data_8QGG
# 
_entry.id   8QGG 
# 
_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   8QGG         pdb_00008qgg 10.2210/pdb8qgg/pdb 
WWPDB D_1292133166 ?            ?                   
# 
_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                        8QGG 
_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 GLYCEROL 92.094    1  ?        ? ? ? 
4 non-polymer syn 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-(3-oxidanylpropyl)amino]methyl]oxolane-3,4-diol
;
627.609   1  ?        ? ? ? 
5 water       nat water 18.015    98 ?        ? ? ? 
# 
_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 GLYCEROL GOL 
4 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-(3-oxidanylpropyl)amino]methyl]oxolane-3,4-diol
;
UJT 
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   TYR n 
1 4   MET n 
1 5   ILE n 
1 6   THR n 
1 7   SER n 
1 8   LYS n 
1 9   GLY n 
1 10  ASP n 
1 11  GLU n 
1 12  LYS n 
1 13  SER n 
1 14  ASP n 
1 15  LEU n 
1 16  LEU n 
1 17  ARG n 
1 18  LEU n 
1 19  ASN n 
1 20  MET n 
1 21  ILE n 
1 22  ALA n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  GLU n 
1 27  TYR n 
1 28  ASP n 
1 29  MET n 
1 30  GLU n 
1 31  TYR n 
1 32  ASP n 
1 33  ASP n 
1 34  VAL n 
1 35  GLU n 
1 36  PRO n 
1 37  GLU n 
1 38  ILE n 
1 39  VAL n 
1 40  ILE n 
1 41  SER n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  ASP n 
1 46  GLY n 
1 47  THR n 
1 48  PHE n 
1 49  LEU n 
1 50  SER n 
1 51  ALA n 
1 52  PHE n 
1 53  HIS n 
1 54  GLN n 
1 55  TYR n 
1 56  GLU n 
1 57  GLU n 
1 58  ARG n 
1 59  LEU n 
1 60  ASP n 
1 61  GLU n 
1 62  ILE n 
1 63  ALA n 
1 64  PHE n 
1 65  ILE n 
1 66  GLY n 
1 67  ILE n 
1 68  HIS n 
1 69  THR n 
1 70  GLY n 
1 71  HIS n 
1 72  LEU n 
1 73  GLY n 
1 74  PHE n 
1 75  TYR n 
1 76  ALA n 
1 77  ASP n 
1 78  TRP n 
1 79  ARG n 
1 80  PRO n 
1 81  ALA n 
1 82  GLU n 
1 83  ALA n 
1 84  ASP n 
1 85  LYS n 
1 86  LEU n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  LYS n 
1 93  GLY n 
1 94  GLU n 
1 95  TYR n 
1 96  GLN n 
1 97  LYS n 
1 98  VAL n 
1 99  SER n 
1 100 TYR n 
1 101 PRO n 
1 102 LEU n 
1 103 LEU n 
1 104 LYS n 
1 105 THR n 
1 106 THR n 
1 107 VAL n 
1 108 LYS n 
1 109 TYR n 
1 110 GLY n 
1 111 ILE n 
1 112 GLY n 
1 113 LYS n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 THR n 
1 118 TYR n 
1 119 LEU n 
1 120 ALA n 
1 121 LEU n 
1 122 ASN n 
1 123 GLU n 
1 124 SER n 
1 125 THR n 
1 126 VAL n 
1 127 LYS n 
1 128 SER n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 PRO n 
1 133 PHE n 
1 134 VAL n 
1 135 VAL n 
1 136 ASP n 
1 137 VAL n 
1 138 VAL n 
1 139 ILE n 
1 140 ASN n 
1 141 ASP n 
1 142 ILE n 
1 143 HIS n 
1 144 PHE n 
1 145 GLU n 
1 146 ARG n 
1 147 PHE n 
1 148 ARG n 
1 149 GLY n 
1 150 ASP n 
1 151 GLY n 
1 152 LEU n 
1 153 CYS n 
1 154 MET n 
1 155 SER n 
1 156 THR n 
1 157 PRO n 
1 158 SER n 
1 159 GLY n 
1 160 THR n 
1 161 THR n 
1 162 ALA n 
1 163 TYR n 
1 164 ASN n 
1 165 LYS n 
1 166 SER n 
1 167 LEU n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 LEU n 
1 172 MET n 
1 173 HIS n 
1 174 PRO n 
1 175 SER n 
1 176 ILE n 
1 177 GLU n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 LEU n 
1 182 THR n 
1 183 GLU n 
1 184 MET n 
1 185 ALA n 
1 186 SER n 
1 187 ILE n 
1 188 ASN n 
1 189 ASN n 
1 190 ARG n 
1 191 VAL n 
1 192 TYR n 
1 193 ARG n 
1 194 THR n 
1 195 ILE n 
1 196 GLY n 
1 197 SER n 
1 198 PRO n 
1 199 LEU n 
1 200 VAL n 
1 201 PHE n 
1 202 PRO n 
1 203 LYS n 
1 204 HIS n 
1 205 HIS n 
1 206 VAL n 
1 207 VAL n 
1 208 SER n 
1 209 LEU n 
1 210 GLN n 
1 211 PRO n 
1 212 VAL n 
1 213 ASN n 
1 214 ASP n 
1 215 LYS n 
1 216 ASP n 
1 217 PHE n 
1 218 GLN n 
1 219 ILE n 
1 220 SER n 
1 221 VAL n 
1 222 ASP n 
1 223 HIS n 
1 224 LEU n 
1 225 SER n 
1 226 ILE n 
1 227 LEU n 
1 228 HIS n 
1 229 ARG n 
1 230 ASP n 
1 231 VAL n 
1 232 GLN n 
1 233 GLU n 
1 234 ILE n 
1 235 ARG n 
1 236 TYR n 
1 237 GLU n 
1 238 VAL n 
1 239 SER n 
1 240 ALA n 
1 241 LYS n 
1 242 LYS n 
1 243 ILE n 
1 244 HIS n 
1 245 PHE n 
1 246 ALA n 
1 247 ARG n 
1 248 PHE n 
1 249 ARG n 
1 250 SER n 
1 251 PHE n 
1 252 PRO n 
1 253 PHE n 
1 254 TRP n 
1 255 ARG n 
1 256 ARG n 
1 257 VAL n 
1 258 HIS n 
1 259 ASP n 
1 260 SER n 
1 261 PHE n 
1 262 ILE n 
1 263 GLU n 
1 264 ASP n 
1 265 LEU n 
1 266 GLU n 
1 267 HIS n 
1 268 HIS n 
1 269 HIS n 
1 270 HIS n 
1 271 HIS n 
1 272 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   272 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nadK1, lmo0968' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Listeria monocytogenes EGD-e' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     169963 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CIT non-polymer         . 'CITRIC ACID' ?                               'C6 H8 O7'       192.124 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'    181.189 
UJT non-polymer         . 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-(3-oxidanylpropyl)amino]methyl]oxolane-3,4-diol
;
?                               'C26 H33 N11 O8' 627.609 
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        UJT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UJT 
_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  301 265 CIT CIT A . 
C 3 GOL 1  302 266 GOL GOL A . 
D 4 UJT 1  303 1   UJT XXX A . 
E 5 HOH 1  401 9   HOH HOH A . 
E 5 HOH 2  402 56  HOH HOH A . 
E 5 HOH 3  403 68  HOH HOH A . 
E 5 HOH 4  404 32  HOH HOH A . 
E 5 HOH 5  405 6   HOH HOH A . 
E 5 HOH 6  406 60  HOH HOH A . 
E 5 HOH 7  407 112 HOH HOH A . 
E 5 HOH 8  408 14  HOH HOH A . 
E 5 HOH 9  409 79  HOH HOH A . 
E 5 HOH 10 410 97  HOH HOH A . 
E 5 HOH 11 411 95  HOH HOH A . 
E 5 HOH 12 412 81  HOH HOH A . 
E 5 HOH 13 413 61  HOH HOH A . 
E 5 HOH 14 414 26  HOH HOH A . 
E 5 HOH 15 415 54  HOH HOH A . 
E 5 HOH 16 416 84  HOH HOH A . 
E 5 HOH 17 417 78  HOH HOH A . 
E 5 HOH 18 418 52  HOH HOH A . 
E 5 HOH 19 419 4   HOH HOH A . 
E 5 HOH 20 420 93  HOH HOH A . 
E 5 HOH 21 421 111 HOH HOH A . 
E 5 HOH 22 422 31  HOH HOH A . 
E 5 HOH 23 423 21  HOH HOH A . 
E 5 HOH 24 424 72  HOH HOH A . 
E 5 HOH 25 425 22  HOH HOH A . 
E 5 HOH 26 426 12  HOH HOH A . 
E 5 HOH 27 427 67  HOH HOH A . 
E 5 HOH 28 428 55  HOH HOH A . 
