE HG13 H N N 210 
ILE HG21 H N N 211 
ILE HG22 H N N 212 
ILE HG23 H N N 213 
ILE HD11 H N N 214 
ILE HD12 H N N 215 
ILE HD13 H N N 216 
ILE HXT  H N N 217 
LEU N    N N N 218 
LEU CA   C N S 219 
LEU C    C N N 220 
LEU O    O N N 221 
LEU CB   C N N 222 
LEU CG   C N N 223 
LEU CD1  C N N 224 
LEU CD2  C N N 225 
LEU OXT  O N N 226 
LEU H    H N N 227 
LEU H2   H N N 228 
LEU HA   H N N 229 
LEU HB2  H N N 230 
LEU HB3  H N N 231 
LEU HG   H N N 232 
LEU HD11 H N N 233 
LEU HD12 H N N 234 
LEU HD13 H N N 235 
LEU HD21 H N N 236 
LEU HD22 H N N 237 
LEU HD23 H N N 238 
LEU HXT  H N N 239 
LYS N    N N N 240 
LYS CA   C N S 241 
LYS C    C N N 242 
LYS O    O N N 243 
LYS CB   C N N 244 
LYS CG   C N N 245 
LYS CD   C N N 246 
LYS CE   C N N 247 
LYS NZ   N N N 248 
LYS OXT  O N N 249 
LYS H    H N N 250 
LYS H2   H N N 251 
LYS HA   H N N 252 
LYS HB2  H N N 253 
LYS HB3  H N N 254 
LYS HG2  H N N 255 
LYS HG3  H N N 256 
LYS HD2  H N N 257 
LYS HD3  H N N 258 
LYS HE2  H N N 259 
LYS HE3  H N N 260 
LYS HZ1  H N N 261 
LYS HZ2  H N N 262 
LYS HZ3  H N N 263 
LYS HXT  H N N 264 
MET N    N N N 265 
MET CA   C N S 266 
MET C    C N N 267 
MET O    O N N 268 
MET CB   C N N 269 
MET CG   C N N 270 
MET SD   S N N 271 
MET CE   C N N 272 
MET OXT  O N N 273 
MET H    H N N 274 
MET H2   H N N 275 
MET HA   H N N 276 
MET HB2  H N N 277 
MET HB3  H N N 278 
MET HG2  H N N 279 
MET HG3  H N N 280 
MET HE1  H N N 281 
MET HE2  H N N 282 
MET HE3  H N N 283 
MET HXT  H N N 284 
PHE N    N N N 285 
PHE CA   C N S 286 
PHE C    C N N 287 
PHE O    O N N 288 
PHE CB   C N N 289 
PHE CG   C Y N 290 
PHE CD1  C Y N 291 
PHE CD2  C Y N 292 
PHE CE1  C Y N 293 
PHE CE2  C Y N 294 
PHE CZ   C Y N 295 
PHE OXT  O N N 296 
PHE H    H N N 297 
PHE H2   H N N 298 
PHE HA   H N N 299 
PHE HB2  H N N 300 
PHE HB3  H N N 301 
PHE HD1  H N N 302 
PHE HD2  H N N 303 
PHE HE1  H N N 304 
PHE HE2  H N N 305 
PHE HZ   H N N 306 
PHE HXT  H N N 307 
PRO N    N N N 308 
PRO CA   C N S 309 
PRO C    C N N 310 
PRO O    O N N 311 
PRO CB   C N N 312 
PRO CG   C N N 313 
PRO CD   C N N 314 
PRO OXT  O N N 315 
PRO H    H N N 316 
PRO HA   H N N 317 
PRO HB2  H N N 318 
PRO HB3  H N N 319 
PRO HG2  H N N 320 
PRO HG3  H N N 321 
PRO HD2  H N N 322 
PRO HD3  H N N 323 
PRO HXT  H N N 324 
SER N    N N N 325 
SER CA   C N S 326 
SER C    C N N 327 
SER O    O N N 328 
SER CB   C N N 329 
SER OG   O N N 330 
SER OXT  O N N 331 
SER H    H N N 332 
SER H2   H N N 333 
SER HA   H N N 334 
SER HB2  H N N 335 
SER HB3  H N N 336 
SER HG   H N N 337 
SER HXT  H N N 338 
THR N    N N N 339 
THR CA   C N S 340 
THR C    C N N 341 
THR O    O N N 342 
THR CB   C N R 343 
THR OG1  O N N 344 
THR CG2  C N N 345 
THR OXT  O N N 346 
THR H    H N N 347 
THR H2   H N N 348 
THR HA   H N N 349 
THR HB   H N N 350 
THR HG1  H N N 351 
THR HG21 H N N 352 
THR HG22 H N N 353 
THR HG23 H N N 354 
THR HXT  H N N 355 
TRP N    N N N 356 
TRP CA   C N S 357 
TRP C    C N N 358 
TRP O    O N N 359 
TRP CB   C N N 360 
TRP CG   C Y N 361 
TRP CD1  C Y N 362 
TRP CD2  C Y N 363 
TRP NE1  N Y N 364 
TRP CE2  C Y N 365 
TRP CE3  C Y N 366 
TRP CZ2  C Y N 367 
TRP CZ3  C Y N 368 
TRP CH2  C Y N 369 
TRP OXT  O N N 370 
TRP H    H N N 371 
TRP H2   H N N 372 
TRP HA   H N N 373 
TRP HB2  H N N 374 
TRP HB3  H N N 375 
TRP HD1  H N N 376 
TRP HE1  H N N 377 
TRP HE3  H N N 378 
TRP HZ2  H N N 379 
TRP HZ3  H N N 380 
TRP HH2  H N N 381 
TRP HXT  H N N 382 
TYR N    N N N 383 
TYR CA   C N S 384 
TYR C    C N N 385 
TYR O    O N N 386 
TYR CB   C N N 387 
TYR CG   C Y N 388 
TYR CD1  C Y N 389 
TYR CD2  C Y N 390 
TYR CE1  C Y N 391 
TYR CE2  C Y N 392 
TYR CZ   C Y N 393 
TYR OH   O N N 394 
TYR OXT  O N N 395 
TYR H    H N N 396 
TYR H2   H N N 397 
TYR HA   H N N 398 
TYR HB2  H N N 399 
TYR HB3  H N N 400 
TYR HD1  H N N 401 
TYR HD2  H N N 402 
TYR HE1  H N N 403 
TYR HE2  H N N 404 
TYR HH   H N N 405 
TYR HXT  H N N 406 
UZ6 N1   N N N 407 
UZ6 C7   C N S 408 
UZ6 C8   C Y N 409 
UZ6 N2   N Y N 410 
UZ6 C9   C Y N 411 
UZ6 O1   O N N 412 
UZ6 C1   C N N 413 
UZ6 O5   O N N 414 
UZ6 C5   C N R 415 
UZ6 C6   C N R 416 
UZ6 N3   N Y N 417 
UZ6 C4   C N R 418 
UZ6 O4   O N N 419 
UZ6 C3   C N N 420 
UZ6 O3   O N N 421 
UZ6 C2   C N N 422 
UZ6 N4   N Y N 423 
UZ6 N    N N N 424 
UZ6 C    C N N 425 
UZ6 O    O N N 426 
UZ6 C10  C Y N 427 
UZ6 C11  C Y N 428 
UZ6 C12  C Y N 429 
UZ6 C13  C N N 430 
UZ6 C14  C N N 431 
UZ6 C15  C N N 432 
UZ6 C16  C N N 433 
UZ6 C17  C N N 434 
UZ6 C18  C N N 435 
UZ6 C19  C N N 436 
UZ6 C20  C N R 437 
UZ6 C21  C N R 438 
UZ6 C22  C N R 439 
UZ6 C23  C N S 440 
UZ6 C24  C Y N 441 
UZ6 C25  C Y N 442 
UZ6 C26  C Y N 443 
UZ6 C27  C Y N 444 
UZ6 C28  C Y N 445 
UZ6 N10  N Y N 446 
UZ6 N11  N Y N 447 
UZ6 N12  N Y N 448 
UZ6 N13  N N N 449 
UZ6 N5   N Y N 450 
UZ6 N6   N N N 451 
UZ6 N7   N N N 452 
UZ6 N8   N N N 453 
UZ6 N9   N Y N 454 
UZ6 O2   O N N 455 
UZ6 O6   O N N 456 
UZ6 H17  H N N 457 
UZ6 H3   H N N 458 
UZ6 H14  H N N 459 
UZ6 H15  H N N 460 
UZ6 H35  H N N 461 
UZ6 H1   H N N 462 
UZ6 H2   H N N 463 
UZ6 H    H N N 464 
UZ6 H19  H N N 465 
UZ6 H18  H N N 466 
UZ6 H21  H N N 467 
UZ6 H16  H N N 468 
UZ6 H12  H N N 469 
UZ6 H11  H N N 470 
UZ6 H13  H N N 471 
UZ6 H22  H N N 472 
UZ6 H25  H N N 473 
UZ6 H26  H N N 474 
UZ6 H27  H N N 475 
UZ6 H28  H N N 476 
UZ6 H30  H N N 477 
UZ6 H29  H N N 478 
UZ6 H31  H N N 479 
UZ6 H32  H N N 480 
UZ6 H33  H N N 481 
UZ6 H34  H N N 482 
UZ6 H7   H N N 483 
UZ6 H8   H N N 484 
UZ6 H9   H N N 485 
UZ6 H10  H N N 486 
UZ6 H37  H N N 487 
UZ6 H38  H N N 488 
UZ6 H40  H N N 489 
UZ6 H39  H N N 490 
UZ6 H24  H N N 491 
UZ6 H23  H N N 492 
UZ6 H6   H N N 493 
UZ6 H4   H N N 494 
UZ6 H20  H N N 495 
UZ6 H36  H N N 496 
VAL N    N N N 497 
VAL CA   C N S 498 
VAL C    C N N 499 
VAL O    O N N 500 
VAL CB   C N N 501 
VAL CG1  C N N 502 
VAL CG2  C N N 503 
VAL OXT  O N N 504 
VAL H    H N N 505 
VAL H2   H N N 506 
VAL HA   H N N 507 
VAL HB   H N N 508 
VAL HG11 H N N 509 
VAL HG12 H N N 510 
VAL HG13 H N N 511 
VAL HG21 H N N 512 
VAL HG22 H N N 513 
VAL HG23 H N N 514 
VAL HXT  H N N 515 
# 
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 
GOL C1  O1   sing N N 149 
GOL C1  C2   sing N N 150 
GOL C1  H11  sing N N 151 
GOL C1  H12  sing N N 152 
GOL O1  HO1  sing N N 153 
GOL C2  O2   sing N N 154 
GOL C2  C3   sing N N 155 
GOL C2  H2   sing N N 156 
GOL O2  HO2  sing N N 157 
GOL C3  O3   sing N N 158 
GOL C3  H31  sing N N 159 
GOL C3  H32  sing N N 160 
GOL O3  HO3  sing N N 161 
HIS N   CA   sing N N 162 
HIS N   H    sing N N 163 
HIS N   H2   sing N N 164 
HIS CA  C    sing N N 165 
HIS CA  CB   sing N N 166 
HIS CA  HA   sing N N 167 
HIS C   O    doub N N 168 
HIS C   OXT  sing N N 169 
HIS CB  CG   sing N N 170 
HIS CB  HB2  sing N N 171 
HIS CB  HB3  sing N N 172 
HIS CG  ND1  sing Y N 173 
HIS CG  CD2  doub Y N 174 
HIS ND1 CE1  doub Y N 175 
HIS ND1 HD1  sing N N 176 
HIS CD2 NE2  sing Y N 177 
HIS CD2 HD2  sing N N 178 
HIS CE1 NE2  sing Y N 179 
HIS CE1 HE1  sing N N 180 
HIS NE2 HE2  sing N N 181 
HIS OXT HXT  sing N N 182 
HOH O   H1   sing N N 183 
HOH O   H2   sing N N 184 
ILE N   CA   sing N N 185 
ILE N   H    sing N N 186 
ILE N   H2   sing N N 187 
ILE CA  C    sing N N 188 
ILE CA  CB   sing N N 189 
ILE CA  HA   sing N N 190 
ILE C   O    doub N N 191 
ILE C   OXT  sing N N 192 
ILE CB  CG1  sing N N 193 
ILE CB  CG2  sing N N 194 
ILE CB  HB   sing N N 195 
ILE CG1 CD1  sing N N 196 
ILE CG1 HG12 sing N N 197 
ILE CG1 HG13 sing N N 198 
ILE CG2 HG21 sing N N 199 
ILE CG2 HG22 sing N N 200 
ILE CG2 HG23 sing N N 201 
ILE CD1 HD11 sing N N 202 
ILE CD1 HD12 sing N N 203 
ILE CD1 HD13 sing N N 204 
ILE OXT HXT  sing N N 205 
LEU N   CA   sing N N 206 
LEU N   H    sing N N 207 
LEU N   H2   sing N N 208 
LEU CA  C    sing N N 209 
LEU CA  CB   sing N N 210 
LEU CA  HA   sing N N 211 
LEU C   O    doub N N 212 
LEU C   OXT  sing N N 213 
LEU CB  CG   sing N N 214 
LEU CB  HB2  sing N N 215 
LEU CB  HB3  sing N N 216 
LEU CG  CD1  sing N N 217 
LEU CG  CD2  sing N N 218 
LEU CG  HG   sing N N 219 
LEU CD1 HD11 sing N N 220 
LEU CD1 HD12 sing N N 221 
LEU CD1 HD13 sing N N 222 
LEU CD2 HD21 sing N N 223 
LEU CD2 HD22 sing N N 224 
LEU CD2 HD23 sing N N 225 
LEU OXT HXT  sing N N 226 
LYS N   CA   sing N N 227 
LYS N   H    sing N N 228 
LYS N   H2   sing N N 229 
LYS CA  C    sing N N 230 
LYS CA  CB   sing N N 231 
LYS CA  HA   sing N N 232 
LYS C   O    doub N N 233 
LYS C   OXT  sing N N 234 
LYS CB  CG   sing N N 235 
LYS CB  HB2  sing N N 236 
LYS CB  HB3  sing N N 237 
LYS CG  CD   sing N N 238 
LYS CG  HG2  sing N N 239 
LYS CG  HG3  sing N N 240 
LYS CD  CE   sing N N 241 
LYS CD  HD2  sing N N 242 
LYS CD  HD3  sing N N 243 
LYS CE  NZ   sing N N 244 
LYS CE  HE2  sing N N 245 
LYS CE  HE3  sing N N 246 
LYS NZ  HZ1  sing N N 247 
LYS NZ  HZ2  sing N N 248 
LYS NZ  HZ3  sing N N 249 
LYS OXT HXT  sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
PHE N   CA   sing N N 270 
PHE N   H    sing N N 271 
PHE N   H2   sing N N 272 
PHE CA  C    sing N N 273 
PHE CA  CB   sing N N 274 
PHE CA  HA   sing N N 275 
PHE C   O    doub N N 276 
PHE C   OXT  sing N N 277 
PHE CB  CG   sing N N 278 
PHE CB  HB2  sing N N 279 
PHE CB  HB3  sing N N 280 
PHE CG  CD1  doub Y N 281 
PHE CG  CD2  sing Y N 282 
PHE CD1 CE1  sing Y N 283 
PHE CD1 HD1  sing N N 284 
PHE CD2 CE2  doub Y N 285 
PHE CD2 HD2  sing N N 286 
PHE CE1 CZ   doub Y N 287 
PHE CE1 HE1  sing N N 288 
PHE CE2 CZ   sing Y N 289 
PHE CE2 HE2  sing N N 290 
PHE CZ  HZ   sing N N 291 
PHE OXT HXT  sing N N 292 
PRO N   CA   sing N N 293 
PRO N   CD   sing N N 294 
PRO N   H    sing N N 295 
PRO CA  C    sing N N 296 
PRO CA  CB   sing N N 297 
PRO CA  HA   sing N N 298 
PRO C   O    doub N N 299 
PRO C   OXT  sing N N 300 
PRO CB  CG   sing N N 301 
PRO CB  HB2  sing N N 302 
PRO CB  HB3  sing N N 303 
PRO CG  CD   sing N N 304 
PRO CG  HG2  sing N N 305 
PRO CG  HG3  sing N N 306 
PRO CD  HD2  sing N N 307 
PRO CD  HD3  sing N N 308 
PRO OXT HXT  sing N N 309 
SER N   CA   sing N N 310 
SER N   H    sing N N 311 
SER N   H2   sing N N 312 
SER CA  C    sing N N 313 
SER CA  CB   sing N N 314 
SER CA  HA   sing N N 315 
SER C   O    doub N N 316 
SER C   OXT  sing N N 317 
SER CB  OG   sing N N 318 
SER CB  HB2  sing N N 319 
SER CB  HB3  sing N N 320 
SER OG  HG   sing N N 321 
SER OXT HXT  sing N N 322 
THR N   CA   sing N N 323 
THR N   H    sing N N 324 
THR N   H2   sing N N 325 
THR CA  C    sing N N 326 
THR CA  CB   sing N N 327 
THR CA  HA   sing N N 328 
THR C   O    doub N N 329 
THR C   OXT  sing N N 330 
THR CB  OG1  sing N N 331 
THR CB  CG2  sing N N 332 
THR CB  HB   sing N N 333 
THR OG1 HG1  sing N N 334 
THR CG2 HG21 sing N N 335 
THR CG2 HG22 sing N N 336 
THR CG2 HG23 sing N N 337 
THR OXT HXT  sing N N 338 
TRP N   CA   sing N N 339 
TRP N   H    sing N N 340 
TRP N   H2   sing N N 341 
TRP CA  C    sing N N 342 
TRP CA  CB   sing N N 343 
TRP CA  HA   sing N N 344 
TRP C   O    doub N N 345 
TRP C   OXT  sing N N 346 
TRP CB  CG   sing N N 347 
TRP CB  HB2  sing N N 348 
TRP CB  HB3  sing N N 349 
TRP CG  CD1  doub Y N 350 
TRP CG  CD2  sing Y N 351 
TRP CD1 NE1  sing Y N 352 
TRP CD1 HD1  sing N N 353 
TRP CD2 CE2  doub Y N 354 
TRP CD2 CE3  sing Y N 355 
TRP NE1 CE2  sing Y N 356 
TRP NE1 HE1  sing N N 357 
TRP CE2 CZ2  sing Y N 358 
TRP CE3 CZ3  doub Y N 359 
TRP CE3 HE3  sing N N 360 
TRP CZ2 CH2  doub Y N 361 
TRP CZ2 HZ2  sing N N 362 
TRP CZ3 CH2  sing Y N 363 
TRP CZ3 HZ3  sing N N 364 
TRP CH2 HH2  sing N N 365 
TRP OXT HXT  sing N N 366 
TYR N   CA   sing N N 367 
TYR N   H    sing N N 368 
TYR N   H2   sing N N 369 
TYR CA  C    sing N N 370 
TYR CA  CB   sing N N 371 
TYR CA  HA   sing N N 372 
TYR C   O    doub N N 373 
TYR C   OXT  sing N N 374 
TYR CB  CG   sing N N 375 
TYR CB  HB2  sing N N 376 
TYR CB  HB3  sing N N 377 
TYR CG  CD1  doub Y N 378 
TYR CG  CD2  sing Y N 379 
TYR CD1 CE1  sing Y N 380 
TYR CD1 HD1  sing N N 381 
TYR CD2 CE2  doub Y N 382 
TYR CD2 HD2  sing N N 383 
TYR CE1 CZ   doub Y N 384 
TYR CE1 HE1  sing N N 385 
TYR CE2 CZ   sing Y N 386 
TYR CE2 HE2  sing N N 387 
TYR CZ  OH   sing N N 388 
TYR OH  HH   sing N N 389 
TYR OXT HXT  sing N N 390 
UZ6 C   C1   sing N N 391 
UZ6 C1  N    sing N N 392 
UZ6 N   C2   sing N N 393 
UZ6 C2  O    doub N N 394 
UZ6 N1  C2   sing N N 395 
UZ6 C3  N1   sing N N 396 
UZ6 C4  C3   sing N N 397 
UZ6 C4  O1   sing N N 398 
UZ6 O1  C5   sing N N 399 
UZ6 C5  C6   sing N N 400 
UZ6 O2  C6   sing N N 401 
UZ6 C6  C7   sing N N 402 
UZ6 C7  C4   sing N N 403 
UZ6 O3  C7   sing N N 404 
UZ6 N2  C5   sing N N 405 
UZ6 N2  C8   sing Y N 406 
UZ6 C8  N3   doub Y N 407 
UZ6 N3  C9   sing Y N 408 
UZ6 C9  C10  doub Y N 409 
UZ6 C10 N2   sing Y N 410 
UZ6 N4  C10  sing Y N 411 
UZ6 C11 N4   doub Y N 412 
UZ6 N5  C11  sing Y N 413 
UZ6 C12 N5   doub Y N 414 
UZ6 C9  C12  sing Y N 415 
UZ6 N6  C12  sing N N 416 
UZ6 C13 C8   sing N N 417 
UZ6 C14 C13  trip N N 418 
UZ6 C15 C14  sing N N 419 
UZ6 N7  C15  sing N N 420 
UZ6 C16 N7   sing N N 421 
UZ6 C17 C16  sing N N 422 
UZ6 C18 C17  sing N N 423 
UZ6 N8  C18  sing N N 424 
UZ6 C19 N7   sing N N 425 
UZ6 C20 C19  sing N N 426 
UZ6 C20 O4   sing N N 427 
UZ6 O4  C21  sing N N 428 
UZ6 C21 C22  sing N N 429 
UZ6 O5  C22  sing N N 430 
UZ6 C22 C23  sing N N 431 
UZ6 C23 C20  sing N N 432 
UZ6 O6  C23  sing N N 433 
UZ6 N9  C21  sing N N 434 
UZ6 N9  C24  sing Y N 435 
UZ6 C24 N10  doub Y N 436 
UZ6 N10 C25  sing Y N 437 
UZ6 C25 C26  doub Y N 438 
UZ6 C26 N9   sing Y N 439 
UZ6 N11 C26  sing Y N 440 
UZ6 C27 N11  doub Y N 441 
UZ6 N12 C27  sing Y N 442 
UZ6 C28 N12  doub Y N 443 
UZ6 C25 C28  sing Y N 444 
UZ6 N13 C28  sing N N 445 
UZ6 N1  H17  sing N N 446 
UZ6 C7  H3   sing N N 447 
UZ6 C1  H14  sing N N 448 
UZ6 C1  H15  sing N N 449 
UZ6 O5  H35  sing N N 450 
UZ6 C5  H1   sing N N 451 
UZ6 C6  H2   sing N N 452 
UZ6 C4  H    sing N N 453 
UZ6 C3  H19  sing N N 454 
UZ6 C3  H18  sing N N 455 
UZ6 O3  H21  sing N N 456 
UZ6 N   H16  sing N N 457 
UZ6 C   H12  sing N N 458 
UZ6 C   H11  sing N N 459 
UZ6 C   H13  sing N N 460 
UZ6 C11 H22  sing N N 461 
UZ6 C15 H25  sing N N 462 
UZ6 C15 H26  sing N N 463 
UZ6 C16 H27  sing N N 464 
UZ6 C16 H28  sing N N 465 
UZ6 C17 H30  sing N N 466 
UZ6 C17 H29  sing N N 467 
UZ6 C18 H31  sing N N 468 
UZ6 C18 H32  sing N N 469 
UZ6 C19 H33  sing N N 470 
UZ6 C19 H34  sing N N 471 
UZ6 C20 H7   sing N N 472 
UZ6 C21 H8   sing N N 473 
UZ6 C22 H9   sing N N 474 
UZ6 C23 H10  sing N N 475 
UZ6 C24 H37  sing N N 476 
UZ6 C27 H38  sing N N 477 
UZ6 N13 H40  sing N N 478 
UZ6 N13 H39  sing N N 479 
UZ6 N6  H24  sing N N 480 
UZ6 N6  H23  sing N N 481 
UZ6 N8  H6   sing N N 482 
UZ6 N8  H4   sing N N 483 
UZ6 O2  H20  sing N N 484 
UZ6 O6  H36  sing N N 485 
VAL N   CA   sing N N 486 
VAL N   H    sing N N 487 
VAL N   H2   sing N N 488 
VAL CA  C    sing N N 489 
VAL CA  CB   sing N N 490 
VAL CA  HA   sing N N 491 
VAL C   O    doub N N 492 
VAL C   OXT  sing N N 493 
VAL CB  CG1  sing N N 494 
VAL CB  CG2  sing N N 495 
VAL CB  HB   sing N N 496 
VAL CG1 HG11 sing N N 497 
VAL CG1 HG12 sing N N 498 
VAL CG1 HG13 sing N N 499 
VAL CG2 HG21 sing N N 500 
VAL CG2 HG22 sing N N 501 
VAL CG2 HG23 sing N N 502 
VAL OXT HXT  sing N N 503 
# 
_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                    8QG4 
_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]   0.015800 
_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]   0.013334 
_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]   0.008433 
_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.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 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   ? 12.06658 36.37211 25.64878  1.000 69.83970 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 11.26492 36.51091 24.43886  1.000 63.20808 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 10.18240 35.42444 24.33003  1.000 54.82695 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.95248  34.66143 25.26906  1.000 52.98680 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 12.18165 36.50123 23.21778  1.000 65.19923 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 13.49970 35.76231 23.43254  1.000 68.68546 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.56823 35.86225 21.97156  1.000 85.07380 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 16.18163 35.89833 22.75827  1.000 81.43032 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.47497  35.40132 23.20360  1.000 51.47787 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.50217  34.34733 22.95108  1.000 50.88383 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 9.24033  33.03680 22.71360  1.000 44.65283 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 10.25304 32.99774 22.00316  1.000 40.99052 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.62088  34.70593 21.74268  1.000 49.38743 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.71849  35.94461 21.96918  1.000 48.52728 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.70578  36.13353 20.81632  1.000 47.81022 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.90700  37.43273 20.87262  1.000 56.04858 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.77642  37.31273 21.83164  1.000 59.94963 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.75235  31.96294 23.33738  1.000 41.27343 ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.36121  30.64356 23.17031  1.000 34.28222 ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 8.25607  29.59400 23.17718  1.000 36.08616 ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 7.13051  29.85670 23.63596  1.000 39.04489 ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.38160 30.34138 24.29013  1.000 38.80429 ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.69407  30.00030 25.60402  1.000 38.05748 ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 9.22429  31.00191 26.45316  1.000 39.26219 ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.48795  28.67750 25.96515  1.000 35.89716 ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.56675  30.67828 27.64960  1.000 41.80064 ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.83831  28.33372 27.12812  1.000 36.07062 ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.38163  29.34636 27.98767  1.000 37.61981 ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.70006  29.02798 29.16176  1.000 40.65547 ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.58206  28.38876 22.68724  1.000 33.65826 ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.72301  27.24033 22.94727  1.000 33.11621 ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.59538  26.00813 23.13884  1.000 29.28086 ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.79006  26.01794 22.85964  1.000 30.54218 ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.65764  27.05703 21.86125  1.000 38.68378 ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.20348  26.70183 20.52310  1.000 34.24145 ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.46757  24.91639 20.39236  1.000 37.82272 ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.75945  24.34142 20.41729  1.000 39.96559 ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.98459  24.93194 23.63041  1.000 27.59997 ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.71099  23.69444 23.91680  1.000 28.83137 ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.89856  22.52070 23.40748  1.000 31.51632 ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.71317  22.39872 23.74558  1.000 30.88655 ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.97418  23.52489 25.43814  1.000 26.66871 ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.64385  24.76863 25.93901  1.000 27.45810 ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.86928  22.26448 25.63356  1.000 28.54097 ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 10.14245 24.64780 27.48422  1.000 31.03797 ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.50909  21.68369 22.54970  1.000 29.94033 ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.86864  20.45796 22.12178  1.000 27.68939 ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.45532  19.30559 22.89924  1.000 30.72169 ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.59280  19.36880 23.35761  1.000 37.71115 ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 8.08856  20.18499 20.61372  1.000 30.27935 ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 9.45087  19.80109 20.41196  1.000 34.10521 ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.83499  21.41465 19.78635  1.000 35.59258 ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.66984  18.25526 23.07019  1.000 33.90672 ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 8.10182  17.09037 23.81905  1.000 32.66079 ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.86601  15.83561 23.00177  1.000 35.80119 ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.82531  15.70241 22.35462  1.000 37.04476 ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.32926  16.97089 25.15103  1.000 33.82346 ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.60511  15.76383 25.82013  1.000 36.49811 ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.79785  14.88987 23.09689  1.000 33.55470 ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.55157  13.55378 22.55748  1.000 34.28633 ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.31261  12.89591 23.17975  1.000 39.72902 ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.73168  11.98367 22.59134  1.000 44.69731 ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.78471  12.67227 22.78112  1.000 40.99807 ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.47011  11.17567 22.80819  1.000 48.39675 ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.58007 10.29780 23.38181  1.000 52.32752 ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.62702 8.96253  22.60880  1.000 53.08754 ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 10.75409 9.18156  21.12252  1.000 54.00144 ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.90270  13.29971 24.36700  1.000 40.28924 ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.68213  12.72804 24.92092  1.000 40.34781 ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.81892  11.55952 25.88142  1.000 44.53553 ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.79705  11.09297 26.40546  1.000 49.77066 ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 7.01931  11.07565 26.15995  1.000 42.89785 ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.12381  10.20758 27.31656  1.000 44.85562 ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.09754  11.03860 28.59866  1.000 49.14410 ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.16247  12.27249 28.57413  1.000 45.79148 ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.38589  9.34392  27.27815  1.000 48.59642 ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.63764  10.14507 26.98594  1.000 52.54209 ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.59959  11.38696 27.07974  1.000 51.31595 ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.66396 9.53125  26.61676  1.000 59.75240 ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.02621  10.33540 29.73205  1.000 51.55671 ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 6.94656  11.01070 31.02465  1.000 51.65708 ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.17970  11.86166 31.29212  1.000 51.15604 ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.06812  12.96485 31.83878  1.000 54.31694 ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 6.76388  9.99473  32.14650  1.000 60.94202 ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.32950  9.71677  32.49680  0.700 64.33588 ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.22077  8.67399  33.56097  0.600 66.75312 ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.17447  8.57130  34.36085  0.600 70.56314 ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 4.19935  7.95209  33.58735  0.600 61.07493 ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.36904  11.34877 30.95862  1.000 45.47171 ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.59357 12.10510 31.20664  1.000 47.44318 ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.55507 13.44470 30.48361  1.000 43.06540 ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.83534 14.49708 31.07147  1.000 43.64712 ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.81839 11.29473 30.76936  0.800 48.38607 ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.14752 11.84550 31.30848  0.700 50.99491 ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.37829 11.13304 30.73916  0.700 51.55651 ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.66704 11.81054 31.23516  0.600 54.57940 ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 16.94324 11.16750 30.77257  0.600 52.21130 ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.16143 13.42645 29.21487  1.000 41.03661 ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.17100 14.63943 28.41008  1.000 39.51455 ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.07598  15.60867 28.82547  1.000 38.96996 ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.29535  16.82848 28.85349  1.000 34.77872 ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.01934 14.26049 26.93212  1.000 36.19766 ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.11465 13.42488 26.55587  1.000 42.30141 ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.88026  15.09741 29.11547  1.000 42.67681 ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.79551  15.99075 29.50562  1.000 38.95408 ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.12772  16.71481 30.79528  1.000 39.24586 ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.84132  17.90762 30.94868  1.000 37.74825 ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.50792  15.19343 29.65997  1.000 42.55488 ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.84358  14.89785 28.34871  1.000 47.46852 ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.31022  15.42091 27.30469  1.000 43.83354 ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.82938  14.15086 28.37149  1.000 52.62222 ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.71606  15.99124 31.74524  1.000 43.55106 ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.04569  16.56120 33.03858  1.000 44.11774 ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.14965  17.59882 32.90065  1.000 40.68940 ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.05587  18.68866 33.48744  1.000 39.09563 ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.45155  15.44563 33.99412  0.800 41.23112 ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.31651  14.48316 34.31894  0.700 48.72485 ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 7.83620  13.46016 35.31142  0.700 49.05406 ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 6.12481  15.24818 34.89381  0.700 47.86492 ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.18419 17.27748 32.12044  1.000 38.58092 ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.23803 18.24689 31.85089  1.000 38.72094 ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.64954 19.49694 31.20045  1.000 37.87253 ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 10.99617 20.62060 31.57380  1.000 34.41459 ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.32261 17.62374 30.94891  1.000 35.82596 ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.60568 18.45010 30.81048  1.000 37.10929 ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.19997 18.81701 32.14581  1.000 38.92293 ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.66149 17.70212 29.99570  1.000 37.23601 ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.71647  19.31485 30.26839  1.000 32.92688 ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.09402  20.47641 29.63619  1.000 33.05717 ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.30339  21.29859 30.66480  1.000 33.16277 ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.39754  22.53720 30.70374  1.000 33.09979 ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.21196  20.03192 28.46228  1.000 29.65375 ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.18532  21.07709 28.11150  1.000 31.44188 ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.44330  20.66038 26.79875  1.000 30.47647 ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.52536  21.70562 26.38660  1.000 32.21835 ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.32533  21.91873 26.89066  1.000 34.68898 ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.84533  21.19063 27.89310  1.000 36.48413 ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.57567  22.89228 26.37929  1.000 37.68044 ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.54162  20.63916 31.53277  1.000 33.95239 ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.78911  21.39228 32.54162  1.000 36.29237 ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.71546  22.15871 33.49283  1.000 35.58945 ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.41639  23.29090 33.91476  1.000 36.30547 ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.87184  20.44608 33.32672  1.000 40.87695 ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.57890  19.96022 32.66858  1.000 44.98980 ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.72886  19.28524 33.69862  1.000 41.20308 ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.80381  21.11620 31.99913  1.000 44.07619 ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.83766  21.54956 33.85081  1.000 36.97661 ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.78565  22.21598 34.73902  1.000 36.86214 ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.48595 23.38336 34.05497  1.000 35.94268 ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.75851 24.39764 34.70120  1.000 37.09003 ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.82013 21.22692 35.24520  1.000 37.80303 ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.41944 20.58816 36.54481  1.000 39.87949 ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.48424  21.03373 37.24267  1.000 40.88481 ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.11967 19.51084 36.88197  1.000 44.68251 ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.78913 23.26776 32.74251  1.000 34.85331 ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.39389 24.40513 32.06037  1.000 34.93906 ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.40286 25.55378 31.94389  1.000 35.69477 ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.77186 26.71298 32.11183  1.000 38.00777 ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.93718 23.99623 30.67709  1.000 31.98182 ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.16715 23.15268 30.80459  1.000 32.33475 ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.79266 22.70381 29.18409  1.000 36.46484 ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.78895 24.16743 28.80725  1.000 34.55795 ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.13899  25.24967 31.65223  1.000 35.49656 ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.12101  26.27845 31.62922  1.000 34.30031 ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 8.05991  26.97315 32.98092  1.000 36.31917 ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 8.02682  28.20241 33.07728  1.000 37.34438 ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.77217  25.65515 31.23505  1.000 35.38645 ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.86226  25.14425 29.78910  1.000 36.99533 ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.65622  26.67176 31.44396  1.000 36.42170 ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.59898  24.58577 29.36073  1.000 38.85392 ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.09998  26.20024 34.05505  1.000 38.33073 ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 8.01285  26.83935 35.35744  1.000 40.04009 ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.21305  27.75783 35.57014  1.000 39.96841 ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.06260  28.89039 36.03852  1.000 41.51321 ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.89362  25.77636 36.45480  1.000 40.29443 ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.39637 27.32888 35.11255  1.000 40.59423 ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.58557 28.15680 35.28470  1.000 44.45763 ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.57418 29.39180 34.40078  1.000 42.40896 ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 12.00185 30.47709 34.81667  1.000 44.62672 ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 11.03594 29.25944 33.19342  1.000 38.71876 ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.88678 30.43242 32.33859  1.000 43.26856 ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.89307  31.41432 32.92888  1.000 43.82354 ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 10.02986 32.62901 32.73346  1.000 47.22143 ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.44125 30.02571 30.93157  1.000 36.35334 ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.54728 29.48437 30.05414  1.000 41.33707 ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.72214 30.19174 29.86667  1.000 43.35346 ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.40269 28.26438 29.43196  1.000 38.90112 ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.72329 29.69723 29.07807  1.000 46.69525 ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.40236 27.74592 28.63439  1.000 38.07363 ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.57045 28.46334 28.45256  1.000 42.00596 ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.92710  30.92850 33.71500  1.000 45.32910 ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.99769  31.83565 34.33662  1.000 46.10344 ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.65345  32.81672 35.28757  1.000 48.06182 ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 8.05533  33.83362 35.61908  1.000 47.79040 ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.90063  32.56257 35.67937  1.000 51.83441 ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.63064 33.48353 36.53713  1.000 49.56988 ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.36600 34.58297 35.76817  1.000 51.49540 ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 12.04316 35.39431 36.41026  1.000 57.79222 ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.61957 32.70409 37.41829  1.000 52.08783 ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.95404 31.69176 38.36135  1.000 48.22327 ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.89783  32.30282 39.28245  1.000 49.89364 ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 10.02489 33.49716 39.73098  1.000 54.88746 ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.94435  31.55527 39.63157  1.000 51.59656 ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.19105 34.67075 34.43622  1.000 47.32137 ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.86488 35.62365 33.54707  1.000 54.01760 ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.85177 36.31114 32.61444  1.000 59.69353 ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.67474  35.93510 32.52163  1.000 54.65336 ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.97221 34.91918 32.70415  1.000 54.76612 ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 14.08706 34.31508 33.55884  1.000 56.10090 ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 15.16010 35.08311 33.99450  1.000 53.50725 ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 14.05163 32.98215 33.94822  1.000 54.02632 ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 16.17199 34.53673 34.80812  1.000 55.98029 ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 15.06763 32.41720 34.74400  1.000 45.73645 ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 16.12866 33.18650 35.16081  1.000 55.88937 ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 17.11218 32.61896 35.98202  1.000 58.20922 ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 11.32181 37.33631 31.90079  1.000 63.58459 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.48578 38.01262 30.91395  1.000 64.78571 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 10.33941 37.11181 29.69836  1.000 64.21502 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.94501 37.35671 28.64415  1.000 67.70413 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 11.08241 39.36241 30.50637  1.000 71.60743 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 10.16773 40.15259 29.59202  0.700 75.85801 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 8.95428  39.85435 29.54889  0.700 75.02119 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 10.66990 41.06829 28.90650  0.700 81.36915 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.57586  36.03646 29.84454  1.000 58.23160 ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.46062  35.06738 28.76897  1.000 56.61592 ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 8.00582  34.66793 28.65567  1.000 55.97199 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.36494  34.35222 29.65944  1.000 56.79154 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.34989 33.84292 29.01741  1.000 52.27901 ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.81214 34.18821 29.25444  1.000 56.99591 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.84226 34.15160 27.74786  1.000 60.46766 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 13.73607 35.71099 27.87697  1.000 71.04929 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.48518  34.69132 27.43821  1.000 48.19787 ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 6.07559  34.42358 27.19046  1.000 53.04526 ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.98771  33.13411 26.38553  1.000 48.29308 ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.67142  33.00000 25.36754  1.000 45.75175 ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.43837  35.60227 26.44876  1.000 58.05547 ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 4.01828  35.38811 25.97980  0.700 55.50634 ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.46077  36.62942 25.31817  0.700 57.53063 ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 4.22094  37.27931 24.57308  0.700 54.60220 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.28048  36.96616 25.56398  0.700 62.77414 ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.23043  32.15404 26.88650  1.000 45.70561 ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 5.00080  30.93236 26.10922  1.000 45.94569 ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 4.06258  31.24626 24.94744  1.000 44.75156 ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.93786  31.70617 25.16613  1.000 48.40253 ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.40021  29.83136 26.98626  1.000 44.91085 ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.41204  28.49151 26.29516  1.000 43.52564 ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.45116  28.14562 25.33212  1.000 42.32455 ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.41898  27.57710 26.55994  1.000 37.78686 ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.50161  26.92239 24.67024  1.000 38.57922 ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.48061  26.37750 25.93566  1.000 39.48016 ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.52205  26.02976 24.97839  1.000 38.95335 ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.67310  24.78925 24.37467  1.000 38.22603 ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.52414  31.02176 23.70850  1.000 43.70150 ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.71128  31.33611 22.53484  1.000 44.11056 ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 4.10712  30.35798 21.45001  1.000 41.28690 ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 5.24344  30.40814 20.94881  1.000 40.45870 ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.92511  32.78097 22.08930  1.000 49.09735 ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 3.07130  33.17506 20.88370  1.000 50.58197 ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.75959  32.34095 20.00481  1.000 49.76046 ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.73446  34.36623 20.81917  1.000 59.05166 ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 3.20386  29.43657 21.11687  1.000 42.15144 ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.54128  28.48855 20.05988  1.000 44.47353 ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.99788  28.92094 18.69807  1.000 43.18070 ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 3.10393  28.15559 17.73757  1.000 41.26672 ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 3.08449  27.06629 20.42290  1.000 39.71137 ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.59049  26.96109 20.60620  1.000 49.29364 ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.87546  27.90536 20.21305  1.000 51.62731 ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 1.11969  25.93122 21.15661  1.000 52.15797 ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.47995  30.14149 18.58122  1.000 44.42997 ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 2.14905  30.68270 17.26429  1.000 44.16357 ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.33370  31.42555 16.65503  1.000 45.78645 ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.70942  31.16430 15.51170  1.000 46.73449 ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.89454  31.57663 17.33395  1.000 48.04852 ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.67893  32.28136 15.98113  1.000 50.15879 ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.30003 30.73727 17.67128  1.000 49.91551 ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.95084  32.35285 17.39162  1.000 46.68606 ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 5.08589  33.13572 16.89044  1.000 45.97951 ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 6.25264  33.09322 17.87833  1.000 42.67491 ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.71588  34.12920 18.36032  1.000 47.44582 ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.66734  34.57876 16.59927  1.000 49.34948 ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 4.19541  34.84472 15.14528  0.800 51.18927 ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 3.88124  36.33122 14.87580  0.700 55.83045 ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 3.00134  36.89338 15.55285  0.700 57.49360 ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 4.52251  36.93675 13.98878  0.700 59.10771 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.77671  31.90486 18.17369  1.000 45.19045 ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.98734  31.81669 19.00137  1.000 42.83314 ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 9.19586  32.46013 18.34512  1.000 43.14266 ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 9.33272  32.48421 17.12121  1.000 42.41775 ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 8.20454  30.29940 19.16088  1.000 36.65069 ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.44146  29.66671 18.03466  1.000 41.56774 ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 6.26439  30.57709 17.78562  1.000 40.03004 ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 10.10180 32.96142 19.17720  1.000 39.83893 ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.43816 33.26676 18.68996  1.000 40.14472 ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.44609 32.18993 19.04691  1.000 38.28764 ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.50288 32.10431 18.40873  1.000 39.99388 ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.94203 34.58642 19.24629  1.000 43.29860 ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 11.03756 35.78448 19.12031  1.000 52.43609 ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 11.56722 36.91077 19.97598  0.700 55.95627 ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 12.77718 37.20283 19.88321  0.700 63.88489 ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.80287 37.46040 20.78383  0.700 56.38306 ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 12.11902 31.34252 20.01918  1.000 36.82706 ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.93836 30.21271 20.41818  1.000 31.85018 ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 12.05024 28.98822 20.45401  1.000 32.11180 ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.95266 29.04087 21.01398  1.000 32.82169 ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.56115 30.46378 21.80332  1.000 38.46417 ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 14.39361 31.73262 21.73714  1.000 42.03843 ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 14.41697 29.27951 22.21291  1.000 36.26467 ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.74727 31.52794 21.11005  1.000 47.02871 ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.51332 27.90506 19.84075  1.000 31.95672 ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.81001 26.62716 19.81913  1.000 29.87591 ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.73954 25.59543 20.46261  1.000 28.61085 ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.83794 25.33048 19.95881  1.000 28.17881 ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.39944 26.22376 18.39542  1.000 29.05813 ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.88868 24.82127 18.37251  1.000 28.38091 ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.30895 27.21205 17.84841  1.000 27.92757 ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.33169 25.06400 21.62470  1.000 29.83290 ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 13.06765 24.01266 22.32270  1.000 28.69914 ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.39523 22.67659 22.06774  1.000 26.79357 ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.19796 22.51923 22.32012  1.000 29.01894 ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 13.10865 24.28046 23.84196  1.000 27.39200 ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.75805 25.63282 24.09915  1.000 28.69838 ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.87944 23.14546 24.54904  1.000 29.45624 ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.54035 26.11149 25.50647  1.000 32.74390 ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.17498 21.69814 21.62316  1.000 28.04607 ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.70293 20.35961 21.36349  1.000 25.20128 ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.26433 19.43246 22.43320  1.000 28.35377 ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.48156 19.33538 22.57346  1.000 32.52399 ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.19396 19.91698 19.95498  1.000 26.12445 ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.65308 18.67453 19.66777  1.000 34.15526 ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.40174 18.70339 23.13794  1.000 29.19345 ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.85839 17.77087 24.17124  1.000 25.87387 ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.55443 16.36215 23.71839  1.000 31.48371 ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.38335 15.95214 23.68876  1.000 29.72730 ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.19912 18.01928 25.52967  1.000 28.73035 ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.42789 19.48072 25.91309  1.000 29.32390 ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.80120 17.00281 26.51494  1.000 32.80471 ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 11.89986 19.92449 27.27558  1.000 29.89533 ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.60003 15.60211 23.38318  1.000 29.95447 ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.33424 14.28151 22.87696  1.000 34.23334 ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.55582 13.68041 22.24194  1.000 36.74102 ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.54967 13.39879 22.93072  1.000 41.17100 ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.42612 13.39664 20.95999  1.000 30.48130 ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.48393 12.81874 20.16652  1.000 32.91053 ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.54834 13.61542 18.88970  1.000 29.06575 ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.90771 14.66254 18.77942  1.000 27.10680 ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.26714 13.09575 17.88491  1.000 30.73799 ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.37298 13.80979 16.63273  1.000 29.26747 ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 15.04693 13.81905 15.86979  1.000 28.02550 ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.76053 14.77179 15.12141  1.000 28.27900 ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.49262 13.15570 15.82229  1.000 23.46612 ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.87638 13.60123 16.23991  1.000 26.34883 ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 19.00284 14.75124 16.73682  1.000 29.06891 ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.81995 12.80238 16.09791  1.000 30.66804 ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.25720 12.73760 15.99589  1.000 27.30809 ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.92859 12.72827 15.40747  1.000 29.82048 ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 12.05821 13.84822 15.93707  1.000 28.22403 ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.35899 14.51755 15.17361  1.000 26.94660 ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 12.09406 14.06713 17.27524  1.000 28.54194 ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.38766 15.18504 17.87449  1.000 25.38399 ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.87032 16.49586 17.30583  1.000 23.90564 ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 11.05926 17.38914 17.02573  1.000 24.71227 ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.58207 15.15316 19.40121  1.000 27.61433 ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.28598 13.82731 19.85395  1.000 31.34384 ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.63640 16.12793 20.03367  1.000 27.67832 ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.19544 16.63227 17.14419  1.000 23.54676 ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.74800 17.86187 16.62167  1.000 27.79205 ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.27743 18.09642 15.18973  1.000 24.59595 ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.88574 19.21329 14.83198  1.000 25.71172 ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.27605 17.84753 16.68119  1.000 27.30249 ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.85945 19.19085 16.37826  1.000 28.00289 ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 16.15712 19.57388 15.05557  1.000 26.83054 ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 16.05678 20.11005 17.40063  1.000 30.48510 ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.64370 20.83334 14.77847  1.000 29.56739 ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.56715 21.36662 17.15006  1.000 29.88061 ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.86900 21.76212 15.82996  1.000 29.87084 ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.27471 17.04334 14.38234  1.000 25.83338 ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.84241 17.18792 12.99562  1.000 27.17354 ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.38769 17.60988 12.93424  1.000 26.80170 ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 11.00843 18.44192 12.11118  1.000 26.35758 ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 13.04759 15.87825 12.24708  1.000 26.41444 ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.48893 15.54519 11.87885  1.000 28.66550 ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.57480 14.13432 11.35490  1.000 29.31150 ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.97102 16.54164 10.88157  1.000 24.67638 ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.55505 17.07829 13.84463  1.000 28.88645 ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 9.15573  17.48186 13.85499  1.000 28.08611 ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.99721  18.94797 14.23673  1.000 29.64724 ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.12046  19.63655 13.70988  1.000 28.96110 ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.36321  16.56970 14.79731  1.000 32.53993 ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.06368  15.38790 14.08180  1.000 38.36477 ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.82061  19.43449 15.16925  1.000 25.96862 ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.76479  20.84127 15.53756  1.000 28.68388 ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.15883 21.70431 14.36116  1.000 27.92613 ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.53574  22.73544 14.11055  1.000 26.61665 ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.70483 21.11787 16.71674  1.000 29.42650 ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.21068 21.29518 13.64488  1.000 26.99572 ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.63028 22.03953 12.45999  1.000 28.87392 ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.47489 22.16937 11.47459  1.000 26.54301 ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 10.15577 23.26703 10.98889  1.000 29.90753 ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.82221 21.32795 11.82826  1.000 23.80085 ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 13.14594 21.81641 10.43602  1.000 26.59731 ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.72234 23.06793 10.25027  1.000 29.52222 ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.88904 21.03340 9.38293   1.000 26.64718 ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 14.04300 23.50127 8.96658   1.000 30.28898 ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 13.19369 21.45874 8.08282   1.000 27.51849 ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.76486 22.70119 7.89933   1.000 29.02474 ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.80041  21.06240 11.20624  1.000 25.93524 ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.73326  21.12465 10.20520  1.000 27.74277 ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.51761  