data_8QGN
# 
_entry.id   8QGN 
# 
_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   8QGN         pdb_00008qgn 10.2210/pdb8qgn/pdb 
WWPDB D_1292133183 ?            ?                   
# 
_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                        8QGN 
_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]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
640.608   1  ?        ? ? ? 
4 water       nat water 18.015    38 ?        ? ? ? 
# 
_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]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
UMU 
4 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   TYR n 
1 4   MET n 
1 5   ILE n 
1 6   THR n 
1 7   SER n 
1 8   LYS n 
1 9   GLY n 
1 10  ASP n 
1 11  GLU n 
1 12  LYS n 
1 13  SER n 
1 14  ASP n 
1 15  LEU n 
1 16  LEU n 
1 17  ARG n 
1 18  LEU n 
1 19  ASN n 
1 20  MET n 
1 21  ILE n 
1 22  ALA n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  GLU n 
1 27  TYR n 
1 28  ASP n 
1 29  MET n 
1 30  GLU n 
1 31  TYR n 
1 32  ASP n 
1 33  ASP n 
1 34  VAL n 
1 35  GLU n 
1 36  PRO n 
1 37  GLU n 
1 38  ILE n 
1 39  VAL n 
1 40  ILE n 
1 41  SER n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  ASP n 
1 46  GLY n 
1 47  THR n 
1 48  PHE n 
1 49  LEU n 
1 50  SER n 
1 51  ALA n 
1 52  PHE n 
1 53  HIS n 
1 54  GLN n 
1 55  TYR n 
1 56  GLU n 
1 57  GLU n 
1 58  ARG n 
1 59  LEU n 
1 60  ASP n 
1 61  GLU n 
1 62  ILE n 
1 63  ALA n 
1 64  PHE n 
1 65  ILE n 
1 66  GLY n 
1 67  ILE n 
1 68  HIS n 
1 69  THR n 
1 70  GLY n 
1 71  HIS n 
1 72  LEU n 
1 73  GLY n 
1 74  PHE n 
1 75  TYR n 
1 76  ALA n 
1 77  ASP n 
1 78  TRP n 
1 79  ARG n 
1 80  PRO n 
1 81  ALA n 
1 82  GLU n 
1 83  ALA n 
1 84  ASP n 
1 85  LYS n 
1 86  LEU n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  LYS n 
1 93  GLY n 
1 94  GLU n 
1 95  TYR n 
1 96  GLN n 
1 97  LYS n 
1 98  VAL n 
1 99  SER n 
1 100 TYR n 
1 101 PRO n 
1 102 LEU n 
1 103 LEU n 
1 104 LYS n 
1 105 THR n 
1 106 THR n 
1 107 VAL n 
1 108 LYS n 
1 109 TYR n 
1 110 GLY n 
1 111 ILE n 
1 112 GLY n 
1 113 LYS n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 THR n 
1 118 TYR n 
1 119 LEU n 
1 120 ALA n 
1 121 LEU n 
1 122 ASN n 
1 123 GLU n 
1 124 SER n 
1 125 THR n 
1 126 VAL n 
1 127 LYS n 
1 128 SER n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 PRO n 
1 133 PHE n 
1 134 VAL n 
1 135 VAL n 
1 136 ASP n 
1 137 VAL n 
1 138 VAL n 
1 139 ILE n 
1 140 ASN n 
1 141 ASP n 
1 142 ILE n 
1 143 HIS n 
1 144 PHE n 
1 145 GLU n 
1 146 ARG n 
1 147 PHE n 
1 148 ARG n 
1 149 GLY n 
1 150 ASP n 
1 151 GLY n 
1 152 LEU n 
1 153 CYS n 
1 154 MET n 
1 155 SER n 
1 156 THR n 
1 157 PRO n 
1 158 SER n 
1 159 GLY n 
1 160 THR n 
1 161 THR n 
1 162 ALA n 
1 163 TYR n 
1 164 ASN n 
1 165 LYS n 
1 166 SER n 
1 167 LEU n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 LEU n 
1 172 MET n 
1 173 HIS n 
1 174 PRO n 
1 175 SER n 
1 176 ILE n 
1 177 GLU n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 LEU n 
1 182 THR n 
1 183 GLU n 
1 184 MET n 
1 185 ALA n 
1 186 SER n 
1 187 ILE n 
1 188 ASN n 
1 189 ASN n 
1 190 ARG n 
1 191 VAL n 
1 192 TYR n 
1 193 ARG n 
1 194 THR n 
1 195 ILE n 
1 196 GLY n 
1 197 SER n 
1 198 PRO n 
1 199 LEU n 
1 200 VAL n 
1 201 PHE n 
1 202 PRO n 
1 203 LYS n 
1 204 HIS n 
1 205 HIS n 
1 206 VAL n 
1 207 VAL n 
1 208 SER n 
1 209 LEU n 
1 210 GLN n 
1 211 PRO n 
1 212 VAL n 
1 213 ASN n 
1 214 ASP n 
1 215 LYS n 
1 216 ASP n 
1 217 PHE n 
1 218 GLN n 
1 219 ILE n 
1 220 SER n 
1 221 VAL n 
1 222 ASP n 
1 223 HIS n 
1 224 LEU n 
1 225 SER n 
1 226 ILE n 
1 227 LEU n 
1 228 HIS n 
1 229 ARG n 
1 230 ASP n 
1 231 VAL n 
1 232 GLN n 
1 233 GLU n 
1 234 ILE n 
1 235 ARG n 
1 236 TYR n 
1 237 GLU n 
1 238 VAL n 
1 239 SER n 
1 240 ALA n 
1 241 LYS n 
1 242 LYS n 
1 243 ILE n 
1 244 HIS n 
1 245 PHE n 
1 246 ALA n 
1 247 ARG n 
1 248 PHE n 
1 249 ARG n 
1 250 SER n 
1 251 PHE n 
1 252 PRO n 
1 253 PHE n 
1 254 TRP n 
1 255 ARG n 
1 256 ARG n 
1 257 VAL n 
1 258 HIS n 
1 259 ASP n 
1 260 SER n 
1 261 PHE n 
1 262 ILE n 
1 263 GLU n 
1 264 ASP n 
1 265 LEU n 
1 266 GLU n 
1 267 HIS n 
1 268 HIS n 
1 269 HIS n 
1 270 HIS n 
1 271 HIS n 
1 272 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   272 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nadK1, lmo0968' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Listeria monocytogenes EGD-e' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     169963 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CIT non-polymer         . 'CITRIC ACID' ? 'C6 H8 O7'       192.124 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
UMU 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]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
? 'C26 H32 N12 O8' 640.608 
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        UMU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UMU 
_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 UMU 1  302 1  UMU DRG A . 
D 4 HOH 1  401 1  HOH HOH A . 
D 4 HOH 2  402 20 HOH HOH A . 
D 4 HOH 3  403 55 HOH HOH A . 
D 4 HOH 4  404 9  HOH HOH A . 
D 4 HOH 5  405 41 HOH HOH A . 
D 4 HOH 6  406 32 HOH HOH A . 
D 4 HOH 7  407 24 HOH HOH A . 
D 4 HOH 8  408 21 HOH HOH A . 
D 4 HOH 9  409 15 HOH HOH A . 
D 4 HOH 10 410 28 HOH HOH A . 
D 4 HOH 11 411 14 HOH HOH A . 
D 4 HOH 12 412 38 HOH HOH A . 
D 4 HOH 13 413 23 HOH HOH A . 
D 4 HOH 14 414 12 HOH HOH A . 
D 4 HOH 15 415 30 HOH HOH A . 
D 4 HOH 16 416 35 HOH HOH A . 
D 4 HOH 17 417 31 HOH HOH A . 
D 4 HOH 18 418 56 HOH HOH A . 
D 4 HOH 19 419 8  HOH HOH A . 
D 4 HOH 20 420 6  HOH HOH A . 
D 4 HOH 21 421 42 HOH HOH A . 
D 4 HOH 22 422 11 HOH HOH A . 
D 4 HOH 23 423 18 HOH HOH A . 
D 4 HOH 24 424 22 HOH HOH A . 
D 4 HOH 25 425 17 HOH HOH A . 
D 4 HOH 26 426 27 HOH HOH A . 
D 4 HOH 27 427 4  HOH HOH A . 
D 4 HOH 28 428 3  HOH HOH A . 
D 4 HOH 29 429 5  HOH HOH A . 
D 4 HOH 30 430 19 HOH HOH A . 
D 4 HOH 31 431 26 HOH HOH A . 
D 4 HOH 32 432 52 HOH HOH A . 
D 4 HOH 33 433 40 HOH HOH A . 
D 4 HOH 34 434 7  HOH HOH A . 
D 4 HOH 35 435 2  HOH HOH A . 
D 4 HOH 36 436 54 HOH HOH A . 
D 4 HOH 37 437 50 HOH HOH A . 
D 4 HOH 38 438 39 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 ASP 28  ? CG  ? A ASP 28  CG  
2  1 Y 1 A ASP 28  ? OD1 ? A ASP 28  OD1 
3  1 Y 1 A ASP 28  ? OD2 ? A ASP 28  OD2 
4  1 Y 1 A LYS 92  ? CG  ? A LYS 92  CG  
5  1 Y 1 A LYS 92  ? CD  ? A LYS 92  CD  
6  1 Y 1 A LYS 92  ? CE  ? A LYS 92  CE  
7  1 Y 1 A LYS 92  ? NZ  ? A LYS 92  NZ  
8  1 Y 1 A LYS 114 ? CG  ? A LYS 114 CG  
9  1 Y 1 A LYS 114 ? CD  ? A LYS 114 CD  
10 1 Y 1 A LYS 114 ? CE  ? A LYS 114 CE  
11 1 Y 1 A LYS 114 ? NZ  ? A LYS 114 NZ  
12 1 Y 1 A ARG 193 ? CG  ? A ARG 193 CG  
13 1 Y 1 A ARG 193 ? CD  ? A ARG 193 CD  
14 1 Y 1 A ARG 193 ? NE  ? A ARG 193 NE  
15 1 Y 1 A ARG 193 ? CZ  ? A ARG 193 CZ  
16 1 Y 1 A ARG 193 ? NH1 ? A ARG 193 NH1 
17 1 Y 1 A ARG 193 ? NH2 ? A ARG 193 NH2 
18 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
19 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
20 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
21 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
22 1 Y 1 A ARG 249 ? CG  ? A ARG 249 CG  
23 1 Y 1 A ARG 249 ? CD  ? A ARG 249 CD  
24 1 Y 1 A ARG 249 ? NE  ? A ARG 249 NE  
25 1 Y 1 A ARG 249 ? CZ  ? A ARG 249 CZ  
26 1 Y 1 A ARG 249 ? NH1 ? A ARG 249 NH1 
27 1 Y 1 A ARG 249 ? NH2 ? A ARG 249 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                  4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                  5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QGN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.362 
_cell.length_a_esd                 ? 
_cell.length_b                     75.709 
_cell.length_b_esd                 ? 
_cell.length_c                     118.922 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         8QGN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_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                   8QGN 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.45 
_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 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-12-13 
_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   0.87260 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.87260 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QGN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.50 
_reflns.d_resolution_low                               48.59 
_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                                     9955 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.1 
_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                                0.129 
_reflns.pdbx_Rpim_I_all                                0.056 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       45015 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.115 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.50 
_reflns_shell.d_res_low                                     2.59 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           4389 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             974 
_reflns_shell.percent_possible_obs                          99.2 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.0 
_reflns_shell.pdbx_Rrim_I_all                               0.704 
_reflns_shell.pdbx_Rpim_I_all                               0.305 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.817 
_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                                  0.629 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_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                                 8QGN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.500 
_refine.ls_d_res_low                             48.590 
_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                     9953 
_refine.ls_number_reflns_R_free                  481 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.24 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2114 
_refine.ls_R_factor_R_free                       0.2658 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2087 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8A9V 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 28.18 
_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                            0.32 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.500 
_refine_hist.d_res_low                        48.590 
_refine_hist.number_atoms_solvent             38 
_refine_hist.number_atoms_total               2160 
_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        2063 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         59 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 2193 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.766  ? 2971 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.315 ? 1284 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 322  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 375  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.5000 2.59   . . 174 3119 98.00 . . . . 0.2590 . . . . . . . . . . . 0.2960 
'X-RAY DIFFRACTION' 2.8617 3.6053 . . 156 3141 98.00 . . . . 0.2263 . . . . . . . . . . . 0.2524 
'X-RAY DIFFRACTION' 3.6053 48.590 . . 151 3212 96.00 . . . . 0.1848 . . . . . . . . . . . 0.2628 
# 
_struct.entry_id                     8QGN 
_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        8QGN 
_struct_keywords.text            'tetrameric NAD-kinase, Transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NADK1_LISMO 
_struct_ref.pdbx_db_accession          Q8Y8D7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIED
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QGN 
_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 8QGN LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGN GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGN HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGN HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGN HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGN HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGN HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGN HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10660 ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  40690 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 63.3620000000 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 63.3620000000 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 GLU A 56  ? LEU A 59  ? GLU A 56  LEU A 59  5 ? 4  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P7 AA7 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 8 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? 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 
# 
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  
AA1 5 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA1 6 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA1 7 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA2 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA2 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA2 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 5 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 6 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 7 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 8 ILE A 142 ? GLY A 149 ? ILE A 142 GLY A 149 
AA3 1 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 2 ALA A 178 ? MET A 184 ? ALA A 178 MET A 184 
AA3 3 GLY A 151 ? SER A 155 ? GLY A 151 SER A 155 
AA3 4 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 5 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 6 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 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 42  ? O ILE A 42  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA1 4 5 N PHE A 64  ? N PHE A 64  O HIS A 244 ? O HIS A 244 
AA1 5 6 O PHE A 245 ? O PHE A 245 N VAL A 98  ? N VAL A 98  
AA1 6 7 N VAL A 107 ? N VAL A 107 O ALA A 116 ? O ALA A 116 
AA2 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA2 2 3 N THR A 6   ? N THR A 6   O ILE A 42  ? O ILE A 42  
AA2 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 4 5 N PHE A 64  ? N PHE A 64  O HIS A 244 ? O HIS A 244 
AA2 5 6 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA2 6 7 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 7 8 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 1 2 O PHE A 201 ? O PHE A 201 N MET A 179 ? N MET A 179 
AA3 2 3 O GLN A 180 ? O GLN A 180 N SER A 155 ? N SER A 155 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N THR A 125 ? N THR A 125 O SER A 220 ? O SER A 220 
AA3 5 6 N ILE A 219 ? N ILE A 219 O ILE A 226 ? O ILE A 226 
# 
_pdbx_entry_details.entry_id                   8QGN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 72  ? ? -101.98 -71.24  
2 1 TYR A 109 ? ? -117.23 -142.43 
3 1 ASN A 122 ? ? -95.73  -73.05  
4 1 ALA A 162 ? ? -100.17 -120.43 
5 1 ASN A 189 ? ? -147.04 -150.92 
6 1 ASN A 213 ? ? -119.83 -90.85  
7 1 ASP A 222 ? ? 59.58   -119.36 
8 1 GLU A 233 ? ? -172.14 137.23  
9 1 GLU A 237 ? ? -172.02 141.29  
# 
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 11.7181 23.1052 22.2520 0.3457 ? 0.0932  ? 0.0043  ? 0.4058 ? -0.0449 ? 0.3375 ? 2.8858 ? -0.6505 
? -1.6876 ? 2.0279 ? 1.2336 ? 5.1294 ? -0.1782 ? -0.1574 ? -0.0163 ? 0.2207  ? 0.0175  ? 0.1905  ? -0.1217 ? -0.3369 ? 0.1834  ? 
2 'X-RAY DIFFRACTION' ? refined 16.2272 25.1314 12.6756 0.2693 ? 0.0673  ? -0.0222 ? 0.3673 ? -0.0228 ? 0.4713 ? 1.4181 ? -0.2843 
? -0.5455 ? 1.8376 ? 0.7224 ? 4.8600 ? 0.0280  ? -0.2602 ? 0.2551  ? 0.0069  ? -0.0202 ? 0.0335  ? -0.6136 ? -0.1408 ? 0.0758  ? 
3 'X-RAY DIFFRACTION' ? refined 18.5855 11.4230 -5.7412 0.2068 ? 0.0390  ? -0.0163 ? 0.2306 ? 0.0300  ? 0.3172 ? 1.2988 ? -0.1399 
? -0.0251 ? 1.9204 ? 0.7547 ? 3.4376 ? 0.0237  ? 0.0950  ? 0.0548  ? -0.0612 ? -0.0507 ? 0.2131  ? 0.0589  ? -0.2685 ? 0.0327  ? 
4 'X-RAY DIFFRACTION' ? refined 27.1965 19.6975 16.1046 0.4288 ? -0.0400 ? 0.0154  ? 0.3667 ? -0.0587 ? 0.3617 ? 2.6852 ? -0.0853 
? -0.2220 ? 2.7655 ? 1.3680 ? 4.5904 ? -0.2817 ? -0.3831 ? 0.2211  ? 0.6389  ? 0.1122  ? -0.4635 ? -0.2952 ? 0.3180  ? -0.0510 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 79 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 80 through 120 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 121 through 238 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 239 through 264 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
UMU C1   C Y N 393 
UMU C2   C Y N 394 
UMU C3   C Y N 395 
UMU C4   C Y N 396 
UMU N1   N Y N 397 
UMU N2   N Y N 398 
UMU C5   C N R 399 
UMU C6   C Y N 400 
UMU C7   C N R 401 
UMU C8   C N S 402 
UMU C9   C N R 403 
UMU C10  C N N 404 
UMU C11  C N N 405 
UMU C12  C N N 406 
UMU C13  C N N 407 
UMU C14  C N N 408 
UMU C15  C N R 409 
UMU C16  C N R 410 
UMU C17  C N R 411 
UMU C18  C N S 412 
UMU C19  C N N 413 
UMU C20  C N N 414 
UMU C21  C N N 415 
UMU C22  C Y N 416 
UMU C23  C Y N 417 
UMU C24  C Y N 418 
UMU C25  C Y N 419 
UMU C26  C Y N 420 
UMU N3   N N N 421 
UMU N4   N Y N 422 
UMU N5   N Y N 423 
UMU N6   N N N 424 
UMU N7   N N N 425 
UMU N8   N Y N 426 
UMU N9   N Y N 427 
UMU N10  N Y N 428 
UMU N11  N Y N 429 
UMU N12  N N N 430 
UMU O1   O N N 431 
UMU O2   O N N 432 
UMU O3   O N N 433 
UMU O4   O N N 434 
UMU O5   O N N 435 
UMU O6   O N N 436 
UMU O7   O N N 437 
UMU O8   O N N 438 
UMU H1   H N N 439 
UMU H2   H N N 440 
UMU H3   H N N 441 
UMU H4   H N N 442 
UMU H5   H N N 443 
UMU H6   H N N 444 
UMU H7   H N N 445 
UMU H8   H N N 446 
UMU H9   H N N 447 
UMU H10  H N N 448 
UMU H11  H N N 449 
UMU H12  H N N 450 
UMU H13  H N N 451 
UMU H14  H N N 452 
UMU H15  H N N 453 
UMU H16  H N N 454 
UMU H17  H N N 455 
UMU H18  H N N 456 
UMU H19  H N N 457 
UMU H20  H N N 458 
UMU H21  H N N 459 
UMU H22  H N N 460 
UMU H23  H N N 461 
UMU H24  H N N 462 
UMU H25  H N N 463 
UMU H26  H N N 464 
UMU H27  H N N 465 
UMU H28  H N N 466 
UMU H29  H N N 467 
UMU H30  H N N 468 
UMU H31  H N N 469 
UMU H32  H N N 470 
VAL N    N N N 471 
VAL CA   C N S 472 
VAL C    C N N 473 
VAL O    O N N 474 
VAL CB   C N N 475 
VAL CG1  C N N 476 
VAL CG2  C N N 477 
VAL OXT  O N N 478 
VAL H    H N N 479 
VAL H2   H N N 480 
VAL HA   H N N 481 
VAL HB   H N N 482 
VAL HG11 H N N 483 
VAL HG12 H N N 484 
VAL HG13 H N N 485 
VAL HG21 H N N 486 
VAL HG22 H N N 487 
VAL HG23 H N N 488 
VAL HXT  H N N 489 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
UMU N12 C26  sing N N 378 
UMU N9  C23  sing Y N 379 
UMU N9  C22  doub Y N 380 
UMU C26 C23  doub Y N 381 
UMU C26 N11  sing Y N 382 
UMU C23 C24  sing Y N 383 
UMU C22 N8   sing Y N 384 
UMU O1  C7   sing N N 385 
UMU C7  C8   sing N N 386 
UMU C7  C5   sing N N 387 
UMU N11 C25  doub Y N 388 
UMU O2  C8   sing N N 389 
UMU C24 N8   sing Y N 390 
UMU C24 N10  doub Y N 391 
UMU N8  C5   sing N N 392 
UMU C8  C9   sing N N 393 
UMU C25 N10  sing Y N 394 
UMU C5  O3   sing N N 395 
UMU O3  C9   sing N N 396 
UMU C9  C10  sing N N 397 
UMU C11 C12  sing N N 398 
UMU C10 O4   sing N N 399 
UMU C12 N6   sing N N 400 
UMU N6  C13  sing N N 401 
UMU N3  C3   sing N N 402 
UMU O4  C21  sing N N 403 
UMU C3  N1   doub Y N 404 
UMU C3  C2   sing Y N 405 
UMU N4  C2   sing Y N 406 
UMU N4  C4   doub Y N 407 
UMU N1  C6   sing Y N 408 
UMU C2  C1   doub Y N 409 
UMU C13 N7   sing N N 410 
UMU C13 O5   doub N N 411 
UMU N7  C14  sing N N 412 
UMU C19 C4   sing N N 413 
UMU C19 C20  trip N N 414 
UMU C4  N5   sing Y N 415 
UMU C20 C21  sing N N 416 
UMU C6  N2   doub Y N 417 
UMU C1  N5   sing Y N 418 
UMU C1  N2   sing Y N 419 
UMU N5  C16  sing N N 420 
UMU O6  C16  sing N N 421 
UMU O6  C15  sing N N 422 
UMU C14 C15  sing N N 423 
UMU C16 C17  sing N N 424 
UMU C15 C18  sing N N 425 
UMU C17 C18  sing N N 426 
UMU C17 O7   sing N N 427 
UMU C18 O8   sing N N 428 
UMU C5  H1   sing N N 429 
UMU C6  H2   sing N N 430 
UMU C7  H3   sing N N 431 
UMU C8  H4   sing N N 432 
UMU C9  H5   sing N N 433 
UMU C10 H6   sing N N 434 
UMU C10 H7   sing N N 435 
UMU C11 H8   sing N N 436 
UMU C11 H9   sing N N 437 
UMU C11 H10  sing N N 438 
UMU C12 H11  sing N N 439 
UMU C12 H12  sing N N 440 
UMU C14 H13  sing N N 441 
UMU C14 H14  sing N N 442 
UMU C15 H15  sing N N 443 
UMU C16 H16  sing N N 444 
UMU C17 H17  sing N N 445 
UMU C18 H18  sing N N 446 
UMU C21 H19  sing N N 447 
UMU C21 H20  sing N N 448 
UMU C22 H21  sing N N 449 
UMU C25 H22  sing N N 450 
UMU N3  H23  sing N N 451 
UMU N3  H24  sing N N 452 
UMU N6  H25  sing N N 453 
UMU N7  H26  sing N N 454 
UMU N12 H27  sing N N 455 
UMU N12 H28  sing N N 456 
UMU O1  H29  sing N N 457 
UMU O2  H30  sing N N 458 
UMU O7  H31  sing N N 459 
UMU O8  H32  sing N N 460 
VAL N   CA   sing N N 461 
VAL N   H    sing N N 462 
VAL N   H2   sing N N 463 
VAL CA  C    sing N N 464 
VAL CA  CB   sing N N 465 
VAL CA  HA   sing N N 466 
VAL C   O    doub N N 467 
VAL C   OXT  sing N N 468 
VAL CB  CG1  sing N N 469 
VAL CB  CG2  sing N N 470 
VAL CB  HB   sing N N 471 
VAL CG1 HG11 sing N N 472 
VAL CG1 HG12 sing N N 473 
VAL CG1 HG13 sing N N 474 
VAL CG2 HG21 sing N N 475 
VAL CG2 HG22 sing N N 476 
VAL CG2 HG23 sing N N 477 
VAL OXT HXT  sing N N 478 
# 
_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' 
# 
_atom_sites.entry_id                    8QGN 
_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]   0.015782 
_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]   0.013208 
_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]   0.008409 
_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 
C 
N 
O 
S 
# 
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   ? 10.880 37.044 25.939  0.60 54.42  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 11.048 36.498 24.598  0.60 52.55  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 10.125 35.302 24.388  0.60 52.37  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 10.079 34.392 25.215  0.60 51.72  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 12.506 36.099 24.361  0.60 50.18  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.764 35.458 23.008  0.60 48.07  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.508 35.502 22.555  0.40 47.02  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.249 34.758 24.005  0.30 45.52  ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.388  35.312 23.280  1.00 53.03  ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.432  34.249 23.007  1.00 50.89  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 9.147  32.936 22.717  1.00 48.20  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 10.163 32.902 22.018  1.00 47.05  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.535  34.633 21.833  0.80 50.76  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.578  35.769 22.143  0.70 52.91  ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.522  35.915 21.067  0.60 53.65  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.500  36.965 21.455  0.50 56.83  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.402  37.058 20.457  0.50 58.51  ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.601  31.847 23.257  1.00 47.36  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.196  30.528 23.105  1.00 44.82  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 8.106  29.470 23.198  1.00 46.15  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.999  29.731 23.675  1.00 49.57  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.266 30.265 24.174  1.00 41.80  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.679  29.860 25.505  1.00 39.33  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 9.156  30.809 26.372  1.00 40.30  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.643  28.526 25.892  1.00 35.92  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.615  30.441 27.588  1.00 39.17  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 9.101  28.148 27.105  1.00 36.24  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.591  29.108 27.951  1.00 37.15  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 8.054  28.729 29.163  1.00 37.28  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.436  28.266 22.738  1.00 43.52  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.590  27.102 22.946  1.00 42.04  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.476  25.885 23.153  1.00 39.70  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.663  25.893 22.816  1.00 38.97  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.625  26.874 21.773  1.00 42.70  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.261  26.319 20.505  1.00 42.16  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.281  24.515 20.425  1.00 43.51  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.657  24.125 21.069  0.80 44.55  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.887  24.836 23.721  1.00 41.05  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.597  23.591 23.991  1.00 41.72  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.748  22.427 23.497  1.00 44.94  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.578  22.299 23.877  1.00 46.17  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.924  23.424 25.489  1.00 40.95  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.661  24.655 26.026  1.00 40.04  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.758  22.168 25.709  1.00 39.52  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.970  24.590 27.508  1.00 40.49  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.329  21.592 22.638  1.00 46.69  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.721  20.345 22.194  1.00 48.24  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.423  19.178 22.877  1.00 48.02  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.610  19.255 23.210  1.00 48.35  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 7.796  20.183 20.668  1.00 49.68  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 7.142  18.969 20.277  1.00 53.37  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 9.237  20.137 20.203  1.00 48.12  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.679  18.096 23.090  1.00 47.32  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 8.151  16.984 23.901  1.00 48.29  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.850  15.664 23.208  1.00 51.84  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.851  15.529 22.496  1.00 53.31  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.505  17.003 25.294  1.00 49.49  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.307  15.692 25.790  1.00 51.78  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.726  14.683 23.443  1.00 54.08  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.533  13.347 22.887  1.00 58.12  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.211  12.730 23.330  1.00 63.74  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.636  11.905 22.609  1.00 63.72  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.711  12.452 23.288  1.00 58.26  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.598  11.004 22.851  1.00 59.97  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.800 10.204 23.314  1.00 61.82  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.671 8.759  22.897  0.94 65.66  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 10.514 8.650  21.428  0.93 65.01  ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.702  13.128 24.493  1.00 69.68  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.453  12.611 25.002  1.00 73.00  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.597  11.574 26.094  1.00 74.90  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.593  11.216 26.722  1.00 78.05  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.807  11.082 26.338  1.00 70.13  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.010  10.141 27.424  1.00 69.15  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.102  10.889 28.754  1.00 67.92  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.113  12.122 28.810  1.00 67.40  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.258  9.294  27.168  1.00 67.94  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.536  10.087 27.283  0.64 65.00  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 10.490 9.589  27.917  0.64 66.07  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 9.580  11.215 26.755  0.62 62.69  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.163  10.120 29.840  1.00 67.55  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.069  10.709 31.172  1.00 65.91  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.222  11.668 31.447  1.00 63.58  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.013  12.777 31.951  1.00 63.03  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.024  9.602  32.222  1.00 67.59  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 6.938  10.113 33.637  1.00 66.16  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 6.603  9.019  34.624  0.40 68.83  ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 5.794  8.127  34.284  0.40 70.48  ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 7.156  9.052  35.742  0.40 69.38  ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.451  11.258 31.124  1.00 63.45  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.613 12.080 31.450  1.00 61.65  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.582 13.413 30.710  1.00 58.36  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.951 14.452 31.270  1.00 57.19  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.899 11.316 31.131  0.80 61.44  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.174 12.078 31.453  0.60 60.47  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.407 11.255 31.113  0.60 61.90  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.686 11.979 31.505  0.50 62.32  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 16.902 11.174 31.192  0.50 63.84  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.129 13.408 29.456  1.00 57.53  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.151 14.625 28.651  1.00 54.41  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.022  15.573 29.036  1.00 53.76  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.234  16.785 29.150  1.00 52.04  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.069 14.269 27.168  1.00 53.23  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.090 13.351 26.819  1.00 53.76  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.812  15.039 29.226  1.00 55.50  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.688  15.883 29.621  1.00 55.80  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 6.964  16.586 30.944  1.00 54.20  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.689  17.783 31.087  1.00 51.90  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.407  15.051 29.714  1.00 60.46  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.814  14.726 28.352  1.00 62.96  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.317  15.253 27.339  1.00 61.99  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.841  13.942 28.293  1.00 66.40  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.520  15.861 31.919  1.00 55.81  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 7.828  16.470 33.208  1.00 56.58  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 8.935  17.506 33.076  1.00 52.87  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 8.868  18.574 33.694  1.00 52.11  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.214  15.390 34.217  1.00 59.72  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.129  14.363 34.549  0.78 63.23  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 7.650  13.333 35.540  0.74 66.14  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 5.883  15.053 35.086  0.74 64.41  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 9.962  17.207 32.277  1.00 51.30  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.024 18.181 32.053  1.00 50.43  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.480 19.436 31.382  1.00 48.55  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 10.937 20.549 31.667  1.00 49.13  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.142 17.557 31.217  1.00 50.37  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.369 18.437 30.973  1.00 50.42  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.001 18.842 32.296  1.00 51.07  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.380 17.725 30.085  1.00 49.86  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.487  19.279 30.502  1.00 45.65  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 8.899  20.441 29.845  1.00 43.23  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.145  21.316 30.839  1.00 44.39  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.218  22.549 30.768  1.00 44.40  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 7.977  19.993 28.713  1.00 43.25  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.236  21.131 28.041  1.00 42.63  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.452  20.641 26.840  1.00 41.53  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.631  21.697 26.259  1.00 40.74  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.410  22.006 26.682  1.00 42.17  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.868  21.340 27.691  1.00 42.33  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.730  22.982 26.096  1.00 43.74  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.426  20.698 31.779  1.00 45.18  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.685  21.471 32.772  1.00 46.22  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.624  22.218 33.708  1.00 46.94  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.339  23.353 34.108  1.00 47.82  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.759  20.556 33.571  0.80 47.16  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.567  19.961 32.824  0.60 46.51  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.708  19.149 33.779  0.60 48.82  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.752  21.060 32.164  0.60 44.74  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.748  21.597 34.072  1.00 46.55  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.698  22.251 34.967  1.00 46.10  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.322 23.476 34.314  1.00 43.80  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.501 24.514 34.964  1.00 43.94  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.778 21.259 35.395  1.00 48.23  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.482 20.622 36.739  1.00 51.99  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.462  20.912 37.366  1.00 54.49  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.376 19.752 37.192  1.00 53.42  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.665 23.375 33.029  1.00 42.49  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.247 24.518 32.335  1.00 42.28  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.228 25.639 32.166  1.00 43.44  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.564 26.818 32.326  1.00 44.68  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.801 24.081 30.981  1.00 42.49  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 12.865 23.001 31.076  1.00 45.10  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.580 22.575 29.477  1.00 45.97  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.438 24.095 29.072  1.00 44.77  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 8.981  25.291 31.840  1.00 44.65  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 7.925  26.298 31.742  1.00 45.05  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 7.745  27.011 33.074  1.00 46.74  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.591  28.238 33.124  1.00 48.39  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.611  25.653 31.266  1.00 44.44  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.733  25.192 29.811  1.00 43.84  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.454  26.626 31.414  1.00 45.17  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.534  24.408 29.318  1.00 44.06  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 7.754  26.255 34.174  1.00 47.21  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 7.715  26.872 35.495  1.00 48.67  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 8.969  27.701 35.745  1.00 49.38  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 8.901  28.779 36.348  1.00 50.76  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.551  25.798 36.570  1.00 49.02  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.123 27.216 35.282  1.00 47.98  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.347 27.986 35.429  1.00 47.71  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.336 29.253 34.597  1.00 47.66  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.780 30.311 35.052  1.00 49.95  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.825 29.165 33.365  1.00 45.58  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.706 30.348 32.521  1.00 43.44  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.711  31.354 33.080  1.00 44.47  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.781  32.539 32.733  1.00 44.35  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.294 29.949 31.102  0.90 40.61  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.420 29.407 30.269  0.80 38.17  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 11.329 28.159 29.678  0.80 35.33  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 12.572 30.147 30.080  0.80 36.88  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 12.364 27.661 28.909  0.80 34.19  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 13.616 29.657 29.314  0.80 43.86  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.512 28.411 28.727  0.80 34.37  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.784  30.910 33.929  1.00 46.63  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.864  31.827 34.578  1.00 50.34  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.533  32.808 35.519  1.00 53.80  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.892  33.783 35.931  1.00 55.46  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.799  32.579 35.863  1.00 55.32  ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.563 33.473 36.720  1.00 57.57  ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.373 34.492 35.928  1.00 56.20  ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 12.238 35.161 36.502  1.00 55.39  ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.495 32.665 37.632  1.00 58.85  ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.864 31.417 38.243  1.00 58.85  ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.746  31.730 39.224  1.00 60.19  ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 8.927  30.829 39.504  1.00 60.58  ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 9.687  32.875 39.719  1.00 61.18  ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.110 34.629 34.629  1.00 55.56  ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.828 35.565 33.779  1.00 56.10  ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.840 36.252 32.848  1.00 59.76  ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.637  35.972 32.865  1.00 60.43  ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.922 34.862 32.967  1.00 51.70  ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 14.028 34.257 33.797  1.00 49.83  ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 15.087 35.033 34.246  1.00 51.42  ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 14.019 32.907 34.122  1.00 47.67  ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 16.103 34.484 34.998  1.00 51.21  ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 15.030 32.350 34.876  1.00 48.19  ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 16.070 33.142 35.310  1.00 50.64  ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 17.081 32.590 36.062  1.00 53.38  ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 11.363 37.155 32.017  0.87 62.46  ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.567 37.825 30.989  0.87 63.03  ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 10.441 36.925 29.757  0.87 61.56  ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.865 37.253 28.649  0.87 62.04  ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 11.181 39.174 30.636  0.87 64.47  ? 28  ASP A CB  1 
ATOM   221  N N   . MET A 1 29  ? 9.846  35.757 29.984  1.00 60.70  ? 29  MET A N   1 
ATOM   222  C CA  . MET A 1 29  ? 9.606  34.765 28.947  1.00 58.67  ? 29  MET A CA  1 
ATOM   223  C C   . MET A 1 29  ? 8.110  34.515 28.826  1.00 60.58  ? 29  MET A C   1 
ATOM   224  O O   . MET A 1 29  ? 7.411  34.358 29.834  1.00 62.94  ? 29  MET A O   1 
ATOM   225  C CB  . MET A 1 29  ? 10.329 33.448 29.255  0.92 56.71  ? 29  MET A CB  1 
ATOM   226  C CG  . MET A 1 29  ? 11.845 33.527 29.191  0.76 57.55  ? 29  MET A CG  1 
ATOM   227  S SD  . MET A 1 29  ? 12.439 33.837 27.521  0.75 57.91  ? 29  MET A SD  1 
ATOM   228  C CE  . MET A 1 29  ? 14.133 33.286 27.667  0.56 57.13  ? 29  MET A CE  1 
ATOM   229  N N   . GLU A 1 30  ? 7.624  34.477 27.590  1.00 59.40  ? 30  GLU A N   1 
ATOM   230  C CA  . GLU A 1 30  ? 6.218  34.240 27.298  1.00 58.51  ? 30  GLU A CA  1 
ATOM   231  C C   . GLU A 1 30  ? 6.090  32.999 26.428  1.00 55.03  ? 30  GLU A C   1 
ATOM   232  O O   . GLU A 1 30  ? 6.737  32.903 25.380  1.00 55.52  ? 30  GLU A O   1 
ATOM   233  C CB  . GLU A 1 30  ? 5.594  35.447 26.593  1.00 60.32  ? 30  GLU A CB  1 
ATOM   234  C CG  . GLU A 1 30  ? 4.178  35.210 26.098  1.00 61.62  ? 30  GLU A CG  1 
ATOM   235  C CD  . GLU A 1 30  ? 3.635  36.379 25.300  0.75 64.88  ? 30  GLU A CD  1 
ATOM   236  O OE1 . GLU A 1 30  ? 4.195  37.490 25.414  0.72 66.19  ? 30  GLU A OE1 1 
ATOM   237  O OE2 . GLU A 1 30  ? 2.652  36.184 24.554  0.71 66.36  ? 30  GLU A OE2 1 
ATOM   238  N N   . TYR A 1 31  ? 5.257  32.055 26.858  1.00 52.50  ? 31  TYR A N   1 
ATOM   239  C CA  . TYR A 1 31  ? 5.026  30.847 26.077  1.00 49.20  ? 31  TYR A CA  1 
ATOM   240  C C   . TYR A 1 31  ? 4.063  31.162 24.939  1.00 50.07  ? 31  TYR A C   1 
ATOM   241  O O   . TYR A 1 31  ? 2.919  31.567 25.175  1.00 50.54  ? 31  TYR A O   1 
ATOM   242  C CB  . TYR A 1 31  ? 4.480  29.719 26.953  1.00 48.10  ? 31  TYR A CB  1 
ATOM   243  C CG  . TYR A 1 31  ? 4.483  28.369 26.260  1.00 47.78  ? 31  TYR A CG  1 
ATOM   244  C CD1 . TYR A 1 31  ? 3.490  28.031 25.349  1.00 48.90  ? 31  TYR A CD1 1 
ATOM   245  C CD2 . TYR A 1 31  ? 5.486  27.440 26.507  1.00 47.54  ? 31  TYR A CD2 1 
ATOM   246  C CE1 . TYR A 1 31  ? 3.491  26.810 24.707  1.00 49.07  ? 31  TYR A CE1 1 
ATOM   247  C CE2 . TYR A 1 31  ? 5.496  26.212 25.868  1.00 47.60  ? 31  TYR A CE2 1 
ATOM   248  C CZ  . TYR A 1 31  ? 4.495  25.904 24.970  1.00 48.91  ? 31  TYR A CZ  1 
ATOM   249  O OH  . TYR A 1 31  ? 4.493  24.686 24.330  1.00 49.98  ? 31  TYR A OH  1 
ATOM   250  N N   . ASP A 1 32  ? 4.527  30.973 23.706  1.00 49.98  ? 32  ASP A N   1 
ATOM   251  C CA  . ASP A 1 32  ? 3.705  31.163 22.514  1.00 52.54  ? 32  ASP A CA  1 
ATOM   252  C C   . ASP A 1 32  ? 4.167  30.154 21.475  1.00 52.58  ? 32  ASP A C   1 
ATOM   253  O O   . ASP A 1 32  ? 5.272  30.279 20.940  1.00 52.26  ? 32  ASP A O   1 
ATOM   254  C CB  . ASP A 1 32  ? 3.819  32.594 21.982  1.00 54.78  ? 32  ASP A CB  1 
ATOM   255  C CG  . ASP A 1 32  ? 2.952  32.840 20.757  0.73 58.37  ? 32  ASP A CG  1 
ATOM   256  O OD1 . ASP A 1 32  ? 2.154  31.951 20.392  0.73 59.62  ? 32  ASP A OD1 1 
ATOM   257  O OD2 . ASP A 1 32  ? 3.070  33.929 20.159  0.73 60.51  ? 32  ASP A OD2 1 
ATOM   258  N N   . ASP A 1 33  ? 3.337  29.152 21.195  1.00 53.11  ? 33  ASP A N   1 
ATOM   259  C CA  . ASP A 1 33  ? 3.658  28.168 20.171  1.00 53.89  ? 33  ASP A CA  1 
ATOM   260  C C   . ASP A 1 33  ? 3.126  28.551 18.796  1.00 54.50  ? 33  ASP A C   1 
ATOM   261  O O   . ASP A 1 33  ? 3.271  27.770 17.851  1.00 54.02  ? 33  ASP A O   1 
ATOM   262  C CB  . ASP A 1 33  ? 3.130  26.782 20.574  1.00 53.81  ? 33  ASP A CB  1 
ATOM   263  C CG  . ASP A 1 33  ? 1.641  26.778 20.872  1.00 56.13  ? 33  ASP A CG  1 
ATOM   264  O OD1 . ASP A 1 33  ? 0.963  27.787 20.587  1.00 58.30  ? 33  ASP A OD1 1 
ATOM   265  O OD2 . ASP A 1 33  ? 1.147  25.758 21.399  1.00 56.93  ? 33  ASP A OD2 1 
ATOM   266  N N   . VAL A 1 34  ? 2.509  29.721 18.664  1.00 55.80  ? 34  VAL A N   1 
ATOM   267  C CA  . VAL A 1 34  ? 2.075  30.210 17.359  1.00 57.67  ? 34  VAL A CA  1 
ATOM   268  C C   . VAL A 1 34  ? 3.179  31.001 16.676  1.00 58.42  ? 34  VAL A C   1 
ATOM   269  O O   . VAL A 1 34  ? 3.540  30.726 15.528  1.00 59.96  ? 34  VAL A O   1 
ATOM   270  C CB  . VAL A 1 34  ? 0.793  31.056 17.507  1.00 60.76  ? 34  VAL A CB  1 
ATOM   271  C CG1 . VAL A 1 34  ? 0.299  31.504 16.142  1.00 61.50  ? 34  VAL A CG1 1 
ATOM   272  C CG2 . VAL A 1 34  ? -0.279 30.270 18.244  1.00 61.67  ? 34  VAL A CG2 1 
ATOM   273  N N   . GLU A 1 35  ? 3.731  31.993 17.372  1.00 58.49  ? 35  GLU A N   1 
ATOM   274  C CA  . GLU A 1 35  ? 4.857  32.782 16.871  1.00 58.11  ? 35  GLU A CA  1 
ATOM   275  C C   . GLU A 1 35  ? 5.997  32.785 17.884  1.00 54.38  ? 35  GLU A C   1 
ATOM   276  O O   . GLU A 1 35  ? 6.337  33.829 18.449  1.00 54.02  ? 35  GLU A O   1 
ATOM   277  C CB  . GLU A 1 35  ? 4.417  34.211 16.556  1.00 63.46  ? 35  GLU A CB  1 
ATOM   278  C CG  . GLU A 1 35  ? 3.257  34.320 15.588  0.88 68.63  ? 35  GLU A CG  1 
ATOM   279  C CD  . GLU A 1 35  ? 2.872  35.760 15.312  0.85 74.57  ? 35  GLU A CD  1 
ATOM   280  O OE1 . GLU A 1 35  ? 3.108  36.235 14.180  0.85 76.73  ? 35  GLU A OE1 1 
ATOM   281  O OE2 . GLU A 1 35  ? 2.341  36.420 16.231  0.85 77.23  ? 35  GLU A OE2 1 
ATOM   282  N N   . PRO A 1 36  ? 6.620  31.634 18.140  1.00 51.19  ? 36  PRO A N   1 
ATOM   283  C CA  . PRO A 1 36  ? 7.786  31.628 19.024  1.00 48.61  ? 36  PRO A CA  1 
ATOM   284  C C   . PRO A 1 36  ? 9.022  32.127 18.297  1.00 47.71  ? 36  PRO A C   1 
ATOM   285  O O   . PRO A 1 36  ? 9.108  32.126 17.067  1.00 51.44  ? 36  PRO A O   1 
ATOM   286  C CB  . PRO A 1 36  ? 7.936  30.156 19.414  1.00 46.81  ? 36  PRO A CB  1 
ATOM   287  C CG  . PRO A 1 36  ? 7.409  29.422 18.247  1.00 47.12  ? 36  PRO A CG  1 
ATOM   288  C CD  . PRO A 1 36  ? 6.306  30.277 17.656  1.00 49.73  ? 36  PRO A CD  1 
ATOM   289  N N   . GLU A 1 37  ? 9.989  32.571 19.094  1.00 44.75  ? 37  GLU A N   1 
ATOM   290  C CA  . GLU A 1 37  ? 11.313 32.895 18.597  1.00 43.35  ? 37  GLU A CA  1 
ATOM   291  C C   . GLU A 1 37  ? 12.359 31.887 19.039  1.00 40.33  ? 37  GLU A C   1 
ATOM   292  O O   . GLU A 1 37  ? 13.412 31.789 18.403  1.00 39.48  ? 37  GLU A O   1 
ATOM   293  C CB  . GLU A 1 37  ? 11.718 34.301 19.060  1.00 45.55  ? 37  GLU A CB  1 
ATOM   294  C CG  . GLU A 1 37  ? 10.613 35.334 18.851  0.60 48.63  ? 37  GLU A CG  1 
ATOM   295  C CD  . GLU A 1 37  ? 11.077 36.760 19.089  0.60 51.37  ? 37  GLU A CD  1 
ATOM   296  O OE1 . GLU A 1 37  ? 12.144 36.947 19.711  0.55 51.11  ? 37  GLU A OE1 1 
ATOM   297  O OE2 . GLU A 1 37  ? 10.376 37.697 18.647  0.55 53.26  ? 37  GLU A OE2 1 
ATOM   298  N N   . ILE A 1 38  ? 12.085 31.141 20.105  1.00 39.40  ? 38  ILE A N   1 
ATOM   299  C CA  . ILE A 1 38  ? 12.909 30.025 20.546  1.00 38.35  ? 38  ILE A CA  1 
ATOM   300  C C   . ILE A 1 38  ? 12.036 28.779 20.549  1.00 38.10  ? 38  ILE A C   1 
ATOM   301  O O   . ILE A 1 38  ? 10.963 28.770 21.162  1.00 38.33  ? 38  ILE A O   1 
ATOM   302  C CB  . ILE A 1 38  ? 13.509 30.277 21.942  1.00 39.31  ? 38  ILE A CB  1 
ATOM   303  C CG1 . ILE A 1 38  ? 14.356 31.551 21.938  1.00 40.92  ? 38  ILE A CG1 1 
ATOM   304  C CG2 . ILE A 1 38  ? 14.335 29.081 22.392  1.00 38.55  ? 38  ILE A CG2 1 
ATOM   305  C CD1 . ILE A 1 38  ? 15.489 31.521 20.949  1.00 40.08  ? 38  ILE A CD1 1 
ATOM   306  N N   . VAL A 1 39  ? 12.480 27.740 19.850  1.00 37.29  ? 39  VAL A N   1 
ATOM   307  C CA  . VAL A 1 39  ? 11.802 26.449 19.836  1.00 35.15  ? 39  VAL A CA  1 
ATOM   308  C C   . VAL A 1 39  ? 12.714 25.436 20.510  1.00 35.82  ? 39  VAL A C   1 
ATOM   309  O O   . VAL A 1 39  ? 13.821 25.167 20.027  1.00 35.73  ? 39  VAL A O   1 
ATOM   310  C CB  . VAL A 1 39  ? 11.436 26.004 18.412  1.00 32.48  ? 39  VAL A CB  1 
ATOM   311  C CG1 . VAL A 1 39  ? 11.069 24.528 18.396  1.00 31.75  ? 39  VAL A CG1 1 
ATOM   312  C CG2 . VAL A 1 39  ? 10.278 26.832 17.893  1.00 33.69  ? 39  VAL A CG2 1 