E 5 HOH 29 430 23  HOH HOH A . 
E 5 HOH 30 431 3   HOH HOH A . 
E 5 HOH 31 432 53  HOH HOH A . 
E 5 HOH 32 433 13  HOH HOH A . 
E 5 HOH 33 434 15  HOH HOH A . 
E 5 HOH 34 435 43  HOH HOH A . 
E 5 HOH 35 436 20  HOH HOH A . 
E 5 HOH 36 437 16  HOH HOH A . 
E 5 HOH 37 438 1   HOH HOH A . 
E 5 HOH 38 439 90  HOH HOH A . 
E 5 HOH 39 440 28  HOH HOH A . 
E 5 HOH 40 441 29  HOH HOH A . 
E 5 HOH 41 442 108 HOH HOH A . 
E 5 HOH 42 443 66  HOH HOH A . 
E 5 HOH 43 444 51  HOH HOH A . 
E 5 HOH 44 445 27  HOH HOH A . 
E 5 HOH 45 446 24  HOH HOH A . 
E 5 HOH 46 447 7   HOH HOH A . 
E 5 HOH 47 448 25  HOH HOH A . 
E 5 HOH 48 449 109 HOH HOH A . 
E 5 HOH 49 450 101 HOH HOH A . 
E 5 HOH 50 451 105 HOH HOH A . 
E 5 HOH 51 452 8   HOH HOH A . 
E 5 HOH 52 453 100 HOH HOH A . 
E 5 HOH 53 454 71  HOH HOH A . 
E 5 HOH 54 455 2   HOH HOH A . 
E 5 HOH 55 456 19  HOH HOH A . 
E 5 HOH 56 457 69  HOH HOH A . 
E 5 HOH 57 458 5   HOH HOH A . 
E 5 HOH 58 459 42  HOH HOH A . 
E 5 HOH 59 460 38  HOH HOH A . 
E 5 HOH 60 461 45  HOH HOH A . 
E 5 HOH 61 462 82  HOH HOH A . 
E 5 HOH 62 463 49  HOH HOH A . 
E 5 HOH 63 464 46  HOH HOH A . 
E 5 HOH 64 465 59  HOH HOH A . 
E 5 HOH 65 466 11  HOH HOH A . 
E 5 HOH 66 467 36  HOH HOH A . 
E 5 HOH 67 468 47  HOH HOH A . 
E 5 HOH 68 469 44  HOH HOH A . 
E 5 HOH 69 470 18  HOH HOH A . 
E 5 HOH 70 471 41  HOH HOH A . 
E 5 HOH 71 472 58  HOH HOH A . 
E 5 HOH 72 473 10  HOH HOH A . 
E 5 HOH 73 474 37  HOH HOH A . 
E 5 HOH 74 475 96  HOH HOH A . 
E 5 HOH 75 476 35  HOH HOH A . 
E 5 HOH 76 477 92  HOH HOH A . 
E 5 HOH 77 478 48  HOH HOH A . 
E 5 HOH 78 479 106 HOH HOH A . 
E 5 HOH 79 480 50  HOH HOH A . 
E 5 HOH 80 481 94  HOH HOH A . 
E 5 HOH 81 482 103 HOH HOH A . 
E 5 HOH 82 483 40  HOH HOH A . 
E 5 HOH 83 484 86  HOH HOH A . 
E 5 HOH 84 485 83  HOH HOH A . 
E 5 HOH 85 486 98  HOH HOH A . 
E 5 HOH 86 487 76  HOH HOH A . 
E 5 HOH 87 488 73  HOH HOH A . 
E 5 HOH 88 489 62  HOH HOH A . 
E 5 HOH 89 490 75  HOH HOH A . 
E 5 HOH 90 491 89  HOH HOH A . 
E 5 HOH 91 492 102 HOH HOH A . 
E 5 HOH 92 493 107 HOH HOH A . 
E 5 HOH 93 494 57  HOH HOH A . 
E 5 HOH 94 495 87  HOH HOH A . 
E 5 HOH 95 496 34  HOH HOH A . 
E 5 HOH 96 497 33  HOH HOH A . 
E 5 HOH 97 498 77  HOH HOH A . 
E 5 HOH 98 499 91  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A LYS 108 ? CG  ? A LYS 108 CG  
6  1 Y 1 A LYS 108 ? CD  ? A LYS 108 CD  
7  1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
8  1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
9  1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
10 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
11 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
12 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.1_4122 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QGG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.898 
_cell.length_a_esd                 ? 
_cell.length_b                     74.279 
_cell.length_b_esd                 ? 
_cell.length_c                     118.386 
_cell.length_c_esd                 ? 
_cell.volume                       553099.448 
_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                         8QGG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QGG 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.77 
_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' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-03-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.96546 
_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 MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96546 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          25.62 
_reflns.entry_id                                       8QGG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.282 
_reflns.d_resolution_low                               55.55 
_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                                     69703 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.28 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.3 
_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                                0.035 
_reflns.pdbx_Rpim_I_all                                0.015 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.032 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.592 
_reflns_shell.d_res_low                                     1.619 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2016 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.440 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.085 
_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                               39.69 
_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                                 8QGG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.59 
_refine.ls_d_res_low                             55.55 
_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                     69703 
_refine.ls_number_reflns_R_free                  3439 
_refine.ls_number_reflns_R_work                  66264 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.03 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1800 
_refine.ls_R_factor_R_free                       0.2165 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1782 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.9295 
_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                            0.1871 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        55.55 
_refine_hist.number_atoms_solvent             99 
_refine_hist.number_atoms_total               2241 
_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        2078 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_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' ? 0.0054  ? 2228 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8445  ? 3020 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0558  ? 325  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0057  ? 413  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.3403 ? 847  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.59 1.61  . . 170 2671 99.02 . . . . 0.2706 . . . . . . . . . . . 0.2904 
'X-RAY DIFFRACTION' 1.61 1.64  . . 167 2646 98.39 . . . . 0.2479 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 1.64 1.66  . . 110 2721 98.09 . . . . 0.2494 . . . . . . . . . . . 0.2782 
'X-RAY DIFFRACTION' 1.66 1.69  . . 128 2649 97.99 . . . . 0.2255 . . . . . . . . . . . 0.2836 
'X-RAY DIFFRACTION' 1.69 1.71  . . 147 2674 97.99 . . . . 0.2213 . . . . . . . . . . . 0.2830 
'X-RAY DIFFRACTION' 1.71 1.74  . . 169 2658 97.48 . . . . 0.2015 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 1.74 1.78  . . 179 2655 97.96 . . . . 0.1946 . . . . . . . . . . . 0.2667 
'X-RAY DIFFRACTION' 1.78 1.81  . . 118 2693 97.74 . . . . 0.1975 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 1.81 1.85  . . 118 2663 97.96 . . . . 0.1699 . . . . . . . . . . . 0.2236 
'X-RAY DIFFRACTION' 1.85 1.89  . . 138 2654 97.49 . . . . 0.1744 . . . . . . . . . . . 0.2229 
'X-RAY DIFFRACTION' 1.89 1.93  . . 153 2643 97.29 . . . . 0.1911 . . . . . . . . . . . 0.2727 
'X-RAY DIFFRACTION' 1.93 1.98  . . 124 2670 97.45 . . . . 0.1566 . . . . . . . . . . . 0.1689 
'X-RAY DIFFRACTION' 1.98 2.03  . . 107 2728 97.42 . . . . 0.1513 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 2.03 2.09  . . 145 2630 97.20 . . . . 0.1544 . . . . . . . . . . . 0.2263 
'X-RAY DIFFRACTION' 2.09 2.16  . . 140 2666 97.33 . . . . 0.1619 . . . . . . . . . . . 0.2195 
'X-RAY DIFFRACTION' 2.16 2.24  . . 145 2649 97.76 . . . . 0.1635 . . . . . . . . . . . 0.2412 
'X-RAY DIFFRACTION' 2.24 2.33  . . 117 2721 97.06 . . . . 0.1656 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 2.33 2.43  . . 142 2628 97.74 . . . . 0.1671 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 2.43 2.56  . . 154 2664 97.27 . . . . 0.1633 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 2.56 2.72  . . 128 2594 95.31 . . . . 0.1791 . . . . . . . . . . . 0.2625 
'X-RAY DIFFRACTION' 2.72 2.93  . . 125 2589 94.80 . . . . 0.1938 . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 2.93 3.23  . . 115 2611 94.75 . . . . 0.1966 . . . . . . . . . . . 0.2454 
'X-RAY DIFFRACTION' 3.23 3.69  . . 132 2525 92.45 . . . . 0.1679 . . . . . . . . . . . 0.1980 
'X-RAY DIFFRACTION' 3.69 4.65  . . 121 2601 94.48 . . . . 0.1559 . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 4.65 55.55 . . 147 2661 97.36 . . . . 0.1952 . . . . . . . . . . . 0.1793 
# 
_struct.entry_id                     8QGG 
_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        8QGG 
_struct_keywords.text            'tetrameric NAD-kinase, Transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NADK1_LISMO 
_struct_ref.pdbx_db_accession          Q8Y8D7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIED
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QGG 
_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 8QGG LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGG GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGG HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGG HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGG HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGG HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGG HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGG HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12340 ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  39880 ? 