21.87595 10.72356  1.000 30.54373 ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.78735  22.48888 9.94306   1.000 32.82728 ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.40386  19.71954 9.75828   1.000 24.64656 ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.45515  19.16894 8.84615   1.000 28.00740 ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.60965  19.66056 7.56539   1.000 30.87685 ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.47725 18.31072 9.05569   1.000 27.18289 ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.64148 19.06044 6.99030   1.000 28.82262 ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.19823 18.24717 7.87588   1.000 26.38827 ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.29645  21.87188 12.03991  1.000 28.14620 ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 6.17099  22.61816 12.58258  1.000 28.90560 ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.36388  24.10563 12.36253  1.000 33.06816 ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.37896  24.84614 12.28253  1.000 37.25471 ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.99446  22.29946 14.08995  1.000 33.86334 ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.85786  23.02335 14.76698  1.000 37.25800 ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.68102  22.60889 16.26853  1.000 40.95471 ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.27053  21.61694 16.73862  1.000 39.49740 ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.85562  23.36837 17.00393  1.000 44.14316 ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.61425  24.56832 12.23159  1.000 32.71118 ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.86312  26.00391 12.09898  1.000 34.94324 ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.60020  26.34685 10.81121  1.000 35.54939 ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.28099  27.37635 10.73231  1.000 32.82588 ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.60913  26.53122 13.31880  1.000 32.49479 ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.69123  26.46421 14.52208  1.000 34.95525 ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.74984  27.44777 14.74169  1.000 34.26568 ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.73375  25.39087 15.40075  1.000 35.47518 ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.85868  27.38430 15.82813  1.000 37.47691 ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.86239  25.31750 16.48612  1.000 36.52170 ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.92881  26.31039 16.69564  1.000 36.68295 ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 5.07383  26.22440 17.79485  1.000 36.54710 ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.44818  25.50986 9.78067   1.000 34.39430 ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.27800  25.72059 8.59372   1.000 39.23739 ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.92993  26.99834 7.84026   1.000 35.88331 ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.68443  27.40671 6.94617   1.000 42.58122 ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.18871  24.51707 7.65853   1.000 34.07479 ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.80256  24.09842 7.23946   0.800 35.80607 ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.91642  23.03747 6.15946   0.700 42.43967 ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.49984  21.97289 6.43423   0.700 35.33207 ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 7.48609  23.30510 5.01673   0.700 47.61436 ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.82757  27.63765 8.16888   1.000 36.04477 ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.45967  28.89121 7.53422   1.000 40.70934 ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.97111  30.11808 8.28203   1.000 44.17774 ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.76908  31.24197 7.80744   1.000 41.17211 ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.93892  28.95387 7.39083   1.000 47.54680 ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.42020  27.85783 6.46332   1.000 51.45059 ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 5.99406  27.97793 5.03451   0.700 54.52940 ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 6.09010  29.12122 4.50613   0.700 54.15909 ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 6.35619  26.93006 4.44169   0.700 55.47809 ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.60236  29.95101 9.45110   1.000 38.88612 ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 9.13966  31.09381 10.18318  1.000 38.69751 ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.60165 30.85590 10.56165  1.000 43.33865 ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 11.08901 31.33354 11.59798  1.000 39.45741 ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.29104  31.40931 11.42722  1.000 39.75351 ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 7.06410  32.28461 11.07245  1.000 47.52769 ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 6.18545  32.80639 12.25700  1.000 52.40848 ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.90181  33.68777 13.17324  1.000 48.69881 ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.51073  33.26249 14.28340  1.000 50.76319 ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.48596  31.98643 14.64130  1.000 48.40155 ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 8.18497  34.12958 15.03392  1.000 47.78820 ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.33695 30.13832 9.71333   1.000 40.75635 ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.69525 29.78254 10.07594  1.000 35.71272 ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.59462 30.98516 10.20474  1.000 37.79780 ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.61947 30.90301 10.88051  1.000 42.97054 ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.30658 28.82775 9.04870   1.000 31.70763 ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.58516 27.49669 8.91732   1.000 32.99839 ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.20051 26.82182 7.69685   1.000 36.24404 ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.76204 26.60531 10.13848  1.000 30.99548 ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.25534 32.09877 9.58851   1.000 37.25819 ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 14.14173 33.23309 9.75760   1.000 41.75878 ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.87846 33.98643 11.05523  1.000 46.71976 ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.67476 34.84399 11.44039  1.000 48.02555 ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 14.02583 34.15637 8.54524   1.000 49.79170 ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 15.36914 34.45645 7.94906   0.700 51.65806 ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 16.02238 33.51234 7.45579   0.700 51.46553 ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.79212 35.62812 8.01799   0.700 61.60410 ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.79959 33.66579 11.74129  1.000 40.59959 ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.42256 34.33177 12.96467  1.000 40.56000 ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.74669 33.51191 14.20837  1.000 40.96601 ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.52583 34.00421 15.31469  1.000 40.90345 ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 10.92531 34.65571 12.94265  1.000 43.31657 ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.52310 35.81121 12.06212  0.700 45.84085 ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 10.35454 35.41133 10.61878  0.700 48.74212 ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 9.99645  34.24193 10.35008  0.700 49.38021 ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 10.58476 36.26766 9.74552   0.700 54.16720 ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.27817 32.30164 14.05558  1.000 38.16132 ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.34415 31.31893 15.13259  1.000 39.91777 ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.77129 30.82757 15.33411  1.000 34.57386 ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.46668 30.50524 14.37372  1.000 34.85128 ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.43251 30.12854 14.80484  1.000 33.68132 ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.97725 30.59737 14.83922  1.000 36.36659 ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.77944 28.89958 15.69946  1.000 33.65984 ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 10.00306 29.50283 14.62120  1.000 38.86726 ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 15.18891 30.68217 16.59088  1.000 34.47838 ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.36783 29.87253 16.88161  1.000 31.46435 ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.92770 28.60583 17.59799  1.000 30.30024 ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.15467 28.68894 18.56633  1.000 33.82759 ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.37510 30.64033 17.73269  1.000 36.83450 ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.47707 27.46543 17.17297  1.000 29.29895 ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 16.14273 26.13281 17.67861  1.000 27.53593 ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.17218 25.65023 18.69801  1.000 29.76770 ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.35778 25.93768 18.56537  1.000 30.32300 ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 16.08105 25.12205 16.52801  1.000 29.24343 ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.88784 25.25789 15.68337  1.000 28.12060 ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 13.77553 24.52378 15.94684  1.000 28.45789 ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 14.89143 26.10145 14.53081  1.000 28.28750 ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 12.64997 24.63088 15.14469  1.000 28.25797 ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 13.76702 26.24822 13.74681  1.000 29.92036 ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.64209 25.49424 14.02025  1.000 30.83435 ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.70731 24.90081 19.71214  1.000 27.99410 ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.57736 24.21810 20.67317  1.000 28.66632 ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 17.02540 22.81362 20.88822  1.000 28.41329 ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.82493 22.65692 21.15506  1.000 31.29265 ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.63194 24.96396 22.02318  1.000 33.58482 ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 18.01365 26.41529 21.82451  1.000 32.35067 ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.62391 24.28510 22.95963  1.000 34.97387 ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.87833 27.19885 23.10485  1.000 38.58240 ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.90686 21.81575 20.92419  1.000 28.10569 ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.50694 20.43410 21.16787  1.000 26.35993 ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 18.08753 19.89240 22.46386  1.000 32.92572 ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.26705 20.09500 22.76229  1.000 34.93340 ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.22073 19.27253 23.26899  1.000 26.20754 ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.62955 18.56729 24.48053  1.000 28.69870 ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.38431 17.09516 24.24140  1.000 31.07344 ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.26867 16.73466 23.87080  1.000 33.70189 ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.78871 19.02298 25.69405  1.000 28.22957 ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 17.00377 20.50023 25.97626  1.000 32.42280 ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 17.06757 18.10244 26.84815  1.000 33.71561 ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.12647 21.01303 27.14721  1.000 35.81484 ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.37395 16.22704 24.49526  1.000 31.09972 ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.17585 14.80616 24.22017  1.000 35.08372 ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.91022 14.09759 25.52678  1.000 44.39354 ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.68552 14.23061 26.48076  1.000 45.95433 ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.34992 14.15345 23.47404  1.000 41.54453 ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.64843 14.23976 24.20075  1.000 49.52984 ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.55613 15.25405 23.98608  1.000 46.33963 ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.18374 13.45178 25.16084  1.000 53.00546 ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.60367 15.07787 24.77796  1.000 50.20654 ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.40263 13.98891 25.49573  1.000 51.69717 ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.77831 13.40476 25.59704  1.000 43.86122 ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.43960 12.69996 26.82448  1.000 46.95345 ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.77445 11.21949 26.73120  1.000 53.02220 ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 16.86871 10.55304 27.77053  1.000 58.83852 ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.95399 12.90796 27.22220  1.000 46.44307 ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.08567 12.79632 26.09390  1.000 48.06368 ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.73646 14.28658 27.91371  1.000 47.28192 ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 17.02716 10.72086 25.52041  1.000 54.86258 ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.70010 9.45625  25.31315  1.000 57.43882 ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 19.18081 9.65427  25.06452  1.000 60.42507 ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.79256 10.61533 25.53924  1.000 58.52753 ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.77640 8.74144  24.31081  1.000 60.31797 ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 21.18373 8.93056  24.00100  1.000 66.93642 ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.36569 10.15285 23.09228  1.000 63.13195 ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.40201 10.70033 22.54821  1.000 62.99724 ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.76069 7.63777  23.42504  0.900 67.28774 ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 21.96512 6.58817  24.48061  0.800 70.44391 ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 21.02205 6.32924  25.45642  0.800 75.84352 ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 23.02387 5.79383  24.76640  0.800 72.10064 ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 21.47691 5.39920  26.27660  0.800 73.89455 ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 22.68961 5.05558  25.87909  0.800 78.34345 ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.60958 10.63927 23.02701  1.000 60.21331 ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 22.94208 11.86070 22.29216  1.000 60.63722 ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.30539 11.85196 20.90027  1.000 59.00799 ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.49647 10.91373 20.12439  1.000 58.14076 ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.47569 12.01124 22.18529  1.000 61.82336 ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 25.08104 13.19040 21.38446  1.000 63.12262 ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 24.71914 14.57143 21.98729  1.000 60.61199 ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.61014 13.06487 21.16735  1.000 50.05784 ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 21.49846 12.87809 20.63463  1.000 50.13981 ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 20.96661 13.12019 19.32191  1.000 40.55164 ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 21.85938 14.14242 18.64979  1.000 44.84929 ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 22.56182 14.90940 19.30670  1.000 43.91855 ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 21.87818 14.11449 17.32400  1.000 32.31163 ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.79013 14.97842 16.62556  1.000 29.63934 ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.31653 16.41738 16.58314  1.000 36.98842 ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.13639 17.33330 16.45954  1.000 42.75163 ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 22.97382 14.45198 15.17246  1.000 30.71345 ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.36139 14.26516 14.85954  1.000 32.55969 ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 25.00738 13.11232 15.20120  1.000 32.86159 ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.06108 15.31271 14.35367  1.000 42.96854 ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 26.38453 12.96479 14.97343  1.000 44.61003 ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.37358 15.20674 14.11209  1.000 33.54173 ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 27.08089 14.03864 14.41100  1.000 39.49316 ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 21.02450 16.65439 16.63850  1.000 27.77129 ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.57234 18.01371 16.72621  1.000 24.48566 ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 20.45499 18.45475 18.22163  1.000 31.07237 ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.10083 19.59285 18.49594  1.000 39.72908 ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.29536 18.19066 15.94954  1.000 25.32707 ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.52034 17.97300 14.45524  1.000 28.11929 ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.37312 18.80233 13.75573  1.000 27.21115 ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.90269 16.92860 13.77204  1.000 26.03537 ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.60482 18.61545 12.36754  1.000 25.59302 ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 19.14436 16.70570 12.39886  1.000 23.50748 ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.98348 17.56106 11.70462  1.000 28.09511 ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.21720 17.35961 10.32620  1.000 24.12635 ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 20.86019 17.60630 19.16242  1.000 37.11210 ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 20.84754 17.92198 20.60853  1.000 35.16347 ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 22.15084 18.58883 21.06443  1.000 37.28517 ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 23.26034 18.10806 20.77640  1.000 40.22472 ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 20.60720 16.62609 21.37817  1.000 28.90253 ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 22.03132 19.71632 21.76836  1.000 44.64495 ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 23.20038 20.30141 22.43723  1.000 42.64709 ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 23.23772 20.09814 23.93763  1.000 46.34255 ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.28186 20.36581 24.55337  1.000 49.27395 ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.27028 21.80670 22.19550  1.000 44.99288 ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.45823 22.13157 20.73408  0.600 42.88695 ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 24.00251 21.25068 20.00951  0.600 41.36484 ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 23.05153 23.25270 20.34429  0.600 40.34540 ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 22.11697 19.71499 24.54088  1.000 41.35038 ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.99809 19.68676 25.97811  1.000 47.07202 ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.47000 18.33606 26.41594  1.000 41.28292 ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.64028 17.72712 25.74508  1.000 37.03787 ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 21.08107 20.83766 26.47637  1.000 46.70533 ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.59108 22.17121 26.04681  0.700 46.48810 ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.34876 22.79515 24.85200  0.700 45.35878 ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.47769 23.02989 26.77793  0.700 48.05332 ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.02123 23.99913 24.80510  0.700 44.60392 ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.73191 24.15878 25.96491  0.700 48.36965 ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 23.07872 22.95899 28.04829  0.700 45.35001 ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.56127 25.20829 26.37432  0.700 48.67030 ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.91047 23.99943 28.44810  0.700 49.65848 ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 24.13442 25.11198 27.61684  0.700 50.01367 ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 21.93498 17.90429 27.54077  1.000 40.32099 ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.41129 16.80464 28.33460  1.000 42.39840 ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.34119 17.33322 29.27749  1.000 45.61942 ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.34036 18.51355 29.61340  1.000 42.98106 ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.52619 16.15510 29.16151  1.000 49.78344 ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 23.66185 15.55966 28.32184  1.000 56.99318 ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 24.93688 15.42496 29.14986  0.800 50.07689 ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.70853 14.70315 30.38494  0.700 58.50482 ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 24.92346 15.21155 31.58957  0.700 62.92565 ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 25.36519 16.44839 31.74581  0.700 66.19962 ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 24.70882 14.45482 32.66328  0.700 64.30964 ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.40869 16.49135 29.68554  1.000 43.32395 ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.33623 16.97831 30.56652  1.000 47.74948 ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 18.86925 17.64643 31.81682  1.000 50.62512 ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.24761 18.58530 32.33460  1.000 49.61045 ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.54440 15.70019 30.87227  1.000 44.31809 ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 17.75944 14.84314 29.65585  1.000 48.49861 ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.21449 15.08366 29.29781  1.000 45.87384 ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.03867 17.21863 32.29263  1.000 48.97103 ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.58272 17.75868 33.52502  1.000 55.75299 ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 20.99957 19.21107 33.37792  1.000 51.47703 ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.08492 19.90154 34.39131  1.000 59.64025 ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.76350 16.90904 34.00940  1.000 59.04684 ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.19912 19.70120 32.16138  1.000 50.88882 ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.56069 21.09632 31.93437  1.000 52.84426 ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.35609 21.99887 31.65693  1.000 53.30230 ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.54296 23.15104 31.24726  1.000 50.70283 ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.54942 21.19710 30.77414  1.000 57.34256 ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 23.91069 20.60324 31.10992  1.000 64.55084 ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.66369 20.07134 29.91711  1.000 52.23017 ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 24.03706 19.55914 28.95286  1.000 52.11324 ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 25.90573 20.14822 29.95407  1.000 60.72547 ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.12932 21.51417 31.86768  1.000 49.69386 ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 17.96391 22.31600 31.50210  1.000 48.07757 ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 17.92222 23.62443 32.28321  1.000 49.35770 ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.65714 24.69001 31.71579  1.000 45.86387 ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.68498 21.51192 31.72577  1.000 52.66438 ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.18781 23.57389 33.59073  1.000 47.87927 ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.11456 24.80684 34.37150  1.000 51.42573 ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.17757 25.78693 33.90748  1.000 53.98653 ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.92634 27.00030 33.81264  1.000 50.40675 ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.26599 24.51372 35.86704  1.000 55.70693 ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.09669 23.71587 36.41840  1.000 59.77332 ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 15.96162 23.90490 35.92315  1.000 60.71703 ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.31362 22.90700 37.34674  1.000 67.65650 ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.37105 25.27256 33.59591  1.000 51.10959 ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.41877 26.14295 33.08661  1.000 55.67472 ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.97290 26.77441 31.77509  1.000 52.57842 ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.18645 27.96887 31.54193  1.000 55.33106 ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.72886 25.35452 32.94791  1.000 53.08467 ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.28144 25.99172 30.93580  1.000 48.28467 ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.75483 26.47493 29.66756  1.000 50.98783 ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.72548 27.58464 29.86120  1.000 51.18110 ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.75437 28.60454 29.15828  1.000 53.63608 ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.13755 25.29501 28.91570  1.000 45.45695 ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.80756 25.51401 27.46339  1.000 46.94010 ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.01334 26.09155 26.77767  1.000 49.57110 ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.50254 24.15212 26.87358  1.000 44.23783 ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.75510 27.36406 30.75364  1.000 46.00218 ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.73351 28.36825 31.02997  1.000 47.23437 ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.38953 29.70592 31.34516  1.000 49.02826 ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 17.07897 30.73795 30.74016  1.000 55.11412 ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.85465 27.90091 32.20770  1.000 48.21602 ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 15.08455 29.08763 32.83691  1.000 46.55983 ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.93831 26.75522 31.75492  1.000 43.97529 ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.31982 29.68846 32.29896  1.000 50.49641 ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 19.02234 30.89862 32.70145  1.000 53.77626 ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.75386 31.54098 31.52507  1.000 60.60359 ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 19.71470 32.76678 31.35573  1.000 63.89596 ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.98203 30.55797 33.84017  1.000 58.17509 ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 20.66744 31.74120 34.47396  1.000 55.98480 ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 21.39547 31.31039 35.73345  1.000 57.92831 ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 22.40431 32.34232 36.18301  1.000 60.14399 ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 22.75572 32.09089 37.60800  1.000 61.77964 ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.43045 30.74037 30.69662  1.000 58.72669 ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 21.21755 31.35652 29.63212  1.000 57.33669 ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 20.31695 31.94391 28.55567  1.000 56.79572 ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.54102 33.07374 28.10648  1.000 59.28349 ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.20267 30.34972 29.03906  1.000 60.50143 ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.37105 30.01458 29.96667  1.000 59.19039 ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 24.32154 29.02095 29.30523  1.000 63.01985 ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 24.10307 31.28509 30.44902  1.000 67.10449 ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 19.27747 31.20490 28.15086  1.000 54.34742 ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.32330 31.73905 27.19009  1.000 52.56109 ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.66974 32.99342 27.71958  1.000 63.54979 ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 17.44032 33.94879 26.96840  1.000 66.67316 ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.25913 30.70710 26.87605  1.000 54.70313 ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 17.53117 29.84368 25.65292  1.000 58.47799 ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 16.53518 28.68526 25.61208  1.000 58.29295 ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 17.52533 30.65530 24.32314  1.000 56.63264 ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 17.33013 32.98653 29.01057  1.000 59.66038 ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 16.69539 34.11767 29.66097  1.000 64.79972 ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 17.45520 35.38740 29.32369  1.000 69.42221 ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.93644 36.25534 28.60845  1.000 72.29463 ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 16.63781 33.89712 31.16718  1.000 64.10128 ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 18.70153 35.48246 29.79594  1.000 65.79881 ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 19.51703 36.64677 29.47021  1.000 71.63693 ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 19.52549 36.90270 27.97166  1.000 72.04183 ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 19.34989 38.03784 27.52162  1.000 77.74853 ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.94475 36.46150 29.97730  1.000 76.74587 ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 21.96119 37.29455 29.19930  1.000 77.32958 ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 22.25500 38.62701 29.89205  1.000 77.11948 ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 20.99714 39.46045 30.11530  1.000 77.43712 ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 21.25894 40.56143 31.09511  1.000 78.99440 ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 19.69756 35.84787 27.18249  1.000 72.58297 ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.88973 35.99832 25.75766  1.000 72.14426 ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 21.34814 36.25396 25.44917  1.000 72.78736 ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 22.23103 35.64276 26.06133  1.000 71.72945 ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 21.61033 37.16042 24.50710  1.000 76.15023 ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 22.95106 37.54071 24.05962  1.000 81.57189 ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 23.74012 36.36749 23.46325  1.000 79.92506 ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 24.94671 36.51066 23.19066  1.000 82.05544 ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 23.75794 38.20500 25.19351  1.000 78.09105 ? 94  GLU A CB  1 
ATOM   741  N N   . TYR A 1 95  ? 23.09070 35.21637 23.25704  1.000 75.30608 ? 95  TYR A N   1 
ATOM   742  C CA  . TYR A 1 95  ? 23.69732 34.04000 22.64530  1.000 67.16841 ? 95  TYR A CA  1 
ATOM   743  C C   . TYR A 1 95  ? 23.94199 34.27894 21.16126  1.000 68.05520 ? 95  TYR A C   1 
ATOM   744  O O   . TYR A 1 95  ? 23.35898 35.17473 20.54428  1.000 71.12494 ? 95  TYR A O   1 
ATOM   745  C CB  . TYR A 1 95  ? 22.78726 32.81837 22.80633  1.000 63.28860 ? 95  TYR A CB  1 
ATOM   746  C CG  . TYR A 1 95  ? 21.35541 33.09441 22.37141  1.000 63.99189 ? 95  TYR A CG  1 
ATOM   747  C CD1 . TYR A 1 95  ? 20.98115 33.03182 21.03623  1.000 61.79703 ? 95  TYR A CD1 1 
ATOM   748  C CD2 . TYR A 1 95  ? 20.38897 33.45142 23.30180  1.000 69.30223 ? 95  TYR A CD2 1 
ATOM   749  C CE1 . TYR A 1 95  ? 19.68039 33.30162 20.64191  1.000 62.51261 ? 95  TYR A CE1 1 
ATOM   750  C CE2 . TYR A 1 95  ? 19.08948 33.71558 22.91573  1.000 68.58352 ? 95  TYR A CE2 1 
ATOM   751  C CZ  . TYR A 1 95  ? 18.74368 33.64428 21.59131  1.000 64.23210 ? 95  TYR A CZ  1 
ATOM   752  O OH  . TYR A 1 95  ? 17.44587 33.91166 21.23046  1.000 70.65228 ? 95  TYR A OH  1 
ATOM   753  N N   . GLN A 1 96  ? 24.78834 33.44667 20.57292  1.000 59.87208 ? 96  GLN A N   1 
ATOM   754  C CA  . GLN A 1 96  ? 25.02576 33.56372 19.14688  1.000 57.17638 ? 96  GLN A CA  1 
ATOM   755  C C   . GLN A 1 96  ? 24.26280 32.48038 18.39401  1.000 55.08705 ? 96  GLN A C   1 
ATOM   756  O O   . GLN A 1 96  ? 23.95470 31.41003 18.93013  1.000 54.23607 ? 96  GLN A O   1 
ATOM   757  C CB  . GLN A 1 96  ? 26.51716 33.50004 18.81842  1.000 59.80505 ? 96  GLN A CB  1 
ATOM   758  C CG  . GLN A 1 96  ? 26.84945 33.92386 17.36615  0.700 62.42818 ? 96  GLN A CG  1 
ATOM   759  C CD  . GLN A 1 96  ? 26.16500 35.22828 16.92000  0.700 60.77920 ? 96  GLN A CD  1 
ATOM   760  O OE1 . GLN A 1 96  ? 25.16722 35.21001 16.18277  0.700 53.71419 ? 96  GLN A OE1 1 
ATOM   761  N NE2 . GLN A 1 96  ? 26.70962 36.35939 17.36010  0.700 66.61390 ? 96  GLN A NE2 1 
ATOM   762  N N   . LYS A 1 97  ? 23.93452 32.78411 17.14666  1.000 50.33565 ? 97  LYS A N   1 
ATOM   763  C CA  . LYS A 1 97  ? 23.18853 31.86988 16.30969  1.000 46.16968 ? 97  LYS A CA  1 
ATOM   764  C C   . LYS A 1 97  ? 24.14541 31.27668 15.29066  1.000 47.64941 ? 97  LYS A C   1 
ATOM   765  O O   . LYS A 1 97  ? 25.07442 31.95458 14.84475  1.000 47.85804 ? 97  LYS A O   1 
ATOM   766  C CB  . LYS A 1 97  ? 22.02255 32.58287 15.61858  1.000 47.19402 ? 97  LYS A CB  1 
ATOM   767  C CG  . LYS A 1 97  ? 21.00874 33.20577 16.59132  0.800 44.59276 ? 97  LYS A CG  1 
ATOM   768  C CD  . LYS A 1 97  ? 19.91233 33.90190 15.82903  0.700 48.70486 ? 97  LYS A CD  1 
ATOM   769  C CE  . LYS A 1 97  ? 19.55927 35.20551 16.50691  0.600 44.84595 ? 97  LYS A CE  1 
ATOM   770  N NZ  . LYS A 1 97  ? 18.61923 36.02049 15.69137  0.600 50.26529 ? 97  LYS A NZ  1 
ATOM   771  N N   . VAL A 1 98  ? 23.96919 29.98388 15.00273  1.000 40.64467 ? 98  VAL A N   1 
ATOM   772  C CA  . VAL A 1 98  ? 24.68009 29.31644 13.92003  1.000 42.23060 ? 98  VAL A CA  1 
ATOM   773  C C   . VAL A 1 98  ? 23.63075 28.79969 12.95483  1.000 35.01119 ? 98  VAL A C   1 
ATOM   774  O O   . VAL A 1 98  ? 22.53244 28.39448 13.36511  1.000 34.78260 ? 98  VAL A O   1 
ATOM   775  C CB  . VAL A 1 98  ? 25.57856 28.15433 14.39580  1.000 43.68668 ? 98  VAL A CB  1 
ATOM   776  C CG1 . VAL A 1 98  ? 26.36475 28.55023 15.62257  1.000 46.60745 ? 98  VAL A CG1 1 
ATOM   777  C CG2 . VAL A 1 98  ? 24.75491 26.95767 14.68854  1.000 46.06005 ? 98  VAL A CG2 1 
ATOM   778  N N   . SER A 1 99  ? 23.98596 28.78231 11.66800  1.000 33.06337 ? 99  SER A N   1 
ATOM   779  C CA  . SER A 1 99  ? 23.05504 28.44689 10.61926  1.000 31.67540 ? 99  SER A CA  1 
ATOM   780  C C   . SER A 1 99  ? 23.55743 27.21122 9.88274   1.000 31.94014 ? 99  SER A C   1 
ATOM   781  O O   . SER A 1 99  ? 24.74717 27.10315 9.58169   1.000 33.30419 ? 99  SER A O   1 
ATOM   782  C CB  . SER A 1 99  ? 22.90156 29.62265 9.61654   1.000 40.92125 ? 99  SER A CB  1 
ATOM   783  O OG  . SER A 1 99  ? 22.37075 30.75289 10.28731  1.000 44.09519 ? 99  SER A OG  1 
ATOM   784  N N   . TYR A 1 100 ? 22.66366 26.31323 9.58710   1.000 30.15996 ? 100 TYR A N   1 
ATOM   785  C CA  . TYR A 1 100 ? 23.00614 25.17422 8.72485   1.000 29.15550 ? 100 TYR A CA  1 
ATOM   786  C C   . TYR A 1 100 ? 22.19730 25.24703 7.44276   1.000 27.57601 ? 100 TYR A C   1 
ATOM   787  O O   . TYR A 1 100 ? 21.06384 25.73154 7.46254   1.000 25.98955 ? 100 TYR A O   1 
ATOM   788  C CB  . TYR A 1 100 ? 22.65523 23.82575 9.34307   1.000 27.53929 ? 100 TYR A CB  1 
ATOM   789  C CG  . TYR A 1 100 ? 23.55708 23.37351 10.49015  1.000 27.35862 ? 100 TYR A CG  1 
ATOM   790  C CD1 . TYR A 1 100 ? 24.67149 24.10205 10.85593  1.000 32.60199 ? 100 TYR A CD1 1 
ATOM   791  C CD2 . TYR A 1 100 ? 23.27013 22.18824 11.17142  1.000 34.21275 ? 100 TYR A CD2 1 
ATOM   792  C CE1 . TYR A 1 100 ? 25.50915 23.67537 11.92143  1.000 35.80027 ? 100 TYR A CE1 1 
ATOM   793  C CE2 . TYR A 1 100 ? 24.08400 21.76657 12.25472  1.000 33.83160 ? 100 TYR A CE2 1 
ATOM   794  C CZ  . TYR A 1 100 ? 25.19678 22.50280 12.59541  1.000 35.16520 ? 100 TYR A CZ  1 
ATOM   795  O OH  . TYR A 1 100 ? 26.01329 22.07669 13.63532  1.000 42.04245 ? 100 TYR A OH  1 
ATOM   796  N N   . PRO A 1 101 ? 22.71546 24.70506 6.34176   1.000 28.56824 ? 101 PRO A N   1 
ATOM   797  C CA  . PRO A 1 101 ? 21.98189 24.77398 5.07729   1.000 24.01363 ? 101 PRO A CA  1 
ATOM   798  C C   . PRO A 1 101 ? 20.85877 23.75039 5.01625   1.000 27.02480 ? 101 PRO A C   1 
ATOM   799  O O   . PRO A 1 101 ? 20.87153 22.71742 5.70761   1.000 26.78579 ? 101 PRO A O   1 
ATOM   800  C CB  . PRO A 1 101 ? 23.06324 24.48209 4.01637   1.000 25.74776 ? 101 PRO A CB  1 
ATOM   801  C CG  . PRO A 1 101 ? 24.45639 24.66081 4.72594   1.000 24.86828 ? 101 PRO A CG  1 
ATOM   802  C CD  . PRO A 1 101 ? 24.09419 24.19393 6.17976   1.000 24.34674 ? 101 PRO A CD  1 
ATOM   803  N N   . LEU A 1 102 ? 19.87841 24.01970 4.12367   1.000 24.36051 ? 102 LEU A N   1 
ATOM   804  C CA  . LEU A 1 102 ? 18.73505 23.14210 3.94271   1.000 21.85797 ? 102 LEU A CA  1 
ATOM   805  C C   . LEU A 1 102 ? 18.60948 22.72607 2.47352   1.000 22.66089 ? 102 LEU A C   1 
ATOM   806  O O   . LEU A 1 102 ? 19.23266 23.32765 1.58978   1.000 22.59615 ? 102 LEU A O   1 
ATOM   807  C CB  . LEU A 1 102 ? 17.43031 23.82474 4.36111   1.000 23.39992 ? 102 LEU A CB  1 
ATOM   808  C CG  . LEU A 1 102 ? 17.48723 24.27333 5.84689   1.000 22.46390 ? 102 LEU A CG  1 
ATOM   809  C CD1 . LEU A 1 102 ? 16.34624 25.24794 6.12005   1.000 25.12993 ? 102 LEU A CD1 1 
ATOM   810  C CD2 . LEU A 1 102 ? 17.47403 23.02400 6.77548   1.000 25.07295 ? 102 LEU A CD2 1 
ATOM   811  N N   . LEU A 1 103 ? 17.76504 21.71145 2.23831   1.000 24.24536 ? 103 LEU A N   1 
ATOM   812  C CA  . LEU A 1 103 ? 17.54870 21.16591 0.89438   1.000 23.28900 ? 103 LEU A CA  1 
ATOM   813  C C   . LEU A 1 103 ? 16.12681 21.47804 0.41619   1.000 24.97932 ? 103 LEU A C   1 
ATOM   814  O O   . LEU A 1 103 ? 15.14228 21.19556 1.12180   1.000 23.61320 ? 103 LEU A O   1 
ATOM   815  C CB  . LEU A 1 103 ? 17.75373 19.65746 0.86849   1.000 22.00144 ? 103 LEU A CB  1 
ATOM   816  C CG  . LEU A 1 103 ? 17.40685 18.96941 -0.47126  1.000 23.35087 ? 103 LEU A CG  1 
ATOM   817  C CD1 . LEU A 1 103 ? 18.42417 19.30178 -1.54931  1.000 22.72841 ? 103 LEU A CD1 1 
ATOM   818  C CD2 . LEU A 1 103 ? 17.40020 17.48878 -0.16225  1.000 25.35327 ? 103 LEU A CD2 1 
ATOM   819  N N   . LYS A 1 104 ? 16.00588 22.04263 -0.79482  1.000 23.83070 ? 104 LYS A N   1 
ATOM   820  C CA  . LYS A 1 104 ? 14.70761 22.29460 -1.41315  1.000 26.49108 ? 104 LYS A CA  1 
ATOM   821  C C   . LYS A 1 104 ? 14.40756 21.17897 -2.41638  1.000 28.70181 ? 104 LYS A C   1 
ATOM   822  O O   . LYS A 1 104 ? 15.24473 20.86582 -3.25585  1.000 26.59711 ? 104 LYS A O   1 
ATOM   823  C CB  . LYS A 1 104 ? 14.69922 23.64218 -2.10929  1.000 29.02996 ? 104 LYS A CB  1 
ATOM   824  C CG  . LYS A 1 104 ? 13.36886 23.92978 -2.85560  1.000 31.06590 ? 104 LYS A CG  1 
ATOM   825  C CD  . LYS A 1 104 ? 13.44974 25.25752 -3.62083  0.800 31.26530 ? 104 LYS A CD  1 
ATOM   826  C CE  . LYS A 1 104 ? 12.15473 25.55681 -4.27255  0.700 35.31036 ? 104 LYS A CE  1 
ATOM   827  N NZ  . LYS A 1 104 ? 12.16266 26.95806 -4.75653  0.600 37.83886 ? 104 LYS A NZ  1 
ATOM   828  N N   . THR A 1 105 ? 13.26530 20.51141 -2.26054  1.000 26.50322 ? 105 THR A N   1 
ATOM   829  C CA  . THR A 1 105 ? 12.78100 19.53499 -3.22950  1.000 29.12994 ? 105 THR A CA  1 
ATOM   830  C C   . THR A 1 105 ? 11.55109 20.11043 -3.93964  1.000 29.50803 ? 105 THR A C   1 
ATOM   831  O O   . THR A 1 105 ? 10.62809 20.59051 -3.28412  1.000 28.73773 ? 105 THR A O   1 
ATOM   832  C CB  . THR A 1 105 ? 12.44833 18.21012 -2.53880  1.000 31.04584 ? 105 THR A CB  1 
ATOM   833  O OG1 . THR A 1 105 ? 13.61910 17.69580 -1.87049  1.000 30.07374 ? 105 THR A OG1 1 
ATOM   834  C CG2 . THR A 1 105 ? 11.95968 17.17244 -3.53171  1.000 29.56264 ? 105 THR A CG2 1 
ATOM   835  N N   . THR A 1 106 ? 11.53066 20.08925 -5.27535  1.000 27.04902 ? 106 THR A N   1 
ATOM   836  C CA  . THR A 1 106 ? 10.34153 20.49817 -6.01402  1.000 29.49319 ? 106 THR A CA  1 
ATOM   837  C C   . THR A 1 106 ? 9.82092  19.29808 -6.78411  1.000 33.63507 ? 106 THR A C   1 
ATOM   838  O O   . THR A 1 106 ? 10.58201 18.63871 -7.50323  1.000 31.39629 ? 106 THR A O   1 
ATOM   839  C CB  . THR A 1 106 ? 10.62882 21.68344 -6.96963  1.000 31.61733 ? 106 THR A CB  1 
ATOM   840  O OG1 . THR A 1 106 ? 11.17040 22.77151 -6.21117  1.000 33.76915 ? 106 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 106 ? 9.32940  22.14687 -7.68354  1.000 35.73576 ? 106 THR A CG2 1 
ATOM   842  N N   . VAL A 1 107 ? 8.52677  19.02055 -6.65099  1.000 30.67999 ? 107 VAL A N   1 
ATOM   843  C CA  . VAL A 1 107 ? 7.88482  17.92568 -7.36232  1.000 35.08907 ? 107 VAL A CA  1 
ATOM   844  C C   . VAL A 1 107 ? 6.90457  18.53703 -8.36210  1.000 39.37567 ? 107 VAL A C   1 
ATOM   845  O O   . VAL A 1 107 ? 5.95382  19.22972 -7.97075  1.000 40.23935 ? 107 VAL A O   1 
ATOM   846  C CB  . VAL A 1 107 ? 7.16265  16.97378 -6.39342  1.000 35.48894 ? 107 VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 107 ? 6.61045  15.80326 -7.11129  1.000 34.70898 ? 107 VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 107 ? 8.10478  16.49016 -5.31802  1.000 34.91712 ? 107 VAL A CG2 1 
ATOM   849  N N   . LYS A 1 108 ? 7.12956  18.28343 -9.63628  1.000 38.43794 ? 108 LYS A N   1 
ATOM   850  C CA  . LYS A 1 108 ? 6.24668  18.74359 -10.69639 1.000 39.37540 ? 108 LYS A CA  1 
ATOM   851  C C   . LYS A 1 108 ? 5.40283  17.58548 -11.21153 1.000 50.52022 ? 108 LYS A C   1 
ATOM   852  O O   . LYS A 1 108 ? 5.90142  16.45924 -11.32776 1.000 45.03114 ? 108 LYS A O   1 
ATOM   853  C CB  . LYS A 1 108 ? 7.05440  19.34032 -11.85405 1.000 48.58067 ? 108 LYS A CB  1 
ATOM   854  C CG  . LYS A 1 108 ? 7.85283  20.58315 -11.50155 0.700 44.51591 ? 108 LYS A CG  1 
ATOM   855  C CD  . LYS A 1 108 ? 8.30348  21.31525 -12.76988 0.700 57.49597 ? 108 LYS A CD  1 
ATOM   856  C CE  . LYS A 1 108 ? 8.80638  22.70578 -12.41920 0.700 59.24701 ? 108 LYS A CE  1 
ATOM   857  N NZ  . LYS A 1 108 ? 9.85867  22.57014 -11.36752 0.700 52.80047 ? 108 LYS A NZ  1 
ATOM   858  N N   . TYR A 1 109 ? 4.14608  17.90061 -11.62345 1.000 54.67795 ? 109 TYR A N   1 
ATOM   859  C CA  . TYR A 1 109 ? 3.13534  16.93549 -12.08672 1.000 55.65243 ? 109 TYR A CA  1 
ATOM   860  C C   . TYR A 1 109 ? 2.56834  17.15579 -13.49045 1.000 63.11862 ? 109 TYR A C   1 
ATOM   861  O O   . TYR A 1 109 ? 3.28056  17.53576 -14.42380 1.000 58.48616 ? 109 TYR A O   1 
ATOM   862  C CB  . TYR A 1 109 ? 1.92756  16.93812 -11.14613 1.000 56.05041 ? 109 TYR A CB  1 
ATOM   863  C CG  . TYR A 1 109 ? 2.30759  16.76850 -9.69511  1.000 53.94810 ? 109 TYR A CG  1 
ATOM   864  C CD1 . TYR A 1 109 ? 2.51487  15.51303 -9.16578  1.000 51.79885 ? 109 TYR A CD1 1 
ATOM   865  C CD2 . TYR A 1 109 ? 2.45062  17.87042 -8.84125  1.000 49.75675 ? 109 TYR A CD2 1 
ATOM   866  C CE1 . TYR A 1 109 ? 2.84289  15.34932 -7.85058  1.000 48.03485 ? 109 TYR A CE1 1 
ATOM   867  C CE2 . TYR A 1 109 ? 2.78412  17.71461 -7.51220  1.000 47.82776 ? 109 TYR A CE2 1 
ATOM   868  C CZ  . TYR A 1 109 ? 2.98963  16.44910 -7.02376  1.000 52.23074 ? 109 TYR A CZ  1 
ATOM   869  O OH  . TYR A 1 109 ? 3.33596  16.25592 -5.70367  1.000 50.32878 ? 109 TYR A OH  1 
ATOM   870  N N   . GLY A 1 110 ? 1.26790  16.89988 -13.64431 1.000 74.37973 ? 110 GLY A N   1 
ATOM   871  C CA  . GLY A 1 110 ? 0.57788  17.15090 -14.89042 1.000 63.39961 ? 110 GLY A CA  1 
ATOM   872  C C   . GLY A 1 110 ? -0.91895 17.42838 -14.82685 1.000 78.44278 ? 110 GLY A C   1 
ATOM   873  O O   . GLY A 1 110 ? -1.53467 17.76873 -15.85253 1.000 71.53040 ? 110 GLY A O   1 
ATOM   874  N N   . LYS A 1 114 ? 0.17548  22.44984 -10.17946 1.000 54.84650 ? 114 LYS A N   1 
ATOM   875  C CA  . LYS A 1 114 ? 0.88295  21.20291 -10.43163 1.000 57.15038 ? 114 LYS A CA  1 
ATOM   876  C C   . LYS A 1 114 ? 2.35565  21.24558 -9.98931  1.000 60.51968 ? 114 LYS A C   1 
ATOM   877  O O   . LYS A 1 114 ? 3.22835  20.75331 -10.73853 1.000 57.79448 ? 114 LYS A O   1 
ATOM   878  C CB  . LYS A 1 114 ? 0.82852  20.83365 -11.91803 1.000 56.33323 ? 114 LYS A CB  1 
ATOM   879  N N   . GLU A 1 115 ? 2.63845  21.80467 -8.80624  1.000 46.21695 ? 115 GLU A N   1 
ATOM   880  C CA  . GLU A 1 115 ? 4.00401  21.78899 -8.26644  1.000 46.50843 ? 115 GLU A CA  1 
ATOM   881  C C   . GLU A 1 115 ? 3.98574  21.93427 -6.75103  1.000 49.30773 ? 115 GLU A C   1 
ATOM   882  O O   . GLU A 1 115 ? 3.33603  22.83357 -6.21850  1.000 50.04811 ? 115 GLU A O   1 
ATOM   883  C CB  . GLU A 1 115 ? 4.82014  22.89617 -8.93457  1.000 54.82140 ? 115 GLU A CB  1 
ATOM   884  C CG  . GLU A 1 115 ? 6.03568  23.30214 -8.24743  1.000 48.64205 ? 115 GLU A CG  1 
ATOM   885  C CD  . GLU A 1 115 ? 6.88106  24.31573 -9.02704  1.000 57.18388 ? 115 GLU A CD  1 
ATOM   886  O OE1 . GLU A 1 115 ? 7.08748  24.14865 -10.25984 1.000 56.95222 ? 115 GLU A OE1 1 
ATOM   887  O OE2 . GLU A 1 115 ? 7.35952  25.27737 -8.36865  1.000 60.88741 ? 115 GLU A OE2 1 
ATOM   888  N N   . ALA A 1 116 ? 4.69225  21.04030 -6.05400  1.000 40.61976 ? 116 ALA A N   1 
ATOM   889  C CA  . ALA A 1 116 ? 4.80091  21.04558 -4.60513  1.000 41.21268 ? 116 ALA A CA  1 
ATOM   890  C C   . ALA A 1 116 ? 6.25996  21.25034 -4.22787  1.000 37.48546 ? 116 ALA A C   1 
ATOM   891  O O   . ALA A 1 116 ? 7.14301  20.70001 -4.88422  1.000 34.33310 ? 116 ALA A O   1 
ATOM   892  C CB  . ALA A 1 116 ? 4.31175  19.72309 -4.03197  1.000 41.50371 ? 116 ALA A CB  1 
ATOM   893  N N   . THR A 1 117 ? 6.53415  22.03000 -3.18205  1.000 34.19249 ? 117 THR A N   1 
ATOM   894  C CA  . THR A 1 117 ? 7.90020  22.14930 -2.69943  1.000 32.03434 ? 117 THR A CA  1 
ATOM   895  C C   . THR A 1 117 ? 7.98775  21.69626 -1.25403  1.000 37.46589 ? 117 THR A C   1 
ATOM   896  O O   . THR A 1 117 ? 7.02190  21.76471 -0.48987  1.000 33.06220 ? 117 THR A O   1 
ATOM   897  C CB  . THR A 1 117 ? 8.45542  23.57629 -2.81483  1.000 34.83165 ? 117 THR A CB  1 
ATOM   898  O OG1 . THR A 1 117 ? 7.63763  24.47861 -2.06461  1.000 42.78951 ? 117 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 117 ? 8.40518  24.02514 -4.24246  1.000 33.32973 ? 117 THR A CG2 1 
ATOM   900  N N   . TYR A 1 118 ? 9.18013  21.25255 -0.88067  1.000 33.28872 ? 118 TYR A N   1 
ATOM   901  C CA  . TYR A 1 118 ? 9.40716  20.71972 0.43670   1.000 28.26977 ? 118 TYR A CA  1 
ATOM   902  C C   . TYR A 1 118 ? 10.77902 21.16562 0.90081   1.000 30.71555 ? 118 TYR A C   1 
ATOM   903  O O   . TYR A 1 118 ? 11.73326 21.15975 0.12035   1.000 29.87017 ? 118 TYR A O   1 
ATOM   904  C CB  . TYR A 1 118 ? 9.37460  19.18669 0.43207   1.000 31.66467 ? 118 TYR A CB  1 
ATOM   905  C CG  . TYR A 1 118 ? 8.09862  18.64284 -0.06460  1.000 33.85861 ? 118 TYR A CG  1 
ATOM   906  C CD1 . TYR A 1 118 ? 7.00600  18.53631 0.78437   1.000 35.62796 ? 118 TYR A CD1 1 
ATOM   907  C CD2 . TYR A 1 118 ? 7.94746  18.29117 -1.40456  1.000 35.23215 ? 118 TYR A CD2 1 
ATOM   908  C CE1 . TYR A 1 118 ? 5.80220  18.07690 0.33480   1.000 37.10826 ? 118 TYR A CE1 1 
ATOM   909  C CE2 . TYR A 1 118 ? 6.70623  17.81298 -1.87967  1.000 37.98570 ? 118 TYR A CE2 1 
ATOM   910  C CZ  . TYR A 1 118 ? 5.64526  17.70917 -0.98263  1.000 38.69767 ? 118 TYR A CZ  1 
ATOM   911  O OH  . TYR A 1 118 ? 4.42601  17.23588 -1.39798  1.000 45.03367 ? 118 TYR A OH  1 
ATOM   912  N N   . LEU A 1 119 ? 10.92206 21.41712 2.20076   1.000 27.00012 ? 119 LEU A N   1 
ATOM   913  C CA  . LEU A 1 119 ? 12.23456 21.71153 2.74774   1.000 28.75071 ? 119 LEU A CA  1 
ATOM   914  C C   . LEU A 1 119 ? 12.69801 20.56196 3.63871   1.000 28.24223 ? 119 LEU A C   1 
ATOM   915  O O   . LEU A 1 119 ? 11.89239 20.01284 4.40217   1.000 26.20922 ? 119 LEU A O   1 
ATOM   916  C CB  . LEU A 1 119 ? 12.15818 23.01274 3.52821   1.000 33.39178 ? 119 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 119 ? 13.29622 23.95258 3.76460   1.000 37.46137 ? 119 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 119 ? 13.67666 24.57967 2.44089   1.000 34.36905 ? 119 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 119 ? 12.76448 25.00255 4.71689   1.000 36.65648 ? 119 LEU A CD2 1 
ATOM   920  N N   . ALA A 1 120 ? 13.95583 20.14846 3.49948   1.000 25.05874 ? 120 ALA A N   1 
ATOM   921  C CA  . ALA A 1 120 ? 14.51336 19.07261 4.33120   1.000 22.54040 ? 120 ALA A CA  1 
ATOM   922  C C   . ALA A 1 120 ? 15.71765 19.53881 5.15827   1.000 25.94548 ? 120 ALA A C   1 
ATOM   923  O O   . ALA A 1 120 ? 16.54563 20.33719 4.69300   1.000 21.09413 ? 120 ALA A O   1 
ATOM   924  C CB  . ALA A 1 120 ? 14.92541 17.84369 3.46556   1.000 27.49567 ? 120 ALA A CB  1 
ATOM   925  N N   . LEU A 1 121 ? 15.78365 19.06805 6.41645   1.000 24.78540 ? 121 LEU A N   1 
ATOM   926  C CA  . LEU A 1 121 ? 16.91206 19.26528 7.32697   1.000 20.18202 ? 121 LEU A CA  1 
ATOM   927  C C   . LEU A 1 121 ? 17.86624 18.09147 7.24091   1.000 23.58106 ? 121 LEU A C   1 
ATOM   928  O O   . LEU A 1 121 ? 19.07752 18.25797 7.41781   1.000 23.96326 ? 121 LEU A O   1 
ATOM   929  C CB  . LEU A 1 121 ? 16.41240 19.45184 8.78131   1.000 22.51488 ? 121 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 121 ? 17.52500 19.54041 9.82485   1.000 25.63157 ? 121 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 121 ? 18.44836 20.68513 9.60111   1.000 23.34025 ? 121 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 121 ? 16.80058 19.77566 11.16485  1.000 24.47176 ? 121 LEU A CD2 1 
ATOM   933  N N   . ASN A 1 122 ? 17.33206 16.87398 7.08310   1.000 19.87714 ? 122 ASN A N   1 
ATOM   934  C CA  . ASN A 1 122 ? 18.21375 15.74602 6.91042   1.000 18.25998 ? 122 ASN A CA  1 
ATOM   935  C C   . ASN A 1 122 ? 18.34469 15.40804 5.41659   1.000 19.40795 ? 122 ASN A C   1 
ATOM   936  O O   . ASN A 1 122 ? 19.43469 15.47636 4.87525   1.000 19.59363 ? 122 ASN A O   1 
ATOM   937  C CB  . ASN A 1 122 ? 17.69369 14.52981 7.61611   1.000 19.79190 ? 122 ASN A CB  1 
ATOM   938  C CG  . ASN A 1 122 ? 18.26347 14.39299 9.02120   1.000 24.68656 ? 122 ASN A CG  1 
ATOM   939  O OD1 . ASN A 1 122 ? 19.16517 15.14168 9.45453   1.000 24.61139 ? 122 ASN A OD1 1 
ATOM   940  N ND2 . ASN A 1 122 ? 17.80974 13.36512 9.68566   1.000 24.42012 ? 122 ASN A ND2 1 
ATOM   941  N N   . GLU A 1 123 ? 17.27187 14.93936 4.80749   1.000 20.60718 ? 123 GLU A N   1 
ATOM   942  C CA  . GLU A 1 123 ? 17.41290 14.51134 3.40284   1.000 21.02595 ? 123 GLU A CA  1 
ATOM   943  C C   . GLU A 1 123 ? 16.04929 14.37158 2.75282   1.000 23.26969 ? 123 GLU A C   1 
ATOM   944  O O   . GLU A 1 123 ? 15.02732 14.34952 3.40774   1.000 21.37804 ? 123 GLU A O   1 
ATOM   945  C CB  . GLU A 1 123 ? 18.15860 13.17341 3.27673   1.000 20.12893 ? 123 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 123 ? 17.31840 11.95479 3.73227   1.000 21.25629 ? 123 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 123 ? 17.20236 11.83615 5.28631   1.000 22.91864 ? 123 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 123 ? 18.31693 11.81395 5.88893   1.000 22.05738 ? 123 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 123 ? 16.06697 11.85987 5.80366   1.000 24.36060 ? 123 GLU A OE2 1 
ATOM   950  N N   . SER A 1 124 ? 16.06796 14.17987 1.43441   1.000 20.95464 ? 124 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 14.86966 13.80336 0.69245   1.000 21.88055 ? 124 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 15.25692 12.56956 -0.08579  1.000 22.97779 ? 124 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 16.31790 12.56013 -0.69980  1.000 23.43919 ? 124 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 14.44312 14.92338 -0.31198  1.000 26.54275 ? 124 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 13.35277 14.53319 -1.09956  1.000 27.19318 ? 124 SER A OG  1 
ATOM   956  N N   . THR A 1 125 ? 14.43987 11.53586 -0.05314  1.000 23.07362 ? 125 THR A N   1 
ATOM   957  C CA  . THR A 1 125 ? 14.75582 10.34670 -0.83661  1.000 19.22132 ? 125 THR A CA  1 
ATOM   958  C C   . THR A 1 125 ? 13.61689 10.06955 -1.80156  1.000 22.35044 ? 125 THR A C   1 
ATOM   959  O O   . THR A 1 125 ? 12.47096 10.49464 -1.62407  1.000 23.34890 ? 125 THR A O   1 
ATOM   960  C CB  . THR A 1 125 ? 14.99000 9.09462  0.04184   1.000 23.39032 ? 125 THR A CB  1 
ATOM   961  O OG1 . THR A 1 125 ? 13.76457 8.61993  0.60373   1.000 27.37447 ? 125 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 125 ? 15.97585 9.43361  1.16363   1.000 23.86793 ? 125 THR A CG2 1 
ATOM   963  N N   . VAL A 1 126 ? 13.92968 9.28634  -2.82238  1.000 22.91929 ? 126 VAL A N   1 
ATOM   964  C CA  . VAL A 1 126 ? 12.91766 8.88327  -3.78322  1.000 23.66261 ? 126 VAL A CA  1 
ATOM   965  C C   . VAL A 1 126 ? 13.07794 7.39233  -4.05418  1.000 21.69610 ? 126 VAL A C   1 
ATOM   966  O O   . VAL A 1 126 ? 14.20963 6.90158  -4.19583  1.000 22.87435 ? 126 VAL A O   1 
ATOM   967  C CB  . VAL A 1 126 ? 13.06533 9.70549  -5.08001  1.000 22.24981 ? 126 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 126 ? 14.44901 9.55239  -5.63986  1.000 28.27912 ? 126 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 126 ? 11.97731 9.30654  -6.12688  1.000 25.10538 ? 126 VAL A CG2 1 
ATOM   970  N N   . LYS A 1 127 ? 11.96772 6.67857  -4.05268  1.000 22.60025 ? 127 LYS A N   1 
ATOM   971  C CA  . LYS A 1 127 ? 11.86304 5.27863  -4.44616  1.000 27.08094 ? 127 LYS A CA  1 
ATOM   972  C C   . LYS A 1 127 ? 10.64199 5.10452  -5.35378  1.000 28.74444 ? 127 LYS A C   1 
ATOM   973  O O   . LYS A 1 127 ? 9.80959  6.00364  -5.49085  1.000 27.39091 ? 127 LYS A O   1 
ATOM   974  C CB  . LYS A 1 127 ? 11.77773 4.38100  -3.20677  1.000 32.53975 ? 127 LYS A CB  1 