ATOM   313  N N   . ILE A 1 40  ? 12.251 24.872 21.622  1.00 36.16  ? 40  ILE A N   1 
ATOM   314  C CA  . ILE A 1 40  ? 13.005 23.890 22.393  1.00 36.21  ? 40  ILE A CA  1 
ATOM   315  C C   . ILE A 1 40  ? 12.377 22.522 22.171  1.00 35.66  ? 40  ILE A C   1 
ATOM   316  O O   . ILE A 1 40  ? 11.173 22.343 22.384  1.00 37.34  ? 40  ILE A O   1 
ATOM   317  C CB  . ILE A 1 40  ? 13.032 24.250 23.889  1.00 36.80  ? 40  ILE A CB  1 
ATOM   318  C CG1 . ILE A 1 40  ? 13.605 25.654 24.089  1.00 38.13  ? 40  ILE A CG1 1 
ATOM   319  C CG2 . ILE A 1 40  ? 13.833 23.221 24.683  1.00 35.89  ? 40  ILE A CG2 1 
ATOM   320  C CD1 . ILE A 1 40  ? 13.698 26.071 25.540  1.00 39.94  ? 40  ILE A CD1 1 
ATOM   321  N N   . SER A 1 41  ? 13.191 21.561 21.746  1.00 34.01  ? 41  SER A N   1 
ATOM   322  C CA  . SER A 1 41  ? 12.740 20.203 21.466  1.00 35.98  ? 41  SER A CA  1 
ATOM   323  C C   . SER A 1 41  ? 13.294 19.268 22.534  1.00 37.19  ? 41  SER A C   1 
ATOM   324  O O   . SER A 1 41  ? 14.513 19.181 22.715  1.00 36.35  ? 41  SER A O   1 
ATOM   325  C CB  . SER A 1 41  ? 13.185 19.757 20.073  1.00 38.15  ? 41  SER A CB  1 
ATOM   326  O OG  . SER A 1 41  ? 12.790 18.422 19.808  1.00 40.47  ? 41  SER A OG  1 
ATOM   327  N N   . ILE A 1 42  ? 12.403 18.577 23.237  1.00 38.64  ? 42  ILE A N   1 
ATOM   328  C CA  . ILE A 1 42  ? 12.781 17.630 24.280  1.00 39.90  ? 42  ILE A CA  1 
ATOM   329  C C   . ILE A 1 42  ? 12.437 16.232 23.781  1.00 41.05  ? 42  ILE A C   1 
ATOM   330  O O   . ILE A 1 42  ? 11.258 15.882 23.648  1.00 42.56  ? 42  ILE A O   1 
ATOM   331  C CB  . ILE A 1 42  ? 12.083 17.933 25.613  1.00 39.65  ? 42  ILE A CB  1 
ATOM   332  C CG1 . ILE A 1 42  ? 12.452 19.334 26.107  1.00 38.61  ? 42  ILE A CG1 1 
ATOM   333  C CG2 . ILE A 1 42  ? 12.460 16.899 26.652  1.00 40.84  ? 42  ILE A CG2 1 
ATOM   334  C CD1 . ILE A 1 42  ? 11.888 19.670 27.475  1.00 39.39  ? 42  ILE A CD1 1 
ATOM   335  N N   . GLY A 1 43  ? 13.463 15.431 23.507  1.00 39.38  ? 43  GLY A N   1 
ATOM   336  C CA  . GLY A 1 43  ? 13.263 14.085 23.007  1.00 40.29  ? 43  GLY A CA  1 
ATOM   337  C C   . GLY A 1 43  ? 14.467 13.543 22.263  1.00 39.86  ? 43  GLY A C   1 
ATOM   338  O O   . GLY A 1 43  ? 15.543 13.379 22.844  1.00 41.32  ? 43  GLY A O   1 
ATOM   339  N N   . GLY A 1 44  ? 14.295 13.249 20.976  1.00 38.46  ? 44  GLY A N   1 
ATOM   340  C CA  . GLY A 1 44  ? 15.398 12.810 20.143  1.00 37.36  ? 44  GLY A CA  1 
ATOM   341  C C   . GLY A 1 44  ? 15.480 13.601 18.854  1.00 35.76  ? 44  GLY A C   1 
ATOM   342  O O   . GLY A 1 44  ? 14.852 14.659 18.738  1.00 33.86  ? 44  GLY A O   1 
ATOM   343  N N   . ASP A 1 45  ? 16.254 13.110 17.880  1.00 35.55  ? 45  ASP A N   1 
ATOM   344  C CA  . ASP A 1 45  ? 16.297 13.764 16.575  1.00 33.72  ? 45  ASP A CA  1 
ATOM   345  C C   . ASP A 1 45  ? 14.940 13.707 15.887  1.00 33.04  ? 45  ASP A C   1 
ATOM   346  O O   . ASP A 1 45  ? 14.570 14.626 15.145  1.00 33.04  ? 45  ASP A O   1 
ATOM   347  C CB  . ASP A 1 45  ? 17.367 13.121 15.694  1.00 33.93  ? 45  ASP A CB  1 
ATOM   348  C CG  . ASP A 1 45  ? 18.769 13.354 16.218  1.00 34.43  ? 45  ASP A CG  1 
ATOM   349  O OD1 . ASP A 1 45  ? 19.061 14.482 16.668  1.00 33.52  ? 45  ASP A OD1 1 
ATOM   350  O OD2 . ASP A 1 45  ? 19.580 12.407 16.186  1.00 35.19  ? 45  ASP A OD2 1 
ATOM   351  N N   . GLY A 1 46  ? 14.185 12.632 16.116  1.00 32.24  ? 46  GLY A N   1 
ATOM   352  C CA  . GLY A 1 46  ? 12.838 12.563 15.575  1.00 32.46  ? 46  GLY A CA  1 
ATOM   353  C C   . GLY A 1 46  ? 11.940 13.646 16.135  1.00 37.12  ? 46  GLY A C   1 
ATOM   354  O O   . GLY A 1 46  ? 11.179 14.284 15.403  1.00 37.03  ? 46  GLY A O   1 
ATOM   355  N N   . THR A 1 47  ? 12.020 13.872 17.450  1.00 36.50  ? 47  THR A N   1 
ATOM   356  C CA  . THR A 1 47  ? 11.299 14.986 18.056  1.00 34.47  ? 47  THR A CA  1 
ATOM   357  C C   . THR A 1 47  ? 11.809 16.320 17.523  1.00 32.20  ? 47  THR A C   1 
ATOM   358  O O   . THR A 1 47  ? 11.024 17.250 17.302  1.00 32.93  ? 47  THR A O   1 
ATOM   359  C CB  . THR A 1 47  ? 11.422 14.928 19.582  1.00 36.19  ? 47  THR A CB  1 
ATOM   360  O OG1 . THR A 1 47  ? 10.944 13.663 20.058  1.00 40.31  ? 47  THR A OG1 1 
ATOM   361  C CG2 . THR A 1 47  ? 10.607 16.038 20.234  1.00 33.25  ? 47  THR A CG2 1 
ATOM   362  N N   . PHE A 1 48  ? 13.122 16.428 17.288  1.00 30.95  ? 48  PHE A N   1 
ATOM   363  C CA  . PHE A 1 48  ? 13.674 17.669 16.752  1.00 31.53  ? 48  PHE A CA  1 
ATOM   364  C C   . PHE A 1 48  ? 13.281 17.866 15.293  1.00 36.38  ? 48  PHE A C   1 
ATOM   365  O O   . PHE A 1 48  ? 12.986 18.992 14.874  1.00 36.52  ? 48  PHE A O   1 
ATOM   366  C CB  . PHE A 1 48  ? 15.196 17.686 16.902  0.90 30.94  ? 48  PHE A CB  1 
ATOM   367  C CG  . PHE A 1 48  ? 15.822 19.000 16.530  0.80 30.75  ? 48  PHE A CG  1 
ATOM   368  C CD1 . PHE A 1 48  ? 15.970 20.002 17.475  0.80 30.34  ? 48  PHE A CD1 1 
ATOM   369  C CD2 . PHE A 1 48  ? 16.255 19.238 15.234  0.80 30.98  ? 48  PHE A CD2 1 
ATOM   370  C CE1 . PHE A 1 48  ? 16.541 21.211 17.135  0.80 30.10  ? 48  PHE A CE1 1 
ATOM   371  C CE2 . PHE A 1 48  ? 16.825 20.447 14.889  0.80 31.62  ? 48  PHE A CE2 1 
ATOM   372  C CZ  . PHE A 1 48  ? 16.964 21.435 15.839  0.80 31.29  ? 48  PHE A CZ  1 
ATOM   373  N N   . LEU A 1 49  ? 13.288 16.789 14.500  1.00 40.03  ? 49  LEU A N   1 
ATOM   374  C CA  . LEU A 1 49  ? 12.837 16.892 13.114  1.00 42.48  ? 49  LEU A CA  1 
ATOM   375  C C   . LEU A 1 49  ? 11.393 17.367 13.043  1.00 45.87  ? 49  LEU A C   1 
ATOM   376  O O   . LEU A 1 49  ? 11.029 18.149 12.155  1.00 43.68  ? 49  LEU A O   1 
ATOM   377  C CB  . LEU A 1 49  ? 12.992 15.545 12.405  1.00 44.88  ? 49  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 49  ? 14.248 15.281 11.566  1.00 46.94  ? 49  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 49  ? 15.289 16.369 11.757  1.00 47.24  ? 49  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 49  ? 14.838 13.919 11.899  1.00 47.87  ? 49  LEU A CD2 1 
ATOM   381  N N   . SER A 1 50  ? 10.559 16.916 13.979  1.00 50.68  ? 50  SER A N   1 
ATOM   382  C CA  . SER A 1 50  ? 9.158  17.319 13.978  1.00 53.76  ? 50  SER A CA  1 
ATOM   383  C C   . SER A 1 50  ? 9.007  18.789 14.354  1.00 51.10  ? 50  SER A C   1 
ATOM   384  O O   . SER A 1 50  ? 8.179  19.503 13.774  1.00 53.08  ? 50  SER A O   1 
ATOM   385  C CB  . SER A 1 50  ? 8.371  16.428 14.934  1.00 58.70  ? 50  SER A CB  1 
ATOM   386  O OG  . SER A 1 50  ? 8.684  15.062 14.710  1.00 62.21  ? 50  SER A OG  1 
ATOM   387  N N   . ALA A 1 51  ? 9.797  19.257 15.324  1.00 45.62  ? 51  ALA A N   1 
ATOM   388  C CA  . ALA A 1 51  ? 9.750  20.665 15.705  1.00 42.53  ? 51  ALA A CA  1 
ATOM   389  C C   . ALA A 1 51  ? 10.146 21.565 14.542  1.00 42.04  ? 51  ALA A C   1 
ATOM   390  O O   . ALA A 1 51  ? 9.548  22.627 14.339  1.00 43.45  ? 51  ALA A O   1 
ATOM   391  C CB  . ALA A 1 51  ? 10.657 20.917 16.907  1.00 40.05  ? 51  ALA A CB  1 
ATOM   392  N N   . PHE A 1 52  ? 11.157 21.157 13.770  1.00 38.97  ? 52  PHE A N   1 
ATOM   393  C CA  . PHE A 1 52  ? 11.584 21.943 12.616  1.00 37.65  ? 52  PHE A CA  1 
ATOM   394  C C   . PHE A 1 52  ? 10.468 22.054 11.585  1.00 39.46  ? 52  PHE A C   1 
ATOM   395  O O   . PHE A 1 52  ? 10.138 23.153 11.126  1.00 40.20  ? 52  PHE A O   1 
ATOM   396  C CB  . PHE A 1 52  ? 12.836 21.316 11.997  1.00 35.73  ? 52  PHE A CB  1 
ATOM   397  C CG  . PHE A 1 52  ? 13.119 21.766 10.585  1.00 35.75  ? 52  PHE A CG  1 
ATOM   398  C CD1 . PHE A 1 52  ? 13.778 22.959 10.339  1.00 35.54  ? 52  PHE A CD1 1 
ATOM   399  C CD2 . PHE A 1 52  ? 12.744 20.981 9.503   1.00 36.35  ? 52  PHE A CD2 1 
ATOM   400  C CE1 . PHE A 1 52  ? 14.044 23.364 9.042   1.00 34.72  ? 52  PHE A CE1 1 
ATOM   401  C CE2 . PHE A 1 52  ? 13.009 21.383 8.204   1.00 36.43  ? 52  PHE A CE2 1 
ATOM   402  C CZ  . PHE A 1 52  ? 13.657 22.576 7.974   1.00 35.59  ? 52  PHE A CZ  1 
ATOM   403  N N   . HIS A 1 53  ? 9.875  20.918 11.207  1.00 39.12  ? 53  HIS A N   1 
ATOM   404  C CA  . HIS A 1 53  ? 8.813  20.933 10.206  1.00 41.56  ? 53  HIS A CA  1 
ATOM   405  C C   . HIS A 1 53  ? 7.534  21.560 10.742  1.00 43.97  ? 53  HIS A C   1 
ATOM   406  O O   . HIS A 1 53  ? 6.680  21.992 9.960   1.00 44.39  ? 53  HIS A O   1 
ATOM   407  C CB  . HIS A 1 53  ? 8.529  19.517 9.713   1.00 43.82  ? 53  HIS A CB  1 
ATOM   408  C CG  . HIS A 1 53  ? 9.615  18.947 8.856   1.00 45.85  ? 53  HIS A CG  1 
ATOM   409  N ND1 . HIS A 1 53  ? 9.785  19.302 7.535   1.00 47.34  ? 53  HIS A ND1 1 
ATOM   410  C CD2 . HIS A 1 53  ? 10.585 18.044 9.130   1.00 45.38  ? 53  HIS A CD2 1 
ATOM   411  C CE1 . HIS A 1 53  ? 10.814 18.643 7.033   1.00 47.30  ? 53  HIS A CE1 1 
ATOM   412  N NE2 . HIS A 1 53  ? 11.319 17.875 7.982   1.00 46.37  ? 53  HIS A NE2 1 
ATOM   413  N N   . GLN A 1 54  ? 7.372  21.605 12.064  1.00 46.36  ? 54  GLN A N   1 
ATOM   414  C CA  . GLN A 1 54  ? 6.211  22.278 12.635  1.00 46.68  ? 54  GLN A CA  1 
ATOM   415  C C   . GLN A 1 54  ? 6.294  23.785 12.437  1.00 46.84  ? 54  GLN A C   1 
ATOM   416  O O   . GLN A 1 54  ? 5.263  24.469 12.427  1.00 49.14  ? 54  GLN A O   1 
ATOM   417  C CB  . GLN A 1 54  ? 6.085  21.931 14.122  1.00 45.33  ? 54  GLN A CB  1 
ATOM   418  C CG  . GLN A 1 54  ? 4.869  22.524 14.814  0.94 46.91  ? 54  GLN A CG  1 
ATOM   419  C CD  . GLN A 1 54  ? 4.766  22.090 16.262  0.58 47.57  ? 54  GLN A CD  1 
ATOM   420  O OE1 . GLN A 1 54  ? 5.174  20.984 16.618  0.55 47.86  ? 54  GLN A OE1 1 
ATOM   421  N NE2 . GLN A 1 54  ? 4.226  22.961 17.106  0.55 48.27  ? 54  GLN A NE2 1 
ATOM   422  N N   . TYR A 1 55  ? 7.504  24.316 12.247  1.00 45.91  ? 55  TYR A N   1 
ATOM   423  C CA  . TYR A 1 55  ? 7.732  25.754 12.176  1.00 47.26  ? 55  TYR A CA  1 
ATOM   424  C C   . TYR A 1 55  ? 8.580  26.129 10.967  1.00 50.52  ? 55  TYR A C   1 
ATOM   425  O O   . TYR A 1 55  ? 9.319  27.116 11.007  1.00 52.76  ? 55  TYR A O   1 
ATOM   426  C CB  . TYR A 1 55  ? 8.393  26.267 13.456  1.00 43.77  ? 55  TYR A CB  1 
ATOM   427  C CG  . TYR A 1 55  ? 7.516  26.174 14.681  1.00 41.93  ? 55  TYR A CG  1 
ATOM   428  C CD1 . TYR A 1 55  ? 6.512  27.103 14.906  1.00 43.32  ? 55  TYR A CD1 1 
ATOM   429  C CD2 . TYR A 1 55  ? 7.692  25.159 15.611  1.00 40.03  ? 55  TYR A CD2 1 
ATOM   430  C CE1 . TYR A 1 55  ? 5.704  27.025 16.022  1.00 44.41  ? 55  TYR A CE1 1 
ATOM   431  C CE2 . TYR A 1 55  ? 6.889  25.073 16.734  1.00 40.78  ? 55  TYR A CE2 1 
ATOM   432  C CZ  . TYR A 1 55  ? 5.897  26.010 16.935  1.00 43.67  ? 55  TYR A CZ  1 
ATOM   433  O OH  . TYR A 1 55  ? 5.093  25.931 18.049  1.00 45.30  ? 55  TYR A OH  1 
ATOM   434  N N   . GLU A 1 56  ? 8.487  25.357 9.883   1.00 50.95  ? 56  GLU A N   1 
ATOM   435  C CA  . GLU A 1 56  ? 9.271  25.672 8.695   1.00 50.89  ? 56  GLU A CA  1 
ATOM   436  C C   . GLU A 1 56  ? 8.818  26.963 8.028   1.00 50.92  ? 56  GLU A C   1 
ATOM   437  O O   . GLU A 1 56  ? 9.529  27.478 7.159   1.00 50.03  ? 56  GLU A O   1 
ATOM   438  C CB  . GLU A 1 56  ? 9.210  24.509 7.700   0.90 51.24  ? 56  GLU A CB  1 
ATOM   439  C CG  . GLU A 1 56  ? 7.832  23.894 7.536   0.80 53.48  ? 56  GLU A CG  1 
ATOM   440  C CD  . GLU A 1 56  ? 7.821  22.729 6.558   0.70 54.75  ? 56  GLU A CD  1 
ATOM   441  O OE1 . GLU A 1 56  ? 6.922  22.691 5.692   0.70 57.16  ? 56  GLU A OE1 1 
ATOM   442  O OE2 . GLU A 1 56  ? 8.711  21.857 6.652   0.70 53.57  ? 56  GLU A OE2 1 
ATOM   443  N N   . GLU A 1 57  ? 7.662  27.499 8.415   1.00 52.04  ? 57  GLU A N   1 
ATOM   444  C CA  . GLU A 1 57  ? 7.174  28.748 7.850   1.00 53.10  ? 57  GLU A CA  1 
ATOM   445  C C   . GLU A 1 57  ? 7.840  29.978 8.451   1.00 50.33  ? 57  GLU A C   1 
ATOM   446  O O   . GLU A 1 57  ? 7.696  31.071 7.891   1.00 52.08  ? 57  GLU A O   1 
ATOM   447  C CB  . GLU A 1 57  ? 5.656  28.840 8.031   1.00 56.84  ? 57  GLU A CB  1 
ATOM   448  C CG  . GLU A 1 57  ? 4.887  28.859 6.728   0.85 61.84  ? 57  GLU A CG  1 
ATOM   449  C CD  . GLU A 1 57  ? 5.409  27.838 5.737   0.81 63.17  ? 57  GLU A CD  1 
ATOM   450  O OE1 . GLU A 1 57  ? 5.476  26.639 6.088   0.54 62.06  ? 57  GLU A OE1 1 
ATOM   451  O OE2 . GLU A 1 57  ? 5.764  28.241 4.608   0.53 64.92  ? 57  GLU A OE2 1 
ATOM   452  N N   . ARG A 1 58  ? 8.553  29.842 9.569   1.00 46.97  ? 58  ARG A N   1 
ATOM   453  C CA  . ARG A 1 58  ? 9.182  30.993 10.207  1.00 47.10  ? 58  ARG A CA  1 
ATOM   454  C C   . ARG A 1 58  ? 10.604 30.653 10.634  1.00 47.74  ? 58  ARG A C   1 
ATOM   455  O O   . ARG A 1 58  ? 11.057 31.040 11.716  1.00 49.16  ? 58  ARG A O   1 
ATOM   456  C CB  . ARG A 1 58  ? 8.351  31.486 11.392  1.00 46.19  ? 58  ARG A CB  1 
ATOM   457  C CG  . ARG A 1 58  ? 6.874  31.718 11.063  0.78 47.49  ? 58  ARG A CG  1 
ATOM   458  C CD  . ARG A 1 58  ? 6.144  32.515 12.140  0.76 48.19  ? 58  ARG A CD  1 
ATOM   459  N NE  . ARG A 1 58  ? 7.056  33.271 12.989  0.75 47.10  ? 58  ARG A NE  1 
ATOM   460  C CZ  . ARG A 1 58  ? 7.429  32.879 14.202  0.72 44.30  ? 58  ARG A CZ  1 
ATOM   461  N NH1 . ARG A 1 58  ? 6.970  31.738 14.696  0.72 43.40  ? 58  ARG A NH1 1 
ATOM   462  N NH2 . ARG A 1 58  ? 8.264  33.620 14.915  0.72 42.95  ? 58  ARG A NH2 1 
ATOM   463  N N   . LEU A 1 59  ? 11.328 29.924 9.780   1.00 46.71  ? 59  LEU A N   1 
ATOM   464  C CA  . LEU A 1 59  ? 12.701 29.541 10.090  1.00 45.12  ? 59  LEU A CA  1 
ATOM   465  C C   . LEU A 1 59  ? 13.632 30.741 10.201  1.00 47.20  ? 59  LEU A C   1 
ATOM   466  O O   . LEU A 1 59  ? 14.693 30.633 10.827  1.00 47.61  ? 59  LEU A O   1 
ATOM   467  C CB  . LEU A 1 59  ? 13.225 28.572 9.031   1.00 44.01  ? 59  LEU A CB  1 
ATOM   468  C CG  . LEU A 1 59  ? 12.464 27.252 8.924   1.00 43.22  ? 59  LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 59  ? 13.010 26.416 7.784   1.00 42.47  ? 59  LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 59  ? 12.528 26.483 10.236  1.00 42.03  ? 59  LEU A CD2 1 
ATOM   471  N N   . ASP A 1 60  ? 13.265 31.879 9.609   1.00 49.63  ? 60  ASP A N   1 
ATOM   472  C CA  . ASP A 1 60  ? 14.071 33.086 9.737   1.00 52.59  ? 60  ASP A CA  1 
ATOM   473  C C   . ASP A 1 60  ? 13.814 33.825 11.043  1.00 51.73  ? 60  ASP A C   1 
ATOM   474  O O   . ASP A 1 60  ? 14.626 34.674 11.428  1.00 53.12  ? 60  ASP A O   1 
ATOM   475  C CB  . ASP A 1 60  ? 13.811 34.025 8.557   1.00 59.53  ? 60  ASP A CB  1 
ATOM   476  C CG  . ASP A 1 60  ? 12.333 34.234 8.294   1.00 65.57  ? 60  ASP A CG  1 
ATOM   477  O OD1 . ASP A 1 60  ? 11.611 33.230 8.106   1.00 66.11  ? 60  ASP A OD1 1 
ATOM   478  O OD2 . ASP A 1 60  ? 11.890 35.402 8.283   1.00 70.33  ? 60  ASP A OD2 1 
ATOM   479  N N   . GLU A 1 61  ? 12.714 33.525 11.730  1.00 49.30  ? 61  GLU A N   1 
ATOM   480  C CA  . GLU A 1 61  ? 12.388 34.165 12.996  1.00 49.12  ? 61  GLU A CA  1 
ATOM   481  C C   . GLU A 1 61  ? 12.637 33.272 14.205  1.00 47.33  ? 61  GLU A C   1 
ATOM   482  O O   . GLU A 1 61  ? 12.345 33.688 15.330  1.00 48.05  ? 61  GLU A O   1 
ATOM   483  C CB  . GLU A 1 61  ? 10.923 34.622 13.003  1.00 52.65  ? 61  GLU A CB  1 
ATOM   484  C CG  . GLU A 1 61  ? 10.596 35.734 12.019  1.00 58.04  ? 61  GLU A CG  1 
ATOM   485  C CD  . GLU A 1 61  ? 9.904  35.222 10.774  0.70 60.91  ? 61  GLU A CD  1 
ATOM   486  O OE1 . GLU A 1 61  ? 9.119  35.983 10.169  0.61 64.61  ? 61  GLU A OE1 1 
ATOM   487  O OE2 . GLU A 1 61  ? 10.139 34.054 10.404  0.61 59.53  ? 61  GLU A OE2 1 
ATOM   488  N N   . ILE A 1 62  ? 13.174 32.069 14.013  1.00 44.04  ? 62  ILE A N   1 
ATOM   489  C CA  . ILE A 1 62  ? 13.212 31.061 15.065  1.00 41.75  ? 62  ILE A CA  1 
ATOM   490  C C   . ILE A 1 62  ? 14.623 30.509 15.195  1.00 40.37  ? 62  ILE A C   1 
ATOM   491  O O   . ILE A 1 62  ? 15.268 30.194 14.188  1.00 40.46  ? 62  ILE A O   1 
ATOM   492  C CB  . ILE A 1 62  ? 12.215 29.919 14.787  1.00 40.74  ? 62  ILE A CB  1 
ATOM   493  C CG1 . ILE A 1 62  ? 10.779 30.435 14.866  1.00 42.55  ? 62  ILE A CG1 1 
ATOM   494  C CG2 . ILE A 1 62  ? 12.425 28.767 15.756  1.00 38.73  ? 62  ILE A CG2 1 
ATOM   495  C CD1 . ILE A 1 62  ? 9.742  29.389 14.554  1.00 41.14  ? 62  ILE A CD1 1 
ATOM   496  N N   . ALA A 1 63  ? 15.097 30.395 16.434  1.00 38.98  ? 63  ALA A N   1 
ATOM   497  C CA  . ALA A 1 63  ? 16.297 29.646 16.772  1.00 36.85  ? 63  ALA A CA  1 
ATOM   498  C C   . ALA A 1 63  ? 15.897 28.386 17.528  1.00 37.08  ? 63  ALA A C   1 
ATOM   499  O O   . ALA A 1 63  ? 15.054 28.433 18.431  1.00 39.72  ? 63  ALA A O   1 
ATOM   500  C CB  . ALA A 1 63  ? 17.260 30.485 17.615  1.00 35.12  ? 63  ALA A CB  1 
ATOM   501  N N   . PHE A 1 64  ? 16.497 27.263 17.150  1.00 35.60  ? 64  PHE A N   1 
ATOM   502  C CA  . PHE A 1 64  ? 16.150 25.963 17.704  1.00 35.18  ? 64  PHE A CA  1 
ATOM   503  C C   . PHE A 1 64  ? 17.154 25.532 18.764  1.00 37.64  ? 64  PHE A C   1 
ATOM   504  O O   . PHE A 1 64  ? 18.350 25.822 18.673  1.00 38.87  ? 64  PHE A O   1 
ATOM   505  C CB  . PHE A 1 64  ? 16.078 24.906 16.603  1.00 32.35  ? 64  PHE A CB  1 
ATOM   506  C CG  . PHE A 1 64  ? 14.922 25.090 15.672  1.00 30.78  ? 64  PHE A CG  1 
ATOM   507  C CD1 . PHE A 1 64  ? 13.739 24.412 15.887  1.00 28.93  ? 64  PHE A CD1 1 
ATOM   508  C CD2 . PHE A 1 64  ? 15.010 25.947 14.591  1.00 32.23  ? 64  PHE A CD2 1 
ATOM   509  C CE1 . PHE A 1 64  ? 12.665 24.576 15.039  1.00 31.26  ? 64  PHE A CE1 1 
ATOM   510  C CE2 . PHE A 1 64  ? 13.935 26.114 13.735  1.00 32.96  ? 64  PHE A CE2 1 
ATOM   511  C CZ  . PHE A 1 64  ? 12.761 25.429 13.962  1.00 33.62  ? 64  PHE A CZ  1 
ATOM   512  N N   . ILE A 1 65  ? 16.647 24.835 19.779  1.00 37.56  ? 65  ILE A N   1 
ATOM   513  C CA  . ILE A 1 65  ? 17.463 24.280 20.855  1.00 37.84  ? 65  ILE A CA  1 
ATOM   514  C C   . ILE A 1 65  ? 16.995 22.856 21.121  1.00 39.98  ? 65  ILE A C   1 
ATOM   515  O O   . ILE A 1 65  ? 15.792 22.609 21.249  1.00 42.14  ? 65  ILE A O   1 
ATOM   516  C CB  . ILE A 1 65  ? 17.377 25.122 22.143  0.70 35.74  ? 65  ILE A CB  1 
ATOM   517  C CG1 . ILE A 1 65  ? 17.829 26.563 21.887  0.70 36.58  ? 65  ILE A CG1 1 
ATOM   518  C CG2 . ILE A 1 65  ? 18.221 24.482 23.247  0.70 35.99  ? 65  ILE A CG2 1 
ATOM   519  C CD1 . ILE A 1 65  ? 17.693 27.463 23.099  0.70 37.85  ? 65  ILE A CD1 1 
ATOM   520  N N   . GLY A 1 66  ? 17.942 21.924 21.203  1.00 39.38  ? 66  GLY A N   1 
ATOM   521  C CA  . GLY A 1 66  ? 17.610 20.528 21.405  1.00 39.75  ? 66  GLY A CA  1 
ATOM   522  C C   . GLY A 1 66  ? 18.081 19.946 22.722  1.00 41.49  ? 66  GLY A C   1 
ATOM   523  O O   . GLY A 1 66  ? 19.270 20.016 23.044  1.00 42.55  ? 66  GLY A O   1 
ATOM   524  N N   . ILE A 1 67  ? 17.157 19.366 23.486  1.00 42.65  ? 67  ILE A N   1 
ATOM   525  C CA  . ILE A 1 67  ? 17.477 18.573 24.669  1.00 43.00  ? 67  ILE A CA  1 
ATOM   526  C C   . ILE A 1 67  ? 17.123 17.126 24.361  1.00 45.13  ? 67  ILE A C   1 
ATOM   527  O O   . ILE A 1 67  ? 15.985 16.834 23.972  1.00 46.27  ? 67  ILE A O   1 
ATOM   528  C CB  . ILE A 1 67  ? 16.716 19.059 25.916  1.00 41.70  ? 67  ILE A CB  1 
ATOM   529  C CG1 . ILE A 1 67  ? 16.890 20.566 26.115  1.00 41.29  ? 67  ILE A CG1 1 
ATOM   530  C CG2 . ILE A 1 67  ? 17.210 18.318 27.153  1.00 42.86  ? 67  ILE A CG2 1 
ATOM   531  C CD1 . ILE A 1 67  ? 16.016 21.165 27.199  1.00 41.20  ? 67  ILE A CD1 1 
ATOM   532  N N   . HIS A 1 68  ? 18.091 16.220 24.516  1.00 46.86  ? 68  HIS A N   1 
ATOM   533  C CA  . HIS A 1 68  ? 17.883 14.809 24.209  1.00 49.65  ? 68  HIS A CA  1 
ATOM   534  C C   . HIS A 1 68  ? 17.686 14.026 25.504  1.00 51.80  ? 68  HIS A C   1 
ATOM   535  O O   . HIS A 1 68  ? 18.576 13.987 26.363  1.00 53.36  ? 68  HIS A O   1 
ATOM   536  C CB  . HIS A 1 68  ? 19.031 14.234 23.366  0.80 51.72  ? 68  HIS A CB  1 
ATOM   537  C CG  . HIS A 1 68  ? 20.279 13.912 24.132  0.70 54.63  ? 68  HIS A CG  1 
ATOM   538  N ND1 . HIS A 1 68  ? 21.075 14.878 24.711  0.70 55.23  ? 68  HIS A ND1 1 
ATOM   539  C CD2 . HIS A 1 68  ? 20.887 12.728 24.380  0.70 56.89  ? 68  HIS A CD2 1 
ATOM   540  C CE1 . HIS A 1 68  ? 22.108 14.300 25.299  0.70 57.39  ? 68  HIS A CE1 1 
ATOM   541  N NE2 . HIS A 1 68  ? 22.017 12.996 25.113  0.70 58.47  ? 68  HIS A NE2 1 
ATOM   542  N N   . THR A 1 69  ? 16.500 13.437 25.653  0.70 51.98  ? 69  THR A N   1 
ATOM   543  C CA  . THR A 1 69  ? 16.212 12.491 26.720  0.70 53.60  ? 69  THR A CA  1 
ATOM   544  C C   . THR A 1 69  ? 16.256 11.052 26.229  0.70 55.82  ? 69  THR A C   1 
ATOM   545  O O   . THR A 1 69  ? 15.795 10.151 26.937  0.70 58.19  ? 69  THR A O   1 
ATOM   546  C CB  . THR A 1 69  ? 14.843 12.783 27.340  0.70 54.29  ? 69  THR A CB  1 
ATOM   547  O OG1 . THR A 1 69  ? 13.813 12.516 26.380  0.70 53.13  ? 69  THR A OG1 1 
ATOM   548  C CG2 . THR A 1 69  ? 14.752 14.235 27.797  0.70 53.91  ? 69  THR A CG2 1 
ATOM   549  N N   . GLY A 1 70  ? 16.794 10.822 25.034  0.50 55.42  ? 70  GLY A N   1 
ATOM   550  C CA  . GLY A 1 70  ? 16.769 9.510  24.421  0.50 56.54  ? 70  GLY A CA  1 
ATOM   551  C C   . GLY A 1 70  ? 18.132 8.872  24.250  0.50 56.63  ? 70  GLY A C   1 
ATOM   552  O O   . GLY A 1 70  ? 19.007 9.015  25.110  0.50 55.66  ? 70  GLY A O   1 
ATOM   553  N N   . HIS A 1 71  ? 18.331 8.177  23.130  0.50 58.29  ? 71  HIS A N   1 
ATOM   554  C CA  . HIS A 1 71  ? 19.517 7.341  22.978  0.50 62.00  ? 71  HIS A CA  1 
ATOM   555  C C   . HIS A 1 71  ? 20.696 8.127  22.413  0.50 63.50  ? 71  HIS A C   1 
ATOM   556  O O   . HIS A 1 71  ? 21.740 8.249  23.061  0.50 63.08  ? 71  HIS A O   1 
ATOM   557  C CB  . HIS A 1 71  ? 19.188 6.138  22.095  0.50 62.91  ? 71  HIS A CB  1 
ATOM   558  C CG  . HIS A 1 71  ? 17.830 5.566  22.352  0.50 63.94  ? 71  HIS A CG  1 
ATOM   559  N ND1 . HIS A 1 71  ? 17.512 4.898  23.515  0.50 66.49  ? 71  HIS A ND1 1 
ATOM   560  C CD2 . HIS A 1 71  ? 16.702 5.577  21.604  0.50 63.43  ? 71  HIS A CD2 1 
ATOM   561  C CE1 . HIS A 1 71  ? 16.248 4.514  23.468  0.50 67.34  ? 71  HIS A CE1 1 
ATOM   562  N NE2 . HIS A 1 71  ? 15.735 4.914  22.318  0.50 65.67  ? 71  HIS A NE2 1 
ATOM   563  N N   . LEU A 1 72  ? 20.553 8.661  21.201  0.70 64.99  ? 72  LEU A N   1 
ATOM   564  C CA  . LEU A 1 72  ? 21.645 9.386  20.560  0.70 64.65  ? 72  LEU A CA  1 
ATOM   565  C C   . LEU A 1 72  ? 21.443 10.894 20.654  0.70 62.20  ? 72  LEU A C   1 
ATOM   566  O O   . LEU A 1 72  ? 22.158 11.580 21.392  0.70 64.43  ? 72  LEU A O   1 
ATOM   567  C CB  . LEU A 1 72  ? 21.778 8.956  19.096  0.70 65.67  ? 72  LEU A CB  1 
ATOM   568  C CG  . LEU A 1 72  ? 22.783 9.687  18.198  0.70 64.46  ? 72  LEU A CG  1 
ATOM   569  C CD1 . LEU A 1 72  ? 24.148 9.775  18.858  0.70 65.27  ? 72  LEU A CD1 1 
ATOM   570  C CD2 . LEU A 1 72  ? 22.888 8.993  16.849  0.70 64.20  ? 72  LEU A CD2 1 
ATOM   571  N N   . GLY A 1 73  ? 20.475 11.418 19.907  0.70 57.35  ? 73  GLY A N   1 
ATOM   572  C CA  . GLY A 1 73  ? 20.236 12.846 19.880  0.70 53.06  ? 73  GLY A CA  1 
ATOM   573  C C   . GLY A 1 73  ? 21.362 13.615 19.221  0.70 51.85  ? 73  GLY A C   1 
ATOM   574  O O   . GLY A 1 73  ? 22.138 14.297 19.897  0.70 53.30  ? 73  GLY A O   1 
ATOM   575  N N   . PHE A 1 74  ? 21.455 13.515 17.892  0.88 48.34  ? 74  PHE A N   1 
ATOM   576  C CA  . PHE A 1 74  ? 22.553 14.163 17.179  0.88 42.62  ? 74  PHE A CA  1 
ATOM   577  C C   . PHE A 1 74  ? 22.386 15.680 17.150  0.88 39.55  ? 74  PHE A C   1 
ATOM   578  O O   . PHE A 1 74  ? 23.375 16.419 17.239  0.88 37.05  ? 74  PHE A O   1 
ATOM   579  C CB  . PHE A 1 74  ? 22.662 13.601 15.759  0.88 40.28  ? 74  PHE A CB  1 
ATOM   580  C CG  . PHE A 1 74  ? 23.819 14.151 14.973  0.88 37.71  ? 74  PHE A CG  1 
ATOM   581  C CD1 . PHE A 1 74  ? 25.078 13.581 15.075  0.88 39.12  ? 74  PHE A CD1 1 
ATOM   582  C CD2 . PHE A 1 74  ? 23.646 15.229 14.120  0.88 35.93  ? 74  PHE A CD2 1 
ATOM   583  C CE1 . PHE A 1 74  ? 26.143 14.084 14.349  0.88 39.57  ? 74  PHE A CE1 1 
ATOM   584  C CE2 . PHE A 1 74  ? 24.709 15.734 13.393  0.88 36.70  ? 74  PHE A CE2 1 
ATOM   585  C CZ  . PHE A 1 74  ? 25.956 15.158 13.508  0.88 38.80  ? 74  PHE A CZ  1 
ATOM   586  N N   . TYR A 1 75  ? 21.149 16.163 17.025  1.00 40.14  ? 75  TYR A N   1 
ATOM   587  C CA  . TYR A 1 75  ? 20.889 17.597 16.947  1.00 40.52  ? 75  TYR A CA  1 
ATOM   588  C C   . TYR A 1 75  ? 20.789 18.264 18.312  1.00 41.89  ? 75  TYR A C   1 
ATOM   589  O O   . TYR A 1 75  ? 20.603 19.484 18.373  1.00 43.33  ? 75  TYR A O   1 
ATOM   590  C CB  . TYR A 1 75  ? 19.602 17.873 16.157  1.00 38.16  ? 75  TYR A CB  1 
ATOM   591  C CG  . TYR A 1 75  ? 19.765 17.746 14.658  1.00 38.55  ? 75  TYR A CG  1 
ATOM   592  C CD1 . TYR A 1 75  ? 19.201 16.684 13.963  1.00 37.38  ? 75  TYR A CD1 1 
ATOM   593  C CD2 . TYR A 1 75  ? 20.488 18.685 13.940  1.00 37.83  ? 75  TYR A CD2 1 
ATOM   594  C CE1 . TYR A 1 75  ? 19.353 16.562 12.593  1.00 37.44  ? 75  TYR A CE1 1 
ATOM   595  C CE2 . TYR A 1 75  ? 20.642 18.573 12.571  1.00 36.08  ? 75  TYR A CE2 1 
ATOM   596  C CZ  . TYR A 1 75  ? 20.075 17.510 11.903  1.00 36.29  ? 75  TYR A CZ  1 
ATOM   597  O OH  . TYR A 1 75  ? 20.228 17.395 10.539  1.00 35.51  ? 75  TYR A OH  1 
ATOM   598  N N   . ALA A 1 76  ? 20.911 17.512 19.398  1.00 43.36  ? 76  ALA A N   1 
ATOM   599  C CA  . ALA A 1 76  ? 20.759 18.068 20.732  1.00 44.52  ? 76  ALA A CA  1 
ATOM   600  C C   . ALA A 1 76  ? 22.083 18.614 21.248  1.00 47.91  ? 76  ALA A C   1 
ATOM   601  O O   . ALA A 1 76  ? 23.163 18.175 20.841  1.00 48.56  ? 76  ALA A O   1 
ATOM   602  C CB  . ALA A 1 76  ? 20.224 17.012 21.695  1.00 43.20  ? 76  ALA A CB  1 
ATOM   603  N N   . ASP A 1 77  ? 21.985 19.583 22.159  1.00 49.45  ? 77  ASP A N   1 
ATOM   604  C CA  . ASP A 1 77  ? 23.146 20.184 22.804  1.00 51.82  ? 77  ASP A CA  1 
ATOM   605  C C   . ASP A 1 77  ? 23.090 20.084 24.323  1.00 52.52  ? 77  ASP A C   1 
ATOM   606  O O   . ASP A 1 77  ? 23.949 20.662 25.001  1.00 54.34  ? 77  ASP A O   1 
ATOM   607  C CB  . ASP A 1 77  ? 23.284 21.657 22.405  1.00 52.60  ? 77  ASP A CB  1 
ATOM   608  C CG  . ASP A 1 77  ? 23.670 21.839 20.952  1.00 54.13  ? 77  ASP A CG  1 
ATOM   609  O OD1 . ASP A 1 77  ? 23.920 20.828 20.264  1.00 54.95  ? 77  ASP A OD1 1 
ATOM   610  O OD2 . ASP A 1 77  ? 23.721 23.001 20.498  1.00 54.49  ? 77  ASP A OD2 1 
ATOM   611  N N   . TRP A 1 78  ? 22.108 19.376 24.879  1.00 53.00  ? 78  TRP A N   1 
ATOM   612  C CA  . TRP A 1 78  ? 21.850 19.465 26.309  1.00 54.37  ? 78  TRP A CA  1 
ATOM   613  C C   . TRP A 1 78  ? 21.422 18.119 26.873  1.00 54.71  ? 78  TRP A C   1 
ATOM   614  O O   . TRP A 1 78  ? 20.639 17.394 26.252  1.00 55.88  ? 78  TRP A O   1 
ATOM   615  C CB  . TRP A 1 78  ? 20.772 20.517 26.602  0.92 53.78  ? 78  TRP A CB  1 
ATOM   616  C CG  . TRP A 1 78  ? 21.189 21.905 26.224  0.82 53.16  ? 78  TRP A CG  1 
ATOM   617  C CD1 . TRP A 1 78  ? 20.938 22.551 25.047  0.82 51.75  ? 78  TRP A CD1 1 
ATOM   618  C CD2 . TRP A 1 78  ? 21.947 22.815 27.027  0.82 53.96  ? 78  TRP A CD2 1 
ATOM   619  N NE1 . TRP A 1 78  ? 21.490 23.810 25.071  0.82 51.76  ? 78  TRP A NE1 1 
ATOM   620  C CE2 . TRP A 1 78  ? 22.116 23.995 26.276  0.82 53.39  ? 78  TRP A CE2 1 
ATOM   621  C CE3 . TRP A 1 78  ? 22.497 22.746 28.310  0.82 54.47  ? 78  TRP A CE3 1 
ATOM   622  C CZ2 . TRP A 1 78  ? 22.812 25.097 26.767  0.82 54.04  ? 78  TRP A CZ2 1 
ATOM   623  C CZ3 . TRP A 1 78  ? 23.186 23.838 28.794  0.82 55.49  ? 78  TRP A CZ3 1 
ATOM   624  C CH2 . TRP A 1 78  ? 23.338 24.999 28.025  0.82 55.55  ? 78  TRP A CH2 1 
ATOM   625  N N   . ARG A 1 79  ? 21.948 17.795 28.055  1.00 54.49  ? 79  ARG A N   1 
ATOM   626  C CA  . ARG A 1 79  ? 21.429 16.716 28.876  1.00 53.46  ? 79  ARG A CA  1 
ATOM   627  C C   . ARG A 1 79  ? 20.276 17.238 29.731  1.00 51.40  ? 79  ARG A C   1 
ATOM   628  O O   . ARG A 1 79  ? 20.206 18.434 30.023  1.00 49.75  ? 79  ARG A O   1 
ATOM   629  C CB  . ARG A 1 79  ? 22.524 16.147 29.778  1.00 55.81  ? 79  ARG A CB  1 
ATOM   630  C CG  . ARG A 1 79  ? 23.614 15.383 29.040  1.00 56.76  ? 79  ARG A CG  1 
ATOM   631  C CD  . ARG A 1 79  ? 24.558 14.664 30.002  0.70 59.15  ? 79  ARG A CD  1 
ATOM   632  N NE  . ARG A 1 79  ? 25.203 15.575 30.944  0.70 59.42  ? 79  ARG A NE  1 
ATOM   633  C CZ  . ARG A 1 79  ? 25.084 15.498 32.266  0.60 60.89  ? 79  ARG A CZ  1 
ATOM   634  N NH1 . ARG A 1 79  ? 24.349 14.541 32.817  0.60 61.95  ? 79  ARG A NH1 1 
ATOM   635  N NH2 . ARG A 1 79  ? 25.710 16.374 33.041  0.60 62.18  ? 79  ARG A NH2 1 
ATOM   636  N N   . PRO A 1 80  ? 19.348 16.365 30.132  1.00 53.42  ? 80  PRO A N   1 
ATOM   637  C CA  . PRO A 1 80  ? 18.234 16.832 30.974  1.00 53.16  ? 80  PRO A CA  1 
ATOM   638  C C   . PRO A 1 80  ? 18.681 17.403 32.309  1.00 53.27  ? 80  PRO A C   1 
ATOM   639  O O   . PRO A 1 80  ? 17.981 18.255 32.871  1.00 52.66  ? 80  PRO A O   1 
ATOM   640  C CB  . PRO A 1 80  ? 17.381 15.569 31.156  1.00 54.73  ? 80  PRO A CB  1 
ATOM   641  C CG  . PRO A 1 80  ? 17.725 14.708 29.982  1.00 53.81  ? 80  PRO A CG  1 
ATOM   642  C CD  . PRO A 1 80  ? 19.178 14.962 29.718  1.00 53.70  ? 80  PRO A CD  1 
ATOM   643  N N   . ALA A 1 81  ? 19.827 16.964 32.838  1.00 53.76  ? 81  ALA A N   1 
ATOM   644  C CA  . ALA A 1 81  ? 20.322 17.511 34.096  1.00 54.37  ? 81  ALA A CA  1 
ATOM   645  C C   . ALA A 1 81  ? 20.821 18.942 33.946  1.00 54.24  ? 81  ALA A C   1 
ATOM   646  O O   . ALA A 1 81  ? 20.857 19.681 34.935  1.00 55.44  ? 81  ALA A O   1 
ATOM   647  C CB  . ALA A 1 81  ? 21.435 16.624 34.653  1.00 55.88  ? 81  ALA A CB  1 
ATOM   648  N N   . GLU A 1 82  ? 21.200 19.346 32.736  1.00 53.00  ? 82  GLU A N   1 
ATOM   649  C CA  . GLU A 1 82  ? 21.666 20.696 32.458  1.00 52.91  ? 82  GLU A CA  1 
ATOM   650  C C   . GLU A 1 82  ? 20.533 21.640 32.071  1.00 52.62  ? 82  GLU A C   1 
ATOM   651  O O   . GLU A 1 82  ? 20.801 22.737 31.568  1.00 53.57  ? 82  GLU A O   1 
ATOM   652  C CB  . GLU A 1 82  ? 22.714 20.656 31.343  0.80 52.21  ? 82  GLU A CB  1 
ATOM   653  C CG  . GLU A 1 82  ? 23.885 21.598 31.531  0.70 53.86  ? 82  GLU A CG  1 
ATOM   654  C CD  . GLU A 1 82  ? 24.934 21.424 30.451  0.60 53.10  ? 82  GLU A CD  1 
ATOM   655  O OE1 . GLU A 1 82  ? 24.724 20.585 29.549  0.60 51.33  ? 82  GLU A OE1 1 
ATOM   656  O OE2 . GLU A 1 82  ? 25.966 22.123 30.504  0.60 53.91  ? 82  GLU A OE2 1 
ATOM   657  N N   . ALA A 1 83  ? 19.279 21.245 32.306  1.00 51.62  ? 83  ALA A N   1 
ATOM   658  C CA  . ALA A 1 83  ? 18.145 21.993 31.771  1.00 52.13  ? 83  ALA A CA  1 
ATOM   659  C C   . ALA A 1 83  ? 17.981 23.340 32.467  1.00 54.96  ? 83  ALA A C   1 
ATOM   660  O O   . ALA A 1 83  ? 17.750 24.362 31.809  1.00 55.46  ? 83  ALA A O   1 
ATOM   661  C CB  . ALA A 1 83  ? 16.867 21.164 31.894  1.00 52.06  ? 83  ALA A CB  1 
ATOM   662  N N   . ASP A 1 84  ? 18.088 23.362 33.799  1.00 55.84  ? 84  ASP A N   1 
ATOM   663  C CA  . ASP A 1 84  ? 17.885 24.612 34.525  1.00 56.61  ? 84  ASP A CA  1 
ATOM   664  C C   . ASP A 1 84  ? 18.981 25.624 34.222  1.00 55.93  ? 84  ASP A C   1 
ATOM   665  O O   . ASP A 1 84  ? 18.742 26.835 34.295  1.00 57.50  ? 84  ASP A O   1 
ATOM   666  C CB  . ASP A 1 84  ? 17.804 24.347 36.026  1.00 58.49  ? 84  ASP A CB  1 
ATOM   667  C CG  . ASP A 1 84  ? 16.591 23.521 36.401  0.70 58.23  ? 84  ASP A CG  1 
ATOM   668  O OD1 . ASP A 1 84  ? 16.760 22.451 37.028  0.50 58.53  ? 84  ASP A OD1 1 
ATOM   669  O OD2 . ASP A 1 84  ? 15.468 23.937 36.048  0.50 57.49  ? 84  ASP A OD2 1 
ATOM   670  N N   . LYS A 1 85  ? 20.178 25.152 33.877  1.00 54.33  ? 85  LYS A N   1 
ATOM   671  C CA  . LYS A 1 85  ? 21.208 26.064 33.401  1.00 54.24  ? 85  LYS A CA  1 
ATOM   672  C C   . LYS A 1 85  ? 20.853 26.625 32.031  1.00 54.98  ? 85  LYS A C   1 
ATOM   673  O O   . LYS A 1 85  ? 21.272 27.736 31.688  1.00 56.36  ? 85  LYS A O   1 
ATOM   674  C CB  . LYS A 1 85  ? 22.557 25.349 33.359  1.00 53.36  ? 85  LYS A CB  1 
ATOM   675  C CG  . LYS A 1 85  ? 23.735 26.245 33.013  0.70 54.87  ? 85  LYS A CG  1 
ATOM   676  C CD  . LYS A 1 85  ? 25.007 25.761 33.689  0.60 57.82  ? 85  LYS A CD  1 
ATOM   677  C CE  . LYS A 1 85  ? 26.191 26.642 33.327  0.60 60.61  ? 85  LYS A CE  1 
ATOM   678  N NZ  . LYS A 1 85  ? 27.371 26.343 34.186  0.60 64.45  ? 85  LYS A NZ  1 
ATOM   679  N N   . LEU A 1 86  ? 20.082 25.880 31.237  1.00 53.00  ? 86  LEU A N   1 
ATOM   680  C CA  . LEU A 1 86  ? 19.664 26.392 29.936  1.00 51.15  ? 86  LEU A CA  1 
ATOM   681  C C   . LEU A 1 86  ? 18.598 27.467 30.089  1.00 51.89  ? 86  LEU A C   1 
ATOM   682  O O   . LEU A 1 86  ? 18.604 28.464 29.353  1.00 52.20  ? 86  LEU A O   1 
ATOM   683  C CB  . LEU A 1 86  ? 19.153 25.251 29.056  1.00 48.09  ? 86  LEU A CB  1 
ATOM   684  C CG  . LEU A 1 86  ? 18.519 25.599 27.705  0.90 46.58  ? 86  LEU A CG  1 
ATOM   685  C CD1 . LEU A 1 86  ? 19.475 26.373 26.816  0.90 46.28  ? 86  LEU A CD1 1 
ATOM   686  C CD2 . LEU A 1 86  ? 18.043 24.340 26.990  0.90 46.14  ? 86  LEU A CD2 1 
ATOM   687  N N   . VAL A 1 87  ? 17.667 27.283 31.031  1.00 52.23  ? 87  VAL A N   1 
ATOM   688  C CA  . VAL A 1 87  ? 16.647 28.297 31.277  1.00 54.00  ? 87  VAL A CA  1 
ATOM   689  C C   . VAL A 1 87  ? 17.304 29.635 31.618  1.00 57.65  ? 87  VAL A C   1 
ATOM   690  O O   . VAL A 1 87  ? 16.909 30.687 31.109  1.00 58.43  ? 87  VAL A O   1 
ATOM   691  C CB  . VAL A 1 87  ? 15.688 27.834 32.389  0.71 53.66  ? 87  VAL A CB  1 
ATOM   692  C CG1 . VAL A 1 87  ? 14.665 28.908 32.725  0.73 53.97  ? 87  VAL A CG1 1 
ATOM   693  C CG2 . VAL A 1 87  ? 14.974 26.551 31.994  0.72 52.66  ? 87  VAL A CG2 1 
ATOM   694  N N   . LYS A 1 88  ? 18.334 29.593 32.466  1.00 58.97  ? 88  LYS A N   1 
ATOM   695  C CA  . LYS A 1 88  ? 18.983 30.819 32.928  1.00 59.70  ? 88  LYS A CA  1 
ATOM   696  C C   . LYS A 1 88  ? 19.707 31.527 31.789  1.00 59.78  ? 88  LYS A C   1 
ATOM   697  O O   . LYS A 1 88  ? 19.518 32.731 31.568  1.00 60.85  ? 88  LYS A O   1 
ATOM   698  C CB  . LYS A 1 88  ? 19.950 30.477 34.063  0.80 59.91  ? 88  LYS A CB  1 
ATOM   699  C CG  . LYS A 1 88  ? 20.282 31.631 34.980  0.70 62.17  ? 88  LYS A CG  1 
ATOM   700  C CD  . LYS A 1 88  ? 20.776 31.133 36.337  0.50 63.28  ? 88  LYS A CD  1 
ATOM   701  C CE  . LYS A 1 88  ? 22.291 31.184 36.446  0.50 64.84  ? 88  LYS A CE  1 
ATOM   702  N NZ  . LYS A 1 88  ? 22.711 32.448 37.107  0.50 68.08  ? 88  LYS A NZ  1 
ATOM   703  N N   . LEU A 1 89  ? 20.558 30.798 31.062  1.00 59.33  ? 89  LEU A N   1 
ATOM   704  C CA  . LEU A 1 89  ? 21.348 31.413 30.000  1.00 48.93  ? 89  LEU A CA  1 
ATOM   705  C C   . LEU A 1 89  ? 20.463 31.926 28.872  1.00 51.33  ? 89  LEU A C   1 
ATOM   706  O O   . LEU A 1 89  ? 20.699 33.017 28.339  1.00 48.96  ? 89  LEU A O   1 
ATOM   707  C CB  . LEU A 1 89  ? 22.371 30.415 29.462  0.73 47.75  ? 89  LEU A CB  1 
ATOM   708  C CG  . LEU A 1 89  ? 23.399 29.905 30.473  0.73 49.09  ? 89  LEU A CG  1 
ATOM   709  C CD1 . LEU A 1 89  ? 24.166 28.700 29.942  0.73 51.62  ? 89  LEU A CD1 1 
ATOM   710  C CD2 . LEU A 1 89  ? 24.358 31.017 30.859  0.73 51.64  ? 89  LEU A CD2 1 
ATOM   711  N N   . LEU A 1 90  ? 19.449 31.148 28.483  1.00 50.20  ? 90  LEU A N   1 
ATOM   712  C CA  . LEU A 1 90  ? 18.507 31.627 27.477  1.00 51.10  ? 90  LEU A CA  1 
ATOM   713  C C   . LEU A 1 90  ? 17.773 32.869 27.961  1.00 54.96  ? 90  LEU A C   1 
ATOM   714  O O   . LEU A 1 90  ? 17.422 33.740 27.154  1.00 55.09  ? 90  LEU A O   1 
ATOM   715  C CB  . LEU A 1 90  ? 17.512 30.521 27.118  1.00 49.89  ? 90  LEU A CB  1 
ATOM   716  C CG  . LEU A 1 90  ? 16.551 30.788 25.952  1.00 51.16  ? 90  LEU A CG  1 
ATOM   717  C CD1 . LEU A 1 90  ? 17.298 30.959 24.632  1.00 50.77  ? 90  LEU A CD1 1 
ATOM   718  C CD2 . LEU A 1 90  ? 15.500 29.688 25.837  1.00 50.38  ? 90  LEU A CD2 1 
ATOM   719  N N   . ALA A 1 91  ? 17.541 32.973 29.271  0.93 59.60  ? 91  ALA A N   1 
ATOM   720  C CA  . ALA A 1 91  ? 16.916 34.171 29.814  0.93 66.76  ? 91  ALA A CA  1 
ATOM   721  C C   . ALA A 1 91  ? 17.893 35.336 29.834  0.93 72.94  ? 91  ALA A C   1 
ATOM   722  O O   . ALA A 1 91  ? 17.506 36.481 29.574  0.93 75.02  ? 91  ALA A O   1 
ATOM   723  C CB  . ALA A 1 91  ? 16.380 33.893 31.216  0.93 69.01  ? 91  ALA A CB  1 
ATOM   724  N N   . LYS A 1 92  ? 19.168 35.060 30.129  1.00 76.35  ? 92  LYS A N   1 
ATOM   725  C CA  . LYS A 1 92  ? 20.194 36.095 30.094  1.00 81.11  ? 92  LYS A CA  1 
ATOM   726  C C   . LYS A 1 92  ? 20.302 36.749 28.724  1.00 83.61  ? 92  LYS A C   1 
ATOM   727  O O   . LYS A 1 92  ? 20.881 37.834 28.608  1.00 84.34  ? 92  LYS A O   1 
ATOM   728  C CB  . LYS A 1 92  ? 21.546 35.508 30.501  1.00 80.94  ? 92  LYS A CB  1 
ATOM   729  N N   . GLY A 1 93  ? 19.773 36.107 27.683  1.00 85.61  ? 93  GLY A N   1 
ATOM   730  C CA  . GLY A 1 93  ? 19.645 36.714 26.383  1.00 88.42  ? 93  GLY A CA  1 
ATOM   731  C C   . GLY A 1 93  ? 20.857 36.589 25.486  1.00 89.07  ? 93  GLY A C   1 
ATOM   732  O O   . GLY A 1 93  ? 20.715 36.703 24.264  1.00 87.73  ? 93  GLY A O   1 
ATOM   733  N N   . GLU A 1 94  ? 22.042 36.359 26.047  1.00 91.44  ? 94  GLU A N   1 
ATOM   734  C CA  . GLU A 1 94  ? 23.269 36.313 25.264  1.00 93.72  ? 94  GLU A CA  1 
ATOM   735  C C   . GLU A 1 94  ? 23.614 34.865 24.939  1.00 90.59  ? 94  GLU A C   1 
ATOM   736  O O   . GLU A 1 94  ? 23.826 34.045 25.840  1.00 90.15  ? 94  GLU A O   1 
ATOM   737  C CB  . GLU A 1 94  ? 24.428 36.993 25.993  1.00 99.34  ? 94  GLU A CB  1 
ATOM   738  C CG  . GLU A 1 94  ? 25.264 37.914 25.101  1.00 103.86 ? 94  GLU A CG  1 
ATOM   739  C CD  . GLU A 1 94  ? 25.649 37.269 23.784  1.00 104.69 ? 94  GLU A CD  1 
ATOM   740  O OE1 . GLU A 1 94  ? 25.181 37.746 22.726  1.00 105.53 ? 94  GLU A OE1 1 
ATOM   741  O OE2 . GLU A 1 94  ? 26.407 36.277 23.810  1.00 104.50 ? 94  GLU A OE2 1 
ATOM   742  N N   . TYR A 1 95  ? 23.659 34.567 23.648  1.00 85.02  ? 95  TYR A N   1 
ATOM   743  C CA  . TYR A 1 95  ? 24.071 33.298 23.068  1.00 78.71  ? 95  TYR A CA  1 
ATOM   744  C C   . TYR A 1 95  ? 24.320 33.602 21.600  1.00 74.83  ? 95  TYR A C   1 
ATOM   745  O O   . TYR A 1 95  ? 23.925 34.660 21.099  1.00 76.68  ? 95  TYR A O   1 
ATOM   746  C CB  . TYR A 1 95  ? 23.011 32.208 23.247  1.00 76.56  ? 95  TYR A CB  1 
ATOM   747  C CG  . TYR A 1 95  ? 21.644 32.631 22.759  1.00 76.12  ? 95  TYR A CG  1 
ATOM   748  C CD1 . TYR A 1 95  ? 20.705 33.156 23.638  1.00 77.04  ? 95  TYR A CD1 1 
ATOM   749  C CD2 . TYR A 1 95  ? 21.294 32.515 21.418  1.00 75.13  ? 95  TYR A CD2 1 
ATOM   750  C CE1 . TYR A 1 95  ? 19.458 33.547 23.196  1.00 77.29  ? 95  TYR A CE1 1 
ATOM   751  C CE2 . TYR A 1 95  ? 20.055 32.903 20.969  1.00 75.14  ? 95  TYR A CE2 1 
ATOM   752  C CZ  . TYR A 1 95  ? 19.140 33.418 21.859  1.00 76.78  ? 95  TYR A CZ  1 
ATOM   753  O OH  . TYR A 1 95  ? 17.902 33.802 21.399  1.00 77.40  ? 95  TYR A OH  1 
ATOM   754  N N   . GLN A 1 96  ? 24.964 32.676 20.904  1.00 69.35  ? 96  GLN A N   1 
ATOM   755  C CA  . GLN A 1 96  ? 25.272 32.906 19.503  1.00 64.63  ? 96  GLN A CA  1 
ATOM   756  C C   . GLN A 1 96  ? 24.494 31.948 18.610  1.00 58.68  ? 96  GLN A C   1 
ATOM   757  O O   . GLN A 1 96  ? 24.229 30.799 18.975  1.00 57.00  ? 96  GLN A O   1 
ATOM   758  C CB  . GLN A 1 96  ? 26.775 32.792 19.243  1.00 65.50  ? 96  GLN A CB  1 
ATOM   759  C CG  . GLN A 1 96  ? 27.560 33.894 19.941  1.00 68.08  ? 96  GLN A CG  1 
ATOM   760  C CD  . GLN A 1 96  ? 28.955 34.072 19.384  0.50 69.77  ? 96  GLN A CD  1 
ATOM   761  O OE1 . GLN A 1 96  ? 29.484 33.187 18.712  0.50 68.73  ? 96  GLN A OE1 1 
ATOM   762  N NE2 . GLN A 1 96  ? 29.559 35.226 19.655  0.50 72.52  ? 96  GLN A NE2 1 
ATOM   763  N N   . LYS A 1 97  ? 24.123 32.446 17.434  1.00 55.75  ? 97  LYS A N   1 
ATOM   764  C CA  . LYS A 1 97  ? 23.299 31.716 16.483  1.00 50.34  ? 97  LYS A CA  1 
ATOM   765  C C   . LYS A 1 97  ? 24.174 31.155 15.371  1.00 48.00  ? 97  LYS A C   1 
ATOM   766  O O   . LYS A 1 97  ? 25.012 31.871 14.811  1.00 50.25  ? 97  LYS A O   1 
ATOM   767  C CB  . LYS A 1 97  ? 22.208 32.620 15.902  1.00 49.94  ? 97  LYS A CB  1 
ATOM   768  C CG  . LYS A 1 97  ? 21.121 32.978 16.902  1.00 49.53  ? 97  LYS A CG  1 
ATOM   769  C CD  . LYS A 1 97  ? 19.963 33.746 16.267  1.00 49.70  ? 97  LYS A CD  1 
ATOM   770  C CE  . LYS A 1 97  ? 20.094 35.251 16.471  1.00 51.97  ? 97  LYS A CE  1 
ATOM   771  N NZ  . LYS A 1 97  ? 18.828 35.982 16.156  0.83 53.03  ? 97  LYS A NZ  1 
ATOM   772  N N   . VAL A 1 98  ? 23.990 29.874 15.068  1.00 45.04  ? 98  VAL A N   1 
ATOM   773  C CA  . VAL A 1 98  ? 24.679 29.224 13.963  1.00 43.26  ? 98  VAL A CA  1 
ATOM   774  C C   . VAL A 1 98  ? 23.628 28.683 13.004  1.00 42.71  ? 98  VAL A C   1 
ATOM   775  O O   . VAL A 1 98  ? 22.531 28.281 13.409  1.00 41.92  ? 98  VAL A O   1 
ATOM   776  C CB  . VAL A 1 98  ? 25.635 28.108 14.445  1.00 40.84  ? 98  VAL A CB  1 
ATOM   777  C CG1 . VAL A 1 98  ? 26.649 28.681 15.411  1.00 40.61  ? 98  VAL A CG1 1 
ATOM   778  C CG2 . VAL A 1 98  ? 24.867 26.981 15.091  1.00 39.84  ? 98  VAL A CG2 1 
ATOM   779  N N   . SER A 1 99  ? 23.965 28.690 11.719  1.00 42.82  ? 99  SER A N   1 
ATOM   780  C CA  . SER A 1 99  ? 23.013 28.379 10.662  1.00 40.72  ? 99  SER A CA  1 
ATOM   781  C C   . SER A 1 99  ? 23.522 27.216 9.825   1.00 37.26  ? 99  SER A C   1 
ATOM   782  O O   . SER A 1 99  ? 24.673 27.224 9.378   1.00 36.86  ? 99  SER A O   1 
ATOM   783  C CB  . SER A 1 99  ? 22.767 29.604 9.779   1.00 44.43  ? 99  SER A CB  1 
ATOM   784  O OG  . SER A 1 99  ? 22.367 30.715 10.562  1.00 46.76  ? 99  SER A OG  1 
ATOM   785  N N   . TYR A 1 100 ? 22.656 26.224 9.607   1.00 35.83  ? 100 TYR A N   1 
ATOM   786  C CA  . TYR A 1 100 ? 22.939 25.063 8.783   1.00 35.22  ? 100 TYR A CA  1 
ATOM   787  C C   . TYR A 1 100 ? 22.167 25.144 7.467   1.00 35.36  ? 100 TYR A C   1 
ATOM   788  O O   . TYR A 1 100 ? 21.048 25.668 7.425   1.00 33.95  ? 100 TYR A O   1 
ATOM   789  C CB  . TYR A 1 100 ? 22.579 23.759 9.508   1.00 35.11  ? 100 TYR A CB  1 
ATOM   790  C CG  . TYR A 1 100 ? 23.559 23.355 10.594  1.00 38.04  ? 100 TYR A CG  1 
ATOM   791  C CD1 . TYR A 1 100 ? 24.632 24.170 10.932  1.00 40.34  ? 100 TYR A CD1 1 
ATOM   792  C CD2 . TYR A 1 100 ? 23.414 22.152 11.271  1.00 38.47  ? 100 TYR A CD2 1 
ATOM   793  C CE1 . TYR A 1 100 ? 25.522 23.802 11.917  1.00 41.19  ? 100 TYR A CE1 1 
ATOM   794  C CE2 . TYR A 1 100 ? 24.301 21.774 12.256  1.00 39.65  ? 100 TYR A CE2 1 
ATOM   795  C CZ  . TYR A 1 100 ? 25.355 22.602 12.574  1.00 41.97  ? 100 TYR A CZ  1 
ATOM   796  O OH  . TYR A 1 100 ? 26.246 22.230 13.554  1.00 44.91  ? 100 TYR A OH  1 
ATOM   797  N N   . PRO A 1 101 ? 22.744 24.658 6.373   1.00 36.53  ? 101 PRO A N   1 
ATOM   798  C CA  . PRO A 1 101 ? 22.037 24.703 5.090   1.00 36.24  ? 101 PRO A CA  1 
ATOM   799  C C   . PRO A 1 101 ? 20.882 23.716 5.057   1.00 36.50  ? 101 PRO A C   1 
ATOM   800  O O   . PRO A 1 101 ? 20.881 22.694 5.747   1.00 36.75  ? 101 PRO A O   1 
ATOM   801  C CB  . PRO A 1 101 ? 23.120 24.326 4.071   1.00 34.98  ? 101 PRO A CB  1 
ATOM   802  C CG  . PRO A 1 101 ? 24.420 24.479 4.800   1.00 36.14  ? 101 PRO A CG  1 
ATOM   803  C CD  . PRO A 1 101 ? 24.117 24.153 6.221   1.00 36.62  ? 101 PRO A CD  1 
ATOM   804  N N   . LEU A 1 102 ? 19.886 24.040 4.239   1.00 36.78  ? 102 LEU A N   1 
ATOM   805  C CA  . LEU A 1 102 ? 18.706 23.209 4.068   1.00 35.60  ? 102 LEU A CA  1 
ATOM   806  C C   . LEU A 1 102 ? 18.578 22.794 2.608   1.00 33.62  ? 102 LEU A C   1 
ATOM   807  O O   . LEU A 1 102 ? 19.141 23.425 1.709   1.00 33.46  ? 102 LEU A O   1 
ATOM   808  C CB  . LEU A 1 102 ? 17.439 23.948 4.520   1.00 36.68  ? 102 LEU A CB  1 
ATOM   809  C CG  . LEU A 1 102 ? 17.438 24.484 5.953   1.00 37.48  ? 102 LEU A CG  1 
ATOM   810  C CD1 . LEU A 1 102 ? 16.203 25.334 6.194   1.00 37.84  ? 102 LEU A CD1 1 
ATOM   811  C CD2 . LEU A 1 102 ? 17.511 23.341 6.960   1.00 36.17  ? 102 LEU A CD2 1 
ATOM   812  N N   . LEU A 1 103 ? 17.827 21.720 2.381   1.00 32.13  ? 103 LEU A N   1 
ATOM   813  C CA  . LEU A 1 103 ? 17.587 21.200 1.042   1.00 30.27  ? 103 LEU A CA  1 
ATOM   814  C C   . LEU A 1 103 ? 16.191 21.584 0.574   1.00 31.71  ? 103 LEU A C   1 
ATOM   815  O O   . LEU A 1 103 ? 15.242 21.601 1.363   1.00 31.63  ? 103 LEU A O   1 
ATOM   816  C CB  . LEU A 1 103 ? 17.741 19.680 1.008   1.00 28.85  ? 103 LEU A CB  1 
ATOM   817  C CG  . LEU A 1 103 ? 17.454 18.983 -0.327  1.00 29.71  ? 103 LEU A CG  1 
ATOM   818  C CD1 . LEU A 1 103 ? 18.451 19.405 -1.403  1.00 28.88  ? 103 LEU A CD1 1 
ATOM   819  C CD2 . LEU A 1 103 ? 17.460 17.478 -0.140  1.00 26.14  ? 103 LEU A CD2 1 
ATOM   820  N N   . LYS A 1 104 ? 16.072 21.889 -0.713  1.00 33.90  ? 104 LYS A N   1 
ATOM   821  C CA  . LYS A 1 104 ? 14.793 22.201 -1.331  1.00 34.83  ? 104 LYS A CA  1 
ATOM   822  C C   . LYS A 1 104 ? 14.445 21.119 -2.343  1.00 35.38  ? 104 LYS A C   1 
ATOM   823  O O   . LYS A 1 104 ? 15.253 20.800 -3.222  1.00 29.34  ? 104 LYS A O   1 
ATOM   824  C CB  . LYS A 1 104 ? 14.827 23.570 -2.012  1.00 30.75  ? 104 LYS A CB  1 
ATOM   825  C CG  . LYS A 1 104 ? 13.476 23.997 -2.555  1.00 38.54  ? 104 LYS A CG  1 
ATOM   826  C CD  . LYS A 1 104 ? 13.558 25.265 -3.393  1.00 40.57  ? 104 LYS A CD  1 
ATOM   827  C CE  . LYS A 1 104 ? 12.167 25.727 -3.802  1.00 44.24  ? 104 LYS A CE  1 
ATOM   828  N NZ  . LYS A 1 104 ? 12.213 26.902 -4.722  0.83 48.11  ? 104 LYS A NZ  1 
ATOM   829  N N   . THR A 1 105 ? 13.251 20.552 -2.209  1.00 36.44  ? 105 THR A N   1 
ATOM   830  C CA  . THR A 1 105 ? 12.724 19.580 -3.154  1.00 35.58  ? 105 THR A CA  1 
ATOM   831  C C   . THR A 1 105 ? 11.478 20.160 -3.804  1.00 38.17  ? 105 THR A C   1 
ATOM   832  O O   . THR A 1 105 ? 10.572 20.628 -3.108  1.00 39.40  ? 105 THR A O   1 
ATOM   833  C CB  . THR A 1 105 ? 12.391 18.254 -2.465  1.00 33.46  ? 105 THR A CB  1 
ATOM   834  O OG1 . THR A 1 105 ? 13.542 17.769 -1.761  1.00 28.35  ? 105 THR A OG1 1 
ATOM   835  C CG2 . THR A 1 105 ? 11.961 17.219 -3.493  1.00 32.24  ? 105 THR A CG2 1 
ATOM   836  N N   . THR A 1 106 ? 11.447 20.148 -5.132  1.00 39.31  ? 106 THR A N   1 
ATOM   837  C CA  . THR A 1 106 ? 10.293 20.590 -5.901  1.00 39.84  ? 106 THR A CA  1 
ATOM   838  C C   . THR A 1 106 ? 9.808  19.431 -6.758  1.00 41.79  ? 106 THR A C   1 
ATOM   839  O O   . THR A 1 106 ? 10.583 18.854 -7.529  1.00 43.06  ? 106 THR A O   1 
ATOM   840  C CB  . THR A 1 106 ? 10.629 21.803 -6.776  1.00 38.58  ? 106 THR A CB  1 
ATOM   841  O OG1 . THR A 1 106 ? 11.037 22.898 -5.947  1.00 37.93  ? 106 THR A OG1 1 
ATOM   842  C CG2 . THR A 1 106 ? 9.420  22.221 -7.594  1.00 40.06  ? 106 THR A CG2 1 
ATOM   843  N N   . VAL A 1 107 ? 8.531  19.089 -6.609  1.00 41.22  ? 107 VAL A N   1 
ATOM   844  C CA  . VAL A 1 107 ? 7.910  17.982 -7.323  1.00 43.22  ? 107 VAL A CA  1 
ATOM   845  C C   . VAL A 1 107 ? 6.852  18.553 -8.253  1.00 45.76  ? 107 VAL A C   1 
ATOM   846  O O   . VAL A 1 107 ? 6.075  19.429 -7.859  1.00 46.53  ? 107 VAL A O   1 
ATOM   847  C CB  . VAL A 1 107 ? 7.294  16.949 -6.354  1.00 44.74  ? 107 VAL A CB  1 
ATOM   848  C CG1 . VAL A 1 107 ? 6.702  15.773 -7.121  1.00 38.21  ? 107 VAL A CG1 1 
ATOM   849  C CG2 . VAL A 1 107 ? 8.336  16.480 -5.359  1.00 43.40  ? 107 VAL A CG2 1 
ATOM   850  N N   . LYS A 1 108 ? 6.821  18.054 -9.485  1.00 47.01  ? 108 LYS A N   1 
ATOM   851  C CA  . LYS A 1 108 ? 5.932  18.567 -10.516 1.00 51.18  ? 108 LYS A CA  1 
ATOM   852  C C   . LYS A 1 108 ? 5.035  17.460 -11.045 1.00 55.11  ? 108 LYS A C   1 
ATOM   853  O O   . LYS A 1 108 ? 5.463  16.309 -11.186 1.00 54.13  ? 108 LYS A O   1 
ATOM   854  C CB  . LYS A 1 108 ? 6.734  19.186 -11.655 0.80 51.65  ? 108 LYS A CB  1 
ATOM   855  C CG  . LYS A 1 108 ? 7.307  20.535 -11.297 0.60 51.71  ? 108 LYS A CG  1 
ATOM   856  C CD  . LYS A 1 108 ? 8.328  20.989 -12.309 0.60 53.35  ? 108 LYS A CD  1 
ATOM   857  C CE  . LYS A 1 108 ? 8.686  22.435 -12.066 0.50 54.75  ? 108 LYS A CE  1 
ATOM   858  N NZ  . LYS A 1 108 ? 9.292  23.042 -13.277 0.50 56.36  ? 108 LYS A NZ  1 
ATOM   859  N N   . TYR A 1 109 ? 3.788  17.819 -11.346 0.80 59.75  ? 109 TYR A N   1 
ATOM   860  C CA  . TYR A 1 109 ? 2.821  16.860 -11.863 0.80 63.54  ? 109 TYR A CA  1 
ATOM   861  C C   . TYR A 1 109 ? 2.367  17.234 -13.268 0.80 67.41  ? 109 TYR A C   1 
ATOM   862  O O   . TYR A 1 109 ? 3.159  17.702 -14.089 0.80 68.01  ? 109 TYR A O   1 
ATOM   863  C CB  . TYR A 1 109 ? 1.605  16.767 -10.935 0.80 66.15  ? 109 TYR A CB  1 
ATOM   864  C CG  . TYR A 1 109 ? 1.981  16.632 -9.477  0.80 65.03  ? 109 TYR A CG  1 
ATOM   865  C CD1 . TYR A 1 109 ? 2.096  15.386 -8.885  0.80 64.76  ? 109 TYR A CD1 1 
ATOM   866  C CD2 . TYR A 1 109 ? 2.206  17.755 -8.697  0.80 64.61  ? 109 TYR A CD2 1 
ATOM   867  C CE1 . TYR A 1 109 ? 2.434  15.259 -7.560  0.80 64.36  ? 109 TYR A CE1 1 
ATOM   868  C CE2 . TYR A 1 109 ? 2.548  17.646 -7.375  0.80 63.93  ? 109 TYR A CE2 1 
ATOM   869  C CZ  . TYR A 1 109 ? 2.660  16.395 -6.807  0.80 64.37  ? 109 TYR A CZ  1 
ATOM   870  O OH  . TYR A 1 109 ? 3.002  16.292 -5.483  0.80 64.01  ? 109 TYR A OH  1 