# 
_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,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 62.8980000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 62.8980000000 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  ? ILE A 62  ? GLU A 56  ILE A 62  5 ? 7  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 8 ? 
AA3 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 2 GLN A 96  ? TYR A 109 ? GLN A 96  TYR A 109 
AA2 3 VAL A 231 ? ARG A 247 ? VAL A 231 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA2 7 ALA A 178 ? SER A 186 ? ALA A 178 SER A 186 
AA2 8 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA3 2 GLN A 96  ? TYR A 109 ? GLN A 96  TYR A 109 
AA3 3 VAL A 231 ? ARG A 247 ? VAL A 231 ARG A 247 
AA3 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA3 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA3 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA3 7 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 8 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 9 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA2 3 4 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA2 6 7 N CYS A 153 ? N CYS A 153 O THR A 182 ? O THR A 182 
AA2 7 8 N LEU A 181 ? N LEU A 181 O LEU A 199 ? O LEU A 199 
AA3 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA3 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA3 3 4 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA3 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA3 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 6 7 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 7 8 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 8 9 N PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QGG 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 94  ? ? 57.10   12.45   
2 1 ASN A 122 ? ? -100.38 -68.23  
3 1 ALA A 162 ? ? -106.75 -129.06 
4 1 ALA A 185 ? ? 43.59   71.46   
5 1 HIS A 204 ? ? 79.29   -10.61  
6 1 ASN A 213 ? ? -125.51 -82.41  
7 1 ASP A 222 ? ? 56.52   -130.30 
8 1 GLU A 233 ? ? -170.45 142.88  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
GOL C1   C N N 158 
GOL O1   O N N 159 
GOL C2   C N N 160 
GOL O2   O N N 161 
GOL C3   C N N 162 
GOL O3   O N N 163 
GOL H11  H N N 164 
GOL H12  H N N 165 
GOL HO1  H N N 166 
GOL H2   H N N 167 
GOL HO2  H N N 168 
GOL H31  H N N 169 
GOL H32  H N N 170 
GOL HO3  H N N 171 
HIS N    N N N 172 
HIS CA   C N S 173 
HIS C    C N N 174 
HIS O    O N N 175 
HIS CB   C N N 176 
HIS CG   C Y N 177 
HIS ND1  N Y N 178 
HIS CD2  C Y N 179 
HIS CE1  C Y N 180 
HIS NE2  N Y N 181 
HIS OXT  O N N 182 
HIS H    H N N 183 
HIS H2   H N N 184 
HIS HA   H N N 185 
HIS HB2  H N N 186 
HIS HB3  H N N 187 
HIS HD1  H N N 188 
HIS HD2  H N N 189 
HIS HE1  H N N 190 
HIS HE2  H N N 191 
HIS HXT  H N N 192 
HOH O    O N N 193 
HOH H1   H N N 194 
HOH H2   H N N 195 
ILE N    N N N 196 
ILE CA   C N S 197 
ILE C    C N N 198 
ILE O    O N N 199 
ILE CB   C N S 200 
ILE CG1  C N N 201 
ILE CG2  C N N 202 
ILE CD1  C N N 203 
ILE OXT  O N N 204 
ILE H    H N N 205 
ILE H2   H N N 206 
ILE HA   H N N 207 
ILE HB   H N N 208 
ILE HG12 H N N 209 
ILE HG13 H N N 210 
ILE HG21 H N N 211 
ILE HG22 H N N 212 
ILE HG23 H N N 213 
ILE HD11 H N N 214 
ILE HD12 H N N 215 
ILE HD13 H N N 216 
ILE HXT  H N N 217 
LEU N    N N N 218 
LEU CA   C N S 219 
LEU C    C N N 220 
LEU O    O N N 221 
LEU CB   C N N 222 
LEU CG   C N N 223 
LEU CD1  C N N 224 
LEU CD2  C N N 225 
LEU OXT  O N N 226 
LEU H    H N N 227 
LEU H2   H N N 228 
LEU HA   H N N 229 
LEU HB2  H N N 230 
LEU HB3  H N N 231 
LEU HG   H N N 232 
LEU HD11 H N N 233 
LEU HD12 H N N 234 
LEU HD13 H N N 235 
LEU HD21 H N N 236 
LEU HD22 H N N 237 
LEU HD23 H N N 238 
LEU HXT  H N N 239 
LYS N    N N N 240 
LYS CA   C N S 241 
LYS C    C N N 242 
LYS O    O N N 243 
LYS CB   C N N 244 
LYS CG   C N N 245 
LYS CD   C N N 246 
LYS CE   C N N 247 
LYS NZ   N N N 248 
LYS OXT  O N N 249 
LYS H    H N N 250 
LYS H2   H N N 251 
LYS HA   H N N 252 
LYS HB2  H N N 253 
LYS HB3  H N N 254 
LYS HG2  H N N 255 
LYS HG3  H N N 256 
LYS HD2  H N N 257 
LYS HD3  H N N 258 
LYS HE2  H N N 259 
LYS HE3  H N N 260 
LYS HZ1  H N N 261 
LYS HZ2  H N N 262 
LYS HZ3  H N N 263 
LYS HXT  H N N 264 
MET N    N N N 265 
MET CA   C N S 266 
MET C    C N N 267 
MET O    O N N 268 
MET CB   C N N 269 
MET CG   C N N 270 
MET SD   S N N 271 
MET CE   C N N 272 
MET OXT  O N N 273 
MET H    H N N 274 
MET H2   H N N 275 
MET HA   H N N 276 
MET HB2  H N N 277 
MET HB3  H N N 278 
MET HG2  H N N 279 
MET HG3  H N N 280 
MET HE1  H N N 281 
MET HE2  H N N 282 
MET HE3  H N N 283 
MET HXT  H N N 284 
PHE N    N N N 285 
PHE CA   C N S 286 
PHE C    C N N 287 
PHE O    O N N 288 
PHE CB   C N N 289 
PHE CG   C Y N 290 
PHE CD1  C Y N 291 
PHE CD2  C Y N 292 
PHE CE1  C Y N 293 
PHE CE2  C Y N 294 
PHE CZ   C Y N 295 
PHE OXT  O N N 296 
PHE H    H N N 297 
PHE H2   H N N 298 
PHE HA   H N N 299 
PHE HB2  H N N 300 
PHE HB3  H N N 301 
PHE HD1  H N N 302 
PHE HD2  H N N 303 
PHE HE1  H N N 304 
PHE HE2  H N N 305 
PHE HZ   H N N 306 
PHE HXT  H N N 307 
PRO N    N N N 308 
PRO CA   C N S 309 
PRO C    C N N 310 
PRO O    O N N 311 
PRO CB   C N N 312 
PRO CG   C N N 313 
PRO CD   C N N 314 
PRO OXT  O N N 315 
PRO H    H N N 316 
PRO HA   H N N 317 
PRO HB2  H N N 318 
PRO HB3  H N N 319 
PRO HG2  H N N 320 
PRO HG3  H N N 321 
PRO HD2  H N N 322 
PRO HD3  H N N 323 
PRO HXT  H N N 324 
SER N    N N N 325 
SER CA   C N S 326 
SER C    C N N 327 
SER O    O N N 328 
SER CB   C N N 329 
SER OG   O N N 330 
SER OXT  O N N 331 
SER H    H N N 332 
SER H2   H N N 333 
SER HA   H N N 334 
SER HB2  H N N 335 
SER HB3  H N N 336 
SER HG   H N N 337 
SER HXT  H N N 338 
THR N    N N N 339 
THR CA   C N S 340 
THR C    C N N 341 
THR O    O N N 342 
THR CB   C N R 343 
THR OG1  O N N 344 
THR CG2  C N N 345 
THR OXT  O N N 346 
THR H    H N N 347 
THR H2   H N N 348 
THR HA   H N N 349 
THR HB   H N N 350 
THR HG1  H N N 351 
THR HG21 H N N 352 
THR HG22 H N N 353 
THR HG23 H N N 354 
THR HXT  H N N 355 
TRP N    N N N 356 
TRP CA   C N S 357 
TRP C    C N N 358 
TRP O    O N N 359 
TRP CB   C N N 360 
TRP CG   C Y N 361 
TRP CD1  C Y N 362 
TRP CD2  C Y N 363 
TRP NE1  N Y N 364 
TRP CE2  C Y N 365 
TRP CE3  C Y N 366 
TRP CZ2  C Y N 367 
TRP CZ3  C Y N 368 
TRP CH2  C Y N 369 
TRP OXT  O N N 370 
TRP H    H N N 371 
TRP H2   H N N 372 
TRP HA   H N N 373 
TRP HB2  H N N 374 
TRP HB3  H N N 375 
TRP HD1  H N N 376 
TRP HE1  H N N 377 
TRP HE3  H N N 378 
TRP HZ2  H N N 379 
TRP HZ3  H N N 380 
TRP HH2  H N N 381 
TRP HXT  H N N 382 
TYR N    N N N 383 
TYR CA   C N S 384 
TYR C    C N N 385 
TYR O    O N N 386 
TYR CB   C N N 387 
TYR CG   C Y N 388 
TYR CD1  C Y N 389 
TYR CD2  C Y N 390 
TYR CE1  C Y N 391 
TYR CE2  C Y N 392 
TYR CZ   C Y N 393 
TYR OH   O N N 394 
TYR OXT  O N N 395 
TYR H    H N N 396 
TYR H2   H N N 397 
TYR HA   H N N 398 
TYR HB2  H N N 399 
TYR HB3  H N N 400 
TYR HD1  H N N 401 
TYR HD2  H N N 402 
TYR HE1  H N N 403 
TYR HE2  H N N 404 
TYR HH   H N N 405 
TYR HXT  H N N 406 
UJT N1   N Y N 407 
UJT C7   C N N 408 
UJT C8   C N N 409 
UJT N2   N Y N 410 
UJT C9   C N N 411 
UJT O1   O N N 412 
UJT C1   C Y N 413 
UJT O5   O N N 414 
UJT C5   C N R 415 
UJT C6   C N R 416 
UJT N3   N Y N 417 
UJT C4   C Y N 418 
UJT O4   O N N 419 
UJT C3   C Y N 420 
UJT O3   O N N 421 
UJT C2   C Y N 422 
UJT N4   N Y N 423 
UJT N    N N N 424 
UJT C    C Y N 425 
UJT O    O N N 426 
UJT C10  C N N 427 
UJT C11  C N N 428 
UJT C12  C N N 429 
UJT C13  C N N 430 
UJT C14  C Y N 431 
UJT C15  C Y N 432 
UJT C16  C Y N 433 
UJT C17  C Y N 434 
UJT C18  C Y N 435 
UJT C19  C N R 436 
UJT C20  C N R 437 
UJT C21  C N N 438 
UJT C22  C N S 439 
UJT C23  C N R 440 
UJT C24  C N S 441 
UJT C25  C N R 442 
UJT N10  N Y N 443 
UJT N5   N N N 444 
UJT N6   N Y N 445 
UJT N7   N N N 446 
UJT N8   N Y N 447 
UJT N9   N Y N 448 
UJT O2   O N N 449 
UJT O6   O N N 450 
UJT O7   O N N 451 
UJT H8   H N N 452 
UJT H9   H N N 453 
UJT H10  H N N 454 
UJT H11  H N N 455 
UJT H13  H N N 456 
UJT H12  H N N 457 
UJT H16  H N N 458 
UJT H6   H N N 459 
UJT H28  H N N 460 
UJT H    H N N 461 
UJT H1   H N N 462 
UJT H26  H N N 463 
UJT H7   H N N 464 
UJT H24  H N N 465 
UJT H5   H N N 466 
UJT H4   H N N 467 
UJT H15  H N N 468 
UJT H14  H N N 469 
UJT H18  H N N 470 
UJT H17  H N N 471 
UJT H21  H N N 472 
UJT H2   H N N 473 
UJT H3   H N N 474 
UJT H23  H N N 475 
UJT H22  H N N 476 
UJT H25  H N N 477 
UJT H27  H N N 478 
UJT H29  H N N 479 
UJT H31  H N N 480 
UJT H19  H N N 481 
UJT H20  H N N 482 
UJT H30  H N N 483 
UJT H32  H N N 484 
VAL N    N N N 485 
VAL CA   C N S 486 
VAL C    C N N 487 
VAL O    O N N 488 
VAL CB   C N N 489 
VAL CG1  C N N 490 
VAL CG2  C N N 491 
VAL OXT  O N N 492 
VAL H    H N N 493 
VAL H2   H N N 494 
VAL HA   H N N 495 
VAL HB   H N N 496 
VAL HG11 H N N 497 
VAL HG12 H N N 498 
VAL HG13 H N N 499 
VAL HG21 H N N 500 
VAL HG22 H N N 501 
VAL HG23 H N N 502 
VAL HXT  H N N 503 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
GOL C1  O1   sing N N 149 
GOL C1  C2   sing N N 150 
GOL C1  H11  sing N N 151 
GOL C1  H12  sing N N 152 
GOL O1  HO1  sing N N 153 
GOL C2  O2   sing N N 154 
GOL C2  C3   sing N N 155 
GOL C2  H2   sing N N 156 
GOL O2  HO2  sing N N 157 
GOL C3  O3   sing N N 158 
GOL C3  H31  sing N N 159 
GOL C3  H32  sing N N 160 
GOL O3  HO3  sing N N 161 
HIS N   CA   sing N N 162 
HIS N   H    sing N N 163 
HIS N   H2   sing N N 164 
HIS CA  C    sing N N 165 
HIS CA  CB   sing N N 166 
HIS CA  HA   sing N N 167 
HIS C   O    doub N N 168 
HIS C   OXT  sing N N 169 
HIS CB  CG   sing N N 170 
HIS CB  HB2  sing N N 171 
HIS CB  HB3  sing N N 172 
HIS CG  ND1  sing Y N 173 