ATOM   975  C CG  . LYS A 1 127 ? 12.93407 4.58588  -2.22208  1.000 31.71361 ? 127 LYS A CG  1 
ATOM   976  C CD  . LYS A 1 127 ? 12.73946 3.68633  -0.98224  0.900 30.62392 ? 127 LYS A CD  1 
ATOM   977  C CE  . LYS A 1 127 ? 13.31872 2.25677  -1.19177  0.700 39.34497 ? 127 LYS A CE  1 
ATOM   978  N NZ  . LYS A 1 127 ? 13.78121 1.63952  0.12348   0.700 38.68363 ? 127 LYS A NZ  1 
ATOM   979  N N   . SER A 1 128 ? 10.50853 3.93382  -5.96408  1.000 29.87114 ? 128 SER A N   1 
ATOM   980  C CA  . SER A 1 128 ? 9.32236  3.70312  -6.77890  1.000 30.53585 ? 128 SER A CA  1 
ATOM   981  C C   . SER A 1 128 ? 8.10348  3.42972  -5.88980  1.000 36.93610 ? 128 SER A C   1 
ATOM   982  O O   . SER A 1 128 ? 8.21792  3.17195  -4.69277  1.000 40.71591 ? 128 SER A O   1 
ATOM   983  C CB  . SER A 1 128 ? 9.49828  2.52393  -7.71218  1.000 38.35900 ? 128 SER A CB  1 
ATOM   984  O OG  . SER A 1 128 ? 9.10733  1.36468  -6.99970  1.000 45.92738 ? 128 SER A OG  1 
ATOM   985  N N   . SER A 1 129 ? 6.91681  3.48252  -6.48060  1.000 39.34179 ? 129 SER A N   1 
ATOM   986  C CA  . SER A 1 129 ? 5.76197  3.24535  -5.63209  1.000 43.36399 ? 129 SER A CA  1 
ATOM   987  C C   . SER A 1 129 ? 5.47216  1.75433  -5.62680  1.000 52.82080 ? 129 SER A C   1 
ATOM   988  O O   . SER A 1 129 ? 4.31781  1.34532  -5.53256  1.000 56.93667 ? 129 SER A O   1 
ATOM   989  C CB  . SER A 1 129 ? 4.55262  4.00739  -6.13820  1.000 45.88350 ? 129 SER A CB  1 
ATOM   990  O OG  . SER A 1 129 ? 4.18722  3.42973  -7.37367  1.000 50.85121 ? 129 SER A OG  1 
ATOM   991  N N   . GLY A 1 130 ? 6.51524  0.94107  -5.73767  1.000 52.93459 ? 130 GLY A N   1 
ATOM   992  C CA  . GLY A 1 130 ? 6.36947  -0.45164 -6.08425  1.000 54.41433 ? 130 GLY A CA  1 
ATOM   993  C C   . GLY A 1 130 ? 6.60954  -0.64945 -7.56950  1.000 58.70555 ? 130 GLY A C   1 
ATOM   994  O O   . GLY A 1 130 ? 6.14312  0.14202  -8.40901  1.000 60.48491 ? 130 GLY A O   1 
ATOM   995  N N   . GLY A 1 131 ? 7.32405  -1.71238 -7.91391  1.000 56.71667 ? 131 GLY A N   1 
ATOM   996  C CA  . GLY A 1 131 ? 7.78467  -1.87938 -9.26781  1.000 47.51423 ? 131 GLY A CA  1 
ATOM   997  C C   . GLY A 1 131 ? 9.14891  -1.23683 -9.40587  1.000 41.27047 ? 131 GLY A C   1 
ATOM   998  O O   . GLY A 1 131 ? 9.62050  -0.55122 -8.50314  1.000 41.25134 ? 131 GLY A O   1 
ATOM   999  N N   . PRO A 1 132 ? 9.82814  -1.45911 -10.52733 1.000 41.79570 ? 132 PRO A N   1 
ATOM   1000 C CA  . PRO A 1 132 ? 11.21571 -1.00260 -10.61820 1.000 40.91910 ? 132 PRO A CA  1 
ATOM   1001 C C   . PRO A 1 132 ? 11.30846 0.52575  -10.59853 1.000 37.10010 ? 132 PRO A C   1 
ATOM   1002 O O   . PRO A 1 132 ? 10.43993 1.24607  -11.11453 1.000 40.21500 ? 132 PRO A O   1 
ATOM   1003 C CB  . PRO A 1 132 ? 11.70972 -1.60305 -11.94543 1.000 35.10199 ? 132 PRO A CB  1 
ATOM   1004 C CG  . PRO A 1 132 ? 10.52602 -1.98998 -12.67081 1.000 38.24403 ? 132 PRO A CG  1 
ATOM   1005 C CD  . PRO A 1 132 ? 9.40977  -2.23917 -11.69382 1.000 42.67100 ? 132 PRO A CD  1 
ATOM   1006 N N   . PHE A 1 133 ? 12.39946 1.00555  -10.01766 1.000 30.32257 ? 133 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 133 ? 12.73681 2.41936  -9.97123  1.000 27.99858 ? 133 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 133 ? 13.72205 2.70863  -11.08551 1.000 31.37350 ? 133 PHE A C   1 
ATOM   1009 O O   . PHE A 1 133 ? 14.83430 2.18729  -11.05630 1.000 27.42793 ? 133 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 133 ? 13.37763 2.76500  -8.62509  1.000 27.55017 ? 133 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 133 ? 13.77572 4.19968  -8.48141  1.000 27.19010 ? 133 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 133 ? 12.81842 5.18513  -8.34364  1.000 27.33058 ? 133 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 133 ? 15.12517 4.56688  -8.50391  1.000 28.60330 ? 133 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 133 ? 13.21087 6.49397  -8.16832  1.000 27.08950 ? 133 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 133 ? 15.53003 5.90262  -8.32611  1.000 23.54630 ? 133 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 133 ? 14.54438 6.86488  -8.17859  1.000 25.03856 ? 133 PHE A CZ  1 
ATOM   1017 N N   . VAL A 1 134 ? 13.32157 3.54283  -12.05423 1.000 25.59933 ? 134 VAL A N   1 
ATOM   1018 C CA  . VAL A 1 134 ? 14.22918 3.96972  -13.11976 1.000 28.78944 ? 134 VAL A CA  1 
ATOM   1019 C C   . VAL A 1 134 ? 14.03582 5.46388  -13.33388 1.000 29.47683 ? 134 VAL A C   1 
ATOM   1020 O O   . VAL A 1 134 ? 12.91783 5.89841  -13.63463 1.000 31.91578 ? 134 VAL A O   1 
ATOM   1021 C CB  . VAL A 1 134 ? 13.93960 3.23112  -14.42787 1.000 30.74883 ? 134 VAL A CB  1 
ATOM   1022 C CG1 . VAL A 1 134 ? 15.01173 3.59121  -15.49858 1.000 29.60438 ? 134 VAL A CG1 1 
ATOM   1023 C CG2 . VAL A 1 134 ? 13.79627 1.72958  -14.17644 1.000 35.58691 ? 134 VAL A CG2 1 
ATOM   1024 N N   . VAL A 1 135 ? 15.10065 6.25034  -13.20594 1.000 25.62941 ? 135 VAL A N   1 
ATOM   1025 C CA  . VAL A 1 135 ? 14.98890 7.68181  -13.49066 1.000 25.87318 ? 135 VAL A CA  1 
ATOM   1026 C C   . VAL A 1 135 ? 16.20375 8.13759  -14.27331 1.000 26.20514 ? 135 VAL A C   1 
ATOM   1027 O O   . VAL A 1 135 ? 17.30244 7.61336  -14.09680 1.000 25.00311 ? 135 VAL A O   1 
ATOM   1028 C CB  . VAL A 1 135 ? 14.87814 8.57530  -12.24158 1.000 24.97961 ? 135 VAL A CB  1 
ATOM   1029 C CG1 . VAL A 1 135 ? 13.56067 8.36299  -11.52563 1.000 28.24444 ? 135 VAL A CG1 1 
ATOM   1030 C CG2 . VAL A 1 135 ? 16.08590 8.34429  -11.32827 1.000 26.18464 ? 135 VAL A CG2 1 
ATOM   1031 N N   . ASP A 1 136 ? 16.00821 9.14855  -15.12964 1.000 27.63326 ? 136 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 136 ? 17.13670 9.85775  -15.72193 1.000 25.14098 ? 136 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 136 ? 17.57612 10.97380 -14.77577 1.000 25.09289 ? 136 ASP A C   1 
ATOM   1034 O O   . ASP A 1 136 ? 16.73786 11.72397 -14.24948 1.000 26.04242 ? 136 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 136 ? 16.78200 10.45145 -17.07838 1.000 27.18631 ? 136 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 136 ? 16.79277 9.41243  -18.19147 1.000 28.42522 ? 136 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 136 ? 17.67617 8.52513  -18.15505 1.000 31.55778 ? 136 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 136 ? 15.92834 9.49276  -19.11741 1.000 32.30087 ? 136 ASP A OD2 1 
ATOM   1039 N N   . VAL A 1 137 ? 18.87503 11.05547 -14.53546 1.000 24.10259 ? 137 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 137 ? 19.45479 12.04263 -13.61890 1.000 23.20721 ? 137 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 137 ? 20.05553 13.15061 -14.47673 1.000 27.25815 ? 137 VAL A C   1 
ATOM   1042 O O   . VAL A 1 137 ? 20.96059 12.87849 -15.28126 1.000 26.27053 ? 137 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 137 ? 20.54189 11.40745 -12.75180 1.000 24.92619 ? 137 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 137 ? 21.15163 12.41608 -11.82295 1.000 24.20265 ? 137 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 137 ? 20.00376 10.16726 -11.98079 1.000 24.19526 ? 137 VAL A CG2 1 
ATOM   1046 N N   . VAL A 1 138 ? 19.56875 14.38589 -14.30531 1.000 24.52804 ? 138 VAL A N   1 
ATOM   1047 C CA  . VAL A 1 138 ? 19.91327 15.52058 -15.17778 1.000 22.94199 ? 138 VAL A CA  1 
ATOM   1048 C C   . VAL A 1 138 ? 20.50968 16.56221 -14.25626 1.000 31.71558 ? 138 VAL A C   1 
ATOM   1049 O O   . VAL A 1 138 ? 19.89432 16.92247 -13.24085 1.000 29.27315 ? 138 VAL A O   1 
ATOM   1050 C CB  . VAL A 1 138 ? 18.70659 16.09573 -15.92198 1.000 25.84945 ? 138 VAL A CB  1 
ATOM   1051 C CG1 . VAL A 1 138 ? 19.11975 17.25547 -16.82184 1.000 28.91462 ? 138 VAL A CG1 1 
ATOM   1052 C CG2 . VAL A 1 138 ? 18.08775 14.98649 -16.80154 1.000 26.38472 ? 138 VAL A CG2 1 
ATOM   1053 N N   . ILE A 1 139 ? 21.71861 17.00279 -14.55491 1.000 24.85125 ? 139 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 139 ? 22.41041 17.94286 -13.68258 1.000 22.74579 ? 139 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 139 ? 22.59855 19.23288 -14.46399 1.000 31.11926 ? 139 ILE A C   1 
ATOM   1056 O O   . ILE A 1 139 ? 23.30346 19.23548 -15.48174 1.000 26.17861 ? 139 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 139 ? 23.77256 17.39881 -13.23943 1.000 24.13135 ? 139 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 139 ? 23.66020 16.08915 -12.41815 1.000 24.08740 ? 139 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 139 ? 24.46507 18.45948 -12.36104 1.000 28.10128 ? 139 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 139 ? 25.02360 15.37107 -12.22995 1.000 24.62146 ? 139 ILE A CD1 1 
ATOM   1061 N N   . ASN A 1 140 ? 21.99701 20.32986 -13.99277 1.000 25.82861 ? 140 ASN A N   1 
ATOM   1062 C CA  . ASN A 1 140 ? 22.07729 21.59033 -14.72573 1.000 25.64136 ? 140 ASN A CA  1 
ATOM   1063 C C   . ASN A 1 140 ? 21.71879 21.38392 -16.19276 1.000 30.06808 ? 140 ASN A C   1 
ATOM   1064 O O   . ASN A 1 140 ? 22.39228 21.89470 -17.10244 1.000 29.92872 ? 140 ASN A O   1 
ATOM   1065 C CB  . ASN A 1 140 ? 23.47166 22.20958 -14.59897 1.000 26.04735 ? 140 ASN A CB  1 
ATOM   1066 C CG  . ASN A 1 140 ? 23.78211 22.53196 -13.17446 1.000 31.81217 ? 140 ASN A CG  1 
ATOM   1067 O OD1 . ASN A 1 140 ? 22.87799 22.90490 -12.43874 1.000 30.11625 ? 140 ASN A OD1 1 
ATOM   1068 N ND2 . ASN A 1 140 ? 25.02888 22.34473 -12.75993 1.000 30.40439 ? 140 ASN A ND2 1 
ATOM   1069 N N   . ASP A 1 141 ? 20.67754 20.58566 -16.42274 1.000 30.38167 ? 141 ASP A N   1 
ATOM   1070 C CA  . ASP A 1 141 ? 20.17140 20.30929 -17.80281 1.000 30.10186 ? 141 ASP A CA  1 
ATOM   1071 C C   . ASP A 1 141 ? 21.04629 19.38201 -18.62717 1.000 32.88136 ? 141 ASP A C   1 
ATOM   1072 O O   . ASP A 1 141 ? 20.77877 19.19485 -19.82837 1.000 39.05668 ? 141 ASP A O   1 
ATOM   1073 C CB  . ASP A 1 141 ? 19.98707 21.60224 -18.58015 1.000 30.76668 ? 141 ASP A CB  1 
ATOM   1074 C CG  . ASP A 1 141 ? 18.95263 22.51275 -17.95845 0.800 38.75641 ? 141 ASP A CG  1 
ATOM   1075 O OD1 . ASP A 1 141 ? 18.05435 22.02708 -17.24180 0.700 37.30997 ? 141 ASP A OD1 1 
ATOM   1076 O OD2 . ASP A 1 141 ? 19.03416 23.72809 -18.20275 0.700 45.21800 ? 141 ASP A OD2 1 
ATOM   1077 N N   . ILE A 1 142 ? 22.08411 18.80175 -18.07340 1.000 29.99397 ? 142 ILE A N   1 
ATOM   1078 C CA  A ILE A 1 142 ? 22.98587 17.87819 -18.74991 0.500 32.41400 ? 142 ILE A CA  1 
ATOM   1079 C CA  B ILE A 1 142 ? 22.84791 17.86083 -18.86608 0.500 32.46562 ? 142 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 142 ? 22.58211 16.45317 -18.35198 1.000 27.36405 ? 142 ILE A C   1 
ATOM   1081 O O   . ILE A 1 142 ? 22.59110 16.15657 -17.15237 1.000 25.69375 ? 142 ILE A O   1 
ATOM   1082 C CB  A ILE A 1 142 ? 24.43510 18.20611 -18.33488 0.500 32.20745 ? 142 ILE A CB  1 
ATOM   1083 C CB  B ILE A 1 142 ? 24.34197 18.21668 -18.97153 0.500 35.25454 ? 142 ILE A CB  1 
ATOM   1084 C CG1 A ILE A 1 142 ? 24.98980 19.36366 -19.19452 0.500 32.67861 ? 142 ILE A CG1 1 
ATOM   1085 C CG1 B ILE A 1 142 ? 25.10891 17.05786 -19.61211 0.500 32.95431 ? 142 ILE A CG1 1 
ATOM   1086 C CG2 A ILE A 1 142 ? 25.31683 16.95658 -18.25264 0.500 28.61473 ? 142 ILE A CG2 1 
ATOM   1087 C CG2 B ILE A 1 142 ? 24.93328 18.56945 -17.66920 0.500 30.21449 ? 142 ILE A CG2 1 
ATOM   1088 C CD1 A ILE A 1 142 ? 24.27236 19.51753 -20.52668 0.500 36.78259 ? 142 ILE A CD1 1 
ATOM   1089 C CD1 B ILE A 1 142 ? 25.69079 16.10902 -18.59086 0.500 31.36378 ? 142 ILE A CD1 1 
ATOM   1090 N N   . HIS A 1 143 ? 22.20673 15.58151 -19.30174 1.000 25.79662 ? 143 HIS A N   1 
ATOM   1091 C CA  A HIS A 1 143 ? 21.84907 14.20073 -18.95158 0.500 27.60428 ? 143 HIS A CA  1 
ATOM   1092 C CA  B HIS A 1 143 ? 21.84930 14.21625 -18.95166 0.500 27.60006 ? 143 HIS A CA  1 
ATOM   1093 C C   . HIS A 1 143 ? 23.08716 13.48146 -18.44120 1.000 29.84760 ? 143 HIS A C   1 
ATOM   1094 O O   . HIS A 1 143 ? 24.07639 13.31062 -19.17275 1.000 28.69981 ? 143 HIS A O   1 
ATOM   1095 C CB  A HIS A 1 143 ? 21.24802 13.40412 -20.12463 0.500 28.38051 ? 143 HIS A CB  1 
ATOM   1096 C CB  B HIS A 1 143 ? 21.20307 13.54839 -20.16924 0.500 28.36462 ? 143 HIS A CB  1 
ATOM   1097 C CG  A HIS A 1 143 ? 21.02488 11.95245 -19.78378 0.500 31.21867 ? 143 HIS A CG  1 
ATOM   1098 C CG  B HIS A 1 143 ? 19.83523 14.07783 -20.44608 0.500 28.97354 ? 143 HIS A CG  1 
ATOM   1099 N ND1 A HIS A 1 143 ? 22.05371 11.03316 -19.71090 0.500 29.13266 ? 143 HIS A ND1 1 
ATOM   1100 N ND1 B HIS A 1 143 ? 18.75569 13.26532 -20.71944 0.500 38.57333 ? 143 HIS A ND1 1 
ATOM   1101 C CD2 A HIS A 1 143 ? 19.90764 11.28508 -19.39114 0.500 33.70462 ? 143 HIS A CD2 1 
ATOM   1102 C CD2 B HIS A 1 143 ? 19.35176 15.34584 -20.42869 0.500 31.34674 ? 143 HIS A CD2 1 
ATOM   1103 C CE1 A HIS A 1 143 ? 21.57385 9.85630  -19.34306 0.500 27.64578 ? 143 HIS A CE1 1 
ATOM   1104 C CE1 B HIS A 1 143 ? 17.67791 14.01047 -20.89937 0.500 32.95501 ? 143 HIS A CE1 1 
ATOM   1105 N NE2 A HIS A 1 143 ? 20.27493 9.97909  -19.14557 0.500 27.10945 ? 143 HIS A NE2 1 
ATOM   1106 N NE2 B HIS A 1 143 ? 18.00922 15.27445 -20.71656 0.500 30.45680 ? 143 HIS A NE2 1 
ATOM   1107 N N   . PHE A 1 144 ? 23.04220 13.07215 -17.17827 1.000 25.05497 ? 144 PHE A N   1 
ATOM   1108 C CA  . PHE A 1 144 ? 24.22751 12.51673 -16.53382 1.000 22.75315 ? 144 PHE A CA  1 
ATOM   1109 C C   . PHE A 1 144 ? 24.23728 10.99609 -16.47017 1.000 24.00133 ? 144 PHE A C   1 
ATOM   1110 O O   . PHE A 1 144 ? 25.26488 10.36458 -16.77591 1.000 23.11246 ? 144 PHE A O   1 
ATOM   1111 C CB  . PHE A 1 144 ? 24.33576 13.08669 -15.12426 1.000 20.89859 ? 144 PHE A CB  1 
ATOM   1112 C CG  . PHE A 1 144 ? 25.53504 12.58084 -14.37722 1.000 21.79863 ? 144 PHE A CG  1 
ATOM   1113 C CD1 . PHE A 1 144 ? 26.79312 13.12358 -14.64434 1.000 22.96010 ? 144 PHE A CD1 1 
ATOM   1114 C CD2 . PHE A 1 144 ? 25.37979 11.61626 -13.40906 1.000 21.86625 ? 144 PHE A CD2 1 
ATOM   1115 C CE1 . PHE A 1 144 ? 27.92628 12.63798 -14.00643 1.000 24.42459 ? 144 PHE A CE1 1 
ATOM   1116 C CE2 . PHE A 1 144 ? 26.51822 11.14904 -12.67606 1.000 22.64724 ? 144 PHE A CE2 1 
ATOM   1117 C CZ  . PHE A 1 144 ? 27.77287 11.64818 -12.97411 1.000 25.73213 ? 144 PHE A CZ  1 
ATOM   1118 N N   . GLU A 1 145 ? 23.12389 10.38375 -16.06739 1.000 22.87494 ? 145 GLU A N   1 
ATOM   1119 C CA  . GLU A 1 145 ? 23.07156 8.92724  -16.05049 1.000 24.47836 ? 145 GLU A CA  1 
ATOM   1120 C C   . GLU A 1 145 ? 21.61160 8.51155  -16.00284 1.000 22.26199 ? 145 GLU A C   1 
ATOM   1121 O O   . GLU A 1 145 ? 20.74105 9.32284  -15.68210 1.000 26.60959 ? 145 GLU A O   1 
ATOM   1122 C CB  . GLU A 1 145 ? 23.82005 8.34605  -14.81668 1.000 19.96733 ? 145 GLU A CB  1 
ATOM   1123 C CG  . GLU A 1 145 ? 23.04818 8.71455  -13.52174 1.000 23.05519 ? 145 GLU A CG  1 
ATOM   1124 C CD  . GLU A 1 145 ? 23.79462 8.35186  -12.26385 1.000 26.55236 ? 145 GLU A CD  1 
ATOM   1125 O OE1 . GLU A 1 145 ? 24.91106 7.84308  -12.36290 1.000 24.56981 ? 145 GLU A OE1 1 
ATOM   1126 O OE2 . GLU A 1 145 ? 23.22969 8.59405  -11.16178 1.000 25.90180 ? 145 GLU A OE2 1 
ATOM   1127 N N   . ARG A 1 146 ? 21.34214 7.26533  -16.38813 1.000 23.76921 ? 146 ARG A N   1 
ATOM   1128 C CA  . ARG A 1 146 ? 20.04877 6.63891  -16.12684 1.000 24.72344 ? 146 ARG A CA  1 
ATOM   1129 C C   . ARG A 1 146 ? 20.26053 5.69135  -14.95020 1.000 25.72765 ? 146 ARG A C   1 
ATOM   1130 O O   . ARG A 1 146 ? 21.10378 4.79038  -15.02525 1.000 27.07888 ? 146 ARG A O   1 
ATOM   1131 C CB  . ARG A 1 146 ? 19.50019 5.89580  -17.34553 1.000 31.37003 ? 146 ARG A CB  1 
ATOM   1132 C CG  . ARG A 1 146 ? 18.21558 5.15499  -17.02827 1.000 28.39154 ? 146 ARG A CG  1 
ATOM   1133 C CD  . ARG A 1 146 ? 17.46979 4.73440  -18.30999 1.000 28.94042 ? 146 ARG A CD  1 
ATOM   1134 N NE  . ARG A 1 146 ? 17.04320 5.92004  -19.01548 1.000 30.58872 ? 146 ARG A NE  1 
ATOM   1135 C CZ  . ARG A 1 146 ? 16.40830 5.85291  -20.17830 1.000 35.44822 ? 146 ARG A CZ  1 
ATOM   1136 N NH1 . ARG A 1 146 ? 16.15594 4.68613  -20.75128 1.000 35.96830 ? 146 ARG A NH1 1 
ATOM   1137 N NH2 . ARG A 1 146 ? 15.98058 6.97438  -20.75495 1.000 37.25611 ? 146 ARG A NH2 1 
ATOM   1138 N N   . PHE A 1 147 ? 19.53796 5.94362  -13.86025 1.000 23.37256 ? 147 PHE A N   1 
ATOM   1139 C CA  . PHE A 1 147 ? 19.68182 5.20995  -12.61138 1.000 24.50397 ? 147 PHE A CA  1 
ATOM   1140 C C   . PHE A 1 147 ? 18.61300 4.12525  -12.51625 1.000 25.63107 ? 147 PHE A C   1 
ATOM   1141 O O   . PHE A 1 147 ? 17.44239 4.40783  -12.69720 1.000 26.39988 ? 147 PHE A O   1 
ATOM   1142 C CB  . PHE A 1 147 ? 19.52475 6.12561  -11.40881 1.000 24.64796 ? 147 PHE A CB  1 
ATOM   1143 C CG  . PHE A 1 147 ? 19.72271 5.37113  -10.09624 1.000 22.52217 ? 147 PHE A CG  1 
ATOM   1144 C CD1 . PHE A 1 147 ? 18.64946 4.73634  -9.44911  1.000 24.75296 ? 147 PHE A CD1 1 
ATOM   1145 C CD2 . PHE A 1 147 ? 20.98780 5.23525  -9.58525  1.000 24.14308 ? 147 PHE A CD2 1 
ATOM   1146 C CE1 . PHE A 1 147 ? 18.84519 4.00985  -8.27346  1.000 24.35981 ? 147 PHE A CE1 1 
ATOM   1147 C CE2 . PHE A 1 147 ? 21.18922 4.51380  -8.35645  1.000 20.92632 ? 147 PHE A CE2 1 
ATOM   1148 C CZ  . PHE A 1 147 ? 20.11768 3.91419  -7.74784  1.000 22.00472 ? 147 PHE A CZ  1 
ATOM   1149 N N   . ARG A 1 148 ? 19.03327 2.87754  -12.29811 1.000 22.10183 ? 148 ARG A N   1 
ATOM   1150 C CA  A ARG A 1 148 ? 18.14430 1.74937  -12.06090 0.500 25.19419 ? 148 ARG A CA  1 
ATOM   1151 C CA  B ARG A 1 148 ? 18.13936 1.75665  -12.06032 0.500 25.19621 ? 148 ARG A CA  1 
ATOM   1152 C C   . ARG A 1 148 ? 18.56884 1.11989  -10.75153 1.000 24.74107 ? 148 ARG A C   1 
ATOM   1153 O O   . ARG A 1 148 ? 19.73439 0.80721  -10.58941 1.000 27.14305 ? 148 ARG A O   1 
ATOM   1154 C CB  A ARG A 1 148 ? 18.22986 0.67976  -13.14538 0.500 28.43210 ? 148 ARG A CB  1 
ATOM   1155 C CB  B ARG A 1 148 ? 18.21044 0.71846  -13.17769 0.500 28.44469 ? 148 ARG A CB  1 
ATOM   1156 C CG  A ARG A 1 148 ? 17.48077 1.00303  -14.39036 0.500 31.58660 ? 148 ARG A CG  1 
ATOM   1157 C CG  B ARG A 1 148 ? 18.14399 1.33238  -14.55298 0.500 31.38736 ? 148 ARG A CG  1 
ATOM   1158 C CD  A ARG A 1 148 ? 17.66314 -0.11372 -15.41053 0.500 35.23896 ? 148 ARG A CD  1 
ATOM   1159 C CD  B ARG A 1 148 ? 18.40520 0.28828  -15.64198 0.500 35.31090 ? 148 ARG A CD  1 
ATOM   1160 N NE  A ARG A 1 148 ? 17.38085 0.34393  -16.77295 0.500 37.06695 ? 148 ARG A NE  1 
ATOM   1161 N NE  B ARG A 1 148 ? 17.77487 0.64222  -16.92087 0.500 36.55144 ? 148 ARG A NE  1 
ATOM   1162 C CZ  A ARG A 1 148 ? 18.18836 1.10921  -17.50114 0.500 34.73989 ? 148 ARG A CZ  1 
ATOM   1163 C CZ  B ARG A 1 148 ? 16.65933 0.08268  -17.38029 0.500 38.60478 ? 148 ARG A CZ  1 
ATOM   1164 N NH1 A ARG A 1 148 ? 19.29897 1.62181  -17.00319 0.500 33.09516 ? 148 ARG A NH1 1 
ATOM   1165 N NH1 B ARG A 1 148 ? 15.99252 -0.81922 -16.67531 0.500 37.51157 ? 148 ARG A NH1 1 
ATOM   1166 N NH2 A ARG A 1 148 ? 17.89401 1.33132  -18.77787 0.500 38.59422 ? 148 ARG A NH2 1 
ATOM   1167 N NH2 B ARG A 1 148 ? 16.19481 0.44103  -18.57296 0.500 33.78187 ? 148 ARG A NH2 1 
ATOM   1168 N N   . GLY A 1 149 ? 17.63548 0.93943  -9.82887  1.000 24.08376 ? 149 GLY A N   1 
ATOM   1169 C CA  . GLY A 1 149 ? 18.06513 0.40164  -8.52943  1.000 22.21347 ? 149 GLY A CA  1 
ATOM   1170 C C   . GLY A 1 149 ? 16.96854 0.62860  -7.51029  1.000 23.56014 ? 149 GLY A C   1 
ATOM   1171 O O   . GLY A 1 149 ? 15.80051 0.72691  -7.86610  1.000 26.72746 ? 149 GLY A O   1 
ATOM   1172 N N   . ASP A 1 150 ? 17.36417 0.72009  -6.24451  1.000 21.17992 ? 150 ASP A N   1 
ATOM   1173 C CA  . ASP A 1 150 ? 16.32110 0.81699  -5.21419  1.000 25.71708 ? 150 ASP A CA  1 
ATOM   1174 C C   . ASP A 1 150 ? 15.83337 2.25211  -4.99046  1.000 25.96169 ? 150 ASP A C   1 
ATOM   1175 O O   . ASP A 1 150 ? 14.69563 2.44905  -4.51497  1.000 28.71504 ? 150 ASP A O   1 
ATOM   1176 C CB  . ASP A 1 150 ? 16.83023 0.27306  -3.86927  1.000 21.62247 ? 150 ASP A CB  1 
ATOM   1177 C CG  . ASP A 1 150 ? 16.85804 -1.22329 -3.84910  1.000 23.79076 ? 150 ASP A CG  1 
ATOM   1178 O OD1 . ASP A 1 150 ? 16.42063 -1.79247 -4.85556  1.000 27.68681 ? 150 ASP A OD1 1 
ATOM   1179 O OD2 . ASP A 1 150 ? 17.26027 -1.81266 -2.81176  1.000 27.17599 ? 150 ASP A OD2 1 
ATOM   1180 N N   . GLY A 1 151 ? 16.67503 3.23565  -5.20329  1.000 22.03475 ? 151 GLY A N   1 
ATOM   1181 C CA  . GLY A 1 151 ? 16.31567 4.61530  -4.93404  1.000 20.97266 ? 151 GLY A CA  1 
ATOM   1182 C C   . GLY A 1 151 ? 17.52805 5.52164  -4.87095  1.000 21.25211 ? 151 GLY A C   1 
ATOM   1183 O O   . GLY A 1 151 ? 18.66878 5.11404  -5.10959  1.000 21.03862 ? 151 GLY A O   1 
ATOM   1184 N N   . LEU A 1 152 ? 17.25541 6.77942  -4.53176  1.000 21.60905 ? 152 LEU A N   1 
ATOM   1185 C CA  . LEU A 1 152 ? 18.26668 7.84339  -4.44809  1.000 18.91695 ? 152 LEU A CA  1 
ATOM   1186 C C   . LEU A 1 152 ? 18.02833 8.66164  -3.18175  1.000 20.97529 ? 152 LEU A C   1 
ATOM   1187 O O   . LEU A 1 152 ? 16.88750 8.82842  -2.76623  1.000 22.07584 ? 152 LEU A O   1 
ATOM   1188 C CB  . LEU A 1 152 ? 18.17996 8.79455  -5.64814  1.000 20.70089 ? 152 LEU A CB  1 
ATOM   1189 C CG  . LEU A 1 152 ? 18.69495 8.11505  -6.92741  1.000 21.95622 ? 152 LEU A CG  1 
ATOM   1190 C CD1 . LEU A 1 152 ? 18.37397 8.95937  -8.17733  1.000 22.69276 ? 152 LEU A CD1 1 
ATOM   1191 C CD2 . LEU A 1 152 ? 20.18966 7.91671  -6.90264  1.000 22.93453 ? 152 LEU A CD2 1 
ATOM   1192 N N   . CYS A 1 153 ? 19.10248 9.18008  -2.58435  1.000 18.01248 ? 153 CYS A N   1 
ATOM   1193 C CA  . CYS A 1 153 ? 19.01997 9.96963  -1.35340  1.000 22.81198 ? 153 CYS A CA  1 
ATOM   1194 C C   . CYS A 1 153 ? 19.76307 11.27279 -1.57415  1.000 19.78708 ? 153 CYS A C   1 
ATOM   1195 O O   . CYS A 1 153 ? 20.91902 11.25582 -2.03914  1.000 18.70493 ? 153 CYS A O   1 
ATOM   1196 C CB  . CYS A 1 153 ? 19.68099 9.18730  -0.20510  1.000 20.35358 ? 153 CYS A CB  1 
ATOM   1197 S SG  . CYS A 1 153 ? 19.71964 10.14638 1.35838   1.000 22.49383 ? 153 CYS A SG  1 
ATOM   1198 N N   . MET A 1 154 ? 19.10492 12.40749 -1.32790  1.000 19.30945 ? 154 MET A N   1 
ATOM   1199 C CA  . MET A 1 154 ? 19.79009 13.69312 -1.41097  1.000 19.23236 ? 154 MET A CA  1 
ATOM   1200 C C   . MET A 1 154 ? 19.84143 14.28424 -0.00044  1.000 19.53560 ? 154 MET A C   1 
ATOM   1201 O O   . MET A 1 154 ? 18.79442 14.61565 0.53848   1.000 21.09287 ? 154 MET A O   1 
ATOM   1202 C CB  . MET A 1 154 ? 19.08641 14.66199 -2.33710  1.000 19.66549 ? 154 MET A CB  1 
ATOM   1203 C CG  . MET A 1 154 ? 19.89055 15.95722 -2.58331  1.000 22.18434 ? 154 MET A CG  1 
ATOM   1204 S SD  . MET A 1 154 ? 21.41237 15.73766 -3.57776  1.000 22.11888 ? 154 MET A SD  1 
ATOM   1205 C CE  . MET A 1 154 ? 20.79958 16.06508 -5.29869  1.000 22.79293 ? 154 MET A CE  1 
ATOM   1206 N N   . SER A 1 155 ? 21.05254 14.54609 0.49053   1.000 18.98145 ? 155 SER A N   1 
ATOM   1207 C CA  . SER A 1 155 ? 21.27697 14.94368 1.88919   1.000 19.59576 ? 155 SER A CA  1 
ATOM   1208 C C   . SER A 1 155 ? 21.75539 16.38415 2.00996   1.000 23.33690 ? 155 SER A C   1 
ATOM   1209 O O   . SER A 1 155 ? 22.52305 16.87774 1.18307   1.000 22.76879 ? 155 SER A O   1 
ATOM   1210 C CB  . SER A 1 155 ? 22.30891 13.99860 2.52330   1.000 20.83996 ? 155 SER A CB  1 
ATOM   1211 O OG  . SER A 1 155 ? 22.52649 14.38741 3.89686   1.000 23.64112 ? 155 SER A OG  1 
ATOM   1212 N N   . THR A 1 156 ? 21.32986 17.06215 3.07719   1.000 19.45583 ? 156 THR A N   1 
ATOM   1213 C CA  . THR A 1 156 ? 21.99712 18.28580 3.49614   1.000 22.00261 ? 156 THR A CA  1 
ATOM   1214 C C   . THR A 1 156 ? 23.31036 17.94875 4.21667   1.000 20.52639 ? 156 THR A C   1 
ATOM   1215 O O   . THR A 1 156 ? 23.61394 16.78310 4.52476   1.000 22.73051 ? 156 THR A O   1 
ATOM   1216 C CB  . THR A 1 156 ? 21.11198 19.02700 4.50534   1.000 21.92048 ? 156 THR A CB  1 
ATOM   1217 O OG1 . THR A 1 156 ? 21.07679 18.18232 5.67403   1.000 22.40583 ? 156 THR A OG1 1 
ATOM   1218 C CG2 . THR A 1 156 ? 19.68939 19.22617 4.05181   1.000 21.71376 ? 156 THR A CG2 1 
ATOM   1219 N N   . PRO A 1 157 ? 24.12603 18.96557 4.50649   1.000 21.71532 ? 157 PRO A N   1 
ATOM   1220 C CA  . PRO A 1 157 ? 25.36781 18.72085 5.27538   1.000 23.87412 ? 157 PRO A CA  1 
ATOM   1221 C C   . PRO A 1 157 ? 25.09266 18.08739 6.61888   1.000 21.21671 ? 157 PRO A C   1 
ATOM   1222 O O   . PRO A 1 157 ? 25.67902 17.03921 6.93391   1.000 21.14629 ? 157 PRO A O   1 
ATOM   1223 C CB  . PRO A 1 157 ? 25.98204 20.11635 5.38593   1.000 24.23418 ? 157 PRO A CB  1 
ATOM   1224 C CG  . PRO A 1 157 ? 25.45637 20.82170 4.09540   1.000 26.58583 ? 157 PRO A CG  1 
ATOM   1225 C CD  . PRO A 1 157 ? 24.02686 20.35823 4.00320   1.000 23.26264 ? 157 PRO A CD  1 
ATOM   1226 N N   . SER A 1 158 ? 24.16158 18.64137 7.40146   1.000 24.24012 ? 158 SER A N   1 
ATOM   1227 C CA  . SER A 1 158 ? 23.90636 18.01846 8.71092   1.000 22.19666 ? 158 SER A CA  1 
ATOM   1228 C C   . SER A 1 158 ? 23.20366 16.67806 8.54898   1.000 22.44036 ? 158 SER A C   1 
ATOM   1229 O O   . SER A 1 158 ? 23.30105 15.81827 9.41334   1.000 22.18502 ? 158 SER A O   1 
ATOM   1230 C CB  . SER A 1 158 ? 23.10529 18.95756 9.63919   1.000 23.15461 ? 158 SER A CB  1 
ATOM   1231 O OG  . SER A 1 158 ? 21.84525 19.34087 9.12000   1.000 25.77179 ? 158 SER A OG  1 
ATOM   1232 N N   . GLY A 1 159 ? 22.53397 16.45338 7.42020   1.000 19.59056 ? 159 GLY A N   1 
ATOM   1233 C CA  . GLY A 1 159 ? 22.04610 15.09227 7.22114   1.000 21.88719 ? 159 GLY A CA  1 
ATOM   1234 C C   . GLY A 1 159 ? 23.08176 14.09155 6.75760   1.000 19.53998 ? 159 GLY A C   1 
ATOM   1235 O O   . GLY A 1 159 ? 22.73532 12.90969 6.65419   1.000 19.99563 ? 159 GLY A O   1 
ATOM   1236 N N   . THR A 1 160 ? 24.33088 14.49604 6.52816   1.000 18.99842 ? 160 THR A N   1 
ATOM   1237 C CA  . THR A 1 160 ? 25.28142 13.51402 6.02418   1.000 18.47702 ? 160 THR A CA  1 
ATOM   1238 C C   . THR A 1 160 ? 25.62664 12.46284 7.04729   1.000 18.08465 ? 160 THR A C   1 
ATOM   1239 O O   . THR A 1 160 ? 25.99987 11.35902 6.64983   1.000 20.12777 ? 160 THR A O   1 
ATOM   1240 C CB  . THR A 1 160 ? 26.57067 14.15252 5.48134   1.000 21.54291 ? 160 THR A CB  1 
ATOM   1241 O OG1 . THR A 1 160 ? 27.23354 14.92916 6.47842   1.000 19.69020 ? 160 THR A OG1 1 
ATOM   1242 C CG2 . THR A 1 160 ? 26.24947 15.02521 4.25871   1.000 24.74371 ? 160 THR A CG2 1 
ATOM   1243 N N   . THR A 1 161 ? 25.36596 12.71998 8.34799   1.000 20.84036 ? 161 THR A N   1 
ATOM   1244 C CA  . THR A 1 161 ? 25.60613 11.71800 9.36549   1.000 22.34847 ? 161 THR A CA  1 
ATOM   1245 C C   . THR A 1 161 ? 24.38861 10.82281 9.59349   1.000 23.79493 ? 161 THR A C   1 
ATOM   1246 O O   . THR A 1 161 ? 24.43769 9.95017  10.46566  1.000 24.09625 ? 161 THR A O   1 
ATOM   1247 C CB  . THR A 1 161 ? 25.96243 12.41745 10.70177  1.000 18.49476 ? 161 THR A CB  1 
ATOM   1248 O OG1 . THR A 1 161 ? 25.09893 13.52656 10.82023  1.000 20.97885 ? 161 THR A OG1 1 
ATOM   1249 C CG2 . THR A 1 161 ? 27.39351 12.91187 10.65267  1.000 21.57443 ? 161 THR A CG2 1 
ATOM   1250 N N   . ALA A 1 162 ? 23.33131 10.97139 8.79461   1.000 22.07515 ? 162 ALA A N   1 
ATOM   1251 C CA  . ALA A 1 162 ? 22.09550 10.19963 8.94150   1.000 21.76272 ? 162 ALA A CA  1 
ATOM   1252 C C   . ALA A 1 162 ? 22.00823 9.16884  7.81026   1.000 22.13654 ? 162 ALA A C   1 
ATOM   1253 O O   . ALA A 1 162 ? 22.97260 8.43343  7.60376   1.000 23.58226 ? 162 ALA A O   1 
ATOM   1254 C CB  . ALA A 1 162 ? 20.87727 11.14126 8.97306   1.000 20.99133 ? 162 ALA A CB  1 
ATOM   1255 N N   . TYR A 1 163 ? 20.87707 9.05248  7.11444   1.000 21.87662 ? 163 TYR A N   1 
ATOM   1256 C CA  . TYR A 1 163 ? 20.75500 8.04013  6.05175   1.000 19.29795 ? 163 TYR A CA  1 
ATOM   1257 C C   . TYR A 1 163 ? 21.93115 8.07616  5.08539   1.000 20.08072 ? 163 TYR A C   1 
ATOM   1258 O O   . TYR A 1 163 ? 22.46033 7.04456  4.69073   1.000 20.18507 ? 163 TYR A O   1 
ATOM   1259 C CB  . TYR A 1 163 ? 19.44023 8.33100  5.33808   1.000 20.25678 ? 163 TYR A CB  1 
ATOM   1260 C CG  . TYR A 1 163 ? 18.75444 7.20929  4.64660   1.000 21.30881 ? 163 TYR A CG  1 
ATOM   1261 C CD1 . TYR A 1 163 ? 19.33328 5.94259  4.51129   1.000 19.43367 ? 163 TYR A CD1 1 
ATOM   1262 C CD2 . TYR A 1 163 ? 17.45608 7.41418  4.14850   1.000 24.65891 ? 163 TYR A CD2 1 
ATOM   1263 C CE1 . TYR A 1 163 ? 18.62062 4.87988  3.85185   1.000 24.58080 ? 163 TYR A CE1 1 
ATOM   1264 C CE2 . TYR A 1 163 ? 16.74238 6.37527  3.51780   1.000 27.46033 ? 163 TYR A CE2 1 
ATOM   1265 C CZ  . TYR A 1 163 ? 17.35760 5.14976  3.30838   1.000 29.88091 ? 163 TYR A CZ  1 
ATOM   1266 O OH  . TYR A 1 163 ? 16.64487 4.14160  2.70395   1.000 28.45576 ? 163 TYR A OH  1 
ATOM   1267 N N   . ASN A 1 164 ? 22.36685 9.26741  4.71502   1.000 17.24441 ? 164 ASN A N   1 
ATOM   1268 C CA  . ASN A 1 164 ? 23.50934 9.41284  3.80481   1.000 18.30285 ? 164 ASN A CA  1 
ATOM   1269 C C   . ASN A 1 164 ? 24.69913 8.54089  4.24768   1.000 19.73886 ? 164 ASN A C   1 
ATOM   1270 O O   . ASN A 1 164 ? 25.32857 7.85817  3.42605   1.000 19.85939 ? 164 ASN A O   1 
ATOM   1271 C CB  . ASN A 1 164 ? 23.88306 10.90090 3.75213   1.000 19.95234 ? 164 ASN A CB  1 
ATOM   1272 C CG  . ASN A 1 164 ? 25.17452 11.16416 3.04026   1.000 23.60459 ? 164 ASN A CG  1 
ATOM   1273 O OD1 . ASN A 1 164 ? 25.20488 11.37148 1.81623   1.000 21.95636 ? 164 ASN A OD1 1 
ATOM   1274 N ND2 . ASN A 1 164 ? 26.27824 11.22743 3.80156   1.000 19.18245 ? 164 ASN A ND2 1 
ATOM   1275 N N   . LYS A 1 165 ? 25.01760 8.56296  5.55324   1.000 19.42131 ? 165 LYS A N   1 
ATOM   1276 C CA  . LYS A 1 165 ? 26.15822 7.79766  6.04633   1.000 17.79438 ? 165 LYS A CA  1 
ATOM   1277 C C   . LYS A 1 165 ? 25.97709 6.31640  5.76561   1.000 19.44383 ? 165 LYS A C   1 
ATOM   1278 O O   . LYS A 1 165 ? 26.90754 5.62869  5.33641   1.000 19.99855 ? 165 LYS A O   1 
ATOM   1279 C CB  . LYS A 1 165 ? 26.32953 8.05007  7.56922   1.000 20.10634 ? 165 LYS A CB  1 
ATOM   1280 C CG  . LYS A 1 165 ? 27.53780 7.38953  8.14093   1.000 20.22047 ? 165 LYS A CG  1 
ATOM   1281 C CD  . LYS A 1 165 ? 27.70943 7.86184  9.60879   1.000 20.40446 ? 165 LYS A CD  1 
ATOM   1282 C CE  . LYS A 1 165 ? 29.04024 7.27608  10.12267  1.000 26.86005 ? 165 LYS A CE  1 
ATOM   1283 N NZ  . LYS A 1 165 ? 28.91061 5.79248  10.30614  1.000 30.65248 ? 165 LYS A NZ  1 
ATOM   1284 N N   . SER A 1 166 ? 24.76719 5.79519  6.03194   1.000 18.44874 ? 166 SER A N   1 
ATOM   1285 C CA  . SER A 1 166 ? 24.48902 4.37746  5.83695   1.000 17.10916 ? 166 SER A CA  1 
ATOM   1286 C C   . SER A 1 166 ? 24.58323 3.95320  4.37604   1.000 19.55733 ? 166 SER A C   1 
ATOM   1287 O O   . SER A 1 166 ? 24.79742 2.77819  4.12285   1.000 21.96573 ? 166 SER A O   1 
ATOM   1288 C CB  . SER A 1 166 ? 23.08380 4.04070  6.32889   1.000 20.93197 ? 166 SER A CB  1 
ATOM   1289 O OG  . SER A 1 166 ? 23.10008 4.22605  7.74676   1.000 24.42502 ? 166 SER A OG  1 
ATOM   1290 N N   . LEU A 1 167 ? 24.44354 4.88808  3.46419   1.000 22.36725 ? 167 LEU A N   1 
ATOM   1291 C CA  . LEU A 1 167 ? 24.52331 4.63966  2.01386   1.000 19.56325 ? 167 LEU A CA  1 
ATOM   1292 C C   . LEU A 1 167 ? 25.91877 4.85424  1.48843   1.000 20.29621 ? 167 LEU A C   1 
ATOM   1293 O O   . LEU A 1 167 ? 26.14299 4.75935  0.25109   1.000 21.77847 ? 167 LEU A O   1 
ATOM   1294 C CB  . LEU A 1 167 ? 23.52979 5.54499  1.26299   1.000 19.65351 ? 167 LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 167 ? 22.05848 5.21947  1.59965   1.000 20.30010 ? 167 LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 167 ? 21.13254 6.26781  1.05568   1.000 20.65413 ? 167 LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 167 ? 21.65992 3.82262  1.11495   1.000 19.38882 ? 167 LEU A CD2 1 
ATOM   1298 N N   . GLY A 1 168 ? 26.87867 5.14655  2.38461   1.000 20.85303 ? 168 GLY A N   1 
ATOM   1299 C CA  . GLY A 1 168 ? 28.28364 5.29036  2.02452   1.000 20.95183 ? 168 GLY A CA  1 
ATOM   1300 C C   . GLY A 1 168 ? 28.69859 6.70047  1.65939   1.000 24.20152 ? 168 GLY A C   1 
ATOM   1301 O O   . GLY A 1 168 ? 29.80527 6.87276  1.13050   1.000 23.95986 ? 168 GLY A O   1 
ATOM   1302 N N   . GLY A 1 169 ? 27.85764 7.69818  1.95677   1.000 20.58751 ? 169 GLY A N   1 
ATOM   1303 C CA  . GLY A 1 169 ? 28.13769 9.08695  1.65640   1.000 19.64795 ? 169 GLY A CA  1 
ATOM   1304 C C   . GLY A 1 169 ? 29.26158 9.62511  2.53360   1.000 22.64827 ? 169 GLY A C   1 
ATOM   1305 O O   . GLY A 1 169 ? 29.59410 9.06109  3.59720   1.000 20.37853 ? 169 GLY A O   1 
ATOM   1306 N N   . ALA A 1 170 ? 29.84409 10.73054 2.09214   1.000 18.23796 ? 170 ALA A N   1 
ATOM   1307 C CA  . ALA A 1 170 ? 30.83523 11.45078 2.88701   1.000 18.30462 ? 170 ALA A CA  1 
ATOM   1308 C C   . ALA A 1 170 ? 30.12238 12.22830 4.00269   1.000 19.02261 ? 170 ALA A C   1 
ATOM   1309 O O   . ALA A 1 170 ? 28.98006 12.67953 3.84605   1.000 19.98106 ? 170 ALA A O   1 
ATOM   1310 C CB  . ALA A 1 170 ? 31.65027 12.42542 2.03011   1.000 22.40093 ? 170 ALA A CB  1 
ATOM   1311 N N   . LEU A 1 171 ? 30.81027 12.40929 5.10975   1.000 18.88756 ? 171 LEU A N   1 
ATOM   1312 C CA  . LEU A 1 171 ? 30.29788 13.33303 6.14389   1.000 20.34554 ? 171 LEU A CA  1 
ATOM   1313 C C   . LEU A 1 171 ? 30.86765 14.71586 5.86307   1.000 20.41497 ? 171 LEU A C   1 
ATOM   1314 O O   . LEU A 1 171 ? 32.08932 14.85337 5.71501   1.000 23.61792 ? 171 LEU A O   1 
ATOM   1315 C CB  . LEU A 1 171 ? 30.75504 12.86104 7.52296   1.000 21.23855 ? 171 LEU A CB  1 
ATOM   1316 C CG  . LEU A 1 171 ? 30.61284 11.36258 7.79207   1.000 22.89903 ? 171 LEU A CG  1 
ATOM   1317 C CD1 . LEU A 1 171 ? 30.97944 11.09684 9.26424   1.000 22.89337 ? 171 LEU A CD1 1 
ATOM   1318 C CD2 . LEU A 1 171 ? 29.17367 10.79061 7.53564   1.000 25.10637 ? 171 LEU A CD2 1 
ATOM   1319 N N   . MET A 1 172 ? 30.01853 15.73320 5.77199   1.000 21.55390 ? 172 MET A N   1 
ATOM   1320 C CA  . MET A 1 172 ? 30.45641 17.06026 5.36653   1.000 22.26357 ? 172 MET A CA  1 
ATOM   1321 C C   . MET A 1 172 ? 30.18286 18.08414 6.45927   1.000 23.11318 ? 172 MET A C   1 
ATOM   1322 O O   . MET A 1 172 ? 29.07512 18.15983 7.00630   1.000 27.45737 ? 172 MET A O   1 
ATOM   1323 C CB  . MET A 1 172 ? 29.77539 17.54907 4.06718   1.000 26.65882 ? 172 MET A CB  1 
ATOM   1324 C CG  . MET A 1 172 ? 29.51720 16.56969 3.01502   1.000 33.45428 ? 172 MET A CG  1 
ATOM   1325 S SD  . MET A 1 172 ? 28.49119 17.39760 1.70427   1.000 36.01319 ? 172 MET A SD  1 
ATOM   1326 C CE  . MET A 1 172 ? 29.49478 18.82151 1.47820   1.000 26.33530 ? 172 MET A CE  1 
ATOM   1327 N N   . HIS A 1 173 ? 31.16938 18.89892 6.73362   1.000 25.70197 ? 173 HIS A N   1 
ATOM   1328 C CA  . HIS A 1 173 ? 30.96703 19.97324 7.70521   1.000 25.09279 ? 173 HIS A CA  1 
ATOM   1329 C C   . HIS A 1 173 ? 29.81881 20.87103 7.25346   1.000 27.64990 ? 173 HIS A C   1 
ATOM   1330 O O   . HIS A 1 173 ? 29.77805 21.29521 6.08776   1.000 27.95243 ? 173 HIS A O   1 
ATOM   1331 C CB  . HIS A 1 173 ? 32.19526 20.85226 7.84729   1.000 25.87929 ? 173 HIS A CB  1 
ATOM   1332 C CG  . HIS A 1 173 ? 32.14063 21.70270 9.07676   1.000 26.65004 ? 173 HIS A CG  1 
ATOM   1333 N ND1 . HIS A 1 173 ? 31.64823 22.99335 9.09133   1.000 31.42114 ? 173 HIS A ND1 1 
ATOM   1334 C CD2 . HIS A 1 173 ? 32.47957 21.41679 10.35801  1.000 29.13092 ? 173 HIS A CD2 1 
ATOM   1335 C CE1 . HIS A 1 173 ? 31.72003 23.48173 10.32132  1.000 32.09448 ? 173 HIS A CE1 1 
ATOM   1336 N NE2 . HIS A 1 173 ? 32.21814 22.54330 11.10802  1.000 28.48041 ? 173 HIS A NE2 1 
ATOM   1337 N N   . PRO A 1 174 ? 28.91792 21.24333 8.17287   1.000 27.21180 ? 174 PRO A N   1 
ATOM   1338 C CA  . PRO A 1 174 ? 27.72495 22.02863 7.79676   1.000 26.81598 ? 174 PRO A CA  1 
ATOM   1339 C C   . PRO A 1 174 ? 27.98622 23.47682 7.40412   1.000 30.86545 ? 174 PRO A C   1 
ATOM   1340 O O   . PRO A 1 174 ? 27.07415 24.14560 6.88616   1.000 32.34016 ? 174 PRO A O   1 
ATOM   1341 C CB  . PRO A 1 174 ? 26.84284 21.92120 9.04997   1.000 32.99844 ? 174 PRO A CB  1 
ATOM   1342 C CG  . PRO A 1 174 ? 27.79045 21.52983 10.19042  1.000 33.92012 ? 174 PRO A CG  1 
ATOM   1343 C CD  . PRO A 1 174 ? 28.89021 20.73793 9.55766   1.000 26.88317 ? 174 PRO A CD  1 
ATOM   1344 N N   . SER A 1 175 ? 29.18425 24.01544 7.58484   1.000 27.38364 ? 175 SER A N   1 
ATOM   1345 C CA  . SER A 1 175 ? 29.42990 25.30905 6.96995   1.000 29.62290 ? 175 SER A CA  1 
ATOM   1346 C C   . SER A 1 175 ? 29.50394 25.22079 5.44274   1.000 32.66401 ? 175 SER A C   1 
ATOM   1347 O O   . SER A 1 175 ? 29.60088 26.25816 4.78371   1.000 37.38325 ? 175 SER A O   1 
ATOM   1348 C CB  . SER A 1 175 ? 30.72637 25.94310 7.50778   1.000 34.82640 ? 175 SER A CB  1 
ATOM   1349 O OG  . SER A 1 175 ? 31.81184 25.09415 7.22656   1.000 36.63054 ? 175 SER A OG  1 
ATOM   1350 N N   . ILE A 1 176 ? 29.52349 24.03023 4.85847   1.000 30.55273 ? 176 ILE A N   1 
ATOM   1351 C CA  . ILE A 1 176 ? 29.66329 23.92613 3.40949   1.000 30.05501 ? 176 ILE A CA  1 
ATOM   1352 C C   . ILE A 1 176 ? 28.26103 23.97911 2.81766   1.000 26.97819 ? 176 ILE A C   1 
ATOM   1353 O O   . ILE A 1 176 ? 27.42581 23.14392 3.16242   1.000 25.95548 ? 176 ILE A O   1 
ATOM   1354 C CB  . ILE A 1 176 ? 30.38423 22.63926 3.00212   1.000 27.04179 ? 176 ILE A CB  1 
ATOM   1355 C CG1 . ILE A 1 176 ? 31.80570 22.64140 3.57436   1.000 30.86291 ? 176 ILE A CG1 1 
ATOM   1356 C CG2 . ILE A 1 176 ? 30.46236 22.52043 1.46158   1.000 26.58011 ? 176 ILE A CG2 1 
ATOM   1357 C CD1 . ILE A 1 176 ? 32.50006 21.28326 3.41516   1.000 27.78789 ? 176 ILE A CD1 1 
ATOM   1358 N N   . GLU A 1 177 ? 28.00655 24.93952 1.91577   1.000 24.90904 ? 177 GLU A N   1 
ATOM   1359 C CA  . GLU A 1 177 ? 26.66568 25.04598 1.33995   1.000 27.25305 ? 177 GLU A CA  1 
ATOM   1360 C C   . GLU A 1 177 ? 26.55369 24.07101 0.16294   1.000 26.94789 ? 177 GLU A C   1 
ATOM   1361 O O   . GLU A 1 177 ? 26.93313 24.37448 -0.96535  1.000 28.28115 ? 177 GLU A O   1 
ATOM   1362 C CB  . GLU A 1 177 ? 26.37103 26.48454 0.95470   1.000 30.97491 ? 177 GLU A CB  1 
ATOM   1363 C CG  . GLU A 1 177 ? 26.27602 27.41456 2.21303   1.000 31.04456 ? 177 GLU A CG  1 
ATOM   1364 C CD  . GLU A 1 177 ? 25.87637 28.82305 1.82833   0.700 38.10984 ? 177 GLU A CD  1 
ATOM   1365 O OE1 . GLU A 1 177 ? 26.64635 29.48829 1.13155   0.700 38.80875 ? 177 GLU A OE1 1 
ATOM   1366 O OE2 . GLU A 1 177 ? 24.76758 29.25307 2.16389   0.700 43.47798 ? 177 GLU A OE2 1 
ATOM   1367 N N   . ALA A 1 178 ? 26.02810 22.87504 0.43540   1.000 24.14731 ? 178 ALA A N   1 
ATOM   1368 C CA  . ALA A 1 178 ? 26.04297 21.81676 -0.57261  1.000 23.97890 ? 178 ALA A CA  1 
ATOM   1369 C C   . ALA A 1 178 ? 24.91629 20.84134 -0.26567  1.000 23.79012 ? 178 ALA A C   1 
ATOM   1370 O O   . ALA A 1 178 ? 24.28157 20.89582 0.79792   1.000 23.60861 ? 178 ALA A O   1 
ATOM   1371 C CB  . ALA A 1 178 ? 27.38644 21.09304 -0.61559  1.000 22.85842 ? 178 ALA A CB  1 
ATOM   1372 N N   . MET A 1 179 ? 24.66738 19.94736 -1.22771  1.000 21.50045 ? 179 MET A N   1 
ATOM   1373 C CA  . MET A 1 179 ? 23.83609 18.78584 -1.03302  1.000 21.38132 ? 179 MET A CA  1 
ATOM   1374 C C   . MET A 1 179 ? 24.57372 17.59354 -1.62576  1.000 21.13118 ? 179 MET A C   1 
ATOM   1375 O O   . MET A 1 179 ? 25.40732 17.74557 -2.53361  1.000 19.47361 ? 179 MET A O   1 
ATOM   1376 C CB  . MET A 1 179 ? 22.42540 18.98529 -1.68621  1.000 21.70969 ? 179 MET A CB  1 
ATOM   1377 C CG  . MET A 1 179 ? 22.55046 19.25841 -3.23641  1.000 21.56589 ? 179 MET A CG  1 
ATOM   1378 S SD  . MET A 1 179 ? 20.97458 19.61278 -4.01459  1.000 22.93150 ? 179 MET A SD  1 
ATOM   1379 C CE  . MET A 1 179 ? 21.54891 19.79292 -5.75849  1.000 22.72513 ? 179 MET A CE  1 
ATOM   1380 N N   . GLN A 1 180 ? 24.26220 16.40374 -1.10816  1.000 19.87805 ? 180 GLN A N   1 
ATOM   1381 C CA  . GLN A 1 180 ? 24.96325 15.20242 -1.50142  1.000 18.00557 ? 180 GLN A CA  1 
ATOM   1382 C C   . GLN A 1 180 ? 24.00235 14.10013 -1.93232  1.000 20.78974 ? 180 GLN A C   1 
ATOM   1383 O O   . GLN A 1 180 ? 23.10367 13.69370 -1.18923  1.000 20.44280 ? 180 GLN A O   1 
ATOM   1384 C CB  . GLN A 1 180 ? 25.92744 14.72716 -0.38386  1.000 19.15913 ? 180 GLN A CB  1 
ATOM   1385 C CG  . GLN A 1 180 ? 26.66997 13.43130 -0.72975  1.000 19.09107 ? 180 GLN A CG  1 
ATOM   1386 C CD  . GLN A 1 180 ? 27.73344 13.01191 0.27457   1.000 21.18538 ? 180 GLN A CD  1 
ATOM   1387 O OE1 . GLN A 1 180 ? 28.43459 12.05615 0.05591   1.000 21.27985 ? 180 GLN A OE1 1 
ATOM   1388 N NE2 . GLN A 1 180 ? 27.77883 13.71636 1.44765   1.000 18.98271 ? 180 GLN A NE2 1 
ATOM   1389 N N   . LEU A 1 181 ? 24.24729 13.56571 -3.13111  1.000 18.82443 ? 181 LEU A N   1 
ATOM   1390 C CA  . LEU A 1 181 ? 23.40687 12.53100 -3.71952  1.000 19.50839 ? 181 LEU A CA  1 
ATOM   1391 C C   . LEU A 1 181 ? 24.08056 11.16607 -3.59115  1.000 18.37400 ? 181 LEU A C   1 
ATOM   1392 O O   . LEU A 1 181 ? 25.22964 10.97459 -4.06304  1.000 20.19684 ? 181 LEU A O   1 
ATOM   1393 C CB  . LEU A 1 181 ? 23.18835 12.86071 -5.20613  1.000 21.25398 ? 181 LEU A CB  1 
ATOM   1394 C CG  . LEU A 1 181 ? 22.36481 11.80043 -5.92622  1.000 21.53338 ? 181 LEU A CG  1 
ATOM   1395 C CD1 . LEU A 1 181 ? 20.91744 11.93639 -5.52182  1.000 22.01923 ? 181 LEU A CD1 1 
ATOM   1396 C CD2 . LEU A 1 181 ? 22.46052 12.04649 -7.51810  1.000 19.69216 ? 181 LEU A CD2 1 
ATOM   1397 N N   . THR A 1 182 ? 23.38339 10.21450 -2.93361  1.000 18.37126 ? 182 THR A N   1 
ATOM   1398 C CA  . THR A 1 182 ? 23.86539 8.84497  -2.79908  1.000 18.51740 ? 182 THR A CA  1 
ATOM   1399 C C   . THR A 1 182 ? 22.89918 7.86219  -3.43162  1.000 19.14468 ? 182 THR A C   1 
ATOM   1400 O O   . THR A 1 182 ? 21.68522 8.07125  -3.44920  1.000 19.46305 ? 182 THR A O   1 
ATOM   1401 C CB  . THR A 1 182 ? 24.07554 8.43783  -1.29518  1.000 20.35485 ? 182 THR A CB  1 
ATOM   1402 O OG1 . THR A 1 182 ? 22.89995 8.74395  -0.54908  1.000 21.01021 ? 182 THR A OG1 1 
ATOM   1403 C CG2 . THR A 1 182 ? 25.28780 9.19499  -0.72941  1.000 20.77435 ? 182 THR A CG2 1 
ATOM   1404 N N   . GLU A 1 183 ? 23.46419 6.75733  -3.92313  1.000 21.73157 ? 183 GLU A N   1 
ATOM   1405 C CA  . GLU A 1 183 ? 22.70069 5.68373  -4.54861  1.000 19.96154 ? 183 GLU A CA  1 
ATOM   1406 C C   . GLU A 1 183 ? 22.24898 4.64986  -3.53689  1.000 22.48318 ? 183 GLU A C   1 
ATOM   1407 O O   . GLU A 1 183 ? 22.97445 4.34752  -2.57451  1.000 21.07394 ? 183 GLU A O   1 
ATOM   1408 C CB  . GLU A 1 183 ? 23.56513 4.93561  -5.56079  1.000 25.72623 ? 183 GLU A CB  1 
ATOM   1409 C CG  . GLU A 1 183 ? 24.22708 5.84933  -6.61840  1.000 23.79153 ? 183 GLU A CG  1 
ATOM   1410 C CD  . GLU A 1 183 ? 24.92015 5.05607  -7.70678  1.000 28.42488 ? 183 GLU A CD  1 
ATOM   1411 O OE1 . GLU A 1 183 ? 25.17246 3.84639  -7.48098  1.000 29.56557 ? 183 GLU A OE1 1 
ATOM   1412 O OE2 . GLU A 1 183 ? 25.29316 5.68317  -8.72990  1.000 26.27086 ? 183 GLU A OE2 1 
ATOM   1413 N N   . MET A 1 184 ? 21.08788 4.05981  -3.78737  1.000 20.77690 ? 184 MET A N   1 
ATOM   1414 C CA  . MET A 1 184 ? 20.61871 2.88337  -3.07338  1.000 18.43322 ? 184 MET A CA  1 
ATOM   1415 C C   . MET A 1 184 ? 20.63423 1.72411  -4.04650  1.000 23.74311 ? 184 MET A C   1 
ATOM   1416 O O   . MET A 1 184 ? 19.74230 1.64920  -4.89486  1.000 25.96716 ? 184 MET A O   1 
ATOM   1417 C CB  . MET A 1 184 ? 19.20374 3.06576  -2.51664  1.000 21.49180 ? 184 MET A CB  1 
ATOM   1418 C CG  . MET A 1 184 ? 19.01795 4.33208  -1.72252  1.000 25.74810 ? 184 MET A CG  1 
ATOM   1419 S SD  . MET A 1 184 ? 17.28159 4.35543  -1.20849  1.000 32.06859 ? 184 MET A SD  1 
ATOM   1420 C CE  . MET A 1 184 ? 17.36154 5.97878  -0.49427  1.000 27.10812 ? 184 MET A CE  1 
ATOM   1421 N N   . ALA A 1 185 ? 21.54607 0.77043  -3.84400  1.000 22.29249 ? 185 ALA A N   1 
ATOM   1422 C CA  . ALA A 1 185 ? 21.61676 -0.47888 -4.61117  1.000 20.51508 ? 185 ALA A CA  1 
ATOM   1423 C C   . ALA A 1 185 ? 21.40112 -0.28287 -6.11189  1.000 23.64675 ? 185 ALA A C   1 
ATOM   1424 O O   . ALA A 1 185 ? 20.39902 -0.74533 -6.63961  1.000 25.59704 ? 185 ALA A O   1 
ATOM   1425 C CB  . ALA A 1 185 ? 20.60531 -1.50812 -4.11480  1.000 24.20441 ? 185 ALA A CB  1 
ATOM   1426 N N   . SER A 1 186 ? 22.30679 0.37382  -6.81387  1.000 25.75824 ? 186 SER A N   1 
ATOM   1427 C CA  . SER A 1 186 ? 22.09680 0.46720  -8.27115  1.000 25.44055 ? 186 SER A CA  1 
ATOM   1428 C C   . SER A 1 186 ? 22.53452 -0.81148 -8.95922  1.000 26.34525 ? 186 SER A C   1 
ATOM   1429 O O   . SER A 1 186 ? 23.45596 -1.49813 -8.50842  1.000 27.92524 ? 186 SER A O   1 
ATOM   1430 C CB  . SER A 1 186 ? 22.89230 1.59832  -8.85877  1.000 32.06157 ? 186 SER A CB  1 
ATOM   1431 O OG  . SER A 1 186 ? 24.22615 1.40341  -8.48048  1.000 35.47309 ? 186 SER A OG  1 
ATOM   1432 N N   . ILE A 1 187 ? 21.93702 -1.08606 -10.13360 1.000 25.62851 ? 187 ILE A N   1 
ATOM   1433 C CA  . ILE A 1 187 ? 22.36615 -2.23232 -10.90874 1.000 30.26968 ? 187 ILE A CA  1 
ATOM   1434 C C   . ILE A 1 187 ? 23.50242 -1.77055 -11.82491 1.000 32.12447 ? 187 ILE A C   1 
ATOM   1435 O O   . ILE A 1 187 ? 23.43817 -0.67715 -12.39280 1.000 30.70640 ? 187 ILE A O   1 
ATOM   1436 C CB  . ILE A 1 187 ? 21.18509 -2.82580 -11.68866 1.000 29.84494 ? 187 ILE A CB  1 
ATOM   1437 C CG1 . ILE A 1 187 ? 21.57972 -4.21263 -12.12957 1.000 29.96970 ? 187 ILE A CG1 1 
ATOM   1438 C CG2 . ILE A 1 187 ? 20.80166 -1.93699 -12.85185 1.000 36.01669 ? 187 ILE A CG2 1 
ATOM   1439 C CD1 . ILE A 1 187 ? 20.44257 -5.04124 -12.75964 1.000 33.85920 ? 187 ILE A CD1 1 
ATOM   1440 N N   . ASN A 1 188 ? 24.57359 -2.55463 -11.92291 1.000 30.05536 ? 188 ASN A N   1 
ATOM   1441 C CA  . ASN A 1 188 ? 25.64871 -2.18835 -12.85915 1.000 32.84238 ? 188 ASN A CA  1 
ATOM   1442 C C   . ASN A 1 188 ? 26.13596 -3.44749 -13.54490 1.000 34.67357 ? 188 ASN A C   1 
ATOM   1443 O O   . ASN A 1 188 ? 26.61914 -4.39588 -12.90503 1.000 33.46679 ? 188 ASN A O   1 
ATOM   1444 C CB  . ASN A 1 188 ? 26.82373 -1.44521 -12.18884 1.000 36.78970 ? 188 ASN A CB  1 
ATOM   1445 C CG  . ASN A 1 188 ? 26.56253 0.08688  -12.01796 1.000 37.90145 ? 188 ASN A CG  1 
ATOM   1446 O OD1 . ASN A 1 188 ? 26.92515 0.91401  -12.86959 1.000 35.51533 ? 188 ASN A OD1 1 
ATOM   1447 N ND2 . ASN A 1 188 ? 25.98601 0.45527  -10.89790 1.000 32.49282 ? 188 ASN A ND2 1 
ATOM   1448 N N   . ASN A 1 189 ? 25.99439 -3.45442 -14.85677 1.000 35.27311 ? 189 ASN A N   1 
ATOM   1449 C CA  . ASN A 1 189 ? 26.49881 -4.54820 -15.65208 1.000 37.10793 ? 189 ASN A CA  1 
ATOM   1450 C C   . ASN A 1 189 ? 26.93748 -3.92837 -16.97553 1.000 37.25505 ? 189 ASN A C   1 
ATOM   1451 O O   . ASN A 1 189 ? 27.08634 -2.70326 -17.08905 1.000 48.27133 ? 189 ASN A O   1 
ATOM   1452 C CB  . ASN A 1 189 ? 25.43046 -5.65033 -15.71056 1.000 36.10063 ? 189 ASN A CB  1 
ATOM   1453 C CG  . ASN A 1 189 ? 24.07647 -5.14147 -16.20368 1.000 40.81895 ? 189 ASN A CG  1 
ATOM   1454 O OD1 . ASN A 1 189 ? 24.00543 -4.19071 -16.98562 1.000 41.71118 ? 189 ASN A OD1 1 
ATOM   1455 N ND2 . ASN A 1 189 ? 23.00082 -5.79355 -15.75404 1.000 40.60385 ? 189 ASN A ND2 1 
ATOM   1456 N N   . ARG A 1 190 ? 27.15755 -4.74276 -17.99195 1.000 47.99707 ? 190 ARG A N   1 
ATOM   1457 C CA  . ARG A 1 190 ? 27.61267 -4.13504 -19.24282 1.000 54.95870 ? 190 ARG A CA  1 
ATOM   1458 C C   . ARG A 1 190 ? 26.52551 -3.28639 -19.93010 1.000 49.74485 ? 190 ARG A C   1 
ATOM   1459 O O   . ARG A 1 190 ? 26.85417 -2.47675 -20.79811 1.000 53.28135 ? 190 ARG A O   1 
ATOM   1460 C CB  . ARG A 1 190 ? 28.17365 -5.24327 -20.16951 1.000 49.73931 ? 190 ARG A CB  1 
ATOM   1461 C CG  . ARG A 1 190 ? 27.22805 -5.73886 -21.22985 1.000 52.00845 ? 190 ARG A CG  1 
ATOM   1462 C CD  . ARG A 1 190 ? 27.85622 -6.82987 -22.09404 0.700 48.90071 ? 190 ARG A CD  1 
ATOM   1463 N NE  . ARG A 1 190 ? 26.84687 -7.40245 -22.96780 0.700 63.35525 ? 190 ARG A NE  1 
ATOM   1464 C CZ  . ARG A 1 190 ? 25.96630 -8.31082 -22.57793 0.700 63.67496 ? 190 ARG A CZ  1 
ATOM   1465 N NH1 . ARG A 1 190 ? 25.95548 -8.76861 -21.33835 0.700 55.64860 ? 190 ARG A NH1 1 
ATOM   1466 N NH2 . ARG A 1 190 ? 25.07801 -8.77494 -23.45485 0.700 65.72353 ? 190 ARG A NH2 1 
ATOM   1467 N N   . VAL A 1 191 ? 25.25734 -3.40421 -19.53399 1.000 48.45657 ? 191 VAL A N   1 
ATOM   1468 C CA  . VAL A 1 191 ? 24.18439 -2.63054 -20.13346 1.000 44.28508 ? 191 VAL A CA  1 
ATOM   1469 C C   . VAL A 1 191 ? 23.70626 -1.46763 -19.25952 1.000 45.13007 ? 191 VAL A C   1 
ATOM   1470 O O   . VAL A 1 191 ? 23.14641 -0.49556 -19.78702 1.000 41.14625 ? 191 VAL A O   1 
ATOM   1471 C CB  . VAL A 1 191 ? 23.00707 -3.56196 -20.47015 0.700 47.34741 ? 191 VAL A CB  1 
ATOM   1472 C CG1 . VAL A 1 191 ? 21.71287 -2.77214 -20.45131 0.700 47.17750 ? 191 VAL A CG1 1 
ATOM   1473 C CG2 . VAL A 1 191 ? 23.22114 -4.22285 -21.80235 0.700 54.00493 ? 191 VAL A CG2 1 
ATOM   1474 N N   . TYR A 1 192 ? 23.82169 -1.57107 -17.93772 1.000 41.38864 ? 192 TYR A N   1 
ATOM   1475 C CA  . TYR A 1 192 ? 23.33677 -0.54572 -17.03246 1.000 37.34224 ? 192 TYR A CA  1 
ATOM   1476 C C   . TYR A 1 192 ? 24.53934 0.04597  -16.29929 1.000 34.46430 ? 192 TYR A C   1 
ATOM   1477 O O   . TYR A 1 192 ? 25.33182 -0.70912 -15.73349 1.000 37.65991 ? 192 TYR A O   1 
ATOM   1478 C CB  . TYR A 1 192 ? 22.34898 -1.14379 -16.02733 1.000 41.62181 ? 192 TYR A CB  1 
ATOM   1479 C CG  . TYR A 1 192 ? 21.12699 -1.77466 -16.65556 0.700 37.55929 ? 192 TYR A CG  1 
ATOM   1480 C CD1 . TYR A 1 192 ? 20.41064 -1.10375 -17.63282 0.700 38.10625 ? 192 TYR A CD1 1 
ATOM   1481 C CD2 . TYR A 1 192 ? 20.68331 -3.03152 -16.26305 0.700 36.64662 ? 192 TYR A CD2 1 
ATOM   1482 C CE1 . TYR A 1 192 ? 19.27879 -1.65228 -18.19389 0.700 41.09641 ? 192 TYR A CE1 1 
ATOM   1483 C CE2 . TYR A 1 192 ? 19.55504 -3.60220 -16.83273 0.700 39.73079 ? 192 TYR A CE2 1 
ATOM   1484 C CZ  . TYR A 1 192 ? 18.85257 -2.88559 -17.80010 0.700 40.40570 ? 192 TYR A CZ  1 
ATOM   1485 O OH  . TYR A 1 192 ? 17.72792 -3.39313 -18.39011 0.700 47.46603 ? 192 TYR A OH  1 
ATOM   1486 N N   . ARG A 1 193 ? 24.66102 1.38186  -16.27943 1.000 33.64061 ? 193 ARG A N   1 
ATOM   1487 C CA  . ARG A 1 193 ? 25.84097 1.99875  -15.65192 1.000 29.59132 ? 193 ARG A CA  1 
ATOM   1488 C C   . ARG A 1 193 ? 25.48046 3.26825  -14.89842 1.000 31.85192 ? 193 ARG A C   1 
ATOM   1489 O O   . ARG A 1 193 ? 24.85111 4.17104  -15.47861 1.000 31.95322 ? 193 ARG A O   1 
ATOM   1490 C CB  . ARG A 1 193 ? 26.87171 2.33778  -16.73429 1.000 40.38659 ? 193 ARG A CB  1 
ATOM   1491 C CG  . ARG A 1 193 ? 28.13557 2.96349  -16.17270 1.000 44.82424 ? 193 ARG A CG  1 
ATOM   1492 C CD  . ARG A 1 193 ? 29.30555 1.97508  -16.18122 0.700 48.07041 ? 193 ARG A CD  1 
ATOM   1493 N NE  . ARG A 1 193 ? 30.46400 2.54405  -16.85847 0.700 48.41755 ? 193 ARG A NE  1 
ATOM   1494 C CZ  . ARG A 1 193 ? 30.71732 2.42430  -18.15721 0.700 48.56847 ? 193 ARG A CZ  1 
ATOM   1495 N NH1 . ARG A 1 193 ? 29.91187 1.75195  -18.96315 0.700 55.89330 ? 193 ARG A NH1 1 
ATOM   1496 N NH2 . ARG A 1 193 ? 31.81312 2.98993  -18.65840 0.700 48.41579 ? 193 ARG A NH2 1 
ATOM   1497 N N   . THR A 1 194 ? 25.88237 3.35584  -13.60995 1.000 23.75655 ? 194 THR A N   1 
ATOM   1498 C CA  . THR A 1 194 ? 25.79970 4.59995  -12.87022 1.000 23.23488 ? 194 THR A CA  1 
ATOM   1499 C C   . THR A 1 194 ? 27.18204 4.98227  -12.35287 1.000 23.50577 ? 194 THR A C   1 
ATOM   1500 O O   . THR A 1 194 ? 28.15901 4.23232  -12.48561 1.000 25.14034 ? 194 THR A O   1 
ATOM   1501 C CB  . THR A 1 194 ? 24.83703 4.51091  -11.67441 1.000 26.59158 ? 194 THR A CB  1 
ATOM   1502 O OG1 . THR A 1 194 ? 25.35629 3.52749  -10.79229 1.000 26.67186 ? 194 THR A OG1 1 
ATOM   1503 C CG2 . THR A 1 194 ? 23.46967 4.09431  -12.17716 1.000 28.33292 ? 194 THR A CG2 1 
ATOM   1504 N N   . ILE A 1 195 ? 27.26349 6.18358  -11.78030 1.000 20.90401 ? 195 ILE A N   1 
ATOM   1505 C CA  . ILE A 1 195 ? 28.56578 6.67734  -11.31893 1.000 24.08811 ? 195 ILE A CA  1 
ATOM   1506 C C   . ILE A 1 195 ? 29.04383 5.91876  -10.07216 1.000 24.52903 ? 195 ILE A C   1 
ATOM   1507 O O   . ILE A 1 195 ? 30.25565 5.70974  -9.88763  1.000 24.40767 ? 195 ILE A O   1 
ATOM   1508 C CB  . ILE A 1 195 ? 28.47995 8.19560  -11.07711 1.000 22.74996 ? 195 ILE A CB  1 
ATOM   1509 C CG1 . ILE A 1 195 ? 29.87991 8.81074  -10.85729 1.000 20.87981 ? 195 ILE A CG1 1 
ATOM   1510 C CG2 . ILE A 1 195 ? 27.51031 8.51187  -9.93797  1.000 21.40578 ? 195 ILE A CG2 1 
ATOM   1511 C CD1 . ILE A 1 195 ? 30.85434 8.73497  -12.07846 1.000 27.06908 ? 195 ILE A CD1 1 
ATOM   1512 N N   . GLY A 1 196 ? 28.09591 5.41733  -9.28007  1.000 23.46685 ? 196 GLY A N   1 
ATOM   1513 C CA  . GLY A 1 196 ? 28.33833 4.63589  -8.02287  1.000 23.96638 ? 196 GLY A CA  1 
ATOM   1514 C C   . GLY A 1 196 ? 28.70274 5.56443  -6.86483  1.000 27.01927 ? 196 GLY A C   1 
ATOM   1515 O O   . GLY A 1 196 ? 28.03712 5.56078  -5.81058  1.000 26.07347 ? 196 GLY A O   1 
ATOM   1516 N N   . SER A 1 197 ? 29.66008 6.44664  -7.09015  1.000 22.24845 ? 197 SER A N   1 
ATOM   1517 C CA  . SER A 1 197 ? 30.16936 7.36213  -6.06173  1.000 21.83433 ? 197 SER A CA  1 
ATOM   1518 C C   . SER A 1 197 ? 29.11135 8.36613  -5.61818  1.000 20.29093 ? 197 SER A C   1 
ATOM   1519 O O   . SER A 1 197 ? 28.37168 8.89545  -6.42983  1.000 20.71745 ? 197 SER A O   1 
ATOM   1520 C CB  . SER A 1 197 ? 31.38174 8.16009  -6.60810  1.000 18.73346 ? 197 SER A CB  1 
ATOM   1521 O OG  . SER A 1 197 ? 32.38128 7.30769  -7.05966  1.000 21.64981 ? 197 SER A OG  1 
ATOM   1522 N N   . PRO A 1 198 ? 29.09976 8.73135  -4.33842  1.000 18.11987 ? 198 PRO A N   1 
ATOM   1523 C CA  . PRO A 1 198 ? 28.30219 9.89701  -3.91944  1.000 19.13172 ? 198 PRO A CA  1 
ATOM   1524 C C   . PRO A 1 198 ? 28.74416 11.10799 -4.72539  1.000 15.72728 ? 198 PRO A C   1 
ATOM   1525 O O   . PRO A 1 198 ? 29.92277 11.25120 -5.05942  1.000 20.40638 ? 198 PRO A O   1 
ATOM   1526 C CB  . PRO A 1 198 ? 28.66568 10.05457 -2.40237  1.000 23.70742 ? 198 PRO A CB  1 
ATOM   1527 C CG  . PRO A 1 198 ? 29.20550 8.70232  -2.02301  1.000 21.63658 ? 198 PRO A CG  1 
ATOM   1528 C CD  . PRO A 1 198 ? 29.94943 8.20027  -3.26927  1.000 18.65560 ? 198 PRO A CD  1 
ATOM   1529 N N   . LEU A 1 199 ? 27.80723 12.00878 -5.00164  1.000 19.77980 ? 199 LEU A N   1 
ATOM   1530 C CA  . LEU A 1 199 ? 28.10493 13.26937 -5.66143  1.000 20.54902 ? 199 LEU A CA  1 
ATOM   1531 C C   . LEU A 1 199 ? 27.76034 14.43864 -4.75539  1.000 18.69663 ? 199 LEU A C   1 
ATOM   1532 O O   . LEU A 1 199 ? 26.66929 14.48014 -4.17306  1.000 21.17935 ? 199 LEU A O   1 
ATOM   1533 C CB  . LEU A 1 199 ? 27.27697 13.41721 -6.96674  1.000 21.04726 ? 199 LEU A CB  1 
ATOM   1534 C CG  . LEU A 1 199 ? 27.41004 12.20690 -7.85388  1.000 17.91363 ? 199 LEU A CG  1 
ATOM   1535 C CD1 . LEU A 1 199 ? 26.50105 12.53285 -9.11274  1.000 22.00891 ? 199 LEU A CD1 1 
ATOM   1536 C CD2 . LEU A 1 199 ? 28.85402 11.95395 -8.36234  1.000 21.53985 ? 199 LEU A CD2 1 
ATOM   1537 N N   . VAL A 1 200 ? 28.65284 15.41942 -4.69600  1.000 20.59983 ? 200 VAL A N   1 
ATOM   1538 C CA  . VAL A 1 200 ? 28.44445 16.61539 -3.85835  1.000 18.82064 ? 200 VAL A CA  1 