ATOM   871  N N   . GLY A 1 110 ? 1.093  17.021 -13.562 1.00 70.34  ? 110 GLY A N   1 
ATOM   872  C CA  . GLY A 1 110 ? 0.582  17.247 -14.904 1.00 70.68  ? 110 GLY A CA  1 
ATOM   873  C C   . GLY A 1 110 ? -0.936 17.359 -14.979 1.00 74.31  ? 110 GLY A C   1 
ATOM   874  O O   . GLY A 1 110 ? -1.493 18.406 -15.343 1.00 76.88  ? 110 GLY A O   1 
ATOM   875  N N   . LYS A 1 114 ? 0.252  20.042 -10.193 1.00 72.83  ? 114 LYS A N   1 
ATOM   876  C CA  . LYS A 1 114 ? 0.833  21.374 -10.057 1.00 72.06  ? 114 LYS A CA  1 
ATOM   877  C C   . LYS A 1 114 ? 2.306  21.325 -9.657  1.00 67.81  ? 114 LYS A C   1 
ATOM   878  O O   . LYS A 1 114 ? 3.138  20.770 -10.376 1.00 67.27  ? 114 LYS A O   1 
ATOM   879  C CB  . LYS A 1 114 ? 0.045  22.198 -9.035  0.80 73.04  ? 114 LYS A CB  1 
ATOM   880  N N   . GLU A 1 115 ? 2.621  21.917 -8.506  1.00 63.57  ? 115 GLU A N   1 
ATOM   881  C CA  . GLU A 1 115 ? 4.005  22.033 -8.057  1.00 57.40  ? 115 GLU A CA  1 
ATOM   882  C C   . GLU A 1 115 ? 4.025  22.048 -6.538  1.00 55.47  ? 115 GLU A C   1 
ATOM   883  O O   . GLU A 1 115 ? 3.456  22.955 -5.922  1.00 57.71  ? 115 GLU A O   1 
ATOM   884  C CB  . GLU A 1 115 ? 4.658  23.302 -8.611  0.80 56.76  ? 115 GLU A CB  1 
ATOM   885  C CG  . GLU A 1 115 ? 6.076  23.098 -9.103  0.70 54.25  ? 115 GLU A CG  1 
ATOM   886  C CD  . GLU A 1 115 ? 6.893  24.374 -9.075  0.60 52.61  ? 115 GLU A CD  1 
ATOM   887  O OE1 . GLU A 1 115 ? 6.885  25.072 -8.038  0.60 50.96  ? 115 GLU A OE1 1 
ATOM   888  O OE2 . GLU A 1 115 ? 7.540  24.684 -10.096 0.60 51.93  ? 115 GLU A OE2 1 
ATOM   889  N N   . ALA A 1 116 ? 4.678  21.052 -5.945  1.00 51.87  ? 116 ALA A N   1 
ATOM   890  C CA  . ALA A 1 116 ? 4.834  20.946 -4.501  1.00 47.90  ? 116 ALA A CA  1 
ATOM   891  C C   . ALA A 1 116 ? 6.303  21.094 -4.124  1.00 46.21  ? 116 ALA A C   1 
ATOM   892  O O   . ALA A 1 116 ? 7.174  20.477 -4.744  1.00 45.88  ? 116 ALA A O   1 
ATOM   893  C CB  . ALA A 1 116 ? 4.296  19.604 -3.993  1.00 46.03  ? 116 ALA A CB  1 
ATOM   894  N N   . THR A 1 117 ? 6.576  21.914 -3.108  1.00 45.41  ? 117 THR A N   1 
ATOM   895  C CA  . THR A 1 117 ? 7.929  22.139 -2.619  1.00 42.61  ? 117 THR A CA  1 
ATOM   896  C C   . THR A 1 117 ? 8.046  21.686 -1.169  1.00 40.66  ? 117 THR A C   1 
ATOM   897  O O   . THR A 1 117 ? 7.068  21.677 -0.417  1.00 42.39  ? 117 THR A O   1 
ATOM   898  C CB  . THR A 1 117 ? 8.336  23.614 -2.726  1.00 42.85  ? 117 THR A CB  1 
ATOM   899  O OG1 . THR A 1 117 ? 7.427  24.418 -1.962  1.00 44.76  ? 117 THR A OG1 1 
ATOM   900  C CG2 . THR A 1 117 ? 8.324  24.075 -4.179  1.00 43.14  ? 117 THR A CG2 1 
ATOM   901  N N   . TYR A 1 118 ? 9.262  21.306 -0.779  1.00 39.80  ? 118 TYR A N   1 
ATOM   902  C CA  . TYR A 1 118 ? 9.511  20.838 0.577   1.00 38.05  ? 118 TYR A CA  1 
ATOM   903  C C   . TYR A 1 118 ? 10.881 21.317 1.036   1.00 38.13  ? 118 TYR A C   1 
ATOM   904  O O   . TYR A 1 118 ? 11.782 21.543 0.222   1.00 39.25  ? 118 TYR A O   1 
ATOM   905  C CB  . TYR A 1 118 ? 9.436  19.308 0.675   1.00 36.56  ? 118 TYR A CB  1 
ATOM   906  C CG  . TYR A 1 118 ? 8.140  18.713 0.172   0.80 32.55  ? 118 TYR A CG  1 
ATOM   907  C CD1 . TYR A 1 118 ? 7.041  18.580 1.012   0.80 33.54  ? 118 TYR A CD1 1 
ATOM   908  C CD2 . TYR A 1 118 ? 8.019  18.275 -1.141  0.80 33.16  ? 118 TYR A CD2 1 
ATOM   909  C CE1 . TYR A 1 118 ? 5.858  18.035 0.557   0.80 38.72  ? 118 TYR A CE1 1 
ATOM   910  C CE2 . TYR A 1 118 ? 6.841  17.727 -1.605  0.80 34.76  ? 118 TYR A CE2 1 
ATOM   911  C CZ  . TYR A 1 118 ? 5.764  17.610 -0.752  0.80 38.92  ? 118 TYR A CZ  1 
ATOM   912  O OH  . TYR A 1 118 ? 4.586  17.065 -1.209  0.80 40.89  ? 118 TYR A OH  1 
ATOM   913  N N   . LEU A 1 119 ? 11.024 21.469 2.350   1.00 37.32  ? 119 LEU A N   1 
ATOM   914  C CA  . LEU A 1 119 ? 12.295 21.785 2.987   1.00 29.03  ? 119 LEU A CA  1 
ATOM   915  C C   . LEU A 1 119 ? 12.730 20.605 3.847   1.00 32.72  ? 119 LEU A C   1 
ATOM   916  O O   . LEU A 1 119 ? 11.919 20.028 4.578   1.00 32.46  ? 119 LEU A O   1 
ATOM   917  C CB  . LEU A 1 119 ? 12.180 23.053 3.840   0.70 36.95  ? 119 LEU A CB  1 
ATOM   918  C CG  . LEU A 1 119 ? 13.221 24.151 3.619   0.60 36.98  ? 119 LEU A CG  1 
ATOM   919  C CD1 . LEU A 1 119 ? 13.405 24.395 2.139   0.60 30.40  ? 119 LEU A CD1 1 
ATOM   920  C CD2 . LEU A 1 119 ? 12.793 25.433 4.320   0.60 37.95  ? 119 LEU A CD2 1 
ATOM   921  N N   . ALA A 1 120 ? 14.009 20.246 3.762   1.00 31.43  ? 120 ALA A N   1 
ATOM   922  C CA  . ALA A 1 120 ? 14.534 19.082 4.462   1.00 30.95  ? 120 ALA A CA  1 
ATOM   923  C C   . ALA A 1 120 ? 15.736 19.472 5.309   1.00 32.51  ? 120 ALA A C   1 
ATOM   924  O O   . ALA A 1 120 ? 16.595 20.242 4.868   1.00 35.00  ? 120 ALA A O   1 
ATOM   925  C CB  . ALA A 1 120 ? 14.932 17.970 3.479   1.00 29.85  ? 120 ALA A CB  1 
ATOM   926  N N   . LEU A 1 121 ? 15.790 18.938 6.530   1.00 30.05  ? 121 LEU A N   1 
ATOM   927  C CA  . LEU A 1 121 ? 16.941 19.097 7.410   1.00 30.43  ? 121 LEU A CA  1 
ATOM   928  C C   . LEU A 1 121 ? 17.918 17.937 7.303   1.00 30.81  ? 121 LEU A C   1 
ATOM   929  O O   . LEU A 1 121 ? 19.134 18.145 7.373   1.00 29.81  ? 121 LEU A O   1 
ATOM   930  C CB  . LEU A 1 121 ? 16.484 19.245 8.866   1.00 31.08  ? 121 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 121 ? 17.574 19.527 9.901   1.00 29.50  ? 121 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 121 ? 18.273 20.830 9.569   1.00 28.41  ? 121 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 121 ? 16.992 19.574 11.305  1.00 30.59  ? 121 LEU A CD2 1 
ATOM   934  N N   . ASN A 1 122 ? 17.414 16.717 7.132   1.00 31.87  ? 122 ASN A N   1 
ATOM   935  C CA  . ASN A 1 122 ? 18.289 15.575 6.915   1.00 32.62  ? 122 ASN A CA  1 
ATOM   936  C C   . ASN A 1 122 ? 18.439 15.289 5.426   1.00 33.53  ? 122 ASN A C   1 
ATOM   937  O O   . ASN A 1 122 ? 19.494 15.563 4.845   1.00 33.14  ? 122 ASN A O   1 
ATOM   938  C CB  . ASN A 1 122 ? 17.767 14.339 7.655   1.00 33.28  ? 122 ASN A CB  1 
ATOM   939  C CG  . ASN A 1 122 ? 18.258 14.269 9.090   1.00 33.99  ? 122 ASN A CG  1 
ATOM   940  O OD1 . ASN A 1 122 ? 19.182 14.986 9.478   1.00 32.42  ? 122 ASN A OD1 1 
ATOM   941  N ND2 . ASN A 1 122 ? 17.650 13.393 9.881   1.00 36.21  ? 122 ASN A ND2 1 
ATOM   942  N N   . GLU A 1 123 ? 17.399 14.746 4.795   1.00 34.60  ? 123 GLU A N   1 
ATOM   943  C CA  . GLU A 1 123 ? 17.526 14.336 3.404   1.00 35.98  ? 123 GLU A CA  1 
ATOM   944  C C   . GLU A 1 123 ? 16.151 14.146 2.786   1.00 37.22  ? 123 GLU A C   1 
ATOM   945  O O   . GLU A 1 123 ? 15.134 14.066 3.482   1.00 38.22  ? 123 GLU A O   1 
ATOM   946  C CB  . GLU A 1 123 ? 18.340 13.043 3.273   1.00 35.84  ? 123 GLU A CB  1 
ATOM   947  C CG  . GLU A 1 123 ? 17.622 11.781 3.750   1.00 36.56  ? 123 GLU A CG  1 
ATOM   948  C CD  . GLU A 1 123 ? 17.430 11.736 5.258   1.00 37.13  ? 123 GLU A CD  1 
ATOM   949  O OE1 . GLU A 1 123 ? 16.297 11.975 5.725   1.00 38.12  ? 123 GLU A OE1 1 
ATOM   950  O OE2 . GLU A 1 123 ? 18.415 11.462 5.974   1.00 37.27  ? 123 GLU A OE2 1 
ATOM   951  N N   . SER A 1 124 ? 16.143 14.083 1.456   1.00 36.41  ? 124 SER A N   1 
ATOM   952  C CA  . SER A 1 124 ? 14.985 13.678 0.676   1.00 35.30  ? 124 SER A CA  1 
ATOM   953  C C   . SER A 1 124 ? 15.390 12.506 -0.203  1.00 32.36  ? 124 SER A C   1 
ATOM   954  O O   . SER A 1 124 ? 16.444 12.547 -0.847  1.00 32.05  ? 124 SER A O   1 
ATOM   955  C CB  . SER A 1 124 ? 14.455 14.828 -0.183  1.00 37.36  ? 124 SER A CB  1 
ATOM   956  O OG  . SER A 1 124 ? 13.448 14.375 -1.072  1.00 38.52  ? 124 SER A OG  1 
ATOM   957  N N   . THR A 1 125 ? 14.567 11.462 -0.218  1.00 31.91  ? 125 THR A N   1 
ATOM   958  C CA  . THR A 1 125 ? 14.870 10.257 -0.971  1.00 30.53  ? 125 THR A CA  1 
ATOM   959  C C   . THR A 1 125 ? 13.712 9.930  -1.901  1.00 34.17  ? 125 THR A C   1 
ATOM   960  O O   . THR A 1 125 ? 12.556 10.270 -1.626  1.00 38.15  ? 125 THR A O   1 
ATOM   961  C CB  . THR A 1 125 ? 15.153 9.059  -0.049  1.00 30.32  ? 125 THR A CB  1 
ATOM   962  O OG1 . THR A 1 125 ? 13.933 8.609  0.550   1.00 32.32  ? 125 THR A OG1 1 
ATOM   963  C CG2 . THR A 1 125 ? 16.140 9.446  1.051   1.00 30.06  ? 125 THR A CG2 1 
ATOM   964  N N   . VAL A 1 126 ? 14.035 9.268  -3.009  1.00 33.15  ? 126 VAL A N   1 
ATOM   965  C CA  . VAL A 1 126 ? 13.045 8.834  -3.984  1.00 32.43  ? 126 VAL A CA  1 
ATOM   966  C C   . VAL A 1 126 ? 13.129 7.325  -4.131  1.00 35.09  ? 126 VAL A C   1 
ATOM   967  O O   . VAL A 1 126 ? 14.222 6.758  -4.224  1.00 36.34  ? 126 VAL A O   1 
ATOM   968  C CB  . VAL A 1 126 ? 13.237 9.510  -5.356  1.00 28.57  ? 126 VAL A CB  1 
ATOM   969  C CG1 . VAL A 1 126 ? 12.044 9.214  -6.255  1.00 29.08  ? 126 VAL A CG1 1 
ATOM   970  C CG2 . VAL A 1 126 ? 13.409 10.995 -5.186  1.00 27.31  ? 126 VAL A CG2 1 
ATOM   971  N N   . LYS A 1 127 ? 11.969 6.678  -4.146  1.00 36.71  ? 127 LYS A N   1 
ATOM   972  C CA  . LYS A 1 127 ? 11.852 5.270  -4.486  1.00 37.80  ? 127 LYS A CA  1 
ATOM   973  C C   . LYS A 1 127 ? 10.616 5.099  -5.356  1.00 41.07  ? 127 LYS A C   1 
ATOM   974  O O   . LYS A 1 127 ? 9.743  5.969  -5.400  1.00 42.54  ? 127 LYS A O   1 
ATOM   975  C CB  . LYS A 1 127 ? 11.755 4.388  -3.233  1.00 38.26  ? 127 LYS A CB  1 
ATOM   976  C CG  . LYS A 1 127 ? 12.937 4.538  -2.294  1.00 37.37  ? 127 LYS A CG  1 
ATOM   977  C CD  . LYS A 1 127 ? 12.680 3.850  -0.970  0.60 38.28  ? 127 LYS A CD  1 
ATOM   978  C CE  . LYS A 1 127 ? 13.796 4.135  0.023   0.60 39.22  ? 127 LYS A CE  1 
ATOM   979  N NZ  . LYS A 1 127 ? 13.537 3.477  1.336   0.60 39.92  ? 127 LYS A NZ  1 
ATOM   980  N N   . SER A 1 128 ? 10.547 3.975  -6.061  1.00 42.28  ? 128 SER A N   1 
ATOM   981  C CA  . SER A 1 128 ? 9.382  3.717  -6.890  1.00 46.77  ? 128 SER A CA  1 
ATOM   982  C C   . SER A 1 128 ? 8.224  3.224  -6.029  1.00 51.89  ? 128 SER A C   1 
ATOM   983  O O   . SER A 1 128 ? 8.412  2.712  -4.922  1.00 51.38  ? 128 SER A O   1 
ATOM   984  C CB  . SER A 1 128 ? 9.697  2.692  -7.979  1.00 47.30  ? 128 SER A CB  1 
ATOM   985  O OG  . SER A 1 128 ? 9.398  1.379  -7.541  0.90 48.77  ? 128 SER A OG  1 
ATOM   986  N N   . SER A 1 129 ? 7.012  3.393  -6.551  1.00 55.42  ? 129 SER A N   1 
ATOM   987  C CA  . SER A 1 129 ? 5.800  2.966  -5.852  1.00 58.20  ? 129 SER A CA  1 
ATOM   988  C C   . SER A 1 129 ? 5.517  1.490  -6.135  1.00 60.81  ? 129 SER A C   1 
ATOM   989  O O   . SER A 1 129 ? 4.447  1.107  -6.609  1.00 63.13  ? 129 SER A O   1 
ATOM   990  C CB  . SER A 1 129 ? 4.622  3.840  -6.261  1.00 59.12  ? 129 SER A CB  1 
ATOM   991  O OG  . SER A 1 129 ? 4.151  3.473  -7.544  1.00 60.27  ? 129 SER A OG  1 
ATOM   992  N N   . GLY A 1 130 ? 6.502  0.655  -5.821  0.84 61.13  ? 130 GLY A N   1 
ATOM   993  C CA  . GLY A 1 130 ? 6.444  -0.738 -6.216  0.84 64.18  ? 130 GLY A CA  1 
ATOM   994  C C   . GLY A 1 130 ? 6.797  -0.895 -7.680  0.84 64.79  ? 130 GLY A C   1 
ATOM   995  O O   . GLY A 1 130 ? 6.288  -0.160 -8.532  0.84 66.22  ? 130 GLY A O   1 
ATOM   996  N N   . GLY A 1 131 ? 7.673  -1.843 -7.991  0.90 61.05  ? 131 GLY A N   1 
ATOM   997  C CA  . GLY A 1 131 ? 8.179  -1.982 -9.334  0.90 58.82  ? 131 GLY A CA  1 
ATOM   998  C C   . GLY A 1 131 ? 9.527  -1.306 -9.471  0.90 54.21  ? 131 GLY A C   1 
ATOM   999  O O   . GLY A 1 131 ? 10.002 -0.626 -8.555  0.90 54.34  ? 131 GLY A O   1 
ATOM   1000 N N   . PRO A 1 132 ? 10.170 -1.478 -10.624 0.89 51.37  ? 132 PRO A N   1 
ATOM   1001 C CA  . PRO A 1 132 ? 11.536 -0.966 -10.782 0.89 47.10  ? 132 PRO A CA  1 
ATOM   1002 C C   . PRO A 1 132 ? 11.574 0.553  -10.768 0.89 44.16  ? 132 PRO A C   1 
ATOM   1003 O O   . PRO A 1 132 ? 10.679 1.225  -11.286 0.89 44.06  ? 132 PRO A O   1 
ATOM   1004 C CB  . PRO A 1 132 ? 11.972 -1.526 -12.141 0.89 47.59  ? 132 PRO A CB  1 
ATOM   1005 C CG  . PRO A 1 132 ? 10.701 -1.766 -12.877 0.89 49.57  ? 132 PRO A CG  1 
ATOM   1006 C CD  . PRO A 1 132 ? 9.684  -2.153 -11.839 0.89 51.05  ? 132 PRO A CD  1 
ATOM   1007 N N   . PHE A 1 133 ? 12.631 1.086  -10.163 1.00 41.02  ? 133 PHE A N   1 
ATOM   1008 C CA  . PHE A 1 133 ? 12.857 2.523  -10.073 1.00 38.83  ? 133 PHE A CA  1 
ATOM   1009 C C   . PHE A 1 133 ? 13.873 2.923  -11.138 1.00 38.49  ? 133 PHE A C   1 
ATOM   1010 O O   . PHE A 1 133 ? 15.046 2.545  -11.058 1.00 37.42  ? 133 PHE A O   1 
ATOM   1011 C CB  . PHE A 1 133 ? 13.346 2.900  -8.677  1.00 35.65  ? 133 PHE A CB  1 
ATOM   1012 C CG  . PHE A 1 133 ? 13.742 4.336  -8.545  1.00 31.80  ? 133 PHE A CG  1 
ATOM   1013 C CD1 . PHE A 1 133 ? 12.775 5.322  -8.498  1.00 30.75  ? 133 PHE A CD1 1 
ATOM   1014 C CD2 . PHE A 1 133 ? 15.076 4.701  -8.455  1.00 30.71  ? 133 PHE A CD2 1 
ATOM   1015 C CE1 . PHE A 1 133 ? 13.124 6.646  -8.372  1.00 29.52  ? 133 PHE A CE1 1 
ATOM   1016 C CE2 . PHE A 1 133 ? 15.433 6.031  -8.326  1.00 29.39  ? 133 PHE A CE2 1 
ATOM   1017 C CZ  . PHE A 1 133 ? 14.454 7.004  -8.284  1.00 28.65  ? 133 PHE A CZ  1 
ATOM   1018 N N   . VAL A 1 134 ? 13.419 3.679  -12.138 1.00 39.20  ? 134 VAL A N   1 
ATOM   1019 C CA  . VAL A 1 134 ? 14.272 4.138  -13.230 1.00 38.04  ? 134 VAL A CA  1 
ATOM   1020 C C   . VAL A 1 134 ? 14.030 5.628  -13.428 1.00 39.61  ? 134 VAL A C   1 
ATOM   1021 O O   . VAL A 1 134 ? 12.889 6.048  -13.653 1.00 42.12  ? 134 VAL A O   1 
ATOM   1022 C CB  . VAL A 1 134 ? 14.002 3.378  -14.542 1.00 37.52  ? 134 VAL A CB  1 
ATOM   1023 C CG1 . VAL A 1 134 ? 15.107 3.654  -15.551 1.00 34.70  ? 134 VAL A CG1 1 
ATOM   1024 C CG2 . VAL A 1 134 ? 13.864 1.882  -14.292 1.00 38.38  ? 134 VAL A CG2 1 
ATOM   1025 N N   . VAL A 1 135 ? 15.099 6.425  -13.345 1.00 38.09  ? 135 VAL A N   1 
ATOM   1026 C CA  . VAL A 1 135 ? 15.038 7.864  -13.580 1.00 37.27  ? 135 VAL A CA  1 
ATOM   1027 C C   . VAL A 1 135 ? 16.284 8.298  -14.336 1.00 37.23  ? 135 VAL A C   1 
ATOM   1028 O O   . VAL A 1 135 ? 17.345 7.673  -14.237 1.00 36.67  ? 135 VAL A O   1 
ATOM   1029 C CB  . VAL A 1 135 ? 14.917 8.683  -12.271 1.00 37.18  ? 135 VAL A CB  1 
ATOM   1030 C CG1 . VAL A 1 135 ? 13.600 8.410  -11.572 1.00 38.11  ? 135 VAL A CG1 1 
ATOM   1031 C CG2 . VAL A 1 135 ? 16.097 8.395  -11.351 1.00 35.85  ? 135 VAL A CG2 1 
ATOM   1032 N N   . ASP A 1 136 ? 16.145 9.380  -15.100 1.00 37.82  ? 136 ASP A N   1 
ATOM   1033 C CA  . ASP A 1 136 ? 17.276 10.037 -15.740 1.00 37.49  ? 136 ASP A CA  1 
ATOM   1034 C C   . ASP A 1 136 ? 17.737 11.188 -14.858 1.00 38.19  ? 136 ASP A C   1 
ATOM   1035 O O   . ASP A 1 136 ? 16.921 12.001 -14.413 1.00 41.51  ? 136 ASP A O   1 
ATOM   1036 C CB  . ASP A 1 136 ? 16.917 10.553 -17.135 1.00 37.78  ? 136 ASP A CB  1 
ATOM   1037 C CG  . ASP A 1 136 ? 16.843 9.448  -18.167 1.00 38.41  ? 136 ASP A CG  1 
ATOM   1038 O OD1 . ASP A 1 136 ? 15.830 9.382  -18.896 1.00 40.18  ? 136 ASP A OD1 1 
ATOM   1039 O OD2 . ASP A 1 136 ? 17.793 8.640  -18.245 1.00 37.94  ? 136 ASP A OD2 1 
ATOM   1040 N N   . VAL A 1 137 ? 19.039 11.253 -14.606 1.00 36.26  ? 137 VAL A N   1 
ATOM   1041 C CA  . VAL A 1 137 ? 19.619 12.250 -13.715 1.00 34.14  ? 137 VAL A CA  1 
ATOM   1042 C C   . VAL A 1 137 ? 20.157 13.393 -14.562 1.00 35.93  ? 137 VAL A C   1 
ATOM   1043 O O   . VAL A 1 137 ? 21.094 13.209 -15.347 1.00 38.83  ? 137 VAL A O   1 
ATOM   1044 C CB  . VAL A 1 137 ? 20.720 11.642 -12.834 1.00 30.67  ? 137 VAL A CB  1 
ATOM   1045 C CG1 . VAL A 1 137 ? 21.237 12.676 -11.843 1.00 29.70  ? 137 VAL A CG1 1 
ATOM   1046 C CG2 . VAL A 1 137 ? 20.183 10.425 -12.100 1.00 29.37  ? 137 VAL A CG2 1 
ATOM   1047 N N   . VAL A 1 138 ? 19.572 14.576 -14.398 1.00 34.96  ? 138 VAL A N   1 
ATOM   1048 C CA  . VAL A 1 138 ? 19.913 15.751 -15.194 1.00 33.73  ? 138 VAL A CA  1 
ATOM   1049 C C   . VAL A 1 138 ? 20.518 16.800 -14.271 1.00 33.27  ? 138 VAL A C   1 
ATOM   1050 O O   . VAL A 1 138 ? 19.844 17.302 -13.363 1.00 33.36  ? 138 VAL A O   1 
ATOM   1051 C CB  . VAL A 1 138 ? 18.686 16.306 -15.932 1.00 32.68  ? 138 VAL A CB  1 
ATOM   1052 C CG1 . VAL A 1 138 ? 19.069 17.497 -16.788 1.00 33.06  ? 138 VAL A CG1 1 
ATOM   1053 C CG2 . VAL A 1 138 ? 18.053 15.223 -16.788 1.00 32.39  ? 138 VAL A CG2 1 
ATOM   1054 N N   . ILE A 1 139 ? 21.783 17.136 -14.505 1.00 31.81  ? 139 ILE A N   1 
ATOM   1055 C CA  . ILE A 1 139 ? 22.501 18.125 -13.709 1.00 30.68  ? 139 ILE A CA  1 
ATOM   1056 C C   . ILE A 1 139 ? 22.659 19.382 -14.551 1.00 33.84  ? 139 ILE A C   1 
ATOM   1057 O O   . ILE A 1 139 ? 23.369 19.369 -15.564 1.00 32.49  ? 139 ILE A O   1 
ATOM   1058 C CB  . ILE A 1 139 ? 23.871 17.596 -13.253 1.00 30.02  ? 139 ILE A CB  1 
ATOM   1059 C CG1 . ILE A 1 139 ? 23.723 16.227 -12.589 1.00 29.02  ? 139 ILE A CG1 1 
ATOM   1060 C CG2 . ILE A 1 139 ? 24.540 18.586 -12.310 1.00 30.64  ? 139 ILE A CG2 1 
ATOM   1061 C CD1 . ILE A 1 139 ? 25.044 15.579 -12.212 1.00 26.94  ? 139 ILE A CD1 1 
ATOM   1062 N N   . ASN A 1 140 ? 22.001 20.467 -14.134 1.00 36.28  ? 140 ASN A N   1 
ATOM   1063 C CA  . ASN A 1 140 ? 22.098 21.760 -14.817 1.00 38.26  ? 140 ASN A CA  1 
ATOM   1064 C C   . ASN A 1 140 ? 21.758 21.624 -16.300 1.00 40.63  ? 140 ASN A C   1 
ATOM   1065 O O   . ASN A 1 140 ? 22.486 22.091 -17.181 1.00 42.01  ? 140 ASN A O   1 
ATOM   1066 C CB  . ASN A 1 140 ? 23.484 22.378 -14.621 1.00 38.95  ? 140 ASN A CB  1 
ATOM   1067 C CG  . ASN A 1 140 ? 23.805 22.630 -13.160 1.00 40.10  ? 140 ASN A CG  1 
ATOM   1068 O OD1 . ASN A 1 140 ? 22.903 22.821 -12.341 1.00 40.25  ? 140 ASN A OD1 1 
ATOM   1069 N ND2 . ASN A 1 140 ? 25.089 22.631 -12.825 1.00 40.11  ? 140 ASN A ND2 1 
ATOM   1070 N N   . ASP A 1 141 ? 20.640 20.946 -16.567 1.00 41.40  ? 141 ASP A N   1 
ATOM   1071 C CA  . ASP A 1 141 ? 20.057 20.749 -17.892 1.00 43.72  ? 141 ASP A CA  1 
ATOM   1072 C C   . ASP A 1 141 ? 20.885 19.837 -18.789 1.00 43.57  ? 141 ASP A C   1 
ATOM   1073 O O   . ASP A 1 141 ? 20.579 19.715 -19.983 1.00 45.47  ? 141 ASP A O   1 
ATOM   1074 C CB  . ASP A 1 141 ? 19.814 22.083 -18.608 0.80 46.70  ? 141 ASP A CB  1 
ATOM   1075 C CG  . ASP A 1 141 ? 18.942 23.024 -17.800 0.60 49.50  ? 141 ASP A CG  1 
ATOM   1076 O OD1 . ASP A 1 141 ? 17.996 22.539 -17.143 0.60 49.44  ? 141 ASP A OD1 1 
ATOM   1077 O OD2 . ASP A 1 141 ? 19.205 24.246 -17.818 0.60 51.75  ? 141 ASP A OD2 1 
ATOM   1078 N N   . ILE A 1 142 ? 21.914 19.183 -18.257 1.00 41.95  ? 142 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 142 ? 22.726 18.235 -19.013 1.00 41.59  ? 142 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 142 ? 22.470 16.845 -18.444 1.00 37.44  ? 142 ILE A C   1 
ATOM   1081 O O   . ILE A 1 142 ? 22.631 16.622 -17.237 1.00 35.04  ? 142 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 142 ? 24.219 18.595 -18.959 1.00 44.81  ? 142 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 142 ? 24.434 20.045 -19.404 0.76 48.27  ? 142 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 142 ? 25.025 17.646 -19.829 0.76 45.37  ? 142 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 142 ? 25.883 20.484 -19.381 0.77 49.98  ? 142 ILE A CD1 1 
ATOM   1086 N N   . HIS A 1 143 ? 22.060 15.917 -19.309 1.00 36.73  ? 143 HIS A N   1 
ATOM   1087 C CA  . HIS A 1 143 ? 21.814 14.547 -18.877 1.00 32.64  ? 143 HIS A CA  1 
ATOM   1088 C C   . HIS A 1 143 ? 23.111 13.891 -18.428 1.00 31.83  ? 143 HIS A C   1 
ATOM   1089 O O   . HIS A 1 143 ? 24.127 13.945 -19.127 1.00 34.56  ? 143 HIS A O   1 
ATOM   1090 C CB  A HIS A 1 143 ? 21.170 13.739 -20.003 0.56 30.44  ? 143 HIS A CB  1 
ATOM   1091 C CB  B HIS A 1 143 ? 21.183 13.736 -20.010 0.44 30.52  ? 143 HIS A CB  1 
ATOM   1092 C CG  A HIS A 1 143 ? 21.007 12.284 -19.687 0.56 28.14  ? 143 HIS A CG  1 
ATOM   1093 C CG  B HIS A 1 143 ? 19.765 14.113 -20.311 0.44 30.96  ? 143 HIS A CG  1 
ATOM   1094 N ND1 A HIS A 1 143 ? 21.989 11.353 -19.950 0.56 27.12  ? 143 HIS A ND1 1 
ATOM   1095 N ND1 B HIS A 1 143 ? 18.695 13.308 -19.984 0.44 31.07  ? 143 HIS A ND1 1 
ATOM   1096 C CD2 A HIS A 1 143 ? 19.983 11.600 -19.123 0.56 27.21  ? 143 HIS A CD2 1 
ATOM   1097 C CD2 B HIS A 1 143 ? 19.241 15.206 -20.915 0.44 32.54  ? 143 HIS A CD2 1 
ATOM   1098 C CE1 A HIS A 1 143 ? 21.576 10.159 -19.567 0.56 26.30  ? 143 HIS A CE1 1 
ATOM   1099 C CE1 B HIS A 1 143 ? 17.574 13.888 -20.372 0.44 31.71  ? 143 HIS A CE1 1 
ATOM   1100 N NE2 A HIS A 1 143 ? 20.362 10.280 -19.061 0.56 26.51  ? 143 HIS A NE2 1 
ATOM   1101 N NE2 B HIS A 1 143 ? 17.877 15.042 -20.940 0.44 32.70  ? 143 HIS A NE2 1 
ATOM   1102 N N   . PHE A 1 144 ? 23.069 13.263 -17.260 1.00 30.39  ? 144 PHE A N   1 
ATOM   1103 C CA  . PHE A 1 144 ? 24.254 12.708 -16.621 1.00 29.83  ? 144 PHE A CA  1 
ATOM   1104 C C   . PHE A 1 144 ? 24.266 11.190 -16.588 1.00 28.60  ? 144 PHE A C   1 
ATOM   1105 O O   . PHE A 1 144 ? 25.306 10.580 -16.843 1.00 30.17  ? 144 PHE A O   1 
ATOM   1106 C CB  . PHE A 1 144 ? 24.371 13.246 -15.191 1.00 29.05  ? 144 PHE A CB  1 
ATOM   1107 C CG  . PHE A 1 144 ? 25.593 12.774 -14.463 1.00 30.30  ? 144 PHE A CG  1 
ATOM   1108 C CD1 . PHE A 1 144 ? 26.821 13.375 -14.687 1.00 31.00  ? 144 PHE A CD1 1 
ATOM   1109 C CD2 . PHE A 1 144 ? 25.516 11.736 -13.548 1.00 28.36  ? 144 PHE A CD2 1 
ATOM   1110 C CE1 . PHE A 1 144 ? 27.952 12.945 -14.015 1.00 30.88  ? 144 PHE A CE1 1 
ATOM   1111 C CE2 . PHE A 1 144 ? 26.643 11.301 -12.874 1.00 28.61  ? 144 PHE A CE2 1 
ATOM   1112 C CZ  . PHE A 1 144 ? 27.863 11.906 -13.107 1.00 29.81  ? 144 PHE A CZ  1 
ATOM   1113 N N   . GLU A 1 145 ? 23.138 10.562 -16.276 1.00 26.56  ? 145 GLU A N   1 
ATOM   1114 C CA  . GLU A 1 145 ? 23.081 9.112  -16.173 1.00 27.62  ? 145 GLU A CA  1 
ATOM   1115 C C   . GLU A 1 145 ? 21.626 8.688  -16.093 1.00 26.73  ? 145 GLU A C   1 
ATOM   1116 O O   . GLU A 1 145 ? 20.743 9.490  -15.776 1.00 28.21  ? 145 GLU A O   1 
ATOM   1117 C CB  . GLU A 1 145 ? 23.846 8.604  -14.946 1.00 27.79  ? 145 GLU A CB  1 
ATOM   1118 C CG  . GLU A 1 145 ? 23.206 8.968  -13.615 1.00 28.91  ? 145 GLU A CG  1 
ATOM   1119 C CD  . GLU A 1 145 ? 23.983 8.425  -12.434 1.00 32.83  ? 145 GLU A CD  1 
ATOM   1120 O OE1 . GLU A 1 145 ? 23.559 8.643  -11.277 1.00 32.45  ? 145 GLU A OE1 1 
ATOM   1121 O OE2 . GLU A 1 145 ? 25.025 7.778  -12.666 1.00 34.37  ? 145 GLU A OE2 1 
ATOM   1122 N N   . ARG A 1 146 ? 21.393 7.416  -16.387 1.00 26.94  ? 146 ARG A N   1 
ATOM   1123 C CA  . ARG A 1 146 ? 20.118 6.764  -16.135 1.00 30.71  ? 146 ARG A CA  1 
ATOM   1124 C C   . ARG A 1 146 ? 20.304 5.814  -14.960 1.00 33.33  ? 146 ARG A C   1 
ATOM   1125 O O   . ARG A 1 146 ? 21.097 4.866  -15.042 1.00 33.85  ? 146 ARG A O   1 
ATOM   1126 C CB  . ARG A 1 146 ? 19.632 6.014  -17.373 1.00 31.94  ? 146 ARG A CB  1 
ATOM   1127 C CG  . ARG A 1 146 ? 18.333 5.255  -17.175 1.00 34.20  ? 146 ARG A CG  1 
ATOM   1128 C CD  . ARG A 1 146 ? 17.676 4.908  -18.503 0.80 27.41  ? 146 ARG A CD  1 
ATOM   1129 N NE  . ARG A 1 146 ? 17.251 6.104  -19.220 0.70 27.83  ? 146 ARG A NE  1 
ATOM   1130 C CZ  . ARG A 1 146 ? 16.498 6.092  -20.314 0.70 34.75  ? 146 ARG A CZ  1 
ATOM   1131 N NH1 . ARG A 1 146 ? 16.083 4.941  -20.821 0.70 30.19  ? 146 ARG A NH1 1 
ATOM   1132 N NH2 . ARG A 1 146 ? 16.157 7.232  -20.898 0.70 29.68  ? 146 ARG A NH2 1 
ATOM   1133 N N   . PHE A 1 147 ? 19.580 6.070  -13.872 1.00 32.14  ? 147 PHE A N   1 
ATOM   1134 C CA  . PHE A 1 147 ? 19.717 5.297  -12.643 1.00 32.39  ? 147 PHE A CA  1 
ATOM   1135 C C   . PHE A 1 147 ? 18.689 4.171  -12.622 1.00 33.54  ? 147 PHE A C   1 
ATOM   1136 O O   . PHE A 1 147 ? 17.491 4.417  -12.787 1.00 33.79  ? 147 PHE A O   1 
ATOM   1137 C CB  . PHE A 1 147 ? 19.554 6.191  -11.413 1.00 31.49  ? 147 PHE A CB  1 
ATOM   1138 C CG  . PHE A 1 147 ? 19.854 5.497  -10.120 1.00 32.30  ? 147 PHE A CG  1 
ATOM   1139 C CD1 . PHE A 1 147 ? 18.849 4.858  -9.411  1.00 34.42  ? 147 PHE A CD1 1 
ATOM   1140 C CD2 . PHE A 1 147 ? 21.142 5.493  -9.608  1.00 32.08  ? 147 PHE A CD2 1 
ATOM   1141 C CE1 . PHE A 1 147 ? 19.122 4.223  -8.220  1.00 35.60  ? 147 PHE A CE1 1 
ATOM   1142 C CE2 . PHE A 1 147 ? 21.421 4.860  -8.415  1.00 33.23  ? 147 PHE A CE2 1 
ATOM   1143 C CZ  . PHE A 1 147 ? 20.409 4.226  -7.719  1.00 34.94  ? 147 PHE A CZ  1 
ATOM   1144 N N   . ARG A 1 148 ? 19.162 2.940  -12.423 1.00 34.95  ? 148 ARG A N   1 
ATOM   1145 C CA  . ARG A 1 148 ? 18.311 1.774  -12.209 1.00 38.22  ? 148 ARG A CA  1 
ATOM   1146 C C   . ARG A 1 148 ? 18.731 1.150  -10.885 1.00 37.81  ? 148 ARG A C   1 
ATOM   1147 O O   . ARG A 1 148 ? 19.861 0.667  -10.751 1.00 36.37  ? 148 ARG A O   1 
ATOM   1148 C CB  . ARG A 1 148 ? 18.437 0.767  -13.354 1.00 42.60  ? 148 ARG A CB  1 
ATOM   1149 C CG  . ARG A 1 148 ? 17.232 0.710  -14.285 1.00 46.96  ? 148 ARG A CG  1 
ATOM   1150 C CD  . ARG A 1 148 ? 17.284 -0.527 -15.173 1.00 52.29  ? 148 ARG A CD  1 
ATOM   1151 N NE  . ARG A 1 148 ? 16.643 -1.693 -14.566 1.00 54.90  ? 148 ARG A NE  1 
ATOM   1152 C CZ  . ARG A 1 148 ? 15.413 -2.111 -14.854 1.00 57.43  ? 148 ARG A CZ  1 
ATOM   1153 N NH1 . ARG A 1 148 ? 14.675 -1.466 -15.746 1.00 57.65  ? 148 ARG A NH1 1 
ATOM   1154 N NH2 . ARG A 1 148 ? 14.923 -3.182 -14.248 1.00 59.21  ? 148 ARG A NH2 1 
ATOM   1155 N N   . GLY A 1 149 ? 17.827 1.171  -9.910  1.00 39.38  ? 149 GLY A N   1 
ATOM   1156 C CA  . GLY A 1 149 ? 18.119 0.630  -8.599  1.00 38.14  ? 149 GLY A CA  1 
ATOM   1157 C C   . GLY A 1 149 ? 16.961 0.747  -7.628  1.00 36.80  ? 149 GLY A C   1 
ATOM   1158 O O   . GLY A 1 149 ? 15.799 0.767  -8.038  1.00 37.37  ? 149 GLY A O   1 
ATOM   1159 N N   . ASP A 1 150 ? 17.253 0.825  -6.333  1.00 35.37  ? 150 ASP A N   1 
ATOM   1160 C CA  . ASP A 1 150 ? 16.194 0.968  -5.341  1.00 33.25  ? 150 ASP A CA  1 
ATOM   1161 C C   . ASP A 1 150 ? 15.796 2.424  -5.133  1.00 32.91  ? 150 ASP A C   1 
ATOM   1162 O O   . ASP A 1 150 ? 14.620 2.714  -4.891  1.00 34.33  ? 150 ASP A O   1 
ATOM   1163 C CB  . ASP A 1 150 ? 16.633 0.345  -4.013  1.00 32.33  ? 150 ASP A CB  1 
ATOM   1164 C CG  . ASP A 1 150 ? 16.773 -1.161 -4.093  1.00 33.78  ? 150 ASP A CG  1 
ATOM   1165 O OD1 . ASP A 1 150 ? 16.447 -1.730 -5.158  1.00 36.06  ? 150 ASP A OD1 1 
ATOM   1166 O OD2 . ASP A 1 150 ? 17.194 -1.769 -3.083  1.00 32.83  ? 150 ASP A OD2 1 
ATOM   1167 N N   . GLY A 1 151 ? 16.742 3.352  -5.213  1.00 31.25  ? 151 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 151 ? 16.393 4.748  -5.053  1.00 27.99  ? 151 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 151 ? 17.621 5.632  -4.965  1.00 26.86  ? 151 GLY A C   1 
ATOM   1170 O O   . GLY A 1 151 ? 18.748 5.198  -5.218  1.00 26.97  ? 151 GLY A O   1 
ATOM   1171 N N   . LEU A 1 152 ? 17.366 6.897  -4.624  1.00 26.28  ? 152 LEU A N   1 
ATOM   1172 C CA  . LEU A 1 152 ? 18.404 7.909  -4.487  1.00 25.53  ? 152 LEU A CA  1 
ATOM   1173 C C   . LEU A 1 152 ? 18.143 8.718  -3.226  1.00 24.54  ? 152 LEU A C   1 
ATOM   1174 O O   . LEU A 1 152 ? 17.005 8.828  -2.768  1.00 24.78  ? 152 LEU A O   1 
ATOM   1175 C CB  . LEU A 1 152 ? 18.460 8.853  -5.698  1.00 25.56  ? 152 LEU A CB  1 
ATOM   1176 C CG  . LEU A 1 152 ? 18.857 8.223  -7.030  1.00 27.17  ? 152 LEU A CG  1 
ATOM   1177 C CD1 . LEU A 1 152 ? 18.607 9.206  -8.148  1.00 26.70  ? 152 LEU A CD1 1 
ATOM   1178 C CD2 . LEU A 1 152 ? 20.316 7.818  -6.994  1.00 27.57  ? 152 LEU A CD2 1 
ATOM   1179 N N   . CYS A 1 153 ? 19.210 9.287  -2.669  1.00 25.56  ? 153 CYS A N   1 
ATOM   1180 C CA  . CYS A 1 153 ? 19.135 10.063 -1.436  1.00 27.11  ? 153 CYS A CA  1 
ATOM   1181 C C   . CYS A 1 153 ? 19.935 11.345 -1.609  1.00 26.36  ? 153 CYS A C   1 
ATOM   1182 O O   . CYS A 1 153 ? 21.135 11.296 -1.894  1.00 25.63  ? 153 CYS A O   1 
ATOM   1183 C CB  . CYS A 1 153 ? 19.660 9.255  -0.245  1.00 27.58  ? 153 CYS A CB  1 
ATOM   1184 S SG  . CYS A 1 153 ? 19.824 10.194 1.288   1.00 27.30  ? 153 CYS A SG  1 
ATOM   1185 N N   . MET A 1 154 ? 19.271 12.483 -1.447  1.00 27.44  ? 154 MET A N   1 
ATOM   1186 C CA  . MET A 1 154 ? 19.903 13.794 -1.497  1.00 26.34  ? 154 MET A CA  1 
ATOM   1187 C C   . MET A 1 154 ? 19.904 14.364 -0.086  1.00 27.66  ? 154 MET A C   1 
ATOM   1188 O O   . MET A 1 154 ? 18.838 14.544 0.513   1.00 26.78  ? 154 MET A O   1 
ATOM   1189 C CB  . MET A 1 154 ? 19.168 14.725 -2.460  1.00 25.78  ? 154 MET A CB  1 
ATOM   1190 C CG  . MET A 1 154 ? 19.851 16.073 -2.659  1.00 28.46  ? 154 MET A CG  1 
ATOM   1191 S SD  . MET A 1 154 ? 21.427 15.946 -3.527  1.00 28.07  ? 154 MET A SD  1 
ATOM   1192 C CE  . MET A 1 154 ? 20.876 15.975 -5.232  1.00 27.33  ? 154 MET A CE  1 
ATOM   1193 N N   . SER A 1 155 ? 21.090 14.650 0.435   1.00 28.47  ? 155 SER A N   1 
ATOM   1194 C CA  . SER A 1 155 ? 21.260 14.986 1.838   1.00 27.03  ? 155 SER A CA  1 
ATOM   1195 C C   . SER A 1 155 ? 21.778 16.406 2.016   1.00 26.81  ? 155 SER A C   1 
ATOM   1196 O O   . SER A 1 155 ? 22.506 16.935 1.171   1.00 28.77  ? 155 SER A O   1 
ATOM   1197 C CB  . SER A 1 155 ? 22.225 14.012 2.514   1.00 27.04  ? 155 SER A CB  1 
ATOM   1198 O OG  . SER A 1 155 ? 22.609 14.491 3.790   1.00 28.78  ? 155 SER A OG  1 
ATOM   1199 N N   . THR A 1 156 ? 21.392 17.011 3.133   1.00 25.53  ? 156 THR A N   1 
ATOM   1200 C CA  . THR A 1 156 ? 21.964 18.267 3.587   1.00 26.21  ? 156 THR A CA  1 
ATOM   1201 C C   . THR A 1 156 ? 23.297 17.988 4.271   1.00 27.24  ? 156 THR A C   1 
ATOM   1202 O O   . THR A 1 156 ? 23.641 16.834 4.525   1.00 28.89  ? 156 THR A O   1 
ATOM   1203 C CB  . THR A 1 156 ? 20.989 18.962 4.535   1.00 27.09  ? 156 THR A CB  1 
ATOM   1204 O OG1 . THR A 1 156 ? 20.935 18.246 5.775   1.00 26.45  ? 156 THR A OG1 1 
ATOM   1205 C CG2 . THR A 1 156 ? 19.603 18.997 3.929   1.00 26.51  ? 156 THR A CG2 1 
ATOM   1206 N N   . PRO A 1 157 ? 24.099 19.030 4.564   1.00 26.76  ? 157 PRO A N   1 
ATOM   1207 C CA  . PRO A 1 157 ? 25.348 18.796 5.306   1.00 25.35  ? 157 PRO A CA  1 
ATOM   1208 C C   . PRO A 1 157 ? 25.131 18.113 6.648   1.00 26.03  ? 157 PRO A C   1 
ATOM   1209 O O   . PRO A 1 157 ? 25.686 17.037 6.892   1.00 25.28  ? 157 PRO A O   1 
ATOM   1210 C CB  . PRO A 1 157 ? 25.916 20.208 5.481   1.00 25.58  ? 157 PRO A CB  1 
ATOM   1211 C CG  . PRO A 1 157 ? 25.436 20.934 4.282   1.00 26.41  ? 157 PRO A CG  1 
ATOM   1212 C CD  . PRO A 1 157 ? 24.050 20.393 4.002   1.00 25.60  ? 157 PRO A CD  1 
ATOM   1213 N N   . SER A 1 158 ? 24.321 18.722 7.522   1.00 27.65  ? 158 SER A N   1 
ATOM   1214 C CA  . SER A 1 158 ? 24.048 18.126 8.827   1.00 27.82  ? 158 SER A CA  1 
ATOM   1215 C C   . SER A 1 158 ? 23.341 16.782 8.716   1.00 25.07  ? 158 SER A C   1 
ATOM   1216 O O   . SER A 1 158 ? 23.350 16.006 9.679   1.00 23.09  ? 158 SER A O   1 
ATOM   1217 C CB  . SER A 1 158 ? 23.205 19.075 9.680   1.00 29.80  ? 158 SER A CB  1 
ATOM   1218 O OG  . SER A 1 158 ? 21.869 19.133 9.207   1.00 30.17  ? 158 SER A OG  1 
ATOM   1219 N N   . GLY A 1 159 ? 22.721 16.497 7.574   1.00 23.83  ? 159 GLY A N   1 
ATOM   1220 C CA  . GLY A 1 159 ? 22.093 15.218 7.335   1.00 24.08  ? 159 GLY A CA  1 
ATOM   1221 C C   . GLY A 1 159 ? 23.006 14.154 6.778   1.00 24.70  ? 159 GLY A C   1 
ATOM   1222 O O   . GLY A 1 159 ? 22.578 13.007 6.617   1.00 26.59  ? 159 GLY A O   1 
ATOM   1223 N N   . THR A 1 160 ? 24.259 14.501 6.470   1.00 22.84  ? 160 THR A N   1 
ATOM   1224 C CA  . THR A 1 160 ? 25.200 13.525 5.935   1.00 24.35  ? 160 THR A CA  1 
ATOM   1225 C C   . THR A 1 160 ? 25.602 12.483 6.969   1.00 29.07  ? 160 THR A C   1 
ATOM   1226 O O   . THR A 1 160 ? 26.044 11.394 6.591   1.00 32.82  ? 160 THR A O   1 
ATOM   1227 C CB  . THR A 1 160 ? 26.446 14.231 5.394   1.00 22.48  ? 160 THR A CB  1 
ATOM   1228 O OG1 . THR A 1 160 ? 26.956 15.140 6.380   1.00 24.10  ? 160 THR A OG1 1 
ATOM   1229 C CG2 . THR A 1 160 ? 26.112 15.000 4.132   1.00 20.75  ? 160 THR A CG2 1 
ATOM   1230 N N   . THR A 1 161 ? 25.459 12.791 8.258   1.00 28.54  ? 161 THR A N   1 
ATOM   1231 C CA  . THR A 1 161 ? 25.711 11.829 9.324   1.00 29.87  ? 161 THR A CA  1 
ATOM   1232 C C   . THR A 1 161 ? 24.538 10.882 9.553   1.00 28.41  ? 161 THR A C   1 
ATOM   1233 O O   . THR A 1 161 ? 24.654 9.959  10.366  1.00 26.07  ? 161 THR A O   1 
ATOM   1234 C CB  . THR A 1 161 ? 26.041 12.560 10.631  1.00 32.36  ? 161 THR A CB  1 
ATOM   1235 O OG1 . THR A 1 161 ? 24.994 13.490 10.946  1.00 33.59  ? 161 THR A OG1 1 
ATOM   1236 C CG2 . THR A 1 161 ? 27.359 13.312 10.509  1.00 32.91  ? 161 THR A CG2 1 
ATOM   1237 N N   . ALA A 1 162 ? 23.421 11.078 8.852   1.00 28.29  ? 162 ALA A N   1 
ATOM   1238 C CA  . ALA A 1 162 ? 22.236 10.252 9.047   1.00 27.66  ? 162 ALA A CA  1 
ATOM   1239 C C   . ALA A 1 162 ? 22.115 9.178  7.970   1.00 28.15  ? 162 ALA A C   1 
ATOM   1240 O O   . ALA A 1 162 ? 23.004 8.333  7.820   1.00 29.66  ? 162 ALA A O   1 
ATOM   1241 C CB  . ALA A 1 162 ? 20.981 11.128 9.069   1.00 26.00  ? 162 ALA A CB  1 
ATOM   1242 N N   . TYR A 1 163 ? 21.007 9.208  7.221   1.00 29.19  ? 163 TYR A N   1 
ATOM   1243 C CA  . TYR A 1 163 ? 20.771 8.216  6.174   1.00 29.91  ? 163 TYR A CA  1 
ATOM   1244 C C   . TYR A 1 163 ? 21.899 8.209  5.150   1.00 27.36  ? 163 TYR A C   1 
ATOM   1245 O O   . TYR A 1 163 ? 22.296 7.146  4.660   1.00 27.04  ? 163 TYR A O   1 
ATOM   1246 C CB  . TYR A 1 163 ? 19.430 8.497  5.493   1.00 32.57  ? 163 TYR A CB  1 
ATOM   1247 C CG  . TYR A 1 163 ? 18.801 7.325  4.765   1.00 36.52  ? 163 TYR A CG  1 
ATOM   1248 C CD1 . TYR A 1 163 ? 19.423 6.081  4.724   1.00 38.02  ? 163 TYR A CD1 1 
ATOM   1249 C CD2 . TYR A 1 163 ? 17.576 7.467  4.115   1.00 40.51  ? 163 TYR A CD2 1 
ATOM   1250 C CE1 . TYR A 1 163 ? 18.844 5.017  4.058   1.00 40.84  ? 163 TYR A CE1 1 
ATOM   1251 C CE2 . TYR A 1 163 ? 16.993 6.409  3.449   1.00 43.50  ? 163 TYR A CE2 1 
ATOM   1252 C CZ  . TYR A 1 163 ? 17.631 5.187  3.423   1.00 44.45  ? 163 TYR A CZ  1 
ATOM   1253 O OH  . TYR A 1 163 ? 17.048 4.133  2.756   1.00 45.99  ? 163 TYR A OH  1 
ATOM   1254 N N   . ASN A 1 164 ? 22.428 9.390  4.817   1.00 25.65  ? 164 ASN A N   1 
ATOM   1255 C CA  . ASN A 1 164 ? 23.504 9.480  3.835   1.00 26.11  ? 164 ASN A CA  1 
ATOM   1256 C C   . ASN A 1 164 ? 24.709 8.651  4.257   1.00 28.87  ? 164 ASN A C   1 
ATOM   1257 O O   . ASN A 1 164 ? 25.360 8.015  3.421   1.00 30.48  ? 164 ASN A O   1 
ATOM   1258 C CB  . ASN A 1 164 ? 23.895 10.947 3.638   1.00 27.12  ? 164 ASN A CB  1 
ATOM   1259 C CG  . ASN A 1 164 ? 25.194 11.114 2.878   1.00 29.84  ? 164 ASN A CG  1 
ATOM   1260 O OD1 . ASN A 1 164 ? 25.202 11.199 1.652   1.00 30.54  ? 164 ASN A OD1 1 
ATOM   1261 N ND2 . ASN A 1 164 ? 26.302 11.176 3.606   1.00 30.63  ? 164 ASN A ND2 1 
ATOM   1262 N N   . LYS A 1 165 ? 25.009 8.634  5.557   1.00 29.18  ? 165 LYS A N   1 
ATOM   1263 C CA  . LYS A 1 165 ? 26.166 7.890  6.043   1.00 28.98  ? 165 LYS A CA  1 
ATOM   1264 C C   . LYS A 1 165 ? 25.998 6.391  5.832   1.00 29.38  ? 165 LYS A C   1 
ATOM   1265 O O   . LYS A 1 165 ? 26.946 5.709  5.429   1.00 29.36  ? 165 LYS A O   1 
ATOM   1266 C CB  . LYS A 1 165 ? 26.399 8.196  7.521   1.00 27.85  ? 165 LYS A CB  1 
ATOM   1267 C CG  . LYS A 1 165 ? 27.567 7.451  8.151   1.00 26.68  ? 165 LYS A CG  1 
ATOM   1268 C CD  . LYS A 1 165 ? 27.750 7.860  9.603   1.00 28.08  ? 165 LYS A CD  1 
ATOM   1269 C CE  . LYS A 1 165 ? 28.911 7.124  10.245  0.90 29.14  ? 165 LYS A CE  1 
ATOM   1270 N NZ  . LYS A 1 165 ? 28.673 5.653  10.278  0.80 31.20  ? 165 LYS A NZ  1 
ATOM   1271 N N   . SER A 1 166 ? 24.806 5.857  6.104   1.00 29.02  ? 166 SER A N   1 
ATOM   1272 C CA  . SER A 1 166 ? 24.595 4.421  5.963   1.00 28.77  ? 166 SER A CA  1 
ATOM   1273 C C   . SER A 1 166 ? 24.668 3.962  4.515   1.00 28.14  ? 166 SER A C   1 
ATOM   1274 O O   . SER A 1 166 ? 24.865 2.767  4.270   1.00 28.48  ? 166 SER A O   1 
ATOM   1275 C CB  . SER A 1 166 ? 23.249 4.024  6.567   1.00 29.93  ? 166 SER A CB  1 
ATOM   1276 O OG  . SER A 1 166 ? 23.299 4.056  7.985   1.00 33.04  ? 166 SER A OG  1 
ATOM   1277 N N   . LEU A 1 167 ? 24.511 4.874  3.559   1.00 28.17  ? 167 LEU A N   1 
ATOM   1278 C CA  . LEU A 1 167 ? 24.597 4.553  2.142   1.00 28.87  ? 167 LEU A CA  1 
ATOM   1279 C C   . LEU A 1 167 ? 26.002 4.733  1.583   1.00 28.71  ? 167 LEU A C   1 
ATOM   1280 O O   . LEU A 1 167 ? 26.181 4.691  0.362   1.00 28.51  ? 167 LEU A O   1 
ATOM   1281 C CB  . LEU A 1 167 ? 23.610 5.412  1.349   1.00 26.78  ? 167 LEU A CB  1 
ATOM   1282 C CG  . LEU A 1 167 ? 22.130 5.164  1.644   1.00 26.35  ? 167 LEU A CG  1 
ATOM   1283 C CD1 . LEU A 1 167 ? 21.271 6.311  1.136   1.00 24.09  ? 167 LEU A CD1 1 
ATOM   1284 C CD2 . LEU A 1 167 ? 21.677 3.842  1.039   1.00 25.31  ? 167 LEU A CD2 1 
ATOM   1285 N N   . GLY A 1 168 ? 26.997 4.944  2.442   1.00 30.21  ? 168 GLY A N   1 
ATOM   1286 C CA  . GLY A 1 168 ? 28.358 5.124  1.990   1.00 30.01  ? 168 GLY A CA  1 
ATOM   1287 C C   . GLY A 1 168 ? 28.754 6.554  1.694   1.00 28.73  ? 168 GLY A C   1 
ATOM   1288 O O   . GLY A 1 168 ? 29.872 6.781  1.217   1.00 30.70  ? 168 GLY A O   1 
ATOM   1289 N N   . GLY A 1 169 ? 27.884 7.522  1.962   1.00 25.29  ? 169 GLY A N   1 
ATOM   1290 C CA  . GLY A 1 169 ? 28.189 8.905  1.666   1.00 24.88  ? 169 GLY A CA  1 
ATOM   1291 C C   . GLY A 1 169 ? 29.249 9.483  2.585   1.00 26.42  ? 169 GLY A C   1 
ATOM   1292 O O   . GLY A 1 169 ? 29.646 8.898  3.593   1.00 25.43  ? 169 GLY A O   1 
ATOM   1293 N N   . ALA A 1 170 ? 29.716 10.669 2.219   1.00 27.47  ? 170 ALA A N   1 
ATOM   1294 C CA  . ALA A 1 170 ? 30.730 11.358 2.999   1.00 27.04  ? 170 ALA A CA  1 
ATOM   1295 C C   . ALA A 1 170 ? 30.080 12.277 4.027   1.00 26.33  ? 170 ALA A C   1 
ATOM   1296 O O   . ALA A 1 170 ? 28.921 12.680 3.895   1.00 26.38  ? 170 ALA A O   1 
ATOM   1297 C CB  . ALA A 1 170 ? 31.660 12.161 2.089   1.00 26.22  ? 170 ALA A CB  1 
ATOM   1298 N N   . LEU A 1 171 ? 30.848 12.607 5.061   1.00 24.94  ? 171 LEU A N   1 
ATOM   1299 C CA  . LEU A 1 171 ? 30.393 13.491 6.125   1.00 24.07  ? 171 LEU A CA  1 
ATOM   1300 C C   . LEU A 1 171 ? 30.851 14.910 5.821   1.00 26.20  ? 171 LEU A C   1 
ATOM   1301 O O   . LEU A 1 171 ? 32.044 15.152 5.622   1.00 29.44  ? 171 LEU A O   1 
ATOM   1302 C CB  . LEU A 1 171 ? 30.921 13.027 7.482   1.00 24.18  ? 171 LEU A CB  1 
ATOM   1303 C CG  . LEU A 1 171 ? 30.639 11.560 7.831   1.00 24.70  ? 171 LEU A CG  1 
ATOM   1304 C CD1 . LEU A 1 171 ? 30.960 11.261 9.287   1.00 25.49  ? 171 LEU A CD1 1 
ATOM   1305 C CD2 . LEU A 1 171 ? 29.198 11.172 7.502   1.00 24.85  ? 171 LEU A CD2 1 
ATOM   1306 N N   . MET A 1 172 ? 29.905 15.841 5.790   1.00 25.83  ? 172 MET A N   1 
ATOM   1307 C CA  . MET A 1 172 ? 30.134 17.187 5.286   1.00 26.66  ? 172 MET A CA  1 
ATOM   1308 C C   . MET A 1 172 ? 29.948 18.199 6.409   1.00 25.16  ? 172 MET A C   1 
ATOM   1309 O O   . MET A 1 172 ? 28.911 18.201 7.081   1.00 24.73  ? 172 MET A O   1 
ATOM   1310 C CB  . MET A 1 172 ? 29.174 17.485 4.129   0.80 28.32  ? 172 MET A CB  1 
ATOM   1311 C CG  . MET A 1 172 ? 29.782 18.268 2.986   0.80 30.58  ? 172 MET A CG  1 
ATOM   1312 S SD  . MET A 1 172 ? 28.888 18.011 1.440   0.80 33.46  ? 172 MET A SD  1 
ATOM   1313 C CE  . MET A 1 172 ? 27.188 18.267 1.943   0.80 32.78  ? 172 MET A CE  1 
ATOM   1314 N N   . HIS A 1 173 ? 30.945 19.059 6.607   1.00 25.45  ? 173 HIS A N   1 
ATOM   1315 C CA  . HIS A 1 173 ? 30.816 20.097 7.621   1.00 27.50  ? 173 HIS A CA  1 
ATOM   1316 C C   . HIS A 1 173 ? 29.756 21.109 7.193   1.00 30.68  ? 173 HIS A C   1 
ATOM   1317 O O   . HIS A 1 173 ? 29.737 21.546 6.039   1.00 32.55  ? 173 HIS A O   1 
ATOM   1318 C CB  . HIS A 1 173 ? 32.143 20.813 7.870   1.00 27.53  ? 173 HIS A CB  1 
ATOM   1319 C CG  . HIS A 1 173 ? 32.090 21.782 9.013   1.00 29.72  ? 173 HIS A CG  1 
ATOM   1320 N ND1 . HIS A 1 173 ? 31.733 23.103 8.851   1.00 30.14  ? 173 HIS A ND1 1 
ATOM   1321 C CD2 . HIS A 1 173 ? 32.327 21.616 10.336  1.00 30.63  ? 173 HIS A CD2 1 
ATOM   1322 C CE1 . HIS A 1 173 ? 31.762 23.713 10.023  1.00 29.87  ? 173 HIS A CE1 1 
ATOM   1323 N NE2 . HIS A 1 173 ? 32.119 22.833 10.941  1.00 31.19  ? 173 HIS A NE2 1 
ATOM   1324 N N   . PRO A 1 174 ? 28.861 21.506 8.107   1.00 31.88  ? 174 PRO A N   1 
ATOM   1325 C CA  . PRO A 1 174 ? 27.711 22.335 7.716   1.00 30.70  ? 174 PRO A CA  1 
ATOM   1326 C C   . PRO A 1 174 ? 28.053 23.770 7.351   1.00 31.67  ? 174 PRO A C   1 
ATOM   1327 O O   . PRO A 1 174 ? 27.151 24.514 6.956   1.00 31.42  ? 174 PRO A O   1 
ATOM   1328 C CB  . PRO A 1 174 ? 26.811 22.282 8.961   1.00 30.87  ? 174 PRO A CB  1 
ATOM   1329 C CG  . PRO A 1 174 ? 27.739 21.978 10.085  1.00 31.37  ? 174 PRO A CG  1 
ATOM   1330 C CD  . PRO A 1 174 ? 28.798 21.088 9.515   1.00 30.94  ? 174 PRO A CD  1 
ATOM   1331 N N   . SER A 1 175 ? 29.309 24.202 7.463   1.00 33.44  ? 175 SER A N   1 
ATOM   1332 C CA  . SER A 1 175 ? 29.662 25.505 6.913   1.00 35.91  ? 175 SER A CA  1 
ATOM   1333 C C   . SER A 1 175 ? 29.699 25.472 5.392   1.00 37.16  ? 175 SER A C   1 
ATOM   1334 O O   . SER A 1 175 ? 29.630 26.526 4.752   1.00 38.16  ? 175 SER A O   1 
ATOM   1335 C CB  . SER A 1 175 ? 31.009 25.978 7.469   1.00 37.86  ? 175 SER A CB  1 
ATOM   1336 O OG  . SER A 1 175 ? 32.075 25.187 6.973   1.00 37.78  ? 175 SER A OG  1 
ATOM   1337 N N   . ILE A 1 176 ? 29.792 24.282 4.807   1.00 36.22  ? 176 ILE A N   1 
ATOM   1338 C CA  . ILE A 1 176 ? 29.770 24.121 3.358   1.00 36.58  ? 176 ILE A CA  1 
ATOM   1339 C C   . ILE A 1 176 ? 28.320 24.099 2.896   1.00 37.93  ? 176 ILE A C   1 
ATOM   1340 O O   . ILE A 1 176 ? 27.533 23.247 3.325   1.00 38.65  ? 176 ILE A O   1 
ATOM   1341 C CB  . ILE A 1 176 ? 30.508 22.842 2.939   1.00 35.00  ? 176 ILE A CB  1 
ATOM   1342 C CG1 . ILE A 1 176 ? 31.965 22.906 3.406   1.00 34.71  ? 176 ILE A CG1 1 
ATOM   1343 C CG2 . ILE A 1 176 ? 30.416 22.642 1.433   1.00 35.21  ? 176 ILE A CG2 1 
ATOM   1344 C CD1 . ILE A 1 176 ? 32.739 21.632 3.189   1.00 34.16  ? 176 ILE A CD1 1 
ATOM   1345 N N   . GLU A 1 177 ? 27.955 25.046 2.033   1.00 36.41  ? 177 GLU A N   1 
ATOM   1346 C CA  . GLU A 1 177 ? 26.600 25.118 1.489   1.00 34.39  ? 177 GLU A CA  1 
ATOM   1347 C C   . GLU A 1 177 ? 26.536 24.169 0.300   1.00 31.41  ? 177 GLU A C   1 
ATOM   1348 O O   . GLU A 1 177 ? 26.875 24.524 -0.830  1.00 28.94  ? 177 GLU A O   1 
ATOM   1349 C CB  . GLU A 1 177 ? 26.241 26.547 1.100   1.00 37.07  ? 177 GLU A CB  1 
ATOM   1350 C CG  . GLU A 1 177 ? 26.441 27.571 2.215   0.80 38.60  ? 177 GLU A CG  1 
ATOM   1351 C CD  . GLU A 1 177 ? 25.733 28.887 1.944   0.60 41.47  ? 177 GLU A CD  1 
ATOM   1352 O OE1 . GLU A 1 177 ? 24.566 29.034 2.364   0.60 42.40  ? 177 GLU A OE1 1 
ATOM   1353 O OE2 . GLU A 1 177 ? 26.341 29.773 1.308   0.60 43.73  ? 177 GLU A OE2 1 
ATOM   1354 N N   . ALA A 1 178 ? 26.101 22.939 0.556   1.00 29.36  ? 178 ALA A N   1 
ATOM   1355 C CA  . ALA A 1 178 ? 26.100 21.918 -0.479  1.00 27.81  ? 178 ALA A CA  1 
ATOM   1356 C C   . ALA A 1 178 ? 25.000 20.901 -0.212  1.00 27.80  ? 178 ALA A C   1 
ATOM   1357 O O   . ALA A 1 178 ? 24.335 20.921 0.826   1.00 27.61  ? 178 ALA A O   1 
ATOM   1358 C CB  . ALA A 1 178 ? 27.461 21.219 -0.569  1.00 22.91  ? 178 ALA A CB  1 
ATOM   1359 N N   . MET A 1 179 ? 24.818 20.007 -1.181  1.00 27.54  ? 179 MET A N   1 
ATOM   1360 C CA  . MET A 1 179 ? 23.944 18.855 -1.045  1.00 29.12  ? 179 MET A CA  1 
ATOM   1361 C C   . MET A 1 179 ? 24.653 17.645 -1.635  1.00 29.46  ? 179 MET A C   1 
ATOM   1362 O O   . MET A 1 179 ? 25.401 17.761 -2.610  1.00 30.63  ? 179 MET A O   1 
ATOM   1363 C CB  . MET A 1 179 ? 22.594 19.075 -1.739  1.00 29.55  ? 179 MET A CB  1 
ATOM   1364 C CG  . MET A 1 179 ? 22.690 19.324 -3.234  1.00 31.64  ? 179 MET A CG  1 
ATOM   1365 S SD  . MET A 1 179 ? 21.071 19.543 -3.993  1.00 32.60  ? 179 MET A SD  1 
ATOM   1366 C CE  . MET A 1 179 ? 21.529 19.802 -5.703  1.00 30.94  ? 179 MET A CE  1 
ATOM   1367 N N   . GLN A 1 180 ? 24.422 16.483 -1.031  1.00 29.01  ? 180 GLN A N   1 
ATOM   1368 C CA  . GLN A 1 180 ? 25.093 15.251 -1.424  1.00 28.49  ? 180 GLN A CA  1 
ATOM   1369 C C   . GLN A 1 180 ? 24.066 14.231 -1.888  1.00 28.95  ? 180 GLN A C   1 
ATOM   1370 O O   . GLN A 1 180 ? 23.086 13.968 -1.184  1.00 27.87  ? 180 GLN A O   1 
ATOM   1371 C CB  . GLN A 1 180 ? 25.923 14.678 -0.272  1.00 28.57  ? 180 GLN A CB  1 
ATOM   1372 C CG  . GLN A 1 180 ? 26.675 13.408 -0.638  1.00 29.71  ? 180 GLN A CG  1 
ATOM   1373 C CD  . GLN A 1 180 ? 27.638 12.960 0.444   1.00 31.22  ? 180 GLN A CD  1 
ATOM   1374 O OE1 . GLN A 1 180 ? 28.300 11.930 0.310   1.00 31.32  ? 180 GLN A OE1 1 
ATOM   1375 N NE2 . GLN A 1 180 ? 27.724 13.734 1.521   1.00 32.54  ? 180 GLN A NE2 1 
ATOM   1376 N N   . LEU A 1 181 ? 24.301 13.655 -3.064  1.00 30.94  ? 181 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 181 ? 23.431 12.642 -3.646  1.00 31.03  ? 181 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 181 ? 24.120 11.287 -3.581  1.00 32.15  ? 181 LEU A C   1 
ATOM   1379 O O   . LEU A 1 181 ? 25.255 11.144 -4.044  1.00 31.35  ? 181 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 181 ? 23.084 12.987 -5.095  1.00 30.94  ? 181 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 181 ? 22.223 11.953 -5.825  1.00 29.74  ? 181 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 181 ? 20.789 11.999 -5.314  1.00 29.37  ? 181 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 181 ? 22.274 12.155 -7.336  1.00 28.18  ? 181 LEU A CD2 1 
ATOM   1384 N N   . THR A 1 182 ? 23.436 10.300 -3.009  1.00 32.41  ? 182 THR A N   1 
ATOM   1385 C CA  . THR A 1 182 ? 23.960 8.948  -2.902  1.00 33.37  ? 182 THR A CA  1 
ATOM   1386 C C   . THR A 1 182 ? 23.001 7.960  -3.555  1.00 35.28  ? 182 THR A C   1 
ATOM   1387 O O   . THR A 1 182 ? 21.810 8.237  -3.728  1.00 36.89  ? 182 THR A O   1 
ATOM   1388 C CB  . THR A 1 182 ? 24.204 8.554  -1.439  1.00 33.82  ? 182 THR A CB  1 
ATOM   1389 O OG1 . THR A 1 182 ? 23.048 8.873  -0.655  1.00 34.90  ? 182 THR A OG1 1 
ATOM   1390 C CG2 . THR A 1 182 ? 25.407 9.295  -0.886  1.00 34.89  ? 182 THR A CG2 1 
ATOM   1391 N N   . GLU A 1 183 ? 23.537 6.800  -3.920  1.00 35.80  ? 183 GLU A N   1 
ATOM   1392 C CA  . GLU A 1 183 ? 22.762 5.767  -4.589  1.00 35.60  ? 183 GLU A CA  1 
ATOM   1393 C C   . GLU A 1 183 ? 22.222 4.753  -3.588  1.00 36.79  ? 183 GLU A C   1 
ATOM   1394 O O   . GLU A 1 183 ? 22.778 4.559  -2.503  1.00 37.60  ? 183 GLU A O   1 
ATOM   1395 C CB  . GLU A 1 183 ? 23.611 5.043  -5.634  1.00 36.96  ? 183 GLU A CB  1 
ATOM   1396 C CG  . GLU A 1 183 ? 24.219 5.945  -6.689  1.00 38.45  ? 183 GLU A CG  1 
ATOM   1397 C CD  . GLU A 1 183 ? 24.942 5.159  -7.763  1.00 40.22  ? 183 GLU A CD  1 
ATOM   1398 O OE1 . GLU A 1 183 ? 25.122 3.934  -7.581  1.00 40.58  ? 183 GLU A OE1 1 
ATOM   1399 O OE2 . GLU A 1 183 ? 25.329 5.759  -8.791  1.00 40.45  ? 183 GLU A OE2 1 
ATOM   1400 N N   . MET A 1 184 ? 21.125 4.104  -3.967  1.00 37.24  ? 184 MET A N   1 
ATOM   1401 C CA  . MET A 1 184 ? 20.549 3.001  -3.202  1.00 36.60  ? 184 MET A CA  1 
ATOM   1402 C C   . MET A 1 184 ? 20.553 1.759  -4.086  1.00 36.90  ? 184 MET A C   1 
ATOM   1403 O O   . MET A 1 184 ? 19.590 1.515  -4.821  1.00 41.18  ? 184 MET A O   1 
ATOM   1404 C CB  . MET A 1 184 ? 19.137 3.325  -2.728  1.00 35.75  ? 184 MET A CB  1 
ATOM   1405 C CG  . MET A 1 184 ? 19.036 4.489  -1.774  0.80 34.24  ? 184 MET A CG  1 
ATOM   1406 S SD  . MET A 1 184 ? 17.335 4.672  -1.212  0.80 34.92  ? 184 MET A SD  1 
ATOM   1407 C CE  . MET A 1 184 ? 17.457 6.184  -0.267  0.80 34.78  ? 184 MET A CE  1 
ATOM   1408 N N   . ALA A 1 185 ? 21.637 0.988  -4.020  1.00 34.75  ? 185 ALA A N   1 
ATOM   1409 C CA  . ALA A 1 185 ? 21.741 -0.315 -4.677  1.00 36.36  ? 185 ALA A CA  1 
ATOM   1410 C C   . ALA A 1 185 ? 21.382 -0.228 -6.164  1.00 38.51  ? 185 ALA A C   1 
ATOM   1411 O O   . ALA A 1 185 ? 20.399 -0.797 -6.638  1.00 39.92  ? 185 ALA A O   1 
ATOM   1412 C CB  . ALA A 1 185 ? 20.862 -1.346 -3.962  1.00 37.26  ? 185 ALA A CB  1 
ATOM   1413 N N   . SER A 1 186 ? 22.213 0.511  -6.891  1.00 36.46  ? 186 SER A N   1 
ATOM   1414 C CA  . SER A 1 186 ? 22.078 0.576  -8.337  1.00 35.30  ? 186 SER A CA  1 
ATOM   1415 C C   . SER A 1 186 ? 22.584 -0.714 -8.967  1.00 35.22  ? 186 SER A C   1 
ATOM   1416 O O   . SER A 1 186 ? 23.509 -1.354 -8.459  1.00 35.93  ? 186 SER A O   1 
ATOM   1417 C CB  . SER A 1 186 ? 22.859 1.759  -8.909  1.00 34.48  ? 186 SER A CB  1 
ATOM   1418 O OG  . SER A 1 186 ? 24.258 1.577  -8.756  1.00 34.66  ? 186 SER A OG  1 
ATOM   1419 N N   . ILE A 1 187 ? 21.976 -1.093 -10.086 1.00 35.28  ? 187 ILE A N   1 
ATOM   1420 C CA  . ILE A 1 187 ? 22.446 -2.240 -10.853 1.00 37.09  ? 187 ILE A CA  1 
ATOM   1421 C C   . ILE A 1 187 ? 23.471 -1.751 -11.869 1.00 33.28  ? 187 ILE A C   1 
ATOM   1422 O O   . ILE A 1 187 ? 23.245 -0.756 -12.569 1.00 28.93  ? 187 ILE A O   1 
ATOM   1423 C CB  . ILE A 1 187 ? 21.281 -2.971 -11.543 1.00 40.85  ? 187 ILE A CB  1 
ATOM   1424 C CG1 . ILE A 1 187 ? 21.822 -4.119 -12.395 1.00 45.02  ? 187 ILE A CG1 1 
ATOM   1425 C CG2 . ILE A 1 187 ? 20.464 -2.021 -12.406 1.00 40.51  ? 187 ILE A CG2 1 
ATOM   1426 C CD1 . ILE A 1 187 ? 20.755 -5.004 -12.947 1.00 49.39  ? 187 ILE A CD1 1 