HIS CG  CD2  doub Y N 174 
HIS ND1 CE1  doub Y N 175 
HIS ND1 HD1  sing N N 176 
HIS CD2 NE2  sing Y N 177 
HIS CD2 HD2  sing N N 178 
HIS CE1 NE2  sing Y N 179 
HIS CE1 HE1  sing N N 180 
HIS NE2 HE2  sing N N 181 
HIS OXT HXT  sing N N 182 
HOH O   H1   sing N N 183 
HOH O   H2   sing N N 184 
ILE N   CA   sing N N 185 
ILE N   H    sing N N 186 
ILE N   H2   sing N N 187 
ILE CA  C    sing N N 188 
ILE CA  CB   sing N N 189 
ILE CA  HA   sing N N 190 
ILE C   O    doub N N 191 
ILE C   OXT  sing N N 192 
ILE CB  CG1  sing N N 193 
ILE CB  CG2  sing N N 194 
ILE CB  HB   sing N N 195 
ILE CG1 CD1  sing N N 196 
ILE CG1 HG12 sing N N 197 
ILE CG1 HG13 sing N N 198 
ILE CG2 HG21 sing N N 199 
ILE CG2 HG22 sing N N 200 
ILE CG2 HG23 sing N N 201 
ILE CD1 HD11 sing N N 202 
ILE CD1 HD12 sing N N 203 
ILE CD1 HD13 sing N N 204 
ILE OXT HXT  sing N N 205 
LEU N   CA   sing N N 206 
LEU N   H    sing N N 207 
LEU N   H2   sing N N 208 
LEU CA  C    sing N N 209 
LEU CA  CB   sing N N 210 
LEU CA  HA   sing N N 211 
LEU C   O    doub N N 212 
LEU C   OXT  sing N N 213 
LEU CB  CG   sing N N 214 
LEU CB  HB2  sing N N 215 
LEU CB  HB3  sing N N 216 
LEU CG  CD1  sing N N 217 
LEU CG  CD2  sing N N 218 
LEU CG  HG   sing N N 219 
LEU CD1 HD11 sing N N 220 
LEU CD1 HD12 sing N N 221 
LEU CD1 HD13 sing N N 222 
LEU CD2 HD21 sing N N 223 
LEU CD2 HD22 sing N N 224 
LEU CD2 HD23 sing N N 225 
LEU OXT HXT  sing N N 226 
LYS N   CA   sing N N 227 
LYS N   H    sing N N 228 
LYS N   H2   sing N N 229 
LYS CA  C    sing N N 230 
LYS CA  CB   sing N N 231 
LYS CA  HA   sing N N 232 
LYS C   O    doub N N 233 
LYS C   OXT  sing N N 234 
LYS CB  CG   sing N N 235 
LYS CB  HB2  sing N N 236 
LYS CB  HB3  sing N N 237 
LYS CG  CD   sing N N 238 
LYS CG  HG2  sing N N 239 
LYS CG  HG3  sing N N 240 
LYS CD  CE   sing N N 241 
LYS CD  HD2  sing N N 242 
LYS CD  HD3  sing N N 243 
LYS CE  NZ   sing N N 244 
LYS CE  HE2  sing N N 245 
LYS CE  HE3  sing N N 246 
LYS NZ  HZ1  sing N N 247 
LYS NZ  HZ2  sing N N 248 
LYS NZ  HZ3  sing N N 249 
LYS OXT HXT  sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
PHE N   CA   sing N N 270 
PHE N   H    sing N N 271 
PHE N   H2   sing N N 272 
PHE CA  C    sing N N 273 
PHE CA  CB   sing N N 274 
PHE CA  HA   sing N N 275 
PHE C   O    doub N N 276 
PHE C   OXT  sing N N 277 
PHE CB  CG   sing N N 278 
PHE CB  HB2  sing N N 279 
PHE CB  HB3  sing N N 280 
PHE CG  CD1  doub Y N 281 
PHE CG  CD2  sing Y N 282 
PHE CD1 CE1  sing Y N 283 
PHE CD1 HD1  sing N N 284 
PHE CD2 CE2  doub Y N 285 
PHE CD2 HD2  sing N N 286 
PHE CE1 CZ   doub Y N 287 
PHE CE1 HE1  sing N N 288 
PHE CE2 CZ   sing Y N 289 
PHE CE2 HE2  sing N N 290 
PHE CZ  HZ   sing N N 291 
PHE OXT HXT  sing N N 292 
PRO N   CA   sing N N 293 
PRO N   CD   sing N N 294 
PRO N   H    sing N N 295 
PRO CA  C    sing N N 296 
PRO CA  CB   sing N N 297 
PRO CA  HA   sing N N 298 
PRO C   O    doub N N 299 
PRO C   OXT  sing N N 300 
PRO CB  CG   sing N N 301 
PRO CB  HB2  sing N N 302 
PRO CB  HB3  sing N N 303 
PRO CG  CD   sing N N 304 
PRO CG  HG2  sing N N 305 
PRO CG  HG3  sing N N 306 
PRO CD  HD2  sing N N 307 
PRO CD  HD3  sing N N 308 
PRO OXT HXT  sing N N 309 
SER N   CA   sing N N 310 
SER N   H    sing N N 311 
SER N   H2   sing N N 312 
SER CA  C    sing N N 313 
SER CA  CB   sing N N 314 
SER CA  HA   sing N N 315 
SER C   O    doub N N 316 
SER C   OXT  sing N N 317 
SER CB  OG   sing N N 318 
SER CB  HB2  sing N N 319 
SER CB  HB3  sing N N 320 
SER OG  HG   sing N N 321 
SER OXT HXT  sing N N 322 
THR N   CA   sing N N 323 
THR N   H    sing N N 324 
THR N   H2   sing N N 325 
THR CA  C    sing N N 326 
THR CA  CB   sing N N 327 
THR CA  HA   sing N N 328 
THR C   O    doub N N 329 
THR C   OXT  sing N N 330 
THR CB  OG1  sing N N 331 
THR CB  CG2  sing N N 332 
THR CB  HB   sing N N 333 
THR OG1 HG1  sing N N 334 
THR CG2 HG21 sing N N 335 
THR CG2 HG22 sing N N 336 
THR CG2 HG23 sing N N 337 
THR OXT HXT  sing N N 338 
TRP N   CA   sing N N 339 
TRP N   H    sing N N 340 
TRP N   H2   sing N N 341 
TRP CA  C    sing N N 342 
TRP CA  CB   sing N N 343 
TRP CA  HA   sing N N 344 
TRP C   O    doub N N 345 
TRP C   OXT  sing N N 346 
TRP CB  CG   sing N N 347 
TRP CB  HB2  sing N N 348 
TRP CB  HB3  sing N N 349 
TRP CG  CD1  doub Y N 350 
TRP CG  CD2  sing Y N 351 
TRP CD1 NE1  sing Y N 352 
TRP CD1 HD1  sing N N 353 
TRP CD2 CE2  doub Y N 354 
TRP CD2 CE3  sing Y N 355 
TRP NE1 CE2  sing Y N 356 
TRP NE1 HE1  sing N N 357 
TRP CE2 CZ2  sing Y N 358 
TRP CE3 CZ3  doub Y N 359 
TRP CE3 HE3  sing N N 360 
TRP CZ2 CH2  doub Y N 361 
TRP CZ2 HZ2  sing N N 362 
TRP CZ3 CH2  sing Y N 363 
TRP CZ3 HZ3  sing N N 364 
TRP CH2 HH2  sing N N 365 
TRP OXT HXT  sing N N 366 
TYR N   CA   sing N N 367 
TYR N   H    sing N N 368 
TYR N   H2   sing N N 369 
TYR CA  C    sing N N 370 
TYR CA  CB   sing N N 371 
TYR CA  HA   sing N N 372 
TYR C   O    doub N N 373 
TYR C   OXT  sing N N 374 
TYR CB  CG   sing N N 375 
TYR CB  HB2  sing N N 376 
TYR CB  HB3  sing N N 377 
TYR CG  CD1  doub Y N 378 
TYR CG  CD2  sing Y N 379 
TYR CD1 CE1  sing Y N 380 
TYR CD1 HD1  sing N N 381 
TYR CD2 CE2  doub Y N 382 
TYR CD2 HD2  sing N N 383 
TYR CE1 CZ   doub Y N 384 
TYR CE1 HE1  sing N N 385 
TYR CE2 CZ   sing Y N 386 
TYR CE2 HE2  sing N N 387 
TYR CZ  OH   sing N N 388 
TYR OH  HH   sing N N 389 
TYR OXT HXT  sing N N 390 
UJT N   C    sing N N 391 
UJT C   N1   doub Y N 392 
UJT N1  C1   sing Y N 393 
UJT C1  N2   doub Y N 394 
UJT N2  C2   sing Y N 395 
UJT C2  N3   sing Y N 396 
UJT C3  N3   sing Y N 397 
UJT N4  C3   doub Y N 398 
UJT C4  N4   sing Y N 399 
UJT C   C4   sing Y N 400 
UJT C2  C4   doub Y N 401 
UJT N3  C5   sing N N 402 
UJT C5  O    sing N N 403 
UJT O   C6   sing N N 404 
UJT C7  C6   sing N N 405 
UJT N5  C7   sing N N 406 
UJT C8  N5   sing N N 407 
UJT C9  C8   sing N N 408 
UJT C10 C9   sing N N 409 
UJT O1  C10  sing N N 410 
UJT C11 N5   sing N N 411 
UJT C12 C11  sing N N 412 
UJT C13 C12  trip N N 413 
UJT C14 C13  sing N N 414 
UJT C14 N6   doub Y N 415 
UJT N6  C15  sing Y N 416 
UJT C15 C16  doub Y N 417 
UJT N7  C16  sing N N 418 
UJT C16 N8   sing Y N 419 
UJT N8  C17  doub Y N 420 
UJT C17 N9   sing Y N 421 
UJT N9  C18  doub Y N 422 
UJT C15 C18  sing Y N 423 
UJT C18 N10  sing Y N 424 
UJT N10 C14  sing Y N 425 
UJT C19 N10  sing N N 426 
UJT C19 O2   sing N N 427 
UJT O2  C20  sing N N 428 
UJT C21 C20  sing N N 429 
UJT O3  C21  sing N N 430 
UJT C20 C22  sing N N 431 
UJT O4  C22  sing N N 432 
UJT C22 C23  sing N N 433 
UJT C23 C19  sing N N 434 
UJT O5  C23  sing N N 435 
UJT C6  C24  sing N N 436 
UJT O6  C24  sing N N 437 
UJT C24 C25  sing N N 438 
UJT C5  C25  sing N N 439 
UJT C25 O7   sing N N 440 
UJT C7  H8   sing N N 441 
UJT C7  H9   sing N N 442 
UJT C8  H10  sing N N 443 
UJT C8  H11  sing N N 444 
UJT C9  H13  sing N N 445 
UJT C9  H12  sing N N 446 
UJT O1  H16  sing N N 447 
UJT C1  H6   sing N N 448 
UJT O5  H28  sing N N 449 
UJT C5  H    sing N N 450 
UJT C6  H1   sing N N 451 
UJT O4  H26  sing N N 452 
UJT C3  H7   sing N N 453 
UJT O3  H24  sing N N 454 
UJT N   H5   sing N N 455 
UJT N   H4   sing N N 456 
UJT C10 H15  sing N N 457 
UJT C10 H14  sing N N 458 
UJT C11 H18  sing N N 459 
UJT C11 H17  sing N N 460 
UJT C17 H21  sing N N 461 
UJT C19 H2   sing N N 462 
UJT C20 H3   sing N N 463 
UJT C21 H23  sing N N 464 
UJT C21 H22  sing N N 465 
UJT C22 H25  sing N N 466 
UJT C23 H27  sing N N 467 
UJT C24 H29  sing N N 468 
UJT C25 H31  sing N N 469 
UJT N7  H19  sing N N 470 
UJT N7  H20  sing N N 471 
UJT O6  H30  sing N N 472 
UJT O7  H32  sing N N 473 
VAL N   CA   sing N N 474 
VAL N   H    sing N N 475 
VAL N   H2   sing N N 476 
VAL CA  C    sing N N 477 
VAL CA  CB   sing N N 478 
VAL CA  HA   sing N N 479 
VAL C   O    doub N N 480 
VAL C   OXT  sing N N 481 
VAL CB  CG1  sing N N 482 
VAL CB  CG2  sing N N 483 
VAL CB  HB   sing N N 484 
VAL CG1 HG11 sing N N 485 
VAL CG1 HG12 sing N N 486 
VAL CG1 HG13 sing N N 487 
VAL CG2 HG21 sing N N 488 
VAL CG2 HG22 sing N N 489 
VAL CG2 HG23 sing N N 490 
VAL OXT HXT  sing N N 491 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-17-CE18-0011-02 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   8A9V 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8QGG 
_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]   0.015899 
_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]   0.013463 