ATOM   1539 C C   . VAL A 1 200 ? 28.29924 17.85022 -4.74392  1.000 20.96698 ? 200 VAL A C   1 
ATOM   1540 O O   . VAL A 1 200 ? 29.20275 18.17466 -5.56024  1.000 21.53851 ? 200 VAL A O   1 
ATOM   1541 C CB  . VAL A 1 200 ? 29.60389 16.79780 -2.85928  1.000 21.58224 ? 200 VAL A CB  1 
ATOM   1542 C CG1 . VAL A 1 200 ? 29.39799 18.07668 -2.09125  1.000 21.78376 ? 200 VAL A CG1 1 
ATOM   1543 C CG2 . VAL A 1 200 ? 29.67185 15.63104 -1.92909  1.000 22.65560 ? 200 VAL A CG2 1 
ATOM   1544 N N   . PHE A 1 201 ? 27.16022 18.53971 -4.59758  1.000 20.44329 ? 201 PHE A N   1 
ATOM   1545 C CA  . PHE A 1 201 ? 26.75895 19.67963 -5.41391  1.000 23.89382 ? 201 PHE A CA  1 
ATOM   1546 C C   . PHE A 1 201 ? 26.78081 20.97364 -4.61589  1.000 25.43853 ? 201 PHE A C   1 
ATOM   1547 O O   . PHE A 1 201 ? 26.32760 21.00018 -3.47046  1.000 26.40798 ? 201 PHE A O   1 
ATOM   1548 C CB  . PHE A 1 201 ? 25.35028 19.47512 -6.00546  1.000 22.02137 ? 201 PHE A CB  1 
ATOM   1549 C CG  . PHE A 1 201 ? 25.22873 18.24732 -6.80585  1.000 20.70334 ? 201 PHE A CG  1 
ATOM   1550 C CD1 . PHE A 1 201 ? 25.49292 18.26037 -8.20087  1.000 23.92069 ? 201 PHE A CD1 1 
ATOM   1551 C CD2 . PHE A 1 201 ? 24.79604 17.09392 -6.24274  1.000 22.52703 ? 201 PHE A CD2 1 
ATOM   1552 C CE1 . PHE A 1 201 ? 25.37408 17.11436 -8.94143  1.000 24.61280 ? 201 PHE A CE1 1 
ATOM   1553 C CE2 . PHE A 1 201 ? 24.66684 15.92601 -6.97937  1.000 22.34964 ? 201 PHE A CE2 1 
ATOM   1554 C CZ  . PHE A 1 201 ? 24.97642 15.94569 -8.37561  1.000 22.32864 ? 201 PHE A CZ  1 
ATOM   1555 N N   . PRO A 1 202 ? 27.26752 22.05072 -5.22395  1.000 24.33523 ? 202 PRO A N   1 
ATOM   1556 C CA  . PRO A 1 202 ? 27.24322 23.37727 -4.59775  1.000 24.49418 ? 202 PRO A CA  1 
ATOM   1557 C C   . PRO A 1 202 ? 25.88971 24.05701 -4.75067  1.000 27.54963 ? 202 PRO A C   1 
ATOM   1558 O O   . PRO A 1 202 ? 24.98675 23.58041 -5.44194  1.000 23.74654 ? 202 PRO A O   1 
ATOM   1559 C CB  . PRO A 1 202 ? 28.30559 24.16592 -5.40029  1.000 28.69153 ? 202 PRO A CB  1 
ATOM   1560 C CG  . PRO A 1 202 ? 28.19940 23.57236 -6.74363  1.000 26.13187 ? 202 PRO A CG  1 
ATOM   1561 C CD  . PRO A 1 202 ? 27.90865 22.09035 -6.56501  1.000 23.92780 ? 202 PRO A CD  1 
ATOM   1562 N N   . LYS A 1 203 ? 25.75518 25.18414 -4.04808  1.000 27.81899 ? 203 LYS A N   1 
ATOM   1563 C CA  . LYS A 1 203 ? 24.62799 26.07647 -4.27056  1.000 30.44722 ? 203 LYS A CA  1 
ATOM   1564 C C   . LYS A 1 203 ? 24.44636 26.34390 -5.74891  1.000 33.69934 ? 203 LYS A C   1 
ATOM   1565 O O   . LYS A 1 203 ? 25.42111 26.52564 -6.47852  1.000 31.50745 ? 203 LYS A O   1 
ATOM   1566 C CB  . LYS A 1 203 ? 24.84217 27.42410 -3.56841  1.000 36.84330 ? 203 LYS A CB  1 
ATOM   1567 C CG  . LYS A 1 203 ? 24.78312 27.36493 -2.11175  0.700 34.20957 ? 203 LYS A CG  1 
ATOM   1568 C CD  . LYS A 1 203 ? 24.26380 28.70774 -1.55147  0.700 35.73597 ? 203 LYS A CD  1 
ATOM   1569 C CE  . LYS A 1 203 ? 22.75962 28.87066 -1.82705  0.700 38.73414 ? 203 LYS A CE  1 
ATOM   1570 N NZ  . LYS A 1 203 ? 21.93058 28.93228 -0.56208  0.700 33.83487 ? 203 LYS A NZ  1 
ATOM   1571 N N   . HIS A 1 204 ? 23.18386 26.44447 -6.16398  1.000 30.93601 ? 204 HIS A N   1 
ATOM   1572 C CA  . HIS A 1 204 ? 22.80358 26.89178 -7.49850  1.000 32.63677 ? 204 HIS A CA  1 
ATOM   1573 C C   . HIS A 1 204 ? 22.85134 25.76416 -8.52857  1.000 30.49916 ? 204 HIS A C   1 
ATOM   1574 O O   . HIS A 1 204 ? 22.27528 25.90769 -9.61341  1.000 36.07749 ? 204 HIS A O   1 
ATOM   1575 C CB  . HIS A 1 204 ? 23.67396 28.06103 -7.97692  1.000 35.08316 ? 204 HIS A CB  1 
ATOM   1576 C CG  . HIS A 1 204 ? 23.62752 29.25228 -7.07254  1.000 35.70098 ? 204 HIS A CG  1 
ATOM   1577 N ND1 . HIS A 1 204 ? 22.45185 29.89471 -6.74421  1.000 40.38650 ? 204 HIS A ND1 1 
ATOM   1578 C CD2 . HIS A 1 204 ? 24.60734 29.90002 -6.39920  1.000 40.92513 ? 204 HIS A CD2 1 
ATOM   1579 C CE1 . HIS A 1 204 ? 22.71259 30.90493 -5.93408  1.000 39.70296 ? 204 HIS A CE1 1 
ATOM   1580 N NE2 . HIS A 1 204 ? 24.01317 30.92885 -5.70964  1.000 44.40021 ? 204 HIS A NE2 1 
ATOM   1581 N N   . HIS A 1 205 ? 23.50783 24.65044 -8.22919  1.000 29.89029 ? 205 HIS A N   1 
ATOM   1582 C CA  . HIS A 1 205 ? 23.35458 23.51009 -9.11325  1.000 26.64301 ? 205 HIS A CA  1 
ATOM   1583 C C   . HIS A 1 205 ? 21.98598 22.88996 -8.87387  1.000 31.49200 ? 205 HIS A C   1 
ATOM   1584 O O   . HIS A 1 205 ? 21.50661 22.82724 -7.74153  1.000 28.12688 ? 205 HIS A O   1 
ATOM   1585 C CB  . HIS A 1 205 ? 24.46368 22.47132 -8.88745  1.000 23.59519 ? 205 HIS A CB  1 
ATOM   1586 C CG  . HIS A 1 205 ? 25.76705 22.89312 -9.46055  1.000 24.95020 ? 205 HIS A CG  1 
ATOM   1587 N ND1 . HIS A 1 205 ? 26.71717 21.99712 -9.87608  1.000 27.11193 ? 205 HIS A ND1 1 
ATOM   1588 C CD2 . HIS A 1 205 ? 26.26054 24.12773 -9.72250  1.000 29.64464 ? 205 HIS A CD2 1 
ATOM   1589 C CE1 . HIS A 1 205 ? 27.74853 22.66166 -10.37425 1.000 30.60814 ? 205 HIS A CE1 1 
ATOM   1590 N NE2 . HIS A 1 205 ? 27.49132 23.95748 -10.30645 1.000 31.40436 ? 205 HIS A NE2 1 
ATOM   1591 N N   . VAL A 1 206 ? 21.37156 22.39222 -9.93866  1.000 26.08266 ? 206 VAL A N   1 
ATOM   1592 C CA  . VAL A 1 206 ? 20.05991 21.78524 -9.86212  1.000 25.76818 ? 206 VAL A CA  1 
ATOM   1593 C C   . VAL A 1 206 ? 20.18042 20.37244 -10.39021 1.000 27.04165 ? 206 VAL A C   1 
ATOM   1594 O O   . VAL A 1 206 ? 20.65480 20.16122 -11.51996 1.000 30.62904 ? 206 VAL A O   1 
ATOM   1595 C CB  . VAL A 1 206 ? 19.01741 22.57118 -10.68260 1.000 32.77445 ? 206 VAL A CB  1 
ATOM   1596 C CG1 . VAL A 1 206 ? 17.66649 21.87713 -10.62712 1.000 34.56709 ? 206 VAL A CG1 1 
ATOM   1597 C CG2 . VAL A 1 206 ? 18.89742 23.99278 -10.17670 1.000 32.08546 ? 206 VAL A CG2 1 
ATOM   1598 N N   . VAL A 1 207 ? 19.64277 19.43435 -9.62828  1.000 23.48434 ? 207 VAL A N   1 
ATOM   1599 C CA  . VAL A 1 207 ? 19.64228 18.03022 -9.97333  1.000 25.75832 ? 207 VAL A CA  1 
ATOM   1600 C C   . VAL A 1 207 ? 18.18416 17.65389 -10.17043 1.000 27.70342 ? 207 VAL A C   1 
ATOM   1601 O O   . VAL A 1 207 ? 17.34887 17.86683 -9.27575  1.000 26.05330 ? 207 VAL A O   1 
ATOM   1602 C CB  . VAL A 1 207 ? 20.29951 17.16983 -8.87394  1.000 25.56734 ? 207 VAL A CB  1 
ATOM   1603 C CG1 . VAL A 1 207 ? 20.15893 15.68972 -9.24138  1.000 24.28027 ? 207 VAL A CG1 1 
ATOM   1604 C CG2 . VAL A 1 207 ? 21.78449 17.54008 -8.70736  1.000 24.57914 ? 207 VAL A CG2 1 
ATOM   1605 N N   . SER A 1 208 ? 17.86270 17.16092 -11.36010 1.000 23.35974 ? 208 SER A N   1 
ATOM   1606 C CA  . SER A 1 208 ? 16.49760 16.84568 -11.73056 1.000 24.22600 ? 208 SER A CA  1 
ATOM   1607 C C   . SER A 1 208 ? 16.39151 15.35265 -12.01980 1.000 31.98530 ? 208 SER A C   1 
ATOM   1608 O O   . SER A 1 208 ? 17.22342 14.80630 -12.74301 1.000 31.13660 ? 208 SER A O   1 
ATOM   1609 C CB  . SER A 1 208 ? 16.11931 17.68980 -12.98727 1.000 31.63844 ? 208 SER A CB  1 
ATOM   1610 O OG  . SER A 1 208 ? 14.86871 17.29614 -13.50266 1.000 38.59230 ? 208 SER A OG  1 
ATOM   1611 N N   . LEU A 1 209 ? 15.38427 14.68354 -11.46224 1.000 27.86512 ? 209 LEU A N   1 
ATOM   1612 C CA  . LEU A 1 209 ? 15.12402 13.28276 -11.78089 1.000 29.29761 ? 209 LEU A CA  1 
ATOM   1613 C C   . LEU A 1 209 ? 13.93171 13.22913 -12.69580 1.000 29.74830 ? 209 LEU A C   1 
ATOM   1614 O O   . LEU A 1 209 ? 12.90732 13.83302 -12.38462 1.000 33.35819 ? 209 LEU A O   1 
ATOM   1615 C CB  . LEU A 1 209 ? 14.80532 12.44740 -10.53349 1.000 26.45680 ? 209 LEU A CB  1 
ATOM   1616 C CG  . LEU A 1 209 ? 15.85963 12.58657 -9.46266  1.000 25.26223 ? 209 LEU A CG  1 
ATOM   1617 C CD1 . LEU A 1 209 ? 15.52844 11.65165 -8.23286  1.000 26.54603 ? 209 LEU A CD1 1 
ATOM   1618 C CD2 . LEU A 1 209 ? 17.27620 12.31452 -9.98434  1.000 24.77412 ? 209 LEU A CD2 1 
ATOM   1619 N N   . GLN A 1 210 ? 14.05257 12.51193 -13.80581 1.000 27.07774 ? 210 GLN A N   1 
ATOM   1620 C CA  . GLN A 1 210 ? 12.98758 12.49536 -14.76722 1.000 28.95234 ? 210 GLN A CA  1 
ATOM   1621 C C   . GLN A 1 210 ? 12.56138 11.04954 -14.97720 1.000 31.15883 ? 210 GLN A C   1 
ATOM   1622 O O   . GLN A 1 210 ? 13.41177 10.19084 -15.27807 1.000 32.53257 ? 210 GLN A O   1 
ATOM   1623 C CB  . GLN A 1 210 ? 13.45184 13.15742 -16.13771 1.000 32.52573 ? 210 GLN A CB  1 
ATOM   1624 C CG  . GLN A 1 210 ? 13.61862 14.66795 -15.89585 1.000 38.98994 ? 210 GLN A CG  1 
ATOM   1625 C CD  . GLN A 1 210 ? 14.36676 15.40156 -16.97729 1.000 41.41912 ? 210 GLN A CD  1 
ATOM   1626 O OE1 . GLN A 1 210 ? 14.29094 15.04571 -18.15172 1.000 44.14554 ? 210 GLN A OE1 1 
ATOM   1627 N NE2 . GLN A 1 210 ? 15.07690 16.47418 -16.58466 1.000 43.73987 ? 210 GLN A NE2 1 
ATOM   1628 N N   . PRO A 1 211 ? 11.27639 10.73953 -14.83592 1.000 34.32160 ? 211 PRO A N   1 
ATOM   1629 C CA  . PRO A 1 211 ? 10.82501 9.36683  -15.01731 1.000 32.84178 ? 211 PRO A CA  1 
ATOM   1630 C C   . PRO A 1 211 ? 11.15715 8.86568  -16.40350 1.000 32.29694 ? 211 PRO A C   1 
ATOM   1631 O O   . PRO A 1 211 ? 11.19000 9.62815  -17.37405 1.000 33.26762 ? 211 PRO A O   1 
ATOM   1632 C CB  . PRO A 1 211 ? 9.30490  9.47656  -14.84527 1.000 35.20267 ? 211 PRO A CB  1 
ATOM   1633 C CG  . PRO A 1 211 ? 9.17270  10.65103 -13.87768 1.000 42.27363 ? 211 PRO A CG  1 
ATOM   1634 C CD  . PRO A 1 211 ? 10.14344 11.61820 -14.48295 1.000 41.12797 ? 211 PRO A CD  1 
ATOM   1635 N N   . VAL A 1 212 ? 11.27963 7.55514  -16.48609 1.000 32.73207 ? 212 VAL A N   1 
ATOM   1636 C CA  . VAL A 1 212 ? 11.52114 6.84164  -17.73259 1.000 36.74361 ? 212 VAL A CA  1 
ATOM   1637 C C   . VAL A 1 212 ? 10.29969 6.04403  -18.15401 1.000 41.75497 ? 212 VAL A C   1 
ATOM   1638 O O   . VAL A 1 212 ? 9.87286  6.11033  -19.30709 1.000 39.55113 ? 212 VAL A O   1 
ATOM   1639 C CB  . VAL A 1 212 ? 12.76857 5.93758  -17.59811 1.000 33.83842 ? 212 VAL A CB  1 
ATOM   1640 C CG1 . VAL A 1 212 ? 12.95549 5.09544  -18.83291 1.000 38.99992 ? 212 VAL A CG1 1 
ATOM   1641 C CG2 . VAL A 1 212 ? 14.00044 6.77221  -17.32474 1.000 33.36657 ? 212 VAL A CG2 1 
ATOM   1642 N N   . ASN A 1 213 ? 9.70196  5.30243  -17.22792 1.000 36.92795 ? 213 ASN A N   1 
ATOM   1643 C CA  . ASN A 1 213 ? 8.47652  4.57845  -17.54383 1.000 41.57777 ? 213 ASN A CA  1 
ATOM   1644 C C   . ASN A 1 213 ? 7.39999  4.88256  -16.51942 1.000 40.53497 ? 213 ASN A C   1 
ATOM   1645 O O   . ASN A 1 213 ? 6.48610  5.65584  -16.79506 1.000 44.56466 ? 213 ASN A O   1 
ATOM   1646 C CB  . ASN A 1 213 ? 8.71851  3.06691  -17.60415 1.000 50.01252 ? 213 ASN A CB  1 
ATOM   1647 C CG  . ASN A 1 213 ? 9.71853  2.67848  -18.69648 0.700 55.17581 ? 213 ASN A CG  1 
ATOM   1648 O OD1 . ASN A 1 213 ? 9.74319  3.28127  -19.77116 0.700 53.13604 ? 213 ASN A OD1 1 
ATOM   1649 N ND2 . ASN A 1 213 ? 10.56778 1.68885  -18.40620 0.700 56.97169 ? 213 ASN A ND2 1 
ATOM   1650 N N   . ASP A 1 214 ? 7.51428  4.28868  -15.33662 1.000 39.87241 ? 214 ASP A N   1 
ATOM   1651 C CA  . ASP A 1 214 ? 6.54763  4.53731  -14.27525 1.000 43.19448 ? 214 ASP A CA  1 
ATOM   1652 C C   . ASP A 1 214 ? 6.70257  5.96506  -13.79331 1.000 39.79170 ? 214 ASP A C   1 
ATOM   1653 O O   . ASP A 1 214 ? 7.81670  6.47324  -13.65611 1.000 41.27781 ? 214 ASP A O   1 
ATOM   1654 C CB  . ASP A 1 214 ? 6.74806  3.57728  -13.09085 1.000 45.65520 ? 214 ASP A CB  1 
ATOM   1655 C CG  . ASP A 1 214 ? 5.58745  3.63716  -12.06222 0.700 45.42592 ? 214 ASP A CG  1 
ATOM   1656 O OD1 . ASP A 1 214 ? 4.40922  3.64954  -12.48294 0.700 55.19423 ? 214 ASP A OD1 1 
ATOM   1657 O OD2 . ASP A 1 214 ? 5.84781  3.61816  -10.83637 0.700 50.04213 ? 214 ASP A OD2 1 
ATOM   1658 N N   . LYS A 1 215 ? 5.58174  6.62287  -13.54465 1.000 41.54665 ? 215 LYS A N   1 
ATOM   1659 C CA  . LYS A 1 215 ? 5.63494  8.00930  -13.12570 1.000 39.75497 ? 215 LYS A CA  1 
ATOM   1660 C C   . LYS A 1 215 ? 5.24595  8.18518  -11.66093 1.000 41.12174 ? 215 LYS A C   1 
ATOM   1661 O O   . LYS A 1 215 ? 5.11998  9.32463  -11.21392 1.000 40.24948 ? 215 LYS A O   1 
ATOM   1662 C CB  . LYS A 1 215 ? 4.73982  8.86231  -14.03784 1.000 43.48931 ? 215 LYS A CB  1 
ATOM   1663 C CG  . LYS A 1 215 ? 5.29082  9.01251  -15.45347 1.000 45.41302 ? 215 LYS A CG  1 
ATOM   1664 C CD  . LYS A 1 215 ? 4.51246  10.05591 -16.27888 0.800 43.56988 ? 215 LYS A CD  1 
ATOM   1665 C CE  . LYS A 1 215 ? 3.09024  9.62446  -16.56996 0.700 52.87385 ? 215 LYS A CE  1 
ATOM   1666 N NZ  . LYS A 1 215 ? 2.37420  10.55781 -17.51491 0.700 61.37207 ? 215 LYS A NZ  1 
ATOM   1667 N N   . ASP A 1 216 ? 5.07228  7.09205  -10.90676 1.000 37.50365 ? 216 ASP A N   1 
ATOM   1668 C CA  . ASP A 1 216 ? 4.65623  7.15653  -9.50139  1.000 39.98167 ? 216 ASP A CA  1 
ATOM   1669 C C   . ASP A 1 216 ? 5.84238  6.87914  -8.59597  1.000 36.34812 ? 216 ASP A C   1 
ATOM   1670 O O   . ASP A 1 216 ? 6.60009  5.93441  -8.83649  1.000 35.05326 ? 216 ASP A O   1 
ATOM   1671 C CB  . ASP A 1 216 ? 3.55691  6.14338  -9.19614  1.000 35.79096 ? 216 ASP A CB  1 
ATOM   1672 C CG  . ASP A 1 216 ? 2.25171  6.44017  -9.94100  1.000 43.93645 ? 216 ASP A CG  1 
ATOM   1673 O OD1 . ASP A 1 216 ? 2.18715  7.45907  -10.66004 1.000 42.72886 ? 216 ASP A OD1 1 
ATOM   1674 O OD2 . ASP A 1 216 ? 1.30052  5.64564  -9.80086  1.000 44.81096 ? 216 ASP A OD2 1 
ATOM   1675 N N   . PHE A 1 217 ? 5.99455  7.68999  -7.54305  1.000 32.06408 ? 217 PHE A N   1 
ATOM   1676 C CA  . PHE A 1 217 ? 7.16220  7.60988  -6.69476  1.000 27.56948 ? 217 PHE A CA  1 
ATOM   1677 C C   . PHE A 1 217 ? 6.76307  7.85867  -5.25585  1.000 33.59618 ? 217 PHE A C   1 
ATOM   1678 O O   . PHE A 1 217 ? 5.86899  8.65660  -4.97968  1.000 32.38456 ? 217 PHE A O   1 
ATOM   1679 C CB  . PHE A 1 217 ? 8.21234  8.66573  -7.04038  1.000 30.31974 ? 217 PHE A CB  1 
ATOM   1680 C CG  . PHE A 1 217 ? 8.70373  8.52510  -8.45467  1.000 30.38774 ? 217 PHE A CG  1 
ATOM   1681 C CD1 . PHE A 1 217 ? 8.02878  9.13903  -9.48920  1.000 36.01763 ? 217 PHE A CD1 1 
ATOM   1682 C CD2 . PHE A 1 217 ? 9.80006  7.71850  -8.73025  1.000 32.61165 ? 217 PHE A CD2 1 
ATOM   1683 C CE1 . PHE A 1 217 ? 8.46749  8.98639  -10.82849 1.000 34.43397 ? 217 PHE A CE1 1 
ATOM   1684 C CE2 . PHE A 1 217 ? 10.25040 7.56174  -10.06027 1.000 31.18766 ? 217 PHE A CE2 1 
ATOM   1685 C CZ  . PHE A 1 217 ? 9.56187  8.19580  -11.09316 1.000 33.83772 ? 217 PHE A CZ  1 
ATOM   1686 N N   . GLN A 1 218 ? 7.51680  7.25458  -4.35755  1.000 28.88925 ? 218 GLN A N   1 
ATOM   1687 C CA  . GLN A 1 218 ? 7.41150  7.53369  -2.92913  1.000 30.04652 ? 218 GLN A CA  1 
ATOM   1688 C C   . GLN A 1 218 ? 8.54809  8.48105  -2.57747  1.000 27.97067 ? 218 GLN A C   1 
ATOM   1689 O O   . GLN A 1 218 ? 9.72361  8.12276  -2.73145  1.000 27.12467 ? 218 GLN A O   1 
ATOM   1690 C CB  . GLN A 1 218 ? 7.49370  6.22061  -2.14427  1.000 35.43426 ? 218 GLN A CB  1 
ATOM   1691 C CG  . GLN A 1 218 ? 7.09300  6.30199  -0.63241  0.800 36.83119 ? 218 GLN A CG  1 
ATOM   1692 C CD  . GLN A 1 218 ? 5.57442  6.31859  -0.42461  0.800 35.83374 ? 218 GLN A CD  1 
ATOM   1693 O OE1 . GLN A 1 218 ? 4.80631  5.82245  -1.24929  0.800 43.06929 ? 218 GLN A OE1 1 
ATOM   1694 N NE2 . GLN A 1 218 ? 5.13982  6.87887  0.69324   0.800 41.73100 ? 218 GLN A NE2 1 
ATOM   1695 N N   . ILE A 1 219 ? 8.22264  9.70462  -2.13794  1.000 26.64621 ? 219 ILE A N   1 
ATOM   1696 C CA  . ILE A 1 219 ? 9.22715  10.72666 -1.86899  1.000 25.14204 ? 219 ILE A CA  1 
ATOM   1697 C C   . ILE A 1 219 ? 9.20027  10.96346 -0.36166  1.000 28.95424 ? 219 ILE A C   1 
ATOM   1698 O O   . ILE A 1 219 ? 8.12690  11.23518 0.19688   1.000 30.44799 ? 219 ILE A O   1 
ATOM   1699 C CB  . ILE A 1 219 ? 8.96305  12.02124 -2.64508  1.000 32.25592 ? 219 ILE A CB  1 
ATOM   1700 C CG1 . ILE A 1 219 ? 9.12019  11.74888 -4.18037  1.000 30.58105 ? 219 ILE A CG1 1 
ATOM   1701 C CG2 . ILE A 1 219 ? 9.99784  13.04548 -2.25064  1.000 34.12085 ? 219 ILE A CG2 1 
ATOM   1702 C CD1 . ILE A 1 219 ? 8.43650  12.77189 -5.06890  1.000 34.13846 ? 219 ILE A CD1 1 
ATOM   1703 N N   . SER A 1 220 ? 10.35257 10.78904 0.29377   1.000 28.22852 ? 220 SER A N   1 
ATOM   1704 C CA  . SER A 1 220 ? 10.43198 11.06196 1.73254   1.000 29.59675 ? 220 SER A CA  1 
ATOM   1705 C C   . SER A 1 220 ? 11.16217 12.38752 1.92038   1.000 32.49383 ? 220 SER A C   1 
ATOM   1706 O O   . SER A 1 220 ? 12.04552 12.74921 1.13484   1.000 34.56210 ? 220 SER A O   1 
ATOM   1707 C CB  . SER A 1 220 ? 11.18602 9.96228  2.43828   1.000 29.30876 ? 220 SER A CB  1 
ATOM   1708 O OG  . SER A 1 220 ? 12.59261 10.30389 2.34396   1.000 32.42604 ? 220 SER A OG  1 
ATOM   1709 N N   . VAL A 1 221 ? 10.72579 13.17164 2.88380   1.000 26.16868 ? 221 VAL A N   1 
ATOM   1710 C CA  . VAL A 1 221 ? 11.45607 14.35567 3.29652   1.000 25.22659 ? 221 VAL A CA  1 
ATOM   1711 C C   . VAL A 1 221 ? 11.60713 14.18211 4.81080   1.000 27.94418 ? 221 VAL A C   1 
ATOM   1712 O O   . VAL A 1 221 ? 10.59627 14.21033 5.52715   1.000 29.77351 ? 221 VAL A O   1 
ATOM   1713 C CB  . VAL A 1 221 ? 10.65727 15.62653 2.99160   1.000 31.18894 ? 221 VAL A CB  1 
ATOM   1714 C CG1 . VAL A 1 221 ? 11.37136 16.84815 3.51930   1.000 31.97748 ? 221 VAL A CG1 1 
ATOM   1715 C CG2 . VAL A 1 221 ? 10.43167 15.74872 1.45841   1.000 33.62263 ? 221 VAL A CG2 1 
ATOM   1716 N N   . ASP A 1 222 ? 12.82510 13.98349 5.28536   1.000 25.08746 ? 222 ASP A N   1 
ATOM   1717 C CA  . ASP A 1 222 ? 13.01496 13.81697 6.73755   1.000 28.95291 ? 222 ASP A CA  1 
ATOM   1718 C C   . ASP A 1 222 ? 12.11290 12.63523 7.12805   1.000 29.73217 ? 222 ASP A C   1 
ATOM   1719 O O   . ASP A 1 222 ? 12.04954 11.62422 6.41567   1.000 32.20464 ? 222 ASP A O   1 
ATOM   1720 C CB  . ASP A 1 222 ? 12.77426 15.15325 7.40285   1.000 28.25715 ? 222 ASP A CB  1 
ATOM   1721 C CG  . ASP A 1 222 ? 13.86272 16.14684 7.05756   1.000 23.54151 ? 222 ASP A CG  1 
ATOM   1722 O OD1 . ASP A 1 222 ? 14.96665 15.72323 6.61641   1.000 23.08058 ? 222 ASP A OD1 1 
ATOM   1723 O OD2 . ASP A 1 222 ? 13.64817 17.34978 7.25476   1.000 28.15976 ? 222 ASP A OD2 1 
ATOM   1724 N N   . HIS A 1 223 ? 11.35020 12.59670 8.21369   1.000 28.41526 ? 223 HIS A N   1 
ATOM   1725 C CA  A HIS A 1 223 ? 10.58828 11.40938 8.57037   0.500 38.21805 ? 223 HIS A CA  1 
ATOM   1726 C CA  B HIS A 1 223 ? 10.77930 11.24018 8.27898   0.500 38.30721 ? 223 HIS A CA  1 
ATOM   1727 C C   . HIS A 1 223 ? 9.39260  11.11370 7.65246   1.000 42.30441 ? 223 HIS A C   1 
ATOM   1728 O O   . HIS A 1 223 ? 8.67346  10.15338 7.94533   1.000 51.05372 ? 223 HIS A O   1 
ATOM   1729 C CB  A HIS A 1 223 ? 10.09169 11.54131 10.02113  0.500 38.37301 ? 223 HIS A CB  1 
ATOM   1730 C CB  B HIS A 1 223 ? 10.74933 10.58844 9.65986   0.500 40.83087 ? 223 HIS A CB  1 
ATOM   1731 C CG  A HIS A 1 223 ? 9.48289  12.87733 10.33888  0.500 40.17576 ? 223 HIS A CG  1 
ATOM   1732 C CG  B HIS A 1 223 ? 10.76224 9.08232  9.55866   0.500 36.69208 ? 223 HIS A CG  1 
ATOM   1733 N ND1 A HIS A 1 223 ? 10.20845 14.05095 10.28961  0.500 34.18261 ? 223 HIS A ND1 1 
ATOM   1734 N ND1 B HIS A 1 223 ? 9.78396  8.27237  10.09918  0.500 42.51176 ? 223 HIS A ND1 1 
ATOM   1735 C CD2 A HIS A 1 223 ? 8.22881  13.22509 10.72344  0.500 45.29158 ? 223 HIS A CD2 1 
ATOM   1736 C CD2 B HIS A 1 223 ? 11.59565 8.25776  8.87569   0.500 36.58005 ? 223 HIS A CD2 1 
ATOM   1737 C CE1 A HIS A 1 223 ? 9.42151  15.06474 10.61059  0.500 37.38046 ? 223 HIS A CE1 1 
ATOM   1738 C CE1 B HIS A 1 223 ? 10.05268 7.00967  9.80856   0.500 42.88937 ? 223 HIS A CE1 1 
ATOM   1739 N NE2 A HIS A 1 223 ? 8.21922  14.59126 10.89139  0.500 42.78765 ? 223 HIS A NE2 1 
ATOM   1740 N NE2 B HIS A 1 223 ? 11.14860 6.97453  9.06872   0.500 39.58921 ? 223 HIS A NE2 1 
ATOM   1741 N N   . LEU A 1 224 ? 9.08443  11.91664 6.64797   1.000 33.17882 ? 224 LEU A N   1 
ATOM   1742 C CA  . LEU A 1 224 ? 7.71620  11.99356 6.13874   1.000 32.75271 ? 224 LEU A CA  1 
ATOM   1743 C C   . LEU A 1 224 ? 7.67075  11.46683 4.69896   1.000 38.35308 ? 224 LEU A C   1 
ATOM   1744 O O   . LEU A 1 224 ? 8.29422  12.04528 3.80997   1.000 37.87564 ? 224 LEU A O   1 
ATOM   1745 C CB  . LEU A 1 224 ? 7.25932  13.44061 6.18334   1.000 32.10981 ? 224 LEU A CB  1 
ATOM   1746 C CG  . LEU A 1 224 ? 5.86202  13.67304 5.58995   0.800 39.09230 ? 224 LEU A CG  1 
ATOM   1747 C CD1 . LEU A 1 224 ? 4.75001  13.36290 6.56536   0.700 47.51615 ? 224 LEU A CD1 1 
ATOM   1748 C CD2 . LEU A 1 224 ? 5.75101  15.08949 5.00610   0.700 47.42955 ? 224 LEU A CD2 1 
ATOM   1749 N N   . SER A 1 225 ? 6.93644  10.38958 4.46255   1.000 35.07779 ? 225 SER A N   1 
ATOM   1750 C CA  . SER A 1 225 ? 6.97105  9.74881  3.15247   1.000 36.93288 ? 225 SER A CA  1 
ATOM   1751 C C   . SER A 1 225 ? 5.61222  9.88674  2.46900   1.000 34.72623 ? 225 SER A C   1 
ATOM   1752 O O   . SER A 1 225 ? 4.60455  9.47334  3.04157   1.000 37.77925 ? 225 SER A O   1 
ATOM   1753 C CB  . SER A 1 225 ? 7.35349  8.27846  3.30339   1.000 41.15817 ? 225 SER A CB  1 
ATOM   1754 O OG  . SER A 1 225 ? 7.70431  7.73715  2.04631   1.000 43.94092 ? 225 SER A OG  1 
ATOM   1755 N N   . ILE A 1 226 ? 5.58807  10.42954 1.23733   1.000 30.87845 ? 226 ILE A N   1 
ATOM   1756 C CA  . ILE A 1 226 ? 4.33309  10.68829 0.52893   1.000 38.87899 ? 226 ILE A CA  1 
ATOM   1757 C C   . ILE A 1 226 ? 4.37151  9.99631  -0.82459  1.000 37.69768 ? 226 ILE A C   1 
ATOM   1758 O O   . ILE A 1 226 ? 5.40296  10.02809 -1.50849  1.000 36.41988 ? 226 ILE A O   1 
ATOM   1759 C CB  . ILE A 1 226 ? 4.09900  12.20403 0.34566   1.000 41.12597 ? 226 ILE A CB  1 
ATOM   1760 C CG1 . ILE A 1 226 ? 3.83142  12.86176 1.70826   1.000 47.75299 ? 226 ILE A CG1 1 
ATOM   1761 C CG2 . ILE A 1 226 ? 2.94650  12.49667 -0.62350  1.000 44.28131 ? 226 ILE A CG2 1 
ATOM   1762 C CD1 . ILE A 1 226 ? 4.24921  14.32922 1.74777   1.000 51.48162 ? 226 ILE A CD1 1 
ATOM   1763 N N   . LEU A 1 227 ? 3.23967  9.39962  -1.22145  1.000 39.01156 ? 227 LEU A N   1 
ATOM   1764 C CA  . LEU A 1 227 ? 3.12144  8.88035  -2.58359  1.000 34.82234 ? 227 LEU A CA  1 
ATOM   1765 C C   . LEU A 1 227 ? 2.79426  10.03375 -3.51642  1.000 43.43949 ? 227 LEU A C   1 
ATOM   1766 O O   . LEU A 1 227 ? 1.80300  10.74186 -3.30975  1.000 45.17672 ? 227 LEU A O   1 
ATOM   1767 C CB  . LEU A 1 227 ? 2.04829  7.80686  -2.66542  1.000 37.50611 ? 227 LEU A CB  1 
ATOM   1768 C CG  . LEU A 1 227 ? 1.70853  7.32707  -4.08380  1.000 39.78342 ? 227 LEU A CG  1 
ATOM   1769 C CD1 . LEU A 1 227 ? 2.94700  6.92218  -4.84062  1.000 40.85972 ? 227 LEU A CD1 1 
ATOM   1770 C CD2 . LEU A 1 227 ? 0.66723  6.19318  -4.06460  1.000 44.53598 ? 227 LEU A CD2 1 
ATOM   1771 N N   . HIS A 1 228 ? 3.59520  10.21804 -4.55617  1.000 37.52432 ? 228 HIS A N   1 
ATOM   1772 C CA  . HIS A 1 228 ? 3.31175  11.20754 -5.58391  1.000 40.32465 ? 228 HIS A CA  1 
ATOM   1773 C C   . HIS A 1 228 ? 2.98606  10.48538 -6.88555  1.000 40.35132 ? 228 HIS A C   1 
ATOM   1774 O O   . HIS A 1 228 ? 3.75197  9.62024  -7.33446  1.000 38.04516 ? 228 HIS A O   1 
ATOM   1775 C CB  . HIS A 1 228 ? 4.50483  12.15615 -5.77266  1.000 39.65879 ? 228 HIS A CB  1 
ATOM   1776 C CG  . HIS A 1 228 ? 4.75915  13.05880 -4.60408  1.000 37.67770 ? 228 HIS A CG  1 
ATOM   1777 N ND1 . HIS A 1 228 ? 4.31514  14.36253 -4.55653  1.000 41.84374 ? 228 HIS A ND1 1 
ATOM   1778 C CD2 . HIS A 1 228 ? 5.41081  12.84298 -3.43519  1.000 42.10916 ? 228 HIS A CD2 1 
ATOM   1779 C CE1 . HIS A 1 228 ? 4.67925  14.91044 -3.40795  1.000 45.26283 ? 228 HIS A CE1 1 
ATOM   1780 N NE2 . HIS A 1 228 ? 5.34564  14.00927 -2.70823  1.000 39.97326 ? 228 HIS A NE2 1 
ATOM   1781 N N   . ARG A 1 229 ? 1.88150  10.86586 -7.50433  1.000 41.78551 ? 229 ARG A N   1 
ATOM   1782 C CA  . ARG A 1 229 ? 1.43405  10.23776 -8.73190  1.000 41.65387 ? 229 ARG A CA  1 
ATOM   1783 C C   . ARG A 1 229 ? 1.62621  11.16967 -9.91668  1.000 45.94804 ? 229 ARG A C   1 
ATOM   1784 O O   . ARG A 1 229 ? 1.56061  12.39073 -9.78872  1.000 45.29576 ? 229 ARG A O   1 
ATOM   1785 C CB  . ARG A 1 229 ? -0.03499 9.82805  -8.63763  1.000 45.74204 ? 229 ARG A CB  1 
ATOM   1786 C CG  . ARG A 1 229 ? -0.26247 8.58100  -7.80825  1.000 48.48670 ? 229 ARG A CG  1 
ATOM   1787 C CD  . ARG A 1 229 ? -1.56675 7.91565  -8.16105  1.000 53.99810 ? 229 ARG A CD  1 
ATOM   1788 N NE  . ARG A 1 229 ? -2.15707 7.21882  -7.02463  0.700 53.28158 ? 229 ARG A NE  1 
ATOM   1789 C CZ  . ARG A 1 229 ? -1.68746 6.09394  -6.50194  0.700 53.28297 ? 229 ARG A CZ  1 
ATOM   1790 N NH1 . ARG A 1 229 ? -0.55320 5.55099  -6.93001  0.700 52.61682 ? 229 ARG A NH1 1 
ATOM   1791 N NH2 . ARG A 1 229 ? -2.36993 5.50129  -5.52310  0.700 52.94924 ? 229 ARG A NH2 1 
ATOM   1792 N N   . ASP A 1 230 ? 1.84732  10.56989 -11.08449 1.000 43.85157 ? 230 ASP A N   1 
ATOM   1793 C CA  . ASP A 1 230 ? 1.95676  11.31123 -12.33851 1.000 49.02983 ? 230 ASP A CA  1 
ATOM   1794 C C   . ASP A 1 230 ? 3.07928  12.36132 -12.29121 1.000 45.51948 ? 230 ASP A C   1 
ATOM   1795 O O   . ASP A 1 230 ? 2.90637  13.51379 -12.68175 1.000 48.23502 ? 230 ASP A O   1 
ATOM   1796 C CB  . ASP A 1 230 ? 0.60892  11.94341 -12.67907 1.000 48.13151 ? 230 ASP A CB  1 
ATOM   1797 C CG  . ASP A 1 230 ? 0.59138  12.54821 -14.04344 1.000 53.12141 ? 230 ASP A CG  1 
ATOM   1798 O OD1 . ASP A 1 230 ? 1.20874  11.95989 -14.96818 1.000 57.44430 ? 230 ASP A OD1 1 
ATOM   1799 O OD2 . ASP A 1 230 ? -0.05330 13.61253 -14.18580 1.000 61.12986 ? 230 ASP A OD2 1 
ATOM   1800 N N   . VAL A 1 231 ? 4.23945  11.95620 -11.81021 1.000 37.66183 ? 231 VAL A N   1 
ATOM   1801 C CA  . VAL A 1 231 ? 5.35287  12.88403 -11.64914 1.000 38.08960 ? 231 VAL A CA  1 
ATOM   1802 C C   . VAL A 1 231 ? 6.03353  13.11423 -12.98475 1.000 42.13023 ? 231 VAL A C   1 
ATOM   1803 O O   . VAL A 1 231 ? 6.24169  12.17318 -13.75325 1.000 41.53437 ? 231 VAL A O   1 
ATOM   1804 C CB  . VAL A 1 231 ? 6.35095  12.34440 -10.61796 1.000 38.89252 ? 231 VAL A CB  1 
ATOM   1805 C CG1 . VAL A 1 231 ? 7.62559  13.12525 -10.70070 1.000 39.29492 ? 231 VAL A CG1 1 
ATOM   1806 C CG2 . VAL A 1 231 ? 5.77095  12.47752 -9.23318  1.000 42.20734 ? 231 VAL A CG2 1 
ATOM   1807 N N   . GLN A 1 232 ? 6.36759  14.37305 -13.27121 1.000 41.37456 ? 232 GLN A N   1 
ATOM   1808 C CA  . GLN A 1 232 ? 7.17454  14.70870 -14.44641 1.000 39.47224 ? 232 GLN A CA  1 
ATOM   1809 C C   . GLN A 1 232 ? 8.62315  14.98717 -14.09281 1.000 39.59839 ? 232 GLN A C   1 
ATOM   1810 O O   . GLN A 1 232 ? 9.52374  14.71928 -14.89734 1.000 40.91324 ? 232 GLN A O   1 
ATOM   1811 C CB  . GLN A 1 232 ? 6.59047  15.92471 -15.17051 1.000 39.64133 ? 232 GLN A CB  1 
ATOM   1812 N N   . GLU A 1 233 ? 8.86553  15.48333 -12.88694 1.000 39.26340 ? 233 GLU A N   1 
ATOM   1813 C CA  . GLU A 1 233 ? 10.19307 15.93295 -12.51217 1.000 36.74474 ? 233 GLU A CA  1 
ATOM   1814 C C   . GLU A 1 233 ? 10.25633 16.00472 -10.99662 1.000 34.22270 ? 233 GLU A C   1 
ATOM   1815 O O   . GLU A 1 233 ? 9.26000  16.34398 -10.35385 1.000 33.13583 ? 233 GLU A O   1 
ATOM   1816 C CB  . GLU A 1 233 ? 10.46403 17.31124 -13.11231 1.000 40.07785 ? 233 GLU A CB  1 
ATOM   1817 C CG  . GLU A 1 233 ? 11.87708 17.80180 -12.96227 1.000 43.02651 ? 233 GLU A CG  1 
ATOM   1818 C CD  . GLU A 1 233 ? 12.10862 19.11825 -13.68702 1.000 45.60608 ? 233 GLU A CD  1 
ATOM   1819 O OE1 . GLU A 1 233 ? 11.12838 19.85792 -13.91731 1.000 52.62445 ? 233 GLU A OE1 1 
ATOM   1820 O OE2 . GLU A 1 233 ? 13.26799 19.40398 -14.05053 1.000 46.82963 ? 233 GLU A OE2 1 
ATOM   1821 N N   . ILE A 1 234 ? 11.42323 15.68600 -10.45173 1.000 28.65574 ? 234 ILE A N   1 
ATOM   1822 C CA  . ILE A 1 234 ? 11.75660 15.98364 -9.05400  1.000 28.76693 ? 234 ILE A CA  1 
ATOM   1823 C C   . ILE A 1 234 ? 13.05300 16.77842 -9.11064  1.000 33.33740 ? 234 ILE A C   1 
ATOM   1824 O O   . ILE A 1 234 ? 14.00979 16.33601 -9.76135  1.000 33.17961 ? 234 ILE A O   1 
ATOM   1825 C CB  . ILE A 1 234 ? 11.93557 14.71757 -8.20448  1.000 29.83765 ? 234 ILE A CB  1 
ATOM   1826 C CG1 . ILE A 1 234 ? 10.68104 13.82956 -8.25104  1.000 30.21540 ? 234 ILE A CG1 1 
ATOM   1827 C CG2 . ILE A 1 234 ? 12.35812 15.10998 -6.76227  1.000 29.25123 ? 234 ILE A CG2 1 
ATOM   1828 C CD1 . ILE A 1 234 ? 10.95251 12.34879 -7.81709  1.000 34.43748 ? 234 ILE A CD1 1 
ATOM   1829 N N   . ARG A 1 235 ? 13.05355 17.98729 -8.53865  1.000 27.23686 ? 235 ARG A N   1 
ATOM   1830 C CA  . ARG A 1 235 ? 14.17882 18.90590 -8.64586  1.000 23.77666 ? 235 ARG A CA  1 
ATOM   1831 C C   . ARG A 1 235 ? 14.76373 19.12557 -7.26148  1.000 25.74057 ? 235 ARG A C   1 
ATOM   1832 O O   . ARG A 1 235 ? 14.01533 19.45876 -6.34412  1.000 28.01270 ? 235 ARG A O   1 
ATOM   1833 C CB  . ARG A 1 235 ? 13.77557 20.26751 -9.20732  1.000 26.29380 ? 235 ARG A CB  1 
ATOM   1834 C CG  . ARG A 1 235 ? 13.25259 20.24488 -10.67960 1.000 35.69384 ? 235 ARG A CG  1 
ATOM   1835 C CD  . ARG A 1 235 ? 12.84505 21.63506 -11.26693 1.000 41.68927 ? 235 ARG A CD  1 
ATOM   1836 N NE  . ARG A 1 235 ? 13.93848 22.52979 -11.62671 0.700 45.66089 ? 235 ARG A NE  1 
ATOM   1837 C CZ  . ARG A 1 235 ? 14.62410 22.48542 -12.76668 0.700 48.57656 ? 235 ARG A CZ  1 
ATOM   1838 N NH1 . ARG A 1 235 ? 14.40276 21.55068 -13.67662 0.700 46.22881 ? 235 ARG A NH1 1 
ATOM   1839 N NH2 . ARG A 1 235 ? 15.56679 23.39943 -12.99495 0.700 46.15417 ? 235 ARG A NH2 1 
ATOM   1840 N N   . TYR A 1 236 ? 16.07665 19.01296 -7.15288  1.000 22.65162 ? 236 TYR A N   1 
ATOM   1841 C CA  . TYR A 1 236 ? 16.82473 19.22129 -5.90115  1.000 23.78074 ? 236 TYR A CA  1 
ATOM   1842 C C   . TYR A 1 236 ? 17.75552 20.40830 -6.05938  1.000 28.69841 ? 236 TYR A C   1 
ATOM   1843 O O   . TYR A 1 236 ? 18.49592 20.47761 -7.03704  1.000 25.65740 ? 236 TYR A O   1 
ATOM   1844 C CB  . TYR A 1 236 ? 17.65849 17.99424 -5.52110  1.000 25.75863 ? 236 TYR A CB  1 
ATOM   1845 C CG  . TYR A 1 236 ? 16.81347 16.80216 -5.15218  1.000 25.12060 ? 236 TYR A CG  1 
ATOM   1846 C CD1 . TYR A 1 236 ? 15.95116 16.83551 -4.04569  1.000 28.15419 ? 236 TYR A CD1 1 
ATOM   1847 C CD2 . TYR A 1 236 ? 16.91414 15.64616 -5.88340  1.000 31.48739 ? 236 TYR A CD2 1 
ATOM   1848 C CE1 . TYR A 1 236 ? 15.18181 15.71129 -3.71086  1.000 30.40610 ? 236 TYR A CE1 1 
ATOM   1849 C CE2 . TYR A 1 236 ? 16.18026 14.56091 -5.55503  1.000 35.89765 ? 236 TYR A CE2 1 
ATOM   1850 C CZ  . TYR A 1 236 ? 15.33860 14.57688 -4.50952  1.000 32.64961 ? 236 TYR A CZ  1 
ATOM   1851 O OH  . TYR A 1 236 ? 14.63275 13.41700 -4.28849  1.000 46.86201 ? 236 TYR A OH  1 
ATOM   1852 N N   . GLU A 1 237 ? 17.77060 21.30515 -5.07430  1.000 26.30300 ? 237 GLU A N   1 
ATOM   1853 C CA  . GLU A 1 237 ? 18.76464 22.35703 -5.02980  1.000 24.60867 ? 237 GLU A CA  1 
ATOM   1854 C C   . GLU A 1 237 ? 18.95607 22.76259 -3.57870  1.000 28.53002 ? 237 GLU A C   1 
ATOM   1855 O O   . GLU A 1 237 ? 18.03287 22.65199 -2.77402  1.000 24.09274 ? 237 GLU A O   1 
ATOM   1856 C CB  . GLU A 1 237 ? 18.37227 23.60215 -5.83601  1.000 28.01798 ? 237 GLU A CB  1 
ATOM   1857 C CG  . GLU A 1 237 ? 17.03232 24.14485 -5.51653  1.000 34.37496 ? 237 GLU A CG  1 
ATOM   1858 C CD  . GLU A 1 237 ? 16.41517 24.84175 -6.74483  1.000 42.62108 ? 237 GLU A CD  1 
ATOM   1859 O OE1 . GLU A 1 237 ? 17.10608 25.71066 -7.31418  1.000 40.35446 ? 237 GLU A OE1 1 
ATOM   1860 O OE2 . GLU A 1 237 ? 15.27062 24.50235 -7.14739  1.000 41.19385 ? 237 GLU A OE2 1 
ATOM   1861 N N   . VAL A 1 238 ? 20.12441 23.31918 -3.28262  1.000 24.20998 ? 238 VAL A N   1 
ATOM   1862 C CA  . VAL A 1 238 ? 20.29731 23.87059 -1.93095  1.000 25.25841 ? 238 VAL A CA  1 
ATOM   1863 C C   . VAL A 1 238 ? 19.35237 25.03937 -1.74537  1.000 26.60833 ? 238 VAL A C   1 
ATOM   1864 O O   . VAL A 1 238 ? 19.21887 25.92205 -2.61609  1.000 28.31876 ? 238 VAL A O   1 
ATOM   1865 C CB  . VAL A 1 238 ? 21.75497 24.26858 -1.70360  1.000 21.78964 ? 238 VAL A CB  1 
ATOM   1866 C CG1 . VAL A 1 238 ? 21.91371 24.96047 -0.28980  1.000 22.81446 ? 238 VAL A CG1 1 
ATOM   1867 C CG2 . VAL A 1 238 ? 22.64955 23.02006 -1.82599  1.000 22.85014 ? 238 VAL A CG2 1 
ATOM   1868 N N   . SER A 1 239 ? 18.62005 25.04046 -0.61476  1.000 26.38457 ? 239 SER A N   1 
ATOM   1869 C CA  . SER A 1 239 ? 17.67823 26.11921 -0.37614  1.000 26.19599 ? 239 SER A CA  1 
ATOM   1870 C C   . SER A 1 239 ? 18.40829 27.42806 -0.06725  1.000 31.53909 ? 239 SER A C   1 
ATOM   1871 O O   . SER A 1 239 ? 19.54944 27.43441 0.41072   1.000 30.91208 ? 239 SER A O   1 
ATOM   1872 C CB  . SER A 1 239 ? 16.74288 25.75247 0.80370   1.000 27.96074 ? 239 SER A CB  1 
ATOM   1873 O OG  . SER A 1 239 ? 15.87654 26.81832 1.13238   1.000 30.49787 ? 239 SER A OG  1 
ATOM   1874 N N   . ALA A 1 240 ? 17.72429 28.54211 -0.36560  1.000 31.34995 ? 240 ALA A N   1 
ATOM   1875 C CA  . ALA A 1 240 ? 18.09257 29.87117 0.10604   1.000 30.37882 ? 240 ALA A CA  1 
ATOM   1876 C C   . ALA A 1 240 ? 17.86070 30.01379 1.60484   1.000 33.74256 ? 240 ALA A C   1 
ATOM   1877 O O   . ALA A 1 240 ? 18.46939 30.88437 2.23019   1.000 37.78229 ? 240 ALA A O   1 
ATOM   1878 C CB  . ALA A 1 240 ? 17.28007 30.92750 -0.62382  1.000 32.57019 ? 240 ALA A CB  1 
ATOM   1879 N N   . LYS A 1 241 ? 17.01416 29.15831 2.18226   1.000 32.66997 ? 241 LYS A N   1 
ATOM   1880 C CA  . LYS A 1 241 ? 16.60210 29.27482 3.58611   1.000 36.48823 ? 241 LYS A CA  1 
ATOM   1881 C C   . LYS A 1 241 ? 17.55019 28.45897 4.44631   1.000 32.44325 ? 241 LYS A C   1 
ATOM   1882 O O   . LYS A 1 241 ? 18.06952 27.43579 4.01190   1.000 30.02019 ? 241 LYS A O   1 
ATOM   1883 C CB  . LYS A 1 241 ? 15.16641 28.76708 3.79293   1.000 35.64326 ? 241 LYS A CB  1 
ATOM   1884 C CG  . LYS A 1 241 ? 14.11291 29.45929 2.95979   0.800 36.18617 ? 241 LYS A CG  1 
ATOM   1885 C CD  . LYS A 1 241 ? 12.85216 28.60939 2.89568   0.700 40.21246 ? 241 LYS A CD  1 
ATOM   1886 C CE  . LYS A 1 241 ? 11.73135 29.35161 2.19287   0.600 43.21215 ? 241 LYS A CE  1 
ATOM   1887 N NZ  . LYS A 1 241 ? 10.49389 28.52379 2.05082   0.600 45.15529 ? 241 LYS A NZ  1 
ATOM   1888 N N   . LYS A 1 242 ? 17.75226 28.90197 5.69469   1.000 31.56636 ? 242 LYS A N   1 
ATOM   1889 C CA  . LYS A 1 242 ? 18.67552 28.20782 6.57342   1.000 30.17891 ? 242 LYS A CA  1 
ATOM   1890 C C   . LYS A 1 242 ? 17.94975 27.97740 7.88834   1.000 30.85098 ? 242 LYS A C   1 
ATOM   1891 O O   . LYS A 1 242 ? 17.00422 28.69779 8.21148   1.000 33.70579 ? 242 LYS A O   1 
ATOM   1892 C CB  . LYS A 1 242 ? 19.95337 29.03171 6.82336   1.000 35.11806 ? 242 LYS A CB  1 
ATOM   1893 C CG  . LYS A 1 242 ? 20.72463 29.41586 5.53693   0.900 39.86943 ? 242 LYS A CG  1 
ATOM   1894 C CD  . LYS A 1 242 ? 22.19797 29.74515 5.80167   0.700 41.19318 ? 242 LYS A CD  1 
ATOM   1895 C CE  . LYS A 1 242 ? 23.03144 28.46522 5.93412   0.700 35.90003 ? 242 LYS A CE  1 
ATOM   1896 N NZ  . LYS A 1 242 ? 24.48557 28.65200 5.67222   0.700 39.17440 ? 242 LYS A NZ  1 
ATOM   1897 N N   . ILE A 1 243 ? 18.39674 26.95861 8.63458   1.000 29.42105 ? 243 ILE A N   1 
ATOM   1898 C CA  . ILE A 1 243 ? 17.91564 26.78432 10.00536  1.000 31.77827 ? 243 ILE A CA  1 
ATOM   1899 C C   . ILE A 1 243 ? 18.93247 27.42776 10.93732  1.000 30.23154 ? 243 ILE A C   1 
ATOM   1900 O O   . ILE A 1 243 ? 20.14354 27.29298 10.73933  1.000 31.01541 ? 243 ILE A O   1 
ATOM   1901 C CB  . ILE A 1 243 ? 17.71135 25.29667 10.35318  1.000 26.83120 ? 243 ILE A CB  1 
ATOM   1902 C CG1 . ILE A 1 243 ? 17.09625 25.15505 11.78072  1.000 31.47493 ? 243 ILE A CG1 1 
ATOM   1903 C CG2 . ILE A 1 243 ? 18.98471 24.50666 10.14069  1.000 31.41117 ? 243 ILE A CG2 1 
ATOM   1904 C CD1 . ILE A 1 243 ? 16.95114 23.73252 12.19428  1.000 30.06350 ? 243 ILE A CD1 1 
ATOM   1905 N N   . HIS A 1 244 ? 18.44150 28.06510 11.97532  1.000 30.92416 ? 244 HIS A N   1 
ATOM   1906 C CA  . HIS A 1 244 ? 19.27735 28.77259 12.93175  1.000 32.38649 ? 244 HIS A CA  1 
ATOM   1907 C C   . HIS A 1 244 ? 19.22121 28.05530 14.26518  1.000 32.19377 ? 244 HIS A C   1 
ATOM   1908 O O   . HIS A 1 244 ? 18.12606 27.77222 14.74848  1.000 34.20261 ? 244 HIS A O   1 
ATOM   1909 C CB  . HIS A 1 244 ? 18.78751 30.20186 13.09204  1.000 35.28804 ? 244 HIS A CB  1 
ATOM   1910 C CG  . HIS A 1 244 ? 18.66973 30.91658 11.78438  1.000 43.45710 ? 244 HIS A CG  1 
ATOM   1911 N ND1 . HIS A 1 244 ? 19.77236 31.30781 11.06295  1.000 39.32706 ? 244 HIS A ND1 1 
ATOM   1912 C CD2 . HIS A 1 244 ? 17.58706 31.29447 11.05990  1.000 45.76310 ? 244 HIS A CD2 1 
ATOM   1913 C CE1 . HIS A 1 244 ? 19.37734 31.90343 9.94911   1.000 43.73434 ? 244 HIS A CE1 1 
ATOM   1914 N NE2 . HIS A 1 244 ? 18.05654 31.89605 9.91630   1.000 45.88204 ? 244 HIS A NE2 1 
ATOM   1915 N N   . PHE A 1 245 ? 20.38387 27.84246 14.88784  1.000 31.25435 ? 245 PHE A N   1 
ATOM   1916 C CA  . PHE A 1 245 ? 20.45244 27.27749 16.24503  1.000 33.75393 ? 245 PHE A CA  1 
ATOM   1917 C C   . PHE A 1 245 ? 20.89627 28.32973 17.25684  1.000 37.03064 ? 245 PHE A C   1 
ATOM   1918 O O   . PHE A 1 245 ? 21.73749 29.17410 16.96267  1.000 37.05391 ? 245 PHE A O   1 
ATOM   1919 C CB  . PHE A 1 245 ? 21.42020 26.09069 16.29400  1.000 32.78569 ? 245 PHE A CB  1 
ATOM   1920 C CG  . PHE A 1 245 ? 21.02475 24.93067 15.41787  1.000 35.19462 ? 245 PHE A CG  1 
ATOM   1921 C CD1 . PHE A 1 245 ? 21.39533 24.88266 14.07910  1.000 31.25094 ? 245 PHE A CD1 1 
ATOM   1922 C CD2 . PHE A 1 245 ? 20.31151 23.86694 15.94002  1.000 36.85338 ? 245 PHE A CD2 1 
ATOM   1923 C CE1 . PHE A 1 245 ? 21.03178 23.82123 13.29008  1.000 33.09416 ? 245 PHE A CE1 1 
ATOM   1924 C CE2 . PHE A 1 245 ? 19.97404 22.78346 15.13677  1.000 36.77682 ? 245 PHE A CE2 1 
ATOM   1925 C CZ  . PHE A 1 245 ? 20.31126 22.77894 13.80980  1.000 31.39876 ? 245 PHE A CZ  1 
ATOM   1926 N N   . ALA A 1 246 ? 20.31926 28.30149 18.45112  1.000 35.03000 ? 246 ALA A N   1 
ATOM   1927 C CA  . ALA A 1 246 ? 20.90222 29.05510 19.55628  1.000 37.52319 ? 246 ALA A CA  1 
ATOM   1928 C C   . ALA A 1 246 ? 22.12917 28.28651 20.04273  1.000 46.47346 ? 246 ALA A C   1 
ATOM   1929 O O   . ALA A 1 246 ? 22.04352 27.08116 20.29564  1.000 47.44097 ? 246 ALA A O   1 
ATOM   1930 C CB  . ALA A 1 246 ? 19.87180 29.22477 20.67466  1.000 41.04011 ? 246 ALA A CB  1 
ATOM   1931 N N   . ARG A 1 247 ? 23.28610 28.94388 20.14331  1.000 48.24562 ? 247 ARG A N   1 
ATOM   1932 C CA  . ARG A 1 247 ? 24.45707 28.27061 20.70182  1.000 46.28553 ? 247 ARG A CA  1 
ATOM   1933 C C   . ARG A 1 247 ? 24.90609 28.96096 21.98098  1.000 50.99380 ? 247 ARG A C   1 
ATOM   1934 O O   . ARG A 1 247 ? 25.00037 30.19100 22.03418  1.000 49.63919 ? 247 ARG A O   1 
ATOM   1935 C CB  . ARG A 1 247 ? 25.59690 28.18375 19.68875  1.000 47.67215 ? 247 ARG A CB  1 
ATOM   1936 C CG  . ARG A 1 247 ? 25.28586 27.14959 18.53775  0.900 45.50585 ? 247 ARG A CG  1 
ATOM   1937 C CD  . ARG A 1 247 ? 25.60102 25.66440 18.90131  0.800 50.28674 ? 247 ARG A CD  1 
ATOM   1938 N NE  . ARG A 1 247 ? 24.52834 24.70313 18.60879  0.700 49.13079 ? 247 ARG A NE  1 
ATOM   1939 C CZ  . ARG A 1 247 ? 24.48583 23.88824 17.55733  0.700 48.55948 ? 247 ARG A CZ  1 
ATOM   1940 N NH1 . ARG A 1 247 ? 25.38847 23.94497 16.59607  0.700 49.52640 ? 247 ARG A NH1 1 
ATOM   1941 N NH2 . ARG A 1 247 ? 23.49934 22.99948 17.45844  0.700 46.12441 ? 247 ARG A NH2 1 
ATOM   1942 N N   . PHE A 1 248 ? 25.15458 28.17205 23.02253  1.000 51.21618 ? 248 PHE A N   1 
ATOM   1943 C CA  . PHE A 1 248 ? 25.57994 28.72828 24.29115  1.000 49.85008 ? 248 PHE A CA  1 
ATOM   1944 C C   . PHE A 1 248 ? 26.99801 28.35143 24.67797  1.000 51.68796 ? 248 PHE A C   1 
ATOM   1945 O O   . PHE A 1 248 ? 27.54275 28.95410 25.61603  1.000 51.42616 ? 248 PHE A O   1 
ATOM   1946 C CB  . PHE A 1 248 ? 24.60575 28.31717 25.39684  1.000 57.14079 ? 248 PHE A CB  1 
ATOM   1947 C CG  . PHE A 1 248 ? 23.26186 28.95462 25.24391  0.800 55.77673 ? 248 PHE A CG  1 
ATOM   1948 C CD1 . PHE A 1 248 ? 22.99635 30.18719 25.82244  0.800 55.53949 ? 248 PHE A CD1 1 
ATOM   1949 C CD2 . PHE A 1 248 ? 22.28536 28.35271 24.46958  0.800 52.39855 ? 248 PHE A CD2 1 
ATOM   1950 C CE1 . PHE A 1 248 ? 21.77247 30.79140 25.66354  0.800 57.13021 ? 248 PHE A CE1 1 
ATOM   1951 C CE2 . PHE A 1 248 ? 21.05093 28.96065 24.30494  0.800 54.40505 ? 248 PHE A CE2 1 
ATOM   1952 C CZ  . PHE A 1 248 ? 20.79985 30.17980 24.90559  0.800 55.49074 ? 248 PHE A CZ  1 
ATOM   1953 N N   . ARG A 1 249 ? 27.62327 27.41903 23.95825  1.000 43.07566 ? 249 ARG A N   1 
ATOM   1954 C CA  . ARG A 1 249 ? 28.97942 26.98420 24.24168  1.000 42.37801 ? 249 ARG A CA  1 
ATOM   1955 C C   . ARG A 1 249 ? 29.48418 26.26582 22.99631  1.000 41.77012 ? 249 ARG A C   1 
ATOM   1956 O O   . ARG A 1 249 ? 28.71681 25.95792 22.07156  1.000 40.96987 ? 249 ARG A O   1 
ATOM   1957 C CB  . ARG A 1 249 ? 29.03423 26.09326 25.50278  1.000 46.84498 ? 249 ARG A CB  1 
ATOM   1958 C CG  . ARG A 1 249 ? 28.12090 24.85627 25.42294  1.000 47.44064 ? 249 ARG A CG  1 
ATOM   1959 C CD  . ARG A 1 249 ? 27.93173 24.08807 26.71114  0.800 49.88635 ? 249 ARG A CD  1 
ATOM   1960 N NE  . ARG A 1 249 ? 26.99113 22.99253 26.50554  0.700 48.95283 ? 249 ARG A NE  1 
ATOM   1961 C CZ  . ARG A 1 249 ? 26.73433 22.04214 27.39471  0.700 54.17711 ? 249 ARG A CZ  1 
ATOM   1962 N NH1 . ARG A 1 249 ? 27.34200 22.01307 28.57178  0.700 51.59816 ? 249 ARG A NH1 1 
ATOM   1963 N NH2 . ARG A 1 249 ? 25.85228 21.09068 27.09223  0.700 53.87986 ? 249 ARG A NH2 1 
ATOM   1964 N N   . SER A 1 250 ? 30.79204 26.03695 22.94879  1.000 42.55932 ? 250 SER A N   1 
ATOM   1965 C CA  . SER A 1 250 ? 31.33565 25.31632 21.79860  1.000 40.40080 ? 250 SER A CA  1 
ATOM   1966 C C   . SER A 1 250 ? 30.99161 23.84403 21.91001  1.000 41.57583 ? 250 SER A C   1 
ATOM   1967 O O   . SER A 1 250 ? 31.25247 23.20299 22.94020  1.000 44.12721 ? 250 SER A O   1 
ATOM   1968 C CB  . SER A 1 250 ? 32.84782 25.47738 21.70495  1.000 48.05128 ? 250 SER A CB  1 
ATOM   1969 O OG  . SER A 1 250 ? 33.35816 24.67802 20.63982  1.000 47.12126 ? 250 SER A OG  1 
ATOM   1970 N N   . PHE A 1 251 ? 30.39609 23.31247 20.85283  1.000 38.77005 ? 251 PHE A N   1 
ATOM   1971 C CA  . PHE A 1 251 ? 30.27350 21.87509 20.66892  1.000 35.77661 ? 251 PHE A CA  1 
ATOM   1972 C C   . PHE A 1 251 ? 30.52939 21.67775 19.17953  1.000 35.64939 ? 251 PHE A C   1 
ATOM   1973 O O   . PHE A 1 251 ? 29.59826 21.68749 18.36735  1.000 35.38610 ? 251 PHE A O   1 
ATOM   1974 C CB  . PHE A 1 251 ? 28.89593 21.36319 21.09739  1.000 40.43665 ? 251 PHE A CB  1 
ATOM   1975 C CG  . PHE A 1 251 ? 28.80999 19.84965 21.23839  1.000 45.69359 ? 251 PHE A CG  1 
ATOM   1976 C CD1 . PHE A 1 251 ? 29.90208 19.04064 20.96408  1.000 42.91643 ? 251 PHE A CD1 1 
ATOM   1977 C CD2 . PHE A 1 251 ? 27.63291 19.24218 21.65304  1.000 48.12236 ? 251 PHE A CD2 1 
ATOM   1978 C CE1 . PHE A 1 251 ? 29.84331 17.66247 21.11549  1.000 36.86673 ? 251 PHE A CE1 1 
ATOM   1979 C CE2 . PHE A 1 251 ? 27.55253 17.85968 21.79530  1.000 49.26633 ? 251 PHE A CE2 1 
ATOM   1980 C CZ  . PHE A 1 251 ? 28.67200 17.06328 21.50483  1.000 43.11397 ? 251 PHE A CZ  1 
ATOM   1981 N N   . PRO A 1 252 ? 31.79805 21.59496 18.77913  1.000 34.97134 ? 252 PRO A N   1 
ATOM   1982 C CA  . PRO A 1 252 ? 32.11972 21.52692 17.35268  1.000 34.49688 ? 252 PRO A CA  1 
ATOM   1983 C C   . PRO A 1 252 ? 31.51137 20.31049 16.67912  1.000 34.08392 ? 252 PRO A C   1 
ATOM   1984 O O   . PRO A 1 252 ? 31.46151 19.22024 17.24999  1.000 28.80034 ? 252 PRO A O   1 
ATOM   1985 C CB  . PRO A 1 252 ? 33.65339 21.44322 17.34366  1.000 34.07096 ? 252 PRO A CB  1 
ATOM   1986 C CG  . PRO A 1 252 ? 34.07889 22.11558 18.59144  1.000 36.17794 ? 252 PRO A CG  1 
ATOM   1987 C CD  . PRO A 1 252 ? 33.01049 21.70566 19.60262  1.000 34.79527 ? 252 PRO A CD  1 
ATOM   1988 N N   . PHE A 1 253 ? 31.09992 20.50147 15.41787  1.000 31.47588 ? 253 PHE A N   1 
ATOM   1989 C CA  . PHE A 1 253 ? 30.55661 19.41025 14.60521  1.000 32.29999 ? 253 PHE A CA  1 
ATOM   1990 C C   . PHE A 1 253 ? 31.43002 18.16578 14.65744  1.000 25.81318 ? 253 PHE A C   1 
ATOM   1991 O O   . PHE A 1 253 ? 30.93229 17.05526 14.85138  1.000 24.84832 ? 253 PHE A O   1 
ATOM   1992 C CB  . PHE A 1 253 ? 30.41906 19.86442 13.15926  1.000 31.23637 ? 253 PHE A CB  1 
ATOM   1993 C CG  . PHE A 1 253 ? 29.87713 18.81224 12.25043  1.000 27.32284 ? 253 PHE A CG  1 
ATOM   1994 C CD1 . PHE A 1 253 ? 28.53188 18.47630 12.27928  1.000 27.55395 ? 253 PHE A CD1 1 
ATOM   1995 C CD2 . PHE A 1 253 ? 30.70687 18.16635 11.34990  1.000 30.66623 ? 253 PHE A CD2 1 
ATOM   1996 C CE1 . PHE A 1 253 ? 28.02371 17.51692 11.39000  1.000 32.20693 ? 253 PHE A CE1 1 
ATOM   1997 C CE2 . PHE A 1 253 ? 30.21506 17.23248 10.46503  1.000 25.60050 ? 253 PHE A CE2 1 
ATOM   1998 C CZ  . PHE A 1 253 ? 28.88957 16.89914 10.47983  1.000 27.05400 ? 253 PHE A CZ  1 
ATOM   1999 N N   . TRP A 1 254 ? 32.73756 18.32400 14.43734  1.000 26.29937 ? 254 TRP A N   1 
ATOM   2000 C CA  . TRP A 1 254 ? 33.58204 17.14039 14.40561  1.000 27.63211 ? 254 TRP A CA  1 
ATOM   2001 C C   . TRP A 1 254 ? 33.65355 16.47224 15.77647  1.000 26.31054 ? 254 TRP A C   1 
ATOM   2002 O O   . TRP A 1 254 ? 33.83608 15.24890 15.85423  1.000 25.85232 ? 254 TRP A O   1 
ATOM   2003 C CB  . TRP A 1 254 ? 34.99061 17.49241 13.88792  1.000 27.80906 ? 254 TRP A CB  1 
ATOM   2004 C CG  . TRP A 1 254 ? 35.00603 17.98088 12.42559  1.000 25.28831 ? 254 TRP A CG  1 
ATOM   2005 C CD1 . TRP A 1 254 ? 35.54108 19.16591 11.95981  1.000 29.35121 ? 254 TRP A CD1 1 
ATOM   2006 C CD2 . TRP A 1 254 ? 34.51021 17.27711 11.28529  1.000 27.81945 ? 254 TRP A CD2 1 
ATOM   2007 N NE1 . TRP A 1 254 ? 35.33433 19.25636 10.57970  1.000 27.33940 ? 254 TRP A NE1 1 
ATOM   2008 C CE2 . TRP A 1 254 ? 34.72910 18.11257 10.13596  1.000 25.42597 ? 254 TRP A CE2 1 
ATOM   2009 C CE3 . TRP A 1 254 ? 33.88731 16.03582 11.11473  1.000 24.11362 ? 254 TRP A CE3 1 
ATOM   2010 C CZ2 . TRP A 1 254 ? 34.37941 17.71480 8.82710   1.000 24.03969 ? 254 TRP A CZ2 1 
ATOM   2011 C CZ3 . TRP A 1 254 ? 33.50140 15.63798 9.77782   1.000 25.65488 ? 254 TRP A CZ3 1 
ATOM   2012 C CH2 . TRP A 1 254 ? 33.74390 16.50725 8.67415   1.000 23.28583 ? 254 TRP A CH2 1 
ATOM   2013 N N   . ARG A 1 255 ? 33.54098 17.24500 16.87618  1.000 28.82565 ? 255 ARG A N   1 
ATOM   2014 C CA  . ARG A 1 255 ? 33.45669 16.58092 18.16542  1.000 26.20110 ? 255 ARG A CA  1 
ATOM   2015 C C   . ARG A 1 255 ? 32.13267 15.82597 18.30155  1.000 29.06262 ? 255 ARG A C   1 
ATOM   2016 O O   . ARG A 1 255 ? 32.09544 14.70385 18.83029  1.000 31.63060 ? 255 ARG A O   1 
ATOM   2017 C CB  . ARG A 1 255 ? 33.63902 17.61634 19.32053  1.000 29.80362 ? 255 ARG A CB  1 
ATOM   2018 C CG  . ARG A 1 255 ? 33.46972 17.00873 20.72636  1.000 35.45028 ? 255 ARG A CG  1 
ATOM   2019 C CD  . ARG A 1 255 ? 34.31504 17.77540 21.80180  1.000 36.36231 ? 255 ARG A CD  1 
ATOM   2020 N NE  . ARG A 1 255 ? 35.66883 17.19709 21.83410  1.000 41.27758 ? 255 ARG A NE  1 
ATOM   2021 C CZ  . ARG A 1 255 ? 36.79244 17.79340 22.22351  0.700 38.41200 ? 255 ARG A CZ  1 
ATOM   2022 N NH1 . ARG A 1 255 ? 36.81942 19.06129 22.61839  0.700 40.10221 ? 255 ARG A NH1 1 
ATOM   2023 N NH2 . ARG A 1 255 ? 37.92312 17.09394 22.22320  0.700 35.51947 ? 255 ARG A NH2 1 
ATOM   2024 N N   . ARG A 1 256 ? 31.04243 16.42239 17.82710  1.000 26.07184 ? 256 ARG A N   1 
ATOM   2025 C CA  . ARG A 1 256 ? 29.75137 15.75187 17.85101  1.000 28.27035 ? 256 ARG A CA  1 
ATOM   2026 C C   . ARG A 1 256 ? 29.79181 14.45769 17.06233  1.000 29.85928 ? 256 ARG A C   1 
ATOM   2027 O O   . ARG A 1 256 ? 29.28740 13.42713 17.51236  1.000 28.29596 ? 256 ARG A O   1 
ATOM   2028 C CB  . ARG A 1 256 ? 28.68313 16.71678 17.34637  1.000 36.80499 ? 256 ARG A CB  1 
ATOM   2029 C CG  . ARG A 1 256 ? 27.27067 16.12879 17.30919  1.000 39.59105 ? 256 ARG A CG  1 
ATOM   2030 C CD  . ARG A 1 256 ? 26.18991 17.23456 17.27521  0.900 45.99855 ? 256 ARG A CD  1 
ATOM   2031 N NE  . ARG A 1 256 ? 26.64695 18.36459 16.49180  0.800 30.72799 ? 256 ARG A NE  1 
ATOM   2032 C CZ  . ARG A 1 256 ? 26.72751 19.61366 16.91475  0.700 39.83475 ? 256 ARG A CZ  1 
ATOM   2033 N NH1 . ARG A 1 256 ? 26.09283 20.02208 18.01627  0.700 38.40434 ? 256 ARG A NH1 1 
ATOM   2034 N NH2 . ARG A 1 256 ? 27.45536 20.48361 16.21440  0.700 38.98719 ? 256 ARG A NH2 1 
ATOM   2035 N N   . VAL A 1 257 ? 30.45959 14.47531 15.89272  1.000 26.61729 ? 257 VAL A N   1 
ATOM   2036 C CA  . VAL A 1 257 ? 30.65925 13.24968 15.13598  1.000 25.40887 ? 257 VAL A CA  1 
ATOM   2037 C C   . VAL A 1 257 ? 31.45628 12.24324 15.93963  1.000 24.57188 ? 257 VAL A C   1 
ATOM   2038 O O   . VAL A 1 257 ? 31.13487 11.04456 15.94377  1.000 25.46091 ? 257 VAL A O   1 
ATOM   2039 C CB  . VAL A 1 257 ? 31.35232 13.57658 13.79959  1.000 22.22600 ? 257 VAL A CB  1 
ATOM   2040 C CG1 . VAL A 1 257 ? 31.78881 12.24319 13.06770  1.000 22.40579 ? 257 VAL A CG1 1 
ATOM   2041 C CG2 . VAL A 1 257 ? 30.43142 14.46655 12.92512  1.000 24.38291 ? 257 VAL A CG2 1 
ATOM   2042 N N   . HIS A 1 258 ? 32.55517 12.68780 16.59205  1.000 23.80081 ? 258 HIS A N   1 
ATOM   2043 C CA  . HIS A 1 258 ? 33.36163 11.73731 17.36003  1.000 27.21662 ? 258 HIS A CA  1 
ATOM   2044 C C   . HIS A 1 258 ? 32.50783 11.09801 18.44769  1.000 28.73722 ? 258 HIS A C   1 
ATOM   2045 O O   . HIS A 1 258 ? 32.55910 9.88529  18.68732  1.000 29.59516 ? 258 HIS A O   1 
ATOM   2046 C CB  . HIS A 1 258 ? 34.55845 12.45666 17.99943  1.000 26.06046 ? 258 HIS A CB  1 
ATOM   2047 C CG  . HIS A 1 258 ? 35.29718 11.65956 19.02758  1.000 25.93994 ? 258 HIS A CG  1 
ATOM   2048 N ND1 . HIS A 1 258 ? 34.98241 11.69460 20.37942  1.000 31.95646 ? 258 HIS A ND1 1 
ATOM   2049 C CD2 . HIS A 1 258 ? 36.40061 10.88053 18.92714  1.000 27.02895 ? 258 HIS A CD2 1 
ATOM   2050 C CE1 . HIS A 1 258 ? 35.84552 10.94511 21.05534  1.000 29.69798 ? 258 HIS A CE1 1 
ATOM   2051 N NE2 . HIS A 1 258 ? 36.69431 10.41315 20.18694  1.000 39.06462 ? 258 HIS A NE2 1 
ATOM   2052 N N   . ASP A 1 259 ? 31.76223 11.93368 19.15828  1.000 29.82883 ? 259 ASP A N   1 
ATOM   2053 C CA  . ASP A 1 259 ? 31.00371 11.46339 20.31062  1.000 31.28975 ? 259 ASP A CA  1 
ATOM   2054 C C   . ASP A 1 259 ? 29.89061 10.48500 19.90239  1.000 32.89101 ? 259 ASP A C   1 
ATOM   2055 O O   . ASP A 1 259 ? 29.55402 9.57477  20.67267  1.000 38.79687 ? 259 ASP A O   1 
ATOM   2056 C CB  . ASP A 1 259 ? 30.41370 12.67280 21.03265  1.000 33.32190 ? 259 ASP A CB  1 
ATOM   2057 C CG  . ASP A 1 259 ? 31.46203 13.48181 21.78371  1.000 38.31126 ? 259 ASP A CG  1 
ATOM   2058 O OD1 . ASP A 1 259 ? 32.64552 13.06946 21.91140  1.000 34.43367 ? 259 ASP A OD1 1 
ATOM   2059 O OD2 . ASP A 1 259 ? 31.07711 14.55388 22.27852  1.000 35.84787 ? 259 ASP A OD2 1 
ATOM   2060 N N   . SER A 1 260 ? 29.32176 10.65596 18.71874  1.000 29.73374 ? 260 SER A N   1 
ATOM   2061 C CA  . SER A 1 260 ? 28.21659 9.80272  18.25393  1.000 33.31573 ? 260 SER A CA  1 
ATOM   2062 C C   . SER A 1 260 ? 28.68857 8.50247  17.62953  1.000 33.63826 ? 260 SER A C   1 
ATOM   2063 O O   . SER A 1 260 ? 28.00652 7.46944  17.76259  1.000 32.06867 ? 260 SER A O   1 
ATOM   2064 C CB  . SER A 1 260 ? 27.36220 10.49065 17.19843  1.000 34.82207 ? 260 SER A CB  1 
ATOM   2065 O OG  . SER A 1 260 ? 26.76279 11.68506 17.63682  1.000 38.23175 ? 260 SER A OG  1 
ATOM   2066 N N   . PHE A 1 261 ? 29.82091 8.53224  16.91062  1.000 26.08725 ? 261 PHE A N   1 
ATOM   2067 C CA  . PHE A 1 261 ? 30.27070 7.35199  16.18847  1.000 27.41303 ? 261 PHE A CA  1 
ATOM   2068 C C   . PHE A 1 261 ? 31.54707 6.70702  16.71220  1.000 30.81730 ? 261 PHE A C   1 
ATOM   2069 O O   . PHE A 1 261 ? 31.76222 5.52215  16.44004  1.000 32.39969 ? 261 PHE A O   1 
ATOM   2070 C CB  . PHE A 1 261 ? 30.44904 7.69826  14.69961  1.000 25.23546 ? 261 PHE A CB  1 
ATOM   2071 C CG  . PHE A 1 261 ? 29.16633 8.13635  14.05007  1.000 26.43257 ? 261 PHE A CG  1 
ATOM   2072 C CD1 . PHE A 1 261 ? 28.17509 7.17787  13.70485  1.000 26.12453 ? 261 PHE A CD1 1 
ATOM   2073 C CD2 . PHE A 1 261 ? 28.89083 9.46609  13.85112  1.000 25.21966 ? 261 PHE A CD2 1 
ATOM   2074 C CE1 . PHE A 1 261 ? 26.95196 7.56672  13.13551  1.000 26.29235 ? 261 PHE A CE1 1 
ATOM   2075 C CE2 . PHE A 1 261 ? 27.66040 9.86356  13.27634  1.000 27.49855 ? 261 PHE A CE2 1 
ATOM   2076 C CZ  . PHE A 1 261 ? 26.67793 8.88658  12.90855  1.000 21.77823 ? 261 PHE A CZ  1 
ATOM   2077 N N   . ILE A 1 262 ? 32.40717 7.43149  17.42462  1.000 25.55729 ? 262 ILE A N   1 
ATOM   2078 C CA  . ILE A 1 262 ? 33.68325 6.83452  17.78612  1.000 27.98888 ? 262 ILE A CA  1 
ATOM   2079 C C   . ILE A 1 262 ? 33.59938 6.35805  19.23342  1.000 35.02851 ? 262 ILE A C   1 
ATOM   2080 O O   . ILE A 1 262 ? 33.86047 5.18528  19.51427  1.000 39.84822 ? 262 ILE A O   1 
ATOM   2081 C CB  . ILE A 1 262 ? 34.87375 7.79662  17.56942  1.000 29.46472 ? 262 ILE A CB  1 
ATOM   2082 C CG1 . ILE A 1 262 ? 34.96666 8.25444  16.12098  1.000 31.14747 ? 262 ILE A CG1 1 
ATOM   2083 C CG2 . ILE A 1 262 ? 36.23535 7.15382  18.08676  1.000 33.25216 ? 262 ILE A CG2 1 
ATOM   2084 C CD1 . ILE A 1 262 ? 35.29726 7.17679  15.16848  1.000 30.92462 ? 262 ILE A CD1 1 
ATOM   2085 N N   . GLU A 1 263 ? 33.25220 7.25224  20.15962  1.000 30.03895 ? 263 GLU A N   1 
ATOM   2086 C CA  . GLU A 1 263 ? 33.24072 6.87279  21.57552  1.000 37.57256 ? 263 GLU A CA  1 
ATOM   2087 C C   . GLU A 1 263 ? 32.72623 8.03354  22.40884  1.000 45.35831 ? 263 GLU A C   1 
ATOM   2088 O O   . GLU A 1 263 ? 32.90926 9.18384  22.01570  1.000 41.24039 ? 263 GLU A O   1 
ATOM   2089 C CB  . GLU A 1 263 ? 34.64894 6.49888  22.05237  0.800 45.72187 ? 263 GLU A CB  1 
ATOM   2090 C CG  . GLU A 1 263 ? 35.70407 7.57972  21.70318  0.700 45.39333 ? 263 GLU A CG  1 
ATOM   2091 C CD  . GLU A 1 263 ? 37.05766 7.36171  22.36947  0.600 43.57643 ? 263 GLU A CD  1 
ATOM   2092 O OE1 . GLU A 1 263 ? 37.08767 6.74615  23.46838  0.600 50.35183 ? 263 GLU A OE1 1 
ATOM   2093 O OE2 . GLU A 1 263 ? 38.09197 7.80326  21.78916  0.600 43.31302 ? 263 GLU A OE2 1 
ATOM   2094 N N   . ASP A 1 264 ? 32.11949 7.77729  23.56659  0.700 47.94224 ? 264 ASP A N   1 
ATOM   2095 C CA  . ASP A 1 264 ? 31.64987 8.89177  24.38830  0.700 50.38720 ? 264 ASP A CA  1 
ATOM   2096 C C   . ASP A 1 264 ? 31.44429 8.47480  25.84554  0.700 56.19906 ? 264 ASP A C   1 
ATOM   2097 O O   . ASP A 1 264 ? 32.40230 8.16021  26.55732  0.700 65.03334 ? 264 ASP A O   1 
ATOM   2098 C CB  . ASP A 1 264 ? 30.34928 9.46660  23.81184  0.700 50.57005 ? 264 ASP A CB  1 
ATOM   2099 C CG  . ASP A 1 264 ? 29.84982 10.69994 24.57881  0.700 54.69108 ? 264 ASP A CG  1 
ATOM   2100 O OD1 . ASP A 1 264 ? 30.46508 11.07987 25.60862  0.700 53.08993 ? 264 ASP A OD1 1 
ATOM   2101 O OD2 . ASP A 1 264 ? 28.83290 11.29043 24.14451  0.700 51.50036 ? 264 ASP A OD2 1 
HETATM 2102 C C1  . CIT B 2 .   ? 31.87789 24.14208 14.33395  1.000 47.39038 ? 301 CIT A C1  1 
HETATM 2103 O O1  . CIT B 2 .   ? 31.77670 22.93478 13.99693  1.000 38.77455 ? 301 CIT A O1  1 
HETATM 2104 O O2  . CIT B 2 .   ? 33.03576 24.55173 14.59650  1.000 51.92142 ? 301 CIT A O2  1 
HETATM 2105 C C2  . CIT B 2 .   ? 30.69923 25.10012 14.43600  1.000 47.79379 ? 301 CIT A C2  1 