ATOM   1427 N N   . ASN A 1 188 ? 24.614 -2.431 -11.928 1.00 35.84  ? 188 ASN A N   1 
ATOM   1428 C CA  . ASN A 1 188 ? 25.685 -2.095 -12.860 1.00 39.48  ? 188 ASN A CA  1 
ATOM   1429 C C   . ASN A 1 188 ? 26.148 -3.365 -13.561 1.00 40.91  ? 188 ASN A C   1 
ATOM   1430 O O   . ASN A 1 188 ? 26.647 -4.289 -12.910 1.00 41.11  ? 188 ASN A O   1 
ATOM   1431 C CB  . ASN A 1 188 ? 26.857 -1.417 -12.138 1.00 41.14  ? 188 ASN A CB  1 
ATOM   1432 C CG  . ASN A 1 188 ? 26.649 0.079  -11.951 1.00 43.85  ? 188 ASN A CG  1 
ATOM   1433 O OD1 . ASN A 1 188 ? 27.053 0.887  -12.790 1.00 46.40  ? 188 ASN A OD1 1 
ATOM   1434 N ND2 . ASN A 1 188 ? 26.025 0.454  -10.842 1.00 43.75  ? 188 ASN A ND2 1 
ATOM   1435 N N   . ASN A 1 189 ? 25.982 -3.408 -14.884 1.00 43.65  ? 189 ASN A N   1 
ATOM   1436 C CA  . ASN A 1 189 ? 26.467 -4.527 -15.683 1.00 48.54  ? 189 ASN A CA  1 
ATOM   1437 C C   . ASN A 1 189 ? 26.903 -4.051 -17.066 1.00 54.37  ? 189 ASN A C   1 
ATOM   1438 O O   . ASN A 1 189 ? 27.312 -2.896 -17.230 1.00 55.49  ? 189 ASN A O   1 
ATOM   1439 C CB  . ASN A 1 189 ? 25.389 -5.611 -15.787 1.00 48.10  ? 189 ASN A CB  1 
ATOM   1440 C CG  . ASN A 1 189 ? 24.044 -5.062 -16.234 1.00 45.82  ? 189 ASN A CG  1 
ATOM   1441 O OD1 . ASN A 1 189 ? 23.967 -4.026 -16.893 1.00 45.09  ? 189 ASN A OD1 1 
ATOM   1442 N ND2 . ASN A 1 189 ? 22.974 -5.750 -15.858 1.00 45.93  ? 189 ASN A ND2 1 
ATOM   1443 N N   . ARG A 1 190 ? 26.800 -4.924 -18.072 1.00 58.09  ? 190 ARG A N   1 
ATOM   1444 C CA  . ARG A 1 190 ? 27.155 -4.529 -19.432 1.00 60.18  ? 190 ARG A CA  1 
ATOM   1445 C C   . ARG A 1 190 ? 26.205 -3.471 -19.979 1.00 59.73  ? 190 ARG A C   1 
ATOM   1446 O O   . ARG A 1 190 ? 26.610 -2.637 -20.797 1.00 61.28  ? 190 ARG A O   1 
ATOM   1447 C CB  . ARG A 1 190 ? 27.154 -5.751 -20.352 0.80 63.59  ? 190 ARG A CB  1 
ATOM   1448 C CG  . ARG A 1 190 ? 27.869 -5.529 -21.678 0.80 66.06  ? 190 ARG A CG  1 
ATOM   1449 C CD  . ARG A 1 190 ? 27.465 -6.547 -22.735 0.70 70.13  ? 190 ARG A CD  1 
ATOM   1450 N NE  . ARG A 1 190 ? 27.171 -7.854 -22.159 0.70 72.39  ? 190 ARG A NE  1 
ATOM   1451 C CZ  . ARG A 1 190 ? 25.998 -8.470 -22.264 0.70 74.00  ? 190 ARG A CZ  1 
ATOM   1452 N NH1 . ARG A 1 190 ? 25.006 -7.907 -22.942 0.60 74.18  ? 190 ARG A NH1 1 
ATOM   1453 N NH2 . ARG A 1 190 ? 25.822 -9.656 -21.701 0.60 75.28  ? 190 ARG A NH2 1 
ATOM   1454 N N   . VAL A 1 191 ? 24.948 -3.480 -19.534 1.00 57.35  ? 191 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 191 ? 23.905 -2.642 -20.114 1.00 56.30  ? 191 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 191 ? 23.650 -1.413 -19.248 1.00 53.06  ? 191 VAL A C   1 
ATOM   1457 O O   . VAL A 1 191 ? 23.365 -0.326 -19.763 1.00 53.84  ? 191 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 191 ? 22.610 -3.453 -20.314 0.85 59.03  ? 191 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 191 ? 21.519 -2.588 -20.925 0.76 60.22  ? 191 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 191 ? 22.884 -4.671 -21.180 0.75 60.82  ? 191 VAL A CG2 1 
ATOM   1461 N N   . TYR A 1 192 ? 23.754 -1.570 -17.933 0.94 49.96  ? 192 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 192 ? 23.438 -0.509 -16.988 0.94 46.70  ? 192 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 192 ? 24.712 -0.003 -16.324 0.94 44.01  ? 192 TYR A C   1 
ATOM   1464 O O   . TYR A 1 192 ? 25.554 -0.796 -15.891 0.94 43.05  ? 192 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 192 ? 22.445 -1.008 -15.937 0.94 46.93  ? 192 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 192 ? 21.201 -1.611 -16.547 0.94 48.93  ? 192 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 192 ? 20.689 -2.817 -16.087 0.94 50.38  ? 192 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 192 ? 20.540 -0.976 -17.591 0.94 49.91  ? 192 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 192 ? 19.554 -3.372 -16.648 0.94 51.51  ? 192 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 192 ? 19.404 -1.521 -18.156 0.94 51.49  ? 192 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 192 ? 18.914 -2.718 -17.681 0.94 52.48  ? 192 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 192 ? 17.783 -3.264 -18.245 0.94 54.52  ? 192 TYR A OH  1 
ATOM   1473 N N   . ARG A 1 193 ? 24.852 1.320  -16.251 1.00 42.71  ? 193 ARG A N   1 
ATOM   1474 C CA  . ARG A 1 193 ? 26.064 1.927  -15.709 1.00 39.61  ? 193 ARG A CA  1 
ATOM   1475 C C   . ARG A 1 193 ? 25.713 3.226  -15.002 1.00 37.37  ? 193 ARG A C   1 
ATOM   1476 O O   . ARG A 1 193 ? 25.088 4.111  -15.595 1.00 38.86  ? 193 ARG A O   1 
ATOM   1477 C CB  . ARG A 1 193 ? 27.092 2.184  -16.814 0.80 39.24  ? 193 ARG A CB  1 
ATOM   1478 N N   . THR A 1 194 ? 26.127 3.340  -13.745 1.00 32.89  ? 194 THR A N   1 
ATOM   1479 C CA  . THR A 1 194 ? 25.981 4.555  -12.961 1.00 30.21  ? 194 THR A CA  1 
ATOM   1480 C C   . THR A 1 194 ? 27.346 4.989  -12.445 1.00 28.58  ? 194 THR A C   1 
ATOM   1481 O O   . THR A 1 194 ? 28.342 4.272  -12.563 1.00 29.47  ? 194 THR A O   1 
ATOM   1482 C CB  . THR A 1 194 ? 25.015 4.351  -11.788 1.00 31.29  ? 194 THR A CB  1 
ATOM   1483 O OG1 . THR A 1 194 ? 25.508 3.310  -10.934 1.00 33.21  ? 194 THR A OG1 1 
ATOM   1484 C CG2 . THR A 1 194 ? 23.634 3.980  -12.294 1.00 30.97  ? 194 THR A CG2 1 
ATOM   1485 N N   . ILE A 1 195 ? 27.382 6.185  -11.856 1.00 28.21  ? 195 ILE A N   1 
ATOM   1486 C CA  . ILE A 1 195 ? 28.643 6.702  -11.338 1.00 31.52  ? 195 ILE A CA  1 
ATOM   1487 C C   . ILE A 1 195 ? 29.048 5.966  -10.066 1.00 33.63  ? 195 ILE A C   1 
ATOM   1488 O O   . ILE A 1 195 ? 30.242 5.839  -9.768  1.00 32.65  ? 195 ILE A O   1 
ATOM   1489 C CB  . ILE A 1 195 ? 28.538 8.222  -11.110 1.00 33.23  ? 195 ILE A CB  1 
ATOM   1490 C CG1 . ILE A 1 195 ? 29.915 8.819  -10.807 1.00 34.76  ? 195 ILE A CG1 1 
ATOM   1491 C CG2 . ILE A 1 195 ? 27.534 8.536  -10.000 1.00 34.25  ? 195 ILE A CG2 1 
ATOM   1492 C CD1 . ILE A 1 195 ? 30.866 8.780  -11.980 1.00 35.50  ? 195 ILE A CD1 1 
ATOM   1493 N N   . GLY A 1 196 ? 28.081 5.465  -9.302  1.00 35.21  ? 196 GLY A N   1 
ATOM   1494 C CA  . GLY A 1 196 ? 28.387 4.782  -8.061  1.00 34.94  ? 196 GLY A CA  1 
ATOM   1495 C C   . GLY A 1 196 ? 28.794 5.709  -6.932  1.00 34.68  ? 196 GLY A C   1 
ATOM   1496 O O   . GLY A 1 196 ? 28.209 5.670  -5.846  1.00 34.39  ? 196 GLY A O   1 
ATOM   1497 N N   . SER A 1 197 ? 29.795 6.550  -7.180  1.00 32.14  ? 197 SER A N   1 
ATOM   1498 C CA  . SER A 1 197 ? 30.296 7.450  -6.155  1.00 29.16  ? 197 SER A CA  1 
ATOM   1499 C C   . SER A 1 197 ? 29.222 8.457  -5.741  1.00 27.14  ? 197 SER A C   1 
ATOM   1500 O O   . SER A 1 197 ? 28.361 8.829  -6.545  1.00 23.55  ? 197 SER A O   1 
ATOM   1501 C CB  . SER A 1 197 ? 31.531 8.193  -6.661  1.00 28.55  ? 197 SER A CB  1 
ATOM   1502 O OG  . SER A 1 197 ? 32.616 7.305  -6.869  1.00 30.62  ? 197 SER A OG  1 
ATOM   1503 N N   . PRO A 1 198 ? 29.241 8.904  -4.485  1.00 27.14  ? 198 PRO A N   1 
ATOM   1504 C CA  . PRO A 1 198 ? 28.387 10.029 -4.095  1.00 26.14  ? 198 PRO A CA  1 
ATOM   1505 C C   . PRO A 1 198 ? 28.829 11.310 -4.782  1.00 26.04  ? 198 PRO A C   1 
ATOM   1506 O O   . PRO A 1 198 ? 29.998 11.482 -5.136  1.00 31.11  ? 198 PRO A O   1 
ATOM   1507 C CB  . PRO A 1 198 ? 28.582 10.118 -2.576  1.00 26.16  ? 198 PRO A CB  1 
ATOM   1508 C CG  . PRO A 1 198 ? 29.125 8.786  -2.176  1.00 26.66  ? 198 PRO A CG  1 
ATOM   1509 C CD  . PRO A 1 198 ? 29.963 8.338  -3.334  1.00 27.18  ? 198 PRO A CD  1 
ATOM   1510 N N   . LEU A 1 199 ? 27.876 12.217 -4.969  1.00 23.13  ? 199 LEU A N   1 
ATOM   1511 C CA  . LEU A 1 199 ? 28.113 13.481 -5.651  1.00 25.01  ? 199 LEU A CA  1 
ATOM   1512 C C   . LEU A 1 199 ? 27.764 14.629 -4.718  1.00 27.59  ? 199 LEU A C   1 
ATOM   1513 O O   . LEU A 1 199 ? 26.690 14.636 -4.111  1.00 30.35  ? 199 LEU A O   1 
ATOM   1514 C CB  . LEU A 1 199 ? 27.290 13.577 -6.935  1.00 25.88  ? 199 LEU A CB  1 
ATOM   1515 C CG  . LEU A 1 199 ? 27.378 12.388 -7.890  1.00 25.18  ? 199 LEU A CG  1 
ATOM   1516 C CD1 . LEU A 1 199 ? 26.588 12.684 -9.149  1.00 20.41  ? 199 LEU A CD1 1 
ATOM   1517 C CD2 . LEU A 1 199 ? 28.828 12.065 -8.221  1.00 20.82  ? 199 LEU A CD2 1 
ATOM   1518 N N   . VAL A 1 200 ? 28.669 15.596 -4.612  1.00 28.06  ? 200 VAL A N   1 
ATOM   1519 C CA  . VAL A 1 200 ? 28.481 16.775 -3.773  1.00 27.45  ? 200 VAL A CA  1 
ATOM   1520 C C   . VAL A 1 200 ? 28.278 17.978 -4.684  1.00 27.57  ? 200 VAL A C   1 
ATOM   1521 O O   . VAL A 1 200 ? 29.184 18.355 -5.438  1.00 25.47  ? 200 VAL A O   1 
ATOM   1522 C CB  . VAL A 1 200 ? 29.672 16.990 -2.827  1.00 27.09  ? 200 VAL A CB  1 
ATOM   1523 C CG1 . VAL A 1 200 ? 29.518 18.292 -2.073  1.00 27.21  ? 200 VAL A CG1 1 
ATOM   1524 C CG2 . VAL A 1 200 ? 29.796 15.826 -1.854  1.00 26.55  ? 200 VAL A CG2 1 
ATOM   1525 N N   . PHE A 1 201 ? 27.084 18.572 -4.623  1.00 28.08  ? 201 PHE A N   1 
ATOM   1526 C CA  . PHE A 1 201 ? 26.739 19.706 -5.469  1.00 29.66  ? 201 PHE A CA  1 
ATOM   1527 C C   . PHE A 1 201 ? 26.769 21.002 -4.672  1.00 31.68  ? 201 PHE A C   1 
ATOM   1528 O O   . PHE A 1 201 ? 26.314 21.033 -3.525  1.00 31.00  ? 201 PHE A O   1 
ATOM   1529 C CB  . PHE A 1 201 ? 25.348 19.534 -6.082  1.00 28.64  ? 201 PHE A CB  1 
ATOM   1530 C CG  . PHE A 1 201 ? 25.207 18.307 -6.929  1.00 29.50  ? 201 PHE A CG  1 
ATOM   1531 C CD1 . PHE A 1 201 ? 24.792 17.110 -6.371  1.00 30.16  ? 201 PHE A CD1 1 
ATOM   1532 C CD2 . PHE A 1 201 ? 25.488 18.349 -8.284  1.00 30.66  ? 201 PHE A CD2 1 
ATOM   1533 C CE1 . PHE A 1 201 ? 24.662 15.976 -7.148  1.00 30.88  ? 201 PHE A CE1 1 
ATOM   1534 C CE2 . PHE A 1 201 ? 25.360 17.220 -9.069  1.00 31.61  ? 201 PHE A CE2 1 
ATOM   1535 C CZ  . PHE A 1 201 ? 24.946 16.031 -8.500  1.00 31.36  ? 201 PHE A CZ  1 
ATOM   1536 N N   . PRO A 1 202 ? 27.288 22.077 -5.249  1.00 34.39  ? 202 PRO A N   1 
ATOM   1537 C CA  . PRO A 1 202 ? 27.305 23.371 -4.563  1.00 35.68  ? 202 PRO A CA  1 
ATOM   1538 C C   . PRO A 1 202 ? 25.949 24.061 -4.683  1.00 36.70  ? 202 PRO A C   1 
ATOM   1539 O O   . PRO A 1 202 ? 24.981 23.504 -5.197  1.00 35.36  ? 202 PRO A O   1 
ATOM   1540 C CB  . PRO A 1 202 ? 28.392 24.138 -5.314  1.00 35.28  ? 202 PRO A CB  1 
ATOM   1541 C CG  . PRO A 1 202 ? 28.284 23.612 -6.708  1.00 35.39  ? 202 PRO A CG  1 
ATOM   1542 C CD  . PRO A 1 202 ? 27.935 22.147 -6.571  1.00 33.72  ? 202 PRO A CD  1 
ATOM   1543 N N   . LYS A 1 203 ? 25.898 25.299 -4.192  1.00 39.98  ? 203 LYS A N   1 
ATOM   1544 C CA  . LYS A 1 203 ? 24.720 26.128 -4.385  1.00 42.74  ? 203 LYS A CA  1 
ATOM   1545 C C   . LYS A 1 203 ? 24.470 26.358 -5.872  1.00 42.19  ? 203 LYS A C   1 
ATOM   1546 O O   . LYS A 1 203 ? 25.349 26.158 -6.718  1.00 43.31  ? 203 LYS A O   1 
ATOM   1547 C CB  . LYS A 1 203 ? 24.877 27.480 -3.684  1.00 47.89  ? 203 LYS A CB  1 
ATOM   1548 C CG  . LYS A 1 203 ? 24.720 27.455 -2.174  1.00 50.54  ? 203 LYS A CG  1 
ATOM   1549 C CD  A LYS A 1 203 ? 24.708 28.870 -1.603  0.46 53.78  ? 203 LYS A CD  1 
ATOM   1550 C CD  B LYS A 1 203 ? 24.757 28.867 -1.599  0.54 53.79  ? 203 LYS A CD  1 
ATOM   1551 C CE  A LYS A 1 203 ? 23.400 29.180 -0.882  0.46 54.56  ? 203 LYS A CE  1 
ATOM   1552 C CE  B LYS A 1 203 ? 26.004 29.622 -2.038  0.54 55.73  ? 203 LYS A CE  1 
ATOM   1553 N NZ  A LYS A 1 203 ? 22.220 29.076 -1.782  0.46 55.27  ? 203 LYS A NZ  1 
ATOM   1554 N NZ  B LYS A 1 203 ? 27.255 29.007 -1.510  0.54 56.27  ? 203 LYS A NZ  1 
ATOM   1555 N N   . HIS A 1 204 ? 23.237 26.763 -6.186  1.00 41.09  ? 204 HIS A N   1 
ATOM   1556 C CA  . HIS A 1 204 ? 22.853 27.179 -7.531  1.00 41.74  ? 204 HIS A CA  1 
ATOM   1557 C C   . HIS A 1 204 ? 22.959 26.049 -8.549  1.00 41.16  ? 204 HIS A C   1 
ATOM   1558 O O   . HIS A 1 204 ? 22.717 26.262 -9.741  1.00 44.23  ? 204 HIS A O   1 
ATOM   1559 C CB  . HIS A 1 204 ? 23.699 28.374 -7.976  1.00 41.20  ? 204 HIS A CB  1 
ATOM   1560 C CG  . HIS A 1 204 ? 23.551 29.575 -7.095  0.70 40.91  ? 204 HIS A CG  1 
ATOM   1561 N ND1 . HIS A 1 204 ? 22.337 29.968 -6.574  0.70 41.09  ? 204 HIS A ND1 1 
ATOM   1562 C CD2 . HIS A 1 204 ? 24.464 30.460 -6.630  0.70 41.62  ? 204 HIS A CD2 1 
ATOM   1563 C CE1 . HIS A 1 204 ? 22.507 31.050 -5.834  0.70 42.03  ? 204 HIS A CE1 1 
ATOM   1564 N NE2 . HIS A 1 204 ? 23.789 31.368 -5.852  0.70 42.64  ? 204 HIS A NE2 1 
ATOM   1565 N N   . HIS A 1 205 ? 23.312 24.849 -8.101  1.00 37.67  ? 205 HIS A N   1 
ATOM   1566 C CA  . HIS A 1 205 ? 23.314 23.670 -8.954  1.00 33.57  ? 205 HIS A CA  1 
ATOM   1567 C C   . HIS A 1 205 ? 21.996 22.932 -8.781  1.00 34.65  ? 205 HIS A C   1 
ATOM   1568 O O   . HIS A 1 205 ? 21.571 22.669 -7.652  1.00 36.22  ? 205 HIS A O   1 
ATOM   1569 C CB  . HIS A 1 205 ? 24.491 22.753 -8.627  1.00 28.50  ? 205 HIS A CB  1 
ATOM   1570 C CG  . HIS A 1 205 ? 25.750 23.113 -9.349  1.00 27.43  ? 205 HIS A CG  1 
ATOM   1571 N ND1 . HIS A 1 205 ? 26.655 22.168 -9.780  1.00 26.53  ? 205 HIS A ND1 1 
ATOM   1572 C CD2 . HIS A 1 205 ? 26.253 24.314 -9.722  1.00 28.86  ? 205 HIS A CD2 1 
ATOM   1573 C CE1 . HIS A 1 205 ? 27.662 22.770 -10.386 1.00 28.63  ? 205 HIS A CE1 1 
ATOM   1574 N NE2 . HIS A 1 205 ? 27.443 24.072 -10.364 1.00 29.86  ? 205 HIS A NE2 1 
ATOM   1575 N N   . VAL A 1 206 ? 21.355 22.599 -9.899  1.00 34.11  ? 206 VAL A N   1 
ATOM   1576 C CA  . VAL A 1 206 ? 20.016 22.021 -9.906  1.00 33.24  ? 206 VAL A CA  1 
ATOM   1577 C C   . VAL A 1 206 ? 20.107 20.585 -10.402 1.00 33.42  ? 206 VAL A C   1 
ATOM   1578 O O   . VAL A 1 206 ? 20.474 20.339 -11.558 1.00 33.30  ? 206 VAL A O   1 
ATOM   1579 C CB  . VAL A 1 206 ? 19.052 22.841 -10.776 1.00 32.97  ? 206 VAL A CB  1 
ATOM   1580 C CG1 . VAL A 1 206 ? 17.675 22.206 -10.783 1.00 32.76  ? 206 VAL A CG1 1 
ATOM   1581 C CG2 . VAL A 1 206 ? 18.984 24.276 -10.279 1.00 31.64  ? 206 VAL A CG2 1 
ATOM   1582 N N   . VAL A 1 207 ? 19.770 19.639 -9.528  1.00 32.96  ? 207 VAL A N   1 
ATOM   1583 C CA  . VAL A 1 207 ? 19.668 18.228 -9.884  1.00 32.17  ? 207 VAL A CA  1 
ATOM   1584 C C   . VAL A 1 207 ? 18.207 17.917 -10.171 1.00 32.98  ? 207 VAL A C   1 
ATOM   1585 O O   . VAL A 1 207 ? 17.331 18.199 -9.343  1.00 32.11  ? 207 VAL A O   1 
ATOM   1586 C CB  . VAL A 1 207 ? 20.213 17.324 -8.764  1.00 32.53  ? 207 VAL A CB  1 
ATOM   1587 C CG1 . VAL A 1 207 ? 19.887 15.867 -9.058  1.00 32.65  ? 207 VAL A CG1 1 
ATOM   1588 C CG2 . VAL A 1 207 ? 21.712 17.521 -8.612  1.00 33.14  ? 207 VAL A CG2 1 
ATOM   1589 N N   . SER A 1 208 ? 17.938 17.347 -11.342 1.00 34.45  ? 208 SER A N   1 
ATOM   1590 C CA  . SER A 1 208 ? 16.580 17.035 -11.766 1.00 35.77  ? 208 SER A CA  1 
ATOM   1591 C C   . SER A 1 208 ? 16.471 15.547 -12.061 1.00 35.87  ? 208 SER A C   1 
ATOM   1592 O O   . SER A 1 208 ? 17.286 14.995 -12.808 1.00 37.73  ? 208 SER A O   1 
ATOM   1593 C CB  . SER A 1 208 ? 16.184 17.853 -13.000 1.00 37.23  ? 208 SER A CB  1 
ATOM   1594 O OG  . SER A 1 208 ? 14.849 17.575 -13.387 0.67 38.03  ? 208 SER A OG  1 
ATOM   1595 N N   . LEU A 1 209 ? 15.469 14.901 -11.473 1.00 34.51  ? 209 LEU A N   1 
ATOM   1596 C CA  . LEU A 1 209 ? 15.158 13.509 -11.765 1.00 32.84  ? 209 LEU A CA  1 
ATOM   1597 C C   . LEU A 1 209 ? 13.948 13.459 -12.689 1.00 33.16  ? 209 LEU A C   1 
ATOM   1598 O O   . LEU A 1 209 ? 12.939 14.126 -12.434 1.00 32.96  ? 209 LEU A O   1 
ATOM   1599 C CB  . LEU A 1 209 ? 14.881 12.723 -10.484 1.00 33.34  ? 209 LEU A CB  1 
ATOM   1600 C CG  . LEU A 1 209 ? 15.975 12.768 -9.415  1.00 34.07  ? 209 LEU A CG  1 
ATOM   1601 C CD1 . LEU A 1 209 ? 15.604 11.877 -8.240  1.00 32.63  ? 209 LEU A CD1 1 
ATOM   1602 C CD2 . LEU A 1 209 ? 17.320 12.362 -9.997  1.00 34.60  ? 209 LEU A CD2 1 
ATOM   1603 N N   . GLN A 1 210 ? 14.053 12.677 -13.761 1.00 32.87  ? 210 GLN A N   1 
ATOM   1604 C CA  . GLN A 1 210 ? 13.015 12.615 -14.786 1.00 33.99  ? 210 GLN A CA  1 
ATOM   1605 C C   . GLN A 1 210 ? 12.607 11.163 -15.000 1.00 34.75  ? 210 GLN A C   1 
ATOM   1606 O O   . GLN A 1 210 ? 13.474 10.316 -15.297 1.00 33.97  ? 210 GLN A O   1 
ATOM   1607 C CB  . GLN A 1 210 ? 13.501 13.258 -16.088 0.80 33.67  ? 210 GLN A CB  1 
ATOM   1608 C CG  . GLN A 1 210 ? 13.722 14.762 -15.961 0.80 35.14  ? 210 GLN A CG  1 
ATOM   1609 C CD  . GLN A 1 210 ? 14.345 15.379 -17.196 0.70 38.42  ? 210 GLN A CD  1 
ATOM   1610 O OE1 . GLN A 1 210 ? 14.360 14.773 -18.269 0.70 39.98  ? 210 GLN A OE1 1 
ATOM   1611 N NE2 . GLN A 1 210 ? 14.869 16.593 -17.050 0.70 38.86  ? 210 GLN A NE2 1 
ATOM   1612 N N   . PRO A 1 211 ? 11.325 10.828 -14.867 1.00 36.91  ? 211 PRO A N   1 
ATOM   1613 C CA  . PRO A 1 211 ? 10.904 9.431  -15.017 1.00 39.04  ? 211 PRO A CA  1 
ATOM   1614 C C   . PRO A 1 211 ? 11.062 8.935  -16.446 1.00 42.07  ? 211 PRO A C   1 
ATOM   1615 O O   . PRO A 1 211 ? 10.967 9.697  -17.412 1.00 43.86  ? 211 PRO A O   1 
ATOM   1616 C CB  . PRO A 1 211 ? 9.427  9.459  -14.603 1.00 39.32  ? 211 PRO A CB  1 
ATOM   1617 C CG  . PRO A 1 211 ? 8.997  10.879 -14.809 1.00 39.84  ? 211 PRO A CG  1 
ATOM   1618 C CD  . PRO A 1 211 ? 10.206 11.710 -14.492 1.00 38.05  ? 211 PRO A CD  1 
ATOM   1619 N N   . VAL A 1 212 ? 11.310 7.633  -16.570 0.80 42.56  ? 212 VAL A N   1 
ATOM   1620 C CA  . VAL A 1 212 ? 11.437 6.977  -17.861 0.80 45.32  ? 212 VAL A CA  1 
ATOM   1621 C C   . VAL A 1 212 ? 10.249 6.068  -18.149 0.80 50.95  ? 212 VAL A C   1 
ATOM   1622 O O   . VAL A 1 212 ? 9.729  6.055  -19.267 0.80 54.04  ? 212 VAL A O   1 
ATOM   1623 C CB  . VAL A 1 212 ? 12.766 6.193  -17.954 0.80 43.48  ? 212 VAL A CB  1 
ATOM   1624 C CG1 . VAL A 1 212 ? 12.944 5.609  -19.348 0.80 43.70  ? 212 VAL A CG1 1 
ATOM   1625 C CG2 . VAL A 1 212 ? 13.944 7.086  -17.590 0.80 41.53  ? 212 VAL A CG2 1 
ATOM   1626 N N   . ASN A 1 213 ? 9.800  5.308  -17.151 1.00 52.11  ? 213 ASN A N   1 
ATOM   1627 C CA  . ASN A 1 213 ? 8.647  4.429  -17.306 1.00 53.86  ? 213 ASN A CA  1 
ATOM   1628 C C   . ASN A 1 213 ? 7.546  4.814  -16.327 1.00 55.29  ? 213 ASN A C   1 
ATOM   1629 O O   . ASN A 1 213 ? 6.689  5.647  -16.638 1.00 55.81  ? 213 ASN A O   1 
ATOM   1630 C CB  . ASN A 1 213 ? 9.050  2.967  -17.094 0.80 54.63  ? 213 ASN A CB  1 
ATOM   1631 C CG  . ASN A 1 213 ? 9.007  2.157  -18.375 0.50 56.97  ? 213 ASN A CG  1 
ATOM   1632 O OD1 . ASN A 1 213 ? 7.942  1.722  -18.813 0.50 58.66  ? 213 ASN A OD1 1 
ATOM   1633 N ND2 . ASN A 1 213 ? 10.171 1.942  -18.979 0.50 57.23  ? 213 ASN A ND2 1 
ATOM   1634 N N   . ASP A 1 214 ? 7.565  4.207  -15.143 1.00 56.52  ? 214 ASP A N   1 
ATOM   1635 C CA  . ASP A 1 214 ? 6.583  4.526  -14.118 1.00 58.17  ? 214 ASP A CA  1 
ATOM   1636 C C   . ASP A 1 214 ? 6.761  5.963  -13.644 1.00 55.84  ? 214 ASP A C   1 
ATOM   1637 O O   . ASP A 1 214 ? 7.885  6.454  -13.503 1.00 54.67  ? 214 ASP A O   1 
ATOM   1638 C CB  . ASP A 1 214 ? 6.721  3.556  -12.942 1.00 60.71  ? 214 ASP A CB  1 
ATOM   1639 C CG  . ASP A 1 214 ? 5.560  3.637  -11.967 0.88 65.63  ? 214 ASP A CG  1 
ATOM   1640 O OD1 . ASP A 1 214 ? 4.660  4.481  -12.163 0.77 67.99  ? 214 ASP A OD1 1 
ATOM   1641 O OD2 . ASP A 1 214 ? 5.545  2.846  -11.002 0.76 67.25  ? 214 ASP A OD2 1 
ATOM   1642 N N   . LYS A 1 215 ? 5.640  6.642  -13.407 1.00 55.75  ? 215 LYS A N   1 
ATOM   1643 C CA  . LYS A 1 215 ? 5.645  8.031  -12.963 1.00 54.19  ? 215 LYS A CA  1 
ATOM   1644 C C   . LYS A 1 215 ? 5.160  8.181  -11.526 1.00 50.90  ? 215 LYS A C   1 
ATOM   1645 O O   . LYS A 1 215 ? 4.914  9.306  -11.077 1.00 48.61  ? 215 LYS A O   1 
ATOM   1646 C CB  . LYS A 1 215 ? 4.796  8.895  -13.900 1.00 58.82  ? 215 LYS A CB  1 
ATOM   1647 C CG  . LYS A 1 215 ? 5.085  8.663  -15.376 1.00 61.69  ? 215 LYS A CG  1 
ATOM   1648 C CD  . LYS A 1 215 ? 4.403  9.706  -16.259 1.00 64.79  ? 215 LYS A CD  1 
ATOM   1649 C CE  . LYS A 1 215 ? 5.194  11.010 -16.310 0.76 63.91  ? 215 LYS A CE  1 
ATOM   1650 N NZ  . LYS A 1 215 ? 4.460  12.099 -17.029 0.77 65.75  ? 215 LYS A NZ  1 
ATOM   1651 N N   . ASP A 1 216 ? 5.014  7.079  -10.799 1.00 51.03  ? 216 ASP A N   1 
ATOM   1652 C CA  . ASP A 1 216 ? 4.631  7.107  -9.394  1.00 52.25  ? 216 ASP A CA  1 
ATOM   1653 C C   . ASP A 1 216 ? 5.850  6.802  -8.534  1.00 51.23  ? 216 ASP A C   1 
ATOM   1654 O O   . ASP A 1 216 ? 6.520  5.783  -8.737  1.00 49.99  ? 216 ASP A O   1 
ATOM   1655 C CB  . ASP A 1 216 ? 3.518  6.096  -9.113  1.00 56.04  ? 216 ASP A CB  1 
ATOM   1656 C CG  . ASP A 1 216 ? 2.262  6.367  -9.918  1.00 61.96  ? 216 ASP A CG  1 
ATOM   1657 O OD1 . ASP A 1 216 ? 2.193  7.435  -10.561 1.00 62.93  ? 216 ASP A OD1 1 
ATOM   1658 O OD2 . ASP A 1 216 ? 1.348  5.511  -9.914  1.00 64.73  ? 216 ASP A OD2 1 
ATOM   1659 N N   . PHE A 1 217 ? 6.134  7.680  -7.573  1.00 51.27  ? 217 PHE A N   1 
ATOM   1660 C CA  . PHE A 1 217 ? 7.295  7.517  -6.711  1.00 49.37  ? 217 PHE A CA  1 
ATOM   1661 C C   . PHE A 1 217 ? 6.912  7.823  -5.271  1.00 49.21  ? 217 PHE A C   1 
ATOM   1662 O O   . PHE A 1 217 ? 6.112  8.727  -5.013  1.00 52.35  ? 217 PHE A O   1 
ATOM   1663 C CB  . PHE A 1 217 ? 8.458  8.433  -7.138  1.00 48.76  ? 217 PHE A CB  1 
ATOM   1664 C CG  . PHE A 1 217 ? 8.720  8.449  -8.624  1.00 50.88  ? 217 PHE A CG  1 
ATOM   1665 C CD1 . PHE A 1 217 ? 9.600  7.547  -9.202  1.00 51.18  ? 217 PHE A CD1 1 
ATOM   1666 C CD2 . PHE A 1 217 ? 8.099  9.383  -9.441  1.00 51.62  ? 217 PHE A CD2 1 
ATOM   1667 C CE1 . PHE A 1 217 ? 9.844  7.568  -10.567 1.00 51.94  ? 217 PHE A CE1 1 
ATOM   1668 C CE2 . PHE A 1 217 ? 8.342  9.406  -10.804 1.00 52.17  ? 217 PHE A CE2 1 
ATOM   1669 C CZ  . PHE A 1 217 ? 9.214  8.498  -11.364 1.00 52.68  ? 217 PHE A CZ  1 
ATOM   1670 N N   . GLN A 1 218 ? 7.484  7.062  -4.339  1.00 45.84  ? 218 GLN A N   1 
ATOM   1671 C CA  . GLN A 1 218 ? 7.351  7.338  -2.913  1.00 43.63  ? 218 GLN A CA  1 
ATOM   1672 C C   . GLN A 1 218 ? 8.487  8.275  -2.513  1.00 39.83  ? 218 GLN A C   1 
ATOM   1673 O O   . GLN A 1 218 ? 9.650  7.862  -2.444  1.00 39.21  ? 218 GLN A O   1 
ATOM   1674 C CB  . GLN A 1 218 ? 7.383  6.044  -2.104  1.00 44.29  ? 218 GLN A CB  1 
ATOM   1675 C CG  . GLN A 1 218 ? 7.050  6.212  -0.626  0.85 43.78  ? 218 GLN A CG  1 
ATOM   1676 C CD  . GLN A 1 218 ? 5.560  6.161  -0.362  0.81 45.66  ? 218 GLN A CD  1 
ATOM   1677 O OE1 . GLN A 1 218 ? 4.804  5.595  -1.149  0.74 46.97  ? 218 GLN A OE1 1 
ATOM   1678 N NE2 . GLN A 1 218 ? 5.130  6.753  0.746   0.74 45.48  ? 218 GLN A NE2 1 
ATOM   1679 N N   . ILE A 1 219 ? 8.156  9.538  -2.271  1.00 38.39  ? 219 ILE A N   1 
ATOM   1680 C CA  . ILE A 1 219 ? 9.138  10.560 -1.928  1.00 35.68  ? 219 ILE A CA  1 
ATOM   1681 C C   . ILE A 1 219 ? 9.125  10.765 -0.421  1.00 35.45  ? 219 ILE A C   1 
ATOM   1682 O O   . ILE A 1 219 ? 8.055  10.841 0.198   1.00 33.50  ? 219 ILE A O   1 
ATOM   1683 C CB  . ILE A 1 219 ? 8.848  11.876 -2.674  1.00 35.89  ? 219 ILE A CB  1 
ATOM   1684 C CG1 . ILE A 1 219 ? 8.871  11.635 -4.184  1.00 35.82  ? 219 ILE A CG1 1 
ATOM   1685 C CG2 . ILE A 1 219 ? 9.857  12.946 -2.294  1.00 34.63  ? 219 ILE A CG2 1 
ATOM   1686 C CD1 . ILE A 1 219 ? 8.511  12.851 -4.999  1.00 36.13  ? 219 ILE A CD1 1 
ATOM   1687 N N   . SER A 1 220 ? 10.313 10.841 0.176   1.00 37.13  ? 220 SER A N   1 
ATOM   1688 C CA  . SER A 1 220 ? 10.453 11.084 1.602   1.00 38.03  ? 220 SER A CA  1 
ATOM   1689 C C   . SER A 1 220 ? 11.119 12.433 1.830   1.00 38.94  ? 220 SER A C   1 
ATOM   1690 O O   . SER A 1 220 ? 11.973 12.862 1.050   1.00 38.47  ? 220 SER A O   1 
ATOM   1691 C CB  . SER A 1 220 ? 11.275 9.980  2.289   1.00 36.16  ? 220 SER A CB  1 
ATOM   1692 O OG  . SER A 1 220 ? 12.667 10.187 2.135   1.00 35.66  ? 220 SER A OG  1 
ATOM   1693 N N   . VAL A 1 221 ? 10.710 13.107 2.902   1.00 39.93  ? 221 VAL A N   1 
ATOM   1694 C CA  . VAL A 1 221 ? 11.377 14.311 3.396   1.00 39.23  ? 221 VAL A CA  1 
ATOM   1695 C C   . VAL A 1 221 ? 11.552 14.110 4.898   1.00 41.81  ? 221 VAL A C   1 
ATOM   1696 O O   . VAL A 1 221 ? 10.597 14.267 5.670   1.00 46.31  ? 221 VAL A O   1 
ATOM   1697 C CB  . VAL A 1 221 ? 10.596 15.596 3.095   1.00 38.97  ? 221 VAL A CB  1 
ATOM   1698 C CG1 . VAL A 1 221 ? 11.316 16.801 3.673   1.00 38.65  ? 221 VAL A CG1 1 
ATOM   1699 C CG2 . VAL A 1 221 ? 10.404 15.772 1.601   1.00 39.46  ? 221 VAL A CG2 1 
ATOM   1700 N N   . ASP A 1 222 ? 12.774 13.767 5.315   1.00 39.48  ? 222 ASP A N   1 
ATOM   1701 C CA  . ASP A 1 222 ? 13.107 13.449 6.709   1.00 38.05  ? 222 ASP A CA  1 
ATOM   1702 C C   . ASP A 1 222 ? 12.251 12.265 7.138   1.00 40.39  ? 222 ASP A C   1 
ATOM   1703 O O   . ASP A 1 222 ? 12.371 11.188 6.527   1.00 41.39  ? 222 ASP A O   1 
ATOM   1704 C CB  . ASP A 1 222 ? 12.970 14.711 7.567   1.00 35.42  ? 222 ASP A CB  1 
ATOM   1705 C CG  . ASP A 1 222 ? 13.848 15.850 7.088   1.00 31.69  ? 222 ASP A CG  1 
ATOM   1706 O OD1 . ASP A 1 222 ? 15.005 15.592 6.691   1.00 29.38  ? 222 ASP A OD1 1 
ATOM   1707 O OD2 . ASP A 1 222 ? 13.371 17.005 7.119   1.00 31.53  ? 222 ASP A OD2 1 
ATOM   1708 N N   . HIS A 1 223 ? 11.398 12.392 8.154   1.00 41.65  ? 223 HIS A N   1 
ATOM   1709 C CA  . HIS A 1 223 ? 10.579 11.274 8.600   1.00 44.76  ? 223 HIS A CA  1 
ATOM   1710 C C   . HIS A 1 223 ? 9.310  11.105 7.780   1.00 47.24  ? 223 HIS A C   1 
ATOM   1711 O O   . HIS A 1 223 ? 8.674  10.053 7.873   1.00 47.79  ? 223 HIS A O   1 
ATOM   1712 C CB  . HIS A 1 223 ? 10.209 11.431 10.080  0.80 46.98  ? 223 HIS A CB  1 
ATOM   1713 C CG  . HIS A 1 223 ? 9.526  12.723 10.407  0.70 49.01  ? 223 HIS A CG  1 
ATOM   1714 N ND1 . HIS A 1 223 ? 10.141 13.945 10.248  0.70 48.27  ? 223 HIS A ND1 1 
ATOM   1715 C CD2 . HIS A 1 223 ? 8.294  12.984 10.905  0.70 51.05  ? 223 HIS A CD2 1 
ATOM   1716 C CE1 . HIS A 1 223 ? 9.315  14.905 10.622  0.70 49.80  ? 223 HIS A CE1 1 
ATOM   1717 N NE2 . HIS A 1 223 ? 8.187  14.348 11.026  0.70 51.33  ? 223 HIS A NE2 1 
ATOM   1718 N N   . LEU A 1 224 ? 8.926  12.101 6.986   1.00 49.00  ? 224 LEU A N   1 
ATOM   1719 C CA  . LEU A 1 224 ? 7.738  11.962 6.157   1.00 51.31  ? 224 LEU A CA  1 
ATOM   1720 C C   . LEU A 1 224 ? 8.011  11.025 4.983   1.00 52.78  ? 224 LEU A C   1 
ATOM   1721 O O   . LEU A 1 224 ? 9.146  10.880 4.522   1.00 52.70  ? 224 LEU A O   1 
ATOM   1722 C CB  . LEU A 1 224 ? 7.271  13.326 5.633   1.00 51.47  ? 224 LEU A CB  1 
ATOM   1723 C CG  . LEU A 1 224 ? 6.488  14.289 6.540   0.78 53.51  ? 224 LEU A CG  1 
ATOM   1724 C CD1 . LEU A 1 224 ? 7.359  14.906 7.635   0.54 52.77  ? 224 LEU A CD1 1 
ATOM   1725 C CD2 . LEU A 1 224 ? 5.816  15.382 5.712   0.55 54.39  ? 224 LEU A CD2 1 
ATOM   1726 N N   . SER A 1 225 ? 6.954  10.368 4.512   1.00 55.70  ? 225 SER A N   1 
ATOM   1727 C CA  . SER A 1 225 ? 7.010  9.548  3.305   1.00 56.26  ? 225 SER A CA  1 
ATOM   1728 C C   . SER A 1 225 ? 5.695  9.723  2.564   1.00 57.66  ? 225 SER A C   1 
ATOM   1729 O O   . SER A 1 225 ? 4.635  9.358  3.083   1.00 55.78  ? 225 SER A O   1 
ATOM   1730 C CB  . SER A 1 225 ? 7.260  8.069  3.626   1.00 58.49  ? 225 SER A CB  1 
ATOM   1731 O OG  . SER A 1 225 ? 7.566  7.336  2.449   1.00 59.33  ? 225 SER A OG  1 
ATOM   1732 N N   . ILE A 1 226 ? 5.765  10.288 1.364   1.00 59.90  ? 226 ILE A N   1 
ATOM   1733 C CA  . ILE A 1 226 ? 4.584  10.609 0.577   1.00 60.78  ? 226 ILE A CA  1 
ATOM   1734 C C   . ILE A 1 226 ? 4.606  9.788  -0.702  1.00 58.38  ? 226 ILE A C   1 
ATOM   1735 O O   . ILE A 1 226 ? 5.671  9.489  -1.252  1.00 56.48  ? 226 ILE A O   1 
ATOM   1736 C CB  . ILE A 1 226 ? 4.513  12.115 0.247   0.80 61.08  ? 226 ILE A CB  1 
ATOM   1737 C CG1 . ILE A 1 226 ? 4.902  12.954 1.463   0.70 61.39  ? 226 ILE A CG1 1 
ATOM   1738 C CG2 . ILE A 1 226 ? 3.122  12.494 -0.236  0.70 62.49  ? 226 ILE A CG2 1 
ATOM   1739 C CD1 . ILE A 1 226 ? 5.087  14.421 1.143   0.70 61.42  ? 226 ILE A CD1 1 
ATOM   1740 N N   . LEU A 1 227 ? 3.419  9.421  -1.172  0.84 60.65  ? 227 LEU A N   1 
ATOM   1741 C CA  . LEU A 1 227 ? 3.259  8.866  -2.507  0.84 62.25  ? 227 LEU A CA  1 
ATOM   1742 C C   . LEU A 1 227 ? 2.824  9.974  -3.456  0.84 62.50  ? 227 LEU A C   1 
ATOM   1743 O O   . LEU A 1 227 ? 1.871  10.706 -3.171  0.84 67.07  ? 227 LEU A O   1 
ATOM   1744 C CB  . LEU A 1 227 ? 2.236  7.731  -2.513  0.84 66.38  ? 227 LEU A CB  1 
ATOM   1745 C CG  . LEU A 1 227 ? 1.847  7.204  -3.896  0.84 69.41  ? 227 LEU A CG  1 
ATOM   1746 C CD1 . LEU A 1 227 ? 3.076  6.746  -4.664  0.84 38.43  ? 227 LEU A CD1 1 
ATOM   1747 C CD2 . LEU A 1 227 ? 0.838  6.074  -3.778  0.84 42.93  ? 227 LEU A CD2 1 
ATOM   1748 N N   . HIS A 1 228 ? 3.530  10.099 -4.576  1.00 57.26  ? 228 HIS A N   1 
ATOM   1749 C CA  . HIS A 1 228 ? 3.226  11.088 -5.598  1.00 58.58  ? 228 HIS A CA  1 
ATOM   1750 C C   . HIS A 1 228 ? 2.908  10.381 -6.908  1.00 57.85  ? 228 HIS A C   1 
ATOM   1751 O O   . HIS A 1 228 ? 3.627  9.465  -7.319  1.00 56.14  ? 228 HIS A O   1 
ATOM   1752 C CB  . HIS A 1 228 ? 4.394  12.063 -5.791  1.00 58.47  ? 228 HIS A CB  1 
ATOM   1753 C CG  . HIS A 1 228 ? 4.650  12.945 -4.607  1.00 60.11  ? 228 HIS A CG  1 
ATOM   1754 N ND1 . HIS A 1 228 ? 4.382  14.297 -4.616  1.00 61.26  ? 228 HIS A ND1 1 
ATOM   1755 C CD2 . HIS A 1 228 ? 5.152  12.670 -3.380  1.00 59.81  ? 228 HIS A CD2 1 
ATOM   1756 C CE1 . HIS A 1 228 ? 4.706  14.817 -3.445  1.00 60.96  ? 228 HIS A CE1 1 
ATOM   1757 N NE2 . HIS A 1 228 ? 5.175  13.850 -2.676  1.00 59.90  ? 228 HIS A NE2 1 
ATOM   1758 N N   . ARG A 1 229 ? 1.832  10.810 -7.561  1.00 56.75  ? 229 ARG A N   1 
ATOM   1759 C CA  . ARG A 1 229 ? 1.397  10.223 -8.818  1.00 56.05  ? 229 ARG A CA  1 
ATOM   1760 C C   . ARG A 1 229 ? 1.538  11.230 -9.951  1.00 58.05  ? 229 ARG A C   1 
ATOM   1761 O O   . ARG A 1 229 ? 1.500  12.445 -9.732  1.00 58.73  ? 229 ARG A O   1 
ATOM   1762 C CB  . ARG A 1 229 ? -0.057 9.751  -8.737  1.00 56.57  ? 229 ARG A CB  1 
ATOM   1763 C CG  . ARG A 1 229 ? -0.332 8.752  -7.632  0.90 55.64  ? 229 ARG A CG  1 
ATOM   1764 C CD  . ARG A 1 229 ? -1.620 7.996  -7.915  0.70 57.40  ? 229 ARG A CD  1 
ATOM   1765 N NE  . ARG A 1 229 ? -2.043 7.178  -6.783  0.60 57.96  ? 229 ARG A NE  1 
ATOM   1766 C CZ  . ARG A 1 229 ? -1.576 5.961  -6.521  0.50 57.96  ? 229 ARG A CZ  1 
ATOM   1767 N NH1 . ARG A 1 229 ? -0.658 5.417  -7.307  0.50 56.95  ? 229 ARG A NH1 1 
ATOM   1768 N NH2 . ARG A 1 229 ? -2.024 5.292  -5.468  0.50 49.37  ? 229 ARG A NH2 1 
ATOM   1769 N N   . ASP A 1 230 ? 1.694  10.705 -11.169 1.00 58.77  ? 230 ASP A N   1 
ATOM   1770 C CA  . ASP A 1 230 ? 1.804  11.522 -12.379 1.00 58.71  ? 230 ASP A CA  1 
ATOM   1771 C C   . ASP A 1 230 ? 2.937  12.539 -12.248 1.00 55.65  ? 230 ASP A C   1 
ATOM   1772 O O   . ASP A 1 230 ? 2.762  13.735 -12.481 1.00 57.08  ? 230 ASP A O   1 
ATOM   1773 C CB  . ASP A 1 230 ? 0.473  12.213 -12.695 0.70 60.03  ? 230 ASP A CB  1 
ATOM   1774 C CG  . ASP A 1 230 ? 0.443  12.823 -14.084 0.50 60.60  ? 230 ASP A CG  1 
ATOM   1775 O OD1 . ASP A 1 230 ? 1.242  12.395 -14.942 0.50 59.12  ? 230 ASP A OD1 1 
ATOM   1776 O OD2 . ASP A 1 230 ? -0.378 13.736 -14.316 0.50 62.82  ? 230 ASP A OD2 1 
ATOM   1777 N N   . VAL A 1 231 ? 4.111  12.051 -11.859 1.00 52.61  ? 231 VAL A N   1 
ATOM   1778 C CA  . VAL A 1 231 ? 5.262  12.907 -11.599 1.00 50.74  ? 231 VAL A CA  1 
ATOM   1779 C C   . VAL A 1 231 ? 5.971  13.209 -12.909 1.00 50.90  ? 231 VAL A C   1 
ATOM   1780 O O   . VAL A 1 231 ? 6.325  12.294 -13.662 1.00 50.68  ? 231 VAL A O   1 
ATOM   1781 C CB  . VAL A 1 231 ? 6.225  12.249 -10.597 1.00 49.15  ? 231 VAL A CB  1 
ATOM   1782 C CG1 . VAL A 1 231 ? 7.537  13.015 -10.553 1.00 46.77  ? 231 VAL A CG1 1 
ATOM   1783 C CG2 . VAL A 1 231 ? 5.595  12.192 -9.219  1.00 50.53  ? 231 VAL A CG2 1 
ATOM   1784 N N   . GLN A 1 232 ? 6.191  14.494 -13.176 1.00 50.73  ? 232 GLN A N   1 
ATOM   1785 C CA  . GLN A 1 232 ? 6.957  14.913 -14.340 1.00 50.06  ? 232 GLN A CA  1 
ATOM   1786 C C   . GLN A 1 232 ? 8.429  15.135 -14.024 1.00 49.33  ? 232 GLN A C   1 
ATOM   1787 O O   . GLN A 1 232 ? 9.275  14.950 -14.908 1.00 48.73  ? 232 GLN A O   1 
ATOM   1788 C CB  . GLN A 1 232 ? 6.363  16.198 -14.925 1.00 51.27  ? 232 GLN A CB  1 
ATOM   1789 N N   . GLU A 1 233 ? 8.758  15.509 -12.787 1.00 48.62  ? 233 GLU A N   1 
ATOM   1790 C CA  . GLU A 1 233 ? 10.111 15.935 -12.459 1.00 44.57  ? 233 GLU A CA  1 
ATOM   1791 C C   . GLU A 1 233 ? 10.245 16.114 -10.953 1.00 46.46  ? 233 GLU A C   1 
ATOM   1792 O O   . GLU A 1 233 ? 9.353  16.670 -10.308 1.00 49.72  ? 233 GLU A O   1 
ATOM   1793 C CB  . GLU A 1 233 ? 10.449 17.247 -13.182 0.90 42.10  ? 233 GLU A CB  1 
ATOM   1794 C CG  . GLU A 1 233 ? 11.749 17.909 -12.764 0.80 39.00  ? 233 GLU A CG  1 
ATOM   1795 C CD  . GLU A 1 233 ? 11.934 19.259 -13.425 0.70 39.30  ? 233 GLU A CD  1 
ATOM   1796 O OE1 . GLU A 1 233 ? 10.920 19.876 -13.810 0.70 41.09  ? 233 GLU A OE1 1 
ATOM   1797 O OE2 . GLU A 1 233 ? 13.091 19.704 -13.566 0.70 38.59  ? 233 GLU A OE2 1 
ATOM   1798 N N   . ILE A 1 234 ? 11.361 15.643 -10.406 1.00 44.11  ? 234 ILE A N   1 
ATOM   1799 C CA  . ILE A 1 234 ? 11.766 15.925 -9.034  1.00 43.92  ? 234 ILE A CA  1 
ATOM   1800 C C   . ILE A 1 234 ? 13.053 16.732 -9.106  1.00 43.92  ? 234 ILE A C   1 
ATOM   1801 O O   . ILE A 1 234 ? 13.975 16.365 -9.845  1.00 43.91  ? 234 ILE A O   1 
ATOM   1802 C CB  . ILE A 1 234 ? 11.964 14.634 -8.218  1.00 41.44  ? 234 ILE A CB  1 
ATOM   1803 C CG1 . ILE A 1 234 ? 10.712 13.759 -8.295  1.00 41.42  ? 234 ILE A CG1 1 
ATOM   1804 C CG2 . ILE A 1 234 ? 12.292 14.960 -6.767  1.00 39.70  ? 234 ILE A CG2 1 
ATOM   1805 C CD1 . ILE A 1 234 ? 10.874 12.387 -7.667  1.00 40.70  ? 234 ILE A CD1 1 
ATOM   1806 N N   . ARG A 1 235 ? 13.108 17.839 -8.366  1.00 42.60  ? 235 ARG A N   1 
ATOM   1807 C CA  . ARG A 1 235 ? 14.200 18.794 -8.496  1.00 40.14  ? 235 ARG A CA  1 
ATOM   1808 C C   . ARG A 1 235 ? 14.830 19.056 -7.138  1.00 37.40  ? 235 ARG A C   1 
ATOM   1809 O O   . ARG A 1 235 ? 14.129 19.373 -6.171  1.00 36.85  ? 235 ARG A O   1 
ATOM   1810 C CB  . ARG A 1 235 ? 13.717 20.103 -9.130  1.00 42.95  ? 235 ARG A CB  1 
ATOM   1811 C CG  . ARG A 1 235 ? 14.602 20.579 -10.274 1.00 45.60  ? 235 ARG A CG  1 
ATOM   1812 C CD  . ARG A 1 235 ? 13.892 21.604 -11.135 0.70 48.44  ? 235 ARG A CD  1 
ATOM   1813 N NE  . ARG A 1 235 ? 13.519 22.801 -10.387 0.60 49.48  ? 235 ARG A NE  1 
ATOM   1814 C CZ  . ARG A 1 235 ? 12.559 23.642 -10.760 0.50 51.69  ? 235 ARG A CZ  1 
ATOM   1815 N NH1 . ARG A 1 235 ? 12.283 24.710 -10.025 0.50 53.11  ? 235 ARG A NH1 1 
ATOM   1816 N NH2 . ARG A 1 235 ? 11.866 23.407 -11.864 0.50 52.46  ? 235 ARG A NH2 1 
ATOM   1817 N N   . TYR A 1 236 ? 16.152 18.927 -7.078  1.00 35.84  ? 236 TYR A N   1 
ATOM   1818 C CA  . TYR A 1 236 ? 16.925 19.149 -5.867  1.00 35.29  ? 236 TYR A CA  1 
ATOM   1819 C C   . TYR A 1 236 ? 17.783 20.398 -6.015  1.00 36.87  ? 236 TYR A C   1 
ATOM   1820 O O   . TYR A 1 236 ? 18.256 20.723 -7.107  1.00 39.78  ? 236 TYR A O   1 
ATOM   1821 C CB  . TYR A 1 236 ? 17.799 17.936 -5.551  1.00 34.73  ? 236 TYR A CB  1 
ATOM   1822 C CG  . TYR A 1 236 ? 16.980 16.745 -5.125  1.00 37.00  ? 236 TYR A CG  1 
ATOM   1823 C CD1 . TYR A 1 236 ? 16.025 16.870 -4.126  1.00 37.98  ? 236 TYR A CD1 1 
ATOM   1824 C CD2 . TYR A 1 236 ? 17.135 15.509 -5.737  1.00 37.33  ? 236 TYR A CD2 1 
ATOM   1825 C CE1 . TYR A 1 236 ? 15.262 15.798 -3.732  1.00 38.29  ? 236 TYR A CE1 1 
ATOM   1826 C CE2 . TYR A 1 236 ? 16.374 14.427 -5.352  1.00 37.68  ? 236 TYR A CE2 1 
ATOM   1827 C CZ  . TYR A 1 236 ? 15.439 14.580 -4.348  1.00 39.56  ? 236 TYR A CZ  1 
ATOM   1828 O OH  . TYR A 1 236 ? 14.674 13.513 -3.954  1.00 42.78  ? 236 TYR A OH  1 
ATOM   1829 N N   . GLU A 1 237 ? 17.996 21.083 -4.894  1.00 36.08  ? 237 GLU A N   1 
ATOM   1830 C CA  . GLU A 1 237 ? 18.576 22.417 -4.903  1.00 36.53  ? 237 GLU A CA  1 
ATOM   1831 C C   . GLU A 1 237 ? 18.865 22.828 -3.467  1.00 36.69  ? 237 GLU A C   1 
ATOM   1832 O O   . GLU A 1 237 ? 18.081 22.520 -2.565  1.00 36.08  ? 237 GLU A O   1 
ATOM   1833 C CB  . GLU A 1 237 ? 17.607 23.408 -5.563  1.00 37.82  ? 237 GLU A CB  1 
ATOM   1834 C CG  . GLU A 1 237 ? 18.207 24.715 -6.026  0.70 37.46  ? 237 GLU A CG  1 
ATOM   1835 C CD  . GLU A 1 237 ? 17.209 25.545 -6.818  0.60 37.07  ? 237 GLU A CD  1 
ATOM   1836 O OE1 . GLU A 1 237 ? 16.107 25.031 -7.107  0.60 35.51  ? 237 GLU A OE1 1 
ATOM   1837 O OE2 . GLU A 1 237 ? 17.522 26.706 -7.149  0.60 37.99  ? 237 GLU A OE2 1 
ATOM   1838 N N   . VAL A 1 238 ? 19.992 23.507 -3.261  1.00 35.76  ? 238 VAL A N   1 
ATOM   1839 C CA  . VAL A 1 238 ? 20.318 24.033 -1.940  1.00 33.46  ? 238 VAL A CA  1 
ATOM   1840 C C   . VAL A 1 238 ? 19.402 25.217 -1.654  1.00 36.55  ? 238 VAL A C   1 
ATOM   1841 O O   . VAL A 1 238 ? 19.364 26.187 -2.418  1.00 41.00  ? 238 VAL A O   1 
ATOM   1842 C CB  . VAL A 1 238 ? 21.798 24.432 -1.857  1.00 29.28  ? 238 VAL A CB  1 
ATOM   1843 C CG1 . VAL A 1 238 ? 22.063 25.266 -0.611  1.00 28.82  ? 238 VAL A CG1 1 
ATOM   1844 C CG2 . VAL A 1 238 ? 22.669 23.191 -1.873  1.00 26.20  ? 238 VAL A CG2 1 
ATOM   1845 N N   . SER A 1 239 ? 18.656 25.135 -0.555  1.00 42.09  ? 239 SER A N   1 
ATOM   1846 C CA  . SER A 1 239 ? 17.687 26.172 -0.230  1.00 34.02  ? 239 SER A CA  1 
ATOM   1847 C C   . SER A 1 239 ? 18.384 27.486 0.100   1.00 35.69  ? 239 SER A C   1 
ATOM   1848 O O   . SER A 1 239 ? 19.530 27.514 0.556   1.00 38.87  ? 239 SER A O   1 
ATOM   1849 C CB  . SER A 1 239 ? 16.822 25.737 0.952   1.00 35.16  ? 239 SER A CB  1 
ATOM   1850 O OG  . SER A 1 239 ? 15.985 26.795 1.378   1.00 37.43  ? 239 SER A OG  1 
ATOM   1851 N N   . ALA A 1 240 ? 17.676 28.587 -0.147  1.00 47.66  ? 240 ALA A N   1 
ATOM   1852 C CA  . ALA A 1 240 ? 18.129 29.886 0.325   1.00 49.76  ? 240 ALA A CA  1 
ATOM   1853 C C   . ALA A 1 240 ? 17.798 30.106 1.793   1.00 46.71  ? 240 ALA A C   1 
ATOM   1854 O O   . ALA A 1 240 ? 18.425 30.953 2.439   1.00 45.10  ? 240 ALA A O   1 
ATOM   1855 C CB  . ALA A 1 240 ? 17.509 31.001 -0.519  1.00 43.30  ? 240 ALA A CB  1 
ATOM   1856 N N   . LYS A 1 241 ? 16.826 29.372 2.324   1.00 46.32  ? 241 LYS A N   1 
ATOM   1857 C CA  . LYS A 1 241 ? 16.503 29.434 3.739   1.00 46.85  ? 241 LYS A CA  1 
ATOM   1858 C C   . LYS A 1 241 ? 17.440 28.529 4.527   1.00 46.01  ? 241 LYS A C   1 
ATOM   1859 O O   . LYS A 1 241 ? 17.889 27.488 4.041   1.00 43.93  ? 241 LYS A O   1 
ATOM   1860 C CB  . LYS A 1 241 ? 15.051 29.016 3.976   1.00 46.77  ? 241 LYS A CB  1 
ATOM   1861 C CG  . LYS A 1 241 ? 14.050 29.715 3.068   1.00 51.32  ? 241 LYS A CG  1 
ATOM   1862 C CD  . LYS A 1 241 ? 12.714 28.988 3.049   0.60 53.31  ? 241 LYS A CD  1 
ATOM   1863 C CE  . LYS A 1 241 ? 11.797 29.537 1.966   0.60 57.27  ? 241 LYS A CE  1 
ATOM   1864 N NZ  . LYS A 1 241 ? 10.579 28.699 1.798   0.60 57.95  ? 241 LYS A NZ  1 
ATOM   1865 N N   . LYS A 1 242 ? 17.740 28.939 5.755   1.00 49.00  ? 242 LYS A N   1 
ATOM   1866 C CA  . LYS A 1 242 ? 18.604 28.168 6.633   1.00 48.22  ? 242 LYS A CA  1 
ATOM   1867 C C   . LYS A 1 242 ? 17.938 28.021 7.992   1.00 48.29  ? 242 LYS A C   1 
ATOM   1868 O O   . LYS A 1 242 ? 17.053 28.797 8.359   1.00 52.28  ? 242 LYS A O   1 
ATOM   1869 C CB  . LYS A 1 242 ? 19.983 28.824 6.791   1.00 51.06  ? 242 LYS A CB  1 
ATOM   1870 C CG  . LYS A 1 242 ? 20.576 29.329 5.484   1.00 54.29  ? 242 LYS A CG  1 
ATOM   1871 C CD  . LYS A 1 242 ? 22.005 29.831 5.654   1.00 56.98  ? 242 LYS A CD  1 
ATOM   1872 C CE  . LYS A 1 242 ? 22.982 28.680 5.844   1.00 56.12  ? 242 LYS A CE  1 
ATOM   1873 N NZ  . LYS A 1 242 ? 24.391 29.158 5.917   0.39 57.40  ? 242 LYS A NZ  1 
ATOM   1874 N N   . ILE A 1 243 ? 18.368 27.006 8.736   1.00 44.77  ? 243 ILE A N   1 
ATOM   1875 C CA  . ILE A 1 243 ? 17.897 26.776 10.097  1.00 43.50  ? 243 ILE A CA  1 
ATOM   1876 C C   . ILE A 1 243 ? 18.910 27.384 11.054  1.00 43.73  ? 243 ILE A C   1 
ATOM   1877 O O   . ILE A 1 243 ? 20.123 27.239 10.862  1.00 44.49  ? 243 ILE A O   1 
ATOM   1878 C CB  . ILE A 1 243 ? 17.694 25.276 10.378  1.00 42.31  ? 243 ILE A CB  1 
ATOM   1879 C CG1 . ILE A 1 243 ? 17.211 25.053 11.815  1.00 42.14  ? 243 ILE A CG1 1 
ATOM   1880 C CG2 . ILE A 1 243 ? 18.977 24.489 10.104  1.00 42.37  ? 243 ILE A CG2 1 
ATOM   1881 C CD1 . ILE A 1 243 ? 17.076 23.592 12.194  1.00 39.96  ? 243 ILE A CD1 1 
ATOM   1882 N N   . HIS A 1 244 ? 18.418 28.083 12.071  1.00 44.10  ? 244 HIS A N   1 
ATOM   1883 C CA  . HIS A 1 244 ? 19.264 28.782 13.027  1.00 44.13  ? 244 HIS A CA  1 
ATOM   1884 C C   . HIS A 1 244 ? 19.239 28.055 14.364  1.00 40.39  ? 244 HIS A C   1 
ATOM   1885 O O   . HIS A 1 244 ? 18.164 27.750 14.892  1.00 39.93  ? 244 HIS A O   1 
ATOM   1886 C CB  . HIS A 1 244 ? 18.808 30.233 13.198  1.00 47.38  ? 244 HIS A CB  1 
ATOM   1887 C CG  . HIS A 1 244 ? 18.828 31.026 11.929  1.00 49.86  ? 244 HIS A CG  1 
ATOM   1888 N ND1 . HIS A 1 244 ? 19.963 31.647 11.456  1.00 50.75  ? 244 HIS A ND1 1 
ATOM   1889 C CD2 . HIS A 1 244 ? 17.849 31.300 11.034  1.00 50.66  ? 244 HIS A CD2 1 
ATOM   1890 C CE1 . HIS A 1 244 ? 19.683 32.270 10.325  1.00 51.68  ? 244 HIS A CE1 1 
ATOM   1891 N NE2 . HIS A 1 244 ? 18.407 32.075 10.047  1.00 51.55  ? 244 HIS A NE2 1 
ATOM   1892 N N   . PHE A 1 245 ? 20.421 27.781 14.907  1.00 39.21  ? 245 PHE A N   1 
ATOM   1893 C CA  . PHE A 1 245 ? 20.563 27.137 16.205  1.00 39.28  ? 245 PHE A CA  1 
ATOM   1894 C C   . PHE A 1 245 ? 21.055 28.144 17.234  1.00 41.31  ? 245 PHE A C   1 
ATOM   1895 O O   . PHE A 1 245 ? 21.956 28.939 16.955  1.00 41.94  ? 245 PHE A O   1 
ATOM   1896 C CB  . PHE A 1 245 ? 21.547 25.964 16.143  1.00 39.52  ? 245 PHE A CB  1 
ATOM   1897 C CG  . PHE A 1 245 ? 21.063 24.800 15.328  1.00 39.28  ? 245 PHE A CG  1 
ATOM   1898 C CD1 . PHE A 1 245 ? 20.345 23.778 15.921  1.00 39.33  ? 245 PHE A CD1 1 
ATOM   1899 C CD2 . PHE A 1 245 ? 21.338 24.721 13.973  1.00 39.58  ? 245 PHE A CD2 1 
ATOM   1900 C CE1 . PHE A 1 245 ? 19.906 22.705 15.178  1.00 38.35  ? 245 PHE A CE1 1 
ATOM   1901 C CE2 . PHE A 1 245 ? 20.897 23.647 13.221  1.00 39.27  ? 245 PHE A CE2 1 
ATOM   1902 C CZ  . PHE A 1 245 ? 20.179 22.640 13.825  1.00 38.20  ? 245 PHE A CZ  1 
ATOM   1903 N N   . ALA A 1 246 ? 20.468 28.103 18.426  1.00 44.33  ? 246 ALA A N   1 
ATOM   1904 C CA  . ALA A 1 246 ? 20.968 28.877 19.555  1.00 46.81  ? 246 ALA A CA  1 
ATOM   1905 C C   . ALA A 1 246 ? 22.031 28.056 20.275  1.00 46.85  ? 246 ALA A C   1 
ATOM   1906 O O   . ALA A 1 246 ? 21.740 26.969 20.787  1.00 45.71  ? 246 ALA A O   1 
ATOM   1907 C CB  . ALA A 1 246 ? 19.835 29.258 20.507  1.00 48.26  ? 246 ALA A CB  1 
ATOM   1908 N N   . ARG A 1 247 ? 23.258 28.569 20.303  1.00 48.01  ? 247 ARG A N   1 
ATOM   1909 C CA  . ARG A 1 247 ? 24.388 27.889 20.920  1.00 49.39  ? 247 ARG A CA  1 
ATOM   1910 C C   . ARG A 1 247 ? 24.865 28.679 22.129  1.00 51.69  ? 247 ARG A C   1 
ATOM   1911 O O   . ARG A 1 247 ? 24.999 29.905 22.069  1.00 53.11  ? 247 ARG A O   1 
ATOM   1912 C CB  . ARG A 1 247 ? 25.538 27.716 19.926  1.00 50.93  ? 247 ARG A CB  1 
ATOM   1913 C CG  . ARG A 1 247 ? 25.190 26.885 18.699  1.00 50.97  ? 247 ARG A CG  1 
ATOM   1914 C CD  . ARG A 1 247 ? 25.614 25.432 18.858  1.00 52.86  ? 247 ARG A CD  1 
ATOM   1915 N NE  . ARG A 1 247 ? 25.644 24.724 17.580  1.00 53.73  ? 247 ARG A NE  1 
ATOM   1916 C CZ  . ARG A 1 247 ? 24.731 23.839 17.189  1.00 54.19  ? 247 ARG A CZ  1 
ATOM   1917 N NH1 . ARG A 1 247 ? 23.711 23.546 17.981  1.00 55.44  ? 247 ARG A NH1 1 
ATOM   1918 N NH2 . ARG A 1 247 ? 24.842 23.243 16.009  1.00 53.03  ? 247 ARG A NH2 1 
ATOM   1919 N N   . PHE A 1 248 ? 25.128 27.968 23.227  1.00 53.13  ? 248 PHE A N   1 
ATOM   1920 C CA  . PHE A 1 248 ? 25.574 28.592 24.464  1.00 56.32  ? 248 PHE A CA  1 
ATOM   1921 C C   . PHE A 1 248 ? 27.002 28.235 24.847  1.00 58.25  ? 248 PHE A C   1 
ATOM   1922 O O   . PHE A 1 248 ? 27.632 28.990 25.594  1.00 62.70  ? 248 PHE A O   1 
ATOM   1923 C CB  . PHE A 1 248 ? 24.634 28.213 25.618  0.90 56.71  ? 248 PHE A CB  1 
ATOM   1924 C CG  . PHE A 1 248 ? 23.216 28.684 25.423  0.80 48.47  ? 248 PHE A CG  1 
ATOM   1925 C CD1 . PHE A 1 248 ? 22.329 27.960 24.642  0.80 46.15  ? 248 PHE A CD1 1 
ATOM   1926 C CD2 . PHE A 1 248 ? 22.770 29.850 26.021  0.80 50.88  ? 248 PHE A CD2 1 
ATOM   1927 C CE1 . PHE A 1 248 ? 21.026 28.394 24.460  0.80 46.41  ? 248 PHE A CE1 1 
ATOM   1928 C CE2 . PHE A 1 248 ? 21.466 30.285 25.847  0.80 51.03  ? 248 PHE A CE2 1 
ATOM   1929 C CZ  . PHE A 1 248 ? 20.594 29.556 25.067  0.80 49.10  ? 248 PHE A CZ  1 
ATOM   1930 N N   . ARG A 1 249 ? 27.520 27.109 24.362  1.00 55.29  ? 249 ARG A N   1 
ATOM   1931 C CA  . ARG A 1 249 ? 28.915 26.730 24.529  1.00 57.56  ? 249 ARG A CA  1 
ATOM   1932 C C   . ARG A 1 249 ? 29.420 26.218 23.187  1.00 56.55  ? 249 ARG A C   1 
ATOM   1933 O O   . ARG A 1 249 ? 28.658 26.096 22.224  1.00 54.72  ? 249 ARG A O   1 
ATOM   1934 C CB  . ARG A 1 249 ? 29.082 25.676 25.631  1.00 58.00  ? 249 ARG A CB  1 
ATOM   1935 N N   . SER A 1 250 ? 30.712 25.907 23.119  1.00 56.84  ? 250 SER A N   1 
ATOM   1936 C CA  . SER A 1 250 ? 31.310 25.397 21.894  1.00 55.14  ? 250 SER A CA  1 
ATOM   1937 C C   . SER A 1 250 ? 31.114 23.887 21.812  1.00 53.29  ? 250 SER A C   1 
ATOM   1938 O O   . SER A 1 250 ? 31.530 23.153 22.712  1.00 54.49  ? 250 SER A O   1 
ATOM   1939 C CB  . SER A 1 250 ? 32.798 25.743 21.834  1.00 57.07  ? 250 SER A CB  1 
ATOM   1940 O OG  . SER A 1 250 ? 33.302 25.563 20.522  0.70 56.00  ? 250 SER A OG  1 
ATOM   1941 N N   . PHE A 1 251 ? 30.462 23.433 20.742  1.00 49.01  ? 251 PHE A N   1 
ATOM   1942 C CA  . PHE A 1 251 ? 30.315 22.006 20.444  1.00 47.90  ? 251 PHE A CA  1 
ATOM   1943 C C   . PHE A 1 251 ? 30.556 21.828 18.954  1.00 45.76  ? 251 PHE A C   1 
ATOM   1944 O O   . PHE A 1 251 ? 29.613 21.802 18.153  1.00 45.47  ? 251 PHE A O   1 
ATOM   1945 C CB  . PHE A 1 251 ? 28.930 21.486 20.846  1.00 47.84  ? 251 PHE A CB  1 
ATOM   1946 C CG  . PHE A 1 251 ? 28.835 19.976 20.918  1.00 48.26  ? 251 PHE A CG  1 
ATOM   1947 C CD1 . PHE A 1 251 ? 29.970 19.185 20.814  0.90 48.89  ? 251 PHE A CD1 1 
ATOM   1948 C CD2 . PHE A 1 251 ? 27.608 19.352 21.087  0.90 47.21  ? 251 PHE A CD2 1 
ATOM   1949 C CE1 . PHE A 1 251 ? 29.883 17.804 20.885  0.90 47.89  ? 251 PHE A CE1 1 
ATOM   1950 C CE2 . PHE A 1 251 ? 27.514 17.969 21.156  0.90 46.36  ? 251 PHE A CE2 1 
ATOM   1951 C CZ  . PHE A 1 251 ? 28.652 17.196 21.055  0.90 46.81  ? 251 PHE A CZ  1 
ATOM   1952 N N   . PRO A 1 252 ? 31.818 21.709 18.542  1.00 45.19  ? 252 PRO A N   1 
ATOM   1953 C CA  . PRO A 1 252 ? 32.118 21.651 17.108  1.00 40.93  ? 252 PRO A CA  1 
ATOM   1954 C C   . PRO A 1 252 ? 31.463 20.450 16.445  1.00 37.45  ? 252 PRO A C   1 
ATOM   1955 O O   . PRO A 1 252 ? 31.221 19.417 17.073  1.00 37.45  ? 252 PRO A O   1 
ATOM   1956 C CB  . PRO A 1 252 ? 33.648 21.550 17.068  1.00 43.33  ? 252 PRO A CB  1 
ATOM   1957 C CG  . PRO A 1 252 ? 34.096 22.097 18.380  1.00 47.09  ? 252 PRO A CG  1 
ATOM   1958 C CD  . PRO A 1 252 ? 33.043 21.670 19.357  1.00 47.19  ? 252 PRO A CD  1 
ATOM   1959 N N   . PHE A 1 253 ? 31.166 20.610 15.153  1.00 35.38  ? 253 PHE A N   1 
ATOM   1960 C CA  . PHE A 1 253 ? 30.507 19.548 14.402  1.00 33.11  ? 253 PHE A CA  1 
ATOM   1961 C C   . PHE A 1 253 ? 31.325 18.263 14.426  1.00 32.76  ? 253 PHE A C   1 
ATOM   1962 O O   . PHE A 1 253 ? 30.765 17.167 14.536  1.00 31.89  ? 253 PHE A O   1 
ATOM   1963 C CB  . PHE A 1 253 ? 30.260 20.006 12.965  1.00 31.52  ? 253 PHE A CB  1 
ATOM   1964 C CG  . PHE A 1 253 ? 29.568 18.982 12.113  1.00 31.30  ? 253 PHE A CG  1 
ATOM   1965 C CD1 . PHE A 1 253 ? 28.196 18.813 12.191  1.00 31.65  ? 253 PHE A CD1 1 
ATOM   1966 C CD2 . PHE A 1 253 ? 30.286 18.189 11.233  1.00 32.15  ? 253 PHE A CD2 1 
ATOM   1967 C CE1 . PHE A 1 253 ? 27.553 17.871 11.410  1.00 31.07  ? 253 PHE A CE1 1 
ATOM   1968 C CE2 . PHE A 1 253 ? 29.649 17.246 10.448  1.00 33.08  ? 253 PHE A CE2 1 
ATOM   1969 C CZ  . PHE A 1 253 ? 28.280 17.087 10.537  1.00 32.67  ? 253 PHE A CZ  1 
ATOM   1970 N N   . TRP A 1 254 ? 32.653 18.380 14.337  1.00 34.42  ? 254 TRP A N   1 
ATOM   1971 C CA  . TRP A 1 254 ? 33.500 17.192 14.315  1.00 37.16  ? 254 TRP A CA  1 
ATOM   1972 C C   . TRP A 1 254 ? 33.534 16.510 15.677  1.00 38.98  ? 254 TRP A C   1 
ATOM   1973 O O   . TRP A 1 254 ? 33.596 15.277 15.759  1.00 36.54  ? 254 TRP A O   1 
ATOM   1974 C CB  . TRP A 1 254 ? 34.909 17.564 13.856  1.00 37.61  ? 254 TRP A CB  1 
ATOM   1975 C CG  . TRP A 1 254 ? 34.965 18.085 12.451  1.00 37.08  ? 254 TRP A CG  1 
ATOM   1976 C CD1 . TRP A 1 254 ? 35.475 19.282 12.042  1.00 37.81  ? 254 TRP A CD1 1 
ATOM   1977 C CD2 . TRP A 1 254 ? 34.491 17.425 11.269  1.00 35.14  ? 254 TRP A CD2 1 
ATOM   1978 N NE1 . TRP A 1 254 ? 35.355 19.407 10.676  1.00 36.74  ? 254 TRP A NE1 1 
ATOM   1979 C CE2 . TRP A 1 254 ? 34.754 18.280 10.179  1.00 35.48  ? 254 TRP A CE2 1 
ATOM   1980 C CE3 . TRP A 1 254 ? 33.875 16.192 11.026  1.00 33.97  ? 254 TRP A CE3 1 
ATOM   1981 C CZ2 . TRP A 1 254 ? 34.422 17.943 8.870   1.00 33.71  ? 254 TRP A CZ2 1 
ATOM   1982 C CZ3 . TRP A 1 254 ? 33.544 15.863 9.724   1.00 33.32  ? 254 TRP A CZ3 1 
ATOM   1983 C CH2 . TRP A 1 254 ? 33.819 16.734 8.664   1.00 33.08  ? 254 TRP A CH2 1 