_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]   0.008447 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 11.55261 36.18129 25.62737  1.000 59.57652 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.75808 36.28133 24.41011  1.000 58.38100 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.71235  35.18388 24.34306  1.000 55.48632 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.58839  34.38439 25.26765  1.000 55.43611 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.66542 36.21400 23.19119  1.000 66.96511 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 13.08917 35.79802 23.51808  1.000 71.42177 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.11889 35.81271 22.02235  1.000 67.58826 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 13.21633 37.02079 21.04803  1.000 71.06834 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 8.96293  35.14924 23.24346  1.000 51.43428 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.04345  34.04687 23.00550  1.000 47.17355 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.84006  32.77199 22.76227  1.000 43.29959 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.82599  32.77835 22.01947  1.000 42.98505 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.13139  34.35366 21.81304  1.000 48.22688 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.08064  35.43029 22.09102  1.000 49.62045 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.26573  35.78846 20.85084  1.000 52.33972 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.18006  36.80684 21.19149  1.000 56.08857 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.66822  37.54275 19.99829  1.000 58.89023 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.42922  31.68442 23.41153  1.000 40.07168 ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.09154  30.39669 23.26172  1.000 38.86085 ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 8.04624  29.29310 23.31582  1.000 38.32920 ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.92455  29.49922 23.78299  1.000 38.92047 ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.14202 30.16218 24.36078  1.000 38.40271 ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.50736  29.77637 25.68075  1.000 38.10953 ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.97897  30.74650 26.52067  1.000 37.31394 ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.40772  28.44472 26.07109  1.000 38.38222 ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.37980  30.40797 27.71408  1.000 40.16344 ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.80817  28.09591 27.26910  1.000 39.72064 ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.29664  29.08242 28.08249  1.000 40.82555 ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.69247  28.74953 29.27222  1.000 42.21088 ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.42762  28.10463 22.84848  1.000 38.19767 ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.60562  26.92804 23.09048  1.000 38.29247 ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.51360  25.71828 23.24122  1.000 34.10696 ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.68991  25.75181 22.87402  1.000 33.83181 ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.56255  26.72232 21.98493  1.000 41.20680 ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.12481  26.36009 20.63166  1.000 41.90759 ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.34216  24.58129 20.44002  1.000 42.51342 ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.64294  24.01291 20.43968  1.000 41.82299 ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.96176  24.64741 23.80752  1.000 32.85219 ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.71269  23.42036 24.03492  1.000 32.32608 ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.90353  22.24383 23.50861  1.000 33.40466 ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.76595  22.02640 23.94527  1.000 33.97693 ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 9.04529  23.21555 25.52520  1.000 31.43548 ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.67466  24.47793 26.11093  1.000 31.20317 ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.98823  22.04478 25.67785  1.000 32.77260 ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 10.04680 24.34323 27.58280  1.000 31.31944 ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.48362  21.48916 22.56820  1.000 33.47571 ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.90567  20.22636 22.13842  1.000 34.66349 ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.52830  19.08831 22.92736  1.000 37.30116 ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.68956  19.15207 23.34124  1.000 41.12322 ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 8.12516  19.97986 20.64025  1.000 39.41294 ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 9.52504  19.81005 20.37892  1.000 41.75220 ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.62892  21.13598 19.83299  1.000 43.73813 ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.74191  18.04589 23.14763  1.000 36.77117 ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 8.19713  16.90111 23.91253  1.000 37.45030 ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 8.00525  15.62494 23.11362  1.000 38.16412 ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 7.01440  15.47446 22.39319  1.000 39.76709 ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.44654  16.78326 25.24698  1.000 36.90384 ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.75790  15.54964 25.86195  1.000 37.12174 ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.96993  14.71179 23.25002  1.000 39.04037 ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.80395  13.34578 22.76491  1.000 41.11474 ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.51830  12.71611 23.28839  1.000 42.41582 ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.89703  11.89746 22.60200  1.000 44.07697 ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 10.02322 12.51546 23.17709  1.000 40.71457 ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.90162  11.02829 22.95204  1.000 43.90820 ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 11.19690 10.32848 23.31128  1.000 48.22768 ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 11.18623 8.88709  22.83338  1.000 51.99942 ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 10.91416 8.80953  21.37523  1.000 55.53111 ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 7.09814  13.08447 24.49134  1.000 42.84117 ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.84823  12.59930 25.03334  1.000 42.61347 ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.95550  11.42734 25.98201  1.000 45.52676 ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.91754  10.91163 26.41482  1.000 46.61840 ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 7.15966  10.97542 26.30870  1.000 47.01800 ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.29976  10.04343 27.41381  1.000 48.90117 ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.40918  10.82871 28.71639  1.000 48.78798 ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.54326  12.05438 28.71779  1.000 48.74093 ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.50666  9.12206  27.21968  1.000 51.29867 ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.80996  9.87886  27.03069  1.000 53.79210 ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.79114  11.12275 27.02141  1.000 53.68099 ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.86317 9.22001  26.88297  1.000 56.22963 ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.35151  10.10363 29.83685  1.000 48.39179 ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.29995  10.75771 31.14265  1.000 49.73411 ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.50376  11.66493 31.36313  1.000 48.45454 ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.35886  12.80466 31.81918  1.000 49.07295 ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.21071  9.71369  32.25648  1.000 52.87137 ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.87424  9.00204  32.34127  1.000 56.71878 ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.77056  8.12161  33.56779  1.000 60.83070 ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.64119  8.24267  34.45822  1.000 62.04237 ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 4.82234  7.31037  33.64101  1.000 61.99154 ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.70300  11.17752 31.04021  1.000 46.98726 ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.91211 11.96122 31.27971  1.000 46.79978 ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.88492 13.27738 30.50762  1.000 45.18725 ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 11.18591 14.34015 31.06070  1.000 45.06975 ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 12.14909 11.14362 30.90995  1.000 50.47882 ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.45425 11.76636 31.38372  1.000 52.34331 ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.68269 11.03674 30.85090  1.000 53.34416 ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.95207 11.63398 31.45494  1.000 55.05984 ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 17.20475 11.15020 30.80290  1.000 55.45660 ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.53451 13.22911 29.21834  1.000 44.92846 ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.51772 14.45852 28.42743  1.000 41.59893 ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.37956  15.38288 28.84817  1.000 40.95137 ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.55855  16.60391 28.91089  1.000 40.49343 ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.41881 14.12593 26.94057  1.000 41.52433 ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.46211 13.24600 26.56173  1.000 41.82777 ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 8.20163  14.82487 29.13478  1.000 42.66804 ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 7.07533  15.65619 29.55316  1.000 43.20900 ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.38035  16.39031 30.85182  1.000 42.82368 ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 7.05568  17.57601 30.99944  1.000 42.22475 ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.82295  14.79836 29.71332  1.000 45.92835 ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 5.09347  14.57428 28.40760  1.000 48.66394 ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.53738  15.11298 27.37127  1.000 49.42290 ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 4.06644  13.86055 28.42392  1.000 51.55879 ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 8.00298  15.69922 31.80684  1.000 44.12474 ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.30297  16.32687 33.08610  1.000 43.56830 ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.38767  17.38683 32.94176  1.000 40.64685 ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.29436  18.45776 33.55123  1.000 40.94399 ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.69996  15.25913 34.10383  1.000 