HETATM 2106 C C3  . CIT B 2 .   ? 29.54559 24.65949 15.36829  1.000 54.54202 ? 301 CIT A C3  1 
HETATM 2107 O O7  . CIT B 2 .   ? 30.00872 24.08258 16.62967  1.000 51.26378 ? 301 CIT A O7  1 
HETATM 2108 C C4  . CIT B 2 .   ? 28.65640 25.84062 15.77573  1.000 57.03200 ? 301 CIT A C4  1 
HETATM 2109 C C5  . CIT B 2 .   ? 29.25970 26.61704 16.95081  1.000 57.19603 ? 301 CIT A C5  1 
HETATM 2110 O O3  . CIT B 2 .   ? 29.81074 27.73937 16.75215  1.000 59.13230 ? 301 CIT A O3  1 
HETATM 2111 O O4  . CIT B 2 .   ? 29.20373 26.14973 18.12341  1.000 54.12266 ? 301 CIT A O4  1 
HETATM 2112 C C6  . CIT B 2 .   ? 28.70115 23.60432 14.65437  1.000 51.12026 ? 301 CIT A C6  1 
HETATM 2113 O O5  . CIT B 2 .   ? 28.32084 23.80319 13.48685  1.000 46.47191 ? 301 CIT A O5  1 
HETATM 2114 O O6  . CIT B 2 .   ? 28.40942 22.51246 15.21621  1.000 51.86235 ? 301 CIT A O6  1 
HETATM 2115 N N1  . UZ6 C 3 .   ? 16.59502 7.02536  12.72160  1.000 28.59913 ? 302 UZ6 A N1  1 
HETATM 2116 C C7  . UZ6 C 3 .   ? 18.70153 8.00976  15.74920  1.000 27.10630 ? 302 UZ6 A C7  1 
HETATM 2117 C C8  . UZ6 C 3 .   ? 18.75330 11.41100 12.86331  1.000 24.18099 ? 302 UZ6 A C8  1 
HETATM 2118 N N2  . UZ6 C 3 .   ? 19.75660 10.61330 13.39795  1.000 22.92898 ? 302 UZ6 A N2  1 
HETATM 2119 C C9  . UZ6 C 3 .   ? 20.58702 12.35217 12.33610  1.000 22.66374 ? 302 UZ6 A C9  1 
HETATM 2120 O O1  . UZ6 C 3 .   ? 19.05201 8.41782  13.43922  1.000 27.19352 ? 302 UZ6 A O1  1 
HETATM 2121 C C1  . UZ6 C 3 .   ? 15.79897 4.11166  10.68513  1.000 32.47766 ? 302 UZ6 A C1  1 
HETATM 2122 O O5  . UZ6 C 3 .   ? 18.05829 10.35937 7.97865   1.000 23.24842 ? 302 UZ6 A O5  1 
HETATM 2123 C C5  . UZ6 C 3 .   ? 19.67638 9.41568  14.20288  1.000 27.14850 ? 302 UZ6 A C5  1 
HETATM 2124 C C6  . UZ6 C 3 .   ? 18.87786 9.49946  15.50597  1.000 26.38406 ? 302 UZ6 A C6  1 
HETATM 2125 N N3  . UZ6 C 3 .   ? 19.20292 12.48005 12.23092  1.000 22.32588 ? 302 UZ6 A N3  1 
HETATM 2126 C C4  . UZ6 C 3 .   ? 18.38546 7.50863  14.34755  1.000 30.81489 ? 302 UZ6 A C4  1 
HETATM 2127 O O4  . UZ6 C 3 .   ? 16.17541 8.41850  9.99937   1.000 26.06556 ? 302 UZ6 A O4  1 
HETATM 2128 C C3  . UZ6 C 3 .   ? 16.90382 7.52847  14.05074  1.000 28.68706 ? 302 UZ6 A C3  1 
HETATM 2129 O O3  . UZ6 C 3 .   ? 19.90415 7.44485  16.22300  1.000 32.28462 ? 302 UZ6 A O3  1 
HETATM 2130 C C2  . UZ6 C 3 .   ? 16.39352 5.72794  12.45840  1.000 33.17585 ? 302 UZ6 A C2  1 
HETATM 2131 N N4  . UZ6 C 3 .   ? 22.17222 10.77907 13.31275  1.000 22.31183 ? 302 UZ6 A N4  1 
HETATM 2132 N N   . UZ6 C 3 .   ? 15.98596 5.47479  11.19506  1.000 33.40738 ? 302 UZ6 A N   1 
HETATM 2133 C C   . UZ6 C 3 .   ? 17.11983 3.35647  10.54441  1.000 36.77176 ? 302 UZ6 A C   1 
HETATM 2134 O O   . UZ6 C 3 .   ? 16.55305 4.84582  13.30814  1.000 31.92579 ? 302 UZ6 A O   1 
HETATM 2135 C C10 . UZ6 C 3 .   ? 20.93691 11.21224 13.04463  1.000 21.73082 ? 302 UZ6 A C10 1 
HETATM 2136 C C11 . UZ6 C 3 .   ? 23.08681 11.60414 12.79598  1.000 23.31388 ? 302 UZ6 A C11 1 
HETATM 2137 C C12 . UZ6 C 3 .   ? 21.64327 13.13578 11.83485  1.000 21.98525 ? 302 UZ6 A C12 1 
HETATM 2138 C C13 . UZ6 C 3 .   ? 17.38864 11.05260 12.95484  1.000 22.48075 ? 302 UZ6 A C13 1 
HETATM 2139 C C14 . UZ6 C 3 .   ? 16.22029 10.81535 12.94208  1.000 23.51466 ? 302 UZ6 A C14 1 
HETATM 2140 C C15 . UZ6 C 3 .   ? 14.80053 10.43347 13.02578  1.000 27.05750 ? 302 UZ6 A C15 1 
HETATM 2141 C C16 . UZ6 C 3 .   ? 13.11431 8.81917  12.47405  1.000 29.89852 ? 302 UZ6 A C16 1 
HETATM 2142 C C17 . UZ6 C 3 .   ? 13.25820 7.73620  13.50257  1.000 41.78307 ? 302 UZ6 A C17 1 
HETATM 2143 C C18 . UZ6 C 3 .   ? 11.98461 7.54907  14.30978  1.000 48.06740 ? 302 UZ6 A C18 1 
HETATM 2144 C C19 . UZ6 C 3 .   ? 14.33002 9.79970  10.67405  1.000 22.95770 ? 302 UZ6 A C19 1 
HETATM 2145 C C20 . UZ6 C 3 .   ? 15.69854 9.77242  10.02884  1.000 25.05026 ? 302 UZ6 A C20 1 
HETATM 2146 C C21 . UZ6 C 3 .   ? 17.19785 8.37372  9.00735   1.000 26.15539 ? 302 UZ6 A C21 1 
HETATM 2147 C C22 . UZ6 C 3 .   ? 16.93338 9.49292  8.00683   1.000 23.63452 ? 302 UZ6 A C22 1 
HETATM 2148 C C23 . UZ6 C 3 .   ? 15.65845 10.15869 8.55764   1.000 24.12944 ? 302 UZ6 A C23 1 
HETATM 2149 C C24 . UZ6 C 3 .   ? 16.20322 6.47026  7.66856   1.000 24.57283 ? 302 UZ6 A C24 1 
HETATM 2150 C C25 . UZ6 C 3 .   ? 17.82986 5.10606  7.62931   1.000 22.15767 ? 302 UZ6 A C25 1 
HETATM 2151 C C26 . UZ6 C 3 .   ? 18.25590 6.18977  8.37487   1.000 25.05216 ? 302 UZ6 A C26 1 
HETATM 2152 C C27 . UZ6 C 3 .   ? 20.26326 5.32493  8.65688   1.000 25.09785 ? 302 UZ6 A C27 1 
HETATM 2153 C C28 . UZ6 C 3 .   ? 18.76614 4.06944  7.42492   1.000 23.65148 ? 302 UZ6 A C28 1 
HETATM 2154 N N10 . UZ6 C 3 .   ? 16.52993 5.29521  7.18510   1.000 25.31568 ? 302 UZ6 A N10 1 
HETATM 2155 N N11 . UZ6 C 3 .   ? 19.46241 6.36216  8.92548   1.000 23.04943 ? 302 UZ6 A N11 1 
HETATM 2156 N N12 . UZ6 C 3 .   ? 19.99570 4.21644  7.95794   1.000 24.25637 ? 302 UZ6 A N12 1 
HETATM 2157 N N13 . UZ6 C 3 .   ? 18.50950 2.96984  6.70926   1.000 24.80607 ? 302 UZ6 A N13 1 
HETATM 2158 N N5  . UZ6 C 3 .   ? 22.90171 12.72146 12.08714  1.000 27.63422 ? 302 UZ6 A N5  1 
HETATM 2159 N N6  . UZ6 C 3 .   ? 21.47539 14.28057 11.16741  1.000 24.42873 ? 302 UZ6 A N6  1 
HETATM 2160 N N7  . UZ6 C 3 .   ? 14.40950 9.39285  12.09202  1.000 25.99246 ? 302 UZ6 A N7  1 
HETATM 2161 N N8  . UZ6 C 3 .   ? 12.27019 6.86334  15.59739  1.000 55.74383 ? 302 UZ6 A N8  1 
HETATM 2162 N N9  . UZ6 C 3 .   ? 17.19598 7.06325  8.40111   1.000 24.34755 ? 302 UZ6 A N9  1 
HETATM 2163 O O2  . UZ6 C 3 .   ? 19.65947 10.13232 16.50260  1.000 30.23288 ? 302 UZ6 A O2  1 
HETATM 2164 O O6  . UZ6 C 3 .   ? 15.67734 11.56436 8.37253   1.000 24.13168 ? 302 UZ6 A O6  1 
HETATM 2165 H H17 . UZ6 C 3 .   ? 16.54491 7.74431  12.00688  1.000 34.32192 ? 302 UZ6 A H17 1 
HETATM 2166 H H3  . UZ6 C 3 .   ? 17.98115 7.75934  16.52654  1.000 32.53052 ? 302 UZ6 A H3  1 
HETATM 2167 H H14 . UZ6 C 3 .   ? 15.12135 3.56903  11.34262  1.000 38.97616 ? 302 UZ6 A H14 1 
HETATM 2168 H H15 . UZ6 C 3 .   ? 15.28213 4.15121  9.72740   1.000 38.97616 ? 302 UZ6 A H15 1 
HETATM 2169 H H35 . UZ6 C 3 .   ? 18.69959 9.97060  7.32778   1.000 27.90107 ? 302 UZ6 A H35 1 
HETATM 2170 H H1  . UZ6 C 3 .   ? 20.70668 9.11627  14.38929  1.000 32.58116 ? 302 UZ6 A H1  1 
HETATM 2171 H H2  . UZ6 C 3 .   ? 17.92192 10.01483 15.42535  1.000 31.66384 ? 302 UZ6 A H2  1 
HETATM 2172 H H   . UZ6 C 3 .   ? 18.82543 6.53679  14.12873  1.000 36.98084 ? 302 UZ6 A H   1 
HETATM 2173 H H19 . UZ6 C 3 .   ? 16.39099 6.93653  14.80740  1.000 34.42743 ? 302 UZ6 A H19 1 
HETATM 2174 H H18 . UZ6 C 3 .   ? 16.54194 8.54957  14.16177  1.000 34.42743 ? 302 UZ6 A H18 1 
HETATM 2175 H H21 . UZ6 C 3 .   ? 19.69754 6.79484  16.94471  1.000 38.74451 ? 302 UZ6 A H21 1 
HETATM 2176 H H16 . UZ6 C 3 .   ? 15.79030 6.22490  10.53986  1.000 40.09182 ? 302 UZ6 A H16 1 
HETATM 2177 H H12 . UZ6 C 3 .   ? 17.43496 2.86803  11.46530  1.000 44.12907 ? 302 UZ6 A H12 1 
HETATM 2178 H H11 . UZ6 C 3 .   ? 17.95165 3.99718  10.25548  1.000 44.12907 ? 302 UZ6 A H11 1 
HETATM 2179 H H13 . UZ6 C 3 .   ? 17.08542 2.56811  9.79393   1.000 44.12907 ? 302 UZ6 A H13 1 
HETATM 2180 H H22 . UZ6 C 3 .   ? 24.12810 11.33782 12.97126  1.000 27.97962 ? 302 UZ6 A H22 1 
HETATM 2181 H H25 . UZ6 C 3 .   ? 14.20241 11.33064 12.87330  1.000 32.47197 ? 302 UZ6 A H25 1 
HETATM 2182 H H26 . UZ6 C 3 .   ? 14.59564 10.12667 14.05038  1.000 32.47197 ? 302 UZ6 A H26 1 
HETATM 2183 H H27 . UZ6 C 3 .   ? 12.58561 8.44455  11.59880  1.000 35.88119 ? 302 UZ6 A H27 1 
HETATM 2184 H H28 . UZ6 C 3 .   ? 12.43931 9.59554  12.83120  1.000 35.88119 ? 302 UZ6 A H28 1 
HETATM 2185 H H30 . UZ6 C 3 .   ? 14.10120 7.96107  14.15427  1.000 50.14264 ? 302 UZ6 A H30 1 
HETATM 2186 H H29 . UZ6 C 3 .   ? 13.54929 6.80654  13.01583  1.000 50.14264 ? 302 UZ6 A H29 1 
HETATM 2187 H H31 . UZ6 C 3 .   ? 11.25292 6.97532  13.74289  1.000 57.68385 ? 302 UZ6 A H31 1 
HETATM 2188 H H32 . UZ6 C 3 .   ? 11.50931 8.50961  14.50312  1.000 57.68385 ? 302 UZ6 A H32 1 
HETATM 2189 H H33 . UZ6 C 3 .   ? 13.91998 10.80047 10.54653  1.000 27.55220 ? 302 UZ6 A H33 1 
HETATM 2190 H H34 . UZ6 C 3 .   ? 13.67173 9.15878  10.08941  1.000 27.55220 ? 302 UZ6 A H34 1 
HETATM 2191 H H7  . UZ6 C 3 .   ? 16.43206 10.34733 10.59218  1.000 30.06328 ? 302 UZ6 A H7  1 
HETATM 2192 H H8  . UZ6 C 3 .   ? 18.12122 8.51197  9.56788   1.000 31.38944 ? 302 UZ6 A H8  1 
HETATM 2193 H H9  . UZ6 C 3 .   ? 16.74441 9.11238  7.00413   1.000 28.36439 ? 302 UZ6 A H9  1 
HETATM 2194 H H10 . UZ6 C 3 .   ? 14.77355 9.70484  8.11390   1.000 28.95830 ? 302 UZ6 A H10 1 
HETATM 2195 H H37 . UZ6 C 3 .   ? 15.23123 6.93252  7.50276   1.000 29.49036 ? 302 UZ6 A H37 1 
HETATM 2196 H H38 . UZ6 C 3 .   ? 21.27628 5.37189  9.05375   1.000 30.12039 ? 302 UZ6 A H38 1 
HETATM 2197 H H40 . UZ6 C 3 .   ? 19.22253 2.25641  6.59601   1.000 29.77024 ? 302 UZ6 A H40 1 
HETATM 2198 H H39 . UZ6 C 3 .   ? 17.60044 2.84335  6.27587   1.000 29.77024 ? 302 UZ6 A H39 1 
HETATM 2199 H H24 . UZ6 C 3 .   ? 22.27888 14.80126 10.83049  1.000 29.31744 ? 302 UZ6 A H24 1 
HETATM 2200 H H23 . UZ6 C 3 .   ? 20.54280 14.64027 10.99103  1.000 29.31744 ? 302 UZ6 A H23 1 
HETATM 2201 H H6  . UZ6 C 3 .   ? 12.64026 5.93157  15.43903  1.000 66.89556 ? 302 UZ6 A H6  1 
HETATM 2202 H H4  . UZ6 C 3 .   ? 11.42775 6.77358  16.15637  1.000 66.89556 ? 302 UZ6 A H4  1 
HETATM 2203 H H20 . UZ6 C 3 .   ? 20.09721 9.40007  17.01077  1.000 36.28242 ? 302 UZ6 A H20 1 
HETATM 2204 H H36 . UZ6 C 3 .   ? 16.45844 11.75841 7.79090   1.000 28.96098 ? 302 UZ6 A H36 1 
HETATM 2205 C C1  . GOL D 4 .   ? 14.09786 9.07244  17.20338  1.000 46.14985 ? 303 GOL A C1  1 
HETATM 2206 O O1  . GOL D 4 .   ? 15.19963 9.93604  16.82545  1.000 33.03321 ? 303 GOL A O1  1 
HETATM 2207 C C2  . GOL D 4 .   ? 13.12120 9.50699  18.50326  1.000 47.68579 ? 303 GOL A C2  1 
HETATM 2208 O O2  . GOL D 4 .   ? 13.67652 9.47680  19.83522  1.000 52.43885 ? 303 GOL A O2  1 
HETATM 2209 C C3  . GOL D 4 .   ? 12.35998 10.81661 18.19767  1.000 44.13338 ? 303 GOL A C3  1 
HETATM 2210 O O3  . GOL D 4 .   ? 13.23058 11.79824 18.59234  1.000 35.83618 ? 303 GOL A O3  1 
HETATM 2211 O O   . HOH E 5 .   ? 19.14797 26.84451 -6.82572  1.000 42.14107 ? 401 HOH A O   1 
HETATM 2212 O O   . HOH E 5 .   ? 27.49917 27.34433 -7.39396  1.000 45.24819 ? 402 HOH A O   1 
HETATM 2213 O O   . HOH E 5 .   ? 14.13708 24.00778 -9.70928  1.000 46.95671 ? 403 HOH A O   1 
HETATM 2214 O O   . HOH E 5 .   ? 24.21251 8.21613  -8.91611  1.000 25.54941 ? 404 HOH A O   1 
HETATM 2215 O O   . HOH E 5 .   ? 9.84617  6.69308  1.30447   1.000 40.06763 ? 405 HOH A O   1 
HETATM 2216 O O   . HOH E 5 .   ? 13.79068 10.93502 4.46645   1.000 21.89652 ? 406 HOH A O   1 
HETATM 2217 O O   . HOH E 5 .   ? 6.63177  19.51160 16.50768  1.000 36.59006 ? 407 HOH A O   1 
HETATM 2218 O O   . HOH E 5 .   ? 10.36351 13.68414 12.77848  1.000 34.11464 ? 408 HOH A O   1 
HETATM 2219 O O   . HOH E 5 .   ? 32.37376 15.61999 24.16467  1.000 45.62491 ? 409 HOH A O   1 
HETATM 2220 O O   . HOH E 5 .   ? 31.64550 5.54606  0.00000   0.50  30.68490 ? 410 HOH A O   1 
HETATM 2221 O O   . HOH E 5 .   ? 8.32483  4.84075  -10.36686 1.000 39.86509 ? 411 HOH A O   1 
HETATM 2222 O O   . HOH E 5 .   ? 8.05095  31.80568 42.01631  1.000 28.27415 ? 412 HOH A O   1 
HETATM 2223 O O   . HOH E 5 .   ? 9.28520  27.36019 4.00243   1.000 52.57272 ? 413 HOH A O   1 
HETATM 2224 O O   . HOH E 5 .   ? 9.26729  12.62404 18.80461  1.000 44.69552 ? 414 HOH A O   1 
HETATM 2225 O O   . HOH E 5 .   ? 26.03450 27.08560 7.02246   1.000 41.50302 ? 415 HOH A O   1 
HETATM 2226 O O   . HOH E 5 .   ? 10.80934 29.68839 6.47851   1.000 45.47473 ? 416 HOH A O   1 
HETATM 2227 O O   . HOH E 5 .   ? 10.67636 25.16008 -7.14887  1.000 44.01310 ? 417 HOH A O   1 
HETATM 2228 O O   . HOH E 5 .   ? 17.21760 11.38669 22.75098  1.000 47.25839 ? 418 HOH A O   1 
HETATM 2229 O O   . HOH E 5 .   ? 10.40748 5.99534  -14.38922 1.000 32.13903 ? 419 HOH A O   1 
HETATM 2230 O O   . HOH E 5 .   ? 27.04188 3.54457  -4.44517  1.000 38.27462 ? 420 HOH A O   1 
HETATM 2231 O O   . HOH E 5 .   ? 25.42757 3.41478  -1.90911  1.000 29.09552 ? 421 HOH A O   1 
HETATM 2232 O O   . HOH E 5 .   ? 20.33126 21.96334 19.64299  1.000 34.05953 ? 422 HOH A O   1 
HETATM 2233 O O   . HOH E 5 .   ? 22.17973 23.40110 -5.24544  1.000 27.10365 ? 423 HOH A O   1 
HETATM 2234 O O   . HOH E 5 .   ? 28.06343 26.21037 -2.50422  1.000 35.49473 ? 424 HOH A O   1 
HETATM 2235 O O   . HOH E 5 .   ? 22.53730 21.14901 7.06676   1.000 25.81509 ? 425 HOH A O   1 
HETATM 2236 O O   . HOH E 5 .   ? 35.39619 23.44973 21.83655  1.000 54.44144 ? 426 HOH A O   1 
HETATM 2237 O O   . HOH E 5 .   ? 27.62091 5.62848  -1.78991  1.000 30.17158 ? 427 HOH A O   1 
HETATM 2238 O O   . HOH E 5 .   ? 15.98698 30.81605 6.93925   1.000 41.36299 ? 428 HOH A O   1 
HETATM 2239 O O   . HOH E 5 .   ? 22.89437 11.31829 0.45772   1.000 20.27160 ? 429 HOH A O   1 
HETATM 2240 O O   . HOH E 5 .   ? 33.791   6.686    -4.857    1.000 20.27379 ? 430 HOH A O   1 
HETATM 2241 O O   . HOH E 5 .   ? 26.03389 -1.07953 -7.83454  1.000 41.23046 ? 431 HOH A O   1 
HETATM 2242 O O   . HOH E 5 .   ? 13.30566 10.46415 -18.82543 1.000 36.36192 ? 432 HOH A O   1 
HETATM 2243 O O   . HOH E 5 .   ? 13.43360 18.88861 0.54326   1.000 33.01133 ? 433 HOH A O   1 
HETATM 2244 O O   . HOH E 5 .   ? 20.41289 26.56086 2.81540   1.000 27.77132 ? 434 HOH A O   1 
HETATM 2245 O O   . HOH E 5 .   ? 11.29984 7.59255  -0.59950  1.000 27.57853 ? 435 HOH A O   1 
HETATM 2246 O O   . HOH E 5 .   ? 13.61550 26.62752 -0.34953  1.000 37.63162 ? 436 HOH A O   1 
HETATM 2247 O O   . HOH E 5 .   ? 13.84681 22.45942 -5.90239  1.000 31.67590 ? 437 HOH A O   1 
HETATM 2248 O O   . HOH E 5 .   ? 24.47793 5.20455  9.87272   1.000 32.28587 ? 438 HOH A O   1 
HETATM 2249 O O   . HOH E 5 .   ? 11.35313 32.76834 7.76869   1.000 51.49525 ? 439 HOH A O   1 
HETATM 2250 O O   . HOH E 5 .   ? 4.13538  32.92036 29.25720  1.000 45.49099 ? 440 HOH A O   1 
HETATM 2251 O O   . HOH E 5 .   ? 14.64365 4.05137  5.66590   1.000 30.47167 ? 441 HOH A O   1 
HETATM 2252 O O   . HOH E 5 .   ? 6.68065  31.12733 30.56908  1.000 48.39132 ? 442 HOH A O   1 
HETATM 2253 O O   . HOH E 5 .   ? 15.210   -0.471   -11.534   1.000 37.05844 ? 443 HOH A O   1 
HETATM 2254 O O   . HOH E 5 .   ? 33.71281 21.03469 13.68953  1.000 33.85313 ? 444 HOH A O   1 
HETATM 2255 O O   . HOH E 5 .   ? 13.86020 3.70682  1.91318   1.000 43.01504 ? 445 HOH A O   1 
HETATM 2256 O O   . HOH E 5 .   ? 5.89767  29.91703 33.17645  1.000 51.64448 ? 446 HOH A O   1 
HETATM 2257 O O   . HOH E 5 .   ? 23.36429 7.56261  11.26212  1.000 28.63375 ? 447 HOH A O   1 
HETATM 2258 O O   . HOH E 5 .   ? 20.66384 26.77503 -4.77952  1.000 31.48821 ? 448 HOH A O   1 
HETATM 2259 O O   . HOH E 5 .   ? 8.70010  20.95854 3.74174   1.000 39.44153 ? 449 HOH A O   1 
HETATM 2260 O O   . HOH E 5 .   ? 26.27931 30.13099 10.99980  1.000 44.20056 ? 450 HOH A O   1 
HETATM 2261 O O   . HOH E 5 .   ? 8.66633  18.17203 18.34699  1.000 34.94118 ? 451 HOH A O   1 
HETATM 2262 O O   . HOH E 5 .   ? 5.92434  18.52928 12.48498  1.000 36.78562 ? 452 HOH A O   1 
HETATM 2263 O O   . HOH E 5 .   ? -0.68925 11.59267 -2.52391  1.000 44.09227 ? 453 HOH A O   1 
HETATM 2264 O O   . HOH E 5 .   ? 20.89172 11.65623 4.93604   1.000 20.35161 ? 454 HOH A O   1 
HETATM 2265 O O   . HOH E 5 .   ? 28.92439 25.73099 11.61428  1.000 47.48059 ? 455 HOH A O   1 
HETATM 2266 O O   . HOH E 5 .   ? 8.11493  13.16996 15.72820  1.000 43.29600 ? 456 HOH A O   1 
HETATM 2267 O O   . HOH E 5 .   ? 12.20800 1.71170  -5.46766  1.000 28.18448 ? 457 HOH A O   1 
HETATM 2268 O O   . HOH E 5 .   ? 31.135   5.298    11.879    1.000 30.41457 ? 458 HOH A O   1 
HETATM 2269 O O   . HOH E 5 .   ? 30.64744 28.18590 3.08213   1.000 50.20780 ? 459 HOH A O   1 
HETATM 2270 O O   . HOH E 5 .   ? 15.58519 28.65259 12.19296  1.000 32.09417 ? 460 HOH A O   1 
HETATM 2271 O O   . HOH E 5 .   ? 26.57036 21.92228 23.96864  1.000 44.86610 ? 461 HOH A O   1 
HETATM 2272 O O   . HOH E 5 .   ? 16.39710 34.33851 15.77501  1.000 49.48395 ? 462 HOH A O   1 
HETATM 2273 O O   . HOH E 5 .   ? 15.44930 28.59829 -1.98433  1.000 40.60784 ? 463 HOH A O   1 
HETATM 2274 O O   . HOH E 5 .   ? 20.55462 7.94946  10.95015  1.000 24.35990 ? 464 HOH A O   1 
HETATM 2275 O O   . HOH E 5 .   ? 20.21892 27.70056 -10.22188 1.000 47.17272 ? 465 HOH A O   1 
HETATM 2276 O O   . HOH E 5 .   ? 25.654   14.467   -21.185   1.000 36.34906 ? 466 HOH A O   1 
HETATM 2277 O O   . HOH E 5 .   ? 3.00695  5.44935  -14.11679 1.000 43.97627 ? 467 HOH A O   1 
HETATM 2278 O O   . HOH E 5 .   ? 27.53699 26.95958 9.87071   1.000 39.88659 ? 468 HOH A O   1 
HETATM 2279 O O   . HOH E 5 .   ? 34.93789 14.68844 22.87783  1.000 43.58505 ? 469 HOH A O   1 
HETATM 2280 O O   . HOH E 5 .   ? 27.09463 21.64800 -14.54309 1.000 36.64849 ? 470 HOH A O   1 
HETATM 2281 O O   . HOH E 5 .   ? 0.67845  16.85289 -4.97554  1.000 56.78493 ? 471 HOH A O   1 
HETATM 2282 O O   . HOH E 5 .   ? 8.91624  16.28643 6.43166   1.000 38.44593 ? 472 HOH A O   1 
HETATM 2283 O O   . HOH E 5 .   ? 12.39936 14.52345 33.41931  1.000 42.44084 ? 473 HOH A O   1 
HETATM 2284 O O   . HOH E 5 .   ? 6.41625  21.83762 2.26532   1.000 42.93252 ? 474 HOH A O   1 
HETATM 2285 O O   . HOH E 5 .   ? 7.14094  11.14984 19.92534  1.000 48.38681 ? 475 HOH A O   1 
HETATM 2286 O O   . HOH E 5 .   ? 1.22174  9.06902  0.72812   1.000 35.58975 ? 476 HOH A O   1 
HETATM 2287 O O   . HOH E 5 .   ? 14.12642 -1.15292 -9.15473  1.000 34.44678 ? 477 HOH A O   1 
HETATM 2288 O O   . HOH E 5 .   ? 4.90248  24.48898 34.40727  1.000 45.20540 ? 478 HOH A O   1 
HETATM 2289 O O   . HOH E 5 .   ? 23.00218 32.73773 8.35927   1.000 55.54653 ? 479 HOH A O   1 
HETATM 2290 O O   . HOH E 5 .   ? 17.69307 10.66872 18.48826  1.000 35.87210 ? 480 HOH A O   1 
HETATM 2291 O O   . HOH E 5 .   ? 28.98228 2.33370  -10.53223 1.000 36.28770 ? 481 HOH A O   1 
HETATM 2292 O O   . HOH E 5 .   ? 4.73126  18.78200 29.12813  1.000 36.48201 ? 482 HOH A O   1 
HETATM 2293 O O   . HOH E 5 .   ? 26.31956 6.77193  -3.80968  1.000 24.86658 ? 483 HOH A O   1 
HETATM 2294 O O   . HOH E 5 .   ? 10.38130 3.99512  -11.91085 1.000 32.64276 ? 484 HOH A O   1 
HETATM 2295 O O   . HOH E 5 .   ? 21.54846 1.40709  -12.95221 1.000 33.16097 ? 485 HOH A O   1 
HETATM 2296 O O   . HOH E 5 .   ? 30.05159 26.77981 1.09229   1.000 37.59910 ? 486 HOH A O   1 
HETATM 2297 O O   . HOH E 5 .   ? 23.33888 -7.96180 -13.89508 1.000 34.60427 ? 487 HOH A O   1 
HETATM 2298 O O   . HOH E 5 .   ? 32.29037 26.67238 25.32335  1.000 47.55313 ? 488 HOH A O   1 
HETATM 2299 O O   . HOH E 5 .   ? 11.21156 26.55587 0.07011   1.000 45.51607 ? 489 HOH A O   1 
HETATM 2300 O O   . HOH E 5 .   ? 23.61677 0.77946  -1.81027  1.000 38.26974 ? 490 HOH A O   1 
HETATM 2301 O O   . HOH E 5 .   ? 15.382   -2.076   -14.127   1.000 43.31038 ? 491 HOH A O   1 
HETATM 2302 O O   . HOH E 5 .   ? 25.48730 9.26210  -6.61219  1.000 23.36788 ? 492 HOH A O   1 
HETATM 2303 O O   . HOH E 5 .   ? 24.67479 1.66704  -5.60464  1.000 32.71368 ? 493 HOH A O   1 
HETATM 2304 O O   . HOH E 5 .   ? 17.19371 28.59293 35.57181  1.000 46.29350 ? 494 HOH A O   1 
HETATM 2305 O O   . HOH E 5 .   ? 15.05947 17.02839 20.52094  1.000 32.33239 ? 495 HOH A O   1 
HETATM 2306 O O   . HOH E 5 .   ? 7.07983  14.23350 -0.33850  1.000 40.39390 ? 496 HOH A O   1 
HETATM 2307 O O   . HOH E 5 .   ? 5.45595  27.12007 9.85976   1.000 43.89978 ? 497 HOH A O   1 
HETATM 2308 O O   . HOH E 5 .   ? 27.90093 28.55225 5.61412   1.000 46.60635 ? 498 HOH A O   1 
HETATM 2309 O O   . HOH E 5 .   ? 2.24650  7.16646  1.35725   1.000 42.73109 ? 499 HOH A O   1 
HETATM 2310 O O   . HOH E 5 .   ? 21.35494 21.11544 1.33416   1.000 27.41379 ? 500 HOH A O   1 
HETATM 2311 O O   . HOH E 5 .   ? 18.78174 19.84611 -14.22517 1.000 32.77071 ? 501 HOH A O   1 
HETATM 2312 O O   . HOH E 5 .   ? 21.02109 14.38044 32.05791  1.000 51.85696 ? 502 HOH A O   1 
HETATM 2313 O O   . HOH E 5 .   ? 17.14149 34.16196 13.82866  1.000 51.82770 ? 503 HOH A O   1 
HETATM 2314 O O   . HOH E 5 .   ? 11.88597 29.07163 -2.60905  1.000 51.73585 ? 504 HOH A O   1 
HETATM 2315 O O   . HOH E 5 .   ? 26.70663 23.68661 22.02933  1.000 47.66582 ? 505 HOH A O   1 
HETATM 2316 O O   . HOH E 5 .   ? 8.42076  13.29991 -17.42831 1.000 47.33372 ? 506 HOH A O   1 
HETATM 2317 O O   . HOH E 5 .   ? 27.38588 1.15818  -8.18298  1.000 40.95856 ? 507 HOH A O   1 
HETATM 2318 O O   . HOH E 5 .   ? 6.98240  16.09797 19.20441  1.000 44.31369 ? 508 HOH A O   1 
HETATM 2319 O O   . HOH E 5 .   ? 19.28901 35.29137 12.65879  1.000 56.59391 ? 509 HOH A O   1 
HETATM 2320 O O   . HOH E 5 .   ? 4.55290  18.93599 23.36566  1.000 45.43096 ? 510 HOH A O   1 
HETATM 2321 O O   . HOH E 5 .   ? 20.53667 24.79677 -13.58454 1.000 43.32754 ? 511 HOH A O   1 
HETATM 2322 O O   . HOH E 5 .   ? 32.47647 20.21386 23.29589  1.000 50.14693 ? 512 HOH A O   1 
HETATM 2323 O O   . HOH E 5 .   ? 2.71254  26.01388 15.30409  1.000 48.57258 ? 513 HOH A O   1 
HETATM 2324 O O   . HOH E 5 .   ? 29.678   4.041    7.473     1.000 43.12955 ? 514 HOH A O   1 
HETATM 2325 O O   . HOH E 5 .   ? 16.46055 27.80612 -3.90006  1.000 43.81208 ? 515 HOH A O   1 
HETATM 2326 O O   . HOH E 5 .   ? 25.77503 23.10799 -17.22208 1.000 46.58289 ? 516 HOH A O   1 
HETATM 2327 O O   . HOH E 5 .   ? 25.16242 16.33541 25.14491  1.000 54.59708 ? 517 HOH A O   1 
HETATM 2328 O O   . HOH E 5 .   ? 26.997   2.930    8.825     1.000 44.20474 ? 518 HOH A O   1 
HETATM 2329 O O   . HOH E 5 .   ? 8.06312  18.09252 4.49880   1.000 45.73076 ? 519 HOH A O   1 
HETATM 2330 O O   . HOH E 5 .   ? 13.17810 31.06429 5.92280   1.000 41.48739 ? 520 HOH A O   1 
HETATM 2331 O O   . HOH E 5 .   ? 36.062   10.431   23.961    1.000 42.93073 ? 521 HOH A O   1 
HETATM 2332 O O   . HOH E 5 .   ? 24.85971 26.20259 -12.67939 1.000 49.37391 ? 522 HOH A O   1 
HETATM 2333 O O   . HOH E 5 .   ? 0.35702  14.30494 -2.48189  1.000 53.00181 ? 523 HOH A O   1 
HETATM 2334 O O   . HOH E 5 .   ? 10.38719 10.28315 16.08688  1.000 46.18747 ? 524 HOH A O   1 
HETATM 2335 O O   . HOH E 5 .   ? 32.01518 4.70121  -4.10951  1.000 31.70342 ? 525 HOH A O   1 
HETATM 2336 O O   . HOH E 5 .   ? 13.089   3.362    7.695     1.000 43.54769 ? 526 HOH A O   1 
HETATM 2337 O O   . HOH E 5 .   ? 14.02630 8.23170  5.68335   1.000 34.74945 ? 527 HOH A O   1 
HETATM 2338 O O   . HOH E 5 .   ? 10.59848 6.63342  4.61119   1.000 45.41196 ? 528 HOH A O   1 
HETATM 2339 O O   A HOH E 5 .   ? 12.35557 7.88643  8.00895   0.500 30.28023 ? 529 HOH A O   1 
HETATM 2340 O O   B HOH E 5 .   ? 10.23974 15.22695 9.72718   0.500 35.92139 ? 529 HOH A O   1 
HETATM 2341 O O   . HOH E 5 .   ? 30.28348 4.54781  -2.20867  1.000 35.09551 ? 530 HOH A O   1 
HETATM 2342 O O   . HOH E 5 .   ? 21.92012 34.49291 12.55049  1.000 56.11813 ? 531 HOH A O   1 
HETATM 2343 O O   . HOH E 5 .   ? 0.92532  25.75850 27.81370  1.000 58.87371 ? 532 HOH A O   1 
HETATM 2344 O O   . HOH E 5 .   ? 33.754   9.664    30.243    1.000 52.17176 ? 533 HOH A O   1 
HETATM 2345 O O   . HOH E 5 .   ? 14.61549 14.74756 32.92319  1.000 51.62056 ? 534 HOH A O   1 
HETATM 2346 O O   . HOH E 5 .   ? 13.12380 5.85804  4.52842   1.000 39.52784 ? 535 HOH A O   1 
HETATM 2347 O O   . HOH E 5 .   ? 12.07502 12.38499 34.93266  1.000 54.64857 ? 536 HOH A O   1 
HETATM 2348 O O   . HOH E 5 .   ? -1.61425 16.11729 -9.26206  1.000 53.35374 ? 537 HOH A O   1 
HETATM 2349 O O   . HOH E 5 .   ? 0.00000  15.08587 0.00000   0.50  48.87833 ? 538 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   ? 1.09340 0.73547 0.82472 0.05993  0.08614  -0.21533 1   MET A N   
2    C CA  . MET A 1   ? 1.01534 0.63500 0.75128 0.08339  0.08791  -0.19412 1   MET A CA  
3    C C   . MET A 1   ? 0.88423 0.55138 0.64756 0.11287  0.08147  -0.17926 1   MET A C   
4    O O   . MET A 1   ? 0.84300 0.55281 0.61744 0.11718  0.07819  -0.18425 1   MET A O   
5    C CB  . MET A 1   ? 1.04716 0.64677 0.78334 0.06291  0.08703  -0.18718 1   MET A CB  
6    C CG  . MET A 1   ? 1.07594 0.70952 0.82427 0.02941  0.08110  -0.19925 1   MET A CG  
7    S SD  . MET A 1   ? 1.28974 0.90290 1.03978 0.00345  0.08270  -0.19177 1   MET A SD  
8    C CE  . MET A 1   ? 1.23081 0.87867 0.98450 -0.04288 0.08084  -0.21664 1   MET A CE  
9    N N   . LYS A 2   ? 0.84039 0.50283 0.61270 0.13319  0.07986  -0.16082 2   LYS A N   
10   C CA  . LYS A 2   ? 0.80520 0.52044 0.60771 0.15586  0.07276  -0.14753 2   LYS A CA  
11   C C   . LYS A 2   ? 0.70632 0.45860 0.53169 0.13983  0.06348  -0.14448 2   LYS A C   
12   O O   . LYS A 2   ? 0.66504 0.40215 0.49026 0.11834  0.06064  -0.14239 2   LYS A O   
13   C CB  . LYS A 2   ? 0.78811 0.49516 0.59323 0.17939  0.07158  -0.13053 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.79463 0.47261 0.57658 0.20201  0.07918  -0.13039 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.78220 0.46787 0.56650 0.23084  0.07533  -0.11329 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.90923 0.55859 0.66177 0.25679  0.08261  -0.11129 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.93924 0.63298 0.70560 0.27719  0.08333  -0.11661 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.63445 0.44611 0.48764 0.14299  0.05814  -0.14005 3   TYR A N   
19   C CA  . TYR A 3   ? 0.52189 0.37728 0.40340 0.12476  0.04854  -0.13076 3   TYR A CA  
20   C C   . TYR A 3   ? 0.51969 0.42375 0.42768 0.13792  0.04703  -0.11998 3   TYR A C   
21   O O   . TYR A 3   ? 0.55331 0.46963 0.46058 0.15746  0.05308  -0.12308 3   TYR A O   
22   C CB  . TYR A 3   ? 0.57544 0.44679 0.45215 0.10406  0.04598  -0.14079 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.55686 0.45686 0.43229 0.11369  0.04950  -0.14482 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.58737 0.46534 0.43908 0.12382  0.05806  -0.15915 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.50894 0.45249 0.40249 0.11299  0.04646  -0.13399 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.61069 0.51713 0.46041 0.13294  0.06250  -0.16274 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.50486 0.47180 0.39386 0.12044  0.05214  -0.13619 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.53637 0.48814 0.40487 0.13040  0.05972  -0.15085 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.56846 0.54516 0.43110 0.13822  0.06678  -0.15347 3   TYR A OH  
30   N N   . MET A 4   ? 0.47214 0.40461 0.40211 0.12589  0.04054  -0.10881 4   MET A N   
31   C CA  . MET A 4   ? 0.44413 0.41993 0.39421 0.12848  0.04220  -0.10153 4   MET A CA  
32   C C   . MET A 4   ? 0.38882 0.37911 0.34461 0.11078  0.03819  -0.09416 4   MET A C   
33   O O   . MET A 4   ? 0.41099 0.38757 0.36190 0.09976  0.03203  -0.09401 4   MET A O   
34   C CB  . MET A 4   ? 0.50220 0.49658 0.47103 0.14056  0.04170  -0.09503 4   MET A CB  
35   C CG  . MET A 4   ? 0.44586 0.43169 0.42347 0.13269  0.03420  -0.08624 4   MET A CG  
36   S SD  . MET A 4   ? 0.47536 0.49040 0.47133 0.11258  0.03267  -0.07655 4   MET A SD  
37   C CE  . MET A 4   ? 0.47993 0.54238 0.49620 0.11876  0.03979  -0.07783 4   MET A CE  
38   N N   . ILE A 5   ? 0.35579 0.37362 0.31927 0.10879  0.04333  -0.08833 5   ILE A N   
39   C CA  . ILE A 5   ? 0.37064 0.39427 0.33055 0.09740  0.04236  -0.07955 5   ILE A CA  
40   C C   . ILE A 5   ? 0.39469 0.43449 0.36830 0.09165  0.04843  -0.07028 5   ILE A C   
41   O O   . ILE A 5   ? 0.37749 0.43819 0.35787 0.09344  0.05774  -0.07281 5   ILE A O   
42   C CB  . ILE A 5   ? 0.34836 0.37740 0.28753 0.09858  0.04662  -0.08275 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.36704 0.38332 0.29292 0.10089  0.04175  -0.09648 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.37555 0.40484 0.30403 0.09329  0.04467  -0.07151 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.41700 0.44336 0.31894 0.10198  0.04292  -0.10209 5   ILE A CD1 
46   N N   . THR A 6   ? 0.37596 0.40792 0.35372 0.08336  0.04430  -0.06156 6   THR A N   
47   C CA  . THR A 6   ? 0.34257 0.38249 0.32700 0.07329  0.05201  -0.05448 6   THR A CA  
48   C C   . THR A 6   ? 0.39365 0.41888 0.35475 0.06880  0.05854  -0.04539 6   THR A C   
49   O O   . THR A 6   ? 0.49104 0.50531 0.43650 0.07546  0.05199  -0.04312 6   THR A O   
50   C CB  . THR A 6   ? 0.37213 0.40751 0.37084 0.06810  0.04521  -0.05095 6   THR A CB  
51   O OG1 . THR A 6   ? 0.43123 0.44601 0.41860 0.06733  0.03886  -0.04471 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.43343 0.47327 0.44565 0.07762  0.03695  -0.05710 6   THR A CG2 
53   N N   . SER A 7   ? 0.43563 0.46125 0.39143 0.05782  0.07258  -0.04089 7   SER A N   
54   C CA  . SER A 7   ? 0.43873 0.43938 0.36286 0.05568  0.08277  -0.03002 7   SER A CA  
55   C C   . SER A 7   ? 0.48647 0.46760 0.40621 0.04047  0.09246  -0.02349 7   SER A C   
56   O O   . SER A 7   ? 0.48954 0.48841 0.42958 0.02485  0.09876  -0.03007 7   SER A O   
57   C CB  . SER A 7   ? 0.45702 0.46388 0.36423 0.05408  0.09771  -0.03076 7   SER A CB  
58   O OG  . SER A 7   ? 0.51408 0.48906 0.38362 0.05209  0.11115  -0.01818 7   SER A OG  
59   N N   . LYS A 8   ? 0.47962 0.42556 0.36975 0.04584  0.09484  -0.01175 8   LYS A N   
60   C CA  . LYS A 8   ? 0.50559 0.41874 0.37839 0.03104  0.10953  -0.00515 8   LYS A CA  
61   C C   . LYS A 8   ? 0.58090 0.48829 0.44033 0.01004  0.13318  -0.00640 8   LYS A C   
62   O O   . LYS A 8   ? 0.65139 0.54127 0.50564 -0.01240 0.14772  -0.00765 8   LYS A O   
63   C CB  . LYS A 8   ? 0.61774 0.48865 0.45135 0.04802  0.11011  0.00910  8   LYS A CB  
64   C CG  . LYS A 8   ? 0.74256 0.56017 0.53613 0.03610  0.13342  0.01878  8   LYS A CG  
65   C CD  . LYS A 8   ? 0.82525 0.59578 0.56718 0.06150  0.13750  0.03552  8   LYS A CD  
66   C CE  . LYS A 8   ? 0.86454 0.57674 0.57581 0.05266  0.15363  0.04243  8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.85739 0.58809 0.60633 0.04278  0.14128  0.03265  8   LYS A NZ  
68   N N   . GLY A 9   ? 0.58612 0.50722 0.43746 0.01415  0.13931  -0.00736 9   GLY A N   
69   C CA  . GLY A 9   ? 0.58991 0.51181 0.43132 -0.00900 0.16367  -0.01025 9   GLY A CA  
70   C C   . GLY A 9   ? 0.68026 0.54711 0.46478 -0.01219 0.18672  0.00417  9   GLY A C   
71   O O   . GLY A 9   ? 0.75095 0.61626 0.52385 -0.03514 0.21034  0.00141  9   GLY A O   
72   N N   . ASP A 10  ? 0.68698 0.50998 0.43296 0.01097  0.18219  0.01936  10  ASP A N   
73   C CA  . ASP A 10  ? 0.74807 0.52198 0.43426 0.01688  0.20287  0.03440  10  ASP A CA  
74   C C   . ASP A 10  ? 0.79353 0.59784 0.47588 0.03317  0.19804  0.03335  10  ASP A C   
75   O O   . ASP A 10  ? 0.72017 0.57672 0.44298 0.04201  0.17776  0.02119  10  ASP A O   
76   C CB  . ASP A 10  ? 0.83014 0.54752 0.46878 0.04278  0.20090  0.05215  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.86141 0.61191 0.52304 0.07335  0.16969  0.05075  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.81343 0.61980 0.51654 0.07595  0.15168  0.03813  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.97102 0.69099 0.60832 0.09391  0.16447  0.06112  10  ASP A OD2 
80   N N   . GLU A 11  ? 0.85570 0.62048 0.48275 0.03775  0.21839  0.04652  11  GLU A N   
81   C CA  . GLU A 11  ? 0.85212 0.64237 0.46824 0.05210  0.21681  0.04562  11  GLU A CA  
82   C C   . GLU A 11  ? 0.83420 0.65211 0.45739 0.08638  0.18703  0.04456  11  GLU A C   
83   O O   . GLU A 11  ? 0.85151 0.71476 0.49752 0.09231  0.17532  0.03246  11  GLU A O   
84   C CB  . GLU A 11  ? 1.01157 0.74629 0.55766 0.05356  0.24491  0.06286  11  GLU A CB  
85   C CG  . GLU A 11  ? 1.05442 0.79047 0.59958 0.01743  0.27504  0.05674  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.11981 0.80335 0.61316 0.01730  0.29119  0.07178  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.18705 0.85032 0.64371 0.05201  0.27984  0.08516  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.05522 0.72020 0.54514 -0.01700 0.31462  0.06880  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.77826 0.57022 0.37923 0.10893  0.17604  0.05578  12  LYS A N   
90   C CA  . LYS A 12  ? 0.78907 0.61590 0.39766 0.13829  0.14859  0.05220  12  LYS A CA  
91   C C   . LYS A 12  ? 0.69411 0.57523 0.36696 0.12782  0.12772  0.03157  12  LYS A C   
92   O O   . LYS A 12  ? 0.68419 0.60383 0.37037 0.13636  0.11362  0.01996  12  LYS A O   
93   C CB  . LYS A 12  ? 0.81959 0.61824 0.40062 0.16327  0.14093  0.06563  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.84098 0.67960 0.41699 0.19641  0.11623  0.06317  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.85849 0.68397 0.41645 0.22329  0.10655  0.07349  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.87515 0.76022 0.43840 0.25164  0.08043  0.06542  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.84961 0.73725 0.39693 0.28305  0.06948  0.07367  12  LYS A NZ  
98   N N   . SER A 13  ? 0.65659 0.53732 0.36530 0.10865  0.12729  0.02634  13  SER A N   
99   C CA  . SER A 13  ? 0.60577 0.52788 0.36773 0.10192  0.10886  0.00972  13  SER A CA  
100  C C   . SER A 13  ? 0.58049 0.53342 0.36677 0.09043  0.11272  -0.00400 13  SER A C   
101  O O   . SER A 13  ? 0.50961 0.49215 0.31967 0.09583  0.09784  -0.01710 13  SER A O   
102  C CB  . SER A 13  ? 0.55880 0.47049 0.34606 0.08733  0.10829  0.00947  13  SER A CB  
103  O OG  . SER A 13  ? 0.65322 0.53716 0.41688 0.10190  0.10426  0.02112  13  SER A OG  
104  N N   . ASP A 14  ? 0.63196 0.57790 0.41167 0.07382  0.13410  -0.00248 14  ASP A N   
105  C CA  . ASP A 14  ? 0.56481 0.54671 0.36856 0.06619  0.13869  -0.01626 14  ASP A CA  
106  C C   . ASP A 14  ? 0.57076 0.56496 0.35545 0.08325  0.13411  -0.02028 14  ASP A C   
107  O O   . ASP A 14  ? 0.53430 0.55798 0.34198 0.08744  0.12605  -0.03495 14  ASP A O   
108  C CB  . ASP A 14  ? 0.61334 0.59203 0.41152 0.04305  0.16481  -0.01489 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.66084 0.65029 0.49245 0.02199  0.16740  -0.02063 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.60183 0.60165 0.46200 0.02813  0.14817  -0.02504 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.72708 0.71704 0.55528 -0.00262 0.18977  -0.02203 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.64925 0.61834 0.38715 0.09482  0.14016  -0.00749 15  LEU A N   
113  C CA  . LEU A 15  ? 0.65996 0.64242 0.37390 0.11112  0.13631  -0.01139 15  LEU A CA  
114  C C   . LEU A 15  ? 0.60341 0.60905 0.33355 0.12486  0.11042  -0.02314 15  LEU A C   
115  O O   . LEU A 15  ? 0.57269 0.60245 0.31031 0.12836  0.10431  -0.03841 15  LEU A O   
116  C CB  . LEU A 15  ? 0.65451 0.60291 0.30917 0.12357  0.14864  0.00723  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.76719 0.68678 0.39735 0.10533  0.17945  0.01737  15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.80892 0.68494 0.36998 0.12275  0.19183  0.03775  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.73802 0.69259 0.38804 0.09270  0.19036  0.00288  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.57782 0.57586 0.31222 0.13077  0.09695  -0.01777 16  LEU A N   
121  C CA  . LEU A 16  ? 0.56488 0.58812 0.31822 0.13732  0.07457  -0.03099 16  LEU A CA  
122  C C   . LEU A 16  ? 0.53572 0.57342 0.32984 0.12405  0.07010  -0.04814 16  LEU A C   
123  O O   . LEU A 16  ? 0.48455 0.53920 0.28386 0.12579  0.06048  -0.06427 16  LEU A O   
124  C CB  . LEU A 16  ? 0.52974 0.54583 0.28566 0.14362  0.06377  -0.02247 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.53090 0.57891 0.30017 0.14951  0.04241  -0.03595 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.55393 0.62841 0.29655 0.16317  0.03549  -0.04392 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.53298 0.57943 0.30239 0.15877  0.03393  -0.02667 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.46751 0.49726 0.28630 0.11158  0.07831  -0.04554 17  ARG A N   
129  C CA  . ARG A 17  ? 0.45404 0.49605 0.30593 0.10557  0.07460  -0.05970 17  ARG A CA  
130  C C   . ARG A 17  ? 0.45292 0.50836 0.29875 0.10975  0.08202  -0.07152 17  ARG A C   
131  O O   . ARG A 17  ? 0.44800 0.50786 0.30178 0.11350  0.07486  -0.08654 17  ARG A O   
132  C CB  . ARG A 17  ? 0.40298 0.44300 0.28073 0.09429  0.08112  -0.05492 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.41104 0.46891 0.31470 0.09447  0.08238  -0.06745 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.38710 0.45250 0.31837 0.08478  0.08476  -0.06440 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.39451 0.48102 0.34862 0.09194  0.08361  -0.07574 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.41420 0.52845 0.37537 0.09473  0.09495  -0.08274 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.43867 0.56192 0.38564 0.08678  0.11033  -0.08022 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.43917 0.57296 0.41956 0.10766  0.09195  -0.09233 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.46822 0.52617 0.29564 0.10891  0.09827  -0.06553 18  LEU A N   
140  C CA  . LEU A 18  ? 0.49498 0.56848 0.31548 0.11415  0.10655  -0.07726 18  LEU A CA  
141  C C   . LEU A 18  ? 0.49340 0.56805 0.29079 0.12471  0.09589  -0.08784 18  LEU A C   
142  O O   . LEU A 18  ? 0.49954 0.58124 0.29866 0.12946  0.09532  -0.10436 18  LEU A O   
143  C CB  . LEU A 18  ? 0.55855 0.63471 0.35988 0.10846  0.12838  -0.06816 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.59762 0.68769 0.42410 0.09331  0.14393  -0.06658 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.55575 0.65104 0.35874 0.08551  0.16774  -0.06231 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.56370 0.68227 0.42872 0.09808  0.13866  -0.08241 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.52074 0.59007 0.29413 0.12950  0.08783  -0.07985 19  ASN A N   
148  C CA  . ASN A 19  ? 0.52238 0.60340 0.27482 0.13760  0.07614  -0.09239 19  ASN A CA  
149  C C   . ASN A 19  ? 0.50261 0.58606 0.27699 0.13143  0.06097  -0.10984 19  ASN A C   
150  O O   . ASN A 19  ? 0.51821 0.60826 0.28278 0.13133  0.05669  -0.12880 19  ASN A O   
151  C CB  . ASN A 19  ? 0.54388 0.62736 0.26511 0.14852  0.07018  -0.07943 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.58471 0.66602 0.26450 0.15902  0.08349  -0.07029 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.59806 0.68299 0.27238 0.15682  0.09582  -0.07772 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.65932 0.73279 0.30562 0.17298  0.08246  -0.05309 19  ASN A ND2 
155  N N   . MET A 20  ? 0.48302 0.55761 0.28364 0.12435  0.05444  -0.10463 20  MET A N   
156  C CA  . MET A 20  ? 0.48007 0.55026 0.29719 0.11596  0.04385  -0.12051 20  MET A CA  
157  C C   . MET A 20  ? 0.49193 0.54680 0.31750 0.11560  0.05157  -0.13316 20  MET A C   
158  O O   . MET A 20  ? 0.52691 0.57153 0.34569 0.11131  0.04830  -0.15167 20  MET A O   
159  C CB  . MET A 20  ? 0.43719 0.50085 0.27712 0.10948  0.03651  -0.11105 20  MET A CB  
160  C CG  . MET A 20  ? 0.43942 0.52037 0.26879 0.11328  0.02666  -0.10392 20  MET A CG  
161  S SD  . MET A 20  ? 0.48542 0.55954 0.34054 0.10670  0.01960  -0.09440 20  MET A SD  
162  C CE  . MET A 20  ? 0.45517 0.53643 0.32144 0.09087  0.00925  -0.11801 20  MET A CE  
163  N N   . ILE A 21  ? 0.48564 0.53917 0.32390 0.12042  0.06286  -0.12456 21  ILE A N   
164  C CA  . ILE A 21  ? 0.47120 0.51707 0.31499 0.12751  0.07065  -0.13587 21  ILE A CA  
165  C C   . ILE A 21  ? 0.50513 0.55258 0.32226 0.13326  0.07542  -0.15145 21  ILE A C   
166  O O   . ILE A 21  ? 0.52750 0.55531 0.33610 0.13642  0.07611  -0.16846 21  ILE A O   
167  C CB  . ILE A 21  ? 0.47319 0.53491 0.33643 0.13177  0.08202  -0.12531 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.48629 0.54457 0.37480 0.12511  0.07603  -0.11392 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.48432 0.54932 0.35022 0.14585  0.09090  -0.13778 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.49573 0.57610 0.40445 0.12558  0.08608  -0.10778 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.53091 0.59658 0.32890 0.13493  0.07961  -0.14612 22  ALA A N   
172  C CA  . ALA A 22  ? 0.56036 0.63001 0.33098 0.14086  0.08432  -0.16155 22  ALA A CA  
173  C C   . ALA A 22  ? 0.56767 0.62725 0.32371 0.13321  0.07204  -0.18063 22  ALA A C   
174  O O   . ALA A 22  ? 0.59704 0.64138 0.33890 0.13422  0.07563  -0.20047 22  ALA A O   
175  C CB  . ALA A 22  ? 0.56487 0.65403 0.31211 0.14487  0.09150  -0.15018 22  ALA A CB  
176  N N   . GLY A 23  ? 0.57155 0.63830 0.33254 0.12373  0.05859  -0.17618 23  GLY A N   
177  C CA  . GLY A 23  ? 0.62387 0.69111 0.37420 0.11117  0.04766  -0.19700 23  GLY A CA  
178  C C   . GLY A 23  ? 0.60721 0.63740 0.36674 0.10079  0.04946  -0.21112 23  GLY A C   
179  O O   . GLY A 23  ? 0.64672 0.66128 0.38762 0.09026  0.04997  -0.23504 23  GLY A O   
180  N N   . PHE A 24  ? 0.55866 0.57040 0.34208 0.10389  0.05213  -0.19710 24  PHE A N   
181  C CA  . PHE A 24  ? 0.63013 0.59894 0.41493 0.09973  0.05618  -0.20715 24  PHE A CA  
182  C C   . PHE A 24  ? 0.65244 0.59501 0.41764 0.11344  0.06897  -0.22016 24  PHE A C   
183  O O   . PHE A 24  ? 0.71632 0.61465 0.46322 0.10904  0.07411  -0.23668 24  PHE A O   
184  C CB  . PHE A 24  ? 0.53648 0.49625 0.34854 0.10465  0.05562  -0.18817 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.59144 0.56009 0.41909 0.08939  0.04461  -0.18047 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.62388 0.58039 0.44296 0.06943  0.03984  -0.19602 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.54625 0.53613 0.39569 0.09353  0.04080  -0.15944 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.65589 0.62753 0.49078 0.05645  0.03081  -0.19008 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.52866 0.52708 0.39088 0.08265  0.03157  -0.15269 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.58231 0.57489 0.43884 0.06528  0.02614  -0.16768 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.66398 0.63039 0.42793 0.12962  0.07614  -0.21433 25  GLY A N   
192  C CA  . GLY A 25  ? 0.68453 0.63154 0.43565 0.14023  0.08814  -0.22222 25  GLY A CA  
193  C C   . GLY A 25  ? 0.72712 0.65170 0.44731 0.12713  0.08972  -0.24377 25  GLY A C   
194  O O   . GLY A 25  ? 0.73865 0.63254 0.44463 0.13306  0.10063  -0.25343 25  GLY A O   
195  N N   . GLU A 26  ? 0.77260 0.71391 0.48296 0.10861  0.07895  -0.25230 26  GLU A N   
196  C CA  . GLU A 26  ? 0.75947 0.68357 0.44039 0.09144  0.07915  -0.27419 26  GLU A CA  
197  C C   . GLU A 26  ? 0.80494 0.67852 0.47313 0.07212  0.07998  -0.28891 26  GLU A C   
198  O O   . GLU A 26  ? 0.89967 0.75525 0.54092 0.05571  0.07867  -0.30723 26  GLU A O   
199  C CB  . GLU A 26  ? 0.77547 0.75105 0.45258 0.08140  0.06575  -0.27564 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.71423 0.72780 0.39023 0.09950  0.06766  -0.26082 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.74709 0.74335 0.40528 0.11017  0.08205  -0.26663 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.82937 0.79208 0.46403 0.10131  0.08749  -0.28683 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 0.75968 0.77620 0.42456 0.12630  0.08925  -0.25122 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.75563 0.60293 0.43944 0.07528  0.08201  -0.28045 27  TYR A N   
205  C CA  . TYR A 27  ? 0.86178 0.65800 0.53264 0.06064  0.08102  -0.28950 27  TYR A CA  
206  C C   . TYR A 27  ? 0.93827 0.70254 0.62728 0.07827  0.09090  -0.28551 27  TYR A C   
207  O O   . TYR A 27  ? 0.86765 0.63971 0.56922 0.10168  0.09836  -0.26821 27  TYR A O   
208  C CB  . TYR A 27  ? 0.85152 0.67973 0.54962 0.03865  0.06964  -0.28506 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.84618 0.73529 0.55010 0.01989  0.05661  -0.29282 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.81832 0.70602 0.50870 -0.00791 0.05289  -0.31147 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.79336 0.74367 0.51573 0.03334  0.04733  -0.28010 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.82557 0.77818 0.52325 -0.02090 0.03984  -0.31839 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.66912 0.67584 0.39282 0.02361  0.03430  -0.28429 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.79924 0.81133 0.51297 -0.00268 0.02992  -0.30374 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.80565 0.88246 0.52358 -0.00785 0.01606  -0.30752 27  TYR A OH  
216  N N   . ASP A 28  ? 1.00904 0.72153 0.68535 0.06642  0.09212  -0.28879 28  ASP A N   
217  C CA  . ASP A 28  ? 1.03880 0.70588 0.71689 0.08393  0.10156  -0.27481 28  ASP A CA  
218  C C   . ASP A 28  ? 1.01829 0.70000 0.72159 0.09160  0.09678  -0.25270 28  ASP A C   
219  O O   . ASP A 28  ? 1.07228 0.72560 0.77457 0.07880  0.09543  -0.24677 28  ASP A O   
220  C CB  . ASP A 28  ? 1.15580 0.75819 0.80677 0.06651  0.10782  -0.28291 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.22980 0.78090 0.87157 0.09034  0.11785  -0.26692 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.20881 0.77805 0.86361 0.12253  0.11950  -0.25400 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 1.32589 0.82062 0.94516 0.07668  0.12448  -0.26602 28  ASP A OD2 
224  N N   . MET A 29  ? 0.92034 0.64725 0.64494 0.11071  0.09436  -0.23959 29  MET A N   
225  C CA  . MET A 29  ? 0.88510 0.63221 0.63385 0.11829  0.08735  -0.21966 29  MET A CA  
226  C C   . MET A 29  ? 0.86106 0.63579 0.62984 0.14903  0.08925  -0.20327 29  MET A C   
227  O O   . MET A 29  ? 0.85968 0.66652 0.63162 0.15854  0.09221  -0.20553 29  MET A O   
228  C CB  . MET A 29  ? 0.80987 0.60421 0.57229 0.10238  0.07580  -0.21924 29  MET A CB  
229  C CG  . MET A 29  ? 0.87600 0.66401 0.62558 0.06840  0.07223  -0.23686 29  MET A CG  
230  S SD  . MET A 29  ? 0.92077 0.69305 0.68367 0.04575  0.06757  -0.22919 29  MET A SD  
231  C CE  . MET A 29  ? 1.08457 0.80144 0.81354 0.01637  0.07600  -0.25260 29  MET A CE  
232  N N   . GLU A 30  ? 0.76083 0.52753 0.54293 0.16291  0.08755  -0.18749 30  GLU A N   
233  C CA  . GLU A 30  ? 0.80453 0.60380 0.60714 0.19034  0.08833  -0.17420 30  GLU A CA  
234  C C   . GLU A 30  ? 0.71968 0.56209 0.55315 0.19048  0.07966  -0.16020 30  GLU A C   
235  O O   . GLU A 30  ? 0.69296 0.51713 0.52827 0.18158  0.07413  -0.15441 30  GLU A O   
236  C CB  . GLU A 30  ? 0.88580 0.64534 0.67471 0.20957  0.09253  -0.16863 30  GLU A CB  
237  C CG  . GLU A 30  ? 0.83353 0.63237 0.64308 0.23855  0.09080  -0.15572 30  GLU A CG  
238  C CD  . GLU A 30  ? 0.88068 0.63770 0.66752 0.26124  0.09411  -0.15030 30  GLU A CD  
239  O OE1 . GLU A 30  ? 0.86931 0.57157 0.63376 0.25276  0.09476  -0.14777 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 0.93945 0.71795 0.72773 0.28754  0.09675  -0.14860 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.66063 0.55926 0.51672 0.19680  0.07977  -0.15614 31  TYR A N   
242  C CA  . TYR A 31  ? 0.63965 0.58036 0.52572 0.19569  0.07385  -0.14421 31  TYR A CA  
243  C C   . TYR A 31  ? 0.61740 0.56513 0.51782 0.21347  0.07154  -0.13409 31  TYR A C   
244  O O   . TYR A 31  ? 0.65656 0.62218 0.56034 0.23153  0.07569  -0.13430 31  TYR A O   
245  C CB  . TYR A 31  ? 0.60258 0.59849 0.50534 0.19324  0.07844  -0.14356 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.56421 0.59407 0.49549 0.17754  0.07318  -0.12940 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.52986 0.59201 0.48627 0.18676  0.07266  -0.12345 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.49206 0.52120 0.42246 0.15460  0.06865  -0.12302 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.46668 0.55382 0.44533 0.16885  0.06913  -0.11290 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.50063 0.54953 0.44991 0.14148  0.06580  -0.11070 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.47718 0.55248 0.45039 0.14611  0.06668  -0.10608 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.45873 0.54733 0.44636 0.12899  0.06509  -0.09570 31  TYR A OH  
253  N N   . ASP A 32  ? 0.60578 0.54191 0.51276 0.20963  0.06423  -0.12571 32  ASP A N   
254  C CA  . ASP A 32  ? 0.60539 0.54914 0.52148 0.22711  0.06022  -0.11592 32  ASP A CA  
255  C C   . ASP A 32  ? 0.55705 0.51858 0.49309 0.21712  0.05227  -0.10770 32  ASP A C   
256  O O   . ASP A 32  ? 0.56334 0.48647 0.48743 0.20430  0.04905  -0.10615 32  ASP A O   
257  C CB  . ASP A 32  ? 0.70007 0.58151 0.58389 0.23760  0.06224  -0.11478 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.71601 0.60452 0.60135 0.26022  0.05735  -0.10351 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.68395 0.61298 0.59374 0.26077  0.04971  -0.09624 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.84491 0.69607 0.70272 0.27801  0.06142  -0.10259 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.53791 0.55940 0.50425 0.22006  0.05010  -0.10433 33  ASP A N   
262  C CA  . ASP A 33  ? 0.55540 0.59372 0.54067 0.20779  0.04289  -0.09707 33  ASP A CA  
263  C C   . ASP A 33  ? 0.53734 0.57905 0.52429 0.22509  0.03583  -0.08998 33  ASP A C   
264  O O   . ASP A 33  ? 0.50067 0.56304 0.50423 0.21839  0.02972  -0.08554 33  ASP A O   
265  C CB  . ASP A 33  ? 0.46682 0.56103 0.48099 0.18713  0.04531  -0.09636 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.56102 0.71676 0.59515 0.20250  0.05069  -0.10336 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.59207 0.74903 0.62051 0.22531  0.04722  -0.10288 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.57744 0.77479 0.62953 0.18343  0.05780  -0.10562 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.56792 0.58620 0.53402 0.24602  0.03642  -0.08810 34  VAL A N   
270  C CA  . VAL A 34  ? 0.57075 0.58016 0.52710 0.26268  0.02949  -0.07904 34  VAL A CA  
271  C C   . VAL A 34  ? 0.62670 0.56169 0.55129 0.25714  0.03013  -0.07272 34  VAL A C   
272  O O   . VAL A 34  ? 0.64068 0.56944 0.56558 0.25388  0.02425  -0.06504 34  VAL A O   
273  C CB  . VAL A 34  ? 0.61791 0.64373 0.56399 0.29178  0.02994  -0.07922 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.65870 0.66442 0.58269 0.31237  0.02342  -0.06880 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.60205 0.71135 0.58316 0.29329  0.02861  -0.08601 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.66638 0.54503 0.56244 0.25326  0.03833  -0.07713 35  GLU A N   
277  C CA  . GLU A 35  ? 0.69181 0.49940 0.55580 0.24218  0.04214  -0.07388 35  GLU A CA  
278  C C   . GLU A 35  ? 0.66201 0.44044 0.51900 0.21568  0.04814  -0.08531 35  GLU A C   
279  O O   . GLU A 35  ? 0.74954 0.47649 0.57670 0.20989  0.05660  -0.09164 35  GLU A O   
280  C CB  . GLU A 35  ? 0.76328 0.52301 0.58877 0.26335  0.04786  -0.06916 35  GLU A CB  
281  C CG  . GLU A 35  ? 0.79121 0.54939 0.60435 0.28337  0.04228  -0.05522 35  GLU A CG  
282  C CD  . GLU A 35  ? 0.88562 0.58577 0.64991 0.30612  0.05009  -0.04937 35  GLU A CD  
283  O OE1 . GLU A 35  ? 0.90725 0.61451 0.66273 0.32792  0.05306  -0.05301 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 0.95614 0.60176 0.68792 0.30238  0.05450  -0.04097 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.67500 0.48585 0.55618 0.19871  0.04392  -0.08918 36  PRO A N   
286  C CA  . PRO A 36  ? 0.65595 0.44430 0.52722 0.17385  0.04729  -0.10057 36  PRO A CA  
287  C C   . PRO A 36  ? 0.68662 0.41919 0.53342 0.15431  0.05067  -0.10119 36  PRO A C   
288  O O   . PRO A 36  ? 0.68251 0.40173 0.52744 0.15579  0.04831  -0.09032 36  PRO A O   
289  C CB  . PRO A 36  ? 0.54498 0.39350 0.45407 0.15493  0.03868  -0.09550 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.58990 0.46960 0.51989 0.16715  0.03262  -0.08417 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.57735 0.44966 0.49395 0.20103  0.03606  -0.08447 36  PRO A CD  
292  N N   . GLU A 37  ? 0.65938 0.36558 0.48874 0.13200  0.05654  -0.11487 37  GLU A N   
293  C CA  . GLU A 37  ? 0.67792 0.35264 0.49476 0.10194  0.05939  -0.11869 37  GLU A CA  
294  C C   . GLU A 37  ? 0.62638 0.35452 0.47386 0.07475  0.05007  -0.12117 37  GLU A C   
295  O O   . GLU A 37  ? 0.64864 0.37281 0.49814 0.05221  0.04946  -0.12125 37  GLU A O   
296  C CB  . GLU A 37  ? 0.74724 0.36866 0.52925 0.08682  0.07136  -0.13304 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.88363 0.46664 0.64206 0.10886  0.07853  -0.12668 37  GLU A CG  
298  C CD  . GLU A 37  ? 0.95146 0.49368 0.68094 0.09008  0.08914  -0.14288 37  GLU A CD  
299  O OE1 . GLU A 37  ? 1.06176 0.58462 0.78095 0.05608  0.09375  -0.15232 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 0.96268 0.49807 0.68156 0.10717  0.09292  -0.14767 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.58401 0.36224 0.45301 0.07898  0.04373  -0.12223 38  ILE A N   
302  C CA  . ILE A 38  ? 0.49635 0.32456 0.38926 0.06246  0.03490  -0.12166 38  ILE A CA  
303  C C   . ILE A 38  ? 0.47729 0.34771 0.39511 0.07815  0.02919  -0.10837 38  ILE A C   
304  O O   . ILE A 38  ? 0.48393 0.36174 0.40140 0.09522  0.03250  -0.10846 38  ILE A O   
305  C CB  . ILE A 38  ? 0.57969 0.41952 0.46225 0.04915  0.03580  -0.13881 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.64880 0.44410 0.50438 0.02780  0.04419  -0.15568 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.52738 0.42058 0.42993 0.03920  0.02596  -0.13658 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.70412 0.51390 0.56886 0.00115  0.04104  -0.15881 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.46012 0.35663 0.39747 0.07127  0.02251  -0.09823 39  VAL A N   
310  C CA  . VAL A 39  ? 0.41603 0.34624 0.37288 0.07951  0.01958  -0.08684 39  VAL A CA  
311  C C   . VAL A 39  ? 0.38966 0.34657 0.35085 0.06981  0.01533  -0.08546 39  VAL A C   
312  O O   . VAL A 39  ? 0.38173 0.34277 0.34617 0.05955  0.01075  -0.08456 39  VAL A O   
313  C CB  . VAL A 39  ? 0.40150 0.33144 0.37114 0.08372  0.01702  -0.07570 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.37675 0.33810 0.36350 0.08407  0.01582  -0.06711 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.39627 0.30657 0.35827 0.10195  0.02040  -0.07596 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.40013 0.37550 0.35789 0.07522  0.01767  -0.08568 40  ILE A N   
317  C CA  . ILE A 40  ? 0.37961 0.37698 0.33384 0.07334  0.01471  -0.08163 40  ILE A CA  
318  C C   . ILE A 40  ? 0.35093 0.35542 0.31168 0.07769  0.01848  -0.06748 40  ILE A C   
319  O O   . ILE A 40  ? 0.37731 0.38460 0.34068 0.08163  0.02574  -0.06560 40  ILE A O   
320  C CB  . ILE A 40  ? 0.36512 0.37298 0.30267 0.07664  0.01656  -0.09062 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.38830 0.38567 0.31643 0.06767  0.01471  -0.10828 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.38709 0.41722 0.31489 0.08070  0.01307  -0.08406 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.44359 0.44653 0.35399 0.07101  0.01784  -0.12007 40  ILE A CD1 
324  N N   . SER A 41  ? 0.36545 0.37355 0.32662 0.07619  0.01515  -0.05906 41  SER A N   
325  C CA  . SER A 41  ? 0.33094 0.33566 0.29093 0.07746  0.02094  -0.04669 41  SER A CA  