ATOM   1984 N N   . ARG A 1 255 ? 33.510 17.290 16.760  1.00 37.63  ? 255 ARG A N   1 
ATOM   1985 C CA  . ARG A 1 255 ? 33.379 16.682 18.080  1.00 40.49  ? 255 ARG A CA  1 
ATOM   1986 C C   . ARG A 1 255 ? 31.999 16.064 18.251  1.00 38.00  ? 255 ARG A C   1 
ATOM   1987 O O   . ARG A 1 255 ? 31.862 14.985 18.841  1.00 37.78  ? 255 ARG A O   1 
ATOM   1988 C CB  . ARG A 1 255 ? 33.654 17.712 19.176  1.00 43.63  ? 255 ARG A CB  1 
ATOM   1989 C CG  . ARG A 1 255 ? 33.369 17.213 20.589  1.00 48.05  ? 255 ARG A CG  1 
ATOM   1990 C CD  . ARG A 1 255 ? 34.325 17.810 21.617  1.00 54.32  ? 255 ARG A CD  1 
ATOM   1991 N NE  . ARG A 1 255 ? 33.642 18.678 22.572  1.00 58.70  ? 255 ARG A NE  1 
ATOM   1992 C CZ  . ARG A 1 255 ? 33.897 19.973 22.727  1.00 62.60  ? 255 ARG A CZ  1 
ATOM   1993 N NH1 . ARG A 1 255 ? 34.836 20.560 21.998  1.00 63.64  ? 255 ARG A NH1 1 
ATOM   1994 N NH2 . ARG A 1 255 ? 33.220 20.678 23.622  1.00 64.79  ? 255 ARG A NH2 1 
ATOM   1995 N N   . ARG A 1 256 ? 30.967 16.730 17.725  1.00 35.29  ? 256 ARG A N   1 
ATOM   1996 C CA  . ARG A 1 256 ? 29.635 16.138 17.702  1.00 33.78  ? 256 ARG A CA  1 
ATOM   1997 C C   . ARG A 1 256 ? 29.637 14.820 16.933  1.00 34.09  ? 256 ARG A C   1 
ATOM   1998 O O   . ARG A 1 256 ? 28.936 13.872 17.307  1.00 32.87  ? 256 ARG A O   1 
ATOM   1999 C CB  A ARG A 1 256 ? 28.631 17.118 17.097  0.49 35.14  ? 256 ARG A CB  1 
ATOM   2000 C CB  B ARG A 1 256 ? 28.642 17.127 17.089  0.51 35.14  ? 256 ARG A CB  1 
ATOM   2001 C CG  A ARG A 1 256 ? 27.188 16.666 17.222  0.49 34.00  ? 256 ARG A CG  1 
ATOM   2002 C CG  B ARG A 1 256 ? 27.243 16.579 16.870  0.51 33.70  ? 256 ARG A CG  1 
ATOM   2003 C CD  A ARG A 1 256 ? 26.247 17.611 16.501  0.49 29.93  ? 256 ARG A CD  1 
ATOM   2004 C CD  B ARG A 1 256 ? 26.341 17.613 16.208  0.51 29.69  ? 256 ARG A CD  1 
ATOM   2005 N NE  A ARG A 1 256 ? 26.274 18.952 17.071  0.49 31.51  ? 256 ARG A NE  1 
ATOM   2006 N NE  B ARG A 1 256 ? 26.040 18.734 17.093  0.51 31.23  ? 256 ARG A NE  1 
ATOM   2007 C CZ  A ARG A 1 256 ? 25.523 19.345 18.095  0.49 34.26  ? 256 ARG A CZ  1 
ATOM   2008 C CZ  B ARG A 1 256 ? 26.669 19.906 17.069  0.51 31.57  ? 256 ARG A CZ  1 
ATOM   2009 N NH1 A ARG A 1 256 ? 24.682 18.497 18.669  0.49 32.14  ? 256 ARG A NH1 1 
ATOM   2010 N NH1 B ARG A 1 256 ? 27.645 20.124 16.197  0.51 31.52  ? 256 ARG A NH1 1 
ATOM   2011 N NH2 A ARG A 1 256 ? 25.614 20.589 18.545  0.49 32.86  ? 256 ARG A NH2 1 
ATOM   2012 N NH2 B ARG A 1 256 ? 26.320 20.864 17.919  0.51 33.45  ? 256 ARG A NH2 1 
ATOM   2013 N N   . VAL A 1 257 ? 30.434 14.740 15.864  1.00 33.93  ? 257 VAL A N   1 
ATOM   2014 C CA  . VAL A 1 257 ? 30.565 13.491 15.115  1.00 32.22  ? 257 VAL A CA  1 
ATOM   2015 C C   . VAL A 1 257 ? 31.284 12.441 15.956  1.00 34.23  ? 257 VAL A C   1 
ATOM   2016 O O   . VAL A 1 257 ? 30.879 11.272 16.004  1.00 34.32  ? 257 VAL A O   1 
ATOM   2017 C CB  . VAL A 1 257 ? 31.292 13.740 13.779  1.00 31.75  ? 257 VAL A CB  1 
ATOM   2018 C CG1 . VAL A 1 257 ? 31.716 12.425 13.151  1.00 32.27  ? 257 VAL A CG1 1 
ATOM   2019 C CG2 . VAL A 1 257 ? 30.407 14.523 12.819  1.00 29.86  ? 257 VAL A CG2 1 
ATOM   2020 N N   . HIS A 1 258 ? 32.363 12.845 16.633  1.00 36.21  ? 258 HIS A N   1 
ATOM   2021 C CA  . HIS A 1 258 ? 33.153 11.900 17.419  1.00 38.60  ? 258 HIS A CA  1 
ATOM   2022 C C   . HIS A 1 258 ? 32.312 11.244 18.510  1.00 39.21  ? 258 HIS A C   1 
ATOM   2023 O O   . HIS A 1 258 ? 32.343 10.020 18.683  1.00 40.26  ? 258 HIS A O   1 
ATOM   2024 C CB  . HIS A 1 258 ? 34.364 12.610 18.026  1.00 41.76  ? 258 HIS A CB  1 
ATOM   2025 C CG  . HIS A 1 258 ? 35.067 11.812 19.081  1.00 43.78  ? 258 HIS A CG  1 
ATOM   2026 N ND1 . HIS A 1 258 ? 34.653 11.789 20.396  1.00 46.32  ? 258 HIS A ND1 1 
ATOM   2027 C CD2 . HIS A 1 258 ? 36.162 11.019 19.019  1.00 45.99  ? 258 HIS A CD2 1 
ATOM   2028 C CE1 . HIS A 1 258 ? 35.459 11.011 21.096  1.00 47.90  ? 258 HIS A CE1 1 
ATOM   2029 N NE2 . HIS A 1 258 ? 36.383 10.531 20.284  1.00 49.68  ? 258 HIS A NE2 1 
ATOM   2030 N N   . ASP A 1 259 ? 31.549 12.046 19.254  1.00 38.84  ? 259 ASP A N   1 
ATOM   2031 C CA  . ASP A 1 259 ? 30.755 11.503 20.352  1.00 41.09  ? 259 ASP A CA  1 
ATOM   2032 C C   . ASP A 1 259 ? 29.692 10.536 19.849  1.00 39.93  ? 259 ASP A C   1 
ATOM   2033 O O   . ASP A 1 259 ? 29.384 9.539  20.512  1.00 39.92  ? 259 ASP A O   1 
ATOM   2034 C CB  . ASP A 1 259 ? 30.111 12.643 21.140  1.00 43.70  ? 259 ASP A CB  1 
ATOM   2035 C CG  . ASP A 1 259 ? 31.135 13.573 21.757  1.00 49.54  ? 259 ASP A CG  1 
ATOM   2036 O OD1 . ASP A 1 259 ? 32.335 13.224 21.749  1.00 52.44  ? 259 ASP A OD1 1 
ATOM   2037 O OD2 . ASP A 1 259 ? 30.741 14.653 22.245  1.00 50.87  ? 259 ASP A OD2 1 
ATOM   2038 N N   . SER A 1 260 ? 29.124 10.808 18.674  1.00 39.08  ? 260 SER A N   1 
ATOM   2039 C CA  . SER A 1 260 ? 28.017 9.995  18.185  1.00 38.33  ? 260 SER A CA  1 
ATOM   2040 C C   . SER A 1 260 ? 28.475 8.663  17.601  1.00 39.10  ? 260 SER A C   1 
ATOM   2041 O O   . SER A 1 260 ? 27.716 7.689  17.639  1.00 38.60  ? 260 SER A O   1 
ATOM   2042 C CB  . SER A 1 260 ? 27.222 10.772 17.135  1.00 37.32  ? 260 SER A CB  1 
ATOM   2043 O OG  . SER A 1 260 ? 26.671 11.953 17.687  1.00 38.21  ? 260 SER A OG  1 
ATOM   2044 N N   . PHE A 1 261 ? 29.693 8.590  17.065  1.00 36.12  ? 261 PHE A N   1 
ATOM   2045 C CA  . PHE A 1 261 ? 30.124 7.412  16.324  1.00 36.69  ? 261 PHE A CA  1 
ATOM   2046 C C   . PHE A 1 261 ? 31.385 6.749  16.858  1.00 42.75  ? 261 PHE A C   1 
ATOM   2047 O O   . PHE A 1 261 ? 31.546 5.541  16.672  1.00 42.35  ? 261 PHE A O   1 
ATOM   2048 C CB  . PHE A 1 261 ? 30.338 7.770  14.847  1.00 35.38  ? 261 PHE A CB  1 
ATOM   2049 C CG  . PHE A 1 261 ? 29.090 8.230  14.152  1.00 32.70  ? 261 PHE A CG  1 
ATOM   2050 C CD1 . PHE A 1 261 ? 28.942 9.550  13.766  1.00 32.35  ? 261 PHE A CD1 1 
ATOM   2051 C CD2 . PHE A 1 261 ? 28.058 7.342  13.898  1.00 33.16  ? 261 PHE A CD2 1 
ATOM   2052 C CE1 . PHE A 1 261 ? 27.792 9.975  13.126  1.00 31.84  ? 261 PHE A CE1 1 
ATOM   2053 C CE2 . PHE A 1 261 ? 26.903 7.762  13.263  1.00 32.91  ? 261 PHE A CE2 1 
ATOM   2054 C CZ  . PHE A 1 261 ? 26.769 9.080  12.878  1.00 31.50  ? 261 PHE A CZ  1 
ATOM   2055 N N   . ILE A 1 262 ? 32.281 7.489  17.508  1.00 47.42  ? 262 ILE A N   1 
ATOM   2056 C CA  . ILE A 1 262 ? 33.508 6.892  18.023  1.00 55.47  ? 262 ILE A CA  1 
ATOM   2057 C C   . ILE A 1 262 ? 33.264 6.384  19.437  1.00 65.61  ? 262 ILE A C   1 
ATOM   2058 O O   . ILE A 1 262 ? 33.299 5.173  19.683  1.00 68.17  ? 262 ILE A O   1 
ATOM   2059 C CB  . ILE A 1 262 ? 34.679 7.890  17.977  1.00 55.02  ? 262 ILE A CB  1 
ATOM   2060 C CG1 . ILE A 1 262 ? 34.817 8.466  16.568  1.00 52.68  ? 262 ILE A CG1 1 
ATOM   2061 C CG2 . ILE A 1 262 ? 35.973 7.209  18.384  1.00 57.35  ? 262 ILE A CG2 1 
ATOM   2062 C CD1 . ILE A 1 262 ? 35.113 7.422  15.510  1.00 52.79  ? 262 ILE A CD1 1 
ATOM   2063 N N   . GLU A 1 263 ? 33.004 7.299  20.367  1.00 71.83  ? 263 GLU A N   1 
ATOM   2064 C CA  . GLU A 1 263 ? 32.713 6.950  21.753  1.00 80.09  ? 263 GLU A CA  1 
ATOM   2065 C C   . GLU A 1 263 ? 32.318 8.222  22.487  1.00 82.60  ? 263 GLU A C   1 
ATOM   2066 O O   . GLU A 1 263 ? 32.537 9.336  22.003  1.00 80.52  ? 263 GLU A O   1 
ATOM   2067 C CB  . GLU A 1 263 ? 33.908 6.284  22.439  0.99 85.93  ? 263 GLU A CB  1 
ATOM   2068 C CG  . GLU A 1 263 ? 35.130 7.179  22.539  0.88 88.57  ? 263 GLU A CG  1 
ATOM   2069 C CD  . GLU A 1 263 ? 36.415 6.391  22.695  0.88 93.56  ? 263 GLU A CD  1 
ATOM   2070 O OE1 . GLU A 1 263 ? 36.398 5.346  23.379  0.88 96.73  ? 263 GLU A OE1 1 
ATOM   2071 O OE2 . GLU A 1 263 ? 37.441 6.809  22.118  0.88 94.65  ? 263 GLU A OE2 1 
ATOM   2072 N N   . ASP A 1 264 ? 31.735 8.040  23.668  1.00 87.95  ? 264 ASP A N   1 
ATOM   2073 C CA  . ASP A 1 264 ? 31.380 9.160  24.533  1.00 90.96  ? 264 ASP A CA  1 
ATOM   2074 C C   . ASP A 1 264 ? 31.230 8.689  25.977  1.00 94.84  ? 264 ASP A C   1 
ATOM   2075 O O   . ASP A 1 264 ? 32.157 8.799  26.779  1.00 97.92  ? 264 ASP A O   1 
ATOM   2076 C CB  . ASP A 1 264 ? 30.088 9.830  24.056  1.00 89.93  ? 264 ASP A CB  1 
ATOM   2077 C CG  . ASP A 1 264 ? 29.868 11.185 24.694  1.00 92.09  ? 264 ASP A CG  1 
ATOM   2078 O OD1 . ASP A 1 264 ? 30.809 11.701 25.330  1.00 94.73  ? 264 ASP A OD1 1 
ATOM   2079 O OD2 . ASP A 1 264 ? 28.755 11.735 24.562  1.00 91.07  ? 264 ASP A OD2 1 
HETATM 2080 C C1  . CIT B 2 .   ? 31.887 24.357 14.413  1.00 79.52  ? 301 CIT A C1  1 
HETATM 2081 O O1  . CIT B 2 .   ? 31.437 23.260 14.022  1.00 78.39  ? 301 CIT A O1  1 
HETATM 2082 O O2  . CIT B 2 .   ? 33.126 24.515 14.452  1.00 78.94  ? 301 CIT A O2  1 
HETATM 2083 C C2  . CIT B 2 .   ? 30.956 25.468 14.844  1.00 82.55  ? 301 CIT A C2  1 
HETATM 2084 C C3  . CIT B 2 .   ? 29.583 24.901 15.193  1.00 85.59  ? 301 CIT A C3  1 
HETATM 2085 O O7  . CIT B 2 .   ? 29.745 23.667 15.939  1.00 87.05  ? 301 CIT A O7  1 
HETATM 2086 C C4  . CIT B 2 .   ? 28.756 25.879 16.017  1.00 86.22  ? 301 CIT A C4  1 
HETATM 2087 C C5  . CIT B 2 .   ? 29.367 26.070 17.384  1.00 86.88  ? 301 CIT A C5  1 
HETATM 2088 O O3  . CIT B 2 .   ? 29.344 27.192 17.936  1.00 86.61  ? 301 CIT A O3  1 
HETATM 2089 O O4  . CIT B 2 .   ? 29.903 25.110 17.978  1.00 86.86  ? 301 CIT A O4  1 
HETATM 2090 C C6  . CIT B 2 .   ? 28.794 24.620 13.926  1.00 86.46  ? 301 CIT A C6  1 
HETATM 2091 O O5  . CIT B 2 .   ? 29.332 24.629 12.797  1.00 86.77  ? 301 CIT A O5  1 
HETATM 2092 O O6  . CIT B 2 .   ? 27.574 24.377 14.019  1.00 86.90  ? 301 CIT A O6  1 
HETATM 2093 C C1  . UMU C 3 .   ? 20.942 10.944 13.164  1.00 31.77  ? 302 UMU A C1  1 
HETATM 2094 C C2  . UMU C 3 .   ? 20.763 12.040 12.466  1.00 31.39  ? 302 UMU A C2  1 
HETATM 2095 C C3  . UMU C 3 .   ? 21.820 12.777 12.118  1.00 29.77  ? 302 UMU A C3  1 
HETATM 2096 C C4  . UMU C 3 .   ? 18.917 11.165 12.861  1.00 32.33  ? 302 UMU A C4  1 
HETATM 2097 N N1  . UMU C 3 .   ? 22.987 12.402 12.421  1.00 29.53  ? 302 UMU A N1  1 
HETATM 2098 N N2  . UMU C 3 .   ? 22.134 10.602 13.453  1.00 31.13  ? 302 UMU A N2  1 
HETATM 2099 C C5  . UMU C 3 .   ? 17.218 8.290  9.092   1.00 37.48  ? 302 UMU A C5  1 
HETATM 2100 C C6  . UMU C 3 .   ? 23.115 11.332 13.094  1.00 30.86  ? 302 UMU A C6  1 
HETATM 2101 C C7  . UMU C 3 .   ? 16.923 9.296  8.044   1.00 37.42  ? 302 UMU A C7  1 
HETATM 2102 C C8  . UMU C 3 .   ? 15.650 9.920  8.524   1.00 37.56  ? 302 UMU A C8  1 
HETATM 2103 C C9  . UMU C 3 .   ? 15.756 9.551  9.958   1.00 37.90  ? 302 UMU A C9  1 
HETATM 2104 C C10 . UMU C 3 .   ? 14.539 9.412  10.738  1.00 40.38  ? 302 UMU A C10 1 
HETATM 2105 C C11 . UMU C 3 .   ? 14.885 3.978  10.368  1.00 41.29  ? 302 UMU A C11 1 
HETATM 2106 C C12 . UMU C 3 .   ? 16.307 3.989  10.800  1.00 40.52  ? 302 UMU A C12 1 
HETATM 2107 C C13 . UMU C 3 .   ? 16.655 5.649  12.492  1.00 38.56  ? 302 UMU A C13 1 
HETATM 2108 C C14 . UMU C 3 .   ? 17.076 7.394  14.031  1.00 36.82  ? 302 UMU A C14 1 
HETATM 2109 C C15 . UMU C 3 .   ? 18.497 7.371  14.217  1.00 36.01  ? 302 UMU A C15 1 
HETATM 2110 C C16 . UMU C 3 .   ? 19.666 9.207  14.131  1.00 34.86  ? 302 UMU A C16 1 
HETATM 2111 C C17 . UMU C 3 .   ? 18.751 9.322  15.309  1.00 35.68  ? 302 UMU A C17 1 
HETATM 2112 C C18 . UMU C 3 .   ? 18.589 7.890  15.582  1.00 35.75  ? 302 UMU A C18 1 
HETATM 2113 C C19 . UMU C 3 .   ? 17.540 10.997 12.857  1.00 36.00  ? 302 UMU A C19 1 
HETATM 2114 C C20 . UMU C 3 .   ? 16.393 10.783 12.896  1.00 38.76  ? 302 UMU A C20 1 
HETATM 2115 C C21 . UMU C 3 .   ? 15.007 10.386 13.000  1.00 40.05  ? 302 UMU A C21 1 
HETATM 2116 C C22 . UMU C 3 .   ? 16.366 6.512  7.775   1.00 34.48  ? 302 UMU A C22 1 
HETATM 2117 C C23 . UMU C 3 .   ? 17.922 5.159  7.739   1.00 34.03  ? 302 UMU A C23 1 
HETATM 2118 C C24 . UMU C 3 .   ? 18.292 6.235  8.449   1.00 34.32  ? 302 UMU A C24 1 
HETATM 2119 C C25 . UMU C 3 .   ? 20.260 5.286  8.809   1.00 32.49  ? 302 UMU A C25 1 
HETATM 2120 C C26 . UMU C 3 .   ? 18.806 4.155  7.574   1.00 32.60  ? 302 UMU A C26 1 
HETATM 2121 N N3  . UMU C 3 .   ? 21.693 13.846 11.447  1.00 30.13  ? 302 UMU A N3  1 
HETATM 2122 N N4  . UMU C 3 .   ? 19.506 12.156 12.323  1.00 32.48  ? 302 UMU A N4  1 
HETATM 2123 N N5  . UMU C 3 .   ? 19.810 10.405 13.386  1.00 32.43  ? 302 UMU A N5  1 
HETATM 2124 N N6  . UMU C 3 .   ? 16.568 5.327  11.266  1.00 39.48  ? 302 UMU A N6  1 
HETATM 2125 N N7  . UMU C 3 .   ? 16.904 6.886  12.728  1.00 38.12  ? 302 UMU A N7  1 
HETATM 2126 N N8  . UMU C 3 .   ? 17.302 7.054  8.455   1.00 34.87  ? 302 UMU A N8  1 
HETATM 2127 N N9  . UMU C 3 .   ? 16.730 5.367  7.333   1.00 34.39  ? 302 UMU A N9  1 
HETATM 2128 N N10 . UMU C 3 .   ? 19.472 6.274  8.988   1.00 32.84  ? 302 UMU A N10 1 
HETATM 2129 N N11 . UMU C 3 .   ? 19.946 4.251  8.142   1.00 32.32  ? 302 UMU A N11 1 
HETATM 2130 N N12 . UMU C 3 .   ? 18.537 3.109  6.889   1.00 32.43  ? 302 UMU A N12 1 
HETATM 2131 O O1  . UMU C 3 .   ? 17.957 10.235 8.020   1.00 37.15  ? 302 UMU A O1  1 
HETATM 2132 O O2  . UMU C 3 .   ? 15.747 11.282 8.338   1.00 37.74  ? 302 UMU A O2  1 
HETATM 2133 O O3  . UMU C 3 .   ? 16.078 8.275  9.807   1.00 38.51  ? 302 UMU A O3  1 
HETATM 2134 O O4  . UMU C 3 .   ? 14.386 10.433 11.707  1.00 44.35  ? 302 UMU A O4  1 
HETATM 2135 O O5  . UMU C 3 .   ? 16.534 4.836  13.354  1.00 39.40  ? 302 UMU A O5  1 
HETATM 2136 O O6  . UMU C 3 .   ? 18.922 8.369  13.398  1.00 35.08  ? 302 UMU A O6  1 
HETATM 2137 O O7  . UMU C 3 .   ? 19.281 9.912  16.437  1.00 35.80  ? 302 UMU A O7  1 
HETATM 2138 O O8  . UMU C 3 .   ? 19.738 7.372  16.106  1.00 37.27  ? 302 UMU A O8  1 
HETATM 2139 O O   . HOH D 4 .   ? 29.726 6.830  4.667   1.00 18.28  ? 401 HOH A O   1 
HETATM 2140 O O   . HOH D 4 .   ? 13.854 10.770 4.736   1.00 25.16  ? 402 HOH A O   1 
HETATM 2141 O O   . HOH D 4 .   ? 13.456 1.418  2.597   1.00 50.32  ? 403 HOH A O   1 
HETATM 2142 O O   . HOH D 4 .   ? 15.447 28.750 12.168  1.00 25.17  ? 404 HOH A O   1 
HETATM 2143 O O   . HOH D 4 .   ? 24.284 8.298  -8.926  1.00 24.54  ? 405 HOH A O   1 
HETATM 2144 O O   . HOH D 4 .   ? 22.979 11.402 0.477   1.00 31.47  ? 406 HOH A O   1 
HETATM 2145 O O   . HOH D 4 .   ? 10.424 5.943  -14.218 1.00 44.28  ? 407 HOH A O   1 
HETATM 2146 O O   . HOH D 4 .   ? 21.880 1.319  -13.124 1.00 35.60  ? 408 HOH A O   1 
HETATM 2147 O O   . HOH D 4 .   ? 24.483 5.080  10.004  1.00 35.39  ? 409 HOH A O   1 
HETATM 2148 O O   . HOH D 4 .   ? 16.223 30.942 7.240   1.00 39.96  ? 410 HOH A O   1 
HETATM 2149 O O   . HOH D 4 .   ? 20.797 11.378 4.770   1.00 28.51  ? 411 HOH A O   1 
HETATM 2150 O O   . HOH D 4 .   ? 1.176  7.377  -12.937 1.00 65.36  ? 412 HOH A O   1 
HETATM 2151 O O   . HOH D 4 .   ? 17.591 10.539 18.340  1.00 47.07  ? 413 HOH A O   1 
HETATM 2152 O O   . HOH D 4 .   ? 20.517 26.752 2.882   1.00 31.88  ? 414 HOH A O   1 
HETATM 2153 O O   . HOH D 4 .   ? 2.679  23.779 22.641  1.00 40.23  ? 415 HOH A O   1 
HETATM 2154 O O   . HOH D 4 .   ? 25.730 9.136  -6.657  1.00 25.01  ? 416 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 12.152 1.890  -5.725  1.00 45.83  ? 417 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 12.744 11.686 18.770  1.00 41.94  ? 418 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 26.191 6.722  -3.727  1.00 31.43  ? 419 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 23.568 7.588  10.922  1.00 25.46  ? 420 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 15.615 28.654 -1.870  1.00 55.49  ? 421 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 14.927 16.825 20.568  1.00 34.38  ? 422 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 27.044 21.806 -14.654 1.00 45.04  ? 423 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 20.625 8.046  10.834  1.00 31.46  ? 424 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 22.651 21.004 7.127   1.00 29.09  ? 425 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 13.521 19.042 0.744   1.00 37.19  ? 426 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 20.686 21.888 19.919  1.00 40.74  ? 427 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 7.822  31.819 41.964  1.00 38.69  ? 428 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 28.408 26.385 -2.415  1.00 44.09  ? 429 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 4.319  18.449 29.560  1.00 40.70  ? 430 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 10.419 4.111  -12.053 1.00 36.94  ? 431 HOH A O   1 
HETATM 2170 O O   . HOH D 4 .   ? 4.578  10.887 6.396   1.00 44.92  ? 432 HOH A O   1 
HETATM 2171 O O   . HOH D 4 .   ? 23.689 0.613  -1.750  1.00 49.85  ? 433 HOH A O   1 
HETATM 2172 O O   . HOH D 4 .   ? 30.063 26.935 0.706   1.00 45.34  ? 434 HOH A O   1 
HETATM 2173 O O   . HOH D 4 .   ? 18.583 20.328 -14.200 1.00 41.02  ? 435 HOH A O   1 
HETATM 2174 O O   . HOH D 4 .   ? 3.896  23.358 -1.489  1.00 51.86  ? 436 HOH A O   1 
HETATM 2175 O O   . HOH D 4 .   ? 30.024 4.622  -2.430  1.00 46.75  ? 437 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 31.755 3.825  -4.038  1.00 36.34  ? 438 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   ? 0.8445 0.5836 0.6396 0.1829  0.0245  -0.1230 1   MET A N   
2    C CA  . MET A 1   ? 0.8130 0.5628 0.6210 0.1798  0.0190  -0.1055 1   MET A CA  
3    C C   . MET A 1   ? 0.7809 0.5920 0.6170 0.1922  0.0115  -0.0949 1   MET A C   
4    O O   . MET A 1   ? 0.7534 0.6059 0.6059 0.1848  0.0086  -0.0990 1   MET A O   
5    C CB  . MET A 1   ? 0.7801 0.5317 0.5947 0.1466  0.0156  -0.1079 1   MET A CB  
6    C CG  . MET A 1   ? 0.7446 0.5095 0.5723 0.1416  0.0107  -0.0914 1   MET A CG  
7    S SD  . MET A 1   ? 0.7365 0.4862 0.5639 0.1056  0.0119  -0.0960 1   MET A SD  
8    C CE  . MET A 1   ? 0.6971 0.4921 0.5404 0.0884  0.0050  -0.1126 1   MET A CE  
9    N N   . LYS A 2   ? 0.7863 0.6026 0.6259 0.2108  0.0094  -0.0819 2   LYS A N   
10   C CA  . LYS A 2   ? 0.7299 0.6064 0.5974 0.2204  0.0035  -0.0756 2   LYS A CA  
11   C C   . LYS A 2   ? 0.6776 0.5868 0.5669 0.1948  -0.0024 -0.0714 2   LYS A C   
12   O O   . LYS A 2   ? 0.6711 0.5608 0.5559 0.1785  -0.0046 -0.0669 2   LYS A O   
13   C CB  . LYS A 2   ? 0.7283 0.6075 0.5928 0.2470  0.0009  -0.0650 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.7692 0.6264 0.6149 0.2809  0.0067  -0.0679 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.7697 0.6509 0.6179 0.3125  0.0014  -0.0576 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.8202 0.6871 0.6520 0.3516  0.0073  -0.0608 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.8275 0.7313 0.6641 0.3872  0.0000  -0.0518 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.6437 0.6005 0.5553 0.1918  -0.0028 -0.0731 3   TYR A N   
19   C CA  . TYR A 3   ? 0.5969 0.5799 0.5263 0.1705  -0.0057 -0.0692 3   TYR A CA  
20   C C   . TYR A 3   ? 0.5895 0.6213 0.5426 0.1733  -0.0032 -0.0688 3   TYR A C   
21   O O   . TYR A 3   ? 0.6249 0.6761 0.5824 0.1890  0.0011  -0.0737 3   TYR A O   
22   C CB  . TYR A 3   ? 0.5639 0.5381 0.4863 0.1538  -0.0046 -0.0746 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.5249 0.5208 0.4486 0.1582  0.0010  -0.0801 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.5463 0.5297 0.4553 0.1720  0.0056  -0.0894 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.4679 0.4927 0.4041 0.1492  0.0039  -0.0756 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.5252 0.5297 0.4332 0.1760  0.0122  -0.0943 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.4676 0.5088 0.4006 0.1529  0.0118  -0.0787 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.4862 0.5198 0.4055 0.1661  0.0155  -0.0881 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.4838 0.5350 0.3978 0.1698  0.0246  -0.0911 3   TYR A OH  
30   N N   . MET A 4   ? 0.5447 0.5959 0.5132 0.1568  -0.0042 -0.0643 4   MET A N   
31   C CA  . MET A 4   ? 0.5056 0.5967 0.4951 0.1512  0.0021  -0.0657 4   MET A CA  
32   C C   . MET A 4   ? 0.4761 0.5640 0.4682 0.1314  0.0052  -0.0613 4   MET A C   
33   O O   . MET A 4   ? 0.4771 0.5428 0.4608 0.1237  -0.0002 -0.0573 4   MET A O   
34   C CB  . MET A 4   ? 0.4965 0.6211 0.5049 0.1564  -0.0011 -0.0668 4   MET A CB  
35   C CG  . MET A 4   ? 0.4890 0.6112 0.5018 0.1444  -0.0071 -0.0620 4   MET A CG  
36   S SD  . MET A 4   ? 0.4916 0.6369 0.5246 0.1195  0.0011  -0.0639 4   MET A SD  
37   C CE  . MET A 4   ? 0.4822 0.6745 0.5362 0.1213  0.0117  -0.0741 4   MET A CE  
38   N N   . ILE A 5   ? 0.4826 0.5921 0.4852 0.1239  0.0157  -0.0620 5   ILE A N   
39   C CA  . ILE A 5   ? 0.4942 0.5958 0.4950 0.1091  0.0219  -0.0560 5   ILE A CA  
40   C C   . ILE A 5   ? 0.5204 0.6460 0.5412 0.0966  0.0322  -0.0581 5   ILE A C   
41   O O   . ILE A 5   ? 0.5234 0.6752 0.5556 0.0965  0.0415  -0.0643 5   ILE A O   
42   C CB  . ILE A 5   ? 0.4941 0.5849 0.4768 0.1116  0.0290  -0.0534 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.4949 0.5673 0.4591 0.1215  0.0193  -0.0567 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.4827 0.5606 0.4581 0.1023  0.0348  -0.0444 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.5089 0.5766 0.4528 0.1257  0.0240  -0.0567 5   ILE A CD1 
46   N N   . THR A 6   ? 0.5433 0.6615 0.5690 0.0847  0.0316  -0.0552 6   THR A N   
47   C CA  . THR A 6   ? 0.5531 0.6855 0.5944 0.0681  0.0437  -0.0591 6   THR A CA  
48   C C   . THR A 6   ? 0.5648 0.6679 0.5918 0.0596  0.0568  -0.0503 6   THR A C   
49   O O   . THR A 6   ? 0.5830 0.6614 0.5925 0.0670  0.0510  -0.0415 6   THR A O   
50   C CB  . THR A 6   ? 0.5633 0.7066 0.6176 0.0615  0.0353  -0.0641 6   THR A CB  
51   O OG1 . THR A 6   ? 0.5998 0.7581 0.6697 0.0423  0.0485  -0.0721 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.5580 0.6712 0.5991 0.0621  0.0275  -0.0559 6   THR A CG2 
53   N N   . SER A 7   ? 0.5525 0.6594 0.5862 0.0446  0.0757  -0.0531 7   SER A N   
54   C CA  . SER A 7   ? 0.5826 0.6555 0.5966 0.0398  0.0928  -0.0425 7   SER A CA  
55   C C   . SER A 7   ? 0.6278 0.6909 0.6508 0.0184  0.1093  -0.0472 7   SER A C   
56   O O   . SER A 7   ? 0.6281 0.7219 0.6755 0.0027  0.1131  -0.0621 7   SER A O   
57   C CB  . SER A 7   ? 0.6016 0.6753 0.6034 0.0431  0.1071  -0.0388 7   SER A CB  
58   O OG  . SER A 7   ? 0.6434 0.6911 0.6329 0.0301  0.1322  -0.0325 7   SER A OG  
59   N N   . LYS A 8   ? 0.6775 0.6982 0.6792 0.0188  0.1197  -0.0357 8   LYS A N   
60   C CA  . LYS A 8   ? 0.7356 0.7336 0.7393 -0.0013 0.1395  -0.0398 8   LYS A CA  
61   C C   . LYS A 8   ? 0.8015 0.8068 0.8134 -0.0234 0.1647  -0.0482 8   LYS A C   
62   O O   . LYS A 8   ? 0.7961 0.8023 0.8226 -0.0482 0.1791  -0.0618 8   LYS A O   
63   C CB  . LYS A 8   ? 0.7651 0.7106 0.7380 0.0101  0.1483  -0.0227 8   LYS A CB  
64   C CG  . LYS A 8   ? 0.8017 0.7083 0.7684 -0.0082 0.1731  -0.0250 8   LYS A CG  
65   C CD  . LYS A 8   ? 0.8543 0.7080 0.7867 0.0113  0.1809  -0.0056 8   LYS A CD  
66   C CE  . LYS A 8   ? 0.9229 0.7275 0.8446 -0.0056 0.2090  -0.0078 8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.8990 0.7225 0.8484 -0.0249 0.2026  -0.0286 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.8770 0.8902 0.8804 -0.0171 0.1714  -0.0427 9   GLY A N   
69   C CA  . GLY A 9   ? 0.9126 0.9368 0.9242 -0.0387 0.1973  -0.0507 9   GLY A CA  
70   C C   . GLY A 9   ? 0.9665 0.9363 0.9429 -0.0419 0.2270  -0.0341 9   GLY A C   
71   O O   . GLY A 9   ? 1.0040 0.9795 0.9821 -0.0593 0.2516  -0.0383 9   GLY A O   
72   N N   . ASP A 10  ? 0.9343 0.8528 0.8775 -0.0243 0.2265  -0.0152 10  ASP A N   
73   C CA  . ASP A 10  ? 0.9543 0.8170 0.8561 -0.0201 0.2539  0.0045  10  ASP A CA  
74   C C   . ASP A 10  ? 0.9431 0.8156 0.8221 0.0032  0.2481  0.0178  10  ASP A C   
75   O O   . ASP A 10  ? 0.9163 0.8335 0.8111 0.0160  0.2227  0.0110  10  ASP A O   
76   C CB  . ASP A 10  ? 0.9669 0.7740 0.8404 -0.0052 0.2556  0.0198  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.9291 0.7478 0.7929 0.0287  0.2240  0.0302  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.9678 0.7479 0.7946 0.0529  0.2274  0.0504  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.8742 0.7415 0.7664 0.0314  0.1966  0.0179  10  ASP A OD2 
80   N N   . GLU A 11  ? 0.9675 0.7940 0.8051 0.0091  0.2736  0.0369  11  GLU A N   
81   C CA  . GLU A 11  ? 0.9517 0.7882 0.7644 0.0276  0.2733  0.0478  11  GLU A CA  
82   C C   . GLU A 11  ? 0.9198 0.7740 0.7218 0.0611  0.2389  0.0541  11  GLU A C   
83   O O   . GLU A 11  ? 0.8976 0.7909 0.7064 0.0703  0.2231  0.0474  11  GLU A O   
84   C CB  . GLU A 11  ? 1.0095 0.7864 0.7723 0.0301  0.3085  0.0701  11  GLU A CB  
85   C CG  . GLU A 11  ? 0.9994 0.7845 0.7300 0.0501  0.3104  0.0824  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.0686 0.7962 0.7506 0.0471  0.3511  0.1034  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.0961 0.7963 0.7854 0.0147  0.3841  0.0986  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.0975 0.8069 0.7318 0.0766  0.3510  0.1242  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.9326 0.7598 0.7185 0.0788  0.2281  0.0652  12  LYS A N   
90   C CA  . LYS A 12  ? 0.9067 0.7537 0.6821 0.1082  0.1977  0.0697  12  LYS A CA  
91   C C   . LYS A 12  ? 0.8343 0.7327 0.6504 0.1030  0.1687  0.0491  12  LYS A C   
92   O O   . LYS A 12  ? 0.8118 0.7372 0.6238 0.1180  0.1491  0.0459  12  LYS A O   
93   C CB  . LYS A 12  ? 0.9213 0.7362 0.6771 0.1272  0.1932  0.0833  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.9025 0.7450 0.6502 0.1558  0.1628  0.0857  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.9345 0.7517 0.6657 0.1764  0.1598  0.0982  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.9295 0.7837 0.6546 0.2036  0.1303  0.0982  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.9588 0.7968 0.6700 0.2273  0.1270  0.1097  12  LYS A NZ  
98   N N   . SER A 13  ? 0.8077 0.7181 0.6601 0.0820  0.1667  0.0347  13  SER A N   
99   C CA  . SER A 13  ? 0.7435 0.6950 0.6288 0.0800  0.1407  0.0183  13  SER A CA  
100  C C   . SER A 13  ? 0.7185 0.7048 0.6192 0.0746  0.1400  0.0064  13  SER A C   
101  O O   . SER A 13  ? 0.6870 0.6972 0.5932 0.0858  0.1198  -0.0004 13  SER A O   
102  C CB  . SER A 13  ? 0.7182 0.6720 0.6322 0.0628  0.1385  0.0080  13  SER A CB  
103  O OG  . SER A 13  ? 0.7413 0.6611 0.6403 0.0692  0.1414  0.0181  13  SER A OG  
104  N N   . ASP A 14  ? 0.7370 0.7266 0.6451 0.0570  0.1635  0.0024  14  ASP A N   
105  C CA  . ASP A 14  ? 0.7227 0.7505 0.6469 0.0540  0.1648  -0.0096 14  ASP A CA  
106  C C   . ASP A 14  ? 0.7118 0.7399 0.6077 0.0748  0.1603  -0.0028 14  ASP A C   
107  O O   . ASP A 14  ? 0.6696 0.7266 0.5757 0.0839  0.1459  -0.0134 14  ASP A O   
108  C CB  . ASP A 14  ? 0.7758 0.8097 0.7117 0.0296  0.1945  -0.0153 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.7873 0.8436 0.7614 0.0069  0.1947  -0.0317 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.7655 0.8340 0.7556 0.0129  0.1709  -0.0375 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.8242 0.8873 0.8114 -0.0183 0.2195  -0.0400 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.7563 0.7508 0.6132 0.0843  0.1728  0.0146  15  LEU A N   
113  C CA  . LEU A 15  ? 0.7754 0.7730 0.6013 0.1047  0.1680  0.0202  15  LEU A CA  
114  C C   . LEU A 15  ? 0.7244 0.7344 0.5500 0.1219  0.1367  0.0150  15  LEU A C   
115  O O   . LEU A 15  ? 0.7098 0.7397 0.5305 0.1319  0.1259  0.0061  15  LEU A O   
116  C CB  . LEU A 15  ? 0.8435 0.8023 0.6234 0.1140  0.1881  0.0419  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.8974 0.8356 0.6695 0.0949  0.2250  0.0483  15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.9685 0.8582 0.6861 0.1091  0.2451  0.0738  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.8953 0.8701 0.6818 0.0863  0.2348  0.0351  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.7070 0.7048 0.5374 0.1240  0.1236  0.0188  16  LEU A N   
121  C CA  . LEU A 16  ? 0.6899 0.7022 0.5240 0.1352  0.0962  0.0116  16  LEU A CA  
122  C C   . LEU A 16  ? 0.6480 0.6845 0.5123 0.1278  0.0833  -0.0065 16  LEU A C   
123  O O   . LEU A 16  ? 0.6528 0.7004 0.5135 0.1361  0.0671  -0.0158 16  LEU A O   
124  C CB  . LEU A 16  ? 0.6925 0.6911 0.5302 0.1369  0.0877  0.0181  16  LEU A CB  
125  C CG  . LEU A 16  ? 0.6860 0.7015 0.5283 0.1455  0.0620  0.0104  16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.7005 0.7272 0.5127 0.1634  0.0541  0.0116  16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.6798 0.6858 0.5288 0.1467  0.0568  0.0164  16  LEU A CD2 
128  N N   . ARG A 17  ? 0.5993 0.6437 0.4915 0.1131  0.0913  -0.0124 17  ARG A N   
129  C CA  . ARG A 17  ? 0.5528 0.6198 0.4699 0.1115  0.0798  -0.0272 17  ARG A CA  
130  C C   . ARG A 17  ? 0.5652 0.6471 0.4744 0.1206  0.0832  -0.0349 17  ARG A C   
131  O O   . ARG A 17  ? 0.5623 0.6505 0.4742 0.1290  0.0696  -0.0452 17  ARG A O   
132  C CB  . ARG A 17  ? 0.5383 0.6190 0.4859 0.0963  0.0868  -0.0326 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.5141 0.6213 0.4846 0.0998  0.0761  -0.0459 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.4832 0.6115 0.4832 0.0862  0.0795  -0.0523 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.4568 0.6153 0.4757 0.0951  0.0698  -0.0636 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.4602 0.6509 0.4913 0.0991  0.0782  -0.0723 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.4620 0.6579 0.4885 0.0912  0.0981  -0.0715 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.4659 0.6836 0.5122 0.1127  0.0680  -0.0814 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.5787 0.6626 0.4754 0.1190  0.1034  -0.0302 18  LEU A N   
140  C CA  . LEU A 18  ? 0.5894 0.6894 0.4773 0.1283  0.1089  -0.0381 18  LEU A CA  
141  C C   . LEU A 18  ? 0.6119 0.7020 0.4695 0.1438  0.0961  -0.0393 18  LEU A C   
142  O O   . LEU A 18  ? 0.6207 0.7205 0.4758 0.1530  0.0902  -0.0521 18  LEU A O   
143  C CB  . LEU A 18  ? 0.6030 0.7068 0.4822 0.1207  0.1364  -0.0319 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.5765 0.7016 0.4892 0.1017  0.1524  -0.0377 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.6092 0.7362 0.5097 0.0919  0.1829  -0.0327 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.5308 0.6932 0.4759 0.1067  0.1411  -0.0551 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.6208 0.6933 0.4545 0.1477  0.0920  -0.0278 19  ASN A N   
148  C CA  . ASN A 19  ? 0.6244 0.6967 0.4305 0.1612  0.0784  -0.0317 19  ASN A CA  
149  C C   . ASN A 19  ? 0.5894 0.6645 0.4101 0.1606  0.0570  -0.0470 19  ASN A C   
150  O O   . ASN A 19  ? 0.5942 0.6735 0.4019 0.1672  0.0493  -0.0605 19  ASN A O   
151  C CB  . ASN A 19  ? 0.6643 0.7245 0.4439 0.1686  0.0774  -0.0158 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.7262 0.7815 0.4678 0.1793  0.0944  -0.0040 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.7570 0.8197 0.4937 0.1785  0.1082  -0.0087 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.7579 0.8013 0.4704 0.1915  0.0944  0.0122  19  ASN A ND2 
155  N N   . MET A 20  ? 0.5663 0.6363 0.4117 0.1515  0.0489  -0.0457 20  MET A N   
156  C CA  . MET A 20  ? 0.5608 0.6278 0.4177 0.1490  0.0321  -0.0584 20  MET A CA  
157  C C   . MET A 20  ? 0.5720 0.6398 0.4388 0.1521  0.0340  -0.0708 20  MET A C   
158  O O   . MET A 20  ? 0.5932 0.6521 0.4523 0.1551  0.0255  -0.0840 20  MET A O   
159  C CB  . MET A 20  ? 0.5584 0.6197 0.4364 0.1395  0.0256  -0.0525 20  MET A CB  
160  C CG  . MET A 20  ? 0.5951 0.6548 0.4638 0.1402  0.0237  -0.0408 20  MET A CG  
161  S SD  . MET A 20  ? 0.6000 0.6541 0.4927 0.1297  0.0165  -0.0368 20  MET A SD  
162  C CE  . MET A 20  ? 0.5827 0.6379 0.4804 0.1251  -0.0007 -0.0526 20  MET A CE  
163  N N   . ILE A 21  ? 0.5780 0.6569 0.4616 0.1516  0.0460  -0.0679 21  ILE A N   
164  C CA  . ILE A 21  ? 0.5777 0.6637 0.4704 0.1601  0.0485  -0.0791 21  ILE A CA  
165  C C   . ILE A 21  ? 0.6073 0.6926 0.4759 0.1712  0.0527  -0.0890 21  ILE A C   
166  O O   . ILE A 21  ? 0.6333 0.7082 0.4971 0.1803  0.0482  -0.1018 21  ILE A O   
167  C CB  . ILE A 21  ? 0.5532 0.6644 0.4708 0.1572  0.0612  -0.0762 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.5370 0.6503 0.4785 0.1472  0.0548  -0.0713 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.5544 0.6820 0.4797 0.1715  0.0652  -0.0880 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.5209 0.6647 0.4885 0.1395  0.0669  -0.0715 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.6171 0.7099 0.4666 0.1715  0.0627  -0.0832 22  ALA A N   
172  C CA  . ALA A 22  ? 0.6447 0.7382 0.4663 0.1819  0.0659  -0.0931 22  ALA A CA  
173  C C   . ALA A 22  ? 0.6650 0.7430 0.4684 0.1822  0.0493  -0.1040 22  ALA A C   
174  O O   . ALA A 22  ? 0.6897 0.7609 0.4782 0.1890  0.0477  -0.1207 22  ALA A O   
175  C CB  . ALA A 22  ? 0.6532 0.7562 0.4531 0.1827  0.0807  -0.0814 22  ALA A CB  
176  N N   . GLY A 23  ? 0.6482 0.7216 0.4532 0.1738  0.0379  -0.0970 23  GLY A N   
177  C CA  . GLY A 23  ? 0.6510 0.7172 0.4444 0.1700  0.0225  -0.1101 23  GLY A CA  
178  C C   . GLY A 23  ? 0.6535 0.6979 0.4594 0.1654  0.0169  -0.1238 23  GLY A C   
179  O O   . GLY A 23  ? 0.6915 0.7238 0.4824 0.1638  0.0121  -0.1423 23  GLY A O   
180  N N   . PHE A 24  ? 0.6215 0.6583 0.4520 0.1633  0.0185  -0.1153 24  PHE A N   
181  C CA  . PHE A 24  ? 0.6009 0.6118 0.4380 0.1632  0.0154  -0.1243 24  PHE A CA  
182  C C   . PHE A 24  ? 0.6212 0.6213 0.4473 0.1780  0.0237  -0.1367 24  PHE A C   
183  O O   . PHE A 24  ? 0.6324 0.6010 0.4516 0.1805  0.0226  -0.1475 24  PHE A O   
184  C CB  . PHE A 24  ? 0.5564 0.5677 0.4190 0.1616  0.0149  -0.1112 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.5229 0.5324 0.3950 0.1471  0.0060  -0.1036 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.4756 0.5024 0.3645 0.1427  0.0073  -0.0891 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.5153 0.5061 0.3797 0.1365  -0.0019 -0.1130 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.4588 0.4843 0.3558 0.1316  0.0001  -0.0830 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.5990 0.5935 0.4740 0.1235  -0.0090 -0.1072 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.4677 0.4796 0.3585 0.1229  -0.0084 -0.0917 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.6421 0.6649 0.4647 0.1883  0.0341  -0.1351 25  GLY A N   
192  C CA  . GLY A 25  ? 0.6948 0.7119 0.5060 0.2043  0.0430  -0.1483 25  GLY A CA  
193  C C   . GLY A 25  ? 0.7558 0.7509 0.5376 0.2035  0.0407  -0.1684 25  GLY A C   
194  O O   . GLY A 25  ? 0.7862 0.7653 0.5558 0.2170  0.0480  -0.1824 25  GLY A O   
195  N N   . GLU A 26  ? 0.7784 0.7747 0.5487 0.1885  0.0308  -0.1720 26  GLU A N   
196  C CA  . GLU A 26  ? 0.8205 0.8025 0.5646 0.1829  0.0269  -0.1950 26  GLU A CA  
197  C C   . GLU A 26  ? 0.8153 0.7595 0.5606 0.1690  0.0210  -0.2071 26  GLU A C   
198  O O   . GLU A 26  ? 0.8142 0.7486 0.5417 0.1566  0.0168  -0.2284 26  GLU A O   
199  C CB  . GLU A 26  ? 0.8307 0.8448 0.5605 0.1758  0.0189  -0.1948 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.8214 0.8667 0.5480 0.1868  0.0265  -0.1760 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.8426 0.8924 0.5521 0.2019  0.0408  -0.1834 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.8401 0.9095 0.5522 0.2096  0.0526  -0.1676 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 0.8663 0.8990 0.5593 0.2051  0.0421  -0.2061 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.8078 0.7313 0.5720 0.1697  0.0216  -0.1949 27  TYR A N   
205  C CA  . TYR A 27  ? 0.8291 0.7109 0.5916 0.1565  0.0196  -0.2027 27  TYR A CA  
206  C C   . TYR A 27  ? 0.8860 0.7328 0.6518 0.1738  0.0278  -0.1951 27  TYR A C   
207  O O   . TYR A 27  ? 0.8861 0.7499 0.6599 0.1952  0.0331  -0.1859 27  TYR A O   
208  C CB  . TYR A 27  ? 0.7624 0.6590 0.5428 0.1371  0.0092  -0.1922 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.7279 0.6610 0.5046 0.1233  -0.0006 -0.2001 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.7548 0.6802 0.5187 0.1045  -0.0044 -0.2245 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.6836 0.6592 0.4683 0.1296  -0.0051 -0.1839 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.7385 0.7072 0.4999 0.0950  -0.0155 -0.2330 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.6812 0.6911 0.4589 0.1231  -0.0147 -0.1891 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.7153 0.7264 0.4825 0.1071  -0.0213 -0.2139 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.7374 0.7924 0.4985 0.1036  -0.0329 -0.2204 27  TYR A OH  
216  N N   . ASP A 28  ? 0.9385 0.7377 0.6971 0.1648  0.0296  -0.1990 28  ASP A N   
217  C CA  . ASP A 28  ? 0.9589 0.7205 0.7156 0.1838  0.0365  -0.1885 28  ASP A CA  
218  C C   . ASP A 28  ? 0.9232 0.7100 0.7057 0.1846  0.0293  -0.1647 28  ASP A C   
219  O O   . ASP A 28  ? 0.9394 0.6967 0.7210 0.1785  0.0290  -0.1566 28  ASP A O   
220  C CB  . ASP A 28  ? 1.0088 0.7004 0.7403 0.1740  0.0448  -0.2012 28  ASP A CB  
221  N N   . MET A 29  ? 0.8873 0.7282 0.6910 0.1911  0.0253  -0.1543 29  MET A N   
222  C CA  . MET A 29  ? 0.8430 0.7140 0.6722 0.1911  0.0196  -0.1351 29  MET A CA  
223  C C   . MET A 29  ? 0.8531 0.7529 0.6958 0.2159  0.0238  -0.1283 29  MET A C   
224  O O   . MET A 29  ? 0.8755 0.7984 0.7176 0.2254  0.0297  -0.1350 29  MET A O   
225  C CB  . MET A 29  ? 0.8003 0.7105 0.6441 0.1722  0.0130  -0.1298 29  MET A CB  
226  C CG  . MET A 29  ? 0.8172 0.7143 0.6553 0.1486  0.0067  -0.1356 29  MET A CG  
227  S SD  . MET A 29  ? 0.8289 0.6978 0.6736 0.1386  0.0041  -0.1257 29  MET A SD  
228  C CE  . MET A 29  ? 0.8112 0.6974 0.6620 0.1104  -0.0037 -0.1311 29  MET A CE  
229  N N   . GLU A 30  ? 0.8331 0.7360 0.6878 0.2260  0.0210  -0.1162 30  GLU A N   
230  C CA  . GLU A 30  ? 0.8036 0.7438 0.6757 0.2490  0.0231  -0.1115 30  GLU A CA  
231  C C   . GLU A 30  ? 0.7358 0.7189 0.6361 0.2380  0.0171  -0.0998 30  GLU A C   
232  O O   . GLU A 30  ? 0.7466 0.7151 0.6476 0.2287  0.0105  -0.0914 30  GLU A O   
233  C CB  . GLU A 30  ? 0.8420 0.7505 0.6994 0.2779  0.0250  -0.1099 30  GLU A CB  
234  C CG  . GLU A 30  ? 0.8350 0.7928 0.7137 0.3043  0.0242  -0.1055 30  GLU A CG  
235  C CD  . GLU A 30  ? 0.8929 0.8192 0.7531 0.3383  0.0245  -0.1007 30  GLU A CD  
236  O OE1 . GLU A 30  ? 0.9433 0.8013 0.7702 0.3433  0.0301  -0.1032 30  GLU A OE1 
237  O OE2 . GLU A 30  ? 0.8913 0.8611 0.7689 0.3602  0.0198  -0.0950 30  GLU A OE2 
238  N N   . TYR A 31  ? 0.6796 0.7135 0.6018 0.2375  0.0212  -0.1006 31  TYR A N   
239  C CA  . TYR A 31  ? 0.6156 0.6892 0.5646 0.2250  0.0183  -0.0929 31  TYR A CA  
240  C C   . TYR A 31  ? 0.6143 0.7114 0.5767 0.2450  0.0137  -0.0906 31  TYR A C   
241  O O   . TYR A 31  ? 0.6086 0.7333 0.5784 0.2673  0.0177  -0.0967 31  TYR A O   
242  C CB  . TYR A 31  ? 0.5827 0.6971 0.5478 0.2140  0.0280  -0.0954 31  TYR A CB  
243  C CG  . TYR A 31  ? 0.5616 0.7043 0.5496 0.1942  0.0280  -0.0891 31  TYR A CG  
244  C CD1 . TYR A 31  ? 0.5533 0.7380 0.5669 0.1981  0.0271  -0.0910 31  TYR A CD1 
245  C CD2 . TYR A 31  ? 0.5651 0.6934 0.5478 0.1728  0.0290  -0.0828 31  TYR A CD2 
246  C CE1 . TYR A 31  ? 0.5412 0.7489 0.5744 0.1774  0.0285  -0.0886 31  TYR A CE1 
247  C CE2 . TYR A 31  ? 0.5540 0.7003 0.5544 0.1556  0.0313  -0.0779 31  TYR A CE2 
248  C CZ  . TYR A 31  ? 0.5496 0.7335 0.5751 0.1561  0.0316  -0.0818 31  TYR A CZ  
249  O OH  . TYR A 31  ? 0.5525 0.7521 0.5946 0.1363  0.0353  -0.0803 31  TYR A OH  
250  N N   . ASP A 32  ? 0.6145 0.7051 0.5796 0.2387  0.0050  -0.0824 32  ASP A N   
251  C CA  . ASP A 32  ? 0.6343 0.7522 0.6098 0.2576  -0.0016 -0.0793 32  ASP A CA  
252  C C   . ASP A 32  ? 0.6246 0.7588 0.6143 0.2364  -0.0079 -0.0737 32  ASP A C   
253  O O   . ASP A 32  ? 0.6388 0.7337 0.6130 0.2252  -0.0120 -0.0663 32  ASP A O   
254  C CB  . ASP A 32  ? 0.6884 0.7588 0.6344 0.2841  -0.0050 -0.0738 32  ASP A CB  
255  C CG  . ASP A 32  ? 0.7221 0.8223 0.6734 0.3102  -0.0131 -0.0687 32  ASP A CG  
256  O OD1 . ASP A 32  ? 0.7055 0.8721 0.6876 0.3072  -0.0167 -0.0735 32  ASP A OD1 
257  O OD2 . ASP A 32  ? 0.7732 0.8301 0.6958 0.3337  -0.0150 -0.0604 32  ASP A OD2 
258  N N   . ASP A 33  ? 0.6020 0.7946 0.6214 0.2290  -0.0072 -0.0792 33  ASP A N   
259  C CA  . ASP A 33  ? 0.6015 0.8115 0.6344 0.2093  -0.0120 -0.0770 33  ASP A CA  
260  C C   . ASP A 33  ? 0.6007 0.8349 0.6353 0.2280  -0.0233 -0.0753 33  ASP A C   
261  O O   . ASP A 33  ? 0.5841 0.8388 0.6297 0.2135  -0.0279 -0.0759 33  ASP A O   
262  C CB  . ASP A 33  ? 0.5763 0.8305 0.6378 0.1858  -0.0026 -0.0858 33  ASP A CB  
263  C CG  . ASP A 33  ? 0.5775 0.8922 0.6631 0.1976  0.0022  -0.0979 33  ASP A CG  
264  O OD1 . ASP A 33  ? 0.6008 0.9310 0.6834 0.2279  -0.0047 -0.0993 33  ASP A OD1 
265  O OD2 . ASP A 33  ? 0.5699 0.9163 0.6767 0.1769  0.0144  -0.1062 33  ASP A OD2 
266  N N   . VAL A 34  ? 0.6223 0.8541 0.6436 0.2618  -0.0274 -0.0733 34  VAL A N   
267  C CA  . VAL A 34  ? 0.6426 0.8918 0.6568 0.2862  -0.0389 -0.0684 34  VAL A CA  
268  C C   . VAL A 34  ? 0.6876 0.8674 0.6645 0.2908  -0.0421 -0.0529 34  VAL A C   
269  O O   . VAL A 34  ? 0.7080 0.8904 0.6798 0.2858  -0.0490 -0.0471 34  VAL A O   
270  C CB  . VAL A 34  ? 0.6694 0.9533 0.6860 0.3260  -0.0411 -0.0726 34  VAL A CB  
271  C CG1 . VAL A 34  ? 0.6736 0.9823 0.6807 0.3558  -0.0544 -0.0666 34  VAL A CG1 
272  C CG2 . VAL A 34  ? 0.6436 1.0000 0.6998 0.3175  -0.0351 -0.0898 34  VAL A CG2 
273  N N   . GLU A 35  ? 0.7185 0.8356 0.6682 0.2984  -0.0353 -0.0477 35  GLU A N   
274  C CA  . GLU A 35  ? 0.7495 0.7947 0.6635 0.2964  -0.0337 -0.0352 35  GLU A CA  
275  C C   . GLU A 35  ? 0.7197 0.7193 0.6272 0.2688  -0.0252 -0.0386 35  GLU A C   
276  O O   . GLU A 35  ? 0.7415 0.6875 0.6236 0.2764  -0.0182 -0.0383 35  GLU A O   
277  C CB  . GLU A 35  ? 0.8420 0.8476 0.7216 0.3358  -0.0324 -0.0262 35  GLU A CB  
278  C CG  . GLU A 35  ? 0.8899 0.9454 0.7724 0.3710  -0.0426 -0.0223 35  GLU A CG  
279  C CD  . GLU A 35  ? 0.9947 1.0021 0.8366 0.4154  -0.0398 -0.0105 35  GLU A CD  
280  O OE1 . GLU A 35  ? 1.0416 1.0206 0.8531 0.4269  -0.0423 0.0047  35  GLU A OE1 
281  O OE2 . GLU A 35  ? 1.0340 1.0288 0.8714 0.4270  -0.0325 -0.0160 35  GLU A OE2 
282  N N   . PRO A 36  ? 0.6656 0.6851 0.5942 0.2374  -0.0252 -0.0429 36  PRO A N   
283  C CA  . PRO A 36  ? 0.6476 0.6306 0.5689 0.2140  -0.0194 -0.0459 36  PRO A CA  
284  C C   . PRO A 36  ? 0.6595 0.5941 0.5590 0.2019  -0.0187 -0.0385 36  PRO A C   
285  O O   . PRO A 36  ? 0.7093 0.6426 0.6025 0.2054  -0.0224 -0.0297 36  PRO A O   
286  C CB  . PRO A 36  ? 0.6019 0.6256 0.5510 0.1906  -0.0194 -0.0507 36  PRO A CB  
287  C CG  . PRO A 36  ? 0.5875 0.6499 0.5529 0.1910  -0.0252 -0.0483 36  PRO A CG  
288  C CD  . PRO A 36  ? 0.6187 0.6939 0.5771 0.2223  -0.0296 -0.0464 36  PRO A CD  
289  N N   . GLU A 37  ? 0.6384 0.5360 0.5259 0.1867  -0.0131 -0.0436 37  GLU A N   
290  C CA  . GLU A 37  ? 0.6379 0.4979 0.5113 0.1670  -0.0103 -0.0407 37  GLU A CA  
291  C C   . GLU A 37  ? 0.5861 0.4680 0.4783 0.1395  -0.0122 -0.0461 37  GLU A C   
292  O O   . GLU A 37  ? 0.5798 0.4503 0.4700 0.1222  -0.0115 -0.0435 37  GLU A O   
293  C CB  . GLU A 37  ? 0.6958 0.4954 0.5395 0.1685  -0.0010 -0.0451 37  GLU A CB  
294  C CG  . GLU A 37  ? 0.7513 0.5239 0.5726 0.2020  0.0026  -0.0399 37  GLU A CG  
295  C CD  . GLU A 37  ? 0.8227 0.5209 0.6081 0.2027  0.0153  -0.0430 37  GLU A CD  
296  O OE1 . GLU A 37  ? 0.8274 0.5043 0.6103 0.1748  0.0207  -0.0545 37  GLU A OE1 
297  O OE2 . GLU A 37  ? 0.8682 0.5290 0.6266 0.2316  0.0207  -0.0346 37  GLU A OE2 
298  N N   . ILE A 38  ? 0.5585 0.4716 0.4670 0.1372  -0.0136 -0.0529 38  ILE A N   
299  C CA  . ILE A 38  ? 0.5317 0.4694 0.4561 0.1186  -0.0156 -0.0554 38  ILE A CA  
300  C C   . ILE A 38  ? 0.5079 0.4867 0.4531 0.1226  -0.0167 -0.0525 38  ILE A C   
301  O O   . ILE A 38  ? 0.5042 0.4988 0.4534 0.1348  -0.0143 -0.0554 38  ILE A O   
302  C CB  . ILE A 38  ? 0.5480 0.4797 0.4659 0.1114  -0.0140 -0.0659 38  ILE A CB  
303  C CG1 . ILE A 38  ? 0.5887 0.4792 0.4870 0.1025  -0.0108 -0.0731 38  ILE A CG1 
304  C CG2 . ILE A 38  ? 0.5247 0.4843 0.4559 0.0986  -0.0168 -0.0661 38  ILE A CG2 
305  C CD1 . ILE A 38  ? 0.5805 0.4621 0.4804 0.0848  -0.0108 -0.0700 38  ILE A CD1 
306  N N   . VAL A 39  ? 0.4877 0.4831 0.4458 0.1113  -0.0184 -0.0483 39  VAL A N   
307  C CA  . VAL A 39  ? 0.4437 0.4718 0.4202 0.1092  -0.0163 -0.0475 39  VAL A CA  
308  C C   . VAL A 39  ? 0.4498 0.4812 0.4301 0.0973  -0.0136 -0.0469 39  VAL A C   
309  O O   . VAL A 39  ? 0.4508 0.4757 0.4309 0.0881  -0.0158 -0.0448 39  VAL A O   
310  C CB  . VAL A 39  ? 0.4017 0.4449 0.3875 0.1081  -0.0190 -0.0447 39  VAL A CB  
311  C CG1 . VAL A 39  ? 0.3774 0.4474 0.3816 0.0979  -0.0142 -0.0468 39  VAL A CG1 
312  C CG2 . VAL A 39  ? 0.4153 0.4669 0.3980 0.1262  -0.0223 -0.0449 39  VAL A CG2 
313  N N   . ILE A 40  ? 0.4500 0.4922 0.4319 0.0994  -0.0079 -0.0481 40  ILE A N   
314  C CA  . ILE A 40  ? 0.4511 0.4943 0.4305 0.0940  -0.0043 -0.0450 40  ILE A CA  
315  C C   . ILE A 40  ? 0.4363 0.4915 0.4271 0.0887  0.0050  -0.0416 40  ILE A C   
316  O O   . ILE A 40  ? 0.4506 0.5195 0.4486 0.0897  0.0118  -0.0443 40  ILE A O   
317  C CB  . ILE A 40  ? 0.4639 0.5051 0.4294 0.1008  -0.0026 -0.0478 40  ILE A CB  
318  C CG1 . ILE A 40  ? 0.4895 0.5159 0.4434 0.1025  -0.0099 -0.0552 40  ILE A CG1 
319  C CG2 . ILE A 40  ? 0.4541 0.4975 0.4120 0.1003  0.0004  -0.0423 40  ILE A CG2 
320  C CD1 . ILE A 40  ? 0.5177 0.5438 0.4561 0.1081  -0.0092 -0.0615 40  ILE A CD1 
321  N N   . SER A 41  ? 0.4165 0.4665 0.4091 0.0822  0.0067  -0.0373 41  SER A N   
322  C CA  . SER A 41  ? 0.4384 0.4901 0.4385 0.0746  0.0181  -0.0353 41  SER A CA  
323  C C   . SER A 41  ? 0.4632 0.5010 0.4490 0.0785  0.0271  -0.0273 41  SER A C   
324  O O   . SER A 41  ? 0.4577 0.4887 0.4347 0.0844  0.0216  -0.0229 41  SER A O   
325  C CB  . SER A 41  ? 0.4631 0.5142 0.4723 0.0666  0.0156  -0.0367 41  SER A CB  
326  O OG  . SER A 41  ? 0.4917 0.5395 0.5064 0.0572  0.0284  -0.0374 41  SER A OG  
327  N N   . ILE A 42  ? 0.4834 0.5188 0.4660 0.0761  0.0415  -0.0252 42  ILE A N   
328  C CA  . ILE A 42  ? 0.5124 0.5286 0.4749 0.0821  0.0534  -0.0147 42  ILE A CA  
329  C C   . ILE A 42  ? 0.5321 0.5304 0.4972 0.0705  0.0711  -0.0124 42  ILE A C   
330  O O   . ILE A 42  ? 0.5456 0.5498 0.5215 0.0566  0.0839  -0.0186 42  ILE A O   
331  C CB  . ILE A 42  ? 0.5123 0.5323 0.4618 0.0881  0.0604  -0.0128 42  ILE A CB  
332  C CG1 . ILE A 42  ? 0.4963 0.5298 0.4411 0.0984  0.0440  -0.0181 42  ILE A CG1 
333  C CG2 . ILE A 42  ? 0.5442 0.5408 0.4668 0.0965  0.0742  0.0008  42  ILE A CG2 
334  C CD1 . ILE A 42  ? 0.5103 0.5476 0.4387 0.1064  0.0502  -0.0176 42  ILE A CD1 
335  N N   . GLY A 43  ? 0.5210 0.4986 0.4766 0.0757  0.0729  -0.0053 43  GLY A N   
336  C CA  . GLY A 43  ? 0.5418 0.4932 0.4958 0.0653  0.0914  -0.0040 43  GLY A CA  
337  C C   . GLY A 43  ? 0.5421 0.4794 0.4933 0.0723  0.0874  -0.0010 43  GLY A C   
338  O O   . GLY A 43  ? 0.5693 0.4976 0.5031 0.0919  0.0834  0.0098  43  GLY A O   
339  N N   . GLY A 44  ? 0.5179 0.4575 0.4860 0.0577  0.0883  -0.0116 44  GLY A N   
340  C CA  . GLY A 44  ? 0.5072 0.4375 0.4749 0.0636  0.0847  -0.0112 44  GLY A CA  
341  C C   . GLY A 44  ? 0.4704 0.4293 0.4591 0.0545  0.0692  -0.0231 44  GLY A C   
342  O O   . GLY A 44  ? 0.4338 0.4188 0.4340 0.0493  0.0581  -0.0288 44  GLY A O   
343  N N   . ASP A 45  ? 0.4692 0.4216 0.4601 0.0546  0.0693  -0.0262 45  ASP A N   
344  C CA  . ASP A 45  ? 0.4328 0.4093 0.4392 0.0454  0.0573  -0.0367 45  ASP A CA  
345  C C   . ASP A 45  ? 0.4159 0.4048 0.4346 0.0262  0.0611  -0.0497 45  ASP A C   
346  O O   . ASP A 45  ? 0.4034 0.4197 0.4322 0.0222  0.0482  -0.0560 45  ASP A O   
347  C CB  . ASP A 45  ? 0.4391 0.4062 0.4439 0.0492  0.0597  -0.0384 45  ASP A CB  
348  C CG  . ASP A 45  ? 0.4462 0.4173 0.4448 0.0687  0.0524  -0.0288 45  ASP A CG  
349  O OD1 . ASP A 45  ? 0.4262 0.4192 0.4281 0.0728  0.0386  -0.0263 45  ASP A OD1 
350  O OD2 . ASP A 45  ? 0.4643 0.4179 0.4547 0.0803  0.0609  -0.0252 45  ASP A OD2 
351  N N   . GLY A 46  ? 0.4129 0.3827 0.4296 0.0145  0.0796  -0.0542 46  GLY A N   
352  C CA  . GLY A 46  ? 0.4032 0.3949 0.4353 -0.0057 0.0835  -0.0698 46  GLY A CA  
353  C C   . GLY A 46  ? 0.4486 0.4719 0.4900 -0.0033 0.0736  -0.0696 46  GLY A C   
354  O O   . GLY A 46  ? 0.4305 0.4899 0.4865 -0.0087 0.0633  -0.0803 46  GLY A O   
355  N N   . THR A 47  ? 0.4482 0.4594 0.4792 0.0075  0.0766  -0.0574 47  THR A N   
356  C CA  . THR A 47  ? 0.4115 0.4496 0.4487 0.0133  0.0673  -0.0569 47  THR A CA  
357  C C   . THR A 47  ? 0.3762 0.4322 0.4151 0.0257  0.0457  -0.0551 47  THR A C   
358  O O   . THR A 47  ? 0.3734 0.4564 0.4213 0.0282  0.0364  -0.0603 47  THR A O   
359  C CB  . THR A 47  ? 0.4450 0.4640 0.4661 0.0233  0.0754  -0.0445 47  THR A CB  
360  O OG1 . THR A 47  ? 0.5077 0.5021 0.5220 0.0114  0.0992  -0.0440 47  THR A OG1 
361  C CG2 . THR A 47  ? 0.3969 0.4426 0.4237 0.0292  0.0680  -0.0463 47  THR A CG2 
362  N N   . PHE A 48  ? 0.3686 0.4091 0.3982 0.0339  0.0390  -0.0481 48  PHE A N   