45.54267 ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.56627  14.28469 34.44130  0.700 47.15138 ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 8.07193  13.12016 35.28614  0.700 48.10411 ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 6.41498  15.00164 35.14861  0.700 47.34909 ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.41827 17.11817 32.13246  1.000 38.93850 ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.44222 18.13241 31.90965  1.000 37.22834 ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.83787 19.36757 31.25907  1.000 35.92506 ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 11.19768 20.50016 31.59864  1.000 36.92419 ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.57819 17.56537 31.05196  1.000 39.53737 ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.79949 18.46173 30.82729  1.000 41.04914 ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.44241 18.88157 32.13143  1.000 43.93035 ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.82787 17.77050 29.92925  1.000 41.03522 ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.90547  19.16429 30.32600  1.000 35.78031 ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.21981  20.28548 29.69373  1.000 34.63867 ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.46946  21.12616 30.72041  1.000 36.17873 ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.54065  22.36080 30.69956  1.000 36.58917 ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.25879  19.77207 28.62353  1.000 33.76763 ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.33252  20.84764 28.10257  1.000 34.85852 ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.51015  20.34552 26.91955  1.000 35.75408 ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.60775  21.37333 26.41830  1.000 36.16348 ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.42999  21.65152 26.95905  1.000 37.16917 ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.96830  20.96987 27.99563  1.000 38.82548 ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.69796  22.63808 26.45024  1.000 39.87775 ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.73331  20.47393 31.62203  1.000 36.30965 ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.98030  21.22537 32.62522  1.000 36.77002 ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.91045  21.97547 33.57451  1.000 36.75867 ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.61883  23.11302 33.96823  1.000 36.63106 ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 6.04594  20.29135 33.40155  1.000 38.67551 ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.81441  19.77511 32.65236  1.000 38.50627 ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.90746  18.97582 33.56352  1.000 38.29595 ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 4.04014  20.92080 31.99409  1.000 38.25289 ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 9.03800  21.36363 33.94661  1.000 37.20200 ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.99564  22.04916 34.81345  1.000 38.12706 ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.64968 23.22837 34.10669  1.000 38.96899 ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.94703 24.24500 34.73840  1.000 41.09208 ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 11.06397 21.07805 35.30159  1.000 39.69044 ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.66074 20.36659 36.56135  1.000 41.41996 ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.73045  20.78928 37.25165  1.000 42.48869 ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.35552 19.28220 36.87692  1.000 42.88346 ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.90848 23.11133 32.79885  1.000 35.57243 ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.48778 24.24914 32.09474  1.000 36.73450 ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.47842 25.37733 31.94259  1.000 38.43804 ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.84329 26.55451 32.01478  1.000 41.83979 ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 12.02541 23.81362 30.73310  1.000 37.14476 ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.25543 22.95987 30.85519  1.000 38.01847 ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.94804 22.57631 29.23948  1.000 40.57130 ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.75561 24.12151 28.83743  1.000 41.05316 ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.20662  25.04151 31.72801  1.000 39.12506 ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.17680  26.07261 31.66369  1.000 36.23695 ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 8.08737  26.80075 32.99427  1.000 34.70914 ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.96631  28.02914 33.04337  1.000 35.61815 ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.82617  25.45650 31.26327  1.000 36.45512 ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.86009  25.02977 29.78979  1.000 33.86375 ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.69333  26.43986 31.52795  1.000 37.47915 ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.70203  24.15364 29.39451  1.000 35.48062 ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.16665  26.05498 34.09213  1.000 35.20446 ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 8.17619  26.69215 35.40026  1.000 37.87874 ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.35979  27.64166 35.53880  1.000 39.21050 ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.21239  28.76165 36.04588  1.000 39.71502 ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 8.20568  25.62914 36.49627  1.000 38.62106 ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.54052 27.21146 35.09027  1.000 39.78947 ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.71648 28.05961 35.19026  1.000 39.08774 ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.62525 29.29259 34.31482  1.000 40.98567 ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 12.07192 30.37654 34.70155  1.000 43.48858 ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 11.05577 29.14443 33.11764  1.000 38.09061 ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.87822 30.30297 32.25004  1.000 40.99582 ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.90794  31.30858 32.85080  1.000 43.18070 ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 10.02990 32.51351 32.59804  1.000 43.81561 ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.40059 29.86255 30.86834  1.000 40.00187 ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.50800 29.38547 29.97645  1.000 41.57874 ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.55590 30.22971 29.65137  1.000 43.48011 ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.50116 28.10021 29.46256  1.000 41.03811 ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.58153 29.80247 28.82835  1.000 43.52144 ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.52204 27.66031 28.63472  1.000 42.26854 ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.56498 28.51353 28.31846  1.000 43.44293 ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.95269  30.84206 33.65376  1.000 44.38724 ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.99796  31.73365 34.27839  1.000 46.07395 ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.60173  32.72054 35.25439  1.000 47.41064 ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.89762  33.63485 35.69343  1.000 48.17900 ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.87554  32.56307 35.60163  1.000 48.64833 ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.55726 33.51511 36.46469  1.000 50.63775 ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.27780 34.60431 35.68196  1.000 52.02381 ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.94979 35.44027 36.29108  1.000 54.34075 ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.54542 32.78466 37.38360  1.000 51.98171 ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.91920 31.64096 38.17331  1.000 51.77300 ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.92112  32.12043 39.22178  1.000 54.32726 ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 10.01893 33.29182 39.66113  1.000 55.03581 ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 9.03717  31.32146 39.61127  1.000 54.85301 ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.14087 34.62773 34.35680  1.000 51.51550 ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.76592 35.63510 33.51192  1.000 53.03783 ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.71641 36.25522 32.59747  1.000 54.98537 ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.56814  35.80690 32.53326  1.000 53.97437 ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.90432 35.03539 32.67307  1.000 52.97520 ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.99322 34.37983 33.48966  1.000 52.54563 ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.89698 33.04788 33.87072  1.000 52.11971 ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 15.12107 35.09122 33.87451  1.000 54.37059 ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.89324 32.44232 34.61708  1.000 52.13482 ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 16.12202 34.49599 34.62057  1.000 54.79418 ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 16.00218 33.17132 34.99066  1.000 54.27707 ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 17.00011 32.57465 35.73365  1.000 55.91987 ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 11.12269 37.30152 31.87760  1.000 57.00028 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.26238 37.88390 30.85440  1.000 58.67161 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 10.22280 36.95094 29.65160  1.000 59.07648 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.79918 37.25032 28.59996  