326  C C   . SER A 41  ? 0.37754 0.38517 0.31460 0.08557  0.02328  -0.04040 41  SER A C   
327  O O   . SER A 41  ? 0.42937 0.44699 0.35941 0.09129  0.01568  -0.04103 41  SER A O   
328  C CB  . SER A 41  ? 0.34130 0.33921 0.31211 0.07321  0.01686  -0.04128 41  SER A CB  
329  O OG  . SER A 41  ? 0.44743 0.43615 0.41417 0.07152  0.02436  -0.03192 41  SER A OG  
330  N N   . ILE A 42  ? 0.39514 0.39557 0.31851 0.08692  0.03460  -0.03405 42  ILE A N   
331  C CA  . ILE A 42  ? 0.36551 0.35973 0.25785 0.09793  0.03927  -0.02515 42  ILE A CA  
332  C C   . ILE A 42  ? 0.45067 0.41693 0.32864 0.09579  0.05078  -0.01161 42  ILE A C   
333  O O   . ILE A 42  ? 0.43192 0.38729 0.31029 0.08353  0.06427  -0.00986 42  ILE A O   
334  C CB  . ILE A 42  ? 0.40525 0.40482 0.28155 0.10087  0.04691  -0.02791 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.40173 0.42247 0.28998 0.10083  0.03720  -0.04404 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.47345 0.46241 0.31058 0.11619  0.05129  -0.01613 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.41156 0.44061 0.28371 0.10511  0.04300  -0.05026 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.43987 0.39509 0.30318 0.10712  0.04698  -0.00344 43  GLY A N   
339  C CA  . GLY A 43  ? 0.51254 0.43110 0.35707 0.10460  0.05978  0.00823  43  GLY A CA  
340  C C   . GLY A 43  ? 0.55015 0.46075 0.38508 0.11970  0.05303  0.01442  43  GLY A C   
341  O O   . GLY A 43  ? 0.61233 0.52867 0.42331 0.14283  0.04811  0.01982  43  GLY A O   
342  N N   . GLY A 44  ? 0.46955 0.36856 0.32004 0.10860  0.05386  0.01366  44  GLY A N   
343  C CA  . GLY A 44  ? 0.50501 0.39625 0.34918 0.12140  0.04908  0.01823  44  GLY A CA  
344  C C   . GLY A 44  ? 0.43598 0.34942 0.31896 0.10738  0.03880  0.00831  44  GLY A C   
345  O O   . GLY A 44  ? 0.39567 0.32923 0.30503 0.09329  0.03430  -0.00084 44  GLY A O   
346  N N   . ASP A 45  ? 0.45996 0.36552 0.34242 0.11282  0.03669  0.01075  45  ASP A N   
347  C CA  . ASP A 45  ? 0.42483 0.34830 0.33890 0.10034  0.02828  0.00273  45  ASP A CA  
348  C C   . ASP A 45  ? 0.40900 0.31944 0.33640 0.07876  0.03447  -0.00064 45  ASP A C   
349  O O   . ASP A 45  ? 0.39713 0.32656 0.35078 0.06866  0.02705  -0.00789 45  ASP A O   
350  C CB  . ASP A 45  ? 0.35490 0.27499 0.26172 0.11346  0.02606  0.00616  45  ASP A CB  
351  C CG  . ASP A 45  ? 0.37709 0.33628 0.28776 0.13074  0.01498  0.00307  45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.39468 0.38619 0.32361 0.12341  0.00680  -0.00591 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.43739 0.39645 0.33140 0.15168  0.01521  0.00820  45  ASP A OD2 
354  N N   . GLY A 46  ? 0.41765 0.29569 0.32425 0.07159  0.04896  0.00395  46  GLY A N   
355  C CA  . GLY A 46  ? 0.44449 0.32294 0.36561 0.04892  0.05504  -0.00261 46  GLY A CA  
356  C C   . GLY A 46  ? 0.40601 0.31639 0.34999 0.04276  0.05083  -0.00961 46  GLY A C   
357  O O   . GLY A 46  ? 0.37413 0.30673 0.34298 0.03366  0.04553  -0.01724 46  GLY A O   
358  N N   . THR A 47  ? 0.41306 0.32600 0.34540 0.05095  0.05333  -0.00700 47  THR A N   
359  C CA  . THR A 47  ? 0.35775 0.29867 0.30806 0.04908  0.04973  -0.01422 47  THR A CA  
360  C C   . THR A 47  ? 0.32462 0.28641 0.29728 0.05447  0.03481  -0.02041 47  THR A C   
361  O O   . THR A 47  ? 0.32298 0.30190 0.31408 0.05114  0.03190  -0.02733 47  THR A O   
362  C CB  . THR A 47  ? 0.39428 0.33187 0.32307 0.05905  0.05435  -0.01039 47  THR A CB  
363  O OG1 . THR A 47  ? 0.46239 0.36795 0.36058 0.05514  0.07091  -0.00181 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.38198 0.34400 0.32567 0.05553  0.05480  -0.01871 47  THR A CG2 
365  N N   . PHE A 48  ? 0.32195 0.28233 0.29038 0.06356  0.02665  -0.01838 48  PHE A N   
366  C CA  . PHE A 48  ? 0.36584 0.33988 0.35025 0.06393  0.01604  -0.02490 48  PHE A CA  
367  C C   . PHE A 48  ? 0.32091 0.29323 0.32039 0.05676  0.01373  -0.02624 48  PHE A C   
368  O O   . PHE A 48  ? 0.32983 0.30739 0.33971 0.05625  0.00972  -0.03128 48  PHE A O   
369  C CB  . PHE A 48  ? 0.35905 0.34049 0.33782 0.07110  0.00961  -0.02467 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.35985 0.35334 0.35079 0.06564  0.00242  -0.03380 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.34300 0.33227 0.34417 0.05895  -0.00018 -0.03465 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.38868 0.39282 0.37679 0.06512  0.00028  -0.04236 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.37580 0.36620 0.38142 0.05098  -0.00285 -0.04263 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.37857 0.38474 0.37202 0.05578  -0.00282 -0.05252 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.37915 0.37563 0.38017 0.04786  -0.00342 -0.05231 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.34118 0.30306 0.33731 0.05294  0.01708  -0.02182 49  LEU A N   
377  C CA  . LEU A 49  ? 0.35350 0.31741 0.36156 0.04669  0.01415  -0.02381 49  LEU A CA  
378  C C   . LEU A 49  ? 0.33961 0.31913 0.35960 0.04255  0.01549  -0.02899 49  LEU A C   
379  O O   . LEU A 49  ? 0.32747 0.31654 0.35745 0.04544  0.00943  -0.03181 49  LEU A O   
380  C CB  . LEU A 49  ? 0.35222 0.30053 0.35088 0.04192  0.01915  -0.02034 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.38649 0.32616 0.37650 0.05014  0.01636  -0.01622 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.40824 0.32392 0.38155 0.04850  0.02444  -0.01286 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.32787 0.27870 0.33102 0.04925  0.00811  -0.01900 49  LEU A CD2 
384  N N   . SER A 50  ? 0.36543 0.34974 0.38238 0.03768  0.02418  -0.03032 50  SER A N   
385  C CA  . SER A 50  ? 0.34153 0.35256 0.37305 0.03466  0.02594  -0.03738 50  SER A CA  
386  C C   . SER A 50  ? 0.35577 0.37712 0.39357 0.04889  0.01954  -0.04042 50  SER A C   
387  O O   . SER A 50  ? 0.33632 0.37840 0.38567 0.05552  0.01584  -0.04515 50  SER A O   
388  C CB  . SER A 50  ? 0.39893 0.41326 0.42418 0.02292  0.03972  -0.03899 50  SER A CB  
389  O OG  . SER A 50  ? 0.47645 0.48355 0.49769 0.00596  0.04716  -0.04054 50  SER A OG  
390  N N   . ALA A 51  ? 0.31743 0.32455 0.34471 0.05502  0.01870  -0.03874 51  ALA A N   
391  C CA  . ALA A 51  ? 0.35210 0.35868 0.37908 0.06611  0.01485  -0.04332 51  ALA A CA  
392  C C   . ALA A 51  ? 0.34656 0.34076 0.37374 0.07102  0.00778  -0.04270 51  ALA A C   
393  O O   . ALA A 51  ? 0.33053 0.32386 0.35691 0.08262  0.00623  -0.04558 51  ALA A O   
394  C CB  . ALA A 51  ? 0.36958 0.36503 0.38346 0.06723  0.01532  -0.04438 51  ALA A CB  
395  N N   . PHE A 52  ? 0.33970 0.32190 0.36411 0.06428  0.00480  -0.03846 52  PHE A N   
396  C CA  . PHE A 52  ? 0.36931 0.33725 0.39051 0.06646  0.00037  -0.03692 52  PHE A CA  
397  C C   . PHE A 52  ? 0.33381 0.31383 0.36088 0.07464  -0.00217 -0.03631 52  PHE A C   
398  O O   . PHE A 52  ? 0.38295 0.35172 0.40168 0.08718  -0.00413 -0.03607 52  PHE A O   
399  C CB  . PHE A 52  ? 0.30730 0.26967 0.32736 0.05751  -0.00102 -0.03311 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.34796 0.29831 0.36431 0.05744  -0.00374 -0.03043 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.39623 0.32473 0.40076 0.05712  -0.00261 -0.03186 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.34493 0.30215 0.36539 0.05593  -0.00552 -0.02732 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.41437 0.32662 0.40985 0.05648  -0.00266 -0.02792 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.36180 0.30821 0.37557 0.05693  -0.00769 -0.02422 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.39304 0.31618 0.39359 0.05797  -0.00590 -0.02351 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.31473 0.31775 0.35294 0.06839  -0.00131 -0.03697 53  HIS A N   
407  C CA  . HIS A 53  ? 0.32717 0.35382 0.37311 0.07487  -0.00534 -0.03921 53  HIS A CA  
408  C C   . HIS A 53  ? 0.35277 0.40340 0.40435 0.09012  -0.00521 -0.04440 53  HIS A C   
409  O O   . HIS A 53  ? 0.37628 0.44296 0.42805 0.10648  -0.01060 -0.04534 53  HIS A O   
410  C CB  . HIS A 53  ? 0.27889 0.32383 0.33374 0.05866  -0.00295 -0.04200 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.33142 0.35449 0.37824 0.05121  -0.00458 -0.03731 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.37005 0.39067 0.41246 0.05817  -0.01126 -0.03505 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.33068 0.33226 0.36988 0.04186  -0.00021 -0.03376 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.35269 0.35433 0.38810 0.05004  -0.01029 -0.03158 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.32602 0.31677 0.35985 0.04161  -0.00396 -0.03089 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.32037 0.37501 0.37405 0.08843  0.00095  -0.04767 54  GLN A N   
417  C CA  . GLN A 54  ? 0.32027 0.39928 0.37873 0.10515  0.00224  -0.05348 54  GLN A CA  
418  C C   . GLN A 54  ? 0.38906 0.43829 0.42909 0.12813  -0.00104 -0.05093 54  GLN A C   
419  O O   . GLN A 54  ? 0.43629 0.50364 0.47557 0.15109  -0.00231 -0.05406 54  GLN A O   
420  C CB  . GLN A 54  ? 0.38034 0.46547 0.44084 0.09760  0.01114  -0.05728 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.41233 0.52532 0.47799 0.11483  0.01433  -0.06448 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.45685 0.57680 0.52244 0.10517  0.02478  -0.06809 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.44416 0.55119 0.50536 0.08567  0.02990  -0.06440 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.49060 0.62945 0.55720 0.12184  0.02866  -0.07476 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.40576 0.40894 0.42818 0.12280  -0.00110 -0.04597 55  TYR A N   
426  C CA  . TYR A 55  ? 0.45612 0.41813 0.45344 0.13936  0.00019  -0.04452 55  TYR A CA  
427  C C   . TYR A 55  ? 0.47954 0.41016 0.46102 0.13851  -0.00234 -0.03714 55  TYR A C   
428  O O   . TYR A 55  ? 0.46978 0.35213 0.42532 0.14015  0.00246  -0.03558 55  TYR A O   
429  C CB  . TYR A 55  ? 0.43883 0.37188 0.42395 0.13106  0.00639  -0.04941 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.45808 0.41808 0.45198 0.13881  0.01002  -0.05624 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.45394 0.41100 0.43700 0.16432  0.01274  -0.05989 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.45029 0.43763 0.45998 0.12295  0.01201  -0.05835 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.48139 0.46889 0.47367 0.17230  0.01719  -0.06712 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.45320 0.46558 0.46888 0.12866  0.01738  -0.06432 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.45616 0.47206 0.46557 0.15223  0.01980  -0.06941 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.44241 0.48759 0.45862 0.15765  0.02634  -0.07632 55  TYR A OH  
437  N N   . GLU A 56  ? 0.45246 0.40804 0.44633 0.13429  -0.00816 -0.03360 56  GLU A N   
438  C CA  . GLU A 56  ? 0.52869 0.45520 0.50695 0.13051  -0.00939 -0.02651 56  GLU A CA  
439  C C   . GLU A 56  ? 0.50741 0.40073 0.45526 0.15564  -0.00855 -0.02062 56  GLU A C   
440  O O   . GLU A 56  ? 0.61153 0.46854 0.53781 0.15235  -0.00609 -0.01392 56  GLU A O   
441  C CB  . GLU A 56  ? 0.44689 0.40578 0.44202 0.12072  -0.01526 -0.02534 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.44753 0.45553 0.45741 0.13304  -0.02148 -0.02937 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.52178 0.55019 0.54055 0.11982  -0.02596 -0.02971 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.42814 0.45684 0.45748 0.09735  -0.02255 -0.03180 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.58647 0.62593 0.59672 0.13405  -0.03238 -0.02749 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.50827 0.41102 0.45024 0.18223  -0.00916 -0.02247 57  GLU A N   
447  C CA  . GLU A 57  ? 0.59278 0.45640 0.49759 0.21315  -0.00696 -0.01548 57  GLU A CA  
448  C C   . GLU A 57  ? 0.66756 0.46946 0.54154 0.20992  0.00516  -0.01586 57  GLU A C   
449  O O   . GLU A 57  ? 0.65374 0.41780 0.49281 0.22378  0.01022  -0.00876 57  GLU A O   
450  C CB  . GLU A 57  ? 0.65814 0.57559 0.57283 0.23898  -0.01412 -0.01710 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.67821 0.65764 0.61904 0.24019  -0.02567 -0.01905 57  GLU A CG  
452  C CD  . GLU A 57  ? 0.73430 0.68606 0.65150 0.24231  -0.02857 -0.00873 57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.75898 0.66275 0.63607 0.25619  -0.02349 0.00091  57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.73148 0.70850 0.66794 0.22166  -0.03354 -0.01046 57  GLU A OE2 
455  N N   . ARG A 58  ? 0.60064 0.39288 0.48398 0.19107  0.01040  -0.02498 58  ARG A N   
456  C CA  . ARG A 58  ? 0.62649 0.36304 0.48080 0.18347  0.02217  -0.02888 58  ARG A CA  
457  C C   . ARG A 58  ? 0.69166 0.40713 0.54788 0.14810  0.02748  -0.03538 58  ARG A C   
458  O O   . ARG A 58  ? 0.65238 0.34665 0.50017 0.13434  0.03468  -0.04563 58  ARG A O   
459  C CB  . ARG A 58  ? 0.63186 0.38619 0.49240 0.19563  0.02375  -0.03679 58  ARG A CB  
460  C CG  . ARG A 58  ? 0.73566 0.49193 0.57825 0.22652  0.02320  -0.03034 58  ARG A CG  
461  C CD  . ARG A 58  ? 0.79378 0.56149 0.63602 0.24136  0.02662  -0.03769 58  ARG A CD  
462  N NE  . ARG A 58  ? 0.77351 0.48595 0.59087 0.22796  0.03817  -0.04482 58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.79321 0.51068 0.62488 0.20727  0.04083  -0.05676 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.73395 0.50383 0.60126 0.19977  0.03394  -0.06099 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.78022 0.44884 0.58668 0.19309  0.05109  -0.06539 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.64980 0.37980 0.51895 0.13015  0.02356  -0.03038 59  LEU A N   
467  C CA  . LEU A 59  ? 0.58147 0.31422 0.46123 0.09620  0.02644  -0.03699 59  LEU A CA  
468  C C   . LEU A 59  ? 0.63947 0.31210 0.48457 0.07936  0.04050  -0.04313 59  LEU A C   
469  O O   . LEU A 59  ? 0.69918 0.38067 0.55284 0.05186  0.04356  -0.05415 59  LEU A O   
470  C CB  . LEU A 59  ? 0.51653 0.27475 0.41347 0.08386  0.02098  -0.03062 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.50341 0.31752 0.43286 0.09194  0.00947  -0.02742 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.54009 0.36257 0.47444 0.08252  0.00680  -0.02129 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.45736 0.30782 0.41251 0.08063  0.00661  -0.03455 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.66697 0.27846 0.47021 0.09465  0.05015  -0.03724 60  ASP A N   
475  C CA  . ASP A 60  ? 0.75345 0.30949 0.52371 0.07077  0.06599  -0.04412 60  ASP A CA  
476  C C   . ASP A 60  ? 0.82373 0.36654 0.58486 0.07041  0.07100  -0.05565 60  ASP A C   
477  O O   . ASP A 60  ? 0.85875 0.36729 0.59872 0.04470  0.08332  -0.06546 60  ASP A O   
478  C CB  . ASP A 60  ? 0.88255 0.39384 0.61547 0.07949  0.07432  -0.02988 60  ASP A CB  
479  C CG  . ASP A 60  ? 0.92120 0.40354 0.63803 0.04426  0.08719  -0.03251 60  ASP A CG  
480  O OD1 . ASP A 60  ? 0.90234 0.41190 0.64122 0.02988  0.08290  -0.03302 60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.07487 0.50902 0.75679 0.02934  0.10289  -0.03541 60  ASP A OD2 
482  N N   . GLU A 61  ? 0.73075 0.30383 0.50802 0.09627  0.06244  -0.05589 61  GLU A N   
483  C CA  . GLU A 61  ? 0.73642 0.29970 0.50498 0.09998  0.06684  -0.06626 61  GLU A CA  
484  C C   . GLU A 61  ? 0.72029 0.32153 0.51471 0.08692  0.06215  -0.08182 61  GLU A C   
485  O O   . GLU A 61  ? 0.72354 0.31969 0.51091 0.08739  0.06584  -0.09257 61  GLU A O   
486  C CB  . GLU A 61  ? 0.76910 0.34262 0.53411 0.13895  0.06260  -0.05694 61  GLU A CB  
487  C CG  . GLU A 61  ? 0.83033 0.35621 0.55520 0.15602  0.07007  -0.04468 61  GLU A CG  
488  C CD  . GLU A 61  ? 0.86370 0.39970 0.58858 0.16779  0.06405  -0.02965 61  GLU A CD  
489  O OE1 . GLU A 61  ? 0.84126 0.43298 0.60198 0.17496  0.05114  -0.02735 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 0.96162 0.44873 0.64775 0.16942  0.07320  -0.02060 61  GLU A OE2 
491  N N   . ILE A 62  ? 0.65453 0.31032 0.48510 0.07251  0.05181  -0.07986 62  ILE A N   
492  C CA  . ILE A 62  ? 0.64529 0.36172 0.50968 0.06583  0.04259  -0.08601 62  ILE A CA  
493  C C   . ILE A 62  ? 0.56377 0.30691 0.44297 0.03389  0.04041  -0.09387 62  ILE A C   
494  O O   . ILE A 62  ? 0.56368 0.31130 0.44921 0.02208  0.03944  -0.08834 62  ILE A O   
495  C CB  . ILE A 62  ? 0.53899 0.30622 0.43452 0.08466  0.03136  -0.07386 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.57855 0.33833 0.46489 0.11700  0.03262  -0.07039 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.51051 0.33264 0.43578 0.07305  0.02401  -0.07682 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.58143 0.39676 0.49859 0.13059  0.02368  -0.06313 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.55149 0.32084 0.43770 0.02271  0.03861  -0.10679 63  ALA A N   
500  C CA  . ALA A 63  ? 0.49001 0.30776 0.39773 0.00265  0.03197  -0.11222 63  ALA A CA  
501  C C   . ALA A 63  ? 0.45065 0.31854 0.38208 0.01765  0.02172  -0.10559 63  ALA A C   
502  O O   . ALA A 63  ? 0.49597 0.36614 0.42318 0.02967  0.02223  -0.10852 63  ALA A O   
503  C CB  . ALA A 63  ? 0.56315 0.37883 0.45756 -0.02360 0.03749  -0.13375 63  ALA A CB  
504  N N   . PHE A 64  ? 0.41915 0.32315 0.37093 0.01610  0.01453  -0.09761 64  PHE A N   
505  C CA  . PHE A 64  ? 0.37946 0.31998 0.34680 0.02931  0.00775  -0.08885 64  PHE A CA  
506  C C   . PHE A 64  ? 0.39413 0.37301 0.36390 0.02347  0.00284  -0.09695 64  PHE A C   
507  O O   . PHE A 64  ? 0.39553 0.38994 0.36666 0.00794  0.00163  -0.10677 64  PHE A O   
508  C CB  . PHE A 64  ? 0.39387 0.34228 0.37497 0.03439  0.00449  -0.07480 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.38653 0.31394 0.36799 0.04530  0.00644  -0.06615 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.38384 0.32427 0.37316 0.05748  0.00589  -0.05989 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.40199 0.29870 0.37411 0.04317  0.00949  -0.06435 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.38221 0.31651 0.37496 0.06787  0.00640  -0.05448 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.42751 0.31145 0.39788 0.05820  0.00958  -0.05657 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.42654 0.33497 0.41005 0.07072  0.00689  -0.05251 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.36579 0.36319 0.33467 0.03661  0.00060  -0.09305 65  ILE A N   
516  C CA  . ILE A 65  ? 0.36225 0.39798 0.32896 0.03968  -0.00516 -0.09646 65  ILE A CA  
517  C C   . ILE A 65  ? 0.35738 0.39894 0.32325 0.05741  -0.00523 -0.08000 65  ILE A C   
518  O O   . ILE A 65  ? 0.40029 0.42557 0.36311 0.06398  0.00029  -0.07397 65  ILE A O   
519  C CB  . ILE A 65  ? 0.42632 0.47050 0.37925 0.03627  -0.00486 -0.11181 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.41939 0.44357 0.36622 0.01530  -0.00058 -0.12966 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.42971 0.52079 0.37835 0.04225  -0.01273 -0.11587 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.50421 0.52775 0.43399 0.01133  0.00165  -0.14623 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.34587 0.41149 0.31053 0.06559  -0.00993 -0.07435 66  GLY A N   
524  C CA  . GLY A 66  ? 0.32910 0.38924 0.28323 0.08215  -0.00698 -0.05857 66  GLY A CA  
525  C C   . GLY A 66  ? 0.41084 0.49518 0.34501 0.09759  -0.01020 -0.05820 66  GLY A C   
526  O O   . GLY A 66  ? 0.42402 0.54489 0.35840 0.09995  -0.01860 -0.06752 66  GLY A O   
527  N N   . ILE A 67  ? 0.33752 0.40492 0.25332 0.10734  -0.00288 -0.04882 67  ILE A N   
528  C CA  . ILE A 67  ? 0.37393 0.45474 0.26175 0.12677  -0.00363 -0.04356 67  ILE A CA  
529  C C   . ILE A 67  ? 0.42095 0.47148 0.28822 0.14095  0.00523  -0.02394 67  ILE A C   
530  O O   . ILE A 67  ? 0.46500 0.48234 0.33318 0.13144  0.01665  -0.01681 67  ILE A O   
531  C CB  . ILE A 67  ? 0.37372 0.45087 0.24800 0.12577  0.00169  -0.04785 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.41541 0.51311 0.30340 0.11144  -0.00479 -0.06891 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.45366 0.53528 0.29210 0.14822  0.00355  -0.03775 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.46485 0.55731 0.33865 0.11151  0.00139  -0.07478 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.42508 0.48613 0.27043 0.16423  0.00145  -0.01603 68  HIS A N   
536  C CA  . HIS A 68  ? 0.49878 0.51783 0.31641 0.17870  0.01276  0.00287  68  HIS A CA  
537  C C   . HIS A 68  ? 0.63786 0.63780 0.41108 0.19783  0.02148  0.01457  68  HIS A C   
538  O O   . HIS A 68  ? 0.65219 0.68546 0.40841 0.21823  0.01237  0.01211  68  HIS A O   
539  C CB  . HIS A 68  ? 0.57802 0.60747 0.39301 0.19698  0.00661  0.00723  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.66504 0.74672 0.47015 0.22225  -0.00681 0.00232  68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.59365 0.73563 0.43142 0.21272  -0.02148 -0.01656 68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.72117 0.80736 0.48544 0.25680  -0.00739 0.01270  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.63149 0.82230 0.45383 0.23886  -0.03184 -0.01980 68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.67631 0.83475 0.45320 0.26911  -0.02456 -0.00121 68  HIS A NE2 
545  N N   . THR A 69  ? 0.65430 0.60401 0.40822 0.18900  0.03976  0.02565  69  THR A N   
546  C CA  . THR A 69  ? 0.71862 0.64096 0.42444 0.20429  0.05232  0.03833  69  THR A CA  
547  C C   . THR A 69  ? 0.82920 0.69939 0.48601 0.22720  0.06494  0.05828  69  THR A C   
548  O O   . THR A 69  ? 0.92806 0.77392 0.53362 0.25036  0.07367  0.07170  69  THR A O   
549  C CB  . THR A 69  ? 0.71808 0.61988 0.42667 0.17897  0.06819  0.03665  69  THR A CB  
550  O OG1 . THR A 69  ? 0.73619 0.61845 0.47156 0.15232  0.07665  0.03392  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.70485 0.65264 0.43900 0.17057  0.05778  0.01987  69  THR A CG2 
552  N N   . GLY A 70  ? 0.85559 0.70639 0.52256 0.22417  0.06610  0.06046  70  GLY A N   
553  C CA  . GLY A 70  ? 0.91750 0.72560 0.53931 0.25306  0.07381  0.07653  70  GLY A CA  
554  C C   . GLY A 70  ? 0.93443 0.79423 0.56722 0.28291  0.05325  0.07243  70  GLY A C   
555  O O   . GLY A 70  ? 0.87954 0.80646 0.53778 0.28735  0.03482  0.05979  70  GLY A O   
556  N N   . HIS A 71  ? 0.94922 0.78027 0.56231 0.30246  0.05733  0.08122  71  HIS A N   
557  C CA  . HIS A 71  ? 1.00502 0.89804 0.64022 0.32369  0.04012  0.07112  71  HIS A CA  
558  C C   . HIS A 71  ? 0.91743 0.86706 0.61423 0.29884  0.02291  0.05431  71  HIS A C   
559  O O   . HIS A 71  ? 0.91040 0.84563 0.63758 0.26117  0.02746  0.04721  71  HIS A O   
560  C CB  . HIS A 71  ? 1.03168 0.88636 0.63860 0.34064  0.05282  0.07655  71  HIS A CB  
561  C CG  . HIS A 71  ? 1.10130 0.92073 0.65452 0.36937  0.06703  0.08571  71  HIS A CG  
562  N ND1 . HIS A 71  ? 1.19557 0.96813 0.71801 0.36500  0.08092  0.09498  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 1.12915 0.95675 0.65359 0.40460  0.06937  0.08652  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 1.19395 0.94238 0.67133 0.39637  0.09130  0.10141  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.23981 1.02076 0.71613 0.42264  0.08460  0.09658  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.84921 0.87042 0.56820 0.31465  0.00503  0.04328  72  LEU A N   
567  C CA  . LEU A 72  ? 0.81625 0.89457 0.59312 0.28561  -0.00822 0.02293  72  LEU A CA  
568  C C   . LEU A 72  ? 0.80068 0.84041 0.60095 0.25710  -0.00002 0.02250  72  LEU A C   
569  O O   . LEU A 72  ? 0.80625 0.81251 0.59032 0.27010  0.00744  0.03165  72  LEU A O   
570  C CB  . LEU A 72  ? 0.80159 0.95473 0.59269 0.30585  -0.02255 0.01192  72  LEU A CB  
571  C CG  . LEU A 72  ? 0.77897 0.99532 0.62408 0.27909  -0.03483 -0.00920 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.72915 0.97399 0.59985 0.24598  -0.04095 -0.02657 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.58865 0.87039 0.44294 0.29284  -0.04134 -0.02045 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.67666 0.71834 0.51008 0.22075  -0.00077 0.01203  73  GLY A N   
575  C CA  . GLY A 73  ? 0.55335 0.57429 0.41314 0.19445  0.00309  0.00867  73  GLY A CA  
576  C C   . GLY A 73  ? 0.57739 0.65203 0.47465 0.18241  -0.00907 -0.00670 73  GLY A C   
577  O O   . GLY A 73  ? 0.54489 0.67052 0.45329 0.18288  -0.01909 -0.01838 73  GLY A O   
578  N N   . PHE A 74  ? 0.41680 0.48026 0.33064 0.17042  -0.00692 -0.00765 74  PHE A N   
579  C CA  . PHE A 74  ? 0.35764 0.46710 0.30142 0.15857  -0.01504 -0.02088 74  PHE A CA  
580  C C   . PHE A 74  ? 0.44016 0.55705 0.40818 0.12773  -0.01759 -0.03304 74  PHE A C   
581  O O   . PHE A 74  ? 0.49325 0.65099 0.48013 0.11493  -0.02315 -0.04697 74  PHE A O   
582  C CB  . PHE A 74  ? 0.37544 0.46715 0.32438 0.15721  -0.01051 -0.01706 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.38085 0.52020 0.33607 0.17299  -0.01563 -0.02234 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.39212 0.53507 0.32139 0.20926  -0.01481 -0.01390 74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.48781 0.67229 0.47251 0.15256  -0.02055 -0.03690 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.51851 0.72052 0.45594 0.22884  -0.02074 -0.02071 74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.34624 0.58728 0.34091 0.16422  -0.02473 -0.04480 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.42297 0.68045 0.39714 0.20391  -0.02603 -0.03760 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.33696 0.41498 0.30324 0.11507  -0.01219 -0.02915 75  TYR A N   
590  C CA  . TYR A 75  ? 0.28932 0.36980 0.27122 0.09298  -0.01378 -0.03982 75  TYR A CA  
591  C C   . TYR A 75  ? 0.37071 0.46646 0.34343 0.09622  -0.01643 -0.04583 75  TYR A C   
592  O O   . TYR A 75  ? 0.47821 0.57300 0.45831 0.08032  -0.01672 -0.05603 75  TYR A O   
593  C CB  . TYR A 75  ? 0.31128 0.35288 0.29816 0.08084  -0.00800 -0.03492 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.34667 0.37944 0.34230 0.07557  -0.00688 -0.03217 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.32486 0.37580 0.33324 0.06403  -0.00951 -0.04044 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.33169 0.33757 0.31996 0.07998  -0.00165 -0.02267 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.30515 0.34834 0.31893 0.05961  -0.00760 -0.03761 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.29996 0.29934 0.29388 0.07582  -0.00087 -0.02134 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.34740 0.36598 0.35410 0.06706  -0.00422 -0.02799 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.29828 0.31029 0.30813 0.06318  -0.00253 -0.02630 75  TYR A OH  
601  N N   . ALA A 76  ? 0.44904 0.55884 0.40222 0.11840  -0.01818 -0.04033 76  ALA A N   
602  C CA  . ALA A 76  ? 0.42240 0.55102 0.36263 0.12466  -0.02135 -0.04575 76  ALA A CA  
603  C C   . ALA A 76  ? 0.42611 0.61514 0.37542 0.12317  -0.03196 -0.06291 76  ALA A C   
604  O O   . ALA A 76  ? 0.44997 0.67629 0.40210 0.13639  -0.03750 -0.06413 76  ALA A O   
605  C CB  . ALA A 76  ? 0.36039 0.46991 0.26786 0.15138  -0.01650 -0.02962 76  ALA A CB  
606  N N   . ASP A 77  ? 0.51340 0.71569 0.46722 0.10622  -0.03416 -0.07842 77  ASP A N   
607  C CA  . ASP A 77  ? 0.46575 0.73027 0.42437 0.10212  -0.04358 -0.09810 77  ASP A CA  
608  C C   . ASP A 77  ? 0.51190 0.80091 0.44800 0.12007  -0.04884 -0.10036 77  ASP A C   
609  O O   . ASP A 77  ? 0.52745 0.87945 0.46529 0.12213  -0.05867 -0.11665 77  ASP A O   
610  C CB  . ASP A 77  ? 0.48999 0.75485 0.46469 0.06627  -0.04138 -0.11916 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.46301 0.71039 0.45611 0.04789  -0.03623 -0.11892 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.43653 0.69917 0.43598 0.06155  -0.03812 -0.10943 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.44044 0.65551 0.43698 0.02243  -0.02944 -0.12763 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.47007 0.71551 0.38555 0.13032  -0.04205 -0.08676 78  TRP A N   
615  C CA  . TRP A 78  ? 0.54534 0.80665 0.43654 0.14378  -0.04483 -0.08932 78  TRP A CA  
616  C C   . TRP A 78  ? 0.49365 0.72241 0.35249 0.17400  -0.03832 -0.06471 78  TRP A C   
617  O O   . TRP A 78  ? 0.45773 0.63506 0.31448 0.17304  -0.02746 -0.04872 78  TRP A O   
618  C CB  . TRP A 78  ? 0.54776 0.78573 0.44111 0.12080  -0.03942 -0.10158 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.53186 0.78697 0.44750 0.09002  -0.04205 -0.12540 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.52139 0.74534 0.45670 0.06824  -0.03612 -0.12741 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.53478 0.84009 0.45094 0.07597  -0.04965 -0.15141 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.50242 0.74553 0.44679 0.04073  -0.03727 -0.15176 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.53599 0.83104 0.47080 0.04242  -0.04539 -0.16838 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.48835 0.84663 0.38811 0.08775  -0.05908 -0.16302 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.52633 0.85873 0.46420 0.01558  -0.04816 -0.19805 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.52494 0.93011 0.43175 0.06247  -0.06463 -0.19381 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.52819 0.91813 0.45397 0.02440  -0.05811 -0.21179 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.48121 0.73872 0.31209 0.19899  -0.04388 -0.06293 79  ARG A N   
629  C CA  . ARG A 79  ? 0.53338 0.75631 0.32125 0.22720  -0.03553 -0.04140 79  ARG A CA  
630  C C   . ARG A 79  ? 0.58544 0.78630 0.36159 0.21516  -0.02782 -0.04435 79  ARG A C   
631  O O   . ARG A 79  ? 0.53730 0.76450 0.33129 0.19475  -0.03335 -0.06526 79  ARG A O   
632  C CB  . ARG A 79  ? 0.62129 0.89140 0.37885 0.26559  -0.04643 -0.03829 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.69868 0.99667 0.47013 0.28258  -0.05241 -0.03585 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.58764 0.95006 0.36500 0.30417  -0.05965 -0.04516 79  ARG A CD  
635  N NE  . ARG A 79  ? 0.71441 1.05520 0.45330 0.33249  -0.05328 -0.03114 79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.75767 1.13812 0.49510 0.33411  -0.05951 -0.04231 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.76765 1.20851 0.53912 0.30671  -0.07083 -0.06882 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.79623 1.15213 0.49511 0.36254  -0.05282 -0.02726 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.58375 0.73379 0.32857 0.22555  -0.01298 -0.02480 80  PRO A N   
640  C CA  . PRO A 80  ? 0.64884 0.78156 0.38385 0.21386  -0.00374 -0.02802 80  PRO A CA  
641  C C   . PRO A 80  ? 0.67402 0.85447 0.39503 0.22185  -0.01466 -0.04337 80  PRO A C   
642  O O   . PRO A 80  ? 0.65789 0.84060 0.38648 0.20425  -0.01221 -0.05743 80  PRO A O   
643  C CB  . PRO A 80  ? 0.63752 0.71412 0.33224 0.22780  0.01499  -0.00302 80  PRO A CB  
644  C CG  . PRO A 80  ? 0.69811 0.74584 0.39877 0.23033  0.01879  0.00940  80  PRO A CG  
645  C CD  . PRO A 80  ? 0.64205 0.74275 0.35820 0.24428  -0.00082 -0.00024 80  PRO A CD  
646  N N   . ALA A 81  ? 0.64560 0.86877 0.34630 0.24922  -0.02735 -0.04297 81  ALA A N   
647  C CA  . ALA A 81  ? 0.71620 0.98628 0.41588 0.25319  -0.03750 -0.05671 81  ALA A CA  
648  C C   . ALA A 81  ? 0.63496 0.95071 0.37022 0.22293  -0.04861 -0.08835 81  ALA A C   
649  O O   . ALA A 81  ? 0.73033 1.07152 0.46421 0.21595  -0.05260 -0.10309 81  ALA A O   
650  C CB  . ALA A 81  ? 0.74933 1.05342 0.44076 0.28607  -0.04580 -0.04795 81  ALA A CB  
651  N N   . GLU A 82  ? 0.61688 0.93633 0.38034 0.20290  -0.05143 -0.09927 82  GLU A N   
652  C CA  . GLU A 82  ? 0.62189 0.97039 0.41557 0.16943  -0.05763 -0.12930 82  GLU A CA  
653  C C   . GLU A 82  ? 0.64145 0.93594 0.44785 0.14232  -0.04469 -0.13434 82  GLU A C   
654  O O   . GLU A 82  ? 0.60031 0.89806 0.42810 0.11378  -0.04555 -0.15585 82  GLU A O   
655  C CB  . GLU A 82  ? 0.65838 1.03631 0.48407 0.15832  -0.06497 -0.13675 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.72624 1.16623 0.56016 0.17901  -0.07545 -0.13542 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.55823 1.01433 0.41195 0.18466  -0.07825 -0.12989 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.57479 0.98381 0.42147 0.18859  -0.07282 -0.11445 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.63761 1.15627 0.51341 0.18571  -0.08454 -0.14177 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.61717 0.86239 0.40857 0.15092  -0.03143 -0.11574 83  ALA A N   
661  C CA  . ALA A 83  ? 0.60635 0.80807 0.41231 0.13054  -0.01975 -0.11990 83  ALA A CA  
662  C C   . ALA A 83  ? 0.62033 0.83309 0.42195 0.11488  -0.02083 -0.14605 83  ALA A C   
663  O O   . ALA A 83  ? 0.57777 0.76857 0.39628 0.09337  -0.01696 -0.15995 83  ALA A O   
664  C CB  . ALA A 83  ? 0.68298 0.84431 0.47372 0.14196  -0.00491 -0.09832 83  ALA A CB  
665  N N   . ASP A 84  ? 0.60076 0.84353 0.37491 0.12652  -0.02518 -0.15336 84  ASP A N   
666  C CA  . ASP A 84  ? 0.64598 0.89583 0.41213 0.11056  -0.02491 -0.18029 84  ASP A CA  
667  C C   . ASP A 84  ? 0.66347 0.93815 0.44963 0.08371  -0.03346 -0.20584 84  ASP A C   
668  O O   . ASP A 84  ? 0.62572 0.87412 0.41538 0.06003  -0.02705 -0.22555 84  ASP A O   
669  C CB  . ASP A 84  ? 0.70015 0.97649 0.43997 0.12573  -0.02842 -0.17872 84  ASP A CB  
670  C CG  . ASP A 84  ? 0.77067 1.01568 0.48476 0.14633  -0.01522 -0.15692 84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.79399 0.99853 0.51445 0.14099  -0.00143 -0.15275 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.87328 1.13304 0.56432 0.16641  -0.01743 -0.14267 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.60703 0.92742 0.40748 0.08641  -0.04546 -0.20351 85  LYS A N   
674  C CA  . LYS A 85  ? 0.64811 0.99426 0.47302 0.05674  -0.05041 -0.22533 85  LYS A CA  
675  C C   . LYS A 85  ? 0.62064 0.91886 0.45824 0.03567  -0.04126 -0.23072 85  LYS A C   
676  O O   . LYS A 85  ? 0.65967 0.93930 0.50336 0.00490  -0.03557 -0.25080 85  LYS A O   
677  C CB  . LYS A 85  ? 0.58849 0.99856 0.42993 0.06853  -0.06302 -0.21993 85  LYS A CB  
678  N N   . LEU A 86  ? 0.57516 0.83800 0.42144 0.05138  -0.03618 -0.20381 86  LEU A N   
679  C CA  . LEU A 86  ? 0.62079 0.83158 0.48493 0.03646  -0.02667 -0.19830 86  LEU A CA  
680  C C   . LEU A 86  ? 0.64469 0.80230 0.49765 0.02604  -0.01443 -0.20781 86  LEU A C   
681  O O   . LEU A 86  ? 0.68601 0.80925 0.54266 0.00449  -0.00759 -0.21965 86  LEU A O   
682  C CB  . LEU A 86  ? 0.55473 0.74436 0.42807 0.05746  -0.02417 -0.16760 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.57957 0.73083 0.47311 0.04671  -0.01823 -0.15942 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.60111 0.77411 0.50825 0.02406  -0.02262 -0.17542 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.54480 0.69121 0.44483 0.06642  -0.01833 -0.13315 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.58861 0.73427 0.42500 0.04364  -0.00964 -0.20085 87  VAL A N   
687  C CA  . VAL A 87  ? 0.62346 0.72377 0.44746 0.04000  0.00228  -0.20999 87  VAL A CA  
688  C C   . VAL A 87  ? 0.65291 0.74641 0.46353 0.01383  0.00398  -0.24154 87  VAL A C   
689  O O   . VAL A 87  ? 0.74836 0.79097 0.55476 0.00033  0.01412  -0.25027 87  VAL A O   
690  C CB  . VAL A 87  ? 0.64004 0.74627 0.44568 0.06088  0.00632  -0.20286 87  VAL A CB  
691  C CG1 . VAL A 87  ? 0.63632 0.70958 0.42316 0.05725  0.01712  -0.22087 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.58600 0.68231 0.40255 0.07978  0.01117  -0.17371 87  VAL A CG2 
693  N N   . LYS A 88  ? 0.65815 0.80221 0.45828 0.00656  -0.00522 -0.25963 88  LYS A N   
694  C CA  . LYS A 88  ? 0.70410 0.84228 0.49688 -0.02278 -0.00318 -0.28273 88  LYS A CA  
695  C C   . LYS A 88  ? 0.79191 0.91180 0.59895 -0.05121 0.00036  -0.29055 88  LYS A C   
696  O O   . LYS A 88  ? 0.85488 0.92410 0.64877 -0.07297 0.01164  -0.30349 88  LYS A O   
697  C CB  . LYS A 88  ? 0.73765 0.94286 0.52988 -0.02279 -0.01589 -0.28937 88  LYS A CB  
698  C CG  . LYS A 88  ? 0.71193 0.91922 0.49602 -0.05195 -0.01372 -0.31445 88  LYS A CG  
699  C CD  . LYS A 88  ? 0.71386 0.99070 0.49645 -0.04444 -0.02621 -0.31980 88  LYS A CD  
700  C CE  . LYS A 88  ? 0.73378 1.03317 0.51825 -0.07744 -0.02597 -0.34665 88  LYS A CE  
701  N NZ  . LYS A 88  ? 0.73948 1.09360 0.51427 -0.06626 -0.03562 -0.35346 88  LYS A NZ  
702  N N   . LEU A 89  ? 0.74811 0.90463 0.57861 -0.05038 -0.00777 -0.28149 89  LEU A N   
703  C CA  . LEU A 89  ? 0.73015 0.87440 0.57398 -0.07975 -0.00304 -0.28894 89  LEU A CA  
704  C C   . LEU A 89  ? 0.75294 0.81689 0.58816 -0.08203 0.01131  -0.28260 89  LEU A C   
705  O O   . LEU A 89  ? 0.80357 0.82037 0.62856 -0.10679 0.02286  -0.29130 89  LEU A O   
706  C CB  . LEU A 89  ? 0.73990 0.94787 0.61101 -0.07623 -0.01493 -0.28121 89  LEU A CB  
707  C CG  . LEU A 89  ? 0.69233 0.98223 0.57441 -0.07691 -0.02709 -0.28972 89  LEU A CG  
708  C CD1 . LEU A 89  ? 0.71186 1.06244 0.62016 -0.06742 -0.03721 -0.28043 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 0.79228 1.08586 0.67153 -0.11285 -0.02002 -0.31453 89  LEU A CD2 
710  N N   . LEU A 90  ? 0.72649 0.77082 0.56765 -0.05248 0.01135  -0.25875 90  LEU A N   
711  C CA  . LEU A 90  ? 0.72937 0.70242 0.56529 -0.04669 0.02350  -0.24611 90  LEU A CA  
712  C C   . LEU A 90  ? 0.89878 0.81350 0.70233 -0.05101 0.03708  -0.26255 90  LEU A C   
713  O O   . LEU A 90  ? 0.96550 0.81540 0.75237 -0.05981 0.04984  -0.26483 90  LEU A O   
714  C CB  . LEU A 90  ? 0.75119 0.72492 0.60236 -0.01379 0.02025  -0.21653 90  LEU A CB  
715  C CG  . LEU A 90  ? 0.78648 0.77275 0.66267 -0.01007 0.01490  -0.19652 90  LEU A CG  
716  C CD1 . LEU A 90  ? 0.77695 0.77259 0.66532 0.01817  0.01198  -0.17181 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 0.78131 0.71570 0.65478 -0.02298 0.02392  -0.19527 90  LEU A CD2 
718  N N   . ALA A 91  ? 0.84786 0.78079 0.63818 -0.04143 0.03538  -0.27215 91  ALA A N   
719  C CA  . ALA A 91  ? 0.94033 0.82130 0.70046 -0.04009 0.04654  -0.28256 91  ALA A CA  
720  C C   . ALA A 91  ? 1.01757 0.85717 0.76299 -0.07029 0.05381  -0.29475 91  ALA A C   
721  O O   . ALA A 91  ? 1.08184 0.85361 0.81142 -0.06707 0.06558  -0.28955 91  ALA A O   
722  C CB  . ALA A 91  ? 0.92162 0.84186 0.67208 -0.03279 0.04085  -0.29130 91  ALA A CB  
723  N N   . LYS A 92  ? 0.95421 0.83917 0.70668 -0.09827 0.04732  -0.30966 92  LYS A N   
724  C CA  . LYS A 92  ? 1.04193 0.89581 0.78414 -0.13206 0.05693  -0.32265 92  LYS A CA  
725  C C   . LYS A 92  ? 1.06147 0.86922 0.80658 -0.13817 0.06600  -0.30957 92  LYS A C   
726  O O   . LYS A 92  ? 1.16462 0.90356 0.88591 -0.14727 0.08083  -0.31017 92  LYS A O   
727  C CB  . LYS A 92  ? 1.07537 1.00432 0.83630 -0.16087 0.04831  -0.33870 92  LYS A CB  
728  C CG  . LYS A 92  ? 1.08683 1.00124 0.85009 -0.19909 0.05962  -0.34771 92  LYS A CG  
729  C CD  . LYS A 92  ? 1.10419 0.98517 0.84082 -0.22570 0.07251  -0.36895 92  LYS A CD  
730  C CE  . LYS A 92  ? 1.15000 0.94282 0.84944 -0.20570 0.08351  -0.36537 92  LYS A CE  
731  N NZ  . LYS A 92  ? 1.18512 0.95786 0.85846 -0.22725 0.09271  -0.38844 92  LYS A NZ  
732  N N   . GLY A 93  ? 1.04775 0.89088 0.81919 -0.13096 0.05784  -0.29646 93  GLY A N   
733  C CA  . GLY A 93  ? 1.05185 0.86158 0.82772 -0.13954 0.06515  -0.28468 93  GLY A CA  
734  C C   . GLY A 93  ? 1.04375 0.88907 0.83277 -0.17787 0.06711  -0.29636 93  GLY A C   
735  O O   . GLY A 93  ? 0.99625 0.92111 0.80803 -0.18775 0.05546  -0.30711 93  GLY A O   
736  N N   . GLU A 94  ? 1.10964 0.90012 0.88360 -0.19749 0.08291  -0.29354 94  GLU A N   
737  C CA  . GLU A 94  ? 1.16655 0.98321 0.94960 -0.23671 0.09086  -0.30428 94  GLU A CA  
738  C C   . GLU A 94  ? 1.10754 1.00022 0.92903 -0.23878 0.07878  -0.29982 94  GLU A C   
739  O O   . GLU A 94  ? 1.11530 1.05117 0.95127 -0.26904 0.08369  -0.31059 94  GLU A O   
740  C CB  . GLU A 94  ? 1.11306 0.96234 0.89171 -0.26540 0.09425  -0.32966 94  GLU A CB  
741  N N   . TYR A 95  ? 1.03737 0.94916 0.87476 -0.20691 0.06464  -0.28511 95  TYR A N   
742  C CA  . TYR A 95  ? 0.90158 0.87854 0.77197 -0.20258 0.05291  -0.27883 95  TYR A CA  
743  C C   . TYR A 95  ? 0.92566 0.86542 0.79470 -0.21551 0.06456  -0.26810 95  TYR A C   
744  O O   . TYR A 95  ? 1.00168 0.85873 0.84202 -0.21721 0.07961  -0.25950 95  TYR A O   
745  C CB  . TYR A 95  ? 0.84351 0.83742 0.72375 -0.16460 0.03826  -0.26579 95  TYR A CB  
746  C CG  . TYR A 95  ? 0.88733 0.79908 0.74499 -0.14215 0.04658  -0.25122 95  TYR A CG  
747  C CD1 . TYR A 95  ? 0.87357 0.74296 0.73147 -0.13427 0.05228  -0.23159 95  TYR A CD1 
748  C CD2 . TYR A 95  ? 0.97106 0.85305 0.80907 -0.12460 0.04842  -0.25308 95  TYR A CD2 
749  C CE1 . TYR A 95  ? 0.90948 0.71525 0.75047 -0.10725 0.05791  -0.21362 95  TYR A CE1 
750  C CE2 . TYR A 95  ? 0.98861 0.80681 0.81044 -0.09856 0.05551  -0.23682 95  TYR A CE2 
751  C CZ  . TYR A 95  ? 0.94434 0.72757 0.76861 -0.08905 0.05940  -0.21676 95  TYR A CZ  
752  O OH  . TYR A 95  ? 1.04780 0.77917 0.85750 -0.05931 0.06447  -0.20070 95  TYR A OH  
753  N N   . GLN A 96  ? 0.79155 0.79361 0.68970 -0.22040 0.05738  -0.26691 96  GLN A N   
754  C CA  . GLN A 96  ? 0.76795 0.73943 0.66506 -0.23120 0.06795  -0.25619 96  GLN A CA  
755  C C   . GLN A 96  ? 0.74045 0.70481 0.64781 -0.20134 0.05781  -0.23795 96  GLN A C   
756  O O   . GLN A 96  ? 0.70753 0.71859 0.63460 -0.17236 0.04098  -0.22996 96  GLN A O   
757  C CB  . GLN A 96  ? 0.77069 0.81098 0.69064 -0.25952 0.07136  -0.26802 96  GLN A CB  
758  C CG  . GLN A 96  ? 0.82081 0.82019 0.73099 -0.27775 0.08821  -0.25931 96  GLN A CG  
759  C CD  . GLN A 96  ? 0.85095 0.74232 0.71607 -0.28585 0.10881  -0.25141 96  GLN A CD  
760  O OE1 . GLN A 96  ? 0.78946 0.61488 0.63655 -0.26340 0.11034  -0.23163 96  GLN A OE1 
761  N NE2 . GLN A 96  ? 0.93697 0.81218 0.78188 -0.31569 0.12516  -0.26671 96  GLN A NE2 
762  N N   . LYS A 97  ? 0.70509 0.60922 0.59821 -0.20220 0.06903  -0.22349 97  LYS A N   
763  C CA  . LYS A 97  ? 0.65091 0.54728 0.55605 -0.16817 0.06060  -0.19616 97  LYS A CA  
764  C C   . LYS A 97  ? 0.64831 0.58673 0.57542 -0.17904 0.05983  -0.19241 97  LYS A C   
765  O O   . LYS A 97  ? 0.65423 0.59034 0.57382 -0.21579 0.07343  -0.20785 97  LYS A O   
766  C CB  . LYS A 97  ? 0.70565 0.50956 0.57795 -0.15285 0.07159  -0.17995 97  LYS A CB  
767  C CG  . LYS A 97  ? 0.69470 0.45603 0.54359 -0.13758 0.07372  -0.18363 97  LYS A CG  
768  C CD  . LYS A 97  ? 0.78606 0.46295 0.60156 -0.11692 0.08416  -0.16743 97  LYS A CD  
769  C CE  . LYS A 97  ? 0.76500 0.39109 0.54785 -0.11882 0.09508  -0.17363 97  LYS A CE  
770  N NZ  . LYS A 97  ? 0.86815 0.42295 0.61875 -0.09470 0.10428  -0.15406 97  LYS A NZ  
771  N N   . VAL A 98  ? 0.53703 0.51696 0.49033 -0.14904 0.04517  -0.17424 98  VAL A N   
772  C CA  . VAL A 98  ? 0.54043 0.55222 0.51192 -0.15090 0.04437  -0.16676 98  VAL A CA  
773  C C   . VAL A 98  ? 0.46465 0.43381 0.43180 -0.12213 0.04191  -0.14015 98  VAL A C   
774  O O   . VAL A 98  ? 0.46744 0.42071 0.43344 -0.09459 0.03399  -0.12788 98  VAL A O   
775  C CB  . VAL A 98  ? 0.51740 0.62146 0.52103 -0.14027 0.02993  -0.17158 98  VAL A CB  
776  C CG1 . VAL A 98  ? 0.53514 0.69205 0.54368 -0.15949 0.02722  -0.19784 98  VAL A CG1 
777  C CG2 . VAL A 98  ? 0.54253 0.65307 0.55448 -0.09976 0.01611  -0.15144 98  VAL A CG2 
778  N N   . SER A 99  ? 0.44468 0.40151 0.41007 -0.12987 0.04902  -0.13273 99  SER A N   
779  C CA  . SER A 99  ? 0.44325 0.35967 0.40060 -0.10703 0.04794  -0.11050 99  SER A CA  
780  C C   . SER A 99  ? 0.42303 0.38631 0.40424 -0.09593 0.04039  -0.10192 99  SER A C   
781  O O   . SER A 99  ? 0.42274 0.42680 0.41587 -0.11412 0.04430  -0.11186 99  SER A O   
782  C CB  . SER A 99  ? 0.59580 0.44063 0.51839 -0.12247 0.06522  -0.10701 99  SER A CB  
783  O OG  . SER A 99  ? 0.66351 0.45453 0.55738 -0.12818 0.07378  -0.11409 99  SER A OG  
784  N N   . TYR A 100 ? 0.40037 0.35845 0.38712 -0.06774 0.03112  -0.08547 100 TYR A N   
785  C CA  . TYR A 100 ? 0.37331 0.35977 0.37470 -0.05635 0.02645  -0.07653 100 TYR A CA  
786  C C   . TYR A 100 ? 0.37309 0.31517 0.35950 -0.04778 0.02946  -0.06176 100 TYR A C   
787  O O   . TYR A 100 ? 0.37146 0.27316 0.34286 -0.03741 0.02910  -0.05489 100 TYR A O   
788  C CB  . TYR A 100 ? 0.33767 0.35436 0.35434 -0.03091 0.01423  -0.07005 100 TYR A CB  
789  C CG  . TYR A 100 ? 0.31252 0.38394 0.34305 -0.02925 0.00854  -0.08114 100 TYR A CG  
790  C CD1 . TYR A 100 ? 0.36618 0.47077 0.40177 -0.05207 0.01267  -0.09881 100 TYR A CD1 
791  C CD2 . TYR A 100 ? 0.39170 0.48131 0.42692 -0.00448 -0.00009 -0.07406 100 TYR A CD2 
792  C CE1 . TYR A 100 ? 0.38187 0.54801 0.43036 -0.04724 0.00529  -0.11041 100 TYR A CE1 
793  C CE2 . TYR A 100 ? 0.36786 0.50760 0.40998 0.00317  -0.00608 -0.08254 100 TYR A CE2 
794  C CZ  . TYR A 100 ? 0.36788 0.55005 0.41818 -0.01643 -0.00476 -0.10069 100 TYR A CZ  
795  O OH  . TYR A 100 ? 0.43274 0.67463 0.49005 -0.00591 -0.01256 -0.11025 100 TYR A OH  
796  N N   . PRO A 101 ? 0.38037 0.33454 0.37056 -0.04827 0.03137  -0.05700 101 PRO A N   
797  C CA  . PRO A 101 ? 0.34085 0.25717 0.31439 -0.03970 0.03345  -0.04390 101 PRO A CA  
798  C C   . PRO A 101 ? 0.37583 0.29445 0.35655 -0.01494 0.02211  -0.03407 101 PRO A C   
799  O O   . PRO A 101 ? 0.35719 0.30569 0.35485 -0.00521 0.01490  -0.03545 101 PRO A O   
800  C CB  . PRO A 101 ? 0.35544 0.29132 0.33153 -0.05097 0.04020  -0.04498 101 PRO A CB  
801  C CG  . PRO A 101 ? 0.32351 0.30566 0.31570 -0.07215 0.04513  -0.06166 101 PRO A CG  
802  C CD  . PRO A 101 ? 0.30422 0.30959 0.31126 -0.05830 0.03335  -0.06567 101 PRO A CD  
803  N N   . LEU A 102 ? 0.35817 0.24481 0.32260 -0.00479 0.02161  -0.02438 102 LEU A N   
804  C CA  . LEU A 102 ? 0.32227 0.21516 0.29307 0.01367  0.01218  -0.01816 102 LEU A CA  
805  C C   . LEU A 102 ? 0.33674 0.22543 0.29884 0.01815  0.01176  -0.01164 102 LEU A C   
806  O O   . LEU A 102 ? 0.34675 0.21897 0.29284 0.00997  0.01939  -0.00923 102 LEU A O   
807  C CB  . LEU A 102 ? 0.35160 0.22400 0.31349 0.02604  0.00911  -0.01545 102 LEU A CB  
808  C CG  . LEU A 102 ? 0.33724 0.21145 0.30483 0.02212  0.01011  -0.02284 102 LEU A CG  
809  C CD1 . LEU A 102 ? 0.38542 0.23192 0.33748 0.03514  0.01044  -0.02067 102 LEU A CD1 
810  C CD2 . LEU A 102 ? 0.35108 0.26059 0.34098 0.02533  0.00396  -0.02592 102 LEU A CD2 
811  N N   . LEU A 103 ? 0.34947 0.25206 0.31969 0.02914  0.00413  -0.00992 103 LEU A N   
812  C CA  . LEU A 103 ? 0.33957 0.24330 0.30201 0.03318  0.00231  -0.00648 103 LEU A CA  
813  C C   . LEU A 103 ? 0.36555 0.26473 0.31882 0.04662  -0.00447 -0.00298 103 LEU A C   
814  O O   . LEU A 103 ? 0.33969 0.25280 0.30471 0.05255  -0.00999 -0.00608 103 LEU A O   
815  C CB  . LEU A 103 ? 0.31222 0.23638 0.28736 0.03283  0.00041  -0.01047 103 LEU A CB  
816  C CG  . LEU A 103 ? 0.33175 0.25753 0.29794 0.03548  -0.00161 -0.01009 103 LEU A CG  
817  C CD1 . LEU A 103 ? 0.33042 0.24960 0.28355 0.03128  0.00464  -0.00730 103 LEU A CD1 
818  C CD2 . LEU A 103 ? 0.35125 0.28628 0.32578 0.03476  -0.00139 -0.01553 103 LEU A CD2 
819  N N   . LYS A 104 ? 0.36339 0.24749 0.29458 0.05265  -0.00378 0.00308  104 LYS A N   
820  C CA  . LYS A 104 ? 0.39901 0.28822 0.31931 0.07022  -0.01190 0.00604  104 LYS A CA  
821  C C   . LYS A 104 ? 0.41729 0.33196 0.34129 0.06945  -0.01776 0.00191  104 LYS A C   
822  O O   . LYS A 104 ? 0.39591 0.30387 0.31079 0.06248  -0.01325 0.00320  104 LYS A O   
823  C CB  . LYS A 104 ? 0.45498 0.30760 0.34043 0.08207  -0.00730 0.01633  104 LYS A CB  
824  C CG  . LYS A 104 ? 0.48226 0.34608 0.35202 0.10787  -0.01730 0.02035  104 LYS A CG  
825  C CD  . LYS A 104 ? 0.51593 0.33200 0.34001 0.12421  -0.01053 0.03363  104 LYS A CD  
826  C CE  . LYS A 104 ? 0.56728 0.40010 0.37426 0.15611  -0.02175 0.03788  104 LYS A CE  
827  N NZ  . LYS A 104 ? 0.63611 0.41038 0.39122 0.17787  -0.01314 0.05285  104 LYS A NZ  
828  N N   . THR A 105 ? 0.37419 0.32017 0.31264 0.07327  -0.02621 -0.00543 105 THR A N   
829  C CA  . THR A 105 ? 0.39875 0.37025 0.33781 0.07040  -0.03176 -0.01274 105 THR A CA  
830  C C   . THR A 105 ? 0.39916 0.39459 0.32743 0.08957  -0.04221 -0.01249 105 THR A C   
831  O O   . THR A 105 ? 0.38099 0.39334 0.31757 0.10103  -0.04690 -0.01369 105 THR A O   
832  C CB  . THR A 105 ? 0.40916 0.40001 0.37044 0.05491  -0.03090 -0.02461 105 THR A CB  
833  O OG1 . THR A 105 ? 0.40259 0.37133 0.36875 0.04448  -0.02184 -0.02312 105 THR A OG1 
834  C CG2 . THR A 105 ? 0.38403 0.39650 0.34272 0.04674  -0.03426 -0.03551 105 THR A CG2 
835  N N   . THR A 106 ? 0.37303 0.37348 0.28124 0.09612  -0.04612 -0.01109 106 THR A N   
836  C CA  . THR A 106 ? 0.39663 0.43036 0.29362 0.11758  -0.05814 -0.01239 106 THR A CA  
837  C C   . THR A 106 ? 0.43168 0.50863 0.33767 0.10509  -0.06497 -0.02834 106 THR A C   
838  O O   . THR A 106 ? 0.41107 0.47389 0.30796 0.09198  -0.06041 -0.03048 106 THR A O   
839  C CB  . THR A 106 ? 0.44791 0.44945 0.30395 0.14113  -0.05734 0.00382  106 THR A CB  
840  O OG1 . THR A 106 ? 0.49530 0.44826 0.33951 0.14659  -0.04747 0.01614  106 THR A OG1 
841  C CG2 . THR A 106 ? 0.49205 0.53295 0.33280 0.17186  -0.07158 0.00354  106 THR A CG2 
842  N N   . VAL A 107 ? 0.37034 0.50206 0.29330 0.10806  -0.07490 -0.04137 107 VAL A N   
843  C CA  . VAL A 107 ? 0.40770 0.58665 0.33888 0.09224  -0.08104 -0.06080 107 VAL A CA  
844  C C   . VAL A 107 ? 0.45039 0.67893 0.36677 0.11942  -0.09650 -0.06263 107 VAL A C   
845  O O   . VAL A 107 ? 0.44697 0.71124 0.37070 0.14142  -0.10459 -0.06227 107 VAL A O   
846  C CB  . VAL A 107 ? 0.39143 0.60198 0.35501 0.06705  -0.07797 -0.07879 107 VAL A CB  
847  C CG1 . VAL A 107 ? 0.36700 0.61671 0.33507 0.04338  -0.08033 -0.10122 107 VAL A CG1 
848  C CG2 . VAL A 107 ? 0.39847 0.55779 0.37043 0.04855  -0.06335 -0.07365 107 VAL A CG2 
849  N N   . LYS A 108 ? 0.44444 0.67772 0.33831 0.12090  -0.10070 -0.06477 108 LYS A N   
850  C CA  . LYS A 108 ? 0.44526 0.73010 0.32073 0.14800  -0.11654 -0.06751 108 LYS A CA  
851  C C   . LYS A 108 ? 0.55690 0.91233 0.45030 0.12486  -0.12488 -0.09633 108 LYS A C   
852  O O   . LYS A 108 ? 0.49107 0.82957 0.39034 0.09049  -0.11601 -0.10906 108 LYS A O   
853  C CB  . LYS A 108 ? 0.59080 0.83332 0.42173 0.16716  -0.11529 -0.04992 108 LYS A CB  
854  C CG  . LYS A 108 ? 0.57152 0.74285 0.37703 0.18761  -0.10501 -0.02299 108 LYS A CG  
855  C CD  . LYS A 108 ? 0.76347 0.90344 0.51767 0.21181  -0.10464 -0.00606 108 LYS A CD  
856  C CE  . LYS A 108 ? 0.81916 0.89040 0.54156 0.23433  -0.09376 0.01912  108 LYS A CE  
857  N NZ  . LYS A 108 ? 0.74599 0.76935 0.49084 0.20428  -0.07734 0.02125  108 LYS A NZ  
858  N N   . TYR A 109 ? 0.58296 1.01245 0.48211 0.14452  -0.13891 -0.10603 109 TYR A N   
859  C CA  . TYR A 109 ? 0.56440 1.06206 0.48808 0.11954  -0.14050 -0.13328 109 TYR A CA  
860  C C   . TYR A 109 ? 0.65167 1.18764 0.55891 0.13889  -0.14800 -0.13566 109 TYR A C   
861  O O   . TYR A 109 ? 0.61697 1.11671 0.48853 0.15613  -0.15010 -0.12130 109 TYR A O   
862  C CB  . TYR A 109 ? 0.53828 1.09165 0.49973 0.11521  -0.13902 -0.14560 109 TYR A CB  
863  C CG  . TYR A 109 ? 0.51519 1.03890 0.49570 0.09793  -0.13165 -0.14398 109 TYR A CG  
864  C CD1 . TYR A 109 ? 0.48466 1.00100 0.48246 0.05149  -0.12182 -0.16265 109 TYR A CD1 
865  C CD2 . TYR A 109 ? 0.47180 0.96898 0.44975 0.12818  -0.13232 -0.12384 109 TYR A CD2 
866  C CE1 . TYR A 109 ? 0.44371 0.92397 0.45743 0.03636  -0.11048 -0.15858 109 TYR A CE1 
867  C CE2 . TYR A 109 ? 0.45089 0.91858 0.44776 0.11208  -0.12323 -0.12167 109 TYR A CE2 
868  C CZ  . TYR A 109 ? 0.50468 0.96005 0.51980 0.06625  -0.11042 -0.13718 109 TYR A CZ  
869  O OH  . TYR A 109 ? 0.48927 0.90363 0.51936 0.05040  -0.09637 -0.13191 109 TYR A OH  
870  N N   . GLY A 110 ? 0.76052 1.37268 0.69289 0.13544  -0.15086 -0.15483 110 GLY A N   
871  C CA  . GLY A 110 ? 0.60932 1.27018 0.52940 0.15710  -0.15882 -0.15940 110 GLY A CA  
872  C C   . GLY A 110 ? 0.76378 1.50969 0.70700 0.17264  -0.16222 -0.17346 110 GLY A C   
873  O O   . GLY A 110 ? 0.66532 1.45637 0.59614 0.19772  -0.16954 -0.17657 110 GLY A O   
874  N N   . LYS A 114 ? 0.55600 1.07367 0.45425 0.29554  -0.14171 -0.07682 114 LYS A N   
875  C CA  . LYS A 114 ? 0.57987 1.09771 0.49388 0.25384  -0.14333 -0.08716 114 LYS A CA  
876  C C   . LYS A 114 ? 0.65579 1.08951 0.55417 0.24246  -0.13800 -0.06958 114 LYS A C   
877  O O   . LYS A 114 ? 0.63600 1.04270 0.51723 0.22840  -0.13886 -0.06722 114 LYS A O   
878  C CB  . LYS A 114 ? 0.56669 1.10964 0.46407 0.25498  -0.14966 -0.09314 114 LYS A CB  
879  N N   . GLU A 115 ? 0.48624 0.88086 0.38893 0.24810  -0.13183 -0.05869 115 GLU A N   
880  C CA  . GLU A 115 ? 0.51750 0.84004 0.40957 0.23575  -0.12613 -0.04458 115 GLU A CA  
881  C C   . GLU A 115 ? 0.54890 0.85802 0.46655 0.22838  -0.11931 -0.04426 115 GLU A C   
882  O O   . GLU A 115 ? 0.55856 0.86931 0.47373 0.25316  -0.11712 -0.03915 115 GLU A O   
883  C CB  . GLU A 115 ? 0.66491 0.91170 0.50636 0.26231  -0.11981 -0.01911 115 GLU A CB  
884  C CG  . GLU A 115 ? 0.61797 0.78311 0.44710 0.25271  -0.10630 -0.00313 115 GLU A CG  
885  C CD  . GLU A 115 ? 0.76919 0.85998 0.54356 0.27282  -0.09797 0.02007  115 GLU A CD  
886  O OE1 . GLU A 115 ? 0.77386 0.86664 0.52342 0.27634  -0.10073 0.02257  115 GLU A OE1 
887  O OE2 . GLU A 115 ? 0.84364 0.87041 0.59939 0.28065  -0.08575 0.03435  115 GLU A OE2 
888  N N   . ALA A 116 ? 0.44033 0.72208 0.38096 0.18750  -0.10758 -0.05032 116 ALA A N   
889  C CA  . ALA A 116 ? 0.44678 0.70878 0.41033 0.17439  -0.09769 -0.05026 116 ALA A CA  
890  C C   . ALA A 116 ? 0.43220 0.61096 0.38111 0.16182  -0.08412 -0.03504 116 ALA A C   
891  O O   . ALA A 116 ? 0.40430 0.55680 0.34341 0.14475  -0.08001 -0.03354 116 ALA A O   
892  C CB  . ALA A 116 ? 0.42316 0.72982 0.42397 0.13729  -0.09467 -0.07193 116 ALA A CB  
893  N N   . THR A 117 ? 0.40342 0.54486 0.35088 0.16966  -0.07686 -0.02560 117 THR A N   
894  C CA  . THR A 117 ? 0.40050 0.47663 0.34002 0.15307  -0.06421 -0.01578 117 THR A CA  
895  C C   . THR A 117 ? 0.46020 0.53600 0.42734 0.13375  -0.05733 -0.02211 117 THR A C   
896  O O   . THR A 117 ? 0.38721 0.49713 0.37187 0.14011  -0.05994 -0.02909 117 THR A O   
897  C CB  . THR A 117 ? 0.46763 0.48498 0.37084 0.17513  -0.05848 0.00154  117 THR A CB  
898  O OG1 . THR A 117 ? 0.56836 0.58885 0.46860 0.19990  -0.05993 0.00345  117 THR A OG1 
899  C CG2 . THR A 117 ? 0.46263 0.47270 0.33104 0.19581  -0.06323 0.01028  117 THR A CG2 
900  N N   . TYR A 118 ? 0.41885 0.45804 0.38793 0.11209  -0.04813 -0.01945 118 TYR A N   
901  C CA  . TYR A 118 ? 0.34951 0.38542 0.33919 0.09504  -0.04148 -0.02414 118 TYR A CA  
902  C C   . TYR A 118 ? 0.39978 0.38796 0.37932 0.08873  -0.03291 -0.01556 118 TYR A C   
903  O O   . TYR A 118 ? 0.40103 0.36699 0.36691 0.08376  -0.02992 -0.01060 118 TYR A O   
904  C CB  . TYR A 118 ? 0.38068 0.43600 0.38644 0.07084  -0.03910 -0.03506 118 TYR A CB  