363  C CA  . PHE A 48  ? 0.3724 0.4239 0.4015 0.0415  0.0225  -0.0467 48  PHE A CA  
364  C C   . PHE A 48  ? 0.4253 0.4945 0.4626 0.0349  0.0166  -0.0552 48  PHE A C   
365  O O   . PHE A 48  ? 0.4228 0.5053 0.4594 0.0409  0.0057  -0.0552 48  PHE A O   
366  C CB  . PHE A 48  ? 0.3727 0.4099 0.3928 0.0489  0.0189  -0.0395 48  PHE A CB  
367  C CG  . PHE A 48  ? 0.3688 0.4128 0.3868 0.0527  0.0059  -0.0386 48  PHE A CG  
368  C CD1 . PHE A 48  ? 0.3659 0.4092 0.3776 0.0595  0.0000  -0.0361 48  PHE A CD1 
369  C CD2 . PHE A 48  ? 0.3697 0.4178 0.3896 0.0481  0.0017  -0.0412 48  PHE A CD2 
370  C CE1 . PHE A 48  ? 0.3646 0.4068 0.3723 0.0596  -0.0084 -0.0367 48  PHE A CE1 
371  C CE2 . PHE A 48  ? 0.3798 0.4273 0.3942 0.0493  -0.0063 -0.0395 48  PHE A CE2 
372  C CZ  . PHE A 48  ? 0.3792 0.4218 0.3878 0.0540  -0.0106 -0.0376 48  PHE A CZ  
373  N N   . LEU A 49  ? 0.4708 0.5379 0.5123 0.0239  0.0244  -0.0623 49  LEU A N   
374  C CA  . LEU A 49  ? 0.4925 0.5817 0.5399 0.0175  0.0186  -0.0724 49  LEU A CA  
375  C C   . LEU A 49  ? 0.5208 0.6432 0.5790 0.0166  0.0141  -0.0806 49  LEU A C   
376  O O   . LEU A 49  ? 0.4855 0.6309 0.5431 0.0228  0.0023  -0.0831 49  LEU A O   
377  C CB  . LEU A 49  ? 0.5250 0.6056 0.5748 0.0037  0.0301  -0.0823 49  LEU A CB  
378  C CG  . LEU A 49  ? 0.5585 0.6250 0.6001 0.0057  0.0294  -0.0805 49  LEU A CG  
379  C CD1 . LEU A 49  ? 0.5662 0.6286 0.6000 0.0192  0.0189  -0.0676 49  LEU A CD1 
380  C CD2 . LEU A 49  ? 0.5821 0.6171 0.6195 0.0022  0.0459  -0.0809 49  LEU A CD2 
381  N N   . SER A 50  ? 0.5774 0.7042 0.6441 0.0107  0.0241  -0.0842 50  SER A N   
382  C CA  . SER A 50  ? 0.5983 0.7649 0.6794 0.0101  0.0210  -0.0941 50  SER A CA  
383  C C   . SER A 50  ? 0.5641 0.7383 0.6392 0.0312  0.0080  -0.0850 50  SER A C   
384  O O   . SER A 50  ? 0.5762 0.7839 0.6567 0.0405  -0.0021 -0.0903 50  SER A O   
385  C CB  . SER A 50  ? 0.6570 0.8248 0.7486 -0.0042 0.0388  -0.1005 50  SER A CB  
386  O OG  . SER A 50  ? 0.7097 0.8537 0.8002 -0.0228 0.0547  -0.1064 50  SER A OG  
387  N N   . ALA A 51  ? 0.5094 0.6526 0.5713 0.0403  0.0083  -0.0723 51  ALA A N   
388  C CA  . ALA A 51  ? 0.4740 0.6153 0.5268 0.0583  -0.0018 -0.0655 51  ALA A CA  
389  C C   . ALA A 51  ? 0.4719 0.6112 0.5141 0.0676  -0.0139 -0.0618 51  ALA A C   
390  O O   . ALA A 51  ? 0.4884 0.6374 0.5252 0.0833  -0.0217 -0.0603 51  ALA A O   
391  C CB  . ALA A 51  ? 0.4573 0.5673 0.4973 0.0625  0.0010  -0.0560 51  ALA A CB  
392  N N   . PHE A 52  ? 0.4399 0.5644 0.4762 0.0598  -0.0141 -0.0595 52  PHE A N   
393  C CA  . PHE A 52  ? 0.4292 0.5491 0.4520 0.0666  -0.0227 -0.0549 52  PHE A CA  
394  C C   . PHE A 52  ? 0.4392 0.5947 0.4655 0.0730  -0.0296 -0.0619 52  PHE A C   
395  O O   . PHE A 52  ? 0.4527 0.6097 0.4651 0.0904  -0.0377 -0.0560 52  PHE A O   
396  C CB  . PHE A 52  ? 0.4118 0.5155 0.4304 0.0555  -0.0192 -0.0534 52  PHE A CB  
397  C CG  . PHE A 52  ? 0.4156 0.5215 0.4213 0.0582  -0.0248 -0.0513 52  PHE A CG  
398  C CD1 . PHE A 52  ? 0.4270 0.5096 0.4137 0.0658  -0.0277 -0.0408 52  PHE A CD1 
399  C CD2 . PHE A 52  ? 0.4139 0.5432 0.4240 0.0518  -0.0253 -0.0606 52  PHE A CD2 
400  C CE1 . PHE A 52  ? 0.4228 0.5035 0.3928 0.0685  -0.0302 -0.0368 52  PHE A CE1 
401  C CE2 . PHE A 52  ? 0.4192 0.5516 0.4133 0.0557  -0.0301 -0.0581 52  PHE A CE2 
402  C CZ  . PHE A 52  ? 0.4241 0.5312 0.3971 0.0649  -0.0322 -0.0447 52  PHE A CZ  
403  N N   . HIS A 53  ? 0.4198 0.6041 0.4627 0.0596  -0.0258 -0.0752 53  HIS A N   
404  C CA  . HIS A 53  ? 0.4336 0.6631 0.4825 0.0641  -0.0338 -0.0859 53  HIS A CA  
405  C C   . HIS A 53  ? 0.4498 0.7122 0.5088 0.0788  -0.0384 -0.0894 53  HIS A C   
406  O O   . HIS A 53  ? 0.4416 0.7441 0.5010 0.0928  -0.0488 -0.0946 53  HIS A O   
407  C CB  . HIS A 53  ? 0.4490 0.7013 0.5146 0.0412  -0.0266 -0.1037 53  HIS A CB  
408  C CG  . HIS A 53  ? 0.4859 0.7157 0.5404 0.0313  -0.0239 -0.1032 53  HIS A CG  
409  N ND1 . HIS A 53  ? 0.5053 0.7480 0.5453 0.0380  -0.0332 -0.1034 53  HIS A ND1 
410  C CD2 . HIS A 53  ? 0.4914 0.6875 0.5453 0.0176  -0.0121 -0.1023 53  HIS A CD2 
411  C CE1 . HIS A 53  ? 0.5150 0.7342 0.5480 0.0268  -0.0267 -0.1040 53  HIS A CE1 
412  N NE2 . HIS A 53  ? 0.5095 0.7008 0.5517 0.0154  -0.0142 -0.1034 53  HIS A NE2 
413  N N   . GLN A 54  ? 0.4816 0.7319 0.5481 0.0780  -0.0308 -0.0872 54  GLN A N   
414  C CA  . GLN A 54  ? 0.4725 0.7531 0.5479 0.0942  -0.0338 -0.0903 54  GLN A CA  
415  C C   . GLN A 54  ? 0.4882 0.7511 0.5403 0.1235  -0.0442 -0.0769 54  GLN A C   
416  O O   . GLN A 54  ? 0.5058 0.8003 0.5610 0.1450  -0.0505 -0.0794 54  GLN A O   
417  C CB  . GLN A 54  ? 0.4562 0.7245 0.5414 0.0856  -0.0211 -0.0908 54  GLN A CB  
418  C CG  . GLN A 54  ? 0.4610 0.7634 0.5578 0.1006  -0.0213 -0.0961 54  GLN A CG  
419  C CD  . GLN A 54  ? 0.4713 0.7614 0.5747 0.0902  -0.0066 -0.0965 54  GLN A CD  
420  O OE1 . GLN A 54  ? 0.4792 0.7529 0.5865 0.0677  0.0057  -0.0980 54  GLN A OE1 
421  N NE2 . GLN A 54  ? 0.4792 0.7742 0.5805 0.1084  -0.0067 -0.0946 54  GLN A NE2 
422  N N   . TYR A 55  ? 0.5013 0.7138 0.5294 0.1250  -0.0447 -0.0633 55  TYR A N   
423  C CA  . TYR A 55  ? 0.5383 0.7179 0.5395 0.1483  -0.0494 -0.0500 55  TYR A CA  
424  C C   . TYR A 55  ? 0.5961 0.7504 0.5729 0.1500  -0.0530 -0.0401 55  TYR A C   
425  O O   . TYR A 55  ? 0.6486 0.7555 0.6004 0.1569  -0.0507 -0.0280 55  TYR A O   
426  C CB  . TYR A 55  ? 0.5111 0.6474 0.5046 0.1459  -0.0422 -0.0445 55  TYR A CB  
427  C CG  . TYR A 55  ? 0.4757 0.6320 0.4855 0.1497  -0.0379 -0.0518 55  TYR A CG  
428  C CD1 . TYR A 55  ? 0.4902 0.6596 0.4962 0.1754  -0.0412 -0.0522 55  TYR A CD1 
429  C CD2 . TYR A 55  ? 0.4446 0.6055 0.4708 0.1299  -0.0292 -0.0576 55  TYR A CD2 
430  C CE1 . TYR A 55  ? 0.4918 0.6826 0.5129 0.1789  -0.0357 -0.0598 55  TYR A CE1 
431  C CE2 . TYR A 55  ? 0.4444 0.6227 0.4824 0.1327  -0.0230 -0.0635 55  TYR A CE2 
432  C CZ  . TYR A 55  ? 0.4756 0.6710 0.5125 0.1561  -0.0262 -0.0655 55  TYR A CZ  
433  O OH  . TYR A 55  ? 0.4855 0.7013 0.5345 0.1589  -0.0187 -0.0723 55  TYR A OH  
434  N N   . GLU A 56  ? 0.5897 0.7741 0.5721 0.1421  -0.0570 -0.0463 56  GLU A N   
435  C CA  . GLU A 56  ? 0.6045 0.7675 0.5617 0.1438  -0.0591 -0.0369 56  GLU A CA  
436  C C   . GLU A 56  ? 0.6184 0.7716 0.5449 0.1748  -0.0658 -0.0241 56  GLU A C   
437  O O   . GLU A 56  ? 0.6271 0.7492 0.5244 0.1785  -0.0644 -0.0120 56  GLU A O   
438  C CB  . GLU A 56  ? 0.5926 0.7927 0.5614 0.1288  -0.0616 -0.0489 56  GLU A CB  
439  C CG  . GLU A 56  ? 0.5918 0.8561 0.5842 0.1310  -0.0682 -0.0661 56  GLU A CG  
440  C CD  . GLU A 56  ? 0.5934 0.8909 0.5961 0.1121  -0.0690 -0.0818 56  GLU A CD  
441  O OE1 . GLU A 56  ? 0.6062 0.9553 0.6102 0.1220  -0.0795 -0.0918 56  GLU A OE1 
442  O OE2 . GLU A 56  ? 0.5845 0.8579 0.5928 0.0889  -0.0593 -0.0851 56  GLU A OE2 
443  N N   . GLU A 57  ? 0.6233 0.8006 0.5535 0.1985  -0.0715 -0.0257 57  GLU A N   
444  C CA  . GLU A 57  ? 0.6520 0.8163 0.5494 0.2344  -0.0771 -0.0119 57  GLU A CA  
445  C C   . GLU A 57  ? 0.6513 0.7416 0.5196 0.2430  -0.0673 0.0035  57  GLU A C   
446  O O   . GLU A 57  ? 0.6962 0.7549 0.5275 0.2710  -0.0675 0.0186  57  GLU A O   
447  C CB  . GLU A 57  ? 0.6735 0.8982 0.5878 0.2600  -0.0868 -0.0211 57  GLU A CB  
448  C CG  . GLU A 57  ? 0.7232 0.9996 0.6269 0.2835  -0.1006 -0.0220 57  GLU A CG  
449  C CD  . GLU A 57  ? 0.7313 1.0289 0.6398 0.2581  -0.1029 -0.0299 57  GLU A CD  
450  O OE1 . GLU A 57  ? 0.6967 1.0214 0.6400 0.2256  -0.0992 -0.0478 57  GLU A OE1 
451  O OE2 . GLU A 57  ? 0.7700 1.0528 0.6440 0.2713  -0.1067 -0.0176 57  GLU A OE2 
452  N N   . ARG A 58  ? 0.6143 0.6749 0.4955 0.2204  -0.0581 -0.0005 58  ARG A N   
453  C CA  . ARG A 58  ? 0.6466 0.6405 0.5026 0.2242  -0.0482 0.0090  58  ARG A CA  
454  C C   . ARG A 58  ? 0.6633 0.6258 0.5249 0.1901  -0.0392 0.0067  58  ARG A C   
455  O O   . ARG A 58  ? 0.6906 0.6237 0.5535 0.1811  -0.0325 0.0033  58  ARG A O   
456  C CB  . ARG A 58  ? 0.6316 0.6277 0.4956 0.2405  -0.0475 0.0036  58  ARG A CB  
457  C CG  . ARG A 58  ? 0.6321 0.6741 0.4983 0.2758  -0.0571 0.0028  58  ARG A CG  
458  C CD  . ARG A 58  ? 0.6449 0.6764 0.5096 0.2982  -0.0537 0.0003  58  ARG A CD  
459  N NE  . ARG A 58  ? 0.6611 0.6219 0.5065 0.2870  -0.0414 0.0034  58  ARG A NE  
460  C CZ  . ARG A 58  ? 0.6193 0.5790 0.4849 0.2641  -0.0362 -0.0077 58  ARG A CZ  
461  N NH1 . ARG A 58  ? 0.5763 0.5939 0.4788 0.2506  -0.0400 -0.0198 58  ARG A NH1 
462  N NH2 . ARG A 58  ? 0.6283 0.5286 0.4751 0.2539  -0.0262 -0.0075 58  ARG A NH2 
463  N N   . LEU A 59  ? 0.6458 0.6184 0.5107 0.1721  -0.0393 0.0070  59  LEU A N   
464  C CA  . LEU A 59  ? 0.6298 0.5823 0.5024 0.1426  -0.0315 0.0040  59  LEU A CA  
465  C C   . LEU A 59  ? 0.6859 0.5774 0.5303 0.1375  -0.0204 0.0121  59  LEU A C   
466  O O   . LEU A 59  ? 0.6923 0.5705 0.5464 0.1145  -0.0141 0.0061  59  LEU A O   
467  C CB  . LEU A 59  ? 0.6057 0.5818 0.4849 0.1284  -0.0327 0.0025  59  LEU A CB  
468  C CG  . LEU A 59  ? 0.5674 0.5992 0.4755 0.1255  -0.0404 -0.0094 59  LEU A CG  
469  C CD1 . LEU A 59  ? 0.5524 0.6002 0.4611 0.1129  -0.0401 -0.0119 59  LEU A CD1 
470  C CD2 . LEU A 59  ? 0.5389 0.5822 0.4757 0.1119  -0.0378 -0.0196 59  LEU A CD2 
471  N N   . ASP A 60  ? 0.7409 0.5952 0.5496 0.1585  -0.0169 0.0248  60  ASP A N   
472  C CA  . ASP A 60  ? 0.8107 0.5982 0.5892 0.1517  -0.0025 0.0315  60  ASP A CA  
473  C C   . ASP A 60  ? 0.8091 0.5695 0.5868 0.1562  0.0014  0.0248  60  ASP A C   
474  O O   . ASP A 60  ? 0.8495 0.5585 0.6102 0.1413  0.0143  0.0234  60  ASP A O   
475  C CB  . ASP A 60  ? 0.9273 0.6744 0.6601 0.1738  0.0033  0.0502  60  ASP A CB  
476  C CG  . ASP A 60  ? 0.9999 0.7688 0.7227 0.2142  -0.0080 0.0567  60  ASP A CG  
477  O OD1 . ASP A 60  ? 0.9750 0.8107 0.7260 0.2202  -0.0225 0.0492  60  ASP A OD1 
478  O OD2 . ASP A 60  ? 1.0884 0.8083 0.7753 0.2402  -0.0015 0.0682  60  ASP A OD2 
479  N N   . GLU A 61  ? 0.7608 0.5558 0.5565 0.1746  -0.0083 0.0188  61  GLU A N   
480  C CA  . GLU A 61  ? 0.7656 0.5400 0.5608 0.1809  -0.0047 0.0110  61  GLU A CA  
481  C C   . GLU A 61  ? 0.7186 0.5301 0.5494 0.1611  -0.0087 -0.0045 61  GLU A C   
482  O O   . GLU A 61  ? 0.7308 0.5325 0.5625 0.1656  -0.0065 -0.0126 61  GLU A O   
483  C CB  . GLU A 61  ? 0.8099 0.5945 0.5960 0.2198  -0.0102 0.0155  61  GLU A CB  
484  C CG  . GLU A 61  ? 0.9089 0.6460 0.6505 0.2485  -0.0050 0.0329  61  GLU A CG  
485  C CD  . GLU A 61  ? 0.9303 0.7127 0.6713 0.2689  -0.0167 0.0423  61  GLU A CD  
486  O OE1 . GLU A 61  ? 0.9923 0.7599 0.7029 0.3062  -0.0180 0.0551  61  GLU A OE1 
487  O OE2 . GLU A 61  ? 0.8864 0.7198 0.6558 0.2490  -0.0245 0.0360  61  GLU A OE2 
488  N N   . ILE A 62  ? 0.6554 0.5062 0.5119 0.1412  -0.0135 -0.0084 62  ILE A N   
489  C CA  . ILE A 62  ? 0.6036 0.4923 0.4904 0.1293  -0.0175 -0.0196 62  ILE A CA  
490  C C   . ILE A 62  ? 0.5821 0.4724 0.4795 0.1019  -0.0149 -0.0242 62  ILE A C   
491  O O   . ILE A 62  ? 0.5830 0.4748 0.4794 0.0920  -0.0138 -0.0195 62  ILE A O   
492  C CB  . ILE A 62  ? 0.5651 0.5073 0.4754 0.1372  -0.0253 -0.0208 62  ILE A CB  
493  C CG1 . ILE A 62  ? 0.5852 0.5397 0.4916 0.1651  -0.0285 -0.0200 62  ILE A CG1 
494  C CG2 . ILE A 62  ? 0.5214 0.4928 0.4575 0.1221  -0.0254 -0.0295 62  ILE A CG2 
495  C CD1 . ILE A 62  ? 0.5396 0.5524 0.4711 0.1698  -0.0351 -0.0248 62  ILE A CD1 
496  N N   . ALA A 63  ? 0.5601 0.4540 0.4669 0.0917  -0.0141 -0.0339 63  ALA A N   
497  C CA  . ALA A 63  ? 0.5221 0.4337 0.4443 0.0714  -0.0144 -0.0397 63  ALA A CA  
498  C C   . ALA A 63  ? 0.5056 0.4550 0.4485 0.0746  -0.0190 -0.0423 63  ALA A C   
499  O O   . ALA A 63  ? 0.5368 0.4919 0.4804 0.0852  -0.0196 -0.0451 63  ALA A O   
500  C CB  . ALA A 63  ? 0.5101 0.4003 0.4241 0.0573  -0.0101 -0.0500 63  ALA A CB  
501  N N   . PHE A 64  ? 0.4744 0.4464 0.4319 0.0659  -0.0201 -0.0411 64  PHE A N   
502  C CA  . PHE A 64  ? 0.4552 0.4539 0.4278 0.0685  -0.0208 -0.0414 64  PHE A CA  
503  C C   . PHE A 64  ? 0.4820 0.4898 0.4584 0.0630  -0.0213 -0.0456 64  PHE A C   
504  O O   . PHE A 64  ? 0.4977 0.5050 0.4740 0.0533  -0.0221 -0.0493 64  PHE A O   
505  C CB  . PHE A 64  ? 0.4109 0.4246 0.3938 0.0653  -0.0201 -0.0379 64  PHE A CB  
506  C CG  . PHE A 64  ? 0.3900 0.4082 0.3712 0.0730  -0.0217 -0.0357 64  PHE A CG  
507  C CD1 . PHE A 64  ? 0.3558 0.3955 0.3480 0.0782  -0.0210 -0.0382 64  PHE A CD1 
508  C CD2 . PHE A 64  ? 0.4178 0.4214 0.3853 0.0755  -0.0231 -0.0314 64  PHE A CD2 
509  C CE1 . PHE A 64  ? 0.3796 0.4349 0.3731 0.0862  -0.0241 -0.0390 64  PHE A CE1 
510  C CE2 . PHE A 64  ? 0.4250 0.4389 0.3886 0.0871  -0.0265 -0.0290 64  PHE A CE2 
511  C CZ  . PHE A 64  ? 0.4182 0.4624 0.3968 0.0928  -0.0282 -0.0340 64  PHE A CZ  
512  N N   . ILE A 65  ? 0.4762 0.4956 0.4553 0.0700  -0.0201 -0.0453 65  ILE A N   
513  C CA  . ILE A 65  ? 0.4760 0.5071 0.4544 0.0708  -0.0209 -0.0470 65  ILE A CA  
514  C C   . ILE A 65  ? 0.4990 0.5385 0.4817 0.0766  -0.0152 -0.0402 65  ILE A C   
515  O O   . ILE A 65  ? 0.5263 0.5648 0.5102 0.0798  -0.0100 -0.0384 65  ILE A O   
516  C CB  . ILE A 65  ? 0.4544 0.4825 0.4211 0.0747  -0.0230 -0.0539 65  ILE A CB  
517  C CG1 . ILE A 65  ? 0.4732 0.4840 0.4327 0.0661  -0.0252 -0.0625 65  ILE A CG1 
518  C CG2 . ILE A 65  ? 0.4526 0.4993 0.4157 0.0788  -0.0255 -0.0551 65  ILE A CG2 
519  C CD1 . ILE A 65  ? 0.4961 0.4998 0.4424 0.0685  -0.0260 -0.0727 65  ILE A CD1 
520  N N   . GLY A 66  ? 0.4882 0.5353 0.4727 0.0781  -0.0145 -0.0369 66  GLY A N   
521  C CA  . GLY A 66  ? 0.4941 0.5383 0.4778 0.0835  -0.0057 -0.0295 66  GLY A CA  
522  C C   . GLY A 66  ? 0.5197 0.5670 0.4897 0.0961  -0.0040 -0.0243 66  GLY A C   
523  O O   . GLY A 66  ? 0.5293 0.5906 0.4968 0.1018  -0.0110 -0.0258 66  GLY A O   
524  N N   . ILE A 67  ? 0.5409 0.5784 0.5013 0.1009  0.0059  -0.0186 67  ILE A N   
525  C CA  . ILE A 67  ? 0.5530 0.5867 0.4940 0.1154  0.0113  -0.0095 67  ILE A CA  
526  C C   . ILE A 67  ? 0.5891 0.5995 0.5261 0.1159  0.0275  0.0001  67  ILE A C   
527  O O   . ILE A 67  ? 0.6046 0.6046 0.5488 0.1039  0.0384  -0.0015 67  ILE A O   
528  C CB  . ILE A 67  ? 0.5409 0.5759 0.4675 0.1201  0.0136  -0.0098 67  ILE A CB  
529  C CG1 . ILE A 67  ? 0.5294 0.5797 0.4596 0.1165  0.0002  -0.0225 67  ILE A CG1 
530  C CG2 . ILE A 67  ? 0.5650 0.5977 0.4657 0.1382  0.0176  0.0009  67  ILE A CG2 
531  C CD1 . ILE A 67  ? 0.5323 0.5832 0.4499 0.1204  0.0032  -0.0258 67  ILE A CD1 
532  N N   . HIS A 68  ? 0.6172 0.6204 0.5427 0.1299  0.0300  0.0087  68  HIS A N   
533  C CA  . HIS A 68  ? 0.6658 0.6374 0.5831 0.1316  0.0480  0.0178  68  HIS A CA  
534  C C   . HIS A 68  ? 0.7111 0.6597 0.5973 0.1475  0.0617  0.0325  68  HIS A C   
535  O O   . HIS A 68  ? 0.7341 0.6920 0.6014 0.1700  0.0547  0.0403  68  HIS A O   
536  C CB  . HIS A 68  ? 0.6904 0.6616 0.6130 0.1391  0.0453  0.0184  68  HIS A CB  
537  C CG  . HIS A 68  ? 0.7295 0.7108 0.6353 0.1660  0.0393  0.0272  68  HIS A CG  
538  N ND1 . HIS A 68  ? 0.7230 0.7437 0.6316 0.1739  0.0207  0.0217  68  HIS A ND1 
539  C CD2 . HIS A 68  ? 0.7722 0.7316 0.6578 0.1882  0.0493  0.0400  68  HIS A CD2 
540  C CE1 . HIS A 68  ? 0.7522 0.7831 0.6453 0.2002  0.0177  0.0299  68  HIS A CE1 
541  N NE2 . HIS A 68  ? 0.7838 0.7762 0.6614 0.2119  0.0348  0.0427  68  HIS A NE2 
542  N N   . THR A 69  ? 0.7242 0.6464 0.6046 0.1354  0.0815  0.0355  69  THR A N   
543  C CA  . THR A 69  ? 0.7670 0.6552 0.6142 0.1469  0.1016  0.0514  69  THR A CA  
544  C C   . THR A 69  ? 0.8149 0.6559 0.6499 0.1463  0.1238  0.0597  69  THR A C   
545  O O   . THR A 69  ? 0.8680 0.6684 0.6745 0.1496  0.1474  0.0727  69  THR A O   
546  C CB  . THR A 69  ? 0.7760 0.6644 0.6225 0.1318  0.1134  0.0487  69  THR A CB  
547  O OG1 . THR A 69  ? 0.7548 0.6383 0.6257 0.1044  0.1252  0.0371  69  THR A OG1 
548  C CG2 . THR A 69  ? 0.7539 0.6835 0.6108 0.1333  0.0932  0.0389  69  THR A CG2 
549  N N   . GLY A 70  ? 0.8035 0.6453 0.6569 0.1415  0.1188  0.0520  70  GLY A N   
550  C CA  . GLY A 70  ? 0.8363 0.6314 0.6805 0.1375  0.1407  0.0552  70  GLY A CA  
551  C C   . GLY A 70  ? 0.8470 0.6284 0.6763 0.1656  0.1379  0.0648  70  GLY A C   
552  O O   . GLY A 70  ? 0.8369 0.6309 0.6472 0.1952  0.1276  0.0770  70  GLY A O   
553  N N   . HIS A 71  ? 0.8721 0.6324 0.7103 0.1577  0.1465  0.0576  71  HIS A N   
554  C CA  . HIS A 71  ? 0.9324 0.6703 0.7528 0.1866  0.1502  0.0674  71  HIS A CA  
555  C C   . HIS A 71  ? 0.9252 0.7181 0.7696 0.1985  0.1232  0.0594  71  HIS A C   
556  O O   . HIS A 71  ? 0.9161 0.7312 0.7493 0.2293  0.1111  0.0690  71  HIS A O   
557  C CB  . HIS A 71  ? 0.9642 0.6471 0.7788 0.1732  0.1759  0.0624  71  HIS A CB  
558  C CG  . HIS A 71  ? 0.9953 0.6348 0.7992 0.1461  0.2026  0.0611  71  HIS A CG  
559  N ND1 . HIS A 71  ? 1.0565 0.6481 0.8218 0.1579  0.2246  0.0804  71  HIS A ND1 
560  C CD2 . HIS A 71  ? 0.9805 0.6220 0.8076 0.1069  0.2114  0.0418  71  HIS A CD2 
561  C CE1 . HIS A 71  ? 1.0758 0.6400 0.8429 0.1240  0.2479  0.0722  71  HIS A CE1 
562  N NE2 . HIS A 71  ? 1.0305 0.6280 0.8366 0.0928  0.2393  0.0477  71  HIS A NE2 
563  N N   . LEU A 72  ? 0.9249 0.7430 0.8015 0.1742  0.1142  0.0413  72  LEU A N   
564  C CA  . LEU A 72  ? 0.8971 0.7633 0.7959 0.1808  0.0929  0.0330  72  LEU A CA  
565  C C   . LEU A 72  ? 0.8424 0.7577 0.7632 0.1655  0.0715  0.0240  72  LEU A C   
566  O O   . LEU A 72  ? 0.8595 0.8088 0.7798 0.1800  0.0560  0.0266  72  LEU A O   
567  C CB  . LEU A 72  ? 0.9078 0.7656 0.8219 0.1674  0.0989  0.0204  72  LEU A CB  
568  C CG  . LEU A 72  ? 0.8685 0.7735 0.8071 0.1674  0.0812  0.0099  72  LEU A CG  
569  C CD1 . LEU A 72  ? 0.8699 0.8054 0.8046 0.1989  0.0701  0.0175  72  LEU A CD1 
570  C CD2 . LEU A 72  ? 0.8690 0.7563 0.8139 0.1583  0.0920  -0.0007 72  LEU A CD2 
571  N N   . GLY A 73  ? 0.7737 0.6930 0.7123 0.1371  0.0709  0.0122  73  GLY A N   
572  C CA  . GLY A 73  ? 0.7011 0.6578 0.6570 0.1242  0.0532  0.0042  73  GLY A CA  
573  C C   . GLY A 73  ? 0.6685 0.6608 0.6408 0.1256  0.0374  -0.0030 73  GLY A C   
574  O O   . GLY A 73  ? 0.6773 0.6977 0.6502 0.1359  0.0248  -0.0023 73  GLY A O   
575  N N   . PHE A 74  ? 0.6195 0.6127 0.6047 0.1135  0.0391  -0.0114 74  PHE A N   
576  C CA  . PHE A 74  ? 0.5317 0.5564 0.5313 0.1128  0.0282  -0.0180 74  PHE A CA  
577  C C   . PHE A 74  ? 0.4816 0.5300 0.4911 0.0985  0.0148  -0.0238 74  PHE A C   
578  O O   . PHE A 74  ? 0.4380 0.5146 0.4552 0.0996  0.0054  -0.0277 74  PHE A O   
579  C CB  . PHE A 74  ? 0.5026 0.5191 0.5088 0.1043  0.0357  -0.0250 74  PHE A CB  
580  C CG  . PHE A 74  ? 0.4552 0.5030 0.4747 0.1032  0.0284  -0.0313 74  PHE A CG  
581  C CD1 . PHE A 74  ? 0.4674 0.5301 0.4889 0.1222  0.0298  -0.0301 74  PHE A CD1 
582  C CD2 . PHE A 74  ? 0.4248 0.4871 0.4534 0.0843  0.0217  -0.0380 74  PHE A CD2 
583  C CE1 . PHE A 74  ? 0.4567 0.5536 0.4933 0.1187  0.0250  -0.0377 74  PHE A CE1 
584  C CE2 . PHE A 74  ? 0.4224 0.5107 0.4614 0.0804  0.0185  -0.0435 74  PHE A CE2 
585  C CZ  . PHE A 74  ? 0.4404 0.5485 0.4854 0.0958  0.0204  -0.0444 74  PHE A CZ  
586  N N   . TYR A 75  ? 0.4927 0.5303 0.5019 0.0850  0.0150  -0.0256 75  TYR A N   
587  C CA  . TYR A 75  ? 0.4916 0.5423 0.5056 0.0744  0.0047  -0.0300 75  TYR A CA  
588  C C   . TYR A 75  ? 0.5093 0.5656 0.5166 0.0805  -0.0013 -0.0281 75  TYR A C   
589  O O   . TYR A 75  ? 0.5255 0.5870 0.5338 0.0729  -0.0083 -0.0325 75  TYR A O   
590  C CB  . TYR A 75  ? 0.4641 0.5059 0.4800 0.0622  0.0065  -0.0332 75  TYR A CB  
591  C CG  . TYR A 75  ? 0.4665 0.5107 0.4874 0.0536  0.0080  -0.0380 75  TYR A CG  
592  C CD1 . TYR A 75  ? 0.4545 0.4895 0.4763 0.0493  0.0168  -0.0417 75  TYR A CD1 
593  C CD2 . TYR A 75  ? 0.4534 0.5079 0.4759 0.0482  0.0022  -0.0400 75  TYR A CD2 
594  C CE1 . TYR A 75  ? 0.4530 0.4928 0.4768 0.0419  0.0177  -0.0477 75  TYR A CE1 
595  C CE2 . TYR A 75  ? 0.4303 0.4871 0.4534 0.0413  0.0045  -0.0435 75  TYR A CE2 
596  C CZ  . TYR A 75  ? 0.4347 0.4859 0.4581 0.0392  0.0112  -0.0475 75  TYR A CZ  
597  O OH  . TYR A 75  ? 0.4238 0.4798 0.4455 0.0328  0.0131  -0.0525 75  TYR A OH  
598  N N   . ALA A 76  ? 0.5327 0.5850 0.5297 0.0949  0.0022  -0.0215 76  ALA A N   
599  C CA  . ALA A 76  ? 0.5486 0.6074 0.5357 0.1017  -0.0029 -0.0202 76  ALA A CA  
600  C C   . ALA A 76  ? 0.5808 0.6696 0.5699 0.1081  -0.0140 -0.0253 76  ALA A C   
601  O O   . ALA A 76  ? 0.5812 0.6866 0.5774 0.1140  -0.0155 -0.0263 76  ALA A O   
602  C CB  . ALA A 76  ? 0.5438 0.5838 0.5138 0.1149  0.0075  -0.0096 76  ALA A CB  
603  N N   . ASP A 77  ? 0.5986 0.6977 0.5824 0.1064  -0.0214 -0.0307 77  ASP A N   
604  C CA  . ASP A 77  ? 0.6167 0.7497 0.6026 0.1091  -0.0324 -0.0399 77  ASP A CA  
605  C C   . ASP A 77  ? 0.6284 0.7714 0.5958 0.1250  -0.0363 -0.0377 77  ASP A C   
606  O O   . ASP A 77  ? 0.6402 0.8166 0.6080 0.1265  -0.0469 -0.0484 77  ASP A O   
607  C CB  . ASP A 77  ? 0.6221 0.7594 0.6172 0.0876  -0.0375 -0.0538 77  ASP A CB  
608  C CG  . ASP A 77  ? 0.6376 0.7718 0.6474 0.0732  -0.0342 -0.0562 77  ASP A CG  
609  O OD1 . ASP A 77  ? 0.6460 0.7807 0.6613 0.0799  -0.0296 -0.0495 77  ASP A OD1 
610  O OD2 . ASP A 77  ? 0.6434 0.7710 0.6561 0.0557  -0.0347 -0.0646 77  ASP A OD2 
611  N N   . TRP A 78  ? 0.6486 0.7660 0.5992 0.1354  -0.0273 -0.0254 78  TRP A N   
612  C CA  . TRP A 78  ? 0.6713 0.7939 0.6005 0.1481  -0.0293 -0.0232 78  TRP A CA  
613  C C   . TRP A 78  ? 0.6907 0.7903 0.5979 0.1676  -0.0168 -0.0047 78  TRP A C   
614  O O   . TRP A 78  ? 0.7155 0.7832 0.6243 0.1623  -0.0029 0.0035  78  TRP A O   
615  C CB  . TRP A 78  ? 0.6689 0.7785 0.5961 0.1346  -0.0283 -0.0306 78  TRP A CB  
616  C CG  . TRP A 78  ? 0.6524 0.7745 0.5930 0.1171  -0.0377 -0.0479 78  TRP A CG  
617  C CD1 . TRP A 78  ? 0.6342 0.7418 0.5901 0.0999  -0.0361 -0.0526 78  TRP A CD1 
618  C CD2 . TRP A 78  ? 0.6549 0.8039 0.5916 0.1143  -0.0485 -0.0634 78  TRP A CD2 
619  N NE1 . TRP A 78  ? 0.6302 0.7465 0.5899 0.0864  -0.0427 -0.0682 78  TRP A NE1 
620  C CE2 . TRP A 78  ? 0.6452 0.7880 0.5952 0.0927  -0.0503 -0.0770 78  TRP A CE2 
621  C CE3 . TRP A 78  ? 0.6569 0.8348 0.5779 0.1279  -0.0563 -0.0679 78  TRP A CE3 
622  C CZ2 . TRP A 78  ? 0.6475 0.8084 0.5974 0.0805  -0.0576 -0.0968 78  TRP A CZ2 
623  C CZ3 . TRP A 78  ? 0.6605 0.8647 0.5834 0.1166  -0.0664 -0.0892 78  TRP A CZ3 
624  C CH2 . TRP A 78  ? 0.6595 0.8534 0.5977 0.0912  -0.0660 -0.1043 78  TRP A CH2 
625  N N   . ARG A 79  ? 0.6901 0.8058 0.5746 0.1898  -0.0209 0.0009  79  ARG A N   
626  C CA  . ARG A 79  ? 0.6966 0.7844 0.5504 0.2092  -0.0070 0.0197  79  ARG A CA  
627  C C   . ARG A 79  ? 0.6790 0.7549 0.5188 0.2022  -0.0011 0.0189  79  ARG A C   
628  O O   . ARG A 79  ? 0.6485 0.7462 0.4958 0.1916  -0.0122 0.0035  79  ARG A O   
629  C CB  . ARG A 79  ? 0.7261 0.8379 0.5565 0.2412  -0.0144 0.0281  79  ARG A CB  
630  C CG  . ARG A 79  ? 0.7317 0.8533 0.5717 0.2557  -0.0167 0.0321  79  ARG A CG  
631  C CD  . ARG A 79  ? 0.7645 0.9074 0.5757 0.2950  -0.0221 0.0442  79  ARG A CD  
632  N NE  . ARG A 79  ? 0.7493 0.9502 0.5582 0.3013  -0.0427 0.0302  79  ARG A NE  
633  C CZ  . ARG A 79  ? 0.7772 0.9855 0.5509 0.3225  -0.0450 0.0378  79  ARG A CZ  
634  N NH1 . ARG A 79  ? 0.8199 0.9776 0.5562 0.3399  -0.0261 0.0620  79  ARG A NH1 
635  N NH2 . ARG A 79  ? 0.7740 1.0404 0.5482 0.3250  -0.0649 0.0204  79  ARG A NH2 
636  N N   . PRO A 80  ? 0.6021 0.8393 0.5882 0.1020  -0.0283 0.0038  80  PRO A N   
637  C CA  . PRO A 80  ? 0.6045 0.8388 0.5765 0.0970  -0.0166 -0.0018 80  PRO A CA  
638  C C   . PRO A 80  ? 0.6108 0.8563 0.5568 0.1028  -0.0239 -0.0114 80  PRO A C   
639  O O   . PRO A 80  ? 0.6036 0.8519 0.5454 0.0987  -0.0175 -0.0229 80  PRO A O   
640  C CB  . PRO A 80  ? 0.6390 0.8518 0.5888 0.0959  -0.0014 0.0146  80  PRO A CB  
641  C CG  . PRO A 80  ? 0.6268 0.8271 0.5908 0.0958  -0.0031 0.0256  80  PRO A CG  
642  C CD  . PRO A 80  ? 0.6171 0.8321 0.5911 0.1058  -0.0215 0.0217  80  PRO A CD  
643  N N   . ALA A 81  ? 0.6206 0.8742 0.5479 0.1138  -0.0377 -0.0078 81  ALA A N   
644  C CA  . ALA A 81  ? 0.6320 0.9000 0.5338 0.1191  -0.0471 -0.0183 81  ALA A CA  
645  C C   . ALA A 81  ? 0.6164 0.9037 0.5409 0.1097  -0.0574 -0.0399 81  ALA A C   
646  O O   . ALA A 81  ? 0.6358 0.9299 0.5409 0.1087  -0.0610 -0.0532 81  ALA A O   
647  C CB  . ALA A 81  ? 0.6571 0.9331 0.5331 0.1358  -0.0609 -0.0086 81  ALA A CB  
648  N N   . GLU A 82  ? 0.5867 0.8792 0.5478 0.1016  -0.0613 -0.0439 82  GLU A N   
649  C CA  . GLU A 82  ? 0.5757 0.8786 0.5561 0.0894  -0.0687 -0.0635 82  GLU A CA  
650  C C   . GLU A 82  ? 0.5755 0.8579 0.5661 0.0808  -0.0557 -0.0719 82  GLU A C   
651  O O   . GLU A 82  ? 0.5833 0.8628 0.5894 0.0702  -0.0591 -0.0858 82  GLU A O   
652  C CB  . GLU A 82  ? 0.5512 0.8697 0.5627 0.0848  -0.0785 -0.0630 82  GLU A CB  
653  C CG  . GLU A 82  ? 0.5609 0.9052 0.5803 0.0745  -0.0933 -0.0812 82  GLU A CG  
654  C CD  . GLU A 82  ? 0.5338 0.8995 0.5843 0.0702  -0.1009 -0.0795 82  GLU A CD  
655  O OE1 . GLU A 82  ? 0.5099 0.8665 0.5737 0.0771  -0.0949 -0.0642 82  GLU A OE1 
656  O OE2 . GLU A 82  ? 0.5316 0.9242 0.5925 0.0586  -0.1123 -0.0943 82  GLU A OE2 
657  N N   . ALA A 83  ? 0.5709 0.8391 0.5512 0.0854  -0.0406 -0.0642 83  ALA A N   
658  C CA  . ALA A 83  ? 0.5772 0.8319 0.5718 0.0815  -0.0282 -0.0703 83  ALA A CA  
659  C C   . ALA A 83  ? 0.6198 0.8682 0.6003 0.0796  -0.0285 -0.0903 83  ALA A C   
660  O O   . ALA A 83  ? 0.6260 0.8611 0.6203 0.0753  -0.0269 -0.1007 83  ALA A O   
661  C CB  . ALA A 83  ? 0.5795 0.8298 0.5687 0.0857  -0.0117 -0.0580 83  ALA A CB  
662  N N   . ASP A 84  ? 0.6397 0.8933 0.5884 0.0836  -0.0302 -0.0959 84  ASP A N   
663  C CA  . ASP A 84  ? 0.6590 0.9029 0.5892 0.0824  -0.0294 -0.1161 84  ASP A CA  
664  C C   . ASP A 84  ? 0.6495 0.8898 0.5859 0.0704  -0.0434 -0.1320 84  ASP A C   
665  O O   . ASP A 84  ? 0.6788 0.8987 0.6071 0.0664  -0.0410 -0.1490 84  ASP A O   
666  C CB  . ASP A 84  ? 0.6934 0.9441 0.5849 0.0890  -0.0284 -0.1185 84  ASP A CB  
667  C CG  . ASP A 84  ? 0.6934 0.9444 0.5747 0.0974  -0.0106 -0.1052 84  ASP A CG  
668  O OD1 . ASP A 84  ? 0.7018 0.9595 0.5625 0.1017  -0.0104 -0.0917 84  ASP A OD1 
669  O OD2 . ASP A 84  ? 0.6822 0.9268 0.5752 0.0995  0.0036  -0.1083 84  ASP A OD2 
670  N N   . LYS A 85  ? 0.6186 0.8779 0.5679 0.0644  -0.0572 -0.1273 85  LYS A N   
671  C CA  . LYS A 85  ? 0.6132 0.8733 0.5745 0.0486  -0.0684 -0.1418 85  LYS A CA  
672  C C   . LYS A 85  ? 0.6215 0.8588 0.6085 0.0423  -0.0613 -0.1409 85  LYS A C   
673  O O   . LYS A 85  ? 0.6444 0.8649 0.6321 0.0284  -0.0640 -0.1557 85  LYS A O   
674  C CB  . LYS A 85  ? 0.5868 0.8819 0.5588 0.0457  -0.0841 -0.1369 85  LYS A CB  
675  C CG  . LYS A 85  ? 0.5980 0.9045 0.5825 0.0258  -0.0959 -0.1536 85  LYS A CG  
676  C CD  . LYS A 85  ? 0.6215 0.9729 0.6026 0.0256  -0.1137 -0.1569 85  LYS A CD  
677  C CE  . LYS A 85  ? 0.6451 1.0155 0.6423 0.0017  -0.1246 -0.1751 85  LYS A CE  
678  N NZ  . LYS A 85  ? 0.6787 1.0998 0.6701 0.0013  -0.1434 -0.1833 85  LYS A NZ  
679  N N   . LEU A 86  ? 0.5915 0.8256 0.5966 0.0513  -0.0519 -0.1240 86  LEU A N   
680  C CA  . LEU A 86  ? 0.5680 0.7810 0.5945 0.0479  -0.0456 -0.1225 86  LEU A CA  
681  C C   . LEU A 86  ? 0.5920 0.7754 0.6043 0.0534  -0.0354 -0.1337 86  LEU A C   
682  O O   . LEU A 86  ? 0.6040 0.7604 0.6191 0.0479  -0.0341 -0.1417 86  LEU A O   
683  C CB  . LEU A 86  ? 0.5192 0.7402 0.5678 0.0554  -0.0398 -0.1026 86  LEU A CB  
684  C CG  . LEU A 86  ? 0.4993 0.7020 0.5686 0.0557  -0.0330 -0.0987 86  LEU A CG  
685  C CD1 . LEU A 86  ? 0.4958 0.6869 0.5758 0.0422  -0.0396 -0.1053 86  LEU A CD1 
686  C CD2 . LEU A 86  ? 0.4839 0.6979 0.5714 0.0614  -0.0283 -0.0804 86  LEU A CD2 
687  N N   . VAL A 87  ? 0.6012 0.7876 0.5957 0.0656  -0.0271 -0.1343 87  VAL A N   
688  C CA  . VAL A 87  ? 0.6367 0.7989 0.6161 0.0749  -0.0169 -0.1463 87  VAL A CA  
689  C C   . VAL A 87  ? 0.7000 0.8338 0.6567 0.0651  -0.0228 -0.1671 87  VAL A C   
690  O O   . VAL A 87  ? 0.7234 0.8228 0.6740 0.0677  -0.0180 -0.1760 87  VAL A O   
691  C CB  . VAL A 87  ? 0.6333 0.8102 0.5954 0.0878  -0.0067 -0.1449 87  VAL A CB  
692  C CG1 . VAL A 87  ? 0.6497 0.8058 0.5951 0.1005  0.0041  -0.1591 87  VAL A CG1 
693  C CG2 . VAL A 87  ? 0.6060 0.8062 0.5886 0.0930  0.0012  -0.1253 87  VAL A CG2 
694  N N   . LYS A 88  ? 0.7174 0.8642 0.6591 0.0536  -0.0337 -0.1750 88  LYS A N   
695  C CA  . LYS A 88  ? 0.7432 0.8650 0.6600 0.0402  -0.0395 -0.1971 88  LYS A CA  
696  C C   . LYS A 88  ? 0.7472 0.8466 0.6775 0.0227  -0.0436 -0.2011 88  LYS A C   
697  O O   . LYS A 88  ? 0.7818 0.8366 0.6935 0.0186  -0.0389 -0.2147 88  LYS A O   
698  C CB  . LYS A 88  ? 0.7415 0.8923 0.6426 0.0313  -0.0522 -0.2041 88  LYS A CB  
699  C CG  . LYS A 88  ? 0.7896 0.9177 0.6548 0.0210  -0.0560 -0.2292 88  LYS A CG  
700  C CD  . LYS A 88  ? 0.8002 0.9605 0.6437 0.0216  -0.0657 -0.2342 88  LYS A CD  
701  C CE  . LYS A 88  ? 0.8090 0.9969 0.6579 -0.0004 -0.0842 -0.2437 88  LYS A CE  
702  N NZ  . LYS A 88  ? 0.8687 1.0321 0.6858 -0.0181 -0.0890 -0.2715 88  LYS A NZ  
703  N N   . LEU A 89  ? 0.7226 0.8498 0.6818 0.0125  -0.0513 -0.1896 89  LEU A N   
704  C CA  . LEU A 89  ? 0.5921 0.7029 0.5640 -0.0069 -0.0542 -0.1932 89  LEU A CA  
705  C C   . LEU A 89  ? 0.6344 0.7051 0.6107 0.0019  -0.0429 -0.1871 89  LEU A C   
706  O O   . LEU A 89  ? 0.6225 0.6519 0.5859 -0.0105 -0.0405 -0.1971 89  LEU A O   
707  C CB  . LEU A 89  ? 0.5521 0.7069 0.5554 -0.0153 -0.0635 -0.1812 89  LEU A CB  
708  C CG  . LEU A 89  ? 0.5550 0.7546 0.5555 -0.0220 -0.0772 -0.1869 89  LEU A CG  
709  C CD1 . LEU A 89  ? 0.5621 0.8062 0.5930 -0.0197 -0.0846 -0.1712 89  LEU A CD1 
710  C CD2 . LEU A 89  ? 0.5945 0.7878 0.5799 -0.0481 -0.0846 -0.2103 89  LEU A CD2 
711  N N   . LEU A 90  ? 0.6112 0.6928 0.6035 0.0226  -0.0361 -0.1708 90  LEU A N   
712  C CA  . LEU A 90  ? 0.6323 0.6815 0.6276 0.0349  -0.0267 -0.1658 90  LEU A CA  
713  C C   . LEU A 90  ? 0.7073 0.7120 0.6689 0.0450  -0.0195 -0.1813 90  LEU A C   
714  O O   . LEU A 90  ? 0.7265 0.6884 0.6782 0.0495  -0.0144 -0.1835 90  LEU A O   
715  C CB  . LEU A 90  ? 0.5999 0.6770 0.6186 0.0536  -0.0213 -0.1481 90  LEU A CB  
716  C CG  . LEU A 90  ? 0.6192 0.6765 0.6480 0.0676  -0.0141 -0.1407 90  LEU A CG  
717  C CD1 . LEU A 90  ? 0.6152 0.6569 0.6569 0.0545  -0.0179 -0.1348 90  LEU A CD1 
718  C CD2 . LEU A 90  ? 0.5909 0.6823 0.6409 0.0831  -0.0087 -0.1269 90  LEU A CD2 
719  N N   . ALA A 91  ? 0.7712 0.7823 0.7109 0.0503  -0.0188 -0.1922 91  ALA A N   
720  C CA  . ALA A 91  ? 0.8889 0.8556 0.7922 0.0608  -0.0117 -0.2091 91  ALA A CA  
721  C C   . ALA A 91  ? 0.9913 0.9131 0.8670 0.0376  -0.0161 -0.2267 91  ALA A C   
722  O O   . ALA A 91  ? 1.0461 0.9109 0.8934 0.0434  -0.0095 -0.2368 91  ALA A O   
723  C CB  . ALA A 91  ? 0.9157 0.9040 0.8022 0.0730  -0.0085 -0.2158 91  ALA A CB  
724  N N   . LYS A 92  ? 1.0241 0.9705 0.9064 0.0112  -0.0271 -0.2310 92  LYS A N   
725  C CA  . LYS A 92  ? 1.1034 1.0146 0.9639 -0.0175 -0.0313 -0.2485 92  LYS A CA  
726  C C   . LYS A 92  ? 1.1495 1.0161 1.0113 -0.0256 -0.0260 -0.2439 92  LYS A C   
727  O O   . LYS A 92  ? 1.1842 1.0025 1.0180 -0.0476 -0.0247 -0.2589 92  LYS A O   
728  C CB  . LYS A 92  ? 1.0786 1.0405 0.9562 -0.0432 -0.0450 -0.2517 92  LYS A CB  
729  N N   . GLY A 93  ? 1.1607 1.0405 1.0514 -0.0101 -0.0225 -0.2237 93  GLY A N   
730  C CA  . GLY A 93  ? 1.2127 1.0471 1.0999 -0.0108 -0.0163 -0.2175 93  GLY A CA  
731  C C   . GLY A 93  ? 1.2114 1.0552 1.1177 -0.0405 -0.0205 -0.2130 93  GLY A C   
732  O O   . GLY A 93  ? 1.1998 1.0210 1.1126 -0.0382 -0.0158 -0.2015 93  GLY A O   
733  N N   . GLU A 94  ? 1.2264 1.1060 1.1419 -0.0676 -0.0293 -0.2220 94  GLU A N   
734  C CA  . GLU A 94  ? 1.2440 1.1386 1.1783 -0.0979 -0.0324 -0.2206 94  GLU A CA  
735  C C   . GLU A 94  ? 1.1653 1.1309 1.1459 -0.0915 -0.0393 -0.2034 94  GLU A C   
736  O O   . GLU A 94  ? 1.1383 1.1550 1.1320 -0.0860 -0.0479 -0.2036 94  GLU A O   
737  C CB  . GLU A 94  ? 1.3203 1.2160 1.2382 -0.1334 -0.0380 -0.2429 94  GLU A CB  
738  C CG  . GLU A 94  ? 1.3946 1.2507 1.3009 -0.1678 -0.0321 -0.2497 94  GLU A CG  
739  C CD  . GLU A 94  ? 1.3849 1.2664 1.3266 -0.1711 -0.0299 -0.2312 94  GLU A CD  
740  O OE1 . GLU A 94  ? 1.4177 1.2462 1.3457 -0.1658 -0.0196 -0.2219 94  GLU A OE1 
741  O OE2 . GLU A 94  ? 1.3455 1.2991 1.3260 -0.1766 -0.0385 -0.2259 94  GLU A OE2 
742  N N   . TYR A 95  ? 1.0887 1.0523 1.0892 -0.0910 -0.0352 -0.1885 95  TYR A N   
743  C CA  . TYR A 95  ? 0.9769 0.9962 1.0174 -0.0870 -0.0398 -0.1724 95  TYR A CA  
744  C C   . TYR A 95  ? 0.9345 0.9279 0.9808 -0.0973 -0.0326 -0.1640 95  TYR A C   
745  O O   . TYR A 95  ? 0.9879 0.9195 1.0059 -0.1003 -0.0243 -0.1674 95  TYR A O   
746  C CB  . TYR A 95  ? 0.9371 0.9800 0.9919 -0.0549 -0.0402 -0.1572 95  TYR A CB  
747  C CG  . TYR A 95  ? 0.9512 0.9497 0.9914 -0.0326 -0.0311 -0.1512 95  TYR A CG  
748  C CD1 . TYR A 95  ? 0.9790 0.9540 0.9940 -0.0168 -0.0278 -0.1597 95  TYR A CD1 
749  C CD2 . TYR A 95  ? 0.9403 0.9231 0.9911 -0.0259 -0.0262 -0.1378 95  TYR A CD2 
750  C CE1 . TYR A 95  ? 0.9972 0.9388 1.0009 0.0066  -0.0201 -0.1552 95  TYR A CE1 
751  C CE2 . TYR A 95  ? 0.9562 0.9045 0.9943 -0.0034 -0.0197 -0.1330 95  TYR A CE2 
752  C CZ  . TYR A 95  ? 0.9906 0.9204 1.0064 0.0136  -0.0168 -0.1418 95  TYR A CZ  
753  O OH  . TYR A 95  ? 1.0110 0.9134 1.0164 0.0391  -0.0109 -0.1376 95  TYR A OH  
754  N N   . GLN A 96  ? 0.8394 0.8769 0.9186 -0.1008 -0.0354 -0.1526 96  GLN A N   
755  C CA  . GLN A 96  ? 0.7848 0.8017 0.8691 -0.1115 -0.0281 -0.1445 96  GLN A CA  
756  C C   . GLN A 96  ? 0.7002 0.7260 0.8032 -0.0858 -0.0263 -0.1245 96  GLN A C   
757  O O   . GLN A 96  ? 0.6582 0.7257 0.7818 -0.0683 -0.0319 -0.1163 96  GLN A O   
758  C CB  . GLN A 96  ? 0.7754 0.8329 0.8803 -0.1413 -0.0304 -0.1502 96  GLN A CB  
759  C CG  . GLN A 96  ? 0.8195 0.8634 0.9038 -0.1735 -0.0308 -0.1719 96  GLN A CG  
760  C CD  . GLN A 96  ? 0.8253 0.8990 0.9266 -0.2084 -0.0289 -0.1784 96  GLN A CD  
761  O OE1 . GLN A 96  ? 0.7854 0.9065 0.9195 -0.2054 -0.0300 -0.1678 96  GLN A OE1 
762  N NE2 . GLN A 96  ? 0.8771 0.9230 0.9552 -0.2428 -0.0251 -0.1968 96  GLN A NE2 
763  N N   . LYS A 97  ? 0.6814 0.6639 0.7728 -0.0843 -0.0182 -0.1171 97  LYS A N   
764  C CA  . LYS A 97  ? 0.6084 0.5922 0.7123 -0.0614 -0.0165 -0.1000 97  LYS A CA  
765  C C   . LYS A 97  ? 0.5639 0.5706 0.6892 -0.0735 -0.0146 -0.0912 97  LYS A C   
766  O O   . LYS A 97  ? 0.6015 0.5898 0.7179 -0.0975 -0.0090 -0.0957 97  LYS A O   
767  C CB  . LYS A 97  ? 0.6337 0.5560 0.7080 -0.0462 -0.0101 -0.0973 97  LYS A CB  
768  C CG  . LYS A 97  ? 0.6393 0.5460 0.6964 -0.0256 -0.0112 -0.1040 97  LYS A CG  
769  C CD  . LYS A 97  ? 0.6678 0.5218 0.6987 -0.0033 -0.0059 -0.1001 97  LYS A CD  
770  C CE  . LYS A 97  ? 0.7340 0.5202 0.7205 -0.0122 0.0000  -0.1125 97  LYS A CE  
771  N NZ  . LYS A 97  ? 0.7734 0.5108 0.7308 0.0182  0.0037  -0.1103 97  LYS A NZ  
772  N N   . VAL A 98  ? 0.5047 0.5504 0.6560 -0.0580 -0.0183 -0.0792 98  VAL A N   
773  C CA  . VAL A 98  ? 0.4688 0.5356 0.6392 -0.0638 -0.0161 -0.0700 98  VAL A CA  
774  C C   . VAL A 98  ? 0.4665 0.5186 0.6377 -0.0420 -0.0143 -0.0559 98  VAL A C   
775  O O   . VAL A 98  ? 0.4564 0.5090 0.6274 -0.0218 -0.0173 -0.0525 98  VAL A O   
776  C CB  . VAL A 98  ? 0.4079 0.5369 0.6069 -0.0660 -0.0226 -0.0700 98  VAL A CB  
777  C CG1 . VAL A 98  ? 0.3982 0.5480 0.5969 -0.0873 -0.0262 -0.0856 98  VAL A CG1 
778  C CG2 . VAL A 98  ? 0.3850 0.5358 0.5928 -0.0420 -0.0287 -0.0629 98  VAL A CG2 
779  N N   . SER A 99  ? 0.4715 0.5125 0.6431 -0.0477 -0.0089 -0.0487 99  SER A N   
780  C CA  . SER A 99  ? 0.4527 0.4745 0.6199 -0.0299 -0.0073 -0.0369 99  SER A CA  
781  C C   . SER A 99  ? 0.3910 0.4450 0.5797 -0.0287 -0.0072 -0.0279 99  SER A C   
782  O O   . SER A 99  ? 0.3789 0.4468 0.5749 -0.0454 -0.0030 -0.0290 99  SER A O   
783  C CB  . SER A 99  ? 0.5288 0.4938 0.6655 -0.0339 -0.0004 -0.0358 99  SER A CB  
784  O OG  . SER A 99  ? 0.5785 0.5076 0.6906 -0.0342 0.0003  -0.0452 99  SER A OG  
785  N N   . TYR A 100 ? 0.3658 0.4318 0.5637 -0.0096 -0.0110 -0.0198 100 TYR A N   
786  C CA  . TYR A 100 ? 0.3457 0.4339 0.5584 -0.0053 -0.0108 -0.0114 100 TYR A CA  
787  C C   . TYR A 100 ? 0.3607 0.4215 0.5613 0.0036  -0.0086 -0.0035 100 TYR A C   
788  O O   . TYR A 100 ? 0.3551 0.3922 0.5425 0.0149  -0.0105 -0.0030 100 TYR A O   
789  C CB  . TYR A 100 ? 0.3291 0.4481 0.5569 0.0072  -0.0164 -0.0087 100 TYR A CB  
790  C CG  . TYR A 100 ? 0.3510 0.5035 0.5909 0.0019  -0.0195 -0.0138 100 TYR A CG  
791  C CD1 . TYR A 100 ? 0.3771 0.5376 0.6179 -0.0149 -0.0184 -0.0225 100 TYR A CD1 
792  C CD2 . TYR A 100 ? 0.3461 0.5217 0.5939 0.0132  -0.0237 -0.0102 100 TYR A CD2 
793  C CE1 . TYR A 100 ? 0.3718 0.5691 0.6242 -0.0182 -0.0232 -0.0282 100 TYR A CE1 
794  C CE2 . TYR A 100 ? 0.3486 0.5543 0.6037 0.0121  -0.0278 -0.0141 100 TYR A CE2 
795  C CZ  . TYR A 100 ? 0.3718 0.5919 0.6308 -0.0026 -0.0285 -0.0234 100 TYR A CZ  
796  O OH  . TYR A 100 ? 0.3943 0.6507 0.6614 -0.0024 -0.0344 -0.0283 100 TYR A OH  
797  N N   . PRO A 101 ? 0.3729 0.4384 0.5768 0.0002  -0.0049 0.0023  101 PRO A N   
798  C CA  . PRO A 101 ? 0.3822 0.4228 0.5720 0.0089  -0.0037 0.0096  101 PRO A CA  
799  C C   . PRO A 101 ? 0.3790 0.4317 0.5763 0.0256  -0.0103 0.0133  101 PRO A C   
800  O O   . PRO A 101 ? 0.3678 0.4477 0.5810 0.0284  -0.0132 0.0127  101 PRO A O   
801  C CB  . PRO A 101 ? 0.3627 0.4112 0.5553 -0.0008 0.0029  0.0133  101 PRO A CB  
802  C CG  . PRO A 101 ? 0.3644 0.4380 0.5706 -0.0172 0.0064  0.0065  101 PRO A CG  
803  C CD  . PRO A 101 ? 0.3595 0.4538 0.5780 -0.0114 -0.0011 0.0014  101 PRO A CD  
804  N N   . LEU A 102 ? 0.3943 0.4258 0.5775 0.0363  -0.0124 0.0169  102 LEU A N   
805  C CA  . LEU A 102 ? 0.3725 0.4177 0.5623 0.0493  -0.0186 0.0189  102 LEU A CA  
806  C C   . LEU A 102 ? 0.3532 0.3902 0.5341 0.0527  -0.0189 0.0247  102 LEU A C   
807  O O   . LEU A 102 ? 0.3645 0.3782 0.5288 0.0488  -0.0144 0.0280  102 LEU A O   
808  C CB  . LEU A 102 ? 0.3908 0.4286 0.5743 0.0624  -0.0232 0.0157  102 LEU A CB  
809  C CG  . LEU A 102 ? 0.3984 0.4399 0.5856 0.0610  -0.0226 0.0090  102 LEU A CG  
810  C CD1 . LEU A 102 ? 0.4102 0.4406 0.5871 0.0774  -0.0258 0.0057  102 LEU A CD1 
811  C CD2 . LEU A 102 ? 0.3639 0.4389 0.5715 0.0569  -0.0236 0.0073  102 LEU A CD2 
812  N N   . LEU A 103 ? 0.3254 0.3805 0.5151 0.0583  -0.0236 0.0255  103 LEU A N   
813  C CA  . LEU A 103 ? 0.3064 0.3565 0.4871 0.0615  -0.0253 0.0292  103 LEU A CA  
814  C C   . LEU A 103 ? 0.3276 0.3764 0.5007 0.0746  -0.0333 0.0286  103 LEU A C   
815  O O   . LEU A 103 ? 0.3172 0.3835 0.5012 0.0805  -0.0377 0.0244  103 LEU A O   
816  C CB  . LEU A 103 ? 0.2787 0.3470 0.4705 0.0571  -0.0251 0.0291  103 LEU A CB  
817  C CG  . LEU A 103 ? 0.2949 0.3581 0.4760 0.0590  -0.0271 0.0310  103 LEU A CG  
818  C CD1 . LEU A 103 ? 0.2961 0.3398 0.4613 0.0570  -0.0211 0.0353  103 LEU A CD1 
819  C CD2 . LEU A 103 ? 0.2432 0.3182 0.4317 0.0545  -0.0266 0.0295  103 LEU A CD2 
820  N N   . LYS A 104 ? 0.3678 0.3989 0.5216 0.0803  -0.0351 0.0325  104 LYS A N   
821  C CA  . LYS A 104 ? 0.3815 0.4154 0.5263 0.0957  -0.0445 0.0319  104 LYS A CA  
822  C C   . LYS A 104 ? 0.3842 0.4315 0.5285 0.0940  -0.0492 0.0317  104 LYS A C   
823  O O   . LYS A 104 ? 0.3171 0.3488 0.4487 0.0881  -0.0446 0.0354  104 LYS A O   
824  C CB  . LYS A 104 ? 0.3521 0.3491 0.4670 0.1070  -0.0442 0.0369  104 LYS A CB  
825  C CG  . LYS A 104 ? 0.4526 0.4549 0.5569 0.1287  -0.0555 0.0363  104 LYS A CG  
826  C CD  . LYS A 104 ? 0.5063 0.4633 0.5720 0.1425  -0.0551 0.0433  104 LYS A CD  
827  C CE  . LYS A 104 ? 0.5530 0.5196 0.6084 0.1696  -0.0680 0.0422  104 LYS A CE  
828  N NZ  . LYS A 104 ? 0.6338 0.5499 0.6440 0.1866  -0.0682 0.0506  104 LYS A NZ  
829  N N   . THR A 105 ? 0.3831 0.4606 0.5407 0.0979  -0.0576 0.0261  105 THR A N   
830  C CA  . THR A 105 ? 0.3682 0.4599 0.5239 0.0950  -0.0637 0.0234  105 THR A CA  
831  C C   . THR A 105 ? 0.3984 0.5047 0.5470 0.1120  -0.0759 0.0211  105 THR A C   
832  O O   . THR A 105 ? 0.4021 0.5312 0.5637 0.1218  -0.0807 0.0170  105 THR A O   
833  C CB  . THR A 105 ? 0.3255 0.4433 0.5024 0.0805  -0.0627 0.0174  105 THR A CB  
834  O OG1 . THR A 105 ? 0.2637 0.3684 0.4452 0.0698  -0.0524 0.0202  105 THR A OG1 
835  C CG2 . THR A 105 ? 0.3098 0.4353 0.4800 0.0738  -0.0679 0.0133  105 THR A CG2 
836  N N   . THR A 106 ? 0.4241 0.5187 0.5507 0.1175  -0.0811 0.0234  106 THR A N   
837  C CA  . THR A 106 ? 0.4285 0.5399 0.5454 0.1356  -0.0948 0.0210  106 THR A CA  
838  C C   . THR A 106 ? 0.4450 0.5796 0.5632 0.1260  -0.1023 0.0144  106 THR A C   
839  O O   . THR A 106 ? 0.4741 0.5860 0.5761 0.1163  -0.0977 0.0169  106 THR A O   
840  C CB  . THR A 106 ? 0.4381 0.5092 0.5188 0.1539  -0.0956 0.0303  106 THR A CB  
841  O OG1 . THR A 106 ? 0.4399 0.4851 0.5164 0.1603  -0.0882 0.0349  106 THR A OG1 
842  C CG2 . THR A 106 ? 0.4548 0.5447 0.5225 0.1770  -0.1116 0.0283  106 THR A CG2 
843  N N   . VAL A 107 ? 0.4158 0.5972 0.5531 0.1278  -0.1132 0.0049  107 VAL A N   
844  C CA  . VAL A 107 ? 0.4309 0.6399 0.5714 0.1151  -0.1212 -0.0044 107 VAL A CA  
845  C C   . VAL A 107 ? 0.4575 0.6933 0.5877 0.1361  -0.1384 -0.0078 107 VAL A C   
846  O O   . VAL A 107 ? 0.4563 0.7161 0.5956 0.1566  -0.1452 -0.0086 107 VAL A O   
847  C CB  . VAL A 107 ? 0.4270 0.6737 0.5994 0.0936  -0.1188 -0.0145 107 VAL A CB  
848  C CG1 . VAL A 107 ? 0.3370 0.6060 0.5086 0.0757  -0.1259 -0.0254 107 VAL A CG1 
849  C CG2 . VAL A 107 ? 0.4173 0.6357 0.5959 0.0783  -0.1029 -0.0097 107 VAL A CG2 
850  N N   . LYS A 108 ? 0.4815 0.7137 0.5911 0.1331  -0.1457 -0.0104 108 LYS A N   
851  C CA  . LYS A 108 ? 0.5321 0.7869 0.6256 0.1548  -0.1634 -0.0130 108 LYS A CA  
852  C C   . LYS A 108 ? 0.5622 0.8645 0.6674 0.1381  -0.1752 -0.0282 108 LYS A C   
853  O O   . LYS A 108 ? 0.5540 0.8444 0.6584 0.1113  -0.1685 -0.0333 108 LYS A O   
854  C CB  . LYS A 108 ? 0.5703 0.7730 0.6191 0.1694  -0.1625 -0.0012 108 LYS A CB  
855  C CG  . LYS A 108 ? 0.5906 0.7515 0.6226 0.1896  -0.1547 0.0124  108 LYS A CG  
856  C CD  . LYS A 108 ? 0.6454 0.7483 0.6332 0.1946  -0.1478 0.0246  108 LYS A CD  
857  C CE  . LYS A 108 ? 0.6849 0.7454 0.6498 0.2152  -0.1419 0.0371  108 LYS A CE  
858  N NZ  . LYS A 108 ? 0.7392 0.7488 0.6533 0.2258  -0.1393 0.0487  108 LYS A NZ  
859  N N   . TYR A 109 ? 0.6000 0.9560 0.7144 0.1547  -0.1929 -0.0363 109 TYR A N   
860  C CA  . TYR A 109 ? 0.6254 1.0360 0.7529 0.1379  -0.2060 -0.0530 109 TYR A CA  
861  C C   . TYR A 109 ? 0.6806 1.1022 0.7784 0.1595  -0.2252 -0.0545 109 TYR A C   
862  O O   . TYR A 109 ? 0.7195 1.0874 0.7772 0.1738  -0.2233 -0.0426 109 TYR A O   
863  C CB  . TYR A 109 ? 0.6193 1.1029 0.7911 0.1336  -0.2112 -0.0655 109 TYR A CB  
864  C CG  . TYR A 109 ? 0.6003 1.0730 0.7977 0.1191  -0.1930 -0.0621 109 TYR A CG  
865  C CD1 . TYR A 109 ? 0.5906 1.0654 0.8045 0.0814  -0.1818 -0.0696 109 TYR A CD1 
866  C CD2 . TYR A 109 ? 0.5992 1.0561 0.7996 0.1435  -0.1872 -0.0517 109 TYR A CD2 
867  C CE1 . TYR A 109 ? 0.5828 1.0468 0.8159 0.0699  -0.1659 -0.0658 109 TYR A CE1 
868  C CE2 . TYR A 109 ? 0.5866 1.0347 0.8078 0.1310  -0.1716 -0.0493 109 TYR A CE2 
869  C CZ  . TYR A 109 ? 0.5849 1.0381 0.8227 0.0949  -0.1613 -0.0559 109 TYR A CZ  
870  O OH  . TYR A 109 ? 0.5781 1.0214 0.8328 0.0842  -0.1463 -0.0527 109 TYR A OH  
871  N N   . GLY A 110 ? 0.6876 1.1810 0.8039 0.1615  -0.2435 -0.0696 110 GLY A N   
872  C CA  . GLY A 110 ? 0.6961 1.2050 0.7843 0.1796  -0.2626 -0.0728 110 GLY A CA  
873  C C   . GLY A 110 ? 0.7138 1.2852 0.8246 0.1817  -0.2703 -0.0837 110 GLY A C   
874  O O   . GLY A 110 ? 0.7501 1.3238 0.8473 0.2138  -0.2757 -0.0774 110 GLY A O   
875  N N   . LYS A 114 ? 0.7014 1.1968 0.8689 0.2164  -0.2151 -0.0492 114 LYS A N   
876  C CA  . LYS A 114 ? 0.7198 1.1593 0.8590 0.2463  -0.2094 -0.0341 114 LYS A CA  
877  C C   . LYS A 114 ? 0.6878 1.0715 0.8170 0.2391  -0.1986 -0.0234 114 LYS A C   
878  O O   . LYS A 114 ? 0.6973 1.0512 0.8073 0.2274  -0.1987 -0.0200 114 LYS A O   
879  C CB  . LYS A 114 ? 0.7207 1.1778 0.8765 0.2600  -0.2027 -0.0356 114 LYS A CB  
880  N N   . GLU A 115 ? 0.6375 1.0012 0.7766 0.2425  -0.1859 -0.0184 115 GLU A N   
881  C CA  . GLU A 115 ? 0.5826 0.8881 0.7104 0.2343  -0.1722 -0.0079 115 GLU A CA  
882  C C   . GLU A 115 ? 0.5439 0.8611 0.7027 0.2246  -0.1604 -0.0108 115 GLU A C   
883  O O   . GLU A 115 ? 0.5701 0.8919 0.7308 0.2425  -0.1585 -0.0108 115 GLU A O   
884  C CB  . GLU A 115 ? 0.6114 0.8515 0.6935 0.2603  -0.1704 0.0066  115 GLU A CB  
885  C CG  . GLU A 115 ? 0.6094 0.7870 0.6648 0.2412  -0.1573 0.0168  115 GLU A CG  
886  C CD  . GLU A 115 ? 0.6232 0.7333 0.6426 0.2562  -0.1477 0.0304  115 GLU A CD  
887  O OE1 . GLU A 115 ? 0.6024 0.7036 0.6303 0.2634  -0.1415 0.0311  115 GLU A OE1 
888  O OE2 . GLU A 115 ? 0.6429 0.7071 0.6230 0.2594  -0.1454 0.0399  115 GLU A OE2 
889  N N   . ALA A 116 ? 0.4948 0.8056 0.6705 0.1917  -0.1480 -0.0125 116 ALA A N   
890  C CA  . ALA A 116 ? 0.4341 0.7510 0.6350 0.1796  -0.1358 -0.0143 116 ALA A CA  
891  C C   . ALA A 116 ? 0.4384 0.6939 0.6234 0.1684  -0.1210 -0.0039 116 ALA A C   
892  O O   . ALA A 116 ? 0.4484 0.6751 0.6197 0.1526  -0.1166 0.0002  116 ALA A O   
893  C CB  . ALA A 116 ? 0.3839 0.7481 0.6171 0.1505  -0.1336 -0.0254 116 ALA A CB  
894  N N   . THR A 117 ? 0.4333 0.6717 0.6202 0.1768  -0.1134 -0.0008 117 THR A N   
895  C CA  . THR A 117 ? 0.4183 0.6070 0.5938 0.1655  -0.1000 0.0070  117 THR A CA  
896  C C   . THR A 117 ? 0.3794 0.5845 0.5809 0.1500  -0.0908 0.0029  117 THR A C   
897  O O   . THR A 117 ? 0.3807 0.6263 0.6036 0.1548  -0.0930 -0.0045 117 THR A O   
898  C CB  . THR A 117 ? 0.4467 0.5889 0.5926 0.1868  -0.0982 0.0146  117 THR A CB  
899  O OG1 . THR A 117 ? 0.4621 0.6231 0.6154 0.2080  -0.1017 0.0099  117 THR A OG1 
900  C CG2 . THR A 117 ? 0.4698 0.5868 0.5824 0.2022  -0.1058 0.0210  117 THR A CG2 
901  N N   . TYR A 118 ? 0.3791 0.5551 0.5781 0.1322  -0.0802 0.0075  118 TYR A N   
902  C CA  . TYR A 118 ? 0.3469 0.5335 0.5652 0.1181  -0.0717 0.0049  118 TYR A CA  
903  C C   . TYR A 118 ? 0.3652 0.5118 0.5719 0.1129  -0.0625 0.0109  118 TYR A C   
904  O O   . TYR A 118 ? 0.3960 0.5110 0.5843 0.1112  -0.0604 0.0169  118 TYR A O   
905  C CB  . TYR A 118 ? 0.3162 0.5237 0.5491 0.0961  -0.0693 0.0016  118 TYR A CB  
906  C CG  . TYR A 118 ? 0.2475 0.4969 0.4924 0.0943  -0.0778 -0.0062 118 TYR A CG  
907  C CD1 . TYR A 118 ? 0.2377 0.5312 0.5053 0.0930  -0.0782 -0.0140 118 TYR A CD1 
908  C CD2 . TYR A 118 ? 0.2594 0.5075 0.4931 0.0925  -0.0850 -0.0069 118 TYR A CD2 
909  C CE1 . TYR A 118 ? 0.2834 0.6226 0.5650 0.0883  -0.0857 -0.0228 118 TYR A CE1 
910  C CE2 . TYR A 118 ? 0.2615 0.5522 0.5068 0.0884  -0.0938 -0.0159 118 TYR A CE2 
911  C CZ  . TYR A 118 ? 0.2899 0.6281 0.5606 0.0855  -0.0941 -0.0241 118 TYR A CZ  
912  O OH  . TYR A 118 ? 0.2936 0.6814 0.5787 0.0785  -0.1026 -0.0347 118 TYR A OH  
913  N N   . LEU A 119 ? 0.3495 0.5013 0.5673 0.1093  -0.0568 0.0086  119 LEU A N   
914  C CA  . LEU A 119 ? 0.2556 0.3802 0.4673 0.1010  -0.0488 0.0118  119 LEU A CA  
915  C C   . LEU A 119 ? 0.2922 0.4318 0.5191 0.0846  -0.0436 0.0110  119 LEU A C   
916  O O   . LEU A 119 ? 0.2750 0.4422 0.5162 0.0817  -0.0435 0.0069  119 LEU A O   
917  C CB  . LEU A 119 ? 0.3621 0.4742 0.5674 0.1121  -0.0472 0.0091  119 LEU A CB  
918  C CG  . LEU A 119 ? 0.3848 0.4529 0.5673 0.1120  -0.0429 0.0126  119 LEU A CG  
919  C CD1 . LEU A 119 ? 0.3160 0.3605 0.4786 0.1164  -0.0452 0.0188  119 LEU A CD1 
920  C CD2 . LEU A 119 ? 0.4068 0.4580 0.5771 0.1262  -0.0425 0.0085  119 LEU A CD2 
921  N N   . ALA A 120 ? 0.2833 0.4055 0.5055 0.0745  -0.0387 0.0152  120 ALA A N   
922  C CA  . ALA A 120 ? 0.2713 0.4025 0.5020 0.0630  -0.0343 0.0159  120 ALA A CA  
923  C C   . ALA A 120 ? 0.2944 0.4164 0.5246 0.0593  -0.0297 0.0167  120 ALA A C   
924  O O   . ALA A 120 ? 0.3344 0.4391 0.5564 0.0589  -0.0280 0.0183  120 ALA A O   
925  C CB  . ALA A 120 ? 0.2612 0.3862 0.4869 0.0566  -0.0337 0.0190  120 ALA A CB  
926  N N   . LEU A 121 ? 0.3403 0.3537 0.4478 0.0753  0.0376  -0.0098 121 LEU A N   
927  C CA  . LEU A 121 ? 0.3578 0.3518 0.4464 0.0711  0.0363  -0.0117 121 LEU A CA  
928  C C   . LEU A 121 ? 0.3663 0.3571 0.4471 0.0611  0.0319  -0.0059 121 LEU A C   
929  O O   . LEU A 121 ? 0.3609 0.3390 0.4328 0.0585  0.0259  -0.0060 121 LEU A O   
930  C CB  . LEU A 121 ? 0.3697 0.3643 0.4470 0.0729  0.0451  -0.0187 121 LEU A CB  
931  C CG  . LEU A 121 ? 0.3632 0.3388 0.4190 0.0701  0.0428  -0.0226 121 LEU A CG  
932  C CD1 . LEU A 121 ? 0.3561 0.3134 0.4101 0.0738  0.0364  -0.0263 121 LEU A CD1 
933  C CD2 . LEU A 121 ? 0.3811 0.3580 0.4230 0.0721  0.0524  -0.0293 121 LEU A CD2 
934  N N   . ASN A 122 ? 0.3749 0.3772 0.4589 0.0555  0.0347  -0.0018 122 ASN A N   
935  C CA  . ASN A 122 ? 0.3893 0.3853 0.4646 0.0486  0.0300  0.0037  122 ASN A CA  