1.000 61.14910 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.75144 39.27525 30.44257  1.000 61.45895 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.76686  39.99725 29.53202  1.000 64.93174 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 8.61296  39.53066 29.40669  1.000 66.49663 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 10.14621 41.03095 28.94035  1.000 66.17908 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.56346  35.80563 29.81247  1.000 58.06032 ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.44353  34.80593 28.76087  1.000 57.82597 ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.99764  34.34633 28.70636  1.000 57.34913 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.42672  33.96725 29.73313  1.000 59.20901 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.37562 33.61461 29.01551  1.000 59.11039 ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.85878 33.96526 29.02958  1.000 61.11882 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.51707 34.47883 27.42759  1.000 62.29524 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 12.34250 32.97361 26.47228  1.000 61.60278 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.40954  34.38605 27.51631  1.000 54.65044 ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 6.00572  34.05265 27.31716  1.000 52.89735 ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.90390  32.77226 26.50527  1.000 49.62933 ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.48081  32.68150 25.41836  1.000 49.27288 ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.28080  35.18869 26.59504  1.000 57.17566 ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.86269  34.86172 26.17056  1.000 60.02412 ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.21609  36.00140 25.40820  1.000 63.53804 ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 3.96012  36.84581 24.86216  1.000 64.04235 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 1.96715  36.05625 25.36231  1.000 65.58116 ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.18200  31.78576 27.02545  1.000 46.49568 ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.92974  30.58793 26.23494  1.000 45.13715 ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.97617  30.92527 25.08903  1.000 45.69198 ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.88319  31.45368 25.31407  1.000 47.25747 ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.35957  29.47261 27.11070  1.000 43.05352 ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.42219  28.12628 26.43821  1.000 39.85916 ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.48905  27.76886 25.46970  1.000 40.93419 ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.43146  27.22020 26.74333  1.000 39.22445 ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.55216  26.54667 24.83177  1.000 40.97870 ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.49737  25.99142 26.11328  1.000 38.74071 ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.55300  25.65992 25.15499  1.000 40.28986 ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.61319  24.43787 24.51381  1.000 42.14156 ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.39406  30.62634 23.85762  1.000 45.95332 ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.58241  30.90465 22.67469  1.000 47.58658 ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 4.01033  29.91569 21.60328  1.000 47.04729 ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 5.11357  30.03513 21.06394  1.000 47.51509 ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.76737  32.34729 22.19933  1.000 51.15608 ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.88379  32.70442 20.99919  1.000 53.39446 ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.54298  31.81796 20.18704  1.000 52.92062 ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.53217  33.89466 20.86505  1.000 56.43737 ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 3.14702  28.95260 21.29131  1.000 47.11700 ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.45282  27.97549 20.25517  1.000 47.96548 ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.90268  28.36400 18.88523  1.000 48.49192 ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 3.00277  27.56740 17.94743  1.000 48.36149 ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.94767  26.58411 20.65705  1.000 49.05544 ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.43507  26.49891 20.74438  1.000 51.77253 ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.74926  27.51454 20.49951  1.000 51.69827 ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.93291  25.40027 21.06741  1.000 52.75388 ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.31922  29.55246 18.75012  1.000 48.40627 ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.90062  30.04163 17.43966  1.000 48.85789 ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.01438  30.83118 16.77002  1.000 48.74648 ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.38419  30.56224 15.62429  1.000 48.46714 ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.61428  30.88344 17.56163  1.000 50.25950 ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.22189  31.42542 16.19971  1.000 50.81227 ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.50932 30.04972 18.15075  1.000 50.82271 ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.57797  31.80986 17.47121  1.000 49.98801 ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.69073  32.60462 16.95223  1.000 51.54464 ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.84282  32.63238 17.94995  1.000 49.96497 ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.24287  33.69857 18.42406  1.000 51.71286 ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.22660  34.02110 16.61552  1.000 55.46058 ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.15038  34.07578 15.54738  1.000 58.57650 ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.88296  35.48544 15.05069  0.700 59.99827 ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 3.63394  36.40879 15.43229  0.700 59.32786 ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 1.91941  35.66753 14.27709  0.700 61.39951 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.42101  31.47533 18.27624  1.000 46.74929 ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.60333  31.48132 19.13876  1.000 45.64712 ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.79767  32.05636 18.40182  1.000 45.14801 ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.87559  32.02164 17.17289  1.000 47.39097 ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.81572  29.99935 19.46061  1.000 43.65385 ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.29636  29.29693 18.25087  1.000 43.05813 ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 6.10157  30.11290 17.80892  1.000 43.96797 ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.72473  32.61728 19.16854  1.000 44.79645 ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.03969 32.93720 18.63775  1.000 45.19299 ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.07982 31.89805 19.02303  1.000 40.97170 ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.12248 31.80708 18.36729  1.000 39.33691 ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.48554 34.32810 19.11089  1.000 48.69721 ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.73613 35.47799 18.42488  0.800 51.91848 ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 11.63626 36.34988 17.55500  0.700 54.55587 ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 12.34841 37.21237 18.11232  0.700 55.76189 ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 11.63312 36.17510 16.31422  0.700 54.49107 ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.80150 31.10503 20.05310  1.000 39.13401 ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.65856 30.01507 20.49451  1.000 38.89332 ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.82328 28.74473 20.50319  1.000 36.80720 ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.73103 28.72310 21.08087  1.000 36.24729 ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.23847 30.28694 21.89533  1.000 40.74999 ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 14.13999 31.51871 21.87106  1.000 43.12293 ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 13.99205 29.07407 22.40300  1.000 42.27400 ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 14.48234 32.04450 23.25157  1.000 45.05962 ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.32973 27.69169 19.86911  1.000 34.70447 ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.69138 26.38267 19.90039  1.000 32.75553 ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.66066 25.39692 20.53246  1.000 31.03082 ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.74889 25.15415 19.99720  1.000 33.27967 ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.26511 25.90687 18.50548  1.000 33.27785 ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.78774 24.48238 18.59075  1.000 33.83216 ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.15913 26.80676 17.95435  1.000 33.52670 ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.26756 24.83799 21.67207  1.000 31.62669 ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 13.05197 23.84514 22.38514  1.000 32.72039 ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.41549 22.48732 22.15704  1.000 30.83191 ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.21515 22.30949 22.39076  1.000 31.20184 ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 13.11618 24.17059 23.88708  1.000 34.89091 ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.71674 25.56018 24.09847  1.000 35.78687 ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.88769 