905  C CG  . TYR A 118 ? 0.38762 0.49437 0.40448 0.06848  -0.04572 -0.04784 118 TYR A CG  
906  C CD1 . TYR A 118 ? 0.39095 0.53531 0.42744 0.06650  -0.04585 -0.05699 118 TYR A CD1 
907  C CD2 . TYR A 118 ? 0.40224 0.52651 0.40991 0.06795  -0.05183 -0.05250 118 TYR A CD2 
908  C CE1 . TYR A 118 ? 0.38573 0.58873 0.43549 0.06168  -0.05151 -0.07191 118 TYR A CE1 
909  C CE2 . TYR A 118 ? 0.41347 0.59680 0.43301 0.06384  -0.05904 -0.06812 118 TYR A CE2 
910  C CZ  . TYR A 118 ? 0.40120 0.62581 0.44333 0.05959  -0.05855 -0.07838 118 TYR A CZ  
911  O OH  . TYR A 118 ? 0.45371 0.74629 0.51107 0.05177  -0.06458 -0.09689 118 TYR A OH  
912  N N   . LEU A 119 ? 0.35291 0.33175 0.34122 0.08573  -0.02833 -0.01613 119 LEU A N   
913  C CA  . LEU A 119 ? 0.38777 0.33390 0.37073 0.07600  -0.02085 -0.01220 119 LEU A CA  
914  C C   . LEU A 119 ? 0.37252 0.32808 0.37248 0.06066  -0.01738 -0.01721 119 LEU A C   
915  O O   . LEU A 119 ? 0.33606 0.31089 0.34889 0.05883  -0.01773 -0.02232 119 LEU A O   
916  C CB  . LEU A 119 ? 0.45766 0.38095 0.43012 0.08589  -0.01774 -0.00957 119 LEU A CB  
917  C CG  . LEU A 119 ? 0.52771 0.41212 0.48352 0.07895  -0.00955 -0.00644 119 LEU A CG  
918  C CD1 . LEU A 119 ? 0.50641 0.36354 0.43592 0.08286  -0.00659 0.00123  119 LEU A CD1 
919  C CD2 . LEU A 119 ? 0.52614 0.39340 0.47324 0.08975  -0.00698 -0.00775 119 LEU A CD2 
920  N N   . ALA A 120 ? 0.33700 0.28056 0.33455 0.05120  -0.01314 -0.01575 120 ALA A N   
921  C CA  . ALA A 120 ? 0.30063 0.24877 0.30704 0.04336  -0.00946 -0.01851 120 ALA A CA  
922  C C   . ALA A 120 ? 0.34601 0.28743 0.35237 0.04078  -0.00598 -0.01794 120 ALA A C   
923  O O   . ALA A 120 ? 0.28984 0.22224 0.28940 0.03752  -0.00386 -0.01670 120 ALA A O   
924  C CB  . ALA A 120 ? 0.36441 0.31280 0.36750 0.03830  -0.00757 -0.01970 120 ALA A CB  
925  N N   . LEU A 121 ? 0.27469 0.32595 0.34109 0.06963  0.04228  -0.03942 121 LEU A N   
926  C CA  . LEU A 121 ? 0.22825 0.25909 0.27949 0.06527  0.04355  -0.04164 121 LEU A CA  
927  C C   . LEU A 121 ? 0.27571 0.30014 0.32012 0.05069  0.04244  -0.03418 121 LEU A C   
928  O O   . LEU A 121 ? 0.29035 0.29531 0.32484 0.04700  0.03960  -0.03356 121 LEU A O   
929  C CB  . LEU A 121 ? 0.25473 0.29888 0.30185 0.06883  0.05129  -0.05029 121 LEU A CB  
930  C CG  . LEU A 121 ? 0.30589 0.33213 0.33586 0.06351  0.05186  -0.05308 121 LEU A CG  
931  C CD1 . LEU A 121 ? 0.28912 0.28596 0.31175 0.06808  0.04563  -0.05634 121 LEU A CD1 
932  C CD2 . LEU A 121 ? 0.28736 0.32987 0.31259 0.06883  0.06014  -0.06233 121 LEU A CD2 
933  N N   . ASN A 122 ? 0.22167 0.26296 0.27062 0.04218  0.04469  -0.02933 122 ASN A N   
934  C CA  . ASN A 122 ? 0.20729 0.23839 0.24812 0.03090  0.04251  -0.02258 122 ASN A CA  
935  C C   . ASN A 122 ? 0.22150 0.24788 0.26803 0.02925  0.03673  -0.01697 122 ASN A C   
936  O O   . ASN A 122 ? 0.23123 0.24076 0.27248 0.02836  0.03259  -0.01436 122 ASN A O   
937  C CB  . ASN A 122 ? 0.22373 0.26767 0.26060 0.02083  0.04758  -0.01990 122 ASN A CB  
938  C CG  . ASN A 122 ? 0.29292 0.33063 0.31442 0.01820  0.05107  -0.02164 122 ASN A CG  
939  O OD1 . ASN A 122 ? 0.29884 0.32295 0.31332 0.02324  0.04867  -0.02545 122 ASN A OD1 
940  N ND2 . ASN A 122 ? 0.28926 0.33499 0.30360 0.00869  0.05586  -0.01811 122 ASN A ND2 
941  N N   . GLU A 123 ? 0.22767 0.27114 0.28417 0.02748  0.03677  -0.01543 123 GLU A N   
942  C CA  . GLU A 123 ? 0.23393 0.27228 0.29268 0.02517  0.03081  -0.01061 123 GLU A CA  
943  C C   . GLU A 123 ? 0.25024 0.31141 0.32250 0.02592  0.02955  -0.01112 123 GLU A C   
944  O O   . GLU A 123 ? 0.21581 0.29959 0.29687 0.02568  0.03412  -0.01455 123 GLU A O   
945  C CB  . GLU A 123 ? 0.22973 0.25677 0.27830 0.01452  0.02963  -0.00599 123 GLU A CB  
946  C CG  . GLU A 123 ? 0.24022 0.27910 0.28832 0.00340  0.03279  -0.00447 123 GLU A CG  
947  C CD  . GLU A 123 ? 0.26196 0.30529 0.30355 0.00002  0.03969  -0.00590 123 GLU A CD  
948  O OE1 . GLU A 123 ? 0.26098 0.28695 0.29014 0.00127  0.03909  -0.00521 123 GLU A OE1 
949  O OE2 . GLU A 123 ? 0.27022 0.33580 0.31957 -0.00276 0.04512  -0.00812 123 GLU A OE2 
950  N N   . SER A 124 ? 0.22175 0.27917 0.29526 0.02575  0.02326  -0.00781 124 SER A N   
951  C CA  . SER A 124 ? 0.22219 0.30175 0.30743 0.02392  0.02001  -0.00802 124 SER A CA  
952  C C   . SER A 124 ? 0.24213 0.31166 0.31927 0.01249  0.01641  -0.00418 124 SER A C   
953  O O   . SER A 124 ? 0.25878 0.30677 0.32503 0.01385  0.01360  -0.00149 124 SER A O   
954  C CB  . SER A 124 ? 0.27803 0.36066 0.36982 0.03778  0.01349  -0.00836 124 SER A CB  
955  O OG  . SER A 124 ? 0.27483 0.38052 0.37787 0.03643  0.00852  -0.00878 124 SER A OG  
956  N N   . THR A 125 ? 0.23690 0.32136 0.31844 0.00085  0.01680  -0.00445 125 THR A N   
957  C CA  . THR A 125 ? 0.19593 0.26690 0.26749 -0.00962 0.01242  -0.00202 125 THR A CA  
958  C C   . THR A 125 ? 0.22494 0.31701 0.30726 -0.01375 0.00642  -0.00366 125 THR A C   
959  O O   . THR A 125 ? 0.22187 0.34402 0.32126 -0.01198 0.00689  -0.00652 125 THR A O   
960  C CB  . THR A 125 ? 0.25624 0.31587 0.31662 -0.02352 0.01670  -0.00026 125 THR A CB  
961  O OG1 . THR A 125 ? 0.29561 0.37898 0.36551 -0.03510 0.02038  -0.00135 125 THR A OG1 
962  C CG2 . THR A 125 ? 0.27030 0.31503 0.32154 -0.01856 0.02198  0.00079  125 THR A CG2 
963  N N   . VAL A 126 ? 0.24025 0.31816 0.31242 -0.01935 0.00040  -0.00273 126 VAL A N   
964  C CA  . VAL A 126 ? 0.24113 0.33713 0.32081 -0.02534 -0.00679 -0.00494 126 VAL A CA  
965  C C   . VAL A 126 ? 0.22663 0.30520 0.29253 -0.04149 -0.00905 -0.00523 126 VAL A C   
966  O O   . VAL A 126 ? 0.25778 0.30577 0.30557 -0.04054 -0.00884 -0.00375 126 VAL A O   
967  C CB  . VAL A 126 ? 0.22415 0.31877 0.30247 -0.01227 -0.01455 -0.00441 126 VAL A CB  
968  C CG1 . VAL A 126 ? 0.31781 0.38033 0.37633 -0.00894 -0.01486 -0.00191 126 VAL A CG1 
969  C CG2 . VAL A 126 ? 0.25086 0.36664 0.33639 -0.01767 -0.02396 -0.00729 126 VAL A CG2 
970  N N   . LYS A 127 ? 0.22882 0.32669 0.30319 -0.05627 -0.01093 -0.00756 127 LYS A N   
971  C CA  . LYS A 127 ? 0.29526 0.37696 0.35673 -0.07371 -0.01500 -0.00885 127 LYS A CA  
972  C C   . LYS A 127 ? 0.30244 0.41264 0.37708 -0.08204 -0.02339 -0.01330 127 LYS A C   
973  O O   . LYS A 127 ? 0.26642 0.41227 0.36205 -0.07436 -0.02516 -0.01494 127 LYS A O   
974  C CB  . LYS A 127 ? 0.36979 0.44181 0.42477 -0.08969 -0.00757 -0.00632 127 LYS A CB  
975  C CG  . LYS A 127 ? 0.37161 0.41924 0.41413 -0.08061 -0.00045 -0.00213 127 LYS A CG  
976  C CD  . LYS A 127 ? 0.36406 0.40216 0.39734 -0.09691 0.00625  0.00148  127 LYS A CD  
977  C CE  . LYS A 127 ? 0.49742 0.49320 0.50430 -0.10780 0.00199  0.00307  127 LYS A CE  
978  N NZ  . LYS A 127 ? 0.50290 0.47476 0.49214 -0.11399 0.00818  0.00899  127 LYS A NZ  
979  N N   . SER A 128 ? 0.32606 0.42079 0.38811 -0.09741 -0.02944 -0.01595 128 SER A N   
980  C CA  . SER A 128 ? 0.32052 0.44435 0.39535 -0.10788 -0.03835 -0.02104 128 SER A CA  
981  C C   . SER A 128 ? 0.38294 0.54209 0.47837 -0.12581 -0.03348 -0.02183 128 SER A C   
982  O O   . SER A 128 ? 0.43342 0.58663 0.52697 -0.13340 -0.02325 -0.01808 128 SER A O   
983  C CB  . SER A 128 ? 0.43586 0.53181 0.48979 -0.12056 -0.04696 -0.02509 128 SER A CB  
984  O OG  . SER A 128 ? 0.53711 0.62251 0.58542 -0.14449 -0.04381 -0.02504 128 SER A OG  
985  N N   . SER A 129 ? 0.39360 0.59243 0.50878 -0.13305 -0.04084 -0.02684 129 SER A N   
986  C CA  . SER A 129 ? 0.42396 0.66246 0.56122 -0.15084 -0.03494 -0.02807 129 SER A CA  
987  C C   . SER A 129 ? 0.55422 0.77463 0.67810 -0.18175 -0.03665 -0.02923 129 SER A C   
988  O O   . SER A 129 ? 0.58809 0.84512 0.73012 -0.20248 -0.03756 -0.03268 129 SER A O   
989  C CB  . SER A 129 ? 0.42597 0.72267 0.59472 -0.14450 -0.04162 -0.03349 129 SER A CB  
990  O OG  . SER A 129 ? 0.48988 0.78762 0.65461 -0.15397 -0.05555 -0.03856 129 SER A OG  
991  N N   . GLY A 130 ? 0.58508 0.74910 0.67710 -0.18496 -0.03741 -0.02676 130 GLY A N   
992  C CA  . GLY A 130 ? 0.61970 0.75519 0.69260 -0.21026 -0.04306 -0.02923 130 GLY A CA  
993  C C   . GLY A 130 ? 0.68339 0.80316 0.74400 -0.20427 -0.05706 -0.03581 130 GLY A C   
994  O O   . GLY A 130 ? 0.68871 0.84295 0.76649 -0.19219 -0.06471 -0.03985 130 GLY A O   
995  N N   . GLY A 131 ? 0.68636 0.75326 0.71535 -0.21173 -0.06098 -0.03723 131 GLY A N   
996  C CA  . GLY A 131 ? 0.58252 0.62838 0.59443 -0.20229 -0.07243 -0.04372 131 GLY A CA  
997  C C   . GLY A 131 ? 0.51649 0.53680 0.51480 -0.17363 -0.06855 -0.04033 131 GLY A C   
998  O O   . GLY A 131 ? 0.51234 0.53677 0.51825 -0.16124 -0.05853 -0.03357 131 GLY A O   
999  N N   . PRO A 132 ? 0.53885 0.53305 0.51614 -0.16346 -0.07606 -0.04547 132 PRO A N   
1000 C CA  . PRO A 132 ? 0.54107 0.50975 0.50393 -0.13929 -0.07109 -0.04250 132 PRO A CA  
1001 C C   . PRO A 132 ? 0.47455 0.47689 0.45820 -0.11894 -0.06706 -0.03744 132 PRO A C   
1002 O O   . PRO A 132 ? 0.49537 0.53516 0.49746 -0.11693 -0.07260 -0.03862 132 PRO A O   
1003 C CB  . PRO A 132 ? 0.48521 0.42615 0.42235 -0.13534 -0.08028 -0.05075 132 PRO A CB  
1004 C CG  . PRO A 132 ? 0.51672 0.47722 0.45916 -0.15285 -0.09133 -0.05760 132 PRO A CG  
1005 C CD  . PRO A 132 ? 0.55766 0.54246 0.52117 -0.17529 -0.08874 -0.05488 132 PRO A CD  
1006 N N   . PHE A 133 ? 0.39548 0.38215 0.37449 -0.10337 -0.05831 -0.03208 133 PHE A N   
1007 C CA  . PHE A 133 ? 0.35472 0.36179 0.34732 -0.08400 -0.05400 -0.02718 133 PHE A CA  
1008 C C   . PHE A 133 ? 0.40880 0.39914 0.38411 -0.06854 -0.05669 -0.02866 133 PHE A C   
1009 O O   . PHE A 133 ? 0.37526 0.33479 0.33209 -0.06356 -0.05318 -0.02950 133 PHE A O   
1010 C CB  . PHE A 133 ? 0.34981 0.35008 0.34690 -0.07854 -0.04283 -0.02102 133 PHE A CB  
1011 C CG  . PHE A 133 ? 0.33606 0.35203 0.34501 -0.06041 -0.03832 -0.01654 133 PHE A CG  
1012 C CD1 . PHE A 133 ? 0.31864 0.36985 0.34995 -0.05694 -0.03897 -0.01524 133 PHE A CD1 
1013 C CD2 . PHE A 133 ? 0.36479 0.35991 0.36210 -0.04665 -0.03378 -0.01416 133 PHE A CD2 
1014 C CE1 . PHE A 133 ? 0.31063 0.36926 0.34939 -0.04037 -0.03524 -0.01129 133 PHE A CE1 
1015 C CE2 . PHE A 133 ? 0.29408 0.29995 0.30063 -0.03251 -0.02955 -0.00987 133 PHE A CE2 
1016 C CZ  . PHE A 133 ? 0.29688 0.33176 0.32271 -0.02947 -0.03071 -0.00838 133 PHE A CZ  
1017 N N   . VAL A 134 ? 0.32677 0.33844 0.30745 -0.06036 -0.06280 -0.02882 134 VAL A N   
1018 C CA  . VAL A 134 ? 0.37706 0.37614 0.34066 -0.04615 -0.06400 -0.02874 134 VAL A CA  
1019 C C   . VAL A 134 ? 0.37388 0.39593 0.35018 -0.03263 -0.06401 -0.02239 134 VAL A C   
1020 O O   . VAL A 134 ? 0.39127 0.44028 0.38110 -0.03363 -0.07155 -0.02258 134 VAL A O   
1021 C CB  . VAL A 134 ? 0.41012 0.40236 0.35584 -0.05155 -0.07450 -0.03641 134 VAL A CB  
1022 C CG1 . VAL A 134 ? 0.40763 0.38532 0.33188 -0.03711 -0.07345 -0.03642 134 VAL A CG1 
1023 C CG2 . VAL A 134 ? 0.48284 0.45215 0.41715 -0.06801 -0.07684 -0.04353 134 VAL A CG2 
1024 N N   . VAL A 135 ? 0.33027 0.34169 0.30184 -0.02008 -0.05644 -0.01704 135 VAL A N   
1025 C CA  . VAL A 135 ? 0.32650 0.35172 0.30484 -0.00761 -0.05704 -0.01052 135 VAL A CA  
1026 C C   . VAL A 135 ? 0.34310 0.35067 0.30190 0.00173  -0.05325 -0.00725 135 VAL A C   
1027 O O   . VAL A 135 ? 0.33739 0.32682 0.28580 0.00143  -0.04622 -0.00897 135 VAL A O   
1028 C CB  . VAL A 135 ? 0.30529 0.34051 0.30331 -0.00293 -0.05021 -0.00565 135 VAL A CB  
1029 C CG1 . VAL A 135 ? 0.33100 0.39166 0.35050 -0.01056 -0.05304 -0.00834 135 VAL A CG1 
1030 C CG2 . VAL A 135 ? 0.32859 0.34390 0.32240 -0.00312 -0.03951 -0.00453 135 VAL A CG2 
1031 N N   . ASP A 136 ? 0.36081 0.37474 0.31439 0.01043  -0.05784 -0.00214 136 ASP A N   
1032 C CA  . ASP A 136 ? 0.33956 0.33915 0.27653 0.01808  -0.05220 0.00346  136 ASP A CA  
1033 C C   . ASP A 136 ? 0.33569 0.33320 0.28452 0.02358  -0.04448 0.01035  136 ASP A C   
1034 O O   . ASP A 136 ? 0.33875 0.34780 0.30295 0.02768  -0.04768 0.01315  136 ASP A O   
1035 C CB  . ASP A 136 ? 0.36995 0.37222 0.29078 0.02391  -0.06055 0.00729  136 ASP A CB  
1036 C CG  . ASP A 136 ? 0.39370 0.39193 0.29439 0.01932  -0.06611 0.00009  136 ASP A CG  
1037 O OD1 . ASP A 136 ? 0.44094 0.42594 0.33217 0.01557  -0.05948 -0.00564 136 ASP A OD1 
1038 O OD2 . ASP A 136 ? 0.44201 0.45004 0.33524 0.02063  -0.07780 -0.00044 136 ASP A OD2 
1039 N N   . VAL A 137 ? 0.32974 0.31400 0.27204 0.02383  -0.03465 0.01188  137 VAL A N   
1040 C CA  . VAL A 137 ? 0.31666 0.29677 0.26835 0.02686  -0.02721 0.01714  137 VAL A CA  
1041 C C   . VAL A 137 ? 0.37610 0.34698 0.31260 0.03120  -0.02543 0.02520  137 VAL A C   
1042 O O   . VAL A 137 ? 0.37101 0.33601 0.29114 0.02942  -0.02120 0.02529  137 VAL A O   
1043 C CB  . VAL A 137 ? 0.33932 0.31322 0.29454 0.02312  -0.01823 0.01342  137 VAL A CB  
1044 C CG1 . VAL A 137 ? 0.32825 0.29892 0.29243 0.02494  -0.01164 0.01778  137 VAL A CG1 
1045 C CG2 . VAL A 137 ? 0.32607 0.30310 0.29014 0.01745  -0.02015 0.00649  137 VAL A CG2 
1046 N N   . VAL A 138 ? 0.34099 0.30958 0.28138 0.03692  -0.02827 0.03183  138 VAL A N   
1047 C CA  . VAL A 138 ? 0.33133 0.28655 0.25380 0.04057  -0.02869 0.04130  138 VAL A CA  
1048 C C   . VAL A 138 ? 0.44410 0.38778 0.37317 0.04060  -0.02202 0.04556  138 VAL A C   
1049 O O   . VAL A 138 ? 0.40656 0.35349 0.35219 0.04467  -0.02373 0.04357  138 VAL A O   
1050 C CB  . VAL A 138 ? 0.36935 0.32689 0.28593 0.04917  -0.04095 0.04568  138 VAL A CB  
1051 C CG1 . VAL A 138 ? 0.42259 0.36040 0.31563 0.05252  -0.04149 0.05710  138 VAL A CG1 
1052 C CG2 . VAL A 138 ? 0.37358 0.34463 0.28428 0.04733  -0.04872 0.03977  138 VAL A CG2 
1053 N N   . ILE A 139 ? 0.36513 0.29718 0.28192 0.03511  -0.01393 0.05031  139 ILE A N   
1054 C CA  . ILE A 139 ? 0.34045 0.26103 0.26275 0.03216  -0.00758 0.05334  139 ILE A CA  
1055 C C   . ILE A 139 ? 0.46044 0.35964 0.36231 0.03221  -0.00852 0.06468  139 ILE A C   
1056 O O   . ILE A 139 ? 0.40533 0.30075 0.28859 0.02638  -0.00441 0.06975  139 ILE A O   
1057 C CB  . ILE A 139 ? 0.35426 0.28105 0.28157 0.02326  0.00305  0.04906  139 ILE A CB  
1058 C CG1 . ILE A 139 ? 0.34307 0.28536 0.28679 0.02374  0.00347  0.03881  139 ILE A CG1 
1059 C CG2 . ILE A 139 ? 0.40657 0.32205 0.33910 0.01862  0.00827  0.05189  139 ILE A CG2 
1060 C CD1 . ILE A 139 ? 0.34665 0.29659 0.29226 0.01832  0.01216  0.03411  139 ILE A CD1 
1061 N N   . ASN A 140 ? 0.39814 0.28182 0.30141 0.03882  -0.01350 0.06869  140 ASN A N   
1062 C CA  . ASN A 140 ? 0.41251 0.26901 0.29273 0.03981  -0.01607 0.08051  140 ASN A CA  
1063 C C   . ASN A 140 ? 0.47587 0.33225 0.33433 0.04273  -0.02184 0.08680  140 ASN A C   
1064 O O   . ASN A 140 ? 0.48760 0.32799 0.32156 0.03591  -0.01825 0.09644  140 ASN A O   
1065 C CB  . ASN A 140 ? 0.42545 0.26707 0.29717 0.02554  -0.00528 0.08524  140 ASN A CB  
1066 C CG  . ASN A 140 ? 0.49293 0.33246 0.38332 0.02307  -0.00156 0.07904  140 ASN A CG  
1067 O OD1 . ASN A 140 ? 0.46982 0.30454 0.36992 0.03384  -0.00794 0.07575  140 ASN A OD1 
1068 N ND2 . ASN A 140 ? 0.47077 0.31732 0.36714 0.00988  0.00846  0.07631  140 ASN A ND2 
1069 N N   . ASP A 141 ? 0.47061 0.34643 0.33732 0.05133  -0.03049 0.08099  141 ASP A N   
1070 C CA  . ASP A 141 ? 0.47290 0.35148 0.31935 0.05540  -0.03856 0.08518  141 ASP A CA  
1071 C C   . ASP A 141 ? 0.50921 0.39717 0.34296 0.04522  -0.03107 0.08304  141 ASP A C   
1072 O O   . ASP A 141 ? 0.59450 0.48260 0.40688 0.04728  -0.03659 0.08657  141 ASP A O   
1073 C CB  . ASP A 141 ? 0.49971 0.34993 0.31935 0.06118  -0.04477 0.09902  141 ASP A CB  
1074 C CG  . ASP A 141 ? 0.60125 0.44129 0.43003 0.07614  -0.05494 0.10044  141 ASP A CG  
1075 O OD1 . ASP A 141 ? 0.56669 0.42959 0.42132 0.08406  -0.05999 0.09067  141 ASP A OD1 
1076 O OD2 . ASP A 141 ? 0.70034 0.50866 0.50909 0.08010  -0.05777 0.11138  141 ASP A OD2 
1077 N N   . ILE A 142 ? 0.46632 0.36259 0.31072 0.03566  -0.01925 0.07702  142 ILE A N   
1078 C CA  A ILE A 142 ? 0.49648 0.40385 0.33126 0.02829  -0.01115 0.07285  142 ILE A CA  
1079 C CA  B ILE A 142 ? 0.49771 0.40506 0.33078 0.02928  -0.01267 0.07308  142 ILE A CA  
1080 C C   . ILE A 142 ? 0.42023 0.34723 0.27225 0.03041  -0.01382 0.05947  142 ILE A C   
1081 O O   . ILE A 142 ? 0.38942 0.32240 0.26442 0.02990  -0.01161 0.05339  142 ILE A O   
1082 C CB  A ILE A 142 ? 0.49376 0.39912 0.33085 0.01752  0.00312  0.07445  142 ILE A CB  
1083 C CB  B ILE A 142 ? 0.53707 0.44053 0.36191 0.01806  0.00166  0.07708  142 ILE A CB  
1084 C CG1 A ILE A 142 ? 0.51489 0.40124 0.32551 0.01086  0.00737  0.08818  142 ILE A CG1 
1085 C CG1 B ILE A 142 ? 0.50417 0.42515 0.32280 0.01453  0.00906  0.06926  142 ILE A CG1 
1086 C CG2 A ILE A 142 ? 0.43876 0.36443 0.28404 0.01367  0.01172  0.06363  142 ILE A CG2 
1087 C CG2 B ILE A 142 ? 0.46627 0.36915 0.31260 0.01338  0.00814  0.07478  142 ILE A CG2 
1088 C CD1 A ILE A 142 ? 0.57910 0.45677 0.36170 0.01644  -0.00121 0.09550  142 ILE A CD1 
1089 C CD1 B ILE A 142 ? 0.47062 0.40736 0.31369 0.01345  0.01498  0.05738  142 ILE A CD1 
1090 N N   . HIS A 143 ? 0.40198 0.33667 0.24150 0.03215  -0.01899 0.05488  143 HIS A N   
1091 C CA  A HIS A 143 ? 0.41609 0.36405 0.26870 0.03216  -0.02181 0.04222  143 HIS A CA  
1092 C CA  B HIS A 143 ? 0.41609 0.36394 0.26865 0.03217  -0.02180 0.04235  143 HIS A CA  
1093 C C   . HIS A 143 ? 0.44097 0.39290 0.30020 0.02748  -0.00988 0.03544  143 HIS A C   
1094 O O   . HIS A 143 ? 0.43126 0.38422 0.27498 0.02517  -0.00189 0.03510  143 HIS A O   
1095 C CB  A HIS A 143 ? 0.43023 0.38285 0.26525 0.03381  -0.03039 0.03745  143 HIS A CB  
1096 C CB  B HIS A 143 ? 0.43063 0.38244 0.26465 0.03422  -0.03088 0.03878  143 HIS A CB  
1097 C CG  A HIS A 143 ? 0.46029 0.42070 0.30517 0.03145  -0.03244 0.02422  143 HIS A CG  
1098 C CG  B HIS A 143 ? 0.43746 0.39145 0.27195 0.04031  -0.04509 0.04307  143 HIS A CG  
1099 N ND1 A HIS A 143 ? 0.43518 0.39470 0.27703 0.02906  -0.02348 0.01631  143 HIS A ND1 
1100 N ND1 B HIS A 143 ? 0.55367 0.51987 0.39207 0.04128  -0.05682 0.03539  143 HIS A ND1 
1101 C CD2 A HIS A 143 ? 0.48468 0.45272 0.34322 0.03062  -0.04216 0.01774  143 HIS A CD2 
1102 C CD2 B HIS A 143 ? 0.47056 0.41685 0.30363 0.04645  -0.05014 0.05363  143 HIS A CD2 
1103 C CE1 A HIS A 143 ? 0.41335 0.37421 0.26285 0.02730  -0.02840 0.00609  143 HIS A CE1 
1104 C CE1 B HIS A 143 ? 0.48019 0.45082 0.32113 0.04840  -0.06848 0.04089  143 HIS A CE1 
1105 N NE2 A HIS A 143 ? 0.40123 0.36778 0.26102 0.02652  -0.03928 0.00696  143 HIS A NE2 
1106 N NE2 B HIS A 143 ? 0.45430 0.41145 0.29147 0.05299  -0.06486 0.05197  143 HIS A NE2 
1107 N N   . PHE A 144 ? 0.37148 0.32720 0.25330 0.02685  -0.00861 0.03001  144 PHE A N   
1108 C CA  . PHE A 144 ? 0.33847 0.29778 0.22827 0.02442  0.00135  0.02450  144 PHE A CA  
1109 C C   . PHE A 144 ? 0.35325 0.31519 0.24350 0.02571  -0.00024 0.01304  144 PHE A C   
1110 O O   . PHE A 144 ? 0.34350 0.30801 0.22666 0.02700  0.00654  0.00754  144 PHE A O   
1111 C CB  . PHE A 144 ? 0.30820 0.26690 0.21896 0.02313  0.00400  0.02642  144 PHE A CB  
1112 C CG  . PHE A 144 ? 0.31467 0.27885 0.23473 0.02155  0.01250  0.02112  144 PHE A CG  
1113 C CD1 . PHE A 144 ? 0.32921 0.29787 0.24530 0.01812  0.02191  0.02403  144 PHE A CD1 
1114 C CD2 . PHE A 144 ? 0.31096 0.27657 0.24328 0.02304  0.01067  0.01391  144 PHE A CD2 
1115 C CE1 . PHE A 144 ? 0.34101 0.31976 0.26726 0.01802  0.02879  0.01828  144 PHE A CE1 
1116 C CE2 . PHE A 144 ? 0.31659 0.28714 0.25677 0.02374  0.01705  0.00923  144 PHE A CE2 
1117 C CZ  . PHE A 144 ? 0.35342 0.33234 0.29195 0.02215  0.02551  0.01080  144 PHE A CZ  
1118 N N   . GLU A 145 ? 0.33661 0.29779 0.23475 0.02532  -0.00897 0.00897  145 GLU A N   
1119 C CA  . GLU A 145 ? 0.35931 0.31677 0.25399 0.02480  -0.01152 -0.00141 145 GLU A CA  
1120 C C   . GLU A 145 ? 0.32929 0.28798 0.22859 0.02108  -0.02259 -0.00368 145 GLU A C   
1121 O O   . GLU A 145 ? 0.37802 0.34410 0.28892 0.02068  -0.02685 0.00204  145 GLU A O   
1122 C CB  . GLU A 145 ? 0.29888 0.25351 0.20628 0.02527  -0.00576 -0.00544 145 GLU A CB  
1123 C CG  . GLU A 145 ? 0.33063 0.28742 0.25794 0.02192  -0.00818 -0.00190 145 GLU A CG  
1124 C CD  . GLU A 145 ? 0.37232 0.32639 0.31016 0.02256  -0.00291 -0.00393 145 GLU A CD  
1125 O OE1 . GLU A 145 ? 0.34988 0.30170 0.28196 0.02661  0.00190  -0.00800 145 GLU A OE1 
1126 O OE2 . GLU A 145 ? 0.35886 0.31468 0.31061 0.01979  -0.00390 -0.00167 145 GLU A OE2 
1127 N N   . ARG A 146 ? 0.35385 0.30595 0.24332 0.01846  -0.02753 -0.01263 146 ARG A N   
1128 C CA  . ARG A 146 ? 0.36289 0.31696 0.25952 0.01130  -0.03712 -0.01638 146 ARG A CA  
1129 C C   . ARG A 146 ? 0.37631 0.32005 0.28117 0.00711  -0.03415 -0.02075 146 ARG A C   
1130 O O   . ARG A 146 ? 0.40255 0.33113 0.29519 0.00960  -0.03113 -0.02698 146 ARG A O   
1131 C CB  . ARG A 146 ? 0.45435 0.40517 0.33239 0.00844  -0.04624 -0.02347 146 ARG A CB  
1132 C CG  . ARG A 146 ? 0.41252 0.36688 0.29935 -0.00213 -0.05595 -0.02829 146 ARG A CG  
1133 C CD  . ARG A 146 ? 0.42400 0.38090 0.29470 -0.00574 -0.06750 -0.03434 146 ARG A CD  
1134 N NE  . ARG A 146 ? 0.43926 0.41294 0.31002 0.00047  -0.07182 -0.02689 146 ARG A NE  
1135 C CZ  . ARG A 146 ? 0.50359 0.48333 0.35996 -0.00016 -0.08262 -0.02988 146 ARG A CZ  
1136 N NH1 . ARG A 146 ? 0.51810 0.48882 0.35970 -0.00762 -0.08953 -0.04098 146 ARG A NH1 
1137 N NH2 . ARG A 146 ? 0.52221 0.51560 0.37776 0.00687  -0.08767 -0.02176 146 ARG A NH2 
1138 N N   . PHE A 147 ? 0.33737 0.28914 0.26154 0.00218  -0.03468 -0.01722 147 PHE A N   
1139 C CA  . PHE A 147 ? 0.35250 0.29482 0.28372 -0.00240 -0.03142 -0.01887 147 PHE A CA  
1140 C C   . PHE A 147 ? 0.36875 0.30646 0.29866 -0.01475 -0.03880 -0.02402 147 PHE A C   
1141 O O   . PHE A 147 ? 0.36935 0.32445 0.30927 -0.02098 -0.04472 -0.02326 147 PHE A O   
1142 C CB  . PHE A 147 ? 0.34372 0.29797 0.29483 -0.00171 -0.02653 -0.01224 147 PHE A CB  
1143 C CG  . PHE A 147 ? 0.31902 0.26276 0.27396 -0.00633 -0.02302 -0.01313 147 PHE A CG  
1144 C CD1 . PHE A 147 ? 0.34449 0.29030 0.30571 -0.01792 -0.02614 -0.01407 147 PHE A CD1 
1145 C CD2 . PHE A 147 ? 0.34485 0.27717 0.29530 0.00032  -0.01709 -0.01308 147 PHE A CD2 
1146 C CE1 . PHE A 147 ? 0.34431 0.27695 0.30430 -0.02298 -0.02289 -0.01360 147 PHE A CE1 
1147 C CE2 . PHE A 147 ? 0.30803 0.22833 0.25875 -0.00276 -0.01511 -0.01311 147 PHE A CE2 
1148 C CZ  . PHE A 147 ? 0.32132 0.23985 0.27491 -0.01441 -0.01795 -0.01287 147 PHE A CZ  
1149 N N   . ARG A 148 ? 0.33647 0.25035 0.25295 -0.01814 -0.03905 -0.02961 148 ARG A N   
1150 C CA  A ARG A 148 ? 0.38076 0.28338 0.29312 -0.03265 -0.04521 -0.03401 148 ARG A CA  
1151 C CA  B ARG A 148 ? 0.38068 0.28349 0.29317 -0.03266 -0.04521 -0.03397 148 ARG A CA  
1152 C C   . ARG A 148 ? 0.38132 0.26559 0.29314 -0.03528 -0.04036 -0.03194 148 ARG A C   
1153 O O   . ARG A 148 ? 0.42141 0.28757 0.32234 -0.02487 -0.03657 -0.03323 148 ARG A O   
1154 C CB  A ARG A 148 ? 0.43692 0.31786 0.32551 -0.03489 -0.05211 -0.04354 148 ARG A CB  
1155 C CB  B ARG A 148 ? 0.43662 0.31861 0.32554 -0.03479 -0.05221 -0.04347 148 ARG A CB  
1156 C CG  A ARG A 148 ? 0.47231 0.36948 0.35836 -0.03733 -0.05996 -0.04668 148 ARG A CG  
1157 C CG  B ARG A 148 ? 0.47118 0.36738 0.35402 -0.02846 -0.05606 -0.04553 148 ARG A CG  
1158 C CD  A ARG A 148 ? 0.53583 0.40809 0.39500 -0.03912 -0.06655 -0.05768 148 ARG A CD  
1159 C CD  B ARG A 148 ? 0.53755 0.41077 0.39333 -0.02829 -0.06189 -0.05644 148 ARG A CD  
1160 N NE  A ARG A 148 ? 0.55706 0.44351 0.40781 -0.03556 -0.07255 -0.06066 148 ARG A NE  
1161 N NE  B ARG A 148 ? 0.55048 0.43868 0.39962 -0.02943 -0.06972 -0.05932 148 ARG A NE  
1162 C CZ  A ARG A 148 ? 0.52769 0.42114 0.37113 -0.02136 -0.06786 -0.05847 148 ARG A CZ  
1163 C CZ  B ARG A 148 ? 0.57685 0.46713 0.42283 -0.04295 -0.08075 -0.06506 148 ARG A CZ  
1164 N NH1 A ARG A 148 ? 0.50563 0.39837 0.35347 -0.01001 -0.05701 -0.05332 148 ARG A NH1 
1165 N NH1 B ARG A 148 ? 0.56546 0.44451 0.41530 -0.05870 -0.08446 -0.06793 148 ARG A NH1 
1166 N NH2 A ARG A 148 ? 0.57842 0.47975 0.40823 -0.01957 -0.07436 -0.06172 148 ARG A NH2 
1167 N NH2 B ARG A 148 ? 0.51374 0.41813 0.35169 -0.04177 -0.08857 -0.06770 148 ARG A NH2 
1168 N N   . GLY A 149 ? 0.36710 0.25783 0.29014 -0.04867 -0.04048 -0.02871 149 GLY A N   
1169 C CA  . GLY A 149 ? 0.35075 0.22296 0.27030 -0.05086 -0.03563 -0.02521 149 GLY A CA  
1170 C C   . GLY A 149 ? 0.35574 0.24708 0.29236 -0.06464 -0.03318 -0.02009 149 GLY A C   
1171 O O   . GLY A 149 ? 0.38522 0.29755 0.33275 -0.07597 -0.03709 -0.02149 149 GLY A O   
1172 N N   . ASP A 150 ? 0.32639 0.21303 0.26532 -0.06304 -0.02671 -0.01467 150 ASP A N   
1173 C CA  . ASP A 150 ? 0.37355 0.27778 0.32580 -0.07713 -0.02307 -0.01031 150 ASP A CA  
1174 C C   . ASP A 150 ? 0.35517 0.29853 0.33273 -0.07073 -0.01885 -0.00791 150 ASP A C   
1175 O O   . ASP A 150 ? 0.37642 0.34516 0.36946 -0.08160 -0.01700 -0.00684 150 ASP A O   
1176 C CB  . ASP A 150 ? 0.33285 0.21493 0.27378 -0.07945 -0.01806 -0.00516 150 ASP A CB  
1177 C CG  . ASP A 150 ? 0.38162 0.22462 0.29771 -0.09106 -0.02262 -0.00614 150 ASP A CG  
1178 O OD1 . ASP A 150 ? 0.43554 0.27118 0.34525 -0.09857 -0.02928 -0.01177 150 ASP A OD1 
1179 O OD2 . ASP A 150 ? 0.43740 0.25611 0.33905 -0.09322 -0.02014 -0.00120 150 ASP A OD2 
1180 N N   . GLY A 151 ? 0.30254 0.25060 0.28408 -0.05386 -0.01666 -0.00704 151 GLY A N   
1181 C CA  . GLY A 151 ? 0.27274 0.24989 0.27424 -0.04630 -0.01312 -0.00481 151 GLY A CA  
1182 C C   . GLY A 151 ? 0.27855 0.25013 0.27880 -0.03057 -0.00954 -0.00294 151 GLY A C   
1183 O O   . GLY A 151 ? 0.28734 0.23814 0.27389 -0.02473 -0.00956 -0.00370 151 GLY A O   
1184 N N   . LEU A 152 ? 0.27145 0.26292 0.28668 -0.02379 -0.00651 -0.00107 152 LEU A N   
1185 C CA  . LEU A 152 ? 0.23817 0.22650 0.25409 -0.01134 -0.00324 0.00079  152 LEU A CA  
1186 C C   . LEU A 152 ? 0.25676 0.25641 0.28380 -0.00912 0.00230  0.00214  152 LEU A C   
1187 O O   . LEU A 152 ? 0.26058 0.27904 0.29916 -0.01308 0.00311  0.00142  152 LEU A O   
1188 C CB  . LEU A 152 ? 0.25727 0.25335 0.27592 -0.00348 -0.00690 0.00139  152 LEU A CB  
1189 C CG  . LEU A 152 ? 0.28223 0.26575 0.28626 -0.00351 -0.01117 -0.00039 152 LEU A CG  
1190 C CD1 . LEU A 152 ? 0.28883 0.28084 0.29255 0.00240  -0.01580 0.00105  152 LEU A CD1 
1191 C CD2 . LEU A 152 ? 0.30380 0.27070 0.29691 0.00161  -0.00727 -0.00052 152 LEU A CD2 
1192 N N   . CYS A 153 ? 0.22338 0.21378 0.24723 -0.00274 0.00604  0.00317  153 CYS A N   
1193 C CA  . CYS A 153 ? 0.27938 0.27705 0.31032 -0.00007 0.01097  0.00322  153 CYS A CA  
1194 C C   . CYS A 153 ? 0.24134 0.23613 0.27435 0.00937  0.01158  0.00361  153 CYS A C   
1195 O O   . CYS A 153 ? 0.23391 0.21714 0.25965 0.01162  0.01110  0.00439  153 CYS A O   
1196 C CB  . CYS A 153 ? 0.25546 0.24108 0.27681 -0.00404 0.01399  0.00383  153 CYS A CB  
1197 S SG  . CYS A 153 ? 0.27857 0.27161 0.30448 -0.00057 0.01982  0.00282  153 CYS A SG  
1198 N N   . MET A 154 ? 0.22875 0.23379 0.27113 0.01486  0.01247  0.00280  154 MET A N   
1199 C CA  . MET A 154 ? 0.23078 0.22756 0.27241 0.02217  0.01293  0.00334  154 MET A CA  
1200 C C   . MET A 154 ? 0.23343 0.23121 0.27762 0.02416  0.01726  0.00026  154 MET A C   
1201 O O   . MET A 154 ? 0.24628 0.25696 0.29819 0.02707  0.01880  -0.00232 154 MET A O   
1202 C CB  . MET A 154 ? 0.23376 0.23401 0.27942 0.02933  0.00901  0.00474  154 MET A CB  
1203 C CG  . MET A 154 ? 0.27282 0.25714 0.31295 0.03464  0.00899  0.00677  154 MET A CG  
1204 S SD  . MET A 154 ? 0.28060 0.25096 0.30886 0.02945  0.00939  0.01077  154 MET A SD  
1205 C CE  . MET A 154 ? 0.29170 0.26060 0.31373 0.03344  0.00349  0.01587  154 MET A CE  
1206 N N   . SER A 155 ? 0.23229 0.21844 0.27048 0.02359  0.01881  -0.00016 155 SER A N   
1207 C CA  . SER A 155 ? 0.24062 0.22612 0.27781 0.02422  0.02212  -0.00383 155 SER A CA  
1208 C C   . SER A 155 ? 0.29162 0.26693 0.32815 0.02893  0.02186  -0.00593 155 SER A C   
1209 O O   . SER A 155 ? 0.28867 0.25390 0.32254 0.02824  0.01993  -0.00339 155 SER A O   
1210 C CB  . SER A 155 ? 0.26056 0.24114 0.29012 0.01923  0.02257  -0.00347 155 SER A CB  
1211 O OG  . SER A 155 ? 0.29717 0.27749 0.32360 0.01978  0.02489  -0.00712 155 SER A OG  
1212 N N   . THR A 156 ? 0.24177 0.21846 0.27900 0.03283  0.02418  -0.01092 156 THR A N   
1213 C CA  . THR A 156 ? 0.28030 0.24256 0.31314 0.03504  0.02369  -0.01444 156 THR A CA  
1214 C C   . THR A 156 ? 0.26473 0.22327 0.29190 0.02821  0.02374  -0.01581 156 THR A C   
1215 O O   . THR A 156 ? 0.29068 0.25677 0.31620 0.02431  0.02415  -0.01416 156 THR A O   
1216 C CB  . THR A 156 ? 0.27808 0.24318 0.31162 0.04259  0.02617  -0.02128 156 THR A CB  
1217 O OG1 . THR A 156 ? 0.28125 0.25786 0.31221 0.03859  0.02992  -0.02375 156 THR A OG1 
1218 C CG2 . THR A 156 ? 0.26863 0.24569 0.31070 0.05136  0.02629  -0.02164 156 THR A CG2 
1219 N N   . PRO A 157 ? 0.28525 0.23126 0.30858 0.02665  0.02244  -0.01904 157 PRO A N   
1220 C CA  . PRO A 157 ? 0.31351 0.26038 0.33321 0.02047  0.02130  -0.02163 157 PRO A CA  
1221 C C   . PRO A 157 ? 0.27869 0.23382 0.29363 0.02176  0.02273  -0.02534 157 PRO A C   
1222 O O   . PRO A 157 ? 0.27636 0.23829 0.28880 0.01897  0.02155  -0.02330 157 PRO A O   
1223 C CB  . PRO A 157 ? 0.32440 0.25560 0.34079 0.01764  0.01953  -0.02564 157 PRO A CB  
1224 C CG  . PRO A 157 ? 0.35776 0.27718 0.37520 0.02030  0.01927  -0.02068 157 PRO A CG  
1225 C CD  . PRO A 157 ? 0.31131 0.24008 0.33249 0.02952  0.02085  -0.01975 157 PRO A CD  
1226 N N   . SER A 158 ? 0.31804 0.27275 0.33022 0.02692  0.02542  -0.03050 158 SER A N   
1227 C CA  . SER A 158 ? 0.29174 0.25511 0.29652 0.02693  0.02790  -0.03343 158 SER A CA  
1228 C C   . SER A 158 ? 0.29040 0.26567 0.29656 0.02523  0.03060  -0.02728 158 SER A C   
1229 O O   . SER A 158 ? 0.28880 0.26799 0.28615 0.02226  0.03158  -0.02610 158 SER A O   
1230 C CB  . SER A 158 ? 0.30574 0.26797 0.30607 0.03325  0.03133  -0.04184 158 SER A CB  
1231 O OG  . SER A 158 ? 0.33448 0.30195 0.34278 0.04063  0.03453  -0.04229 158 SER A OG  
1232 N N   . GLY A 159 ? 0.25001 0.22912 0.26522 0.02611  0.03102  -0.02292 159 GLY A N   
1233 C CA  . GLY A 159 ? 0.27650 0.26367 0.29144 0.02160  0.03233  -0.01734 159 GLY A CA  
1234 C C   . GLY A 159 ? 0.25057 0.23075 0.26112 0.01757  0.02821  -0.01245 159 GLY A C   
1235 O O   . GLY A 159 ? 0.25726 0.23844 0.26405 0.01359  0.02852  -0.00816 159 GLY A O   
1236 N N   . THR A 160 ? 0.24595 0.21955 0.25636 0.01825  0.02447  -0.01351 160 THR A N   
1237 C CA  . THR A 160 ? 0.24105 0.21197 0.24902 0.01695  0.02090  -0.00996 160 THR A CA  
1238 C C   . THR A 160 ? 0.24085 0.20931 0.23697 0.01636  0.01924  -0.00864 160 THR A C   
1239 O O   . THR A 160 ? 0.26984 0.23350 0.26142 0.01679  0.01653  -0.00509 160 THR A O   
1240 C CB  . THR A 160 ? 0.27839 0.24882 0.29132 0.01710  0.01807  -0.01162 160 THR A CB  
1241 O OG1 . THR A 160 ? 0.25553 0.22619 0.26643 0.01630  0.01665  -0.01663 160 THR A OG1 
1242 C CG2 . THR A 160 ? 0.31712 0.28545 0.33757 0.01681  0.01943  -0.01039 160 THR A CG2 
1243 N N   . THR A 161 ? 0.27795 0.24756 0.26633 0.01592  0.02091  -0.01118 161 THR A N   
1244 C CA  . THR A 161 ? 0.30375 0.26862 0.27677 0.01519  0.01912  -0.00850 161 THR A CA  
1245 C C   . THR A 161 ? 0.32521 0.28824 0.29065 0.00999  0.02375  -0.00358 161 THR A C   
1246 O O   . THR A 161 ? 0.33706 0.29251 0.28597 0.00777  0.02301  0.00025  161 THR A O   
1247 C CB  . THR A 161 ? 0.25688 0.22403 0.22181 0.01632  0.01854  -0.01366 161 THR A CB  
1248 O OG1 . THR A 161 ? 0.28440 0.25701 0.25569 0.01624  0.02399  -0.01871 161 THR A OG1 
1249 C CG2 . THR A 161 ? 0.29383 0.26278 0.26312 0.01897  0.01193  -0.01765 161 THR A CG2 
1250 N N   . ALA A 162 ? 0.29758 0.26727 0.27391 0.00728  0.02786  -0.00309 162 ALA A N   
1251 C CA  . ALA A 162 ? 0.29362 0.26684 0.26643 -0.00023 0.03270  0.00075  162 ALA A CA  
1252 C C   . ALA A 162 ? 0.30092 0.26563 0.27453 -0.00392 0.02947  0.00531  162 ALA A C   
1253 O O   . ALA A 162 ? 0.32722 0.27694 0.29186 -0.00141 0.02396  0.00765  162 ALA A O   
1254 C CB  . ALA A 162 ? 0.27326 0.26528 0.25903 0.00002  0.03916  -0.00363 162 ALA A CB  
1255 N N   . TYR A 163 ? 0.29119 0.26559 0.27443 -0.00925 0.03221  0.00585  163 TYR A N   
1256 C CA  . TYR A 163 ? 0.26227 0.22702 0.24394 -0.01388 0.02846  0.00905  163 TYR A CA  
1257 C C   . TYR A 163 ? 0.27529 0.22967 0.25802 -0.00572 0.02248  0.00790  163 TYR A C   
1258 O O   . TYR A 163 ? 0.28555 0.22353 0.25786 -0.00584 0.01825  0.01001  163 TYR A O   
1259 C CB  . TYR A 163 ? 0.26309 0.24654 0.26003 -0.01850 0.03105  0.00756  163 TYR A CB  
1260 C CG  . TYR A 163 ? 0.27868 0.25796 0.27300 -0.02907 0.02917  0.01031  163 TYR A CG  
1261 C CD1 . TYR A 163 ? 0.26935 0.22287 0.24617 -0.03337 0.02490  0.01391  163 TYR A CD1 
1262 C CD2 . TYR A 163 ? 0.30864 0.31033 0.31796 -0.03476 0.03109  0.00856  163 TYR A CD2 
1263 C CE1 . TYR A 163 ? 0.33849 0.28459 0.31088 -0.04516 0.02260  0.01557  163 TYR A CE1 
1264 C CE2 . TYR A 163 ? 0.34532 0.34517 0.35288 -0.04721 0.02875  0.01023  163 TYR A CE2 
1265 C CZ  . TYR A 163 ? 0.39213 0.36240 0.38081 -0.05260 0.02433  0.01343  163 TYR A CZ  
1266 O OH  . TYR A 163 ? 0.37711 0.34203 0.36205 -0.06615 0.02151  0.01421  163 TYR A OH  
1267 N N   . ASN A 164 ? 0.23267 0.19579 0.22675 0.00140  0.02240  0.00432  164 ASN A N   
1268 C CA  . ASN A 164 ? 0.24716 0.20502 0.24324 0.00758  0.01842  0.00324  164 ASN A CA  
1269 C C   . ASN A 164 ? 0.27353 0.21893 0.25753 0.01117  0.01454  0.00408  164 ASN A C   
1270 O O   . ASN A 164 ? 0.27867 0.21654 0.25936 0.01464  0.01116  0.00405  164 ASN A O   
1271 C CB  . ASN A 164 ? 0.26177 0.22820 0.26813 0.01205  0.01968  0.00003  164 ASN A CB  
1272 C CG  . ASN A 164 ? 0.30794 0.27254 0.31639 0.01599  0.01715  -0.00094 164 ASN A CG  
1273 O OD1 . ASN A 164 ? 0.28525 0.25094 0.29805 0.01667  0.01677  -0.00024 164 ASN A OD1 
1274 N ND2 . ASN A 164 ? 0.25293 0.21738 0.25854 0.01830  0.01547  -0.00280 164 ASN A ND2 
1275 N N   . LYS A 165 ? 0.27259 0.21635 0.24899 0.01181  0.01456  0.00427  165 LYS A N   
1276 C CA  . LYS A 165 ? 0.25930 0.19272 0.22408 0.01748  0.00931  0.00505  165 LYS A CA  
1277 C C   . LYS A 165 ? 0.29156 0.20544 0.24178 0.01643  0.00624  0.00903  165 LYS A C   
1278 O O   . LYS A 165 ? 0.30340 0.20812 0.24834 0.02431  0.00112  0.00826  165 LYS A O   
1279 C CB  . LYS A 165 ? 0.29129 0.22557 0.24709 0.01749  0.00924  0.00515  165 LYS A CB  
1280 C CG  . LYS A 165 ? 0.29921 0.22552 0.24355 0.02521  0.00220  0.00574  165 LYS A CG  
1281 C CD  . LYS A 165 ? 0.30315 0.23327 0.23886 0.02504  0.00161  0.00487  165 LYS A CD  
1282 C CE  . LYS A 165 ? 0.38957 0.31535 0.31564 0.03487  -0.00754 0.00487  165 LYS A CE  
1283 N NZ  . LYS A 165 ? 0.45288 0.35433 0.35744 0.03719  -0.01147 0.01191  165 LYS A NZ  
1284 N N   . SER A 166 ? 0.28364 0.19075 0.22658 0.00641  0.00938  0.01286  166 SER A N   
1285 C CA  . SER A 166 ? 0.28014 0.16372 0.20621 0.00216  0.00636  0.01698  166 SER A CA  
1286 C C   . SER A 166 ? 0.31158 0.18971 0.24179 0.00443  0.00355  0.01423  166 SER A C   
1287 O O   . SER A 166 ? 0.35533 0.20958 0.26968 0.00557  -0.00109 0.01559  166 SER A O   
1288 C CB  . SER A 166 ? 0.33062 0.21336 0.25134 -0.01281 0.01154  0.02123  166 SER A CB  
1289 O OG  . SER A 166 ? 0.37778 0.26167 0.28859 -0.01427 0.01414  0.02412  166 SER A OG  
1290 N N   . LEU A 167 ? 0.33479 0.23200 0.28306 0.00562  0.00592  0.01043  167 LEU A N   
1291 C CA  . LEU A 167 ? 0.29880 0.19408 0.25043 0.00790  0.00379  0.00742  167 LEU A CA  
1292 C C   . LEU A 167 ? 0.30581 0.20471 0.26065 0.02046  0.00161  0.00366  167 LEU A C   
1293 O O   . LEU A 167 ? 0.32343 0.22354 0.28051 0.02375  0.00087  0.00053  167 LEU A O   
1294 C CB  . LEU A 167 ? 0.28841 0.20261 0.25572 0.00222  0.00715  0.00634  167 LEU A CB  
1295 C CG  . LEU A 167 ? 0.29576 0.21250 0.26305 -0.01067 0.00924  0.00880  167 LEU A CG  
1296 C CD1 . LEU A 167 ? 0.28662 0.22660 0.27154 -0.01262 0.01173  0.00726  167 LEU A CD1 
1297 C CD2 . LEU A 167 ? 0.29590 0.19191 0.24887 -0.01838 0.00532  0.00954  167 LEU A CD2 
1298 N N   . GLY A 168 ? 0.31128 0.21458 0.26646 0.02725  0.00064  0.00340  168 GLY A N   
1299 C CA  . GLY A 168 ? 0.30805 0.21988 0.26815 0.03863  -0.00147 -0.00066 168 GLY A CA  
1300 C C   . GLY A 168 ? 0.33531 0.27086 0.31338 0.03786  0.00253  -0.00300 168 GLY A C   
1301 O O   . GLY A 168 ? 0.32627 0.27336 0.31073 0.04457  0.00226  -0.00652 168 GLY A O   
1302 N N   . GLY A 169 ? 0.28471 0.22734 0.27019 0.02996  0.00627  -0.00133 169 GLY A N   
1303 C CA  . GLY A 169 ? 0.26321 0.22124 0.26208 0.02817  0.00949  -0.00283 169 GLY A CA  
1304 C C   . GLY A 169 ? 0.29650 0.26427 0.29976 0.03084  0.00814  -0.00542 169 GLY A C   
1305 O O   . GLY A 169 ? 0.27161 0.23528 0.26740 0.03416  0.00458  -0.00553 169 GLY A O   
1306 N N   . ALA A 170 ? 0.23298 0.21297 0.24701 0.02845  0.01045  -0.00725 170 ALA A N   
1307 C CA  . ALA A 170 ? 0.22803 0.21928 0.24819 0.02763  0.00906  -0.01053 170 ALA A CA  
1308 C C   . ALA A 170 ? 0.23972 0.22553 0.25752 0.02321  0.00949  -0.01091 170 ALA A C   
1309 O O   . ALA A 170 ? 0.25448 0.23318 0.27153 0.02019  0.01258  -0.00911 170 ALA A O   
1310 C CB  . ALA A 170 ? 0.27186 0.27622 0.30305 0.02309  0.01204  -0.01202 170 ALA A CB  
1311 N N   . LEU A 171 ? 0.23660 0.22768 0.25336 0.02381  0.00609  -0.01413 171 LEU A N   
1312 C CA  . LEU A 171 ? 0.25732 0.24447 0.27125 0.01973  0.00682  -0.01650 171 LEU A CA  
1313 C C   . LEU A 171 ? 0.25345 0.24555 0.27668 0.01339  0.00781  -0.02010 171 LEU A C   
1314 O O   . LEU A 171 ? 0.28730 0.29228 0.31779 0.01144  0.00540  -0.02266 171 LEU A O   
1315 C CB  . LEU A 171 ? 0.27121 0.25985 0.27591 0.02288  0.00181  -0.01853 171 LEU A CB  
1316 C CG  . LEU A 171 ? 0.29882 0.27987 0.29137 0.02916  -0.00102 -0.01410 171 LEU A CG  
1317 C CD1 . LEU A 171 ? 0.30332 0.28342 0.28310 0.03190  -0.00631 -0.01526 171 LEU A CD1 
1318 C CD2 . LEU A 171 ? 0.33362 0.30146 0.31885 0.02678  0.00377  -0.00901 171 LEU A CD2 
1319 N N   . MET A 172 ? 0.27128 0.25345 0.29421 0.01008  0.01110  -0.02047 172 MET A N   
1320 C CA  . MET A 172 ? 0.27955 0.25871 0.30765 0.00315  0.01196  -0.02260 172 MET A CA  
1321 C C   . MET A 172 ? 0.29532 0.26493 0.31794 0.00102  0.01089  -0.02850 172 MET A C   
1322 O O   . MET A 172 ? 0.35506 0.31681 0.37139 0.00582  0.01271  -0.02948 172 MET A O   
1323 C CB  . MET A 172 ? 0.33774 0.30768 0.36750 0.00228  0.01571  -0.01770 172 MET A CB  
1324 C CG  . MET A 172 ? 0.42187 0.39635 0.45289 0.00595  0.01719  -0.01252 172 MET A CG  
1325 S SD  . MET A 172 ? 0.45915 0.42053 0.48866 0.00582  0.01983  -0.00730 172 MET A SD  
1326 C CE  . MET A 172 ? 0.33869 0.29322 0.36872 -0.00394 0.02040  -0.00798 172 MET A CE  
1327 N N   . HIS A 173 ? 0.32676 0.29794 0.35185 -0.00665 0.00826  -0.03313 173 HIS A N   
1328 C CA  . HIS A 173 ? 0.32577 0.28406 0.34358 -0.00934 0.00664  -0.04020 173 HIS A CA  
1329 C C   . HIS A 173 ? 0.36660 0.30403 0.37994 -0.00644 0.01021  -0.03915 173 HIS A C   
1330 O O   . HIS A 173 ? 0.37190 0.30174 0.38842 -0.00929 0.01211  -0.03397 173 HIS A O   
1331 C CB  . HIS A 173 ? 0.33390 0.29411 0.35528 -0.02127 0.00300  -0.04532 173 HIS A CB  
1332 C CG  . HIS A 173 ? 0.35085 0.29935 0.36238 -0.02357 -0.00050 -0.05462 173 HIS A CG  
1333 N ND1 . HIS A 173 ? 0.42245 0.34527 0.42614 -0.02652 0.00031  -0.05852 173 HIS A ND1 
1334 C CD2 . HIS A 173 ? 0.38135 0.33852 0.38698 -0.02204 -0.00533 -0.06125 173 HIS A CD2 
1335 C CE1 . HIS A 173 ? 0.43633 0.35284 0.43028 -0.02724 -0.00350 -0.06828 173 HIS A CE1 
1336 N NE2 . HIS A 173 ? 0.38302 0.32125 0.37785 -0.02500 -0.00691 -0.06990 173 HIS A NE2 
1337 N N   . PRO A 174 ? 0.36698 0.29507 0.37188 -0.00016 0.01090  -0.04448 174 PRO A N   
1338 C CA  . PRO A 174 ? 0.36865 0.27993 0.37031 0.00663  0.01374  -0.04444 174 PRO A CA  
1339 C C   . PRO A 174 ? 0.42975 0.31633 0.42667 0.00167  0.01186  -0.04683 174 PRO A C   
1340 O O   . PRO A 174 ? 0.45498 0.32514 0.44866 0.00887  0.01296  -0.04545 174 PRO A O   
1341 C CB  . PRO A 174 ? 0.44854 0.36243 0.44283 0.01494  0.01560  -0.05111 174 PRO A CB  
1342 C CG  . PRO A 174 ? 0.45892 0.38203 0.44786 0.00970  0.01220  -0.05610 174 PRO A CG  
1343 C CD  . PRO A 174 ? 0.36245 0.29891 0.36007 0.00300  0.00948  -0.04994 174 PRO A CD  
1344 N N   . SER A 175 ? 0.38752 0.26964 0.38329 -0.01066 0.00851  -0.05008 175 SER A N   
1345 C CA  . SER A 175 ? 0.42682 0.28200 0.41672 -0.01819 0.00719  -0.04966 175 SER A CA  
1346 C C   . SER A 175 ? 0.46415 0.31817 0.45876 -0.02157 0.00962  -0.03832 175 SER A C   
1347 O O   . SER A 175 ? 0.53497 0.36354 0.52189 -0.02762 0.00895  -0.03537 175 SER A O   
1348 C CB  . SER A 175 ? 0.49454 0.34624 0.48247 -0.03429 0.00304  -0.05610 175 SER A CB  
1349 O OG  . SER A 175 ? 0.50336 0.38434 0.50409 -0.04297 0.00294  -0.05255 175 SER A OG  
1350 N N   . ILE A 176 ? 0.42604 0.30437 0.43045 -0.01871 0.01213  -0.03193 176 ILE A N   
1351 C CA  . ILE A 176 ? 0.41888 0.29738 0.42569 -0.02224 0.01455  -0.02214 176 ILE A CA  
1352 C C   . ILE A 176 ? 0.38506 0.25229 0.38770 -0.00892 0.01519  -0.01771 176 ILE A C   
1353 O O   . ILE A 176 ? 0.36598 0.24716 0.37305 0.00159  0.01594  -0.01890 176 ILE A O   
1354 C CB  . ILE A 176 ? 0.36701 0.27560 0.38485 -0.02446 0.01646  -0.01883 176 ILE A CB  
1355 C CG1 . ILE A 176 ? 0.40805 0.33229 0.43231 -0.03624 0.01485  -0.02387 176 ILE A CG1 
1356 C CG2 . ILE A 176 ? 0.36095 0.27008 0.37889 -0.02714 0.01968  -0.00951 176 ILE A CG2 
1357 C CD1 . ILE A 176 ? 0.35513 0.31042 0.39026 -0.03377 0.01550  -0.02283 176 ILE A CD1 
1358 N N   . GLU A 177 ? 0.37001 0.21274 0.36368 -0.00990 0.01448  -0.01221 177 GLU A N   
1359 C CA  . GLU A 177 ? 0.40378 0.23772 0.39399 0.00448  0.01340  -0.00838 177 GLU A CA  
1360 C C   . GLU A 177 ? 0.39215 0.24415 0.38760 0.00522  0.01516  0.00002  177 GLU A C   
1361 O O   . GLU A 177 ? 0.41413 0.25720 0.40323 -0.00091 0.01565  0.00790  177 GLU A O   
1362 C CB  . GLU A 177 ? 0.46835 0.26489 0.44366 0.00612  0.01021  -0.00625 177 GLU A CB  
1363 C CG  . GLU A 177 ? 0.47842 0.25443 0.44670 0.00877  0.00785  -0.01710 177 GLU A CG  
1364 C CD  . GLU A 177 ? 0.58806 0.32115 0.53879 0.01329  0.00366  -0.01541 177 GLU A CD  
1365 O OE1 . GLU A 177 ? 0.60809 0.31842 0.54805 -0.00054 0.00296  -0.00872 177 GLU A OE1 
1366 O OE2 . GLU A 177 ? 0.66103 0.38298 0.60796 0.03116  0.00112  -0.02020 177 GLU A OE2 
1367 N N   . ALA A 178 ? 0.34540 0.22164 0.35045 0.01194  0.01621  -0.00181 178 ALA A N   
1368 C CA  . ALA A 178 ? 0.33635 0.22934 0.34540 0.01146  0.01746  0.00411  178 ALA A CA  
1369 C C   . ALA A 178 ? 0.32620 0.23555 0.34216 0.02107  0.01702  0.00201  178 ALA A C   
1370 O O   . ALA A 178 ? 0.32199 0.23423 0.34080 0.02666  0.01714  -0.00385 178 ALA A O   
1371 C CB  . ALA A 178 ? 0.31541 0.22408 0.32903 0.00124  0.02016  0.00396  178 ALA A CB  
1372 N N   . MET A 179 ? 0.29300 0.21333 0.31058 0.02185  0.01685  0.00656  179 MET A N   
1373 C CA  . MET A 179 ? 0.28382 0.22092 0.30765 0.02607  0.01666  0.00501  179 MET A CA  
1374 C C   . MET A 179 ? 0.27749 0.22434 0.30106 0.02088  0.01769  0.00700  179 MET A C   
1375 O O   . MET A 179 ? 0.25902 0.20269 0.27821 0.01664  0.01855  0.01049  179 MET A O   
1376 C CB  . MET A 179 ? 0.28685 0.22582 0.31220 0.03464  0.01340  0.00711  179 MET A CB  
1377 C CG  . MET A 179 ? 0.29039 0.22117 0.30785 0.03432  0.01066  0.01429  179 MET A CG  
1378 S SD  . MET A 179 ? 0.30642 0.24000 0.32487 0.04596  0.00440  0.01671  179 MET A SD  
1379 C CE  . MET A 179 ? 0.31289 0.23438 0.31618 0.04238  0.00198  0.02589  179 MET A CE  
1380 N N   . GLN A 180 ? 0.25691 0.21466 0.28370 0.02129  0.01791  0.00465  180 GLN A N   
1381 C CA  . GLN A 180 ? 0.23207 0.19530 0.25677 0.01857  0.01817  0.00508  180 GLN A CA  
1382 C C   . GLN A 180 ? 0.26599 0.23396 0.28996 0.01956  0.01624  0.00568  180 GLN A C   
1383 O O   . GLN A 180 ? 0.25915 0.23157 0.28602 0.01954  0.01612  0.00414  180 GLN A O   
1384 C CB  . GLN A 180 ? 0.24545 0.21179 0.27072 0.01682  0.01913  0.00157  180 GLN A CB  
1385 C CG  . GLN A 180 ? 0.24428 0.21462 0.26647 0.01729  0.01847  0.00123  180 GLN A CG  
1386 C CD  . GLN A 180 ? 0.26945 0.24370 0.29179 0.01798  0.01778  -0.00189 180 GLN A CD  
1387 O OE1 . GLN A 180 ? 0.27058 0.24755 0.29041 0.02090  0.01658  -0.00286 180 GLN A OE1 
1388 N NE2 . GLN A 180 ? 0.24105 0.21505 0.26515 0.01658  0.01774  -0.00414 180 GLN A NE2 
1389 N N   . LEU A 181 ? 0.24285 0.21045 0.26194 0.01913  0.01507  0.00746  181 LEU A N   
1390 C CA  . LEU A 181 ? 0.25165 0.22149 0.26809 0.01855  0.01216  0.00728  181 LEU A CA  
1391 C C   . LEU A 181 ? 0.24052 0.20678 0.25083 0.01740  0.01205  0.00484  181 LEU A C   
1392 O O   . LEU A 181 ? 0.26538 0.23047 0.27153 0.01934  0.01336  0.00395  181 LEU A O   
1393 C CB  . LEU A 181 ? 0.27567 0.24484 0.28705 0.01988  0.00985  0.01007  181 LEU A CB  
1394 C CG  . LEU A 181 ? 0.27970 0.25129 0.28718 0.01832  0.00563  0.00874  181 LEU A CG  
1395 C CD1 . LEU A 181 ? 0.27980 0.26061 0.29622 0.01770  0.00274  0.00845  181 LEU A CD1 
1396 C CD2 . LEU A 181 ? 0.26019 0.23011 0.25792 0.02006  0.00324  0.01114  181 LEU A CD2 
1397 N N   . THR A 182 ? 0.24154 0.20589 0.25059 0.01440  0.01066  0.00370  182 THR A N   
1398 C CA  . THR A 182 ? 0.24990 0.20426 0.24942 0.01390  0.00916  0.00189  182 THR A CA  
1399 C C   . THR A 182 ? 0.26151 0.21077 0.25514 0.00886  0.00556  0.00114  182 THR A C   
1400 O O   . THR A 182 ? 0.26071 0.21829 0.26051 0.00382  0.00459  0.00204  182 THR A O   
1401 C CB  . THR A 182 ? 0.27535 0.22514 0.27290 0.01292  0.01016  0.00204  182 THR A CB  
1402 O OG1 . THR A 182 ? 0.27969 0.23596 0.28265 0.00762  0.01174  0.00336  182 THR A OG1 
1403 C CG2 . THR A 182 ? 0.27787 0.23214 0.27932 0.01787  0.01204  0.00120  182 THR A CG2 
1404 N N   . GLU A 183 ? 0.30268 0.23871 0.28431 0.01051  0.00319  -0.00140 183 GLU A N   
1405 C CA  . GLU A 183 ? 0.28675 0.21259 0.25911 0.00470  -0.00118 -0.00341 183 GLU A CA  
1406 C C   . GLU A 183 ? 0.32575 0.23763 0.29089 -0.00263 -0.00236 -0.00245 183 GLU A C   
1407 O O   . GLU A 183 ? 0.31278 0.21517 0.27276 0.00098  -0.00117 -0.00126 183 GLU A O   
1408 C CB  . GLU A 183 ? 0.36821 0.28185 0.32741 0.01105  -0.00330 -0.00788 183 GLU A CB  
1409 C CG  . GLU A 183 ? 0.33839 0.26481 0.30077 0.01765  -0.00078 -0.00839 183 GLU A CG  
1410 C CD  . GLU A 183 ? 0.40473 0.32223 0.35305 0.02366  -0.00205 -0.01400 183 GLU A CD  
1411 O OE1 . GLU A 183 ? 0.42917 0.32833 0.36585 0.02599  -0.00491 -0.01806 183 GLU A OE1 
1412 O OE2 . GLU A 183 ? 0.37430 0.30207 0.32181 0.02687  0.00025  -0.01424 183 GLU A OE2 
1413 N N   . MET A 184 ? 0.30544 0.21542 0.26857 -0.01356 -0.00525 -0.00282 184 MET A N   
1414 C CA  . MET A 184 ? 0.28569 0.17740 0.23729 -0.02398 -0.00678 -0.00164 184 MET A CA  
1415 C C   . MET A 184 ? 0.36599 0.23519 0.30095 -0.02668 -0.01281 -0.00615 184 MET A C   
1416 O O   . MET A 184 ? 0.39063 0.26753 0.32848 -0.03462 -0.01616 -0.00870 184 MET A O   
1417 C CB  . MET A 184 ? 0.31496 0.22396 0.27767 -0.03789 -0.00476 0.00092  184 MET A CB  
1418 C CG  . MET A 184 ? 0.35503 0.28858 0.33470 -0.03378 0.00101  0.00336  184 MET A CG  
1419 S SD  . MET A 184 ? 0.42246 0.38047 0.41552 -0.04944 0.00365  0.00443  184 MET A SD  
1420 C CE  . MET A 184 ? 0.34599 0.32798 0.35602 -0.03766 0.00958  0.00492  184 MET A CE  
1421 N N   . ALA A 185 ? 0.36323 0.20390 0.27989 -0.02050 -0.01502 -0.00753 185 ALA A N   
1422 C CA  . ALA A 185 ? 0.35739 0.16862 0.25346 -0.02193 -0.02120 -0.01281 185 ALA A CA  
1423 C C   . ALA A 185 ? 0.39338 0.21419 0.29089 -0.02048 -0.02409 -0.01907 185 ALA A C   
1424 O O   . ALA A 185 ? 0.42037 0.23791 0.31429 -0.03350 -0.02850 -0.02144 185 ALA A O   
1425 C CB  . ALA A 185 ? 0.41518 0.20526 0.29922 -0.04045 -0.02423 -0.01054 185 ALA A CB  
1426 N N   . SER A 186 ? 0.41461 0.24786 0.31623 -0.00621 -0.02185 -0.02178 186 SER A N   
1427 C CA  . SER A 186 ? 0.40980 0.24917 0.30766 -0.00524 -0.02478 -0.02739 186 SER A CA  
1428 C C   . SER A 186 ? 0.43956 0.24812 0.31332 -0.00098 -0.02983 -0.03576 186 SER A C   
1429 O O   . SER A 186 ? 0.47057 0.25779 0.33267 0.00902  -0.02973 -0.03776 186 SER A O   
1430 C CB  . SER A 186 ? 0.48293 0.34499 0.39028 0.00660  -0.01981 -0.02680 186 SER A CB  
1431 O OG  . SER A 186 ? 0.52972 0.38499 0.43310 0.01951  -0.01638 -0.02832 186 SER A OG  
1432 N N   . ILE A 187 ? 0.43392 0.24069 0.29915 -0.00629 -0.03487 -0.04165 187 ILE A N   
1433 C CA  . ILE A 187 ? 0.51097 0.28784 0.35130 -0.00091 -0.03976 -0.05152 187 ILE A CA  
1434 C C   . ILE A 187 ? 0.53116 0.32065 0.36877 0.01701  -0.03522 -0.05634 187 ILE A C   
1435 O O   . ILE A 187 ? 0.49948 0.31801 0.34921 0.01792  -0.03167 -0.05320 187 ILE A O   
1436 C CB  . ILE A 187 ? 0.51208 0.27962 0.34227 -0.01664 -0.04805 -0.05677 187 ILE A CB  
1437 C CG1 . ILE A 187 ? 0.53740 0.26304 0.33827 -0.01302 -0.05387 -0.06706 187 ILE A CG1 
1438 C CG2 . ILE A 187 ? 0.57806 0.37490 0.41551 -0.01622 -0.04881 -0.05813 187 ILE A CG2 
1439 C CD1 . ILE A 187 ? 0.59743 0.30503 0.38403 -0.03150 -0.06357 -0.07359 187 ILE A CD1 
1440 N N   . ASN A 188 ? 0.51706 0.28593 0.33898 0.03180  -0.03483 -0.06341 188 ASN A N   
1441 C CA  . ASN A 188 ? 0.54798 0.33272 0.36717 0.04804  -0.02936 -0.06924 188 ASN A CA  
1442 C C   . ASN A 188 ? 0.59032 0.34444 0.38268 0.05896  -0.03357 -0.08230 188 ASN A C   
1443 O O   . ASN A 188 ? 0.58838 0.31380 0.36941 0.06731  -0.03654 -0.08567 188 ASN A O   
1444 C CB  . ASN A 188 ? 0.58475 0.39213 0.42096 0.06034  -0.02101 -0.06457 188 ASN A CB  
1445 C CG  . ASN A 188 ? 0.57938 0.42156 0.43914 0.05266  -0.01524 -0.05424 188 ASN A CG  
1446 O OD1 . ASN A 188 ? 0.54045 0.40517 0.40380 0.05557  -0.00999 -0.05388 188 ASN A OD1 
1447 N ND2 . ASN A 188 ? 0.50556 0.34995 0.37907 0.04350  -0.01592 -0.04597 188 ASN A ND2 
1448 N N   . ASN A 189 ? 0.60065 0.35898 0.38059 0.05978  -0.03443 -0.08986 189 ASN A N   
1449 C CA  . ASN A 189 ? 0.64173 0.37348 0.39472 0.07202  -0.03759 -0.10422 189 ASN A CA  
1450 C C   . ASN A 189 ? 0.63594 0.39470 0.38488 0.07944  -0.03156 -0.10932 189 ASN A C   
1451 O O   . ASN A 189 ? 0.75744 0.55198 0.52467 0.07723  -0.02427 -0.10057 189 ASN A O   
1452 C CB  . ASN A 189 ? 0.64912 0.34073 0.38181 0.05791  -0.04918 -0.10939 189 ASN A CB  
1453 C CG  . ASN A 189 ? 0.70186 0.40833 0.44074 0.03662  -0.05396 -0.10533 189 ASN A CG  
1454 O OD1 . ASN A 189 ? 0.69988 0.43830 0.44665 0.03690  -0.05035 -0.10318 189 ASN A OD1 
1455 N ND2 . ASN A 189 ? 0.70833 0.39167 0.44276 0.01801  -0.06246 -0.10418 189 ASN A ND2 
1456 N N   . ARG A 190 ? 0.78679 0.52727 0.50960 0.08799  -0.03427 -0.12335 190 ARG A N   
1457 C CA  . ARG A 190 ? 0.86786 0.63572 0.58460 0.09485  -0.02725 -0.12763 190 ARG A CA  
1458 C C   . ARG A 190 ? 0.79503 0.58067 0.51438 0.07761  -0.03038 -0.12053 190 ARG A C   
1459 O O   . ARG A 190 ? 0.83132 0.64389 0.54924 0.08064  -0.02361 -0.11877 190 ARG A O   
1460 C CB  . ARG A 190 ? 0.81991 0.56426 0.50570 0.11061  -0.02878 -0.14618 190 ARG A CB  
1461 C CG  . ARG A 190 ? 0.86251 0.58893 0.52464 0.09995  -0.03783 -0.15416 190 ARG A CG  
1462 C CD  . ARG A 190 ? 0.83238 0.54686 0.47876 0.11200  -0.03705 -0.16638 190 ARG A CD  
1463 N NE  . ARG A 190 ? 1.02882 0.72351 0.65487 0.09906  -0.04718 -0.17339 190 ARG A NE  
1464 C CZ  . ARG A 190 ? 1.04640 0.70665 0.66631 0.08572  -0.05864 -0.17470 190 ARG A CZ  
1465 N NH1 . ARG A 190 ? 0.94833 0.58776 0.57831 0.08362  -0.06122 -0.16861 190 ARG A NH1 
1466 N NH2 . ARG A 190 ? 1.08217 0.72983 0.68519 0.07320  -0.06753 -0.18181 190 ARG A NH2 
1467 N N   . VAL A 191 ? 0.78122 0.55481 0.50510 0.05978  -0.04022 -0.11564 191 VAL A N   
1468 C CA  . VAL A 191 ? 0.72071 0.51309 0.44883 0.04554  -0.04494 -0.10944 191 VAL A CA  
1469 C C   . VAL A 191 ? 0.71285 0.53053 0.47136 0.03647  -0.04235 -0.09329 191 VAL A C   
1470 O O   . VAL A 191 ? 0.65276 0.49328 0.41733 0.03087  -0.04328 -0.08627 191 VAL A O   
1471 C CB  . VAL A 191 ? 0.77331 0.54022 0.48546 0.03135  -0.05875 -0.11738 191 VAL A CB  
1472 C CG1 . VAL A 191 ? 0.75807 0.54731 0.48715 0.01439  -0.06513 -0.10765 191 VAL A CG1 
1473 C CG2 . VAL A 191 ? 0.87305 0.62575 0.55314 0.03810  -0.06226 -0.13246 191 VAL A CG2 
1474 N N   . TYR A 192 ? 0.66178 0.47356 0.43724 0.03493  -0.04038 -0.08759 192 TYR A N   
1475 C CA  . TYR A 192 ? 0.59443 0.42751 0.39689 0.02689  -0.03811 -0.07411 192 TYR A CA  
1476 C C   . TYR A 192 ? 0.54905 0.39478 0.36565 0.03823  -0.02733 -0.06865 192 TYR A C   
1477 O O   . TYR A 192 ? 0.59625 0.42598 0.40868 0.04711  -0.02538 -0.07336 192 TYR A O   
1478 C CB  . TYR A 192 ? 0.65120 0.46902 0.46122 0.01284  -0.04494 -0.07191 192 TYR A CB  
1479 C CG  . TYR A 192 ? 0.60683 0.41456 0.40569 -0.00153 -0.05616 -0.07777 192 TYR A CG  
1480 C CD1 . TYR A 192 ? 0.60629 0.43573 0.40584 -0.00596 -0.06069 -0.07693 192 TYR A CD1 
1481 C CD2 . TYR A 192 ? 0.60990 0.38584 0.39666 -0.01147 -0.06299 -0.08383 192 TYR A CD2 
1482 C CE1 . TYR A 192 ? 0.64843 0.47317 0.43988 -0.01973 -0.07212 -0.08283 192 TYR A CE1 
1483 C CE2 . TYR A 192 ? 0.65452 0.42295 0.43212 -0.02743 -0.07370 -0.08977 192 TYR A CE2 
1484 C CZ  . TYR A 192 ? 0.65256 0.44847 0.43421 -0.03134 -0.07838 -0.08959 192 TYR A CZ  
1485 O OH  . TYR A 192 ? 0.74499 0.53890 0.51960 -0.04726 -0.09008 -0.09598 192 TYR A OH  
1486 N N   . ARG A 193 ? 0.52422 0.39715 0.35682 0.03780  -0.02138 -0.05889 193 ARG A N   
1487 C CA  . ARG A 193 ? 0.46373 0.35083 0.30978 0.04645  -0.01143 -0.05448 193 ARG A CA  
1488 C C   . ARG A 193 ? 0.47896 0.38402 0.34725 0.03961  -0.00887 -0.04231 193 ARG A C   
1489 O O   . ARG A 193 ? 0.47563 0.39276 0.34569 0.03438  -0.01012 -0.03645 193 ARG A O   
1490 C CB  . ARG A 193 ? 0.59902 0.50065 0.43484 0.05596  -0.00353 -0.05799 193 ARG A CB  
1491 C CG  . ARG A 193 ? 0.64383 0.56459 0.49470 0.06299  0.00683  -0.05448 193 ARG A CG  
1492 C CD  . ARG A 193 ? 0.68881 0.60539 0.53226 0.07800  0.01041  -0.06567 193 ARG A CD  
1493 N NE  . ARG A 193 ? 0.68393 0.62739 0.52833 0.08487  0.02156  -0.06703 193 ARG A NE  
1494 C CZ  . ARG A 193 ? 0.68998 0.63950 0.51590 0.08894  0.02551  -0.07319 193 ARG A CZ  
1495 N NH1 . ARG A 193 ? 0.79675 0.72614 0.60079 0.08772  0.01812  -0.07946 193 ARG A NH1 
1496 N NH2 . ARG A 193 ? 0.67765 0.65540 0.50652 0.09335  0.03736  -0.07341 193 ARG A NH2 
1497 N N   . THR A 194 ? 0.37125 0.27674 0.25465 0.04076  -0.00595 -0.03879 194 THR A N   
1498 C CA  . THR A 194 ? 0.35274 0.27456 0.25552 0.03662  -0.00220 -0.02904 194 THR A CA  
1499 C C   . THR A 194 ? 0.34946 0.28261 0.26104 0.04409  0.00590  -0.02840 194 THR A C   
1500 O O   . THR A 194 ? 0.37321 0.30390 0.27811 0.05365  0.00829  -0.03552 194 THR A O   
1501 C CB  . THR A 194 ? 0.39335 0.30924 0.30777 0.02864  -0.00658 -0.02508 194 THR A CB  
1502 O OG1 . THR A 194 ? 0.40032 0.30107 0.31203 0.03239  -0.00694 -0.02878 194 THR A OG1 
1503 C CG2 . THR A 194 ? 0.41929 0.32931 0.32792 0.01975  -0.01465 -0.02654 194 THR A CG2 