936  C C   . ASN A 122 ? 0.3952 0.3958 0.4830 0.0477  0.0239  0.0085  122 ASN A C   
937  O O   . ASN A 122 ? 0.3930 0.3863 0.4799 0.0483  0.0173  0.0100  122 ASN A O   
938  C CB  . ASN A 122 ? 0.4010 0.3983 0.4653 0.0418  0.0367  0.0058  122 ASN A CB  
939  C CG  . ASN A 122 ? 0.4219 0.4065 0.4632 0.0417  0.0392  0.0035  122 ASN A CG  
940  O OD1 . ASN A 122 ? 0.4073 0.3832 0.4414 0.0459  0.0336  0.0002  122 ASN A OD1 
941  N ND2 . ASN A 122 ? 0.4551 0.4379 0.4828 0.0358  0.0475  0.0053  122 ASN A ND2 
942  N N   . GLU A 123 ? 0.4004 0.4146 0.4998 0.0454  0.0264  0.0102  123 GLU A N   
943  C CA  . GLU A 123 ? 0.4141 0.4316 0.5216 0.0441  0.0203  0.0142  123 GLU A CA  
944  C C   . GLU A 123 ? 0.4177 0.4549 0.5414 0.0433  0.0223  0.0134  123 GLU A C   
945  O O   . GLU A 123 ? 0.4241 0.4746 0.5534 0.0416  0.0297  0.0099  123 GLU A O   
946  C CB  . GLU A 123 ? 0.4196 0.4271 0.5150 0.0379  0.0174  0.0180  123 GLU A CB  
947  C CG  . GLU A 123 ? 0.4309 0.4385 0.5195 0.0295  0.0230  0.0190  123 GLU A CG  
948  C CD  . GLU A 123 ? 0.4445 0.4466 0.5197 0.0276  0.0305  0.0173  123 GLU A CD  
949  O OE1 . GLU A 123 ? 0.4499 0.4656 0.5328 0.0252  0.0386  0.0142  123 GLU A OE1 
950  O OE2 . GLU A 123 ? 0.4578 0.4438 0.5146 0.0292  0.0282  0.0185  123 GLU A OE2 
951  N N   . SER A 124 ? 0.4037 0.4449 0.5350 0.0445  0.0157  0.0160  124 SER A N   
952  C CA  . SER A 124 ? 0.3780 0.4394 0.5240 0.0424  0.0146  0.0150  124 SER A CA  
953  C C   . SER A 124 ? 0.3446 0.4003 0.4846 0.0344  0.0101  0.0182  124 SER A C   
954  O O   . SER A 124 ? 0.3483 0.3900 0.4796 0.0368  0.0049  0.0215  124 SER A O   
955  C CB  . SER A 124 ? 0.3966 0.4679 0.5550 0.0541  0.0092  0.0144  124 SER A CB  
956  O OG  . SER A 124 ? 0.3995 0.4924 0.5718 0.0527  0.0054  0.0130  124 SER A OG  
957  N N   . THR A 125 ? 0.3342 0.4001 0.4781 0.0243  0.0128  0.0164  125 THR A N   
958  C CA  . THR A 125 ? 0.3228 0.3793 0.4581 0.0160  0.0091  0.0182  125 THR A CA  
959  C C   . THR A 125 ? 0.3563 0.4350 0.5069 0.0108  0.0057  0.0148  125 THR A C   
960  O O   . THR A 125 ? 0.3924 0.4965 0.5608 0.0099  0.0089  0.0105  125 THR A O   
961  C CB  . THR A 125 ? 0.3321 0.3704 0.4496 0.0055  0.0152  0.0193  125 THR A CB  
962  O OG1 . THR A 125 ? 0.3503 0.4028 0.4749 -0.0057 0.0232  0.0161  125 THR A OG1 
963  C CG2 . THR A 125 ? 0.3390 0.3607 0.4424 0.0116  0.0178  0.0215  125 THR A CG2 
964  N N   . VAL A 126 ? 0.3479 0.4192 0.4923 0.0079  -0.0011 0.0156  126 VAL A N   
965  C CA  . VAL A 126 ? 0.3285 0.4191 0.4844 0.0018  -0.0063 0.0115  126 VAL A CA  
966  C C   . VAL A 126 ? 0.3722 0.4468 0.5142 -0.0132 -0.0053 0.0102  126 VAL A C   
967  O O   . VAL A 126 ? 0.4042 0.4509 0.5258 -0.0120 -0.0061 0.0134  126 VAL A O   
968  C CB  . VAL A 126 ? 0.2773 0.3726 0.4355 0.0129  -0.0169 0.0129  126 VAL A CB  
969  C CG1 . VAL A 126 ? 0.2703 0.3918 0.4429 0.0083  -0.0238 0.0074  126 VAL A CG1 
970  C CG2 . VAL A 126 ? 0.2585 0.3570 0.4223 0.0280  -0.0176 0.0157  126 VAL A CG2 
971  N N   . LYS A 127 ? 0.3832 0.4756 0.5360 -0.0272 -0.0033 0.0047  127 LYS A N   
972  C CA  . LYS A 127 ? 0.4066 0.4833 0.5463 -0.0436 -0.0034 0.0021  127 LYS A CA  
973  C C   . LYS A 127 ? 0.4308 0.5393 0.5904 -0.0528 -0.0093 -0.0056 127 LYS A C   
974  O O   . LYS A 127 ? 0.4288 0.5737 0.6136 -0.0472 -0.0111 -0.0089 127 LYS A O   
975  C CB  . LYS A 127 ? 0.4233 0.4812 0.5493 -0.0581 0.0083  0.0033  127 LYS A CB  
976  C CG  . LYS A 127 ? 0.4285 0.4574 0.5342 -0.0480 0.0125  0.0102  127 LYS A CG  
977  C CD  . LYS A 127 ? 0.4500 0.4631 0.5413 -0.0608 0.0243  0.0120  127 LYS A CD  
978  C CE  . LYS A 127 ? 0.4762 0.4655 0.5486 -0.0487 0.0268  0.0181  127 LYS A CE  
979  N NZ  . LYS A 127 ? 0.4974 0.4685 0.5509 -0.0602 0.0380  0.0208  127 LYS A NZ  
980  N N   . SER A 128 ? 0.4546 0.5495 0.6023 -0.0658 -0.0131 -0.0093 128 SER A N   
981  C CA  . SER A 128 ? 0.4950 0.6211 0.6610 -0.0769 -0.0198 -0.0182 128 SER A CA  
982  C C   . SER A 128 ? 0.5476 0.6951 0.7291 -0.0980 -0.0098 -0.0238 128 SER A C   
983  O O   . SER A 128 ? 0.5528 0.6785 0.7210 -0.1080 0.0025  -0.0203 128 SER A O   
984  C CB  . SER A 128 ? 0.5160 0.6191 0.6623 -0.0847 -0.0277 -0.0218 128 SER A CB  
985  O OG  . SER A 128 ? 0.5460 0.6281 0.6789 -0.1080 -0.0207 -0.0254 128 SER A OG  
986  N N   . SER A 129 ? 0.5678 0.7603 0.7775 -0.1046 -0.0152 -0.0327 129 SER A N   
987  C CA  . SER A 129 ? 0.5859 0.8090 0.8162 -0.1265 -0.0054 -0.0401 129 SER A CA  
988  C C   . SER A 129 ? 0.6304 0.8341 0.8461 -0.1552 -0.0038 -0.0459 129 SER A C   
989  O O   . SER A 129 ? 0.6413 0.8795 0.8777 -0.1727 -0.0073 -0.0566 129 SER A O   
990  C CB  . SER A 129 ? 0.5635 0.8490 0.8338 -0.1194 -0.0124 -0.0485 129 SER A CB  
991  O OG  . SER A 129 ? 0.5698 0.8731 0.8473 -0.1249 -0.0270 -0.0566 129 SER A OG  
992  N N   . GLY A 130 ? 0.6657 0.8126 0.8444 -0.1598 0.0013  -0.0391 130 GLY A N   
993  C CA  . GLY A 130 ? 0.7223 0.8377 0.8787 -0.1832 0.0011  -0.0437 130 GLY A CA  
994  C C   . GLY A 130 ? 0.7349 0.8434 0.8835 -0.1751 -0.0153 -0.0481 130 GLY A C   
995  O O   . GLY A 130 ? 0.7308 0.8812 0.9042 -0.1655 -0.0269 -0.0533 130 GLY A O   
996  N N   . GLY A 131 ? 0.7175 0.7725 0.8296 -0.1774 -0.0166 -0.0460 131 GLY A N   
997  C CA  . GLY A 131 ? 0.6972 0.7408 0.7969 -0.1671 -0.0305 -0.0495 131 GLY A CA  
998  C C   . GLY A 131 ? 0.6506 0.6735 0.7358 -0.1378 -0.0332 -0.0398 131 GLY A C   
999  O O   . GLY A 131 ? 0.6512 0.6736 0.7398 -0.1253 -0.0260 -0.0311 131 GLY A O   
1000 N N   . PRO A 132 ? 0.6255 0.6324 0.6941 -0.1274 -0.0433 -0.0419 132 PRO A N   
1001 C CA  . PRO A 132 ? 0.5834 0.5696 0.6367 -0.1024 -0.0441 -0.0336 132 PRO A CA  
1002 C C   . PRO A 132 ? 0.5263 0.5480 0.6035 -0.0836 -0.0464 -0.0278 132 PRO A C   
1003 O O   . PRO A 132 ? 0.5043 0.5652 0.6048 -0.0832 -0.0536 -0.0316 132 PRO A O   
1004 C CB  . PRO A 132 ? 0.6027 0.5706 0.6350 -0.0990 -0.0538 -0.0396 132 PRO A CB  
1005 C CG  . PRO A 132 ? 0.6133 0.6098 0.6601 -0.1161 -0.0622 -0.0505 132 PRO A CG  
1006 C CD  . PRO A 132 ? 0.6229 0.6313 0.6855 -0.1389 -0.0539 -0.0530 132 PRO A CD  
1007 N N   . PHE A 133 ? 0.4940 0.5005 0.5641 -0.0677 -0.0410 -0.0188 133 PHE A N   
1008 C CA  . PHE A 133 ? 0.4527 0.4830 0.5398 -0.0501 -0.0419 -0.0127 133 PHE A CA  
1009 C C   . PHE A 133 ? 0.4561 0.4765 0.5296 -0.0339 -0.0480 -0.0100 133 PHE A C   
1010 O O   . PHE A 133 ? 0.4585 0.4507 0.5124 -0.0270 -0.0446 -0.0071 133 PHE A O   
1011 C CB  . PHE A 133 ? 0.4149 0.4366 0.5032 -0.0455 -0.0316 -0.0057 133 PHE A CB  
1012 C CG  . PHE A 133 ? 0.3565 0.3943 0.4573 -0.0282 -0.0321 0.0002  133 PHE A CG  
1013 C CD1 . PHE A 133 ? 0.3237 0.3956 0.4490 -0.0252 -0.0341 -0.0008 133 PHE A CD1 
1014 C CD2 . PHE A 133 ? 0.3534 0.3722 0.4412 -0.0149 -0.0304 0.0060  133 PHE A CD2 
1015 C CE1 . PHE A 133 ? 0.3027 0.3830 0.4357 -0.0094 -0.0345 0.0045  133 PHE A CE1 
1016 C CE2 . PHE A 133 ? 0.3295 0.3601 0.4272 -0.0019 -0.0303 0.0109  133 PHE A CE2 
1017 C CZ  . PHE A 133 ? 0.3040 0.3620 0.4224 0.0009  -0.0322 0.0105  133 PHE A CZ  
1018 N N   . VAL A 134 ? 0.4538 0.4984 0.5370 -0.0272 -0.0570 -0.0112 134 VAL A N   
1019 C CA  . VAL A 134 ? 0.4465 0.4835 0.5153 -0.0133 -0.0620 -0.0083 134 VAL A CA  
1020 C C   . VAL A 134 ? 0.4539 0.5140 0.5372 -0.0002 -0.0655 -0.0026 134 VAL A C   
1021 O O   . VAL A 134 ? 0.4708 0.5584 0.5710 -0.0011 -0.0725 -0.0055 134 VAL A O   
1022 C CB  . VAL A 134 ? 0.4460 0.4794 0.5003 -0.0185 -0.0712 -0.0160 134 VAL A CB  
1023 C CG1 . VAL A 134 ? 0.4221 0.4409 0.4553 -0.0052 -0.0726 -0.0128 134 VAL A CG1 
1024 C CG2 . VAL A 134 ? 0.4686 0.4795 0.5103 -0.0348 -0.0687 -0.0235 134 VAL A CG2 
1025 N N   . VAL A 135 ? 0.4408 0.4895 0.5170 0.0119  -0.0610 0.0051  135 VAL A N   
1026 C CA  . VAL A 135 ? 0.4242 0.4847 0.5072 0.0245  -0.0635 0.0115  135 VAL A CA  
1027 C C   . VAL A 135 ? 0.4361 0.4792 0.4993 0.0331  -0.0616 0.0171  135 VAL A C   
1028 O O   . VAL A 135 ? 0.4388 0.4646 0.4899 0.0316  -0.0554 0.0167  135 VAL A O   
1029 C CB  . VAL A 135 ? 0.4152 0.4822 0.5151 0.0276  -0.0568 0.0154  135 VAL A CB  
1030 C CG1 . VAL A 135 ? 0.4123 0.5022 0.5335 0.0196  -0.0574 0.0098  135 VAL A CG1 
1031 C CG2 . VAL A 135 ? 0.4077 0.4542 0.5003 0.0261  -0.0468 0.0181  135 VAL A CG2 
1032 N N   . ASP A 136 ? 0.4433 0.4913 0.5025 0.0427  -0.0666 0.0223  136 ASP A N   
1033 C CA  . ASP A 136 ? 0.4503 0.4828 0.4913 0.0494  -0.0627 0.0290  136 ASP A CA  
1034 C C   . ASP A 136 ? 0.4580 0.4861 0.5071 0.0540  -0.0557 0.0358  136 ASP A C   
1035 O O   . ASP A 136 ? 0.4929 0.5300 0.5545 0.0589  -0.0589 0.0377  136 ASP A O   
1036 C CB  . ASP A 136 ? 0.4590 0.4925 0.4838 0.0563  -0.0717 0.0318  136 ASP A CB  
1037 C CG  . ASP A 136 ? 0.4725 0.5047 0.4820 0.0519  -0.0772 0.0249  136 ASP A CG  
1038 O OD1 . ASP A 136 ? 0.4913 0.5360 0.4993 0.0533  -0.0891 0.0215  136 ASP A OD1 
1039 O OD2 . ASP A 136 ? 0.4745 0.4939 0.4731 0.0478  -0.0702 0.0219  136 ASP A OD2 
1040 N N   . VAL A 137 ? 0.4400 0.4556 0.4822 0.0527  -0.0465 0.0383  137 VAL A N   
1041 C CA  . VAL A 137 ? 0.4126 0.4230 0.4615 0.0543  -0.0396 0.0431  137 VAL A CA  
1042 C C   . VAL A 137 ? 0.4442 0.4433 0.4775 0.0584  -0.0380 0.0507  137 VAL A C   
1043 O O   . VAL A 137 ? 0.4880 0.4809 0.5065 0.0563  -0.0336 0.0518  137 VAL A O   
1044 C CB  . VAL A 137 ? 0.3685 0.3754 0.4213 0.0497  -0.0314 0.0402  137 VAL A CB  
1045 C CG1 . VAL A 137 ? 0.3547 0.3584 0.4154 0.0500  -0.0257 0.0435  137 VAL A CG1 
1046 C CG2 . VAL A 137 ? 0.3480 0.3590 0.4089 0.0453  -0.0329 0.0339  137 VAL A CG2 
1047 N N   . VAL A 138 ? 0.4328 0.4278 0.4678 0.0643  -0.0407 0.0557  138 VAL A N   
1048 C CA  . VAL A 138 ? 0.4293 0.4071 0.4451 0.0682  -0.0398 0.0642  138 VAL A CA  
1049 C C   . VAL A 138 ? 0.4264 0.3917 0.4461 0.0661  -0.0321 0.0676  138 VAL A C   
1050 O O   . VAL A 138 ? 0.4228 0.3896 0.4553 0.0706  -0.0342 0.0664  138 VAL A O   
1051 C CB  . VAL A 138 ? 0.4188 0.3962 0.4269 0.0793  -0.0514 0.0677  138 VAL A CB  
1052 C CG1 . VAL A 138 ? 0.4408 0.3931 0.4222 0.0838  -0.0503 0.0779  138 VAL A CG1 
1053 C CG2 . VAL A 138 ? 0.4108 0.4033 0.4165 0.0796  -0.0602 0.0624  138 VAL A CG2 
1054 N N   . ILE A 139 ? 0.4151 0.3696 0.4240 0.0586  -0.0229 0.0707  139 ILE A N   
1055 C CA  . ILE A 139 ? 0.4041 0.3464 0.4152 0.0533  -0.0153 0.0727  139 ILE A CA  
1056 C C   . ILE A 139 ? 0.4611 0.3770 0.4475 0.0536  -0.0133 0.0823  139 ILE A C   
1057 O O   . ILE A 139 ? 0.4521 0.3619 0.4206 0.0481  -0.0082 0.0863  139 ILE A O   
1058 C CB  . ILE A 139 ? 0.3895 0.3420 0.4090 0.0426  -0.0060 0.0679  139 ILE A CB  
1059 C CG1 . ILE A 139 ? 0.3645 0.3371 0.4011 0.0440  -0.0088 0.0597  139 ILE A CG1 
1060 C CG2 . ILE A 139 ? 0.3987 0.3422 0.4233 0.0358  0.0003  0.0680  139 ILE A CG2 
1061 C CD1 . ILE A 139 ? 0.3320 0.3161 0.3756 0.0378  -0.0019 0.0544  139 ILE A CD1 
1062 N N   . ASN A 140 ? 0.4991 0.3972 0.4820 0.0605  -0.0167 0.0859  140 ASN A N   
1063 C CA  . ASN A 140 ? 0.5446 0.4093 0.4999 0.0618  -0.0151 0.0959  140 ASN A CA  
1064 C C   . ASN A 140 ? 0.5850 0.4429 0.5158 0.0678  -0.0204 0.1027  140 ASN A C   
1065 O O   . ASN A 140 ? 0.6178 0.4557 0.5227 0.0606  -0.0136 0.1102  140 ASN A O   
1066 C CB  . ASN A 140 ? 0.5606 0.4107 0.5086 0.0449  -0.0019 0.0977  140 ASN A CB  
1067 C CG  . ASN A 140 ? 0.5668 0.4212 0.5356 0.0394  0.0016  0.0905  140 ASN A CG  
1068 O OD1 . ASN A 140 ? 0.5649 0.4197 0.5447 0.0498  -0.0047 0.0873  140 ASN A OD1 
1069 N ND2 . ASN A 140 ? 0.5631 0.4234 0.5377 0.0233  0.0117  0.0872  140 ASN A ND2 
1070 N N   . ASP A 141 ? 0.5859 0.4624 0.5248 0.0800  -0.0324 0.0995  141 ASP A N   
1071 C CA  . ASP A 141 ? 0.6231 0.4974 0.5408 0.0887  -0.0414 0.1040  141 ASP A CA  
1072 C C   . ASP A 141 ? 0.6216 0.5048 0.5290 0.0787  -0.0357 0.1029  141 ASP A C   
1073 O O   . ASP A 141 ? 0.6552 0.5332 0.5393 0.0842  -0.0417 0.1069  141 ASP A O   
1074 C CB  . ASP A 141 ? 0.6843 0.5216 0.5684 0.0977  -0.0445 0.1161  141 ASP A CB  
1075 C CG  . ASP A 141 ? 0.7211 0.5470 0.6125 0.1114  -0.0510 0.1167  141 ASP A CG  
1076 O OD1 . ASP A 141 ? 0.7018 0.5556 0.6212 0.1202  -0.0591 0.1083  141 ASP A OD1 
1077 O OD2 . ASP A 141 ? 0.7701 0.5580 0.6382 0.1128  -0.0473 0.1250  141 ASP A OD2 
1078 N N   . ILE A 142 ? 0.5913 0.4882 0.5142 0.0659  -0.0249 0.0968  142 ILE A N   
1079 C CA  . ILE A 142 ? 0.5854 0.4937 0.5013 0.0585  -0.0188 0.0935  142 ILE A CA  
1080 C C   . ILE A 142 ? 0.5153 0.4508 0.4565 0.0589  -0.0229 0.0821  142 ILE A C   
1081 O O   . ILE A 142 ? 0.4734 0.4192 0.4387 0.0559  -0.0203 0.0768  142 ILE A O   
1082 C CB  . ILE A 142 ? 0.6295 0.5324 0.5409 0.0443  -0.0026 0.0952  142 ILE A CB  
1083 C CG1 . ILE A 142 ? 0.6932 0.5633 0.5776 0.0409  0.0025  0.1070  142 ILE A CG1 
1084 C CG2 . ILE A 142 ? 0.6348 0.5512 0.5379 0.0394  0.0041  0.0912  142 ILE A CG2 
1085 C CD1 . ILE A 142 ? 0.7174 0.5837 0.5979 0.0235  0.0195  0.1083  142 ILE A CD1 
1086 N N   . HIS A 143 ? 0.5061 0.4505 0.4390 0.0624  -0.0294 0.0783  143 HIS A N   
1087 C CA  . HIS A 143 ? 0.4416 0.4056 0.3931 0.0614  -0.0330 0.0676  143 HIS A CA  
1088 C C   . HIS A 143 ? 0.4263 0.3970 0.3861 0.0539  -0.0213 0.0624  143 HIS A C   
1089 O O   . HIS A 143 ? 0.4667 0.4345 0.4120 0.0501  -0.0123 0.0638  143 HIS A O   
1090 C CB  A HIS A 143 ? 0.4172 0.3855 0.3538 0.0652  -0.0424 0.0640  143 HIS A CB  
1091 C CB  B HIS A 143 ? 0.4184 0.3866 0.3548 0.0652  -0.0423 0.0640  143 HIS A CB  
1092 C CG  A HIS A 143 ? 0.3791 0.3610 0.3290 0.0621  -0.0449 0.0528  143 HIS A CG  
1093 C CG  B HIS A 143 ? 0.4233 0.3942 0.3587 0.0739  -0.0569 0.0658  143 HIS A CG  
1094 N ND1 A HIS A 143 ? 0.3682 0.3503 0.3117 0.0584  -0.0374 0.0471  143 HIS A ND1 
1095 N ND1 B HIS A 143 ? 0.4127 0.4017 0.3660 0.0748  -0.0672 0.0575  143 HIS A ND1 
1096 C CD2 A HIS A 143 ? 0.3577 0.3513 0.3251 0.0618  -0.0535 0.0462  143 HIS A CD2 
1097 C CD2 B HIS A 143 ? 0.4531 0.4118 0.3713 0.0825  -0.0633 0.0746  143 HIS A CD2 
1098 C CE1 A HIS A 143 ? 0.3524 0.3408 0.3061 0.0566  -0.0419 0.0380  143 HIS A CE1 
1099 C CE1 B HIS A 143 ? 0.4201 0.4135 0.3711 0.0840  -0.0796 0.0601  143 HIS A CE1 
1100 N NE2 A HIS A 143 ? 0.3478 0.3433 0.3160 0.0569  -0.0512 0.0375  143 HIS A NE2 
1101 N NE2 B HIS A 143 ? 0.4467 0.4205 0.3754 0.0904  -0.0783 0.0707  143 HIS A NE2 
1102 N N   . PHE A 144 ? 0.3971 0.3781 0.3797 0.0525  -0.0215 0.0560  144 PHE A N   
1103 C CA  . PHE A 144 ? 0.3842 0.3725 0.3769 0.0484  -0.0125 0.0509  144 PHE A CA  
1104 C C   . PHE A 144 ? 0.3657 0.3603 0.3608 0.0501  -0.0150 0.0419  144 PHE A C   
1105 O O   . PHE A 144 ? 0.3856 0.3841 0.3766 0.0504  -0.0085 0.0374  144 PHE A O   
1106 C CB  . PHE A 144 ? 0.3670 0.3574 0.3795 0.0461  -0.0102 0.0512  144 PHE A CB  
1107 C CG  . PHE A 144 ? 0.3759 0.3759 0.3993 0.0433  -0.0029 0.0459  144 PHE A CG  
1108 C CD1 . PHE A 144 ? 0.3841 0.3880 0.4056 0.0380  0.0066  0.0472  144 PHE A CD1 
1109 C CD2 . PHE A 144 ? 0.3458 0.3512 0.3806 0.0457  -0.0057 0.0396  144 PHE A CD2 
1110 C CE1 . PHE A 144 ? 0.3735 0.3919 0.4078 0.0368  0.0120  0.0411  144 PHE A CE1 
1111 C CE2 . PHE A 144 ? 0.3432 0.3575 0.3864 0.0460  -0.0009 0.0347  144 PHE A CE2 
1112 C CZ  . PHE A 144 ? 0.3548 0.3783 0.3996 0.0423  0.0073  0.0349  144 PHE A CZ  
1113 N N   . GLU A 145 ? 0.3376 0.3328 0.3387 0.0511  -0.0238 0.0385  145 GLU A N   
1114 C CA  . GLU A 145 ? 0.3515 0.3460 0.3518 0.0509  -0.0261 0.0301  145 GLU A CA  
1115 C C   . GLU A 145 ? 0.3382 0.3342 0.3431 0.0486  -0.0361 0.0275  145 GLU A C   
1116 O O   . GLU A 145 ? 0.3516 0.3535 0.3668 0.0488  -0.0403 0.0315  145 GLU A O   
1117 C CB  . GLU A 145 ? 0.3494 0.3447 0.3619 0.0510  -0.0209 0.0268  145 GLU A CB  
1118 C CG  . GLU A 145 ? 0.3571 0.3545 0.3868 0.0485  -0.0227 0.0288  145 GLU A CG  
1119 C CD  . GLU A 145 ? 0.4048 0.4011 0.4417 0.0496  -0.0187 0.0257  145 GLU A CD  
1120 O OE1 . GLU A 145 ? 0.3961 0.3928 0.4440 0.0476  -0.0191 0.0269  145 GLU A OE1 
1121 O OE2 . GLU A 145 ? 0.4267 0.4222 0.4571 0.0537  -0.0153 0.0218  145 GLU A OE2 
1122 N N   . ARG A 146 ? 0.3451 0.3360 0.3424 0.0464  -0.0395 0.0200  146 ARG A N   
1123 C CA  . ARG A 146 ? 0.3898 0.3832 0.3938 0.0403  -0.0473 0.0153  146 ARG A CA  
1124 C C   . ARG A 146 ? 0.4239 0.4085 0.4340 0.0362  -0.0434 0.0114  146 ARG A C   
1125 O O   . ARG A 146 ? 0.4393 0.4100 0.4368 0.0381  -0.0403 0.0069  146 ARG A O   
1126 C CB  . ARG A 146 ? 0.4121 0.4024 0.3993 0.0383  -0.0548 0.0090  146 ARG A CB  
1127 C CG  . ARG A 146 ? 0.4366 0.4315 0.4313 0.0288  -0.0628 0.0023  146 ARG A CG  
1128 C CD  . ARG A 146 ? 0.3544 0.3524 0.3347 0.0269  -0.0731 -0.0035 146 ARG A CD  
1129 N NE  . ARG A 146 ? 0.3550 0.3673 0.3353 0.0341  -0.0793 0.0026  146 ARG A NE  
1130 C CZ  . ARG A 146 ? 0.4433 0.4637 0.4134 0.0346  -0.0908 -0.0009 146 ARG A CZ  
1131 N NH1 . ARG A 146 ? 0.3899 0.4067 0.3505 0.0263  -0.0969 -0.0116 146 ARG A NH1 
1132 N NH2 . ARG A 146 ? 0.3769 0.4068 0.3440 0.0437  -0.0968 0.0061  146 ARG A NH2 
1133 N N   . PHE A 147 ? 0.4009 0.3924 0.4280 0.0317  -0.0433 0.0132  147 PHE A N   
1134 C CA  . PHE A 147 ? 0.4064 0.3875 0.4366 0.0276  -0.0390 0.0113  147 PHE A CA  
1135 C C   . PHE A 147 ? 0.4241 0.3991 0.4512 0.0163  -0.0429 0.0050  147 PHE A C   
1136 O O   . PHE A 147 ? 0.4180 0.4092 0.4566 0.0097  -0.0478 0.0034  147 PHE A O   
1137 C CB  . PHE A 147 ? 0.3862 0.3767 0.4336 0.0281  -0.0351 0.0163  147 PHE A CB  
1138 C CG  . PHE A 147 ? 0.4010 0.3791 0.4472 0.0255  -0.0303 0.0157  147 PHE A CG  
1139 C CD1 . PHE A 147 ? 0.4275 0.4032 0.4771 0.0153  -0.0299 0.0135  147 PHE A CD1 
1140 C CD2 . PHE A 147 ? 0.4027 0.3725 0.4437 0.0330  -0.0261 0.0173  147 PHE A CD2 
1141 C CE1 . PHE A 147 ? 0.4498 0.4098 0.4930 0.0129  -0.0251 0.0141  147 PHE A CE1 
1142 C CE2 . PHE A 147 ? 0.4230 0.3799 0.4595 0.0326  -0.0232 0.0172  147 PHE A CE2 
1143 C CZ  . PHE A 147 ? 0.4476 0.3969 0.4830 0.0227  -0.0225 0.0163  147 PHE A CZ  
1144 N N   . ARG A 148 ? 0.4552 0.4066 0.4662 0.0143  -0.0408 0.0008  148 ARG A N   
1145 C CA  . ARG A 148 ? 0.5035 0.4411 0.5077 0.0009  -0.0425 -0.0050 148 ARG A CA  
1146 C C   . ARG A 148 ? 0.5077 0.4239 0.5052 -0.0002 -0.0361 -0.0028 148 ARG A C   
1147 O O   . ARG A 148 ? 0.5013 0.3974 0.4833 0.0100  -0.0338 -0.0027 148 ARG A O   
1148 C CB  . ARG A 148 ? 0.5722 0.4919 0.5547 -0.0007 -0.0471 -0.0128 148 ARG A CB  
1149 C CG  . ARG A 148 ? 0.6210 0.5558 0.6076 -0.0116 -0.0554 -0.0187 148 ARG A CG  
1150 C CD  . ARG A 148 ? 0.7051 0.6151 0.6666 -0.0166 -0.0595 -0.0282 148 ARG A CD  
1151 N NE  . ARG A 148 ? 0.7480 0.6360 0.7019 -0.0333 -0.0583 -0.0336 148 ARG A NE  
1152 C CZ  . ARG A 148 ? 0.7754 0.6720 0.7345 -0.0515 -0.0638 -0.0407 148 ARG A CZ  
1153 N NH1 . ARG A 148 ? 0.7630 0.6918 0.7357 -0.0529 -0.0725 -0.0437 148 ARG A NH1 
1154 N NH2 . ARG A 148 ? 0.8091 0.6818 0.7588 -0.0689 -0.0607 -0.0450 148 ARG A NH2 
1155 N N   . GLY A 149 ? 0.5221 0.4438 0.5305 -0.0114 -0.0332 -0.0013 149 GLY A N   
1156 C CA  . GLY A 149 ? 0.5167 0.4170 0.5157 -0.0132 -0.0269 0.0018  149 GLY A CA  
1157 C C   . GLY A 149 ? 0.4916 0.4030 0.5036 -0.0277 -0.0223 0.0030  149 GLY A C   
1158 O O   . GLY A 149 ? 0.4881 0.4185 0.5133 -0.0404 -0.0244 -0.0012 149 GLY A O   
1159 N N   . ASP A 150 ? 0.4776 0.3799 0.4863 -0.0259 -0.0160 0.0081  150 ASP A N   
1160 C CA  . ASP A 150 ? 0.4432 0.3570 0.4630 -0.0393 -0.0095 0.0092  150 ASP A CA  
1161 C C   . ASP A 150 ? 0.4170 0.3684 0.4649 -0.0334 -0.0089 0.0109  150 ASP A C   
1162 O O   . ASP A 150 ? 0.4209 0.3964 0.4869 -0.0438 -0.0061 0.0085  150 ASP A O   
1163 C CB  . ASP A 150 ? 0.4489 0.3323 0.4471 -0.0403 -0.0027 0.0140  150 ASP A CB  
1164 C CG  . ASP A 150 ? 0.4921 0.3326 0.4590 -0.0482 -0.0024 0.0125  150 ASP A CG  
1165 O OD1 . ASP A 150 ? 0.5233 0.3595 0.4873 -0.0552 -0.0069 0.0065  150 ASP A OD1 
1166 O OD2 . ASP A 150 ? 0.4984 0.3073 0.4415 -0.0472 0.0020  0.0171  150 ASP A OD2 
1167 N N   . GLY A 151 ? 0.3927 0.3499 0.4446 -0.0171 -0.0112 0.0144  151 GLY A N   
1168 C CA  . GLY A 151 ? 0.3344 0.3204 0.4087 -0.0110 -0.0110 0.0159  151 GLY A CA  
1169 C C   . GLY A 151 ? 0.3212 0.3049 0.3942 0.0039  -0.0120 0.0199  151 GLY A C   
1170 O O   . GLY A 151 ? 0.3331 0.2999 0.3917 0.0105  -0.0137 0.0207  151 GLY A O   
1171 N N   . LEU A 152 ? 0.3025 0.3046 0.3913 0.0091  -0.0108 0.0214  152 LEU A N   
1172 C CA  . LEU A 152 ? 0.2930 0.2946 0.3825 0.0201  -0.0111 0.0244  152 LEU A CA  
1173 C C   . LEU A 152 ? 0.2759 0.2836 0.3728 0.0214  -0.0060 0.0252  152 LEU A C   
1174 O O   . LEU A 152 ? 0.2716 0.2916 0.3784 0.0164  -0.0028 0.0233  152 LEU A O   
1175 C CB  . LEU A 152 ? 0.2872 0.2999 0.3841 0.0265  -0.0160 0.0255  152 LEU A CB  
1176 C CG  . LEU A 152 ? 0.3127 0.3198 0.3998 0.0269  -0.0208 0.0246  152 LEU A CG  
1177 C CD1 . LEU A 152 ? 0.3014 0.3196 0.3936 0.0320  -0.0253 0.0265  152 LEU A CD1 
1178 C CD2 . LEU A 152 ? 0.3267 0.3196 0.4011 0.0316  -0.0192 0.0252  152 LEU A CD2 
1179 N N   . CYS A 153 ? 0.2927 0.2935 0.3851 0.0280  -0.0052 0.0268  153 CYS A N   
1180 C CA  . CYS A 153 ? 0.3106 0.3136 0.4060 0.0298  -0.0010 0.0265  153 CYS A CA  
1181 C C   . CYS A 153 ? 0.2990 0.3037 0.3988 0.0368  -0.0028 0.0272  153 CYS A C   
1182 O O   . CYS A 153 ? 0.2936 0.2926 0.3876 0.0393  -0.0051 0.0278  153 CYS A O   
1183 C CB  . CYS A 153 ? 0.3267 0.3147 0.4065 0.0280  0.0019  0.0268  153 CYS A CB  
1184 S SG  . CYS A 153 ? 0.3236 0.3118 0.4018 0.0312  0.0061  0.0256  153 CYS A SG  
1185 N N   . MET A 154 ? 0.3069 0.3194 0.4164 0.0398  -0.0014 0.0265  154 MET A N   
1186 C CA  . MET A 154 ? 0.2938 0.3024 0.4045 0.0447  -0.0022 0.0270  154 MET A CA  
1187 C C   . MET A 154 ? 0.3123 0.3176 0.4212 0.0457  0.0018  0.0239  154 MET A C   
1188 O O   . MET A 154 ? 0.2972 0.3091 0.4112 0.0469  0.0055  0.0217  154 MET A O   
1189 C CB  . MET A 154 ? 0.2828 0.2960 0.4009 0.0496  -0.0048 0.0286  154 MET A CB  
1190 C CG  . MET A 154 ? 0.3217 0.3235 0.4361 0.0532  -0.0052 0.0302  154 MET A CG  
1191 S SD  . MET A 154 ? 0.3219 0.3166 0.4281 0.0484  -0.0063 0.0330  154 MET A SD  
1192 C CE  . MET A 154 ? 0.3128 0.3088 0.4167 0.0514  -0.0105 0.0379  154 MET A CE  
1193 N N   . SER A 155 ? 0.3273 0.3249 0.4295 0.0453  0.0012  0.0227  155 SER A N   
1194 C CA  . SER A 155 ? 0.3125 0.3057 0.4088 0.0456  0.0038  0.0190  155 SER A CA  
1195 C C   . SER A 155 ? 0.3119 0.2983 0.4086 0.0469  0.0033  0.0163  155 SER A C   
1196 O O   . SER A 155 ? 0.3370 0.3205 0.4355 0.0453  0.0010  0.0179  155 SER A O   
1197 C CB  . SER A 155 ? 0.3175 0.3070 0.4028 0.0440  0.0018  0.0184  155 SER A CB  
1198 O OG  . SER A 155 ? 0.3436 0.3287 0.4213 0.0447  0.0025  0.0144  155 SER A OG  
1199 N N   . THR A 156 ? 0.2982 0.2806 0.3912 0.0489  0.0065  0.0119  156 THR A N   
1200 C CA  . THR A 156 ? 0.3118 0.2833 0.4007 0.0487  0.0061  0.0076  156 THR A CA  
1201 C C   . THR A 156 ? 0.3273 0.2987 0.4092 0.0439  0.0026  0.0043  156 THR A C   
1202 O O   . THR A 156 ? 0.3472 0.3251 0.4254 0.0436  0.0007  0.0057  156 THR A O   
1203 C CB  . THR A 156 ? 0.3253 0.2926 0.4115 0.0541  0.0109  0.0027  156 THR A CB  
1204 O OG1 . THR A 156 ? 0.3190 0.2897 0.3964 0.0530  0.0135  -0.0002 156 THR A OG1 
1205 C CG2 . THR A 156 ? 0.3117 0.2873 0.4081 0.0606  0.0136  0.0049  156 THR A CG2 
1206 N N   . PRO A 157 ? 0.3247 0.2884 0.4038 0.0400  0.0009  -0.0006 157 PRO A N   
1207 C CA  . PRO A 157 ? 0.3065 0.2755 0.3811 0.0357  -0.0038 -0.0055 157 PRO A CA  
1208 C C   . PRO A 157 ? 0.3188 0.2887 0.3815 0.0397  -0.0042 -0.0084 157 PRO A C   
1209 O O   . PRO A 157 ? 0.3082 0.2857 0.3667 0.0414  -0.0082 -0.0070 157 PRO A O   
1210 C CB  . PRO A 157 ? 0.3135 0.2717 0.3865 0.0293  -0.0042 -0.0116 157 PRO A CB  
1211 C CG  . PRO A 157 ? 0.3261 0.2737 0.4038 0.0287  -0.0009 -0.0065 157 PRO A CG  
1212 C CD  . PRO A 157 ? 0.3143 0.2639 0.3943 0.0383  0.0022  -0.0012 157 PRO A CD  
1213 N N   . SER A 158 ? 0.3451 0.3055 0.3998 0.0423  0.0001  -0.0123 158 SER A N   
1214 C CA  . SER A 158 ? 0.3527 0.3121 0.3923 0.0454  0.0013  -0.0146 158 SER A CA  
1215 C C   . SER A 158 ? 0.3172 0.2811 0.3544 0.0477  0.0048  -0.0075 158 SER A C   
1216 O O   . SER A 158 ? 0.2985 0.2593 0.3194 0.0490  0.0050  -0.0072 158 SER A O   
1217 C CB  . SER A 158 ? 0.3837 0.3332 0.4156 0.0482  0.0074  -0.0207 158 SER A CB  
1218 O OG  . SER A 158 ? 0.3847 0.3365 0.4252 0.0526  0.0150  -0.0175 158 SER A OG  
1219 N N   . GLY A 159 ? 0.2952 0.2643 0.3458 0.0475  0.0072  -0.0019 159 GLY A N   
1220 C CA  . GLY A 159 ? 0.2979 0.2702 0.3469 0.0470  0.0100  0.0040  159 GLY A CA  
1221 C C   . GLY A 159 ? 0.3063 0.2791 0.3530 0.0466  0.0038  0.0080  159 GLY A C   
1222 O O   . GLY A 159 ? 0.3330 0.3030 0.3742 0.0456  0.0056  0.0126  159 GLY A O   
1223 N N   . THR A 160 ? 0.2802 0.2567 0.3309 0.0471  -0.0031 0.0057  160 THR A N   
1224 C CA  . THR A 160 ? 0.2983 0.2785 0.3482 0.0493  -0.0090 0.0081  160 THR A CA  
1225 C C   . THR A 160 ? 0.3673 0.3399 0.3972 0.0542  -0.0127 0.0086  160 THR A C   
1226 O O   . THR A 160 ? 0.4174 0.3875 0.4420 0.0584  -0.0164 0.0117  160 THR A O   
1227 C CB  . THR A 160 ? 0.2670 0.2585 0.3286 0.0479  -0.0141 0.0041  160 THR A CB  
1228 O OG1 . THR A 160 ? 0.2885 0.2806 0.3467 0.0460  -0.0166 -0.0026 160 THR A OG1 
1229 C CG2 . THR A 160 ? 0.2395 0.2334 0.3155 0.0435  -0.0105 0.0063  160 THR A CG2 
1230 N N   . THR A 161 ? 0.3673 0.3337 0.3833 0.0548  -0.0120 0.0055  161 THR A N   
1231 C CA  . THR A 161 ? 0.3965 0.3511 0.3875 0.0600  -0.0151 0.0072  161 THR A CA  
1232 C C   . THR A 161 ? 0.3881 0.3271 0.3644 0.0571  -0.0067 0.0138  161 THR A C   
1233 O O   . THR A 161 ? 0.3723 0.2951 0.3229 0.0605  -0.0081 0.0171  161 THR A O   
1234 C CB  . THR A 161 ? 0.4325 0.3860 0.4110 0.0612  -0.0178 0.0009  161 THR A CB  
1235 O OG1 . THR A 161 ? 0.4476 0.3992 0.4295 0.0560  -0.0085 -0.0016 161 THR A OG1 
1236 C CG2 . THR A 161 ? 0.4299 0.3994 0.4210 0.0622  -0.0275 -0.0066 161 THR A CG2 
1237 N N   . ALA A 162 ? 0.3802 0.3236 0.3710 0.0505  0.0017  0.0156  162 ALA A N   
1238 C CA  . ALA A 162 ? 0.3789 0.3126 0.3597 0.0444  0.0108  0.0203  162 ALA A CA  
1239 C C   . ALA A 162 ? 0.3857 0.3144 0.3694 0.0420  0.0098  0.0252  162 ALA A C   
1240 O O   . ALA A 162 ? 0.4128 0.3301 0.3842 0.0477  0.0026  0.0275  162 ALA A O   
1241 C CB  . ALA A 162 ? 0.3485 0.2947 0.3445 0.0392  0.0206  0.0175  162 ALA A CB  
1242 N N   . TYR A 163 ? 0.3905 0.3283 0.3901 0.0345  0.0162  0.0259  163 TYR A N   
1243 C CA  . TYR A 163 ? 0.4007 0.3336 0.4024 0.0304  0.0153  0.0292  163 TYR A CA  
1244 C C   . TYR A 163 ? 0.3647 0.3007 0.3742 0.0380  0.0059  0.0286  163 TYR A C   
1245 O O   . TYR A 163 ? 0.3685 0.2914 0.3675 0.0397  0.0023  0.0309  163 TYR A O   
1246 C CB  . TYR A 163 ? 0.4219 0.3715 0.4440 0.0220  0.0218  0.0280  163 TYR A CB  
1247 C CG  . TYR A 163 ? 0.4750 0.4178 0.4946 0.0129  0.0236  0.0303  163 TYR A CG  
1248 C CD1 . TYR A 163 ? 0.5101 0.4273 0.5071 0.0131  0.0202  0.0338  163 TYR A CD1 
1249 C CD2 . TYR A 163 ? 0.5127 0.4745 0.5519 0.0046  0.0280  0.0282  163 TYR A CD2 
1250 C CE1 . TYR A 163 ? 0.5510 0.4577 0.5430 0.0034  0.0219  0.0350  163 TYR A CE1 
1251 C CE2 . TYR A 163 ? 0.5530 0.5096 0.5902 -0.0058 0.0290  0.0289  163 TYR A CE2 
1252 C CZ  . TYR A 163 ? 0.5831 0.5101 0.5957 -0.0073 0.0263  0.0323  163 TYR A CZ  
1253 O OH  . TYR A 163 ? 0.6072 0.5250 0.6153 -0.0189 0.0273  0.0321  163 TYR A OH  
1254 N N   . ASN A 164 ? 0.3321 0.2840 0.3585 0.0422  0.0026  0.0251  164 ASN A N   
1255 C CA  . ASN A 164 ? 0.3328 0.2914 0.3680 0.0474  -0.0043 0.0241  164 ASN A CA  
1256 C C   . ASN A 164 ? 0.3760 0.3255 0.3955 0.0557  -0.0109 0.0240  164 ASN A C   
1257 O O   . ASN A 164 ? 0.3964 0.3455 0.4163 0.0604  -0.0150 0.0241  164 ASN A O   
1258 C CB  . ASN A 164 ? 0.3352 0.3085 0.3868 0.0480  -0.0053 0.0206  164 ASN A CB  
1259 C CG  . ASN A 164 ? 0.3642 0.3465 0.4232 0.0516  -0.0109 0.0188  164 ASN A CG  
1260 O OD1 . ASN A 164 ? 0.3679 0.3559 0.4366 0.0503  -0.0107 0.0200  164 ASN A OD1 
1261 N ND2 . ASN A 164 ? 0.3745 0.3603 0.4289 0.0560  -0.0159 0.0152  164 ASN A ND2 
1262 N N   . LYS A 165 ? 0.3875 0.3296 0.3916 0.0590  -0.0125 0.0233  165 LYS A N   
1263 C CA  . LYS A 165 ? 0.3929 0.3275 0.3809 0.0698  -0.0208 0.0228  165 LYS A CA  
1264 C C   . LYS A 165 ? 0.4128 0.3234 0.3802 0.0730  -0.0212 0.0276  165 LYS A C   
1265 O O   . LYS A 165 ? 0.4150 0.3230 0.3776 0.0836  -0.0282 0.0267  165 LYS A O   
1266 C CB  . LYS A 165 ? 0.3855 0.3154 0.3575 0.0728  -0.0230 0.0212  165 LYS A CB  
1267 C CG  . LYS A 165 ? 0.3792 0.3022 0.3323 0.0863  -0.0336 0.0205  165 LYS A CG  
1268 C CD  . LYS A 165 ? 0.4037 0.3233 0.3398 0.0888  -0.0366 0.0184  165 LYS A CD  
1269 C CE  . LYS A 165 ? 0.4257 0.3399 0.3418 0.1046  -0.0493 0.0175  165 LYS A CE  
1270 N NZ  . LYS A 165 ? 0.4723 0.3539 0.3592 0.1113  -0.0494 0.0255  165 LYS A NZ  
1271 N N   . SER A 166 ? 0.4186 0.3110 0.3730 0.0636  -0.0134 0.0321  166 SER A N   
1272 C CA  . SER A 166 ? 0.4331 0.2963 0.3638 0.0639  -0.0130 0.0367  166 SER A CA  
1273 C C   . SER A 166 ? 0.4204 0.2861 0.3626 0.0639  -0.0145 0.0355  166 SER A C   
1274 O O   . SER A 166 ? 0.4400 0.2803 0.3618 0.0682  -0.0169 0.0375  166 SER A O   
1275 C CB  . SER A 166 ? 0.4582 0.3044 0.3744 0.0496  -0.0024 0.0411  166 SER A CB  
1276 O OG  . SER A 166 ? 0.5095 0.3430 0.4028 0.0516  -0.0010 0.0434  166 SER A OG  
1277 N N   . LEU A 167 ? 0.4024 0.2946 0.3733 0.0598  -0.0133 0.0322  167 LEU A N   
1278 C CA  . LEU A 167 ? 0.4065 0.3030 0.3873 0.0600  -0.0148 0.0306  167 LEU A CA  
1279 C C   . LEU A 167 ? 0.3970 0.3078 0.3862 0.0729  -0.0216 0.0267  167 LEU A C   
1280 O O   . LEU A 167 ? 0.3882 0.3075 0.3876 0.0735  -0.0219 0.0247  167 LEU A O   
1281 C CB  . LEU A 167 ? 0.3659 0.2819 0.3698 0.0491  -0.0100 0.0298  167 LEU A CB  
1282 C CG  . LEU A 167 ? 0.3632 0.2731 0.3649 0.0357  -0.0029 0.0318  167 LEU A CG  
1283 C CD1 . LEU A 167 ? 0.3176 0.2530 0.3446 0.0298  0.0001  0.0301  167 LEU A CD1 
1284 C CD2 . LEU A 167 ? 0.3618 0.2509 0.3492 0.0296  -0.0024 0.0325  167 LEU A CD2 
1285 N N   . GLY A 168 ? 0.4154 0.3316 0.4008 0.0828  -0.0268 0.0250  168 GLY A N   
1286 C CA  . GLY A 168 ? 0.4025 0.3385 0.3991 0.0943  -0.0328 0.0199  168 GLY A CA  
1287 C C   . GLY A 168 ? 0.3670 0.3343 0.3902 0.0889  -0.0314 0.0163  168 GLY A C   
1288 O O   . GLY A 168 ? 0.3808 0.3691 0.4165 0.0951  -0.0346 0.0114  168 GLY A O   
1289 N N   . GLY A 169 ? 0.3198 0.2900 0.3510 0.0775  -0.0264 0.0180  169 GLY A N   
1290 C CA  . GLY A 169 ? 0.3005 0.2925 0.3524 0.0716  -0.0247 0.0150  169 GLY A CA  
1291 C C   . GLY A 169 ? 0.3142 0.3202 0.3696 0.0752  -0.0299 0.0099  169 GLY A C   
1292 O O   . GLY A 169 ? 0.3085 0.3081 0.3498 0.0833  -0.0354 0.0088  169 GLY A O   
1293 N N   . ALA A 170 ? 0.3154 0.3397 0.3886 0.0685  -0.0283 0.0064  170 ALA A N   
1294 C CA  . ALA A 170 ? 0.3022 0.3431 0.3819 0.0684  -0.0331 -0.0003 170 ALA A CA  
1295 C C   . ALA A 170 ? 0.2981 0.3295 0.3729 0.0617  -0.0316 -0.0009 170 ALA A C   
1296 O O   . ALA A 170 ? 0.3038 0.3217 0.3767 0.0562  -0.0253 0.0031  170 ALA A O   
1297 C CB  . ALA A 170 ? 0.2772 0.3418 0.3772 0.0618  -0.0312 -0.0046 170 ALA A CB  
1298 N N   . LEU A 171 ? 0.2781 0.3185 0.3509 0.0633  -0.0378 -0.0072 171 LEU A N   
1299 C CA  . LEU A 171 ? 0.2723 0.3040 0.3382 0.0579  -0.0371 -0.0099 171 LEU A CA  
1300 C C   . LEU A 171 ? 0.2903 0.3329 0.3721 0.0462  -0.0352 -0.0156 171 LEU A C   
1301 O O   . LEU A 171 ? 0.3199 0.3843 0.4144 0.0434  -0.0395 -0.0218 171 LEU A O   
1302 C CB  . LEU A 171 ? 0.2791 0.3108 0.3288 0.0661  -0.0458 -0.0138 171 LEU A CB  
1303 C CG  . LEU A 171 ? 0.2981 0.3138 0.3266 0.0782  -0.0484 -0.0076 171 LEU A CG  
1304 C CD1 . LEU A 171 ? 0.3178 0.3269 0.3237 0.0860  -0.0564 -0.0101 171 LEU A CD1 
1305 C CD2 . LEU A 171 ? 0.3101 0.3036 0.3303 0.0742  -0.0384 0.0007  171 LEU A CD2 
1306 N N   . MET A 172 ? 0.2912 0.3184 0.3717 0.0393  -0.0285 -0.0140 172 MET A N   
1307 C CA  . MET A 172 ? 0.2981 0.3256 0.3892 0.0279  -0.0250 -0.0171 172 MET A CA  
1308 C C   . MET A 172 ? 0.2858 0.3019 0.3682 0.0235  -0.0256 -0.0238 172 MET A C   
1309 O O   . MET A 172 ? 0.2898 0.2900 0.3598 0.0283  -0.0227 -0.0221 172 MET A O   
1310 C CB  . MET A 172 ? 0.3222 0.3372 0.4166 0.0260  -0.0173 -0.0095 172 MET A CB  
1311 C CG  . MET A 172 ? 0.3457 0.3651 0.4509 0.0163  -0.0140 -0.0091 172 MET A CG  
1312 S SD  . MET A 172 ? 0.3846 0.3957 0.4910 0.0190  -0.0084 0.0012  172 MET A SD  
1313 C CE  . MET A 172 ? 0.3858 0.3764 0.4832 0.0256  -0.0060 0.0045  172 MET A CE  
1314 N N   . HIS A 173 ? 0.2845 0.3094 0.3732 0.0135  -0.0288 -0.0321 173 HIS A N   
1315 C CA  . HIS A 173 ? 0.3184 0.3295 0.3972 0.0081  -0.0297 -0.0399 173 HIS A CA  
1316 C C   . HIS A 173 ? 0.3690 0.3534 0.4432 0.0052  -0.0211 -0.0365 173 HIS A C   
1317 O O   . HIS A 173 ? 0.3917 0.3714 0.4737 -0.0004 -0.0164 -0.0317 173 HIS A O   
1318 C CB  . HIS A 173 ? 0.3107 0.3373 0.3979 -0.0047 -0.0352 -0.0508 173 HIS A CB  
1319 C CG  . HIS A 173 ? 0.3477 0.3595 0.4219 -0.0103 -0.0377 -0.0606 173 HIS A CG  
1320 N ND1 . HIS A 173 ? 0.3632 0.3497 0.4324 -0.0206 -0.0318 -0.0633 173 HIS A ND1 
1321 C CD2 . HIS A 173 ? 0.3621 0.3778 0.4239 -0.0061 -0.0457 -0.0686 173 HIS A CD2 
1322 C CE1 . HIS A 173 ? 0.3678 0.3437 0.4233 -0.0230 -0.0357 -0.0735 173 HIS A CE1 
1323 N NE2 . HIS A 173 ? 0.3799 0.3744 0.4307 -0.0146 -0.0442 -0.0770 173 HIS A NE2 
1324 N N   . PRO A 174 ? 0.3951 0.3612 0.4550 0.0102  -0.0190 -0.0390 174 PRO A N   
1325 C CA  . PRO A 174 ? 0.3894 0.3319 0.4451 0.0126  -0.0115 -0.0357 174 PRO A CA  
1326 C C   . PRO A 174 ? 0.4088 0.3318 0.4628 0.0018  -0.0096 -0.0400 174 PRO A C   
1327 O O   . PRO A 174 ? 0.4149 0.3153 0.4636 0.0059  -0.0043 -0.0370 174 PRO A O   
1328 C CB  . PRO A 174 ? 0.3995 0.3330 0.4406 0.0216  -0.0096 -0.0395 174 PRO A CB  
1329 C CG  . PRO A 174 ? 0.4051 0.3488 0.4380 0.0189  -0.0171 -0.0475 174 PRO A CG  
1330 C CD  . PRO A 174 ? 0.3875 0.3550 0.4330 0.0163  -0.0233 -0.0445 174 PRO A CD  
1331 N N   . SER A 175 ? 0.4275 0.3577 0.4852 -0.0120 -0.0138 -0.0472 175 SER A N   
1332 C CA  . SER A 175 ? 0.4669 0.3756 0.5220 -0.0257 -0.0105 -0.0497 175 SER A CA  
1333 C C   . SER A 175 ? 0.4800 0.3884 0.5436 -0.0291 -0.0055 -0.0391 175 SER A C   
1334 O O   . SER A 175 ? 0.5041 0.3858 0.5601 -0.0370 -0.0008 -0.0370 175 SER A O   
1335 C CB  . SER A 175 ? 0.4870 0.4064 0.5450 -0.0428 -0.0158 -0.0616 175 SER A CB  
1336 O OG  . SER A 175 ? 0.4679 0.4232 0.5445 -0.0485 -0.0191 -0.0609 175 SER A OG  
1337 N N   . ILE A 176 ? 0.4553 0.3896 0.5312 -0.0229 -0.0064 -0.0323 176 ILE A N   
1338 C CA  . ILE A 176 ? 0.4575 0.3930 0.5394 -0.0244 -0.0019 -0.0224 176 ILE A CA  
1339 C C   . ILE A 176 ? 0.4832 0.4002 0.5579 -0.0103 0.0012  -0.0137 176 ILE A C   
1340 O O   . ILE A 176 ? 0.4888 0.4148 0.5649 0.0024  -0.0004 -0.0121 176 ILE A O   
1341 C CB  . ILE A 176 ? 0.4208 0.3913 0.5177 -0.0228 -0.0044 -0.0206 176 ILE A CB  
1342 C CG1 . ILE A 176 ? 0.4056 0.4005 0.5128 -0.0353 -0.0084 -0.0307 176 ILE A CG1 
1343 C CG2 . ILE A 176 ? 0.4223 0.3931 0.5226 -0.0234 0.0007  -0.0109 176 ILE A CG2 
1344 C CD1 . ILE A 176 ? 0.3817 0.4127 0.5033 -0.0297 -0.0124 -0.0311 176 ILE A CD1 
1345 N N   . GLU A 177 ? 0.4755 0.3663 0.5415 -0.0127 0.0054  -0.0084 177 GLU A N   
1346 C CA  . GLU A 177 ? 0.4570 0.3327 0.5172 0.0019  0.0069  -0.0006 177 GLU A CA  
1347 C C   . GLU A 177 ? 0.4104 0.3041 0.4790 0.0050  0.0071  0.0083  177 GLU A C   
1348 O O   . GLU A 177 ? 0.3834 0.2686 0.4477 -0.0012 0.0098  0.0144  177 GLU A O   
1349 C CB  . GLU A 177 ? 0.5096 0.3460 0.5530 0.0009  0.0097  0.0013  177 GLU A CB  
1350 C CG  . GLU A 177 ? 0.5403 0.3539 0.5724 -0.0043 0.0098  -0.0089 177 GLU A CG  
1351 C CD  . GLU A 177 ? 0.5981 0.3673 0.6101 0.0017  0.0121  -0.0069 177 GLU A CD  
1352 O OE1 . GLU A 177 ? 0.6139 0.3750 0.6221 0.0198  0.0113  -0.0081 177 GLU A OE1 
1353 O OE2 . GLU A 177 ? 0.6403 0.3821 0.6392 -0.0115 0.0149  -0.0043 177 GLU A OE2 
1354 N N   . ALA A 178 ? 0.3737 0.2902 0.4515 0.0139  0.0046  0.0089  178 ALA A N   
1355 C CA  . ALA A 178 ? 0.3463 0.2796 0.4309 0.0164  0.0041  0.0154  178 ALA A CA  
1356 C C   . ALA A 178 ? 0.3409 0.2855 0.4300 0.0283  0.0022  0.0169  178 ALA A C   
1357 O O   . ALA A 178 ? 0.3393 0.2823 0.4273 0.0338  0.0022  0.0129  178 ALA A O   
1358 C CB  . ALA A 178 ? 0.2739 0.2296 0.3668 0.0076  0.0035  0.0125  178 ALA A CB  
1359 N N   . MET A 179 ? 0.3326 0.2883 0.4256 0.0308  0.0014  0.0222  179 MET A N   
1360 C CA  . MET A 179 ? 0.3471 0.3149 0.4445 0.0380  -0.0002 0.0233  179 MET A CA  
1361 C C   . MET A 179 ? 0.3458 0.3276 0.4459 0.0358  -0.0016 0.0246  179 MET A C   
1362 O O   . MET A 179 ? 0.3602 0.3437 0.4598 0.0316  -0.0009 0.0269  179 MET A O   
1363 C CB  . MET A 179 ? 0.3536 0.3177 0.4517 0.0458  -0.0008 0.0275  179 MET A CB  
1364 C CG  . MET A 179 ? 0.3831 0.3421 0.4770 0.0455  -0.0020 0.0338  179 MET A CG  
1365 S SD  . MET A 179 ? 0.3950 0.3536 0.4900 0.0573  -0.0057 0.0377  179 MET A SD  
1366 C CE  . MET A 179 ? 0.3811 0.3302 0.4645 0.0555  -0.0074 0.0455  179 MET A CE  
1367 N N   . GLN A 180 ? 0.3372 0.3272 0.4380 0.0388  -0.0030 0.0231  180 GLN A N   
1368 C CA  . GLN A 180 ? 0.3276 0.3267 0.4280 0.0391  -0.0049 0.0233  180 GLN A CA  
1369 C C   . GLN A 180 ? 0.3339 0.3333 0.4329 0.0421  -0.0055 0.0262  180 GLN A C   
1370 O O   . GLN A 180 ? 0.3209 0.3185 0.4194 0.0432  -0.0045 0.0257  180 GLN A O   
1371 C CB  . GLN A 180 ? 0.3280 0.3317 0.4257 0.0401  -0.0070 0.0188  180 GLN A CB  
1372 C CG  . GLN A 180 ? 0.3408 0.3516 0.4363 0.0437  -0.0097 0.0184  180 GLN A CG  
1373 C CD  . GLN A 180 ? 0.3593 0.3755 0.4513 0.0474  -0.0137 0.0138  180 GLN A CD  
1374 O OE1 . GLN A 180 ? 0.3603 0.3810 0.4489 0.0534  -0.0169 0.0127  180 GLN A OE1 
1375 N NE2 . GLN A 180 ? 0.3767 0.3917 0.4679 0.0451  -0.0144 0.0104  180 GLN A NE2 
1376 N N   . LEU A 181 ? 0.3584 0.3607 0.4564 0.0423  -0.0066 0.0282  181 LEU A N   
1377 C CA  . LEU A 181 ? 0.3605 0.3625 0.4560 0.0433  -0.0081 0.0297  181 LEU A CA  
1378 C C   . LEU A 181 ? 0.3777 0.3780 0.4660 0.0450  -0.0095 0.0277  181 LEU A C   
1379 O O   . LEU A 181 ? 0.3664 0.3711 0.4536 0.0471  -0.0099 0.0264  181 LEU A O   
1380 C CB  . LEU A 181 ? 0.3590 0.3621 0.4545 0.0435  -0.0093 0.0328  181 LEU A CB  
1381 C CG  . LEU A 181 ? 0.3442 0.3487 0.4372 0.0433  -0.0122 0.0328  181 LEU A CG  
1382 C CD1 . LEU A 181 ? 0.3358 0.3445 0.4358 0.0423  -0.0127 0.0322  181 LEU A CD1 
1383 C CD2 . LEU A 181 ? 0.3258 0.3310 0.4140 0.0443  -0.0143 0.0353  181 LEU A CD2 
1384 N N   . THR A 182 ? 0.3852 0.3787 0.4676 0.0443  -0.0098 0.0273  182 THR A N   
1385 C CA  . THR A 182 ? 0.4044 0.3887 0.4749 0.0471  -0.0115 0.0260  182 THR A CA  
1386 C C   . THR A 182 ? 0.4332 0.4095 0.4976 0.0430  -0.0121 0.0263  182 THR A C   
1387 O O   . THR A 182 ? 0.4497 0.4310 0.5210 0.0373  -0.0110 0.0271  182 THR A O   
1388 C CB  . THR A 182 ? 0.4158 0.3916 0.4774 0.0491  -0.0114 0.0254  182 THR A CB  
1389 O OG1 . THR A 182 ? 0.4295 0.4038 0.4928 0.0434  -0.0078 0.0266  182 THR A OG1 
1390 C CG2 . THR A 182 ? 0.4248 0.4099 0.4908 0.0537  -0.0131 0.0231  182 THR A CG2 
1391 N N   . GLU A 183 ? 0.4480 0.4127 0.4997 0.0463  -0.0140 0.0248  183 GLU A N   
1392 C CA  . GLU A 183 ? 0.4522 0.4055 0.4951 0.0413  -0.0150 0.0237  183 GLU A CA  
1393 C C   . GLU A 183 ? 0.4785 0.4119 0.5073 0.0362  -0.0133 0.0243  183 GLU A C   
1394 O O   . GLU A 183 ? 0.4952 0.4188 0.5148 0.0408  -0.0127 0.0256  183 GLU A O   
1395 C CB  . GLU A 183 ? 0.4747 0.4217 0.5078 0.0479  -0.0176 0.0208  183 GLU A CB  
1396 C CG  . GLU A 183 ? 0.4844 0.4492 0.5274 0.0515  -0.0175 0.0205  183 GLU A CG  
1397 C CD  . GLU A 183 ? 0.5121 0.4719 0.5441 0.0577  -0.0186 0.0167  183 GLU A CD  
1398 O OE1 . GLU A 183 ? 0.5281 0.4690 0.5449 0.0616  -0.0202 0.0138  183 GLU A OE1 
1399 O OE2 . GLU A 183 ? 0.5094 0.4819 0.5456 0.0589  -0.0174 0.0165  183 GLU A OE2 
1400 N N   . MET A 184 ? 0.4875 0.4145 0.5132 0.0258  -0.0126 0.0232  184 MET A N   
1401 C CA  . MET A 184 ? 0.4926 0.3965 0.5014 0.0172  -0.0096 0.0237  184 MET A CA  
1402 C C   . MET A 184 ? 0.5094 0.3914 0.5012 0.0145  -0.0124 0.0205  184 MET A C   
1403 O O   . MET A 184 ? 0.5603 0.4472 0.5570 0.0032  -0.0130 0.0174  184 MET A O   
1404 C CB  . MET A 184 ? 0.4734 0.3906 0.4945 0.0034  -0.0046 0.0240  184 MET A CB  
1405 C CG  . MET A 184 ? 0.4438 0.3788 0.4785 0.0064  -0.0009 0.0261  184 MET A CG  
1406 S SD  . MET A 184 ? 0.4421 0.3943 0.4905 -0.0088 0.0064  0.0247  184 MET A SD  
1407 C CE  . MET A 184 ? 0.4295 0.4003 0.4918 0.0001  0.0095  0.0258  184 MET A CE  
1408 N N   . ALA A 185 ? 0.4966 0.3553 0.4683 0.0258  -0.0149 0.0201  185 ALA A N   
1409 C CA  . ALA A 185 ? 0.5345 0.3636 0.4835 0.0256  -0.0173 0.0166  185 ALA A CA  
1410 C C   . ALA A 185 ? 0.5543 0.3967 0.5122 0.0217  -0.0202 0.0114  185 ALA A C   
1411 O O   . ALA A 185 ? 0.5761 0.4108 0.5299 0.0076  -0.0205 0.0082  185 ALA A O   
1412 C CB  . ALA A 185 ? 0.5631 0.3610 0.4917 0.0109  -0.0134 0.0180  185 ALA A CB  
1413 N N   . SER A 186 ? 0.5176 0.3808 0.4869 0.0336  -0.0224 0.0104  186 SER A N   
1414 C CA  . SER A 186 ? 0.4987 0.3717 0.4708 0.0328  -0.0254 0.0059  186 SER A CA  
1415 C C   . SER A 186 ? 0.5160 0.3595 0.4628 0.0384  -0.0275 0.0001  186 SER A C   
1416 O O   . SER A 186 ? 0.5368 0.3603 0.4682 0.0506  -0.0273 -0.0002 186 SER A O   
1417 C CB  . SER A 186 ? 0.4737 0.3746 0.4617 0.0426  -0.0252 0.0073  186 SER A CB  
1418 O OG  . SER A 186 ? 0.4791 0.3769 0.4610 0.0574  -0.0243 0.0062  186 SER A OG  
1419 N N   . ILE A 187 ? 0.5196 0.3602 0.4608 0.0309  -0.0304 -0.0052 187 ILE A N   
1420 C CA  . ILE A 187 ? 0.5602 0.3728 0.4761 0.0369  -0.0326 -0.0124 187 ILE A CA  
1421 C C   . ILE A 187 ? 0.5047 0.3357 0.4239 0.0518  -0.0326 -0.0150 187 ILE A C   
1422 O O   . ILE A 187 ? 0.4350 0.2944 0.3699 0.0491  -0.0329 -0.0135 187 ILE A O   
1423 C CB  . ILE A 187 ? 0.6161 0.4143 0.5215 0.0197  -0.0360 -0.0184 187 ILE A CB  
1424 C CG1 . ILE A 187 ? 0.6892 0.4555 0.5657 0.0270  -0.0383 -0.0271 187 ILE A CG1 
1425 C CG2 . ILE A 187 ? 0.5931 0.4266 0.5193 0.0114  -0.0393 -0.0189 187 ILE A CG2 
1426 C CD1 . ILE A 187 ? 0.7567 0.5016 0.6183 0.0087  -0.0419 -0.0344 187 ILE A CD1 
1427 N N   . ASN A 188 ? 0.5478 0.3626 0.4513 0.0682  -0.0317 -0.0190 188 ASN A N   
1428 C CA  . ASN A 188 ? 0.5871 0.4202 0.4926 0.0825  -0.0297 -0.0228 188 ASN A CA  
1429 C C   . ASN A 188 ? 0.6245 0.4278 0.5020 0.0929  -0.0309 -0.0323 188 ASN A C   
1430 O O   . ASN A 188 ? 0.6420 0.4171 0.5028 0.1037  -0.0317 -0.0344 188 ASN A O   
1431 C CB  . ASN A 188 ? 0.5953 0.4510 0.5169 0.0958  -0.0263 -0.0191 188 ASN A CB  
1432 C CG  . ASN A 188 ? 0.6093 0.4992 0.5576 0.0876  -0.0239 -0.0120 188 ASN A CG  
1433 O OD1 . ASN A 188 ? 0.6306 0.5443 0.5882 0.0888  -0.0208 -0.0119 188 ASN A OD1 
1434 N ND2 . ASN A 188 ? 0.6048 0.4945 0.5629 0.0793  -0.0248 -0.0059 188 ASN A ND2 
1435 N N   . ASN A 189 ? 0.6605 0.4678 0.5303 0.0908  -0.0314 -0.0384 189 ASN A N   
1436 C CA  . ASN A 189 ? 0.7406 0.5211 0.5827 0.1019  -0.0319 -0.0490 189 ASN A CA  
1437 C C   . ASN A 189 ? 0.8066 0.6106 0.6486 0.1070  -0.0288 -0.0538 189 ASN A C   
1438 O O   . ASN A 189 ? 0.8017 0.6420 0.6646 0.1080  -0.0245 -0.0483 189 ASN A O   
1439 C CB  . ASN A 189 ? 0.7563 0.4963 0.5748 0.0879  -0.0372 -0.0540 189 ASN A CB  
1440 C CG  . ASN A 189 ? 0.7186 0.4741 0.5483 0.0654  -0.0411 -0.0521 189 ASN A CG  
1441 O OD1 . ASN A 189 ? 0.6925 0.4824 0.5385 0.0639  -0.0407 -0.0493 189 ASN A OD1 
1442 N ND2 . ASN A 189 ? 0.7313 0.4618 0.5520 0.0479  -0.0448 -0.0536 189 ASN A ND2 
1443 N N   . ARG A 190 ? 0.8702 0.6511 0.6859 0.1091  -0.0307 -0.0641 190 ARG A N   
1444 C CA  . ARG A 190 ? 0.8919 0.6923 0.7023 0.1133  -0.0274 -0.0690 190 ARG A CA  
1445 C C   . ARG A 190 ? 0.8740 0.6985 0.6968 0.0965  -0.0303 -0.0625 190 ARG A C   
1446 O O   . ARG A 190 ? 0.8837 0.7341 0.7104 0.0994  -0.0257 -0.0606 190 ARG A O   
1447 C CB  . ARG A 190 ? 0.9578 0.7243 0.7338 0.1188  -0.0296 -0.0826 190 ARG A CB  
1448 C CG  . ARG A 190 ? 0.9869 0.7708 0.7523 0.1294  -0.0237 -0.0895 190 ARG A CG  
1449 C CD  . ARG A 190 ? 1.0610 0.8125 0.7913 0.1284  -0.0280 -0.1028 190 ARG A CD  
1450 N NE  . ARG A 190 ? 1.1124 0.8159 0.8221 0.1288  -0.0334 -0.1095 190 ARG A NE  
1451 C CZ  . ARG A 190 ? 1.1480 0.8216 0.8422 0.1102  -0.0420 -0.1135 190 ARG A CZ  
1452 N NH1 . ARG A 190 ? 1.1427 0.8339 0.8417 0.0920  -0.0476 -0.1123 190 ARG A NH1 
1453 N NH2 . ARG A 190 ? 1.1873 0.8130 0.8599 0.1099  -0.0452 -0.1189 190 ARG A NH2 
1454 N N   . VAL A 191 ? 0.8445 0.6613 0.6731 0.0793  -0.0375 -0.0591 191 VAL A N   
1455 C CA  . VAL A 191 ? 0.8214 0.6586 0.6591 0.0653  -0.0429 -0.0550 191 VAL A CA  
1456 C C   . VAL A 191 ? 0.7612 0.6256 0.6293 0.0604  -0.0415 -0.0426 191 VAL A C   
1457 O O   . VAL A 191 ? 0.7599 0.6482 0.6375 0.0576  -0.0424 -0.0368 191 VAL A O   
1458 C CB  . VAL A 191 ? 0.8668 0.6833 0.6928 0.0490  -0.0524 -0.0618 191 VAL A CB  
1459 C CG1 . VAL A 191 ? 0.8695 0.7119 0.7066 0.0371  -0.0598 -0.0587 191 VAL A CG1 
1460 C CG2 . VAL A 191 ? 0.9111 0.6960 0.7036 0.0535  -0.0540 -0.0753 191 VAL A CG2 
1461 N N   . TYR A 192 ? 0.7200 0.5780 0.6002 0.0602  -0.0395 -0.0385 192 TYR A N   
1462 C CA  . TYR A 192 ? 0.6628 0.5423 0.5695 0.0552  -0.0383 -0.0282 192 TYR A CA  
1463 C C   . TYR A 192 ? 0.6210 0.5123 0.5388 0.0678  -0.0308 -0.0237 192 TYR A C   
1464 O O   . TYR A 192 ? 0.6168 0.4931 0.5258 0.0785  -0.0283 -0.0277 192 TYR A O   
1465 C CB  . TYR A 192 ? 0.6684 0.5343 0.5803 0.0426  -0.0417 -0.0272 192 TYR A CB  
1466 C CG  . TYR A 192 ? 0.6998 0.5565 0.6028 0.0278  -0.0490 -0.0336 192 TYR A CG  
1467 C CD1 . TYR A 192 ? 0.7329 0.5593 0.6220 0.0177  -0.0507 -0.0390 192 TYR A CD1 
1468 C CD2 . TYR A 192 ? 0.7040 0.5816 0.6107 0.0232  -0.0547 -0.0344 192 TYR A CD2 
1469 C CE1 . TYR A 192 ? 0.7514 0.5719 0.6339 0.0013  -0.0574 -0.0463 192 TYR A CE1 
1470 C CE2 . TYR A 192 ? 0.7274 0.6013 0.6278 0.0094  -0.0630 -0.0417 192 TYR A CE2 
1471 C CZ  . TYR A 192 ? 0.7524 0.5994 0.6423 -0.0027 -0.0640 -0.0482 192 TYR A CZ  
1472 O OH  . TYR A 192 ? 0.7802 0.6259 0.6654 -0.0192 -0.0722 -0.0568 192 TYR A OH  
1473 N N   . ARG A 193 ? 0.5895 0.5073 0.5260 0.0668  -0.0279 -0.0160 193 ARG A N   
1474 C CA  . ARG A 193 ? 0.5408 0.4744 0.4898 0.0759  -0.0210 -0.0127 193 ARG A CA  
1475 C C   . ARG A 193 ? 0.4992 0.4508 0.4699 0.0691  -0.0202 -0.0036 193 ARG A C   
1476 O O   . ARG A 193 ? 0.5137 0.4752 0.4878 0.0629  -0.0217 0.0009  193 ARG A O   
1477 C CB  . ARG A 193 ? 0.5340 0.4809 0.4761 0.0839  -0.0146 -0.0157 193 ARG A CB  
1478 N N   . THR A 194 ? 0.4377 0.3915 0.4206 0.0715  -0.0186 -0.0012 194 THR A N   
1479 C CA  . THR A 194 ? 0.3923 0.3612 0.3942 0.0666  -0.0171 0.0060  194 THR A CA  
1480 C C   . THR A 194 ? 0.3634 0.3472 0.3754 0.0737  -0.0117 0.0058  194 THR A C   
1481 O O   . THR A 194 ? 0.3763 0.3607 0.3828 0.0838  -0.0097 0.0000  194 THR A O   
1482 C CB  . THR A 194 ? 0.4074 0.3666 0.4149 0.0603  -0.0207 0.0083  194 THR A CB  
1483 O OG1 . THR A 194 ? 0.4397 0.3830 0.4392 0.0662  -0.0210 0.0051  194 THR A OG1 
1484 C CG2 . THR A 194 ? 0.4077 0.3591 0.4099 0.0510  -0.0258 0.0073  194 THR A CG2 
1485 N N   . ILE A 195 ? 0.3492 0.3461 0.3766 0.0687  -0.0097 0.0112  195 ILE A N   
1486 C CA  . ILE A 195 ? 0.3813 0.3957 0.4206 0.0724  -0.0051 0.0102  195 ILE A CA  
1487 C C   . ILE A 195 ? 0.4090 0.4187 0.4503 0.0798  -0.0084 0.0071  195 ILE A C   
1488 O O   . ILE A 195 ? 0.3897 0.4137 0.4370 0.0880  -0.0068 0.0027  195 ILE A O   
1489 C CB  . ILE A 195 ? 0.3954 0.4203 0.4471 0.0634  -0.0022 0.0162  195 ILE A CB  
1490 C CG1 . ILE A 195 ? 0.4035 0.4494 0.4677 0.0637  0.0033  0.0138  195 ILE A CG1 
1491 C CG2 . ILE A 195 ? 0.4094 0.4252 0.4669 0.0592  -0.0066 0.0199  195 ILE A CG2 
1492 C CD1 . ILE A 195 ? 0.4092 0.4695 0.4702 0.0653  0.0104  0.0105  195 ILE A CD1 
1493 N N   . GLY A 196 ? 0.4372 0.4280 0.4728 0.0773  -0.0130 0.0091  196 GLY A N   
1494 C CA  . GLY A 196 ? 0.4382 0.4194 0.4702 0.0840  -0.0161 0.0077  196 GLY A CA  
1495 C C   . GLY A 196 ? 0.4254 0.4208 0.4716 0.0826  -0.0159 0.0098  196 GLY A C   
1496 O O   . GLY A 196 ? 0.4260 0.4105 0.4699 0.0798  -0.0180 0.0125  196 GLY A O   
1497 N N   . SER A 197 ? 0.3805 0.4003 0.4405 0.0831  -0.0127 0.0079  197 SER A N   
1498 C CA  . SER A 197 ? 0.3335 0.3676 0.4068 0.0806  -0.0130 0.0080  197 SER A CA  
1499 C C   . SER A 197 ? 0.3089 0.3361 0.3861 0.0691  -0.0120 0.0137  197 SER A C   
1500 O O   . SER A 197 ? 0.2658 0.2874 0.3414 0.0627  -0.0100 0.0174  197 SER A O   
1501 C CB  . SER A 197 ? 0.3115 0.3740 0.3994 0.0795  -0.0085 0.0042  197 SER A CB  
1502 O OG  . SER A 197 ? 0.3335 0.4087 0.4213 0.0925  -0.0094 -0.0028 197 SER A OG  
1503 N N   . PRO A 198 ? 0.3073 0.3353 0.3887 0.0678  -0.0140 0.0138  198 PRO A N   
1504 C CA  . PRO A 198 ? 0.2941 0.3185 0.3807 0.0586  -0.0121 0.0176  198 PRO A CA  
1505 C C   . PRO A 198 ? 0.2855 0.3217 0.3820 0.0513  -0.0078 0.0182  198 PRO A C   
1506 O O   . PRO A 198 ? 0.3421 0.3948 0.4452 0.0512  -0.0058 0.0147  198 PRO A O   
1507 C CB  . PRO A 198 ? 0.2948 0.3181 0.3809 0.0605  -0.0151 0.0157  198 PRO A CB  
1508 C CG  . PRO A 198 ? 0.3064 0.3246 0.3818 0.0712  -0.0196 0.0133  198 PRO A CG  
1509 C CD  . PRO A 198 ? 0.3082 0.3377 0.3866 0.0765  -0.0188 0.0102  198 PRO A CD  
1510 N N   . LEU A 199 ? 0.2515 0.2790 0.3483 0.0452  -0.0061 0.0227  199 LEU A N   
1511 C CA  . LEU A 199 ? 0.2736 0.3030 0.3736 0.0380  -0.0019 0.0251  199 LEU A CA  
1512 C C   . LEU A 199 ? 0.3078 0.3299 0.4108 0.0335  -0.0017 0.0254  199 LEU A C   
1513 O O   . LEU A 199 ? 0.3465 0.3591 0.4476 0.0362  -0.0037 0.0268  199 LEU A O   
1514 C CB  . LEU A 199 ? 0.2899 0.3109 0.3824 0.0377  -0.0011 0.0304  199 LEU A CB  
1515 C CG  . LEU A 199 ? 0.2824 0.3062 0.3683 0.0424  -0.0019 0.0293  199 LEU A CG  
1516 C CD1 . LEU A 199 ? 0.2274 0.2436 0.3045 0.0413  -0.0021 0.0342  199 LEU A CD1 
1517 C CD2 . LEU A 199 ? 0.2210 0.2602 0.3098 0.0433  0.0018  0.0248  199 LEU A CD2 
1518 N N   . VAL A 200 ? 0.3106 0.3375 0.4181 0.0261  0.0013  0.0234  200 VAL A N   
1519 C CA  . VAL A 200 ? 0.3061 0.3228 0.4140 0.0208  0.0018  0.0224  200 VAL A CA  
1520 C C   . VAL A 200 ? 0.3148 0.3165 0.4163 0.0142  0.0062  0.0277  200 VAL A C   
1521 O O   . VAL A 200 ? 0.2866 0.2933 0.3879 0.0058  0.0110  0.0282  200 VAL A O   
1522 C CB  . VAL A 200 ? 0.2944 0.3249 0.4101 0.0158  0.0009  0.0149  200 VAL A CB  
1523 C CG1 . VAL A 200 ? 0.3013 0.3178 0.4147 0.0087  0.0017  0.0129  200 VAL A CG1 
1524 C CG2 . VAL A 200 ? 0.2839 0.3241 0.4008 0.0250  -0.0049 0.0108  200 VAL A CG2 
1525 N N   . PHE A 201 ? 0.3296 0.3128 0.4246 0.0184  0.0049  0.0316  201 PHE A N   
1526 C CA  . PHE A 201 ? 0.3600 0.3230 0.4441 0.0157  0.0076  0.0377  201 PHE A CA  
1527 C C   . PHE A 201 ? 0.3932 0.3374 0.4731 0.0108  0.0090  0.0355  201 PHE A C   
1528 O O   . PHE A 201 ? 0.3835 0.3270 0.4673 0.0154  0.0065  0.0308  201 PHE A O   
1529 C CB  . PHE A 201 ? 0.3514 0.3066 0.4302 0.0265  0.0037  0.0431  201 PHE A CB  
1530 C CG  . PHE A 201 ? 0.3571 0.3266 0.4371 0.0302  0.0017  0.0446  201 PHE A CG  
1531 C CD1 . PHE A 201 ? 0.3583 0.3411 0.4464 0.0351  -0.0016 0.0409  201 PHE A CD1 
1532 C CD2 . PHE A 201 ? 0.3762 0.3426 0.4461 0.0282  0.0036  0.0496  201 PHE A CD2 
1533 C CE1 . PHE A 201 ? 0.3651 0.3565 0.4517 0.0376  -0.0036 0.0413  201 PHE A CE1 
1534 C CE2 . PHE A 201 ? 0.3849 0.3626 0.4537 0.0318  0.0015  0.0497  201 PHE A CE2 
1535 C CZ  . PHE A 201 ? 0.3748 0.3643 0.4523 0.0364  -0.0024 0.0451  201 PHE A CZ  
1536 N N   . PRO A 202 ? 0.4369 0.3634 0.5064 0.0011  0.0136  0.0386  202 PRO A N   
1537 C CA  . PRO A 202 ? 0.4642 0.3659 0.5256 -0.0043 0.0151  0.0362  202 PRO A CA  
1538 C C   . PRO A 202 ? 0.4900 0.3652 0.5391 0.0087  0.0122  0.0411  202 PRO A C   
1539 O O   . PRO A 202 ? 0.4707 0.3518 0.5209 0.0214  0.0084  0.0454  202 PRO A O   
1540 C CB  . PRO A 202 ? 0.4654 0.3569 0.5182 -0.0215 0.0222  0.0385  202 PRO A CB  
1541 C CG  . PRO A 202 ? 0.4671 0.3634 0.5140 -0.0184 0.0240  0.0468  202 PRO A CG  
1542 C CD  . PRO A 202 ? 0.4311 0.3571 0.4930 -0.0067 0.0188  0.0442  202 PRO A CD  
1543 N N   . LYS A 203 ? 0.5453 0.3913 0.5826 0.0059  0.0137  0.0393  203 LYS A N   
1544 C CA  . LYS A 203 ? 0.5948 0.4116 0.6177 0.0199  0.0111  0.0438  203 LYS A CA  
1545 C C   . LYS A 203 ? 0.5982 0.3995 0.6053 0.0231  0.0111  0.0550  203 LYS A C   
1546 O O   . LYS A 203 ? 0.6124 0.4179 0.6154 0.0106  0.0155  0.0592  203 LYS A O   
1547 C CB  . LYS A 203 ? 0.6766 0.4581 0.6848 0.0152  0.0133  0.0396  203 LYS A CB  
1548 C CG  . LYS A 203 ? 0.7043 0.4938 0.7221 0.0180  0.0119  0.0285  203 LYS A CG  
1549 C CD  A LYS A 203 ? 0.7654 0.5137 0.7642 0.0159  0.0136  0.0241  203 LYS A CD  
1550 C CD  B LYS A 203 ? 0.7655 0.5140 0.7644 0.0151  0.0137  0.0240  203 LYS A CD  
1551 C CE  A LYS A 203 ? 0.7791 0.5182 0.7758 0.0371  0.0106  0.0202  203 LYS A CE  
1552 C CE  B LYS A 203 ? 0.8015 0.5285 0.7877 -0.0078 0.0189  0.0251  203 LYS A CE  
1553 N NZ  A LYS A 203 ? 0.7889 0.5272 0.7839 0.0566  0.0070  0.0286  203 LYS A NZ  
1554 N NZ  B LYS A 203 ? 0.7913 0.5513 0.7953 -0.0261 0.0204  0.0174  203 LYS A NZ  
1555 N N   . HIS A 204 ? 0.5926 0.3779 0.5905 0.0411  0.0058  0.0594  204 HIS A N   
1556 C CA  . HIS A 204 ? 0.6150 0.3788 0.5922 0.0478  0.0037  0.0704  204 HIS A CA  
1557 C C   . HIS A 204 ? 0.5962 0.3879 0.5799 0.0466  0.0023  0.0747  204 HIS A C   
1558 O O   . HIS A 204 ? 0.6461 0.4232 0.6112 0.0512  0.0003  0.0838  204 HIS A O   
1559 C CB  . HIS A 204 ? 0.6313 0.3527 0.5813 0.0337  0.0103  0.0759  204 HIS A CB  
1560 C CG  . HIS A 204 ? 0.6438 0.3291 0.5815 0.0353  0.0111  0.0717  204 HIS A CG  
1561 N ND1 . HIS A 204 ? 0.6497 0.3248 0.5866 0.0575  0.0046  0.0691  204 HIS A ND1 
1562 C CD2 . HIS A 204 ? 0.6660 0.3236 0.5917 0.0172  0.0178  0.0684  204 HIS A CD2 
1563 C CE1 . HIS A 204 ? 0.6782 0.3177 0.6009 0.0545  0.0073  0.0645  204 HIS A CE1 
1564 N NE2 . HIS A 204 ? 0.6926 0.3196 0.6077 0.0292  0.0150  0.0641  204 HIS A NE2 
1565 N N   . HIS A 205 ? 0.5319 0.3607 0.5386 0.0413  0.0030  0.0683  205 HIS A N   
1566 C CA  . HIS A 205 ? 0.4693 0.3238 0.4824 0.0421  0.0011  0.0704  205 HIS A CA  
1567 C C   . HIS A 205 ? 0.4718 0.3464 0.4984 0.0576  -0.0071 0.0679  205 HIS A C   
1568 O O   . HIS A 205 ? 0.4821 0.3696 0.5245 0.0611  -0.0080 0.0609  205 HIS A O   
1569 C CB  . HIS A 205 ? 0.3916 0.2720 0.4194 0.0286  0.0063  0.0646  205 HIS A CB  
1570 C CG  . HIS A 205 ? 0.3840 0.2574 0.4009 0.0131  0.0144  0.0678  205 HIS A CG  
1571 N ND1 . HIS A 205 ? 0.3613 0.2601 0.3864 0.0057  0.0184  0.0655  205 HIS A ND1 
1572 C CD2 . HIS A 205 ? 0.4184 0.2621 0.4161 0.0031  0.0203  0.0729  205 HIS A CD2 
1573 C CE1 . HIS A 205 ? 0.3946 0.2846 0.4088 -0.0086 0.0270  0.0684  205 HIS A CE1 
1574 N NE2 . HIS A 205 ? 0.4276 0.2829 0.4242 -0.0120 0.0286  0.0733  205 HIS A NE2 
1575 N N   . VAL A 206 ? 0.4661 0.3443 0.4856 0.0657  -0.0127 0.0731  206 VAL A N   
1576 C CA  . VAL A 206 ? 0.4444 0.3424 0.4762 0.0794  -0.0212 0.0706  206 VAL A CA  
1577 C C   . VAL A 206 ? 0.4347 0.3593 0.4757 0.0746  -0.0228 0.0682  206 VAL A C   
1578 O O   . VAL A 206 ? 0.4388 0.3602 0.4662 0.0720  -0.0233 0.0729  206 VAL A O   
1579 C CB  . VAL A 206 ? 0.4518 0.3331 0.4677 0.0950  -0.0292 0.0771  206 VAL A CB  
1580 C CG1 . VAL A 206 ? 0.4339 0.3437 0.4671 0.1080  -0.0384 0.0726  206 VAL A CG1 
1581 C CG2 . VAL A 206 ? 0.4503 0.2987 0.4531 0.1011  -0.0275 0.0792  206 VAL A CG2 
1582 N N   . VAL A 207 ? 0.4146 0.3623 0.4756 0.0733  -0.0229 0.0609  207 VAL A N   
1583 C CA  . VAL A 207 ? 0.3949 0.3639 0.4635 0.0696  -0.0251 0.0577  207 VAL A CA  
1584 C C   . VAL A 207 ? 0.3970 0.3820 0.4742 0.0789  -0.0336 0.0557  207 VAL A C   
1585 O O   . VAL A 207 ? 0.3787 0.3724 0.4690 0.0849  -0.0347 0.0521  207 VAL A O   
1586 C CB  . VAL A 207 ? 0.3914 0.3719 0.4727 0.0616  -0.0201 0.0514  207 VAL A CB  
1587 C CG1 . VAL A 207 ? 0.3857 0.3826 0.4724 0.0590  -0.0229 0.0478  207 VAL A CG1 
1588 C CG2 . VAL A 207 ? 0.4039 0.3759 0.4793 0.0530  -0.0134 0.0520  207 VAL A CG2 
1589 N N   . SER A 208 ? 0.4158 0.4071 0.4860 0.0798  -0.0395 0.0572  208 SER A N   
1590 C CA  . SER A 208 ? 0.4233 0.4336 0.5021 0.0875  -0.0492 0.0543  208 SER A CA  
1591 C C   . SER A 208 ? 0.4172 0.4443 0.5016 0.0785  -0.0509 0.0488  208 SER A C   
1592 O O   . SER A 208 ? 0.4479 0.4671 0.5185 0.0729  -0.0495 0.0501  208 SER A O   
1593 C CB  . SER A 208 ? 0.4513 0.4510 0.5124 0.0989  -0.0577 0.0608  208 SER A CB  
1594 O OG  . SER A 208 ? 0.4500 0.4732 0.5219 0.1074  -0.0688 0.0568  208 SER A OG  
1595 N N   . LEU A 209 ? 0.3861 0.4354 0.4897 0.0766  -0.0532 0.0420  209 LEU A N   
1596 C CA  . LEU A 209 ? 0.3591 0.4219 0.4668 0.0670  -0.0557 0.0360  209 LEU A CA  
1597 C C   . LEU A 209 ? 0.3550 0.4377 0.4674 0.0723  -0.0676 0.0330  209 LEU A C   
1598 O O   . LEU A 209 ? 0.3419 0.4416 0.4688 0.0813  -0.0722 0.0315  209 LEU A O   
1599 C CB  . LEU A 209 ? 0.3569 0.4295 0.4804 0.0576  -0.0491 0.0302  209 LEU A CB  
1600 C CG  . LEU A 209 ? 0.3730 0.4289 0.4926 0.0539  -0.0391 0.0322  209 LEU A CG  
1601 C CD1 . LEU A 209 ? 0.3490 0.4122 0.4788 0.0447  -0.0335 0.0272  209 LEU A CD1 
1602 C CD2 . LEU A 209 ? 0.3914 0.4296 0.4936 0.0509  -0.0368 0.0349  209 LEU A CD2 
1603 N N   . GLN A 210 ? 0.3556 0.4376 0.4558 0.0678  -0.0732 0.0313  210 GLN A N   
1604 C CA  . GLN A 210 ? 0.3633 0.4638 0.4644 0.0727  -0.0865 0.0281  210 GLN A CA  
1605 C C   . GLN A 210 ? 0.3671 0.4804 0.4730 0.0584  -0.0893 0.0187  210 GLN A C   
1606 O O   . GLN A 210 ? 0.3685 0.4636 0.4585 0.0501  -0.0850 0.0180  210 GLN A O   
1607 C CB  . GLN A 210 ? 0.3741 0.4569 0.4482 0.0824  -0.0924 0.0354  210 GLN A CB  
1608 C CG  . GLN A 210 ? 0.4007 0.4674 0.4671 0.0961  -0.0910 0.0447  210 GLN A CG  
1609 C CD  . GLN A 210 ? 0.4609 0.5036 0.4953 0.1028  -0.0939 0.0536  210 GLN A CD  
1610 O OE1 . GLN A 210 ? 0.4853 0.5292 0.5045 0.1007  -0.1000 0.0521  210 GLN A OE1 
1611 N NE2 . GLN A 210 ? 0.4787 0.4974 0.5004 0.1098  -0.0890 0.0626  210 GLN A NE2 
1612 N N   . PRO A 211 ? 0.3770 0.5210 0.5043 0.0548  -0.0960 0.0107  211 PRO A N   
1613 C CA  . PRO A 211 ? 0.3995 0.5531 0.5307 0.0377  -0.0979 0.0011  211 PRO A CA  
1614 C C   . PRO A 211 ? 0.4476 0.5940 0.5571 0.0371  -0.1080 -0.0012 211 PRO A C   
1615 O O   . PRO A 211 ? 0.4735 0.6214 0.5714 0.0506  -0.1176 0.0027  211 PRO A O   
1616 C CB  . PRO A 211 ? 0.3793 0.5736 0.5412 0.0350  -0.1030 -0.0070 211 PRO A CB  
1617 C CG  . PRO A 211 ? 0.3794 0.5866 0.5477 0.0564  -0.1101 -0.0021 211 PRO A CG  
1618 C CD  . PRO A 211 ? 0.3745 0.5466 0.5245 0.0658  -0.1012 0.0092  211 PRO A CD  
1619 N N   . VAL A 212 ? 0.4604 0.5957 0.5610 0.0218  -0.1056 -0.0078 212 VAL A N   
1620 C CA  . VAL A 212 ? 0.5054 0.6324 0.5839 0.0191  -0.1143 -0.0125 212 VAL A CA  
1621 C C   . VAL A 212 ? 0.5646 0.7159 0.6555 0.0046  -0.1239 -0.0254 212 VAL A C   
1622 O O   . VAL A 212 ? 0.6018 0.7661 0.6854 0.0073  -0.1378 -0.0302 212 VAL A O   
1623 C CB  . VAL A 212 ? 0.5025 0.5936 0.5560 0.0147  -0.1048 -0.0112 212 VAL A CB  
1624 C CG1 . VAL A 212 ? 0.5172 0.5984 0.5448 0.0142  -0.1131 -0.0164 212 VAL A CG1 
1625 C CG2 . VAL A 212 ? 0.4863 0.5594 0.5322 0.0265  -0.0947 0.0000  212 VAL A CG2 
1626 N N   . ASN A 213 ? 0.5714 0.7290 0.6797 -0.0120 -0.1168 -0.0312 213 ASN A N   
1627 C CA  . ASN A 213 ? 0.5806 0.7627 0.7032 -0.0302 -0.1239 -0.0442 213 ASN A CA  
1628 C C   . ASN A 213 ? 0.5736 0.7944 0.7329 -0.0348 -0.1214 -0.0471 213 ASN A C   
1629 O O   . ASN A 213 ? 0.5611 0.8192 0.7402 -0.0237 -0.1317 -0.0488 213 ASN A O   
1630 C CB  . ASN A 213 ? 0.6063 0.7572 0.7120 -0.0504 -0.1166 -0.0502 213 ASN A CB  
1631 C CG  . ASN A 213 ? 0.6466 0.7877 0.7302 -0.0570 -0.1278 -0.0595 213 ASN A CG  
1632 O OD1 . ASN A 213 ? 0.6554 0.8227 0.7507 -0.0702 -0.1381 -0.0710 213 ASN A OD1 
1633 N ND2 . ASN A 213 ? 0.6725 0.7775 0.7244 -0.0483 -0.1255 -0.0558 213 ASN A ND2 
1634 N N   . ASP A 214 ? 0.5895 0.8016 0.7565 -0.0501 -0.1075 -0.0477 214 ASP A N   
1635 C CA  . ASP A 214 ? 0.5874 0.8353 0.7876 -0.0558 -0.1018 -0.0506 214 ASP A CA  
1636 C C   . ASP A 214 ? 0.5511 0.8085 0.7620 -0.0322 -0.0995 -0.0412 214 ASP A C   
1637 O O   . ASP A 214 ? 0.5537 0.7784 0.7452 -0.0195 -0.0942 -0.0309 214 ASP A O   
1638 C CB  . ASP A 214 ? 0.6272 0.8547 0.8249 -0.0770 -0.0858 -0.0514 214 ASP A CB  
1639 C CG  . ASP A 214 ? 0.6650 0.9327 0.8961 -0.0890 -0.0787 -0.0571 214 ASP A CG  
1640 O OD1 . ASP A 214 ? 0.6698 0.9842 0.9292 -0.0787 -0.0863 -0.0611 214 ASP A OD1 
1641 O OD2 . ASP A 214 ? 0.6917 0.9439 0.9194 -0.1083 -0.0651 -0.0576 214 ASP A OD2 
1642 N N   . LYS A 215 ? 0.5243 0.8275 0.7665 -0.0265 -0.1036 -0.0459 215 LYS A N   
1643 C CA  . LYS A 215 ? 0.4979 0.8107 0.7506 -0.0032 -0.1024 -0.0388 215 LYS A CA  
1644 C C   . LYS A 215 ? 0.4423 0.7733 0.7186 -0.0089 -0.0882 -0.0406 215 LYS A C   
1645 O O   . LYS A 215 ? 0.4038 0.7497 0.6935 0.0096  -0.0871 -0.0377 215 LYS A O   
1646 C CB  . LYS A 215 ? 0.5401 0.8886 0.8061 0.0156  -0.1199 -0.0420 215 LYS A CB  
1647 C CG  . LYS A 215 ? 0.5888 0.9244 0.8308 0.0194  -0.1350 -0.0419 215 LYS A CG  
1648 C CD  . LYS A 215 ? 0.6169 0.9797 0.8649 0.0434  -0.1529 -0.0420 215 LYS A CD  
1649 C CE  . LYS A 215 ? 0.6230 0.9546 0.8507 0.0685  -0.1516 -0.0278 215 LYS A CE  
1650 N NZ  . LYS A 215 ? 0.6374 0.9916 0.8690 0.0945  -0.1686 -0.0268 215 LYS A NZ  
1651 N N   . ASP A 216 ? 0.4442 0.7717 0.7231 -0.0337 -0.0768 -0.0452 216 ASP A N   
1652 C CA  . ASP A 216 ? 0.4498 0.7898 0.7454 -0.0417 -0.0611 -0.0463 216 ASP A CA  
1653 C C   . ASP A 216 ? 0.4630 0.7525 0.7312 -0.0453 -0.0477 -0.0366 216 ASP A C   
1654 O O   . ASP A 216 ? 0.4669 0.7215 0.7110 -0.0586 -0.0460 -0.0351 216 ASP A O   
1655 C CB  . ASP A 216 ? 0.4798 0.8528 0.7967 -0.0691 -0.0565 -0.0581 216 ASP A CB  
1656 C CG  . ASP A 216 ? 0.5249 0.9560 0.8734 -0.0662 -0.0706 -0.0697 216 ASP A CG  
1657 O OD1 . ASP A 216 ? 0.5306 0.9760 0.8845 -0.0397 -0.0834 -0.0675 216 ASP A OD1 
1658 O OD2 . ASP A 216 ? 0.5436 1.0054 0.9106 -0.0906 -0.0694 -0.0811 216 ASP A OD2 
1659 N N   . PHE A 217 ? 0.4639 0.7494 0.7348 -0.0324 -0.0391 -0.0311 217 PHE A N   
1660 C CA  . PHE A 217 ? 0.4624 0.7044 0.7088 -0.0333 -0.0281 -0.0225 217 PHE A CA  
1661 C C   . PHE A 217 ? 0.4528 0.7063 0.7106 -0.0357 -0.0138 -0.0230 217 PHE A C   
1662 O O   . PHE A 217 ? 0.4728 0.7614 0.7548 -0.0246 -0.0136 -0.0270 217 PHE A O   
1663 C CB  . PHE A 217 ? 0.4701 0.6842 0.6985 -0.0120 -0.0336 -0.0135 217 PHE A CB  
1664 C CG  . PHE A 217 ? 0.5019 0.7109 0.7204 -0.0052 -0.0476 -0.0128 217 PHE A CG  
1665 C CD1 . PHE A 217 ? 0.5244 0.7018 0.7184 -0.0128 -0.0492 -0.0108 217 PHE A CD1 
1666 C CD2 . PHE A 217 ? 0.4986 0.7331 0.7298 0.0105  -0.0593 -0.0142 217 PHE A CD2 
1667 C CE1 . PHE A 217 ? 0.5393 0.7121 0.7219 -0.0065 -0.0610 -0.0106 217 PHE A CE1 
1668 C CE2 . PHE A 217 ? 0.5121 0.7400 0.7300 0.0169  -0.0720 -0.0130 217 PHE A CE2 
1669 C CZ  . PHE A 217 ? 0.5367 0.7344 0.7304 0.0076  -0.0723 -0.0114 217 PHE A CZ  
1670 N N   . GLN A 218 ? 0.4268 0.6498 0.6653 -0.0488 -0.0021 -0.0193 218 GLN A N   
1671 C CA  . GLN A 218 ? 0.3974 0.6222 0.6380 -0.0503 0.0122  -0.0182 218 GLN A CA  
1672 C C   . GLN A 218 ? 0.3637 0.5612 0.5887 -0.0306 0.0119  -0.0103 218 GLN A C   
1673 O O   . GLN A 218 ? 0.3773 0.5361 0.5764 -0.0307 0.0117  -0.0039 218 GLN A O   
1674 C CB  . GLN A 218 ? 0.4191 0.6215 0.6421 -0.0742 0.0243  -0.0174 218 GLN A CB  
1675 C CG  . GLN A 218 ? 0.4104 0.6185 0.6346 -0.0791 0.0403  -0.0172 218 GLN A CG  
1676 C CD  . GLN A 218 ? 0.4074 0.6652 0.6623 -0.0924 0.0482  -0.0269 218 GLN A CD  
1677 O OE1 . GLN A 218 ? 0.4107 0.6924 0.6815 -0.1060 0.0432  -0.0338 218 GLN A OE1 
1678 N NE2 . GLN A 218 ? 0.3958 0.6720 0.6601 -0.0890 0.0606  -0.0286 218 GLN A NE2 
1679 N N   . ILE A 219 ? 0.3333 0.5513 0.5741 -0.0134 0.0115  -0.0116 219 ILE A N   
1680 C CA  . ILE A 219 ? 0.3114 0.5053 0.5391 0.0041  0.0109  -0.0057 219 ILE A CA  
1681 C C   . ILE A 219 ? 0.3109 0.5013 0.5349 0.0024  0.0244  -0.0061 219 ILE A C   
1682 O O   . ILE A 219 ? 0.2700 0.4909 0.5120 -0.0015 0.0327  -0.0125 219 ILE A O   
1683 C CB  . ILE A 219 ? 0.3042 0.5141 0.5454 0.0253  0.0010  -0.0065 219 ILE A CB  
1684 C CG1 . ILE A 219 ? 0.3029 0.5146 0.5434 0.0268  -0.0126 -0.0055 219 ILE A CG1 
1685 C CG2 . ILE A 219 ? 0.3027 0.4845 0.5288 0.0402  0.0014  -0.0009 219 ILE A CG2 
1686 C CD1 . ILE A 219 ? 0.2995 0.5243 0.5491 0.0478  -0.0234 -0.0054 219 ILE A CD1 
1687 N N   . SER A 220 ? 0.3516 0.5071 0.5519 0.0053  0.0267  -0.0002 220 SER A N   
1688 C CA  . SER A 220 ? 0.3687 0.5163 0.5601 0.0052  0.0380  -0.0003 220 SER A CA  
1689 C C   . SER A 220 ? 0.3854 0.5214 0.5727 0.0235  0.0348  0.0009  220 SER A C   
1690 O O   . SER A 220 ? 0.3872 0.5066 0.5679 0.0317  0.0254  0.0050  220 SER A O   
1691 C CB  . SER A 220 ? 0.3649 0.4802 0.5288 -0.0074 0.0431  0.0047  220 SER A CB  
1692 O OG  . SER A 220 ? 0.3745 0.4601 0.5202 0.0013  0.0361  0.0101  220 SER A OG  
1693 N N   . VAL A 221 ? 0.3941 0.5386 0.5845 0.0289  0.0435  -0.0032 221 VAL A N   
1694 C CA  . VAL A 221 ? 0.3938 0.5214 0.5753 0.0433  0.0425  -0.0032 221 VAL A CA  
1695 C C   . VAL A 221 ? 0.4351 0.5526 0.6007 0.0378  0.0538  -0.0046 221 VAL A C   
1696 O O   . VAL A 221 ? 0.4822 0.6206 0.6566 0.0375  0.0642  -0.0105 221 VAL A O   
1697 C CB  . VAL A 221 ? 0.3781 0.5247 0.5778 0.0606  0.0399  -0.0084 221 VAL A CB  
1698 C CG1 . VAL A 221 ? 0.3867 0.5091 0.5727 0.0731  0.0397  -0.0089 221 VAL A CG1 
1699 C CG2 . VAL A 221 ? 0.3778 0.5325 0.5890 0.0670  0.0277  -0.0061 221 VAL A CG2 
1700 N N   . ASP A 222 ? 0.4236 0.5111 0.5655 0.0342  0.0518  0.0002  222 ASP A N   
1701 C CA  . ASP A 222 ? 0.4173 0.4903 0.5379 0.0291  0.0603  0.0001  222 ASP A CA  
1702 C C   . ASP A 222 ? 0.4442 0.5275 0.5630 0.0136  0.0708  0.0005  222 ASP A C   
1703 O O   . ASP A 222 ? 0.4603 0.5368 0.5754 0.0030  0.0677  0.0049  222 ASP A O   
1704 C CB  . ASP A 222 ? 0.3838 0.4585 0.5037 0.0408  0.0646  -0.0062 222 ASP A CB  
1705 C CG  . ASP A 222 ? 0.3420 0.4012 0.4610 0.0528  0.0545  -0.0063 222 ASP A CG  
1706 O OD1 . ASP A 222 ? 0.3225 0.3629 0.4309 0.0503  0.0464  -0.0013 222 ASP A OD1 
1707 O OD2 . ASP A 222 ? 0.3347 0.4003 0.4629 0.0647  0.0553  -0.0117 222 ASP A OD2 
1708 N N   . HIS A 223 ? 0.4550 0.5530 0.5746 0.0106  0.0839  -0.0044 223 HIS A N   
1709 C CA  . HIS A 223 ? 0.4924 0.5995 0.6086 -0.0074 0.0960  -0.0039 223 HIS A CA  
1710 C C   . HIS A 223 ? 0.5002 0.6459 0.6488 -0.0136 0.0983  -0.0088 223 HIS A C   
1711 O O   . HIS A 223 ? 0.5049 0.6580 0.6531 -0.0325 0.1066  -0.0083 223 HIS A O   
1712 C CB  . HIS A 223 ? 0.5253 0.6331 0.6265 -0.0098 0.1110  -0.0070 223 HIS A CB  
1713 C CG  . HIS A 223 ? 0.5357 0.6703 0.6562 0.0045  0.1159  -0.0165 223 HIS A CG  
1714 N ND1 . HIS A 223 ? 0.5288 0.6542 0.6509 0.0233  0.1064  -0.0190 223 HIS A ND1 
1715 C CD2 . HIS A 223 ? 0.5443 0.7134 0.6818 0.0032  0.1299  -0.0245 223 HIS A CD2 
1716 C CE1 . HIS A 223 ? 0.5352 0.6843 0.6725 0.0345  0.1134  -0.0281 223 HIS A CE1 
1717 N NE2 . HIS A 223 ? 0.5412 0.7197 0.6895 0.0237  0.1277  -0.0319 223 HIS A NE2 
1718 N N   . LEU A 224 ? 0.5057 0.6751 0.6808 0.0012  0.0907  -0.0138 224 LEU A N   
1719 C CA  . LEU A 224 ? 0.5110 0.7207 0.7179 -0.0026 0.0902  -0.0193 224 LEU A CA  
1720 C C   . LEU A 224 ? 0.5326 0.7335 0.7393 -0.0132 0.0798  -0.0145 224 LEU A C   
1721 O O   . LEU A 224 ? 0.5486 0.7167 0.7371 -0.0096 0.0699  -0.0077 224 LEU A O   
1722 C CB  . LEU A 224 ? 0.4968 0.7309 0.7281 0.0199  0.0832  -0.0254 224 LEU A CB  
1723 C CG  . LEU A 224 ? 0.5104 0.7691 0.7537 0.0324  0.0937  -0.0344 224 LEU A CG  
1724 C CD1 . LEU A 224 ? 0.5215 0.7464 0.7370 0.0401  0.0982  -0.0330 224 LEU A CD1 
1725 C CD2 . LEU A 224 ? 0.5032 0.7895 0.7737 0.0541  0.0845  -0.0405 224 LEU A CD2 
1726 N N   . SER A 225 ? 0.5521 0.7845 0.7797 -0.0269 0.0825  -0.0192 225 SER A N   
1727 C CA  . SER A 225 ? 0.5591 0.7887 0.7897 -0.0366 0.0720  -0.0173 225 SER A CA  
1728 C C   . SER A 225 ? 0.5474 0.8286 0.8150 -0.0375 0.0692  -0.0265 225 SER A C   
1729 O O   . SER A 225 ? 0.5069 0.8212 0.7913 -0.0515 0.0811  -0.0333 225 SER A O   
1730 C CB  . SER A 225 ? 0.6047 0.8066 0.8111 -0.0607 0.0788  -0.0127 225 SER A CB  
1731 O OG  . SER A 225 ? 0.6207 0.8100 0.8237 -0.0669 0.0673  -0.0108 225 SER A OG  
1732 N N   . ILE A 226 ? 0.5689 0.8584 0.8487 -0.0227 0.0534  -0.0269 226 ILE A N   
1733 C CA  . ILE A 226 ? 0.5520 0.8912 0.8662 -0.0179 0.0468  -0.0358 226 ILE A CA  
1734 C C   . ILE A 226 ? 0.5220 0.8597 0.8364 -0.0285 0.0344  -0.0354 226 ILE A C   
1735 O O   . ILE A 226 ? 0.5195 0.8172 0.8093 -0.0277 0.0267  -0.0277 226 ILE A O   
1736 C CB  . ILE A 226 ? 0.5480 0.8987 0.8742 0.0124  0.0377  -0.0372 226 ILE A CB  
1737 C CG1 . ILE A 226 ? 0.5613 0.8954 0.8759 0.0242  0.0481  -0.0360 226 ILE A CG1 
1738 C CG2 . ILE A 226 ? 0.5337 0.9430 0.8978 0.0200  0.0333  -0.0480 226 ILE A CG2 
1739 C CD1 . ILE A 226 ? 0.5628 0.8917 0.8793 0.0531  0.0389  -0.0357 226 ILE A CD1 
1740 N N   . LEU A 227 ? 0.5258 0.9098 0.8689 -0.0386 0.0325  -0.0448 227 LEU A N   
1741 C CA  . LEU A 227 ? 0.5422 0.9332 0.8899 -0.0448 0.0179  -0.0471 227 LEU A CA  
1742 C C   . LEU A 227 ? 0.5286 0.9493 0.8966 -0.0189 0.0019  -0.0504 227 LEU A C   
1743 O O   . LEU A 227 ? 0.5621 1.0274 0.9588 -0.0070 0.0034  -0.0581 227 LEU A O   
1744 C CB  . LEU A 227 ? 0.5780 1.0010 0.9432 -0.0741 0.0238  -0.0564 227 LEU A CB  
1745 C CG  . LEU A 227 ? 0.6076 1.0475 0.9824 -0.0812 0.0076  -0.0620 227 LEU A CG  
1746 C CD1 . LEU A 227 ? 0.2455 0.6300 0.5846 -0.0800 -0.0018 -0.0530 227 LEU A CD1 
1747 C CD2 . LEU A 227 ? 0.2561 0.7268 0.6481 -0.1140 0.0152  -0.0723 227 LEU A CD2 
1748 N N   . HIS A 228 ? 0.4765 0.8716 0.8277 -0.0090 -0.0131 -0.0447 228 HIS A N   
1749 C CA  . HIS A 228 ? 0.4834 0.8972 0.8453 0.0156  -0.0297 -0.0457 228 HIS A CA  
1750 C C   . HIS A 228 ? 0.4688 0.8957 0.8334 0.0067  -0.0444 -0.0498 228 HIS A C   
1751 O O   . HIS A 228 ? 0.4661 0.8596 0.8075 -0.0086 -0.0452 -0.0459 228 HIS A O   
1752 C CB  . HIS A 228 ? 0.5059 0.8746 0.8411 0.0372  -0.0342 -0.0344 228 HIS A CB  
1753 C CG  . HIS A 228 ? 0.5312 0.8887 0.8640 0.0490  -0.0228 -0.0320 228 HIS A CG  
1754 N ND1 . HIS A 228 ? 0.5409 0.9061 0.8806 0.0755  -0.0276 -0.0323 228 HIS A ND1 
1755 C CD2 . HIS A 228 ? 0.5381 0.8748 0.8596 0.0385  -0.0074 -0.0296 228 HIS A CD2 
1756 C CE1 . HIS A 228 ? 0.5442 0.8942 0.8778 0.0798  -0.0153 -0.0311 228 HIS A CE1 
1757 N NE2 . HIS A 228 ? 0.5397 0.8738 0.8625 0.0576  -0.0031 -0.0294 228 HIS A NE2 
1758 N N   . ARG A 229 ? 0.4295 0.9051 0.8215 0.0177  -0.0565 -0.0584 229 ARG A N   
1759 C CA  . ARG A 229 ? 0.4128 0.9075 0.8095 0.0107  -0.0724 -0.0642 229 ARG A CA  
1760 C C   . ARG A 229 ? 0.4425 0.9330 0.8301 0.0399  -0.0915 -0.0597 229 ARG A C   
1761 O O   . ARG A 229 ? 0.4499 0.9414 0.8403 0.0661  -0.0932 -0.0560 229 ARG A O   
1762 C CB  . ARG A 229 ? 0.3837 0.9449 0.8209 -0.0035 -0.0730 -0.0797 229 ARG A CB  
1763 C CG  . ARG A 229 ? 0.3671 0.9344 0.8127 -0.0350 -0.0529 -0.0845 229 ARG A CG  
1764 C CD  . ARG A 229 ? 0.3664 0.9780 0.8364 -0.0560 -0.0548 -0.0966 229 ARG A CD  
1765 N NE  . ARG A 229 ? 0.3689 0.9870 0.8462 -0.0848 -0.0338 -0.1004 229 ARG A NE  
1766 C CZ  . ARG A 229 ? 0.3836 0.9743 0.8444 -0.1164 -0.0242 -0.1003 229 ARG A CZ  
1767 N NH1 . ARG A 229 ? 0.3945 0.9425 0.8267 -0.1209 -0.0336 -0.0956 229 ARG A NH1 
1768 N NH2 . ARG A 229 ? 0.2736 0.8658 0.7365 -0.1410 -0.0045 -0.1022 229 ARG A NH2 
1769 N N   . ASP A 230 ? 0.4588 0.9418 0.8325 0.0350  -0.1055 -0.0601 230 ASP A N   
1770 C CA  . ASP A 230 ? 0.4646 0.9417 0.8245 0.0601  -0.1245 -0.0555 230 ASP A CA  
1771 C C   . ASP A 230 ? 0.4529 0.8787 0.7830 0.0802  -0.1206 -0.0408 230 ASP A C   
1772 O O   . ASP A 230 ? 0.4708 0.8981 0.7998 0.1072  -0.1285 -0.0369 230 ASP A O   
1773 C CB  . ASP A 230 ? 0.4561 0.9822 0.8426 0.0773  -0.1359 -0.0628 230 ASP A CB  
1774 C CG  . ASP A 230 ? 0.4745 0.9886 0.8395 0.0980  -0.1556 -0.0575 230 ASP A CG  
1775 O OD1 . ASP A 230 ? 0.4720 0.9616 0.8125 0.0943  -0.1642 -0.0541 230 ASP A OD1 
1776 O OD2 . ASP A 230 ? 0.4959 1.0241 0.8669 0.1182  -0.1621 -0.0570 230 ASP A OD2 
1777 N N   . VAL A 231 ? 0.4381 0.8176 0.7434 0.0665  -0.1083 -0.0331 231 VAL A N   
1778 C CA  . VAL A 231 ? 0.4384 0.7714 0.7179 0.0801  -0.1023 -0.0206 231 VAL A CA  
1779 C C   . VAL A 231 ? 0.4605 0.7638 0.7096 0.0904  -0.1141 -0.0125 231 VAL A C   
1780 O O   . VAL A 231 ? 0.4660 0.7589 0.7007 0.0770  -0.1179 -0.0135 231 VAL A O   
1781 C CB  . VAL A 231 ? 0.4330 0.7340 0.7006 0.0620  -0.0849 -0.0168 231 VAL A CB  
1782 C CG1 . VAL A 231 ? 0.4277 0.6821 0.6674 0.0731  -0.0809 -0.0049 231 VAL A CG1 
1783 C CG2 . VAL A 231 ? 0.4345 0.7591 0.7263 0.0552  -0.0718 -0.0226 231 VAL A CG2 
1784 N N   . GLN A 232 ? 0.4681 0.7546 0.7046 0.1139  -0.1190 -0.0046 232 GLN A N   
1785 C CA  . GLN A 232 ? 0.4821 0.7349 0.6851 0.1235  -0.1274 0.0050  232 GLN A CA  
1786 C C   . GLN A 232 ? 0.4977 0.7019 0.6746 0.1187  -0.1147 0.0154  232 GLN A C   
1787 O O   . GLN A 232 ? 0.5080 0.6855 0.6579 0.1157  -0.1166 0.0214  232 GLN A O   
1788 C CB  . GLN A 232 ? 0.4974 0.7546 0.6961 0.1516  -0.1409 0.0088  232 GLN A CB  
1789 N N   . GLU A 233 ? 0.4893 0.6841 0.6739 0.1175  -0.1017 0.0167  233 GLU A N   
1790 C CA  . GLU A 233 ? 0.4595 0.6123 0.6217 0.1155  -0.0913 0.0257  233 GLU A CA  
1791 C C   . GLU A 233 ? 0.4792 0.6310 0.6549 0.1115  -0.0781 0.0235  233 GLU A C   
1792 O O   . GLU A 233 ? 0.5072 0.6799 0.7019 0.1216  -0.0781 0.0190  233 GLU A O   
1793 C CB  . GLU A 233 ? 0.4453 0.5705 0.5837 0.1339  -0.0972 0.0354  233 GLU A CB  
1794 C CG  . GLU A 233 ? 0.4262 0.5111 0.5445 0.1314  -0.0861 0.0437  233 GLU A CG  
1795 C CD  . GLU A 233 ? 0.4481 0.5033 0.5418 0.1482  -0.0913 0.0532  233 GLU A CD  
1796 O OE1 . GLU A 233 ? 0.4660 0.5325 0.5625 0.1666  -0.1026 0.0526  233 GLU A OE1 
1797 O OE2 . GLU A 233 ? 0.4582 0.4789 0.5291 0.1430  -0.0841 0.0609  233 GLU A OE2 
1798 N N   . ILE A 234 ? 0.4605 0.5895 0.6259 0.0982  -0.0674 0.0262  234 ILE A N   
1799 C CA  . ILE A 234 ? 0.4596 0.5794 0.6297 0.0953  -0.0555 0.0258  234 ILE A CA  
1800 C C   . ILE A 234 ? 0.4793 0.5624 0.6269 0.0983  -0.0517 0.0339  234 ILE A C   
1801 O O   . ILE A 234 ? 0.4903 0.5568 0.6213 0.0919  -0.0521 0.0383  234 ILE A O   
1802 C CB  . ILE A 234 ? 0.4239 0.5499 0.6009 0.0769  -0.0469 0.0212  234 ILE A CB  
1803 C CG1 . ILE A 234 ? 0.4052 0.5662 0.6025 0.0694  -0.0501 0.0130  234 ILE A CG1 
1804 C CG2 . ILE A 234 ? 0.4035 0.5214 0.5834 0.0753  -0.0357 0.0205  234 ILE A CG2 
1805 C CD1 . ILE A 234 ? 0.3960 0.5563 0.5940 0.0495  -0.0421 0.0094  234 ILE A CD1 
1806 N N   . ARG A 235 ? 0.4669 0.5378 0.6138 0.1074  -0.0478 0.0351  235 ARG A N   
1807 C CA  . ARG A 235 ? 0.4545 0.4904 0.5801 0.1098  -0.0449 0.0422  235 ARG A CA  
1808 C C   . ARG A 235 ? 0.4228 0.4478 0.5503 0.1042  -0.0347 0.0398  235 ARG A C   
1809 O O   . ARG A 235 ? 0.4083 0.4437 0.5481 0.1098  -0.0318 0.0345  235 ARG A O   
1810 C CB  . ARG A 235 ? 0.4984 0.5202 0.6132 0.1279  -0.0522 0.0468  235 ARG A CB  
1811 C CG  . ARG A 235 ? 0.5514 0.5429 0.6385 0.1273  -0.0545 0.0563  235 ARG A CG  
1812 C CD  . ARG A 235 ? 0.5960 0.5753 0.6692 0.1464  -0.0647 0.0616  235 ARG A CD  
1813 N NE  . ARG A 235 ? 0.6148 0.5783 0.6869 0.1603  -0.0635 0.0608  235 ARG A NE  
1814 C CZ  . ARG A 235 ? 0.6452 0.6058 0.7130 0.1822  -0.0730 0.0620  235 ARG A CZ  
1815 N NH1 . ARG A 235 ? 0.6701 0.6129 0.7351 0.1955  -0.0710 0.0604  235 ARG A NH1 
1816 N NH2 . ARG A 235 ? 0.6509 0.6262 0.7160 0.1922  -0.0853 0.0641  235 ARG A NH2 
1817 N N   . TYR A 236 ? 0.4135 0.4195 0.5285 0.0935  -0.0296 0.0430  236 TYR A N   
1818 C CA  . TYR A 236 ? 0.4104 0.4058 0.5247 0.0872  -0.0216 0.0405  236 TYR A CA  
1819 C C   . TYR A 236 ? 0.4461 0.4114 0.5436 0.0882  -0.0198 0.0449  236 TYR A C   
1820 O O   . TYR A 236 ? 0.4924 0.4434 0.5757 0.0875  -0.0221 0.0512  236 TYR A O   
1821 C CB  . TYR A 236 ? 0.4011 0.4022 0.5164 0.0738  -0.0177 0.0389  236 TYR A CB  
1822 C CG  . TYR A 236 ? 0.4179 0.4415 0.5463 0.0702  -0.0174 0.0342  236 TYR A CG  
1823 C CD1 . TYR A 236 ? 0.4221 0.4585 0.5624 0.0735  -0.0143 0.0293  236 TYR A CD1 
1824 C CD2 . TYR A 236 ? 0.4202 0.4507 0.5474 0.0629  -0.0193 0.0343  236 TYR A CD2 
1825 C CE1 . TYR A 236 ? 0.4158 0.4721 0.5669 0.0673  -0.0123 0.0252  236 TYR A CE1 
1826 C CE2 . TYR A 236 ? 0.4163 0.4627 0.5527 0.0571  -0.0184 0.0301  236 TYR A CE2 
1827 C CZ  . TYR A 236 ? 0.4316 0.4913 0.5802 0.0582  -0.0145 0.0258  236 TYR A CZ  
1828 O OH  . TYR A 236 ? 0.4645 0.5397 0.6214 0.0495  -0.0119 0.0218  236 TYR A OH  
1829 N N   . GLU A 237 ? 0.4397 0.3942 0.5369 0.0884  -0.0150 0.0411  237 GLU A N   
1830 C CA  . GLU A 237 ? 0.4613 0.3844 0.5423 0.0895  -0.0133 0.0437  237 GLU A CA  
1831 C C   . GLU A 237 ? 0.4647 0.3815 0.5476 0.0867  -0.0080 0.0367  237 GLU A C   
1832 O O   . GLU A 237 ? 0.4476 0.3808 0.5423 0.0921  -0.0066 0.0307  237 GLU A O   
1833 C CB  . GLU A 237 ? 0.4852 0.3941 0.5577 0.1062  -0.0190 0.0474  237 GLU A CB  
1834 C CG  . GLU A 237 ? 0.5022 0.3707 0.5503 0.1066  -0.0183 0.0533  237 GLU A CG  
1835 C CD  . GLU A 237 ? 0.5064 0.3594 0.5426 0.1261  -0.0258 0.0582  237 GLU A CD  
1836 O OE1 . GLU A 237 ? 0.4728 0.3532 0.5232 0.1384  -0.0324 0.0565  237 GLU A OE1 
1837 O OE2 . GLU A 237 ? 0.5394 0.3526 0.5514 0.1290  -0.0255 0.0635  237 GLU A OE2 
1838 N N   . VAL A 238 ? 0.4645 0.3589 0.5353 0.0769  -0.0046 0.0369  238 VAL A N   
1839 C CA  . VAL A 238 ? 0.4391 0.3241 0.5083 0.0739  -0.0007 0.0295  238 VAL A CA  
1840 C C   . VAL A 238 ? 0.4879 0.3518 0.5492 0.0885  -0.0014 0.0273  238 VAL A C   
1841 O O   . VAL A 238 ? 0.5587 0.3946 0.6044 0.0934  -0.0033 0.0326  238 VAL A O   
1842 C CB  . VAL A 238 ? 0.3941 0.2642 0.4543 0.0576  0.0022  0.0289  238 VAL A CB  
1843 C CG1 . VAL A 238 ? 0.3958 0.2494 0.4498 0.0551  0.0047  0.0207  238 VAL A CG1 
1844 C CG2 . VAL A 238 ? 0.3429 0.2389 0.4137 0.0470  0.0027  0.0284  238 VAL A CG2 
1845 N N   . SER A 239 ? 0.5937 0.5271 0.4785 -0.0032 0.0677  0.0038  239 SER A N   
1846 C CA  . SER A 239 ? 0.5083 0.4139 0.3706 0.0257  0.0517  0.0005  239 SER A CA  
1847 C C   . SER A 239 ? 0.5621 0.3975 0.3962 0.0220  0.0417  0.0128  239 SER A C   
1848 O O   . SER A 239 ? 0.6063 0.4230 0.4477 -0.0028 0.0470  0.0173  239 SER A O   
1849 C CB  . SER A 239 ? 0.5058 0.4404 0.3897 0.0410  0.0524  -0.0208 239 SER A CB  
1850 O OG  . SER A 239 ? 0.5503 0.4573 0.4146 0.0699  0.0375  -0.0263 239 SER A OG  
1851 N N   . ALA A 240 ? 0.7378 0.5337 0.5393 0.0474  0.0265  0.0172  240 ALA A N   
1852 C CA  . ALA A 240 ? 0.7987 0.5209 0.5710 0.0478  0.0161  0.0248  240 ALA A CA  
1853 C C   . ALA A 240 ? 0.7590 0.4741 0.5418 0.0605  0.0111  0.0057  240 ALA A C   
1854 O O   . ALA A 240 ? 0.7620 0.4224 0.5293 0.0520  0.0056  0.0073  240 ALA A O   
1855 C CB  . ALA A 240 ? 0.7481 0.4214 0.4756 0.0730  0.0011  0.0380  240 ALA A CB  
1856 N N   . LYS A 241 ? 0.7278 0.4970 0.5352 0.0788  0.0139  -0.0133 241 LYS A N   
1857 C CA  . LYS A 241 ? 0.7308 0.5012 0.5481 0.0888  0.0128  -0.0323 241 LYS A CA  
1858 C C   . LYS A 241 ? 0.7042 0.4969 0.5469 0.0596  0.0252  -0.0360 241 LYS A C   
1859 O O   . LYS A 241 ? 0.6578 0.4894 0.5221 0.0401  0.0372  -0.0308 241 LYS A O   
1860 C CB  . LYS A 241 ? 0.7073 0.5296 0.5400 0.1186  0.0131  -0.0515 241 LYS A CB  
1861 C CG  . LYS A 241 ? 0.7732 0.5899 0.5868 0.1513  -0.0005 -0.0493 241 LYS A CG  
1862 C CD  . LYS A 241 ? 0.7647 0.6555 0.6053 0.1729  0.0030  -0.0689 241 LYS A CD  
1863 C CE  . LYS A 241 ? 0.8181 0.7147 0.6431 0.2047  -0.0124 -0.0658 241 LYS A CE  
1864 N NZ  . LYS A 241 ? 0.7876 0.7686 0.6455 0.2196  -0.0082 -0.0861 241 LYS A NZ  
1865 N N   . LYS A 242 ? 0.7523 0.5189 0.5904 0.0585  0.0212  -0.0457 242 LYS A N   
1866 C CA  . LYS A 242 ? 0.7300 0.5146 0.5875 0.0356  0.0292  -0.0497 242 LYS A CA  
1867 C C   . LYS A 242 ? 0.7263 0.5233 0.5851 0.0511  0.0298  -0.0695 242 LYS A C   
1868 O O   . LYS A 242 ? 0.7883 0.5674 0.6308 0.0766  0.0223  -0.0808 242 LYS A O   
1869 C CB  . LYS A 242 ? 0.7841 0.5234 0.6326 0.0105  0.0231  -0.0404 242 LYS A CB  
1870 C CG  . LYS A 242 ? 0.8375 0.5505 0.6747 -0.0041 0.0224  -0.0208 242 LYS A CG  
1871 C CD  . LYS A 242 ? 0.8831 0.5627 0.7190 -0.0352 0.0201  -0.0138 242 LYS A CD  
1872 C CE  . LYS A 242 ? 0.8443 0.5729 0.7153 -0.0588 0.0303  -0.0139 242 LYS A CE  
1873 N NZ  . LYS A 242 ? 0.8661 0.5731 0.7419 -0.0899 0.0280  -0.0088 242 LYS A NZ  
1874 N N   . ILE A 243 ? 0.6658 0.4931 0.5420 0.0366  0.0392  -0.0737 243 ILE A N   
1875 C CA  . ILE A 243 ? 0.6475 0.4849 0.5202 0.0464  0.0419  -0.0904 243 ILE A CA  
1876 C C   . ILE A 243 ? 0.6685 0.4664 0.5265 0.0351  0.0313  -0.0925 243 ILE A C   
1877 O O   . ILE A 243 ? 0.6780 0.4683 0.5442 0.0120  0.0287  -0.0818 243 ILE A O   
1878 C CB  . ILE A 243 ? 0.6085 0.4972 0.5019 0.0384  0.0588  -0.0927 243 ILE A CB  
1879 C CG1 . ILE A 243 ? 0.6075 0.5031 0.4905 0.0469  0.0634  -0.1082 243 ILE A CG1 
1880 C CG2 . ILE A 243 ? 0.6021 0.4971 0.5107 0.0130  0.0622  -0.0791 243 ILE A CG2 
1881 C CD1 . ILE A 243 ? 0.5625 0.4971 0.4587 0.0367  0.0809  -0.1084 243 ILE A CD1 
1882 N N   . HIS A 244 ? 0.6875 0.4631 0.5250 0.0513  0.0250  -0.1084 244 HIS A N   
1883 C CA  . HIS A 244 ? 0.7070 0.4430 0.5267 0.0423  0.0129  -0.1146 244 HIS A CA  
1884 C C   . HIS A 244 ? 0.6530 0.4125 0.4690 0.0425  0.0181  -0.1262 244 HIS A C   
1885 O O   . HIS A 244 ? 0.6414 0.4235 0.4523 0.0605  0.0276  -0.1383 244 HIS A O   
1886 C CB  . HIS A 244 ? 0.7750 0.4578 0.5674 0.0608  0.0004  -0.1253 244 HIS A CB  
1887 C CG  . HIS A 244 ? 0.8196 0.4685 0.6064 0.0623  -0.0057 -0.1117 244 HIS A CG  
1888 N ND1 . HIS A 244 ? 0.8468 0.4539 0.6277 0.0382  -0.0137 -0.0993 244 HIS A ND1 
1889 C CD2 . HIS A 244 ? 0.8302 0.4807 0.6141 0.0849  -0.0052 -0.1082 244 HIS A CD2 
1890 C CE1 . HIS A 244 ? 0.8715 0.4504 0.6415 0.0451  -0.0164 -0.0868 244 HIS A CE1 
1891 N NE2 . HIS A 244 ? 0.8612 0.4656 0.6321 0.0753  -0.0129 -0.0918 244 HIS A NE2 
1892 N N   . PHE A 245 ? 0.6388 0.3946 0.4565 0.0224  0.0120  -0.1226 245 PHE A N   
1893 C CA  . PHE A 245 ? 0.6380 0.4093 0.4450 0.0222  0.0137  -0.1311 245 PHE A CA  
1894 C C   . PHE A 245 ? 0.6854 0.4179 0.4664 0.0215  -0.0030 -0.1455 245 PHE A C   
1895 O O   . PHE A 245 ? 0.7032 0.4049 0.4854 0.0069  -0.0167 -0.1435 245 PHE A O   
1896 C CB  . PHE A 245 ? 0.6248 0.4249 0.4517 0.0040  0.0168  -0.1175 245 PHE A CB  
1897 C CG  . PHE A 245 ? 0.6020 0.4396 0.4509 0.0039  0.0347  -0.1064 245 PHE A CG  
1898 C CD1 . PHE A 245 ? 0.5959 0.4592 0.4393 0.0110  0.0496  -0.1092 245 PHE A CD1 
1899 C CD2 . PHE A 245 ? 0.5953 0.4407 0.4679 -0.0052 0.0376  -0.0938 245 PHE A CD2 
1900 C CE1 . PHE A 245 ? 0.5665 0.4610 0.4297 0.0082  0.0664  -0.1011 245 PHE A CE1 
1901 C CE2 . PHE A 245 ? 0.5737 0.4531 0.4653 -0.0060 0.0535  -0.0863 245 PHE A CE2 
1902 C CZ  . PHE A 245 ? 0.5534 0.4566 0.4414 0.0003  0.0676  -0.0907 245 PHE A CZ  
1903 N N   . ALA A 246 ? 0.7312 0.4655 0.4876 0.0353  -0.0007 -0.1612 246 ALA A N   
1904 C CA  . ALA A 246 ? 0.7824 0.4853 0.5110 0.0340  -0.0162 -0.1773 246 ALA A CA  
1905 C C   . ALA A 246 ? 0.7763 0.4987 0.5051 0.0184  -0.0226 -0.1720 246 ALA A C   
1906 O O   . ALA A 246 ? 0.7535 0.5061 0.4771 0.0230  -0.0112 -0.1678 246 ALA A O   
1907 C CB  . ALA A 246 ? 0.8129 0.5093 0.5115 0.0577  -0.0104 -0.1984 246 ALA A CB  
1908 N N   . ARG A 247 ? 0.7948 0.5001 0.5292 -0.0002 -0.0408 -0.1723 247 ARG A N   
1909 C CA  . ARG A 247 ? 0.8036 0.5306 0.5423 -0.0134 -0.0514 -0.1685 247 ARG A CA  
1910 C C   . ARG A 247 ? 0.8508 0.5535 0.5596 -0.0157 -0.0709 -0.1891 247 ARG A C   
1911 O O   . ARG A 247 ? 0.8843 0.5484 0.5854 -0.0217 -0.0816 -0.2021 247 ARG A O   
1912 C CB  . ARG A 247 ? 0.8056 0.5465 0.5832 -0.0355 -0.0568 -0.1539 247 ARG A CB  
1913 C CG  . ARG A 247 ? 0.7880 0.5543 0.5945 -0.0348 -0.0384 -0.1346 247 ARG A CG  
1914 C CD  . ARG A 247 ? 0.7939 0.6004 0.6143 -0.0348 -0.0327 -0.1225 247 ARG A CD  
1915 N NE  . ARG A 247 ? 0.7862 0.6157 0.6394 -0.0403 -0.0186 -0.1060 247 ARG A NE  
1916 C CZ  . ARG A 247 ? 0.7859 0.6318 0.6413 -0.0300 0.0005  -0.0985 247 ARG A CZ  
1917 N NH1 . ARG A 247 ? 0.8113 0.6553 0.6400 -0.0149 0.0095  -0.1051 247 ARG A NH1 
1918 N NH2 . ARG A 247 ? 0.7549 0.6208 0.6393 -0.0364 0.0117  -0.0859 247 ARG A NH2 
1919 N N   . PHE A 248 ? 0.8693 0.5915 0.5578 -0.0112 -0.0759 -0.1920 248 PHE A N   
1920 C CA  . PHE A 248 ? 0.9263 0.6313 0.5821 -0.0123 -0.0953 -0.2126 248 PHE A CA  
1921 C C   . PHE A 248 ? 0.9390 0.6669 0.6072 -0.0278 -0.1167 -0.2106 248 PHE A C   
1922 O O   . PHE A 248 ? 1.0056 0.7191 0.6578 -0.0362 -0.1376 -0.2296 248 PHE A O   
1923 C CB  . PHE A 248 ? 0.9458 0.6522 0.5566 0.0085  -0.0858 -0.2218 248 PHE A CB  
1924 C CG  . PHE A 248 ? 0.8510 0.5408 0.4497 0.0258  -0.0667 -0.2304 248 PHE A CG  
1925 C CD1 . PHE A 248 ? 0.8080 0.5194 0.4260 0.0339  -0.0434 -0.2155 248 PHE A CD1 
1926 C CD2 . PHE A 248 ? 0.9032 0.5575 0.4725 0.0349  -0.0728 -0.2556 248 PHE A CD2 
1927 C CE1 . PHE A 248 ? 0.8159 0.5204 0.4273 0.0514  -0.0276 -0.2256 248 PHE A CE1 
1928 C CE2 . PHE A 248 ? 0.9115 0.5548 0.4724 0.0548  -0.0562 -0.2653 248 PHE A CE2 
1929 C CZ  . PHE A 248 ? 0.8701 0.5418 0.4537 0.0633  -0.0341 -0.2503 248 PHE A CZ  
1930 N N   . ARG A 249 ? 0.8799 0.6442 0.5766 -0.0307 -0.1125 -0.1901 249 ARG A N   
1931 C CA  . ARG A 249 ? 0.8916 0.6853 0.6102 -0.0430 -0.1327 -0.1874 249 ARG A CA  
1932 C C   . ARG A 249 ? 0.8531 0.6720 0.6236 -0.0545 -0.1236 -0.1686 249 ARG A C   
1933 O O   . ARG A 249 ? 0.8279 0.6401 0.6111 -0.0520 -0.1027 -0.1574 249 ARG A O   
1934 C CB  . ARG A 249 ? 0.8999 0.7146 0.5892 -0.0272 -0.1393 -0.1828 249 ARG A CB  
1935 N N   . SER A 250 ? 0.8354 0.6875 0.6367 -0.0663 -0.1396 -0.1667 250 SER A N   
1936 C CA  . SER A 250 ? 0.7875 0.6687 0.6390 -0.0773 -0.1311 -0.1513 250 SER A CA  
1937 C C   . SER A 250 ? 0.7547 0.6610 0.6089 -0.0586 -0.1189 -0.1325 250 SER A C   
1938 O O   . SER A 250 ? 0.7697 0.6924 0.6083 -0.0455 -0.1313 -0.1312 250 SER A O   
1939 C CB  . SER A 250 ? 0.7895 0.7012 0.6777 -0.0985 -0.1524 -0.1602 250 SER A CB  
1940 O OG  . SER A 250 ? 0.7522 0.6867 0.6887 -0.1138 -0.1408 -0.1487 250 SER A OG  
1941 N N   . PHE A 251 ? 0.6954 0.6009 0.5659 -0.0571 -0.0951 -0.1181 251 PHE A N   
1942 C CA  . PHE A 251 ? 0.6719 0.5976 0.5504 -0.0437 -0.0810 -0.1009 251 PHE A CA  
1943 C C   . PHE A 251 ? 0.6239 0.5672 0.5476 -0.0558 -0.0668 -0.0910 251 PHE A C   
1944 O O   . PHE A 251 ? 0.6244 0.5552 0.5479 -0.0553 -0.0466 -0.0847 251 PHE A O   
1945 C CB  . PHE A 251 ? 0.6916 0.5952 0.5311 -0.0272 -0.0620 -0.0958 251 PHE A CB  
1946 C CG  . PHE A 251 ? 0.6943 0.6097 0.5295 -0.0138 -0.0505 -0.0800 251 PHE A CG  
1947 C CD1 . PHE A 251 ? 0.6856 0.6270 0.5452 -0.0109 -0.0611 -0.0722 251 PHE A CD1 
1948 C CD2 . PHE A 251 ? 0.6957 0.5955 0.5027 -0.0042 -0.0285 -0.0739 251 PHE A CD2 
1949 C CE1 . PHE A 251 ? 0.6750 0.6181 0.5265 0.0032  -0.0508 -0.0574 251 PHE A CE1 
1950 C CE2 . PHE A 251 ? 0.6865 0.5889 0.4859 0.0053  -0.0165 -0.0592 251 PHE A CE2 
1951 C CZ  . PHE A 251 ? 0.6797 0.5995 0.4992 0.0099  -0.0280 -0.0503 251 PHE A CZ  
1952 N N   . PRO A 252 ? 0.5924 0.5687 0.5557 -0.0667 -0.0772 -0.0908 252 PRO A N   
1953 C CA  . PRO A 252 ? 0.5188 0.5130 0.5233 -0.0808 -0.0629 -0.0832 252 PRO A CA  
1954 C C   . PRO A 252 ? 0.4720 0.4714 0.4796 -0.0678 -0.0407 -0.0688 252 PRO A C   
1955 O O   . PRO A 252 ? 0.4779 0.4775 0.4675 -0.0493 -0.0389 -0.0631 252 PRO A O   
1956 C CB  . PRO A 252 ? 0.5212 0.5586 0.5665 -0.0912 -0.0790 -0.0881 252 PRO A CB  
1957 C CG  . PRO A 252 ? 0.5764 0.6109 0.6018 -0.0901 -0.1049 -0.1025 252 PRO A CG  
1958 C CD  . PRO A 252 ? 0.6055 0.6088 0.5789 -0.0671 -0.1028 -0.0994 252 PRO A CD  
1959 N N   . PHE A 253 ? 0.4387 0.4393 0.4662 -0.0787 -0.0236 -0.0632 253 PHE A N   
1960 C CA  . PHE A 253 ? 0.4068 0.4128 0.4386 -0.0696 -0.0020 -0.0524 253 PHE A CA  
1961 C C   . PHE A 253 ? 0.3854 0.4207 0.4387 -0.0596 -0.0023 -0.0470 253 PHE A C   
1962 O O   . PHE A 253 ? 0.3810 0.4099 0.4209 -0.0451 0.0095  -0.0400 253 PHE A O   
1963 C CB  . PHE A 253 ? 0.3799 0.3873 0.4304 -0.0841 0.0127  -0.0485 253 PHE A CB  
1964 C CG  . PHE A 253 ? 0.3730 0.3880 0.4284 -0.0771 0.0341  -0.0405 253 PHE A CG  
1965 C CD1 . PHE A 253 ? 0.3928 0.3880 0.4217 -0.0674 0.0458  -0.0398 253 PHE A CD1 
1966 C CD2 . PHE A 253 ? 0.3629 0.4078 0.4510 -0.0807 0.0429  -0.0360 253 PHE A CD2 
1967 C CE1 . PHE A 253 ? 0.3804 0.3849 0.4152 -0.0638 0.0649  -0.0350 253 PHE A CE1 
1968 C CE2 . PHE A 253 ? 0.3721 0.4218 0.4630 -0.0754 0.0623  -0.0311 253 PHE A CE2 
1969 C CZ  . PHE A 253 ? 0.3826 0.4118 0.4469 -0.0681 0.0729  -0.0307 253 PHE A CZ  
1970 N N   . TRP A 254 ? 0.3844 0.4520 0.4714 -0.0670 -0.0156 -0.0512 254 TRP A N   
1971 C CA  . TRP A 254 ? 0.4007 0.4992 0.5120 -0.0538 -0.0175 -0.0476 254 TRP A CA  
1972 C C   . TRP A 254 ? 0.4375 0.5250 0.5185 -0.0309 -0.0322 -0.0458 254 TRP A C   
1973 O O   . TRP A 254 ? 0.4072 0.4956 0.4856 -0.0123 -0.0270 -0.0378 254 TRP A O   
1974 C CB  . TRP A 254 ? 0.3751 0.5190 0.5348 -0.0678 -0.0277 -0.0552 254 TRP A CB  
1975 C CG  . TRP A 254 ? 0.3558 0.5106 0.5424 -0.0906 -0.0103 -0.0544 254 TRP A CG  
1976 C CD1 . TRP A 254 ? 0.3570 0.5193 0.5604 -0.1172 -0.0139 -0.0608 254 TRP A CD1 
1977 C CD2 . TRP A 254 ? 0.3279 0.4843 0.5230 -0.0899 0.0139  -0.0467 254 TRP A CD2 
1978 N NE1 . TRP A 254 ? 0.3365 0.5039 0.5555 -0.1323 0.0069  -0.0554 254 TRP A NE1 
1979 C CE2 . TRP A 254 ? 0.3223 0.4887 0.5371 -0.1152 0.0234  -0.0476 254 TRP A CE2 
1980 C CE3 . TRP A 254 ? 0.3190 0.4673 0.5046 -0.0718 0.0288  -0.0397 254 TRP A CE3 
1981 C CZ2 . TRP A 254 ? 0.2951 0.4668 0.5188 -0.1208 0.0458  -0.0417 254 TRP A CZ2 
1982 C CZ3 . TRP A 254 ? 0.3045 0.4589 0.5025 -0.0788 0.0507  -0.0362 254 TRP A CZ3 
1983 C CH2 . TRP A 254 ? 0.2910 0.4587 0.5072 -0.1020 0.0584  -0.0372 254 TRP A CH2 
1984 N N   . ARG A 255 ? 0.4339 0.5076 0.4883 -0.0316 -0.0507 -0.0532 255 ARG A N   
1985 C CA  . ARG A 255 ? 0.4890 0.5462 0.5033 -0.0099 -0.0631 -0.0501 255 ARG A CA  
1986 C C   . ARG A 255 ? 0.4844 0.5024 0.4570 -0.0005 -0.0418 -0.0402 255 ARG A C   
1987 O O   . ARG A 255 ? 0.4949 0.4988 0.4417 0.0180  -0.0397 -0.0305 255 ARG A O   
1988 C CB  . ARG A 255 ? 0.5373 0.5900 0.5304 -0.0143 -0.0875 -0.0629 255 ARG A CB  
1989 C CG  . ARG A 255 ? 0.6182 0.6487 0.5589 0.0070  -0.0992 -0.0597 255 ARG A CG  
1990 C CD  . ARG A 255 ? 0.6930 0.7421 0.6289 0.0083  -0.1320 -0.0730 255 ARG A CD  
1991 N NE  . ARG A 255 ? 0.7745 0.7924 0.6634 0.0050  -0.1384 -0.0830 255 ARG A NE  
1992 C CZ  . ARG A 255 ? 0.8212 0.8406 0.7166 -0.0137 -0.1517 -0.1009 255 ARG A CZ  
1993 N NH1 . ARG A 255 ? 0.8067 0.8579 0.7536 -0.0336 -0.1595 -0.1097 255 ARG A NH1 
1994 N NH2 . ARG A 255 ? 0.8750 0.8627 0.7240 -0.0133 -0.1561 -0.1110 255 ARG A NH2 
1995 N N   . ARG A 256 ? 0.4584 0.4585 0.4239 -0.0133 -0.0255 -0.0427 256 ARG A N   
1996 C CA  . ARG A 256 ? 0.4579 0.4315 0.3941 -0.0076 -0.0026 -0.0360 256 ARG A CA  
1997 C C   . ARG A 256 ? 0.4542 0.4339 0.4073 -0.0021 0.0149  -0.0253 256 ARG A C   
1998 O O   . ARG A 256 ? 0.4556 0.4132 0.3802 0.0071  0.0286  -0.0176 256 ARG A O   
1999 C CB  A ARG A 256 ? 0.4789 0.4419 0.4142 -0.0203 0.0095  -0.0424 256 ARG A CB  
2000 C CB  B ARG A 256 ? 0.4787 0.4421 0.4145 -0.0205 0.0093  -0.0425 256 ARG A CB  
2001 C CG  A ARG A 256 ? 0.4807 0.4240 0.3872 -0.0153 0.0310  -0.0400 256 ARG A CG  
2002 C CG  B ARG A 256 ? 0.4720 0.4200 0.3885 -0.0173 0.0339  -0.0388 256 ARG A CG  
2003 C CD  A ARG A 256 ? 0.4286 0.3683 0.3402 -0.0237 0.0407  -0.0471 256 ARG A CD  
2004 C CD  B ARG A 256 ? 0.4214 0.3651 0.3415 -0.0259 0.0416  -0.0463 256 ARG A CD  
2005 N NE  A ARG A 256 ? 0.4579 0.3842 0.3552 -0.0258 0.0248  -0.0582 256 ARG A NE  
2006 N NE  B ARG A 256 ? 0.4557 0.3814 0.3494 -0.0239 0.0294  -0.0571 256 ARG A NE  
2007 C CZ  A ARG A 256 ? 0.5112 0.4189 0.3719 -0.0178 0.0238  -0.0662 256 ARG A CZ  
2008 C CZ  B ARG A 256 ? 0.4587 0.3803 0.3606 -0.0319 0.0122  -0.0646 256 ARG A CZ  
2009 N NH1 A ARG A 256 ? 0.4946 0.3972 0.3292 -0.0093 0.0390  -0.0632 256 ARG A NH1 
2010 N NH1 B ARG A 256 ? 0.4410 0.3787 0.3781 -0.0443 0.0063  -0.0616 256 ARG A NH1 
2011 N NH2 A ARG A 256 ? 0.5023 0.3951 0.3512 -0.0197 0.0089  -0.0783 256 ARG A NH2 
2012 N NH2 B ARG A 256 ? 0.4988 0.3994 0.3729 -0.0288 0.0022  -0.0763 256 ARG A NH2 
2013 N N   . VAL A 257 ? 0.4276 0.4358 0.4257 -0.0088 0.0159  -0.0256 257 VAL A N   
2014 C CA  . VAL A 257 ? 0.3979 0.4125 0.4138 -0.0023 0.0313  -0.0183 257 VAL A CA  
2015 C C   . VAL A 257 ? 0.4290 0.4388 0.4329 0.0193  0.0198  -0.0113 257 VAL A C   
2016 O O   . VAL A 257 ? 0.4438 0.4306 0.4296 0.0302  0.0336  -0.0025 257 VAL A O   
2017 C CB  . VAL A 257 ? 0.3637 0.4131 0.4294 -0.0147 0.0353  -0.0222 257 VAL A CB  
2018 C CG1 . VAL A 257 ? 0.3600 0.4198 0.4461 -0.0041 0.0467  -0.0177 257 VAL A CG1 
2019 C CG2 . VAL A 257 ? 0.3401 0.3857 0.4089 -0.0325 0.0502  -0.0250 257 VAL A CG2 
2020 N N   . HIS A 258 ? 0.4444 0.4745 0.4570 0.0259  -0.0063 -0.0156 258 HIS A N   
2021 C CA  . HIS A 258 ? 0.4783 0.5079 0.4806 0.0505  -0.0218 -0.0091 258 HIS A CA  
2022 C C   . HIS A 258 ? 0.5226 0.5041 0.4630 0.0642  -0.0176 0.0020  258 HIS A C   
2023 O O   . HIS A 258 ? 0.5495 0.5080 0.4721 0.0819  -0.0116 0.0136  258 HIS A O   
2024 C CB  . HIS A 258 ? 0.5001 0.5654 0.5214 0.0534  -0.0533 -0.0188 258 HIS A CB  
2025 C CG  . HIS A 258 ? 0.5334 0.5963 0.5335 0.0820  -0.0751 -0.0126 258 HIS A CG  
2026 N ND1 . HIS A 258 ? 0.5961 0.6257 0.5380 0.0935  -0.0866 -0.0072 258 HIS A ND1 
2027 C CD2 . HIS A 258 ? 0.5434 0.6335 0.5705 0.1036  -0.0885 -0.0112 258 HIS A CD2 
2028 C CE1 . HIS A 258 ? 0.6188 0.6520 0.5493 0.1210  -0.1072 -0.0008 258 HIS A CE1 
2029 N NE2 . HIS A 258 ? 0.6114 0.6817 0.5947 0.1290  -0.1094 -0.0035 258 HIS A NE2 
2030 N N   . ASP A 259 ? 0.5360 0.4990 0.4407 0.0558  -0.0192 -0.0016 259 ASP A N   
2031 C CA  . ASP A 259 ? 0.5994 0.5196 0.4422 0.0662  -0.0136 0.0080  259 ASP A CA  
2032 C C   . ASP A 259 ? 0.5995 0.4897 0.4279 0.0622  0.0186  0.0174  259 ASP A C   
2033 O O   . ASP A 259 ? 0.6259 0.4793 0.4115 0.0740  0.0261  0.0303  259 ASP A O   
2034 C CB  . ASP A 259 ? 0.6454 0.5574 0.4576 0.0566  -0.0189 -0.0015 259 ASP A CB  
2035 C CG  . ASP A 259 ? 0.7083 0.6451 0.5290 0.0587  -0.0514 -0.0127 259 ASP A CG  
2036 O OD1 . ASP A 259 ? 0.7282 0.6904 0.5740 0.0701  -0.0711 -0.0117 259 ASP A OD1 
2037 O OD2 . ASP A 259 ? 0.7323 0.6648 0.5359 0.0490  -0.0574 -0.0244 259 ASP A OD2 
2038 N N   . SER A 260 ? 0.5731 0.4771 0.4346 0.0448  0.0377  0.0109  260 SER A N   
2039 C CA  . SER A 260 ? 0.5752 0.4562 0.4251 0.0372  0.0679  0.0157  260 SER A CA  
2040 C C   . SER A 260 ? 0.5839 0.4547 0.4470 0.0466  0.0771  0.0243  260 SER A C   
2041 O O   . SER A 260 ? 0.5975 0.4346 0.4345 0.0448  0.0987  0.0315  260 SER A O   
2042 C CB  . SER A 260 ? 0.5459 0.4477 0.4245 0.0174  0.0826  0.0046  260 SER A CB  
2043 O OG  . SER A 260 ? 0.5619 0.4657 0.4243 0.0114  0.0762  -0.0039 260 SER A OG  
2044 N N   . PHE A 261 ? 0.5235 0.4225 0.4266 0.0559  0.0623  0.0223  261 PHE A N   
2045 C CA  . PHE A 261 ? 0.5260 0.4197 0.4485 0.0653  0.0725  0.0266  261 PHE A CA  
2046 C C   . PHE A 261 ? 0.6025 0.4959 0.5259 0.0932  0.0509  0.0334  261 PHE A C   
2047 O O   . PHE A 261 ? 0.6086 0.4754 0.5253 0.1077  0.0598  0.0409  261 PHE A O   
2048 C CB  . PHE A 261 ? 0.4777 0.4113 0.4553 0.0511  0.0814  0.0153  261 PHE A CB  
2049 C CG  . PHE A 261 ? 0.4437 0.3774 0.4215 0.0278  0.1027  0.0092  261 PHE A CG  
2050 C CD1 . PHE A 261 ? 0.4235 0.3855 0.4201 0.0128  0.0971  0.0005  261 PHE A CD1 
2051 C CD2 . PHE A 261 ? 0.4659 0.3702 0.4239 0.0213  0.1277  0.0114  261 PHE A CD2 
2052 C CE1 . PHE A 261 ? 0.4168 0.3801 0.4127 -0.0040 0.1141  -0.0050 261 PHE A CE1 
2053 C CE2 . PHE A 261 ? 0.4589 0.3710 0.4203 0.0015  0.1451  0.0037  261 PHE A CE2 
2054 C CZ  . PHE A 261 ? 0.4247 0.3671 0.4049 -0.0089 0.1373  -0.0041 261 PHE A CZ  
2055 N N   . ILE A 262 ? 0.6494 0.5713 0.5809 0.1021  0.0221  0.0299  262 ILE A N   
2056 C CA  . ILE A 262 ? 0.7471 0.6773 0.6830 0.1315  -0.0018 0.0345  262 ILE A CA  
2057 C C   . ILE A 262 ? 0.9142 0.7959 0.7829 0.1502  -0.0119 0.0494  262 ILE A C   
2058 O O   . ILE A 262 ? 0.9703 0.8100 0.8099 0.1706  -0.0070 0.0631  262 ILE A O   
2059 C CB  . ILE A 262 ? 0.7050 0.6976 0.6880 0.1308  -0.0288 0.0209  262 ILE A CB  
2060 C CG1 . ILE A 262 ? 0.6417 0.6766 0.6833 0.1077  -0.0149 0.0080  262 ILE A CG1 
2061 C CG2 . ILE A 262 ? 0.7233 0.7354 0.7203 0.1634  -0.0538 0.0229  262 ILE A CG2 
2062 C CD1 . ILE A 262 ? 0.6313 0.6711 0.7033 0.1166  0.0020  0.0082  262 ILE A CD1 
2063 N N   . GLU A 263 ? 1.0021 0.8851 0.8420 0.1432  -0.0253 0.0470  263 GLU A N   
2064 C CA  . GLU A 263 ? 1.1448 0.9835 0.9147 0.1581  -0.0341 0.0604  263 GLU A CA  
2065 C C   . GLU A 263 ? 1.1791 1.0300 0.9294 0.1429  -0.0442 0.0506  263 GLU A C   
2066 O O   . GLU A 263 ? 1.1242 1.0177 0.9173 0.1260  -0.0510 0.0342  263 GLU A O   
2067 C CB  . GLU A 263 ? 1.2222 1.0616 0.9813 0.1937  -0.0640 0.0690  263 GLU A CB  
2068 C CG  . GLU A 263 ? 1.2183 1.1234 1.0234 0.1995  -0.0983 0.0531  263 GLU A CG  
2069 C CD  . GLU A 263 ? 1.2696 1.1934 1.0919 0.2355  -0.1240 0.0571  263 GLU A CD  
2070 O OE1 . GLU A 263 ? 1.3438 1.2178 1.1137 0.2632  -0.1278 0.0757  263 GLU A OE1 
2071 O OE2 . GLU A 263 ? 1.2402 1.2281 1.1281 0.2365  -0.1397 0.0415  263 GLU A OE2 
2072 N N   . ASP A 264 ? 1.2834 1.0928 0.9653 0.1490  -0.0441 0.0608  264 ASP A N   
2073 C CA  . ASP A 264 ? 1.3287 1.1445 0.9827 0.1390  -0.0547 0.0508  264 ASP A CA  
2074 C C   . ASP A 264 ? 1.4184 1.1919 0.9932 0.1567  -0.0638 0.0649  264 ASP A C   
2075 O O   . ASP A 264 ? 1.4585 1.2441 1.0178 0.1768  -0.0965 0.0651  264 ASP A O   
2076 C CB  . ASP A 264 ? 1.3155 1.1278 0.9737 0.1109  -0.0261 0.0415  264 ASP A CB  
2077 C CG  . ASP A 264 ? 1.3418 1.1693 0.9880 0.1007  -0.0389 0.0255  264 ASP A CG  
2078 O OD1 . ASP A 264 ? 1.3686 1.2164 1.0141 0.1106  -0.0704 0.0188  264 ASP A OD1 
2079 O OD2 . ASP A 264 ? 1.3339 1.1542 0.9722 0.0835  -0.0179 0.0180  264 ASP A OD2 
# 