1504 N N   . ILE A 195 ? 0.30692 0.25358 0.23375 0.04010  0.00967  -0.02056 195 ILE A N   
1505 C CA  . ILE A 195 ? 0.33913 0.30015 0.27596 0.04443  0.01692  -0.01998 195 ILE A CA  
1506 C C   . ILE A 195 ? 0.34471 0.29959 0.28769 0.04977  0.01515  -0.02332 195 ILE A C   
1507 O O   . ILE A 195 ? 0.33855 0.30369 0.28515 0.05793  0.01891  -0.02739 195 ILE A O   
1508 C CB  . ILE A 195 ? 0.31453 0.28689 0.26298 0.03717  0.02043  -0.01113 195 ILE A CB  
1509 C CG1 . ILE A 195 ? 0.28187 0.27194 0.23952 0.03831  0.02834  -0.01082 195 ILE A CG1 
1510 C CG2 . ILE A 195 ? 0.29635 0.26180 0.25518 0.03222  0.01590  -0.00694 195 ILE A CG2 
1511 C CD1 . ILE A 195 ? 0.35850 0.36263 0.30737 0.04162  0.03541  -0.01420 195 ILE A CD1 
1512 N N   . GLY A 196 ? 0.33674 0.27559 0.27930 0.04562  0.00914  -0.02198 196 GLY A N   
1513 C CA  . GLY A 196 ? 0.34663 0.27377 0.29021 0.04925  0.00617  -0.02332 196 GLY A CA  
1514 C C   . GLY A 196 ? 0.37568 0.31583 0.33510 0.04715  0.00895  -0.01832 196 GLY A C   
1515 O O   . GLY A 196 ? 0.36512 0.29787 0.32768 0.04198  0.00645  -0.01476 196 GLY A O   
1516 N N   . SER A 197 ? 0.30544 0.26567 0.27424 0.04905  0.01446  -0.01794 197 SER A N   
1517 C CA  . SER A 197 ? 0.29125 0.26415 0.27421 0.04651  0.01670  -0.01478 197 SER A CA  
1518 C C   . SER A 197 ? 0.27057 0.24103 0.25936 0.03678  0.01644  -0.00859 197 SER A C   
1519 O O   . SER A 197 ? 0.27703 0.24658 0.26356 0.03221  0.01694  -0.00566 197 SER A O   
1520 C CB  . SER A 197 ? 0.24149 0.23750 0.23279 0.04711  0.02318  -0.01579 197 SER A CB  
1521 O OG  . SER A 197 ? 0.27676 0.28091 0.26493 0.05770  0.02440  -0.02261 197 SER A OG  
1522 N N   . PRO A 198 ? 0.24047 0.21149 0.23652 0.03483  0.01560  -0.00698 198 PRO A N   
1523 C CA  . PRO A 198 ? 0.25078 0.22264 0.25350 0.02777  0.01653  -0.00262 198 PRO A CA  
1524 C C   . PRO A 198 ? 0.20339 0.18414 0.21004 0.02434  0.02062  -0.00025 198 PRO A C   
1525 O O   . PRO A 198 ? 0.25802 0.25008 0.26725 0.02515  0.02397  -0.00197 198 PRO A O   
1526 C CB  . PRO A 198 ? 0.30644 0.27983 0.31450 0.02794  0.01568  -0.00334 198 PRO A CB  
1527 C CG  . PRO A 198 ? 0.28445 0.25219 0.28545 0.03481  0.01244  -0.00638 198 PRO A CG  
1528 C CD  . PRO A 198 ? 0.24622 0.21868 0.24392 0.04048  0.01366  -0.00966 198 PRO A CD  
1529 N N   . LEU A 199 ? 0.25620 0.23226 0.26308 0.02040  0.02033  0.00391  199 LEU A N   
1530 C CA  . LEU A 199 ? 0.26542 0.24298 0.27237 0.01626  0.02340  0.00788  199 LEU A CA  
1531 C C   . LEU A 199 ? 0.24190 0.21396 0.25452 0.01326  0.02301  0.00967  199 LEU A C   
1532 O O   . LEU A 199 ? 0.27444 0.24139 0.28888 0.01538  0.02013  0.00958  199 LEU A O   
1533 C CB  . LEU A 199 ? 0.27657 0.24880 0.27433 0.01653  0.02187  0.01174  199 LEU A CB  
1534 C CG  . LEU A 199 ? 0.23881 0.21352 0.22831 0.01987  0.02127  0.00850  199 LEU A CG  
1535 C CD1 . LEU A 199 ? 0.29572 0.26555 0.27497 0.01952  0.01845  0.01260  199 LEU A CD1 
1536 C CD2 . LEU A 199 ? 0.28171 0.26737 0.26934 0.02072  0.02689  0.00580  199 LEU A CD2 
1537 N N   . VAL A 200 ? 0.26487 0.23820 0.27963 0.00781  0.02613  0.01085  200 VAL A N   
1538 C CA  . VAL A 200 ? 0.24455 0.20848 0.26207 0.00464  0.02545  0.01138  200 VAL A CA  
1539 C C   . VAL A 200 ? 0.27870 0.22946 0.28848 0.00040  0.02637  0.01755  200 VAL A C   
1540 O O   . VAL A 200 ? 0.28637 0.23995 0.29205 -0.00655 0.03033  0.02074  200 VAL A O   
1541 C CB  . VAL A 200 ? 0.27435 0.24657 0.29911 -0.00001 0.02675  0.00695  200 VAL A CB  
1542 C CG1 . VAL A 200 ? 0.28135 0.24039 0.30594 -0.00398 0.02570  0.00646  200 VAL A CG1 
1543 C CG2 . VAL A 200 ? 0.28373 0.26460 0.31248 0.00570  0.02448  0.00211  200 VAL A CG2 
1544 N N   . PHE A 201 ? 0.27780 0.21438 0.28457 0.00494  0.02284  0.01947  201 PHE A N   
1545 C CA  . PHE A 201 ? 0.33106 0.24953 0.32726 0.00452  0.02145  0.02608  201 PHE A CA  
1546 C C   . PHE A 201 ? 0.35735 0.25734 0.35187 0.00246  0.02048  0.02527  201 PHE A C   
1547 O O   . PHE A 201 ? 0.36718 0.26775 0.36845 0.00723  0.01887  0.01927  201 PHE A O   
1548 C CB  . PHE A 201 ? 0.30909 0.22547 0.30215 0.01446  0.01632  0.02846  201 PHE A CB  
1549 C CG  . PHE A 201 ? 0.28790 0.21854 0.28019 0.01573  0.01607  0.02832  201 PHE A CG  
1550 C CD1 . PHE A 201 ? 0.33357 0.26192 0.31339 0.01354  0.01665  0.03398  201 PHE A CD1 
1551 C CD2 . PHE A 201 ? 0.30383 0.24747 0.30462 0.01871  0.01499  0.02284  201 PHE A CD2 
1552 C CE1 . PHE A 201 ? 0.33943 0.27922 0.31653 0.01522  0.01599  0.03227  201 PHE A CE1 
1553 C CE2 . PHE A 201 ? 0.29966 0.25202 0.29751 0.01937  0.01395  0.02178  201 PHE A CE2 
1554 C CZ  . PHE A 201 ? 0.30402 0.25454 0.28983 0.01811  0.01431  0.02591  201 PHE A CZ  
1555 N N   . PRO A 202 ? 0.35329 0.23480 0.33654 -0.00492 0.02150  0.03121  202 PRO A N   
1556 C CA  . PRO A 202 ? 0.36579 0.22186 0.34302 -0.00717 0.01956  0.03066  202 PRO A CA  
1557 C C   . PRO A 202 ? 0.41383 0.24965 0.38328 0.00648  0.01351  0.03288  202 PRO A C   
1558 O O   . PRO A 202 ? 0.36339 0.20646 0.33242 0.01620  0.01048  0.03584  202 PRO A O   
1559 C CB  . PRO A 202 ? 0.42740 0.27000 0.39274 -0.02253 0.02326  0.03792  202 PRO A CB  
1560 C CG  . PRO A 202 ? 0.39403 0.24594 0.35292 -0.02118 0.02489  0.04502  202 PRO A CG  
1561 C CD  . PRO A 202 ? 0.35166 0.23305 0.32444 -0.01278 0.02499  0.03899  202 PRO A CD  
1562 N N   . LYS A 203 ? 0.42748 0.23845 0.39106 0.00787  0.01109  0.03021  203 LYS A N   
1563 C CA  . LYS A 203 ? 0.47242 0.25877 0.42566 0.02185  0.00485  0.03259  203 LYS A CA  
1564 C C   . LYS A 203 ? 0.52315 0.29625 0.46102 0.02250  0.00229  0.04441  203 LYS A C   
1565 O O   . LYS A 203 ? 0.50134 0.26697 0.42883 0.00784  0.00610  0.05161  203 LYS A O   
1566 C CB  . LYS A 203 ? 0.56877 0.32027 0.51084 0.02004  0.00281  0.02951  203 LYS A CB  
1567 C CG  . LYS A 203 ? 0.52922 0.28871 0.48188 0.02301  0.00371  0.01730  203 LYS A CG  
1568 C CD  . LYS A 203 ? 0.56526 0.28768 0.50486 0.03248  -0.00118 0.01276  203 LYS A CD  
1569 C CE  . LYS A 203 ? 0.60377 0.32464 0.54332 0.05597  -0.00653 0.01280  203 LYS A CE  
1570 N NZ  . LYS A 203 ? 0.53551 0.26580 0.48425 0.07089  -0.00673 -0.00020 203 LYS A NZ  
1571 N N   . HIS A 204 ? 0.48976 0.26033 0.42533 0.03964  -0.00437 0.04626  204 HIS A N   
1572 C CA  . HIS A 204 ? 0.52335 0.27609 0.44061 0.04426  -0.00956 0.05754  204 HIS A CA  
1573 C C   . HIS A 204 ? 0.48649 0.26616 0.40617 0.04076  -0.00798 0.06184  204 HIS A C   
1574 O O   . HIS A 204 ? 0.56383 0.33652 0.47043 0.04790  -0.01374 0.06968  204 HIS A O   
1575 C CB  . HIS A 204 ? 0.57564 0.28847 0.46889 0.03179  -0.00858 0.06676  204 HIS A CB  
1576 C CG  . HIS A 204 ? 0.59734 0.27583 0.48330 0.03480  -0.01142 0.06253  204 HIS A CG  
1577 N ND1 . HIS A 204 ? 0.66329 0.32494 0.54628 0.05642  -0.01967 0.05910  204 HIS A ND1 
1578 C CD2 . HIS A 204 ? 0.67160 0.33049 0.55288 0.01936  -0.00747 0.05975  204 HIS A CD2 
1579 C CE1 . HIS A 204 ? 0.66841 0.29746 0.54266 0.05500  -0.02055 0.05441  204 HIS A CE1 
1580 N NE2 . HIS A 204 ? 0.72939 0.35549 0.60213 0.03153  -0.01352 0.05480  204 HIS A NE2 
1581 N N   . HIS A 205 ? 0.46436 0.27287 0.39847 0.03120  -0.00126 0.05654  205 HIS A N   
1582 C CA  . HIS A 205 ? 0.41442 0.24708 0.35081 0.03129  -0.00103 0.05805  205 HIS A CA  
1583 C C   . HIS A 205 ? 0.46503 0.31678 0.41474 0.04573  -0.00732 0.05250  205 HIS A C   
1584 O O   . HIS A 205 ? 0.41472 0.27478 0.37919 0.05126  -0.00737 0.04462  205 HIS A O   
1585 C CB  . HIS A 205 ? 0.36492 0.22033 0.31127 0.01895  0.00727  0.05349  205 HIS A CB  
1586 C CG  . HIS A 205 ? 0.38886 0.23571 0.32342 0.00417  0.01388  0.05942  205 HIS A CG  
1587 N ND1 . HIS A 205 ? 0.40801 0.27637 0.34575 -0.00441 0.02064  0.05801  205 HIS A ND1 
1588 C CD2 . HIS A 205 ? 0.46275 0.28205 0.38156 -0.00404 0.01500  0.06686  205 HIS A CD2 
1589 C CE1 . HIS A 205 ? 0.45894 0.31846 0.38557 -0.01779 0.02654  0.06413  205 HIS A CE1 
1590 N NE2 . HIS A 205 ? 0.48363 0.31190 0.39769 -0.01926 0.02324  0.07024  205 HIS A NE2 
1591 N N   . VAL A 206 ? 0.39512 0.25634 0.33956 0.05056  -0.01228 0.05616  206 VAL A N   
1592 C CA  . VAL A 206 ? 0.37958 0.26239 0.33710 0.06186  -0.01886 0.05119  206 VAL A CA  
1593 C C   . VAL A 206 ? 0.38675 0.29254 0.34817 0.05513  -0.01728 0.04852  206 VAL A C   
1594 O O   . VAL A 206 ? 0.43860 0.34045 0.38471 0.05036  -0.01711 0.05388  206 VAL A O   
1595 C CB  . VAL A 206 ? 0.47531 0.34773 0.42224 0.07608  -0.02953 0.05714  206 VAL A CB  
1596 C CG1 . VAL A 206 ? 0.48231 0.38471 0.44637 0.08622  -0.03644 0.05096  206 VAL A CG1 
1597 C CG2 . VAL A 206 ? 0.47855 0.32213 0.41841 0.08474  -0.03194 0.05937  206 VAL A CG2 
1598 N N   . VAL A 207 ? 0.32819 0.25636 0.30774 0.05544  -0.01677 0.04033  207 VAL A N   
1599 C CA  . VAL A 207 ? 0.34981 0.29604 0.33285 0.04926  -0.01619 0.03644  207 VAL A CA  
1600 C C   . VAL A 207 ? 0.36495 0.33007 0.35759 0.05618  -0.02456 0.03346  207 VAL A C   
1601 O O   . VAL A 207 ? 0.33512 0.31157 0.34321 0.06185  -0.02570 0.02927  207 VAL A O   
1602 C CB  . VAL A 207 ? 0.34122 0.29506 0.33516 0.04149  -0.00876 0.03000  207 VAL A CB  
1603 C CG1 . VAL A 207 ? 0.32010 0.28734 0.31510 0.03641  -0.00969 0.02578  207 VAL A CG1 
1604 C CG2 . VAL A 207 ? 0.33539 0.27617 0.32233 0.03468  -0.00137 0.03210  207 VAL A CG2 
1605 N N   . SER A 208 ? 0.31129 0.28166 0.29461 0.05588  -0.03056 0.03521  208 SER A N   
1606 C CA  . SER A 208 ? 0.31267 0.30336 0.30444 0.06142  -0.04019 0.03250  208 SER A CA  
1607 C C   . SER A 208 ? 0.40563 0.41036 0.39931 0.05119  -0.04076 0.02660  208 SER A C   
1608 O O   . SER A 208 ? 0.40335 0.39809 0.38161 0.04523  -0.03843 0.02738  208 SER A O   
1609 C CB  . SER A 208 ? 0.41508 0.39679 0.39025 0.07105  -0.04967 0.04003  208 SER A CB  
1610 O OG  . SER A 208 ? 0.49299 0.49771 0.47563 0.07597  -0.06051 0.03694  208 SER A OG  
1611 N N   . LEU A 209 ? 0.34000 0.36724 0.35150 0.04864  -0.04351 0.02031  209 LEU A N   
1612 C CA  . LEU A 209 ? 0.35474 0.39212 0.36632 0.03771  -0.04584 0.01464  209 LEU A CA  
1613 C C   . LEU A 209 ? 0.35325 0.40982 0.36723 0.04083  -0.05804 0.01337  209 LEU A C   
1614 O O   . LEU A 209 ? 0.38706 0.46332 0.41708 0.04861  -0.06288 0.01286  209 LEU A O   
1615 C CB  . LEU A 209 ? 0.30942 0.35837 0.33745 0.02860  -0.04055 0.00888  209 LEU A CB  
1616 C CG  . LEU A 209 ? 0.29963 0.33307 0.32715 0.02729  -0.02995 0.00986  209 LEU A CG  
1617 C CD1 . LEU A 209 ? 0.30887 0.35152 0.34824 0.01742  -0.02507 0.00516  209 LEU A CD1 
1618 C CD2 . LEU A 209 ? 0.30697 0.31814 0.31618 0.02511  -0.02573 0.01179  209 LEU A CD2 
1619 N N   . GLN A 210 ? 0.32593 0.37862 0.32428 0.03571  -0.06340 0.01193  210 GLN A N   
1620 C CA  . GLN A 210 ? 0.34374 0.41446 0.34185 0.03874  -0.07652 0.01063  210 GLN A CA  
1621 C C   . GLN A 210 ? 0.36778 0.44873 0.36739 0.02407  -0.08031 0.00208  210 GLN A C   
1622 O O   . GLN A 210 ? 0.39716 0.45872 0.38021 0.01619  -0.07620 -0.00056 210 GLN A O   
1623 C CB  . GLN A 210 ? 0.40339 0.45748 0.37496 0.04722  -0.08195 0.01757  210 GLN A CB  
1624 C CG  . GLN A 210 ? 0.48930 0.53225 0.45988 0.06103  -0.08038 0.02651  210 GLN A CG  
1625 C CD  . GLN A 210 ? 0.53770 0.55652 0.47951 0.06642  -0.08129 0.03569  210 GLN A CD  
1626 O OE1 . GLN A 210 ? 0.57846 0.59706 0.50181 0.06535  -0.08826 0.03615  210 GLN A OE1 
1627 N NE2 . GLN A 210 ? 0.57602 0.57364 0.51226 0.07144  -0.07432 0.04320  210 GLN A NE2 
1628 N N   . PRO A 211 ? 0.39155 0.50234 0.41018 0.01991  -0.08817 -0.00295 211 PRO A N   
1629 C CA  . PRO A 211 ? 0.37003 0.48848 0.38932 0.00297  -0.09230 -0.01120 211 PRO A CA  
1630 C C   . PRO A 211 ? 0.37663 0.48068 0.36983 0.00109  -0.10006 -0.01343 211 PRO A C   
1631 O O   . PRO A 211 ? 0.39381 0.49641 0.37380 0.01280  -0.10677 -0.00888 211 PRO A O   
1632 C CB  . PRO A 211 ? 0.37742 0.53727 0.42285 0.00143  -0.10125 -0.01503 211 PRO A CB  
1633 C CG  . PRO A 211 ? 0.45767 0.62753 0.52101 0.01528  -0.09478 -0.01016 211 PRO A CG  
1634 C CD  . PRO A 211 ? 0.46013 0.60095 0.50159 0.03025  -0.09376 -0.00214 211 PRO A CD  
1635 N N   . VAL A 212 ? 0.38826 0.48216 0.37324 -0.01407 -0.10013 -0.02088 212 VAL A N   
1636 C CA  . VAL A 212 ? 0.45226 0.53219 0.41164 -0.01804 -0.10755 -0.02617 212 VAL A CA  
1637 C C   . VAL A 212 ? 0.50614 0.60786 0.47249 -0.03158 -0.12070 -0.03483 212 VAL A C   
1638 O O   . VAL A 212 ? 0.47932 0.58954 0.43391 -0.02901 -0.13302 -0.03735 212 VAL A O   
1639 C CB  . VAL A 212 ? 0.43364 0.47885 0.37322 -0.02293 -0.09787 -0.02943 212 VAL A CB  
1640 C CG1 . VAL A 212 ? 0.51287 0.54350 0.42544 -0.02701 -0.10529 -0.03728 212 VAL A CG1 
1641 C CG2 . VAL A 212 ? 0.43513 0.46419 0.36845 -0.01018 -0.08603 -0.02147 212 VAL A CG2 
1642 N N   . ASN A 213 ? 0.43531 0.54752 0.42026 -0.04720 -0.11859 -0.03927 213 ASN A N   
1643 C CA  . ASN A 213 ? 0.48241 0.61971 0.47764 -0.06330 -0.13073 -0.04754 213 ASN A CA  
1644 C C   . ASN A 213 ? 0.44427 0.62067 0.47520 -0.06885 -0.12924 -0.04656 213 ASN A C   
1645 O O   . ASN A 213 ? 0.47675 0.69043 0.52608 -0.06040 -0.13786 -0.04584 213 ASN A O   
1646 C CB  . ASN A 213 ? 0.60434 0.71382 0.58209 -0.08324 -0.13101 -0.05627 213 ASN A CB  
1647 C CG  . ASN A 213 ? 0.69363 0.76745 0.63534 -0.07689 -0.13299 -0.05988 213 ASN A CG  
1648 O OD1 . ASN A 213 ? 0.66977 0.74988 0.59927 -0.06497 -0.14046 -0.05893 213 ASN A OD1 
1649 N ND2 . ASN A 213 ? 0.73508 0.77115 0.65844 -0.08352 -0.12597 -0.06383 213 ASN A ND2 
1650 N N   . ASP A 214 ? 0.43552 0.60416 0.47529 -0.08182 -0.11827 -0.04651 214 ASP A N   
1651 C CA  . ASP A 214 ? 0.45410 0.66060 0.52649 -0.08813 -0.11419 -0.04576 214 ASP A CA  
1652 C C   . ASP A 214 ? 0.40206 0.62172 0.48813 -0.06499 -0.10822 -0.03827 214 ASP A C   
1653 O O   . ASP A 214 ? 0.43615 0.62518 0.50704 -0.05166 -0.10045 -0.03235 214 ASP A O   
1654 C CB  . ASP A 214 ? 0.49082 0.68022 0.56366 -0.10739 -0.10267 -0.04593 214 ASP A CB  
1655 C CG  . ASP A 214 ? 0.46221 0.69588 0.56789 -0.11935 -0.09840 -0.04655 214 ASP A CG  
1656 O OD1 . ASP A 214 ? 0.56497 0.84144 0.69072 -0.12650 -0.10822 -0.05184 214 ASP A OD1 
1657 O OD2 . ASP A 214 ? 0.52096 0.74847 0.63194 -0.12254 -0.08526 -0.04231 214 ASP A OD2 
1658 N N   . LYS A 215 ? 0.39929 0.66515 0.51415 -0.06000 -0.11221 -0.03924 215 LYS A N   
1659 C CA  . LYS A 215 ? 0.36913 0.64570 0.49568 -0.03647 -0.10812 -0.03339 215 LYS A CA  
1660 C C   . LYS A 215 ? 0.37119 0.66915 0.52209 -0.03966 -0.09574 -0.03328 215 LYS A C   
1661 O O   . LYS A 215 ? 0.35169 0.66262 0.51498 -0.02041 -0.09263 -0.03040 215 LYS A O   
1662 C CB  . LYS A 215 ? 0.40158 0.71175 0.53906 -0.02022 -0.12312 -0.03428 215 LYS A CB  
1663 C CG  . LYS A 215 ? 0.44435 0.72859 0.55255 -0.01139 -0.13394 -0.03181 215 LYS A CG  
1664 C CD  . LYS A 215 ? 0.40955 0.72134 0.52457 0.00938  -0.14887 -0.03013 215 LYS A CD  
1665 C CE  . LYS A 215 ? 0.50152 0.86582 0.64163 0.00057  -0.16220 -0.03879 215 LYS A CE  
1666 N NZ  . LYS A 215 ? 0.59974 0.98931 0.74281 0.02241  -0.17963 -0.03734 215 LYS A NZ  
1667 N N   . ASP A 216 ? 0.32365 0.62258 0.47874 -0.06336 -0.08856 -0.03626 216 ASP A N   
1668 C CA  . ASP A 216 ? 0.34080 0.66172 0.51660 -0.06918 -0.07598 -0.03612 216 ASP A CA  
1669 C C   . ASP A 216 ? 0.31576 0.59294 0.47236 -0.07196 -0.06254 -0.03091 216 ASP A C   
1670 O O   . ASP A 216 ? 0.31996 0.55893 0.45297 -0.08383 -0.06232 -0.03019 216 ASP A O   
1671 C CB  . ASP A 216 ? 0.27025 0.62567 0.46398 -0.09613 -0.07654 -0.04195 216 ASP A CB  
1672 C CG  . ASP A 216 ? 0.34649 0.75691 0.56599 -0.09403 -0.08988 -0.04835 216 ASP A CG  
1673 O OD1 . ASP A 216 ? 0.32733 0.74687 0.54930 -0.06940 -0.09902 -0.04760 216 ASP A OD1 
1674 O OD2 . ASP A 216 ? 0.34068 0.78476 0.57717 -0.11757 -0.09159 -0.05387 216 ASP A OD2 
1675 N N   . PHE A 217 ? 0.25633 0.53945 0.42251 -0.06015 -0.05200 -0.02810 217 PHE A N   
1676 C CA  . PHE A 217 ? 0.21831 0.46246 0.36674 -0.05923 -0.04077 -0.02321 217 PHE A CA  
1677 C C   . PHE A 217 ? 0.28235 0.54774 0.44641 -0.06143 -0.02847 -0.02320 217 PHE A C   
1678 O O   . PHE A 217 ? 0.24575 0.55131 0.43341 -0.05150 -0.02787 -0.02633 217 PHE A O   
1679 C CB  . PHE A 217 ? 0.26688 0.48334 0.40179 -0.03637 -0.04116 -0.01889 217 PHE A CB  
1680 C CG  . PHE A 217 ? 0.28093 0.47608 0.39758 -0.03265 -0.05156 -0.01822 217 PHE A CG  
1681 C CD1 . PHE A 217 ? 0.34286 0.55928 0.46637 -0.02196 -0.06313 -0.01954 217 PHE A CD1 
1682 C CD2 . PHE A 217 ? 0.33054 0.48609 0.42246 -0.03969 -0.04992 -0.01680 217 PHE A CD2 
1683 C CE1 . PHE A 217 ? 0.33600 0.53295 0.43939 -0.01919 -0.07264 -0.01884 217 PHE A CE1 
1684 C CE2 . PHE A 217 ? 0.32450 0.46235 0.39813 -0.03613 -0.05851 -0.01722 217 PHE A CE2 
1685 C CZ  . PHE A 217 ? 0.34932 0.50816 0.42820 -0.02684 -0.06953 -0.01804 217 PHE A CZ  
1686 N N   . GLN A 218 ? 0.23756 0.47389 0.38620 -0.07126 -0.01894 -0.01974 218 GLN A N   
1687 C CA  . GLN A 218 ? 0.24606 0.49355 0.40202 -0.07165 -0.00626 -0.01874 218 GLN A CA  
1688 C C   . GLN A 218 ? 0.23316 0.45235 0.37724 -0.05148 -0.00246 -0.01562 218 GLN A C   
1689 O O   . GLN A 218 ? 0.24335 0.42197 0.36530 -0.05150 -0.00283 -0.01194 218 GLN A O   
1690 C CB  . GLN A 218 ? 0.32373 0.55551 0.46710 -0.09662 0.00071  -0.01609 218 GLN A CB  
1691 C CG  . GLN A 218 ? 0.33230 0.58376 0.48335 -0.10298 0.01446  -0.01513 218 GLN A CG  
1692 C CD  . GLN A 218 ? 0.29079 0.60006 0.47067 -0.11349 0.01725  -0.02010 218 GLN A CD  
1693 O OE1 . GLN A 218 ? 0.37180 0.70196 0.56268 -0.12552 0.00929  -0.02330 218 GLN A OE1 
1694 N NE2 . GLN A 218 ? 0.35189 0.68945 0.54425 -0.10925 0.02867  -0.02157 218 GLN A NE2 
1695 N N   . ILE A 219 ? 0.20450 0.44487 0.36306 -0.03378 0.00065  -0.01781 219 ILE A N   
1696 C CA  . ILE A 219 ? 0.19773 0.41183 0.34572 -0.01535 0.00301  -0.01572 219 ILE A CA  
1697 C C   . ILE A 219 ? 0.24264 0.46412 0.39336 -0.01558 0.01509  -0.01700 219 ILE A C   
1698 O O   . ILE A 219 ? 0.24225 0.50236 0.41228 -0.01469 0.01968  -0.02162 219 ILE A O   
1699 C CB  . ILE A 219 ? 0.28197 0.50508 0.43853 0.00672  -0.00463 -0.01724 219 ILE A CB  
1700 C CG1 . ILE A 219 ? 0.26742 0.47896 0.41557 0.00641  -0.01672 -0.01498 219 ILE A CG1 
1701 C CG2 . ILE A 219 ? 0.31962 0.51296 0.46385 0.02181  -0.00128 -0.01512 219 ILE A CG2 
1702 C CD1 . ILE A 219 ? 0.30289 0.53277 0.46145 0.02467  -0.02671 -0.01623 219 ILE A CD1 
1703 N N   . SER A 220 ? 0.25120 0.43872 0.38263 -0.01739 0.02015  -0.01346 220 SER A N   
1704 C CA  . SER A 220 ? 0.26780 0.45903 0.39771 -0.01662 0.03083  -0.01473 220 SER A CA  
1705 C C   . SER A 220 ? 0.31140 0.48618 0.43704 0.00351  0.03064  -0.01630 220 SER A C   
1706 O O   . SER A 220 ? 0.34969 0.49791 0.46560 0.01076  0.02428  -0.01360 220 SER A O   
1707 C CB  . SER A 220 ? 0.27952 0.44462 0.38946 -0.03229 0.03551  -0.00986 220 SER A CB  
1708 O OG  . SER A 220 ? 0.33665 0.46542 0.42997 -0.02285 0.03282  -0.00734 220 SER A OG  
1709 N N   . VAL A 221 ? 0.22301 0.41503 0.35625 0.01259  0.03743  -0.02132 221 VAL A N   
1710 C CA  . VAL A 221 ? 0.22033 0.39223 0.34594 0.02875  0.03815  -0.02365 221 VAL A CA  
1711 C C   . VAL A 221 ? 0.25671 0.43042 0.37462 0.02339  0.04872  -0.02583 221 VAL A C   
1712 O O   . VAL A 221 ? 0.26518 0.47147 0.39461 0.02283  0.05608  -0.03065 221 VAL A O   
1713 C CB  . VAL A 221 ? 0.28479 0.47493 0.42532 0.04892  0.03503  -0.02962 221 VAL A CB  
1714 C CG1 . VAL A 221 ? 0.30656 0.47178 0.43665 0.06394  0.03600  -0.03283 221 VAL A CG1 
1715 C CG2 . VAL A 221 ? 0.31408 0.50344 0.45998 0.05405  0.02350  -0.02645 221 VAL A CG2 
1716 N N   . ASP A 222 ? 0.23731 0.37972 0.33618 0.01947  0.04946  -0.02255 222 ASP A N   
1717 C CA  . ASP A 222 ? 0.28986 0.43226 0.37796 0.01482  0.05833  -0.02422 222 ASP A CA  
1718 C C   . ASP A 222 ? 0.29067 0.45681 0.38221 -0.00256 0.06470  -0.02156 222 ASP A C   
1719 O O   . ASP A 222 ? 0.32360 0.48553 0.41450 -0.01534 0.06071  -0.01604 222 ASP A O   
1720 C CB  . ASP A 222 ? 0.27724 0.42720 0.36921 0.03146  0.06187  -0.03285 222 ASP A CB  
1721 C CG  . ASP A 222 ? 0.23121 0.34894 0.31432 0.04297  0.05519  -0.03374 222 ASP A CG  
1722 O OD1 . ASP A 222 ? 0.23757 0.32958 0.30981 0.03650  0.05016  -0.02777 222 ASP A OD1 
1723 O OD2 . ASP A 222 ? 0.28879 0.40621 0.37494 0.05815  0.05515  -0.04073 222 ASP A OD2 
1724 N N   . HIS A 223 ? 0.26467 0.45628 0.35870 -0.00645 0.07500  -0.02499 223 HIS A N   
1725 C CA  A HIS A 223 ? 0.38230 0.59311 0.47671 -0.02701 0.08153  -0.02084 223 HIS A CA  
1726 C CA  B HIS A 223 ? 0.38659 0.58956 0.47934 -0.02842 0.07868  -0.01909 223 HIS A CA  
1727 C C   . HIS A 223 ? 0.41484 0.65955 0.53298 -0.03305 0.07940  -0.02215 223 HIS A C   
1728 O O   . HIS A 223 ? 0.51870 0.78233 0.63878 -0.05272 0.08526  -0.01920 223 HIS A O   
1729 C CB  A HIS A 223 ? 0.37867 0.61091 0.46843 -0.02969 0.09470  -0.02440 223 HIS A CB  
1730 C CB  B HIS A 223 ? 0.42396 0.62773 0.49970 -0.04187 0.08933  -0.01609 223 HIS A CB  
1731 C CG  A HIS A 223 ? 0.38717 0.64677 0.49255 -0.00956 0.09890  -0.03566 223 HIS A CG  
1732 C CG  B HIS A 223 ? 0.38063 0.57016 0.44334 -0.06508 0.08887  -0.00658 223 HIS A CG  
1733 N ND1 A HIS A 223 ? 0.32001 0.55771 0.42106 0.01076  0.09361  -0.04101 223 HIS A ND1 
1734 N ND1 B HIS A 223 ? 0.44614 0.65940 0.50971 -0.08512 0.09804  -0.00375 223 HIS A ND1 
1735 C CD2 A HIS A 223 ? 0.43002 0.73633 0.55452 -0.00615 0.10782  -0.04320 223 HIS A CD2 
1736 C CD2 B HIS A 223 ? 0.39586 0.54929 0.44473 -0.07115 0.07981  0.00015  223 HIS A CD2 
1737 C CE1 A HIS A 223 ? 0.34675 0.61189 0.46165 0.02702  0.09828  -0.05141 223 HIS A CE1 
1738 C CE1 B HIS A 223 ? 0.46499 0.65174 0.51287 -0.10330 0.09410  0.00496  223 HIS A CE1 
1739 N NE2 A HIS A 223 ? 0.39548 0.70462 0.52564 0.01840  0.10718  -0.05334 223 HIS A NE2 
1740 N NE2 B HIS A 223 ? 0.43841 0.58862 0.47718 -0.09377 0.08286  0.00690  223 HIS A NE2 
1741 N N   . LEU A 224 ? 0.28986 0.54531 0.42548 -0.01783 0.07166  -0.02658 224 LEU A N   
1742 C CA  . LEU A 224 ? 0.26006 0.56181 0.42258 -0.01790 0.07148  -0.03133 224 LEU A CA  
1743 C C   . LEU A 224 ? 0.33140 0.62668 0.49916 -0.02371 0.05943  -0.02763 224 LEU A C   
1744 O O   . LEU A 224 ? 0.33446 0.60623 0.49841 -0.00995 0.04978  -0.02685 224 LEU A O   
1745 C CB  . LEU A 224 ? 0.23992 0.56216 0.41795 0.00809  0.07123  -0.04054 224 LEU A CB  
1746 C CG  . LEU A 224 ? 0.30117 0.67461 0.50955 0.01364  0.06895  -0.04661 224 LEU A CG  
1747 C CD1 . LEU A 224 ? 0.38585 0.80980 0.60974 0.00413  0.08230  -0.05183 224 LEU A CD1 
1748 C CD2 . LEU A 224 ? 0.40370 0.77691 0.62150 0.04351  0.06071  -0.05276 224 LEU A CD2 
1749 N N   . SER A 225 ? 0.28082 0.59624 0.45574 -0.04489 0.06004  -0.02554 225 SER A N   
1750 C CA  . SER A 225 ? 0.30790 0.61243 0.48295 -0.05283 0.04841  -0.02255 225 SER A CA  
1751 C C   . SER A 225 ? 0.25343 0.60837 0.45764 -0.05299 0.04405  -0.02830 225 SER A C   
1752 O O   . SER A 225 ? 0.27353 0.66884 0.49307 -0.06705 0.05187  -0.03096 225 SER A O   
1753 C CB  . SER A 225 ? 0.37691 0.65478 0.53213 -0.07862 0.04975  -0.01562 225 SER A CB  
1754 O OG  . SER A 225 ? 0.42188 0.67724 0.57044 -0.08248 0.03798  -0.01353 225 SER A OG  
1755 N N   . ILE A 226 ? 0.20266 0.55669 0.41389 -0.03846 0.03142  -0.02991 226 ILE A N   
1756 C CA  . ILE A 226 ? 0.27833 0.68135 0.51754 -0.03426 0.02474  -0.03582 226 ILE A CA  
1757 C C   . ILE A 226 ? 0.26877 0.66009 0.50348 -0.04405 0.01141  -0.03347 226 ILE A C   
1758 O O   . ILE A 226 ? 0.27443 0.62140 0.48796 -0.03817 0.00468  -0.02899 226 ILE A O   
1759 C CB  . ILE A 226 ? 0.29788 0.71494 0.54978 -0.00232 0.02067  -0.04103 226 ILE A CB  
1760 C CG1 . ILE A 226 ? 0.37290 0.80955 0.63194 0.00729  0.03410  -0.04620 226 ILE A CG1 
1761 C CG2 . ILE A 226 ? 0.31423 0.77615 0.59211 0.00622  0.00955  -0.04629 226 ILE A CG2 
1762 C CD1 . ILE A 226 ? 0.42766 0.84600 0.68241 0.03830  0.03129  -0.04925 226 ILE A CD1 
1763 N N   . LEU A 227 ? 0.26459 0.69813 0.51954 -0.05897 0.00764  -0.03730 227 LEU A N   
1764 C CA  . LEU A 227 ? 0.21400 0.64245 0.46664 -0.06575 -0.00687 -0.03722 227 LEU A CA  
1765 C C   . LEU A 227 ? 0.31331 0.75883 0.57836 -0.03832 -0.01890 -0.04042 227 LEU A C   
1766 O O   . LEU A 227 ? 0.31016 0.80430 0.60206 -0.02543 -0.01894 -0.04638 227 LEU A O   
1767 C CB  . LEU A 227 ? 0.23000 0.69633 0.49873 -0.09393 -0.00760 -0.04061 227 LEU A CB  
1768 C CG  . LEU A 227 ? 0.25708 0.72749 0.52701 -0.10094 -0.02403 -0.04298 227 LEU A CG  
1769 C CD1 . LEU A 227 ? 0.30289 0.71059 0.53900 -0.10033 -0.03061 -0.03783 227 LEU A CD1 
1770 C CD2 . LEU A 227 ? 0.30402 0.80290 0.58525 -0.13158 -0.02397 -0.04608 227 LEU A CD2 
1771 N N   . HIS A 228 ? 0.25796 0.66485 0.50294 -0.02881 -0.02925 -0.03654 228 HIS A N   
1772 C CA  . HIS A 228 ? 0.28812 0.70500 0.53903 -0.00499 -0.04242 -0.03774 228 HIS A CA  
1773 C C   . HIS A 228 ? 0.28780 0.70958 0.53579 -0.01629 -0.05662 -0.03872 228 HIS A C   
1774 O O   . HIS A 228 ? 0.27900 0.66296 0.50358 -0.03119 -0.05809 -0.03554 228 HIS A O   
1775 C CB  . HIS A 228 ? 0.30372 0.67190 0.53123 0.01586  -0.04276 -0.03189 228 HIS A CB  
1776 C CG  . HIS A 228 ? 0.27910 0.64309 0.50939 0.03022  -0.03159 -0.03244 228 HIS A CG  
1777 N ND1 . HIS A 228 ? 0.32316 0.70207 0.56464 0.05672  -0.03471 -0.03527 228 HIS A ND1 
1778 C CD2 . HIS A 228 ? 0.34458 0.68946 0.56592 0.02236  -0.01812 -0.03108 228 HIS A CD2 
1779 C CE1 . HIS A 228 ? 0.37056 0.73934 0.60988 0.06382  -0.02320 -0.03651 228 HIS A CE1 
1780 N NE2 . HIS A 228 ? 0.31393 0.66353 0.54134 0.04297  -0.01308 -0.03388 228 HIS A NE2 
1781 N N   . ARG A 229 ? 0.28315 0.75080 0.55371 -0.00741 -0.06778 -0.04381 229 ARG A N   
1782 C CA  . ARG A 229 ? 0.27796 0.75698 0.54772 -0.01765 -0.08282 -0.04618 229 ARG A CA  
1783 C C   . ARG A 229 ? 0.34062 0.80639 0.59881 0.00780  -0.09748 -0.04330 229 ARG A C   
1784 O O   . ARG A 229 ? 0.32941 0.79888 0.59274 0.03457  -0.09857 -0.04178 229 ARG A O   
1785 C CB  . ARG A 229 ? 0.29850 0.83917 0.60032 -0.03005 -0.08591 -0.05389 229 ARG A CB  
1786 C CG  . ARG A 229 ? 0.33109 0.87553 0.63565 -0.06331 -0.07396 -0.05524 229 ARG A CG  
1787 C CD  . ARG A 229 ? 0.38473 0.96228 0.70467 -0.07970 -0.07902 -0.06020 229 ARG A CD  
1788 N NE  . ARG A 229 ? 0.36697 0.96052 0.69697 -0.10178 -0.06409 -0.06109 229 ARG A NE  
1789 C CZ  . ARG A 229 ? 0.38123 0.94776 0.69551 -0.12967 -0.05568 -0.05829 229 ARG A CZ  
1790 N NH1 . ARG A 229 ? 0.39636 0.91792 0.68492 -0.13838 -0.05970 -0.05520 229 ARG A NH1 
1791 N NH2 . ARG A 229 ? 0.36893 0.95176 0.69114 -0.14875 -0.04308 -0.05837 229 ARG A NH2 
1792 N N   . ASP A 230 ? 0.32591 0.77424 0.56601 -0.00102 -0.10909 -0.04267 230 ASP A N   
1793 C CA  . ASP A 230 ? 0.39998 0.83722 0.62571 0.01970  -0.12426 -0.03947 230 ASP A CA  
1794 C C   . ASP A 230 ? 0.37930 0.76872 0.58151 0.04125  -0.11904 -0.03067 230 ASP A C   
1795 O O   . ASP A 230 ? 0.41351 0.80428 0.61491 0.06649  -0.12668 -0.02747 230 ASP A O   
1796 C CB  . ASP A 230 ? 0.35970 0.85466 0.61441 0.03526  -0.13743 -0.04474 230 ASP A CB  
1797 C CG  . ASP A 230 ? 0.43274 0.91587 0.66977 0.05368  -0.15479 -0.04096 230 ASP A CG  
1798 O OD1 . ASP A 230 ? 0.50629 0.95983 0.71651 0.04351  -0.16119 -0.03890 230 ASP A OD1 
1799 O OD2 . ASP A 230 ? 0.52845 1.02127 0.77294 0.07715  -0.15937 -0.03899 230 ASP A OD2 
1800 N N   . VAL A 231 ? 0.30078 0.64708 0.48311 0.03084  -0.10652 -0.02671 231 VAL A N   
1801 C CA  . VAL A 231 ? 0.32721 0.63069 0.48933 0.04692  -0.10010 -0.01906 231 VAL A CA  
1802 C C   . VAL A 231 ? 0.39891 0.67009 0.53176 0.05382  -0.10950 -0.01318 231 VAL A C   
1803 O O   . VAL A 231 ? 0.39896 0.66137 0.51778 0.03938  -0.11414 -0.01482 231 VAL A O   
1804 C CB  . VAL A 231 ? 0.35009 0.62421 0.50344 0.03329  -0.08391 -0.01759 231 VAL A CB  
1805 C CG1 . VAL A 231 ? 0.37808 0.60717 0.50778 0.04536  -0.07919 -0.01016 231 VAL A CG1 
1806 C CG2 . VAL A 231 ? 0.37471 0.67641 0.55256 0.03207  -0.07354 -0.02157 231 VAL A CG2 
1807 N N   . GLN A 232 ? 0.39946 0.65153 0.52105 0.07563  -0.11226 -0.00647 232 GLN A N   
1808 C CA  . GLN A 232 ? 0.39788 0.61430 0.48759 0.08159  -0.11821 0.00112  232 GLN A CA  
1809 C C   . GLN A 232 ? 0.42148 0.59282 0.49026 0.07986  -0.10525 0.00748  232 GLN A C   
1810 O O   . GLN A 232 ? 0.45605 0.59941 0.49906 0.07450  -0.10486 0.01160  232 GLN A O   
1811 C CB  . GLN A 232 ? 0.39959 0.62100 0.48560 0.10578  -0.13171 0.00601  232 GLN A CB  
1812 N N   . GLU A 233 ? 0.41508 0.58173 0.49502 0.08362  -0.09441 0.00739  233 GLU A N   
1813 C CA  . GLU A 233 ? 0.40214 0.52946 0.46454 0.08357  -0.08358 0.01313  233 GLU A CA  
1814 C C   . GLU A 233 ? 0.36266 0.49528 0.44237 0.08140  -0.07175 0.00915  233 GLU A C   
1815 O O   . GLU A 233 ? 0.33210 0.49319 0.43372 0.08938  -0.07293 0.00446  233 GLU A O   
1816 C CB  . GLU A 233 ? 0.45835 0.56109 0.50333 0.10159  -0.08892 0.02170  233 GLU A CB  
1817 C CG  . GLU A 233 ? 0.51602 0.57838 0.54041 0.09881  -0.07905 0.02832  233 GLU A CG  
1818 C CD  . GLU A 233 ? 0.56504 0.59963 0.56814 0.11343  -0.08509 0.03805  233 GLU A CD  
1819 O OE1 . GLU A 233 ? 0.64895 0.69356 0.65698 0.13050  -0.09586 0.03895  233 GLU A OE1 
1820 O OE2 . GLU A 233 ? 0.59854 0.60152 0.57925 0.10779  -0.07932 0.04500  233 GLU A OE2 
1821 N N   . ILE A 234 ? 0.30397 0.41139 0.37343 0.07144  -0.06071 0.01060  234 ILE A N   
1822 C CA  . ILE A 234 ? 0.30376 0.40700 0.38225 0.07141  -0.04970 0.00849  234 ILE A CA  
1823 C C   . ILE A 234 ? 0.38077 0.44634 0.43956 0.07505  -0.04500 0.01476  234 ILE A C   
1824 O O   . ILE A 234 ? 0.39070 0.43738 0.43259 0.06682  -0.04344 0.01829  234 ILE A O   
1825 C CB  . ILE A 234 ? 0.31238 0.42345 0.39787 0.05374  -0.04131 0.00385  234 ILE A CB  
1826 C CG1 . ILE A 234 ? 0.29925 0.44645 0.40235 0.04519  -0.04584 -0.00182 234 ILE A CG1 
1827 C CG2 . ILE A 234 ? 0.30529 0.40996 0.39617 0.05482  -0.03046 0.00229  234 ILE A CG2 
1828 C CD1 . ILE A 234 ? 0.35428 0.49905 0.45514 0.02413  -0.04013 -0.00451 234 ILE A CD1 
1829 N N   . ARG A 235 ? 0.30654 0.36173 0.36661 0.08770  -0.04349 0.01580  235 ARG A N   
1830 C CA  . ARG A 235 ? 0.28101 0.30013 0.32227 0.09032  -0.04035 0.02197  235 ARG A CA  
1831 C C   . ARG A 235 ? 0.30676 0.31792 0.35335 0.08714  -0.03028 0.01811  235 ARG A C   
1832 O O   . ARG A 235 ? 0.32582 0.35171 0.38683 0.09489  -0.02891 0.01239  235 ARG A O   
1833 C CB  . ARG A 235 ? 0.32103 0.32490 0.35311 0.10776  -0.04864 0.02703  235 ARG A CB  
1834 C CG  . ARG A 235 ? 0.44244 0.44983 0.46393 0.11326  -0.06053 0.03252  235 ARG A CG  
1835 C CD  . ARG A 235 ? 0.52948 0.51685 0.53767 0.13261  -0.07041 0.03913  235 ARG A CD  
1836 N NE  . ARG A 235 ? 0.60310 0.54695 0.58486 0.13087  -0.06774 0.04851  235 ARG A NE  
1837 C CZ  . ARG A 235 ? 0.65414 0.57936 0.61219 0.12362  -0.06917 0.05745  235 ARG A CZ  
1838 N NH1 . ARG A 235 ? 0.61900 0.56285 0.57464 0.11797  -0.07345 0.05751  235 ARG A NH1 
1839 N NH2 . ARG A 235 ? 0.64390 0.53076 0.57899 0.12080  -0.06581 0.06617  235 ARG A NH2 
1840 N N   . TYR A 236 ? 0.27880 0.26848 0.31338 0.07707  -0.02382 0.02085  236 TYR A N   
1841 C CA  . TYR A 236 ? 0.29558 0.27571 0.33227 0.07282  -0.01534 0.01749  236 TYR A CA  
1842 C C   . TYR A 236 ? 0.37361 0.32197 0.39483 0.07461  -0.01452 0.02239  236 TYR A C   
1843 O O   . TYR A 236 ? 0.34476 0.27848 0.35163 0.06932  -0.01530 0.02901  236 TYR A O   
1844 C CB  . TYR A 236 ? 0.31899 0.30355 0.35617 0.05842  -0.00894 0.01565  236 TYR A CB  
1845 C CG  . TYR A 236 ? 0.29813 0.30827 0.34807 0.05351  -0.00867 0.01094  236 TYR A CG  
1846 C CD1 . TYR A 236 ? 0.32579 0.35398 0.38995 0.05643  -0.00593 0.00546  236 TYR A CD1 
1847 C CD2 . TYR A 236 ? 0.37844 0.39339 0.42455 0.04488  -0.01053 0.01167  236 TYR A CD2 
1848 C CE1 . TYR A 236 ? 0.34291 0.39468 0.41770 0.04849  -0.00479 0.00206  236 TYR A CE1 
1849 C CE2 . TYR A 236 ? 0.42499 0.45866 0.48029 0.03780  -0.01052 0.00780  236 TYR A CE2 
1850 C CZ  . TYR A 236 ? 0.37310 0.42497 0.44247 0.03836  -0.00758 0.00373  236 TYR A CZ  
1851 O OH  . TYR A 236 ? 0.54474 0.61443 0.62137 0.02778  -0.00729 0.00092  236 TYR A OH  
1852 N N   . GLU A 237 ? 0.34637 0.28375 0.36928 0.08036  -0.01226 0.01872  237 GLU A N   
1853 C CA  . GLU A 237 ? 0.34052 0.24583 0.34867 0.07786  -0.01067 0.02218  237 GLU A CA  
1854 C C   . GLU A 237 ? 0.38963 0.29117 0.40321 0.07849  -0.00584 0.01432  237 GLU A C   
1855 O O   . GLU A 237 ? 0.32343 0.24270 0.34929 0.08697  -0.00531 0.00727  237 GLU A O   
1856 C CB  . GLU A 237 ? 0.39679 0.27700 0.39076 0.08945  -0.01812 0.02837  237 GLU A CB  
1857 C CG  . GLU A 237 ? 0.47192 0.35989 0.47428 0.10846  -0.02397 0.02365  237 GLU A CG  
1858 C CD  . GLU A 237 ? 0.58528 0.45923 0.57490 0.12130  -0.03439 0.03156  237 GLU A CD  
1859 O OE1 . GLU A 237 ? 0.57597 0.41355 0.54376 0.11894  -0.03619 0.03969  237 GLU A OE1 
1860 O OE2 . GLU A 237 ? 0.55502 0.45460 0.55556 0.13254  -0.04098 0.03002  237 GLU A OE2 
1861 N N   . VAL A 238 ? 0.34580 0.22474 0.34932 0.06955  -0.00258 0.01530  238 VAL A N   
1862 C CA  . VAL A 238 ? 0.36098 0.23242 0.36631 0.07087  0.00047  0.00713  238 VAL A CA  
1863 C C   . VAL A 238 ? 0.38472 0.24020 0.38608 0.08792  -0.00432 0.00401  238 VAL A C   
1864 O O   . VAL A 238 ? 0.41905 0.24954 0.40739 0.09423  -0.01010 0.01033  238 VAL A O   
1865 C CB  . VAL A 238 ? 0.32679 0.17851 0.32260 0.05649  0.00365  0.00825  238 VAL A CB  
1866 C CG1 . VAL A 238 ? 0.34375 0.18448 0.33862 0.05806  0.00530  -0.00138 238 VAL A CG1 
1867 C CG2 . VAL A 238 ? 0.33118 0.20376 0.33326 0.04324  0.00808  0.00980  238 VAL A CG2 
1868 N N   . SER A 239 ? 0.37361 0.24381 0.38508 0.09715  -0.00209 -0.00587 239 SER A N   
1869 C CA  . SER A 239 ? 0.37609 0.23419 0.38504 0.11653  -0.00636 -0.01092 239 SER A CA  
1870 C C   . SER A 239 ? 0.46480 0.27872 0.45482 0.11626  -0.00810 -0.01238 239 SER A C   
1871 O O   . SER A 239 ? 0.46286 0.26483 0.44683 0.10053  -0.00429 -0.01327 239 SER A O   
1872 C CB  . SER A 239 ? 0.38283 0.27204 0.40751 0.12574  -0.00171 -0.02224 239 SER A CB  
1873 O OG  . SER A 239 ? 0.41885 0.29828 0.44165 0.14665  -0.00508 -0.02931 239 SER A OG  
1874 N N   . ALA A 240 ? 0.47391 0.26308 0.45416 0.13415  -0.01482 -0.01281 240 ALA A N   
1875 C CA  . ALA A 240 ? 0.48279 0.22724 0.44423 0.13844  -0.01741 -0.01711 240 ALA A CA  
1876 C C   . ALA A 240 ? 0.52069 0.27367 0.48771 0.14466  -0.01260 -0.03223 240 ALA A C   
1877 O O   . ALA A 240 ? 0.58819 0.30729 0.54007 0.14125  -0.01297 -0.03783 240 ALA A O   
1878 C CB  . ALA A 240 ? 0.52119 0.24358 0.47275 0.15589  -0.02591 -0.01323 240 ALA A CB  
1879 N N   . LYS A 241 ? 0.48543 0.28327 0.47261 0.15177  -0.00783 -0.03882 241 LYS A N   
1880 C CA  . LYS A 241 ? 0.52795 0.33868 0.51975 0.16012  -0.00241 -0.05333 241 LYS A CA  
1881 C C   . LYS A 241 ? 0.47148 0.29576 0.46546 0.13934  0.00486  -0.05547 241 LYS A C   
1882 O O   . LYS A 241 ? 0.43240 0.27464 0.43359 0.12357  0.00694  -0.04718 241 LYS A O   
1883 C CB  . LYS A 241 ? 0.49537 0.35117 0.50774 0.17710  0.00009  -0.05903 241 LYS A CB  
1884 C CG  . LYS A 241 ? 0.50085 0.35737 0.51669 0.19399  -0.00713 -0.05570 241 LYS A CG  
1885 C CD  . LYS A 241 ? 0.52547 0.43622 0.56620 0.20286  -0.00482 -0.05807 241 LYS A CD  
1886 C CE  . LYS A 241 ? 0.56042 0.47590 0.60555 0.22015  -0.01249 -0.05639 241 LYS A CE  
1887 N NZ  . LYS A 241 ? 0.55788 0.52904 0.62878 0.22649  -0.01116 -0.05861 241 LYS A NZ  
1888 N N   . LYS A 242 ? 0.46573 0.28136 0.45228 0.14091  0.00815  -0.06737 242 LYS A N   
1889 C CA  . LYS A 242 ? 0.44472 0.27121 0.43073 0.12283  0.01341  -0.06971 242 LYS A CA  
1890 C C   . LYS A 242 ? 0.44332 0.29525 0.43363 0.13203  0.02016  -0.08216 242 LYS A C   
1891 O O   . LYS A 242 ? 0.48029 0.33064 0.46973 0.15179  0.02035  -0.09141 242 LYS A O   
1892 C CB  . LYS A 242 ? 0.52655 0.31330 0.49448 0.11022  0.00988  -0.07164 242 LYS A CB  
1893 C CG  . LYS A 242 ? 0.59831 0.35736 0.55918 0.09931  0.00436  -0.05929 242 LYS A CG  
1894 C CD  . LYS A 242 ? 0.62611 0.36297 0.57607 0.07830  0.00315  -0.05942 242 LYS A CD  
1895 C CE  . LYS A 242 ? 0.54386 0.31410 0.50607 0.06156  0.00718  -0.05505 242 LYS A CE  
1896 N NZ  . LYS A 242 ? 0.59149 0.34839 0.54857 0.04052  0.00541  -0.05102 242 LYS A NZ  
1897 N N   . ILE A 243 ? 0.41618 0.29174 0.40995 0.11839  0.02575  -0.08222 243 ILE A N   
1898 C CA  . ILE A 243 ? 0.44002 0.33534 0.43208 0.12369  0.03279  -0.09367 243 ILE A CA  
1899 C C   . ILE A 243 ? 0.43583 0.30365 0.40918 0.11688  0.03095  -0.10213 243 ILE A C   
1900 O O   . ILE A 243 ? 0.45243 0.30546 0.42056 0.10045  0.02693  -0.09667 243 ILE A O   
1901 C CB  . ILE A 243 ? 0.36063 0.29536 0.36348 0.11322  0.03963  -0.08843 243 ILE A CB  
1902 C CG1 . ILE A 243 ? 0.41357 0.37002 0.41231 0.11878  0.04823  -0.09966 243 ILE A CG1 
1903 C CG2 . ILE A 243 ? 0.42155 0.35065 0.42128 0.09356  0.03703  -0.07923 243 ILE A CG2 
1904 C CD1 . ILE A 243 ? 0.38308 0.37178 0.38741 0.10642  0.05485  -0.09349 243 ILE A CD1 
1905 N N   . HIS A 244 ? 0.44868 0.31360 0.41270 0.12913  0.03407  -0.11619 244 HIS A N   
1906 C CA  . HIS A 244 ? 0.48279 0.32073 0.42702 0.12432  0.03161  -0.12689 244 HIS A CA  
1907 C C   . HIS A 244 ? 0.47280 0.33806 0.41236 0.12078  0.03887  -0.13361 244 HIS A C   
1908 O O   . HIS A 244 ? 0.48700 0.38048 0.43207 0.13271  0.04692  -0.13864 244 HIS A O   
1909 C CB  . HIS A 244 ? 0.53471 0.33996 0.46612 0.14279  0.02847  -0.13959 244 HIS A CB  
1910 C CG  . HIS A 244 ? 0.64533 0.42543 0.58041 0.14627  0.02163  -0.13006 244 HIS A CG  
1911 N ND1 . HIS A 244 ? 0.60795 0.35238 0.53391 0.13215  0.01408  -0.12314 244 HIS A ND1 
1912 C CD2 . HIS A 244 ? 0.66870 0.45555 0.61454 0.16136  0.02099  -0.12572 244 HIS A CD2 
1913 C CE1 . HIS A 244 ? 0.66807 0.39657 0.59707 0.13827  0.00963  -0.11423 244 HIS A CE1 
1914 N NE2 . HIS A 244 ? 0.68298 0.43646 0.62388 0.15680  0.01291  -0.11580 244 HIS A NE2 
1915 N N   . PHE A 245 ? 0.46743 0.32444 0.39565 0.10502  0.03582  -0.13441 245 PHE A N   
1916 C CA  . PHE A 245 ? 0.49612 0.37272 0.41366 0.10168  0.04102  -0.14114 245 PHE A CA  
1917 C C   . PHE A 245 ? 0.55403 0.40379 0.44917 0.10433  0.03756  -0.15754 245 PHE A C   
1918 O O   . PHE A 245 ? 0.56819 0.38396 0.45573 0.09801  0.02893  -0.16024 245 PHE A O   
1919 C CB  . PHE A 245 ? 0.47816 0.36939 0.39816 0.08328  0.03904  -0.12988 245 PHE A CB  
1920 C CG  . PHE A 245 ? 0.49431 0.41018 0.43274 0.07955  0.04238  -0.11494 245 PHE A CG  
1921 C CD1 . PHE A 245 ? 0.44305 0.35001 0.39433 0.07465  0.03734  -0.10440 245 PHE A CD1 
1922 C CD2 . PHE A 245 ? 0.50429 0.45095 0.44501 0.07938  0.05058  -0.11145 245 PHE A CD2 
1923 C CE1 . PHE A 245 ? 0.45457 0.38234 0.42051 0.07135  0.03980  -0.09227 245 PHE A CE1 
1924 C CE2 . PHE A 245 ? 0.49195 0.45766 0.44775 0.07409  0.05275  -0.09838 245 PHE A CE2 
1925 C CZ  . PHE A 245 ? 0.42281 0.37889 0.39131 0.07100  0.04707  -0.08961 245 PHE A CZ  
1926 N N   . ALA A 246 ? 0.52780 0.39225 0.41094 0.11277  0.04451  -0.16903 246 ALA A N   
1927 C CA  . ALA A 246 ? 0.57480 0.41732 0.43359 0.11185  0.04075  -0.18458 246 ALA A CA  
1928 C C   . ALA A 246 ? 0.68810 0.53733 0.54035 0.09204  0.03553  -0.17881 246 ALA A C   
1929 O O   . ALA A 246 ? 0.68873 0.56834 0.54547 0.08648  0.04041  -0.16927 246 ALA A O   
1930 C CB  . ALA A 246 ? 0.61644 0.47718 0.46571 0.12514  0.05100  -0.19582 246 ALA A CB  
1931 N N   . ARG A 247 ? 0.72330 0.54458 0.56523 0.08088  0.02498  -0.18399 247 ARG A N   
1932 C CA  . ARG A 247 ? 0.69711 0.52844 0.53308 0.06433  0.01879  -0.18063 247 ARG A CA  
1933 C C   . ARG A 247 ? 0.77048 0.58678 0.58027 0.06316  0.01403  -0.19831 247 ARG A C   
1934 O O   . ARG A 247 ? 0.76805 0.55113 0.56688 0.06582  0.00937  -0.21138 247 ARG A O   
1935 C CB  . ARG A 247 ? 0.71254 0.53565 0.56314 0.04838  0.00991  -0.16972 247 ARG A CB  
1936 C CG  . ARG A 247 ? 0.66999 0.51481 0.54422 0.04780  0.01446  -0.15112 247 ARG A CG  
1937 C CD  . ARG A 247 ? 0.71902 0.59533 0.59631 0.04170  0.01584  -0.14074 247 ARG A CD  
1938 N NE  . ARG A 247 ? 0.69358 0.59271 0.58046 0.04895  0.02547  -0.13099 247 ARG A NE  
1939 C CZ  . ARG A 247 ? 0.67668 0.58699 0.58137 0.04563  0.02652  -0.11686 247 ARG A CZ  
1940 N NH1 . ARG A 247 ? 0.68786 0.58994 0.60398 0.03707  0.01988  -0.11031 247 ARG A NH1 
1941 N NH2 . ARG A 247 ? 0.63695 0.56792 0.54764 0.05021  0.03480  -0.10964 247 ARG A NH2 
1942 N N   . PHE A 248 ? 0.77020 0.60846 0.56732 0.05950  0.01478  -0.19890 248 PHE A N   
1943 C CA  . PHE A 248 ? 0.76563 0.59284 0.53561 0.05826  0.00978  -0.21572 248 PHE A CA  
1944 C C   . PHE A 248 ? 0.78899 0.62073 0.55418 0.04119  -0.00272 -0.21367 248 PHE A C   
1945 O O   . PHE A 248 ? 0.79712 0.61619 0.54065 0.03729  -0.01017 -0.22860 248 PHE A O   
1946 C CB  . PHE A 248 ? 0.85709 0.70481 0.60919 0.07048  0.02099  -0.22181 248 PHE A CB  
1947 C CG  . PHE A 248 ? 0.83852 0.68422 0.59652 0.08639  0.03284  -0.22607 248 PHE A CG  
1948 C CD1 . PHE A 248 ? 0.84649 0.67056 0.59320 0.09168  0.03352  -0.23916 248 PHE A CD1 
1949 C CD2 . PHE A 248 ? 0.78225 0.64878 0.55988 0.09524  0.04253  -0.21609 248 PHE A CD2 
1950 C CE1 . PHE A 248 ? 0.86388 0.68821 0.61859 0.10720  0.04335  -0.24226 248 PHE A CE1 
1951 C CE2 . PHE A 248 ? 0.80364 0.67276 0.59074 0.10959  0.05214  -0.21889 248 PHE A CE2 
1952 C CZ  . PHE A 248 ? 0.82820 0.67637 0.60383 0.11635  0.05229  -0.23198 248 PHE A CZ  
1953 N N   . ARG A 249 ? 0.66746 0.51684 0.45239 0.03167  -0.00598 -0.19688 249 ARG A N   
1954 C CA  . ARG A 249 ? 0.65544 0.51480 0.43993 0.01766  -0.01824 -0.19427 249 ARG A CA  
1955 C C   . ARG A 249 ? 0.63414 0.50620 0.44673 0.01059  -0.01978 -0.17689 249 ARG A C   
1956 O O   . ARG A 249 ? 0.61793 0.49252 0.44621 0.01660  -0.01109 -0.16653 249 ARG A O   
1957 C CB  . ARG A 249 ? 0.71218 0.59235 0.47537 0.02018  -0.01878 -0.19429 249 ARG A CB  
1958 C CG  . ARG A 249 ? 0.71147 0.61326 0.47781 0.02819  -0.00706 -0.17937 249 ARG A CG  
1959 C CD  . ARG A 249 ? 0.74649 0.66305 0.48592 0.03137  -0.00496 -0.17919 249 ARG A CD  
1960 N NE  . ARG A 249 ? 0.72773 0.66100 0.47125 0.03616  0.00723  -0.16447 249 ARG A NE  
1961 C CZ  . ARG A 249 ? 0.79648 0.74316 0.51884 0.03704  0.01106  -0.15805 249 ARG A CZ  
1962 N NH1 . ARG A 249 ? 0.77313 0.71980 0.46756 0.03534  0.00329  -0.16459 249 ARG A NH1 
1963 N NH2 . ARG A 249 ? 0.78663 0.74611 0.51445 0.03861  0.02247  -0.14437 249 ARG A NH2 
1964 N N   . SER A 250 ? 0.63875 0.52019 0.45812 -0.00196 -0.03123 -0.17481 250 SER A N   
1965 C CA  . SER A 250 ? 0.59786 0.49413 0.44306 -0.00754 -0.03236 -0.15957 250 SER A CA  
1966 C C   . SER A 250 ? 0.60488 0.52406 0.45076 0.00009  -0.02790 -0.14606 250 SER A C   
1967 O O   . SER A 250 ? 0.63873 0.56998 0.46792 0.00206  -0.03215 -0.14677 250 SER A O   
1968 C CB  . SER A 250 ? 0.68860 0.59379 0.54334 -0.02240 -0.04535 -0.16199 250 SER A CB  
1969 O OG  . SER A 250 ? 0.66262 0.58626 0.54151 -0.02551 -0.04531 -0.14785 250 SER A OG  
1970 N N   . PHE A 251 ? 0.56254 0.48524 0.42531 0.00398  -0.01993 -0.13365 251 PHE A N   
1971 C CA  . PHE A 251 ? 0.51712 0.45808 0.38415 0.00788  -0.01741 -0.11936 251 PHE A CA  
1972 C C   . PHE A 251 ? 0.50617 0.44945 0.39889 0.00445  -0.01642 -0.10945 251 PHE A C   
1973 O O   . PHE A 251 ? 0.50157 0.43958 0.40336 0.00873  -0.00775 -0.10404 251 PHE A O   
1974 C CB  . PHE A 251 ? 0.57951 0.52225 0.43465 0.01712  -0.00576 -0.11585 251 PHE A CB  
1975 C CG  . PHE A 251 ? 0.64290 0.59958 0.49368 0.01899  -0.00443 -0.10220 251 PHE A CG  
1976 C CD1 . PHE A 251 ? 0.60275 0.56788 0.45999 0.01597  -0.01386 -0.09453 251 PHE A CD1 
1977 C CD2 . PHE A 251 ? 0.67604 0.63687 0.51551 0.02370  0.00627  -0.09737 251 PHE A CD2 
1978 C CE1 . PHE A 251 ? 0.52656 0.49809 0.37612 0.01887  -0.01385 -0.08230 251 PHE A CE1 
1979 C CE2 . PHE A 251 ? 0.69065 0.65858 0.52267 0.02339  0.00715  -0.08427 251 PHE A CE2 
1980 C CZ  . PHE A 251 ? 0.61059 0.58088 0.44667 0.02160  -0.00352 -0.07652 251 PHE A CZ  
1981 N N   . PRO A 252 ? 0.49036 0.44299 0.39540 -0.00346 -0.02534 -0.10814 252 PRO A N   
1982 C CA  . PRO A 252 ? 0.47577 0.43126 0.40370 -0.00764 -0.02378 -0.10012 252 PRO A CA  
1983 C C   . PRO A 252 ? 0.46574 0.42906 0.40023 -0.00024 -0.01754 -0.08691 252 PRO A C   
1984 O O   . PRO A 252 ? 0.39887 0.37133 0.32408 0.00516  -0.01870 -0.08172 252 PRO A O   
1985 C CB  . PRO A 252 ? 0.46129 0.43404 0.39921 -0.01639 -0.03456 -0.10214 252 PRO A CB  
1986 C CG  . PRO A 252 ? 0.49422 0.46403 0.41634 -0.02060 -0.04230 -0.11504 252 PRO A CG  
1987 C CD  . PRO A 252 ? 0.48671 0.44950 0.38584 -0.00959 -0.03741 -0.11561 252 PRO A CD  
1988 N N   . PHE A 253 ? 0.42974 0.38740 0.37880 -0.00086 -0.01178 -0.08124 253 PHE A N   
1989 C CA  . PHE A 253 ? 0.43562 0.39951 0.39213 0.00445  -0.00659 -0.06962 253 PHE A CA  
1990 C C   . PHE A 253 ? 0.34762 0.32724 0.30593 0.00599  -0.01236 -0.06355 253 PHE A C   
1991 O O   . PHE A 253 ? 0.33740 0.31861 0.28811 0.01184  -0.01030 -0.05653 253 PHE A O   
1992 C CB  . PHE A 253 ? 0.41879 0.37692 0.39114 0.00162  -0.00287 -0.06532 253 PHE A CB  
1993 C CG  . PHE A 253 ? 0.36500 0.32868 0.34446 0.00623  0.00161  -0.05485 253 PHE A CG  
1994 C CD1 . PHE A 253 ? 0.37057 0.33071 0.34564 0.01220  0.00828  -0.05171 253 PHE A CD1 
1995 C CD2 . PHE A 253 ? 0.40012 0.37411 0.39095 0.00426  -0.00078 -0.04909 253 PHE A CD2 
1996 C CE1 . PHE A 253 ? 0.42594 0.39036 0.40742 0.01447  0.01155  -0.04277 253 PHE A CE1 
1997 C CE2 . PHE A 253 ? 0.33371 0.30983 0.32917 0.00826  0.00279  -0.04078 253 PHE A CE2 
1998 C CZ  . PHE A 253 ? 0.35574 0.32599 0.34620 0.01257  0.00838  -0.03753 253 PHE A CZ  
1999 N N   . TRP A 254 ? 0.34642 0.33780 0.31504 0.00080  -0.01970 -0.06612 254 TRP A N   
2000 C CA  . TRP A 254 ? 0.35676 0.36448 0.32865 0.00552  -0.02574 -0.06105 254 TRP A CA  
2001 C C   . TRP A 254 ? 0.34611 0.35545 0.29812 0.01156  -0.03177 -0.06183 254 TRP A C   
2002 O O   . TRP A 254 ? 0.34088 0.35396 0.28743 0.01929  -0.03496 -0.05475 254 TRP A O   
2003 C CB  . TRP A 254 ? 0.34668 0.37329 0.33665 -0.00100 -0.03194 -0.06480 254 TRP A CB  
2004 C CG  . TRP A 254 ? 0.30927 0.33501 0.31657 -0.00740 -0.02538 -0.06169 254 TRP A CG  
2005 C CD1 . TRP A 254 ? 0.35719 0.38327 0.37475 -0.02011 -0.02500 -0.06652 254 TRP A CD1 
2006 C CD2 . TRP A 254 ? 0.34014 0.36343 0.35345 -0.00235 -0.01902 -0.05296 254 TRP A CD2 
2007 N NE1 . TRP A 254 ? 0.32930 0.35213 0.35734 -0.02261 -0.01793 -0.06011 254 TRP A NE1 
2008 C CE2 . TRP A 254 ? 0.30571 0.32836 0.33200 -0.01145 -0.01453 -0.05242 254 TRP A CE2 
2009 C CE3 . TRP A 254 ? 0.29662 0.31599 0.30360 0.00778  -0.01689 -0.04555 254 TRP A CE3 
2010 C CZ2 . TRP A 254 ? 0.28642 0.30749 0.31949 -0.00925 -0.00837 -0.04508 254 TRP A CZ2 
2011 C CZ3 . TRP A 254 ? 0.31434 0.33108 0.32935 0.00932  -0.01092 -0.03907 254 TRP A CZ3 
2012 C CH2 . TRP A 254 ? 0.27957 0.29799 0.30720 0.00137  -0.00686 -0.03923 254 TRP A CH2 
2013 N N   . ARG A 255 ? 0.38420 0.38855 0.32250 0.00857  -0.03401 -0.07042 255 ARG A N   
2014 C CA  . ARG A 255 ? 0.35885 0.36272 0.27396 0.01444  -0.03852 -0.06986 255 ARG A CA  
2015 C C   . ARG A 255 ? 0.40406 0.39524 0.30494 0.01932  -0.02897 -0.06141 255 ARG A C   
2016 O O   . ARG A 255 ? 0.44244 0.43193 0.32746 0.02479  -0.03154 -0.05392 255 ARG A O   
2017 C CB  . ARG A 255 ? 0.40975 0.41144 0.31122 0.00987  -0.04305 -0.08240 255 ARG A CB  
2018 C CG  . ARG A 255 ? 0.49136 0.49148 0.36411 0.01565  -0.04704 -0.08201 255 ARG A CG  
2019 C CD  . ARG A 255 ? 0.50436 0.51088 0.36636 0.01166  -0.05824 -0.09488 255 ARG A CD  
2020 N NE  . ARG A 255 ? 0.55720 0.58386 0.42730 0.01371  -0.07215 -0.09357 255 ARG A NE  
2021 C CZ  . ARG A 255 ? 0.51374 0.55609 0.38966 0.00805  -0.08430 -0.10387 255 ARG A CZ  
2022 N NH1 . ARG A 255 ? 0.53808 0.57444 0.41117 -0.00204 -0.08518 -0.11709 255 ARG A NH1 
2023 N NH2 . ARG A 255 ? 0.46668 0.53155 0.35135 0.01291  -0.09649 -0.10151 255 ARG A NH2 
2024 N N   . ARG A 256 ? 0.36746 0.34976 0.27339 0.01711  -0.01834 -0.06229 256 ARG A N   
2025 C CA  . ARG A 256 ? 0.40038 0.37627 0.29749 0.01975  -0.00861 -0.05494 256 ARG A CA  
2026 C C   . ARG A 256 ? 0.41885 0.39458 0.32108 0.02207  -0.00886 -0.04311 256 ARG A C   
2027 O O   . ARG A 256 ? 0.40621 0.37650 0.29240 0.02364  -0.00680 -0.03533 256 ARG A O   
2028 C CB  . ARG A 256 ? 0.50696 0.47798 0.41348 0.01859  0.00113  -0.05934 256 ARG A CB  
2029 C CG  . ARG A 256 ? 0.54376 0.51464 0.44588 0.02022  0.01181  -0.05315 256 ARG A CG  
2030 C CD  . ARG A 256 ? 0.62376 0.59353 0.53045 0.02240  0.02032  -0.06102 256 ARG A CD  
2031 N NE  . ARG A 256 ? 0.42778 0.39049 0.34925 0.02200  0.01692  -0.06701 256 ARG A NE  
2032 C CZ  . ARG A 256 ? 0.54733 0.50140 0.46481 0.02296  0.01579  -0.07845 256 ARG A CZ  
2033 N NH1 . ARG A 256 ? 0.53471 0.48820 0.43628 0.02709  0.02008  -0.08683 256 ARG A NH1 
2034 N NH2 . ARG A 256 ? 0.53623 0.48079 0.46431 0.01918  0.01059  -0.08186 256 ARG A NH2 
2035 N N   . VAL A 257 ? 0.36948 0.34986 0.29200 0.02178  -0.01172 -0.04180 257 VAL A N   
2036 C CA  . VAL A 257 ? 0.35333 0.33267 0.27943 0.02550  -0.01330 -0.03258 257 VAL A CA  
2037 C C   . VAL A 257 ? 0.34811 0.32728 0.25822 0.03163  -0.02275 -0.02901 257 VAL A C   
2038 O O   . VAL A 257 ? 0.36721 0.33535 0.26484 0.03517  -0.02272 -0.02014 257 VAL A O   
2039 C CB  . VAL A 257 ? 0.30251 0.28995 0.25203 0.02449  -0.01442 -0.03370 257 VAL A CB  
2040 C CG1 . VAL A 257 ? 0.30417 0.29142 0.25573 0.03084  -0.01767 -0.02624 257 VAL A CG1 
2041 C CG2 . VAL A 257 ? 0.32737 0.31029 0.28878 0.01968  -0.00558 -0.03489 257 VAL A CG2 
2042 N N   . HIS A 258 ? 0.33471 0.32515 0.24446 0.03311  -0.03218 -0.03579 258 HIS A N   
2043 C CA  . HIS A 258 ? 0.38279 0.37435 0.27696 0.04138  -0.04318 -0.03242 258 HIS A CA  
2044 C C   . HIS A 258 ? 0.41784 0.39259 0.28146 0.04206  -0.04074 -0.02607 258 HIS A C   
2045 O O   . HIS A 258 ? 0.43860 0.40101 0.28487 0.04827  -0.04491 -0.01688 258 HIS A O   
2046 C CB  . HIS A 258 ? 0.36053 0.37043 0.25922 0.04140  -0.05402 -0.04217 258 HIS A CB  
2047 C CG  . HIS A 258 ? 0.36477 0.37689 0.24394 0.05075  -0.06674 -0.03995 258 HIS A CG  
2048 N ND1 . HIS A 258 ? 0.45303 0.45691 0.30426 0.05060  -0.06941 -0.04048 258 HIS A ND1 
2049 C CD2 . HIS A 258 ? 0.37347 0.39691 0.25660 0.06166  -0.07853 -0.03813 258 HIS A CD2 
2050 C CE1 . HIS A 258 ? 0.42778 0.43557 0.26504 0.06071  -0.08298 -0.03787 258 HIS A CE1 
2051 N NE2 . HIS A 258 ? 0.53604 0.55540 0.39283 0.06853  -0.08890 -0.03635 258 HIS A NE2 
2052 N N   . ASP A 259 ? 0.43503 0.40844 0.28989 0.03579  -0.03417 -0.03132 259 ASP A N   
2053 C CA  . ASP A 259 ? 0.46744 0.42943 0.29201 0.03502  -0.03075 -0.02656 259 ASP A CA  
2054 C C   . ASP A 259 ? 0.49482 0.44261 0.31227 0.03210  -0.02109 -0.01506 259 ASP A C   
2055 O O   . ASP A 259 ? 0.58313 0.51769 0.37328 0.03191  -0.02102 -0.00632 259 ASP A O   
2056 C CB  . ASP A 259 ? 0.49327 0.45983 0.31299 0.02983  -0.02423 -0.03692 259 ASP A CB  
2057 C CG  . ASP A 259 ? 0.55436 0.53040 0.37089 0.03098  -0.03520 -0.04806 259 ASP A CG  
2058 O OD1 . ASP A 259 ? 0.50289 0.48575 0.31968 0.03592  -0.04843 -0.04741 259 ASP A OD1 
2059 O OD2 . ASP A 259 ? 0.52385 0.50107 0.33714 0.02724  -0.03089 -0.05848 259 ASP A OD2 
2060 N N   . SER A 260 ? 0.44675 0.39640 0.28660 0.02873  -0.01348 -0.01469 260 SER A N   
2061 C CA  . SER A 260 ? 0.49692 0.43593 0.33300 0.02383  -0.00461 -0.00528 260 SER A CA  
2062 C C   . SER A 260 ? 0.50699 0.43169 0.33942 0.02801  -0.01112 0.00403  260 SER A C   
2063 O O   . SER A 260 ? 0.49850 0.40657 0.31339 0.02373  -0.00773 0.01378  260 SER A O   
2064 C CB  . SER A 260 ? 0.50491 0.45237 0.36579 0.01934  0.00495  -0.00897 260 SER A CB  
2065 O OG  . SER A 260 ? 0.54329 0.50109 0.40825 0.01725  0.01176  -0.01787 260 SER A OG  
2066 N N   . PHE A 261 ? 0.40398 0.33463 0.25258 0.03579  -0.01991 0.00079  261 PHE A N   
2067 C CA  . PHE A 261 ? 0.42564 0.34330 0.27263 0.04222  -0.02567 0.00752  261 PHE A CA  
2068 C C   . PHE A 261 ? 0.47397 0.38831 0.30864 0.05482  -0.03973 0.00885  261 PHE A C   
2069 O O   . PHE A 261 ? 0.50426 0.39980 0.32699 0.06177  -0.04496 0.01598  261 PHE A O   
2070 C CB  . PHE A 261 ? 0.38489 0.31298 0.26096 0.04272  -0.02318 0.00334  261 PHE A CB  
2071 C CG  . PHE A 261 ? 0.39611 0.32524 0.28298 0.03267  -0.01135 0.00345  261 PHE A CG  
2072 C CD1 . PHE A 261 ? 0.40073 0.31372 0.27816 0.02714  -0.00633 0.01126  261 PHE A CD1 
2073 C CD2 . PHE A 261 ? 0.36976 0.31446 0.27402 0.02849  -0.00590 -0.00408 261 PHE A CD2 
2074 C CE1 . PHE A 261 ? 0.39713 0.31580 0.28606 0.01815  0.00364  0.01085  261 PHE A CE1 
2075 C CE2 . PHE A 261 ? 0.39471 0.34151 0.30860 0.02172  0.00388  -0.00403 261 PHE A CE2 
2076 C CZ  . PHE A 261 ? 0.32787 0.26426 0.23534 0.01669  0.00856  0.00338  261 PHE A CZ  
2077 N N   . ILE A 262 ? 0.40083 0.33236 0.23787 0.05869  -0.04692 0.00167  262 ILE A N   
2078 C CA  . ILE A 262 ? 0.43298 0.36725 0.26322 0.07249  -0.06167 0.00191  262 ILE A CA  
2079 C C   . ILE A 262 ? 0.53898 0.45819 0.33375 0.07484  -0.06766 0.00783  262 ILE A C   
2080 O O   . ILE A 262 ? 0.61463 0.51275 0.38668 0.08434  -0.07572 0.01672  262 ILE A O   
2081 C CB  . ILE A 262 ? 0.43211 0.39850 0.28892 0.07562  -0.06832 -0.00978 262 ILE A CB  
2082 C CG1 . ILE A 262 ? 0.43838 0.41824 0.32685 0.07215  -0.06158 -0.01422 262 ILE A CG1 
2083 C CG2 . ILE A 262 ? 0.47913 0.45469 0.32961 0.09174  -0.08536 -0.01039 262 ILE A CG2 
2084 C CD1 . ILE A 262 ? 0.43659 0.40932 0.32909 0.08242  -0.06398 -0.00974 262 ILE A CD1 
2085 N N   . GLU A 263 ? 0.47551 0.40313 0.26270 0.06700  -0.06420 0.00293  263 GLU A N   
2086 C CA  . GLU A 263 ? 0.58692 0.50252 0.33814 0.06918  -0.07008 0.00793  263 GLU A CA  
2087 C C   . GLU A 263 ? 0.68306 0.61042 0.42992 0.05939  -0.06325 -0.00031 263 GLU A C   
2088 O O   . GLU A 263 ? 0.61565 0.56295 0.38835 0.05527  -0.06064 -0.01196 263 GLU A O   
2089 C CB  . GLU A 263 ? 0.68969 0.61283 0.43470 0.08446  -0.08885 0.00657  263 GLU A CB  
2090 C CG  . GLU A 263 ? 0.66255 0.62117 0.44102 0.08609  -0.09516 -0.00792 263 GLU A CG  
2091 C CD  . GLU A 263 ? 0.63606 0.61019 0.40946 0.09980  -0.11427 -0.01127 263 GLU A CD  
2092 O OE1 . GLU A 263 ? 0.73875 0.69715 0.47724 0.10626  -0.12268 -0.00445 263 GLU A OE1 
2093 O OE2 . GLU A 263 ? 0.61267 0.61625 0.41678 0.10384  -0.12097 -0.02053 263 GLU A OE2 
2094 N N   . ASP A 264 ? 0.73152 0.64577 0.44429 0.05575  -0.06044 0.00508  264 ASP A N   
2095 C CA  . ASP A 264 ? 0.76054 0.68649 0.46746 0.04830  -0.05380 -0.00459 264 ASP A CA  
2096 C C   . ASP A 264 ? 0.85261 0.76656 0.51613 0.04828  -0.05608 0.00117  264 ASP A C   
2097 O O   . ASP A 264 ? 0.97094 0.88373 0.61630 0.05731  -0.07138 0.00218  264 ASP A O   
2098 C CB  . ASP A 264 ? 0.75664 0.68546 0.47933 0.03751  -0.03554 -0.00716 264 ASP A CB  
2099 C CG  . ASP A 264 ? 0.80626 0.74690 0.52485 0.03244  -0.02829 -0.01936 264 ASP A CG  
2100 O OD1 . ASP A 264 ? 0.79064 0.73538 0.49115 0.03549  -0.03691 -0.02567 264 ASP A OD1 
2101 O OD2 . ASP A 264 ? 0.75938 0.70514 0.49226 0.02640  -0.01453 -0.02336 264 ASP A OD2 
# 