23.09318 24.64224  1.000 35.34826 ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.47895 26.10480 25.50144  1.000 36.21534 ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.21215 21.53485 21.68746  1.000 29.67905 ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.76912 20.17636 21.42964  1.000 31.05540 ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.38186 19.25949 22.47332  1.000 32.61098 ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.60425 19.25033 22.64565  1.000 33.74810 ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.18660 19.74564 20.01367  1.000 33.37663 ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 13.03626 18.35700 19.82174  1.000 38.86278 ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.54134 18.51131 23.18602  1.000 31.98693 ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 13.00754 17.60775 24.23509  1.000 32.57192 ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.69035 16.18369 23.81198  1.000 32.06902 ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.52125 15.78064 23.77819  1.000 32.98357 ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.38567 17.91500 25.60003  1.000 33.13846 ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.61072 19.38181 25.97292  1.000 31.69932 ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 13.00284 16.97935 26.64080  1.000 35.73258 ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 12.12361 19.74098 27.39692  1.000 31.41193 ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.72796 15.42568 23.48149  1.000 33.10306 ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.55184 14.05362 23.05592  1.000 35.75304 ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.78150 13.54010 22.34741  1.000 39.69313 ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.85447 13.43237 22.94883  1.000 44.93383 ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.63543 13.21645 21.06815  1.000 36.90467 ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.77009 12.82271 20.26538  1.000 34.35244 ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.73065 13.55990 18.94825  1.000 34.42691 ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 15.02683 14.56475 18.81748  1.000 33.48705 ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.47438 13.06803 17.96173  1.000 35.92633 ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.51002 13.76257 16.68455  1.000 35.20305 ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 15.17168 13.68350 15.96219  1.000 36.30330 ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.82975 14.59891 15.20438  1.000 34.62031 ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.64049 13.20658 15.81945  1.000 35.56046 ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 19.01078 13.66218 16.29571  1.000 36.51153 ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 19.10402 14.75444 16.89191  1.000 38.25242 ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 20.00181 12.93661 16.07827  1.000 40.33609 ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.39844 12.61666 16.18691  1.000 35.90570 ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 13.06760 12.55265 15.60210  1.000 34.06372 ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 12.17223 13.66970 16.10200  1.000 34.70069 ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.50250 14.34953 15.31693  1.000 35.53022 ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 12.14839 13.87052 17.42675  1.000 33.42993 ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.42969 14.99786 18.00156  1.000 31.68345 ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.90671 16.31641 17.41522  1.000 29.13726 ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 11.09374 17.19557 17.10887  1.000 30.77662 ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.60150 15.00293 19.52618  1.000 34.64244 ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.39894 13.67917 20.02596  1.000 39.95825 ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.60250 15.94487 20.18889  1.000 32.35705 ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.22160 16.47065 17.24140  1.000 28.48218 ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.74313 17.71619 16.69766  1.000 28.53763 ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.31200 17.90295 15.24653  1.000 29.09521 ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.90081 19.00207 14.85742  1.000 29.52729 ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.26727 17.75647 16.81161  1.000 31.28195 ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.84968 19.10025 16.48009  1.000 31.70141 ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 16.08482 19.47164 15.15847  1.000 31.29992 ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 16.14541 20.00353 17.48112  1.000 33.83317 ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.60742 20.71550 14.85508  1.000 34.37118 ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.67351 21.24855 17.18200  1.000 34.69222 ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.90506 21.60618 15.86516  1.000 33.71055 ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.40453 16.84456 14.43287  1.000 27.24734 ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.91046 16.93623 13.05874  1.000 28.23750 ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.45517 17.37113 13.03672  1.000 29.45292 ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 11.05035 18.17465 12.19282  1.000 30.45684 ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 13.06192 15.59526 12.32864  1.000 31.22481 ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.27216 15.25517 11.44594  1.000 35.42744 ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.85857 16.47685 10.74610  1.000 33.24910 ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 15.34436 14.49219 12.18506  1.000 42.61704 ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.65093 16.86419 13.97139  1.000 29.52095 ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 9.24236  17.23992 13.97809  1.000 32.86139 ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 9.06169  18.69676 14.37901  1.000 32.52998 ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.19389  19.38874 13.83428  1.000 33.41314 ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.45464  16.30753 14.89239  1.000 37.31003 ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.21256  15.09231 14.20596  1.000 40.68162 ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.87659  19.18596 15.31826  1.000 31.50975 ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.81854  20.59976 15.66934  1.000 31.85755 ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.13930 21.46998 14.46406  1.000 31.65809 ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.46651  22.47556 14.20926  1.000 33.96258 ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.78505 20.90477 16.81675  1.000 32.12488 ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.18552 21.10361 13.72366  1.000 30.07320 ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.56174 21.84346 12.52604  1.000 31.37273 ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.40095 21.93196 11.54227  1.000 33.91075 ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 10.09602 23.00315 11.00195  1.000 36.19288 ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.76813 21.16071 11.88144  1.000 28.91620 ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 13.06380 21.64318 10.49766  1.000 30.92769 ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.65935 22.87271 10.29132  1.000 33.74913 ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.74796 20.86079 9.39834   1.000 30.00359 ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.93580 23.31460 9.00141   1.000 35.12407 ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 13.01517 21.29924 8.11189   1.000 33.27288 ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.60773 22.52524 7.91528   1.000 34.81197 ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.73508  20.80720 11.29929  1.000 33.84726 ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.64647  20.81945 10.33314  1.000 32.94396 ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.40115  21.49225 10.88409  1.000 36.43772 ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.63631  22.08070 10.11659  1.000 39.58424 ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.36262  19.40111 9.86329   1.000 32.21356 ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.39324  18.90769 8.90567   1.000 32.68475 ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.44881  19.33765 7.59784   1.000 33.61936 ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.45017 18.08098 9.07917   1.000 31.96459 ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.48119 18.77263 6.99895   1.000 33.08186 ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.10940 18.01222 7.87770   1.000 32.42547 ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.18790  21.44813 12.20170  1.000 37.36501 ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 6.06122  22.18178 12.76665  1.000 38.61512 ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.17562  23.67657 12.48804  1.000 40.93883 ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.15592  24.35512 12.31936  1.000 43.96580 ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.96006  21.92220 14.27554  1.000 40.65170 ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.68876  22.46488 14.91194  1.000 43.63720 ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.58807  22.15922 16.40623  1.000 46.43204 ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.32470  21.32461 16.93309  1.000 46.86090 ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.66368  22.83391 17.08981  1.000 48.16253 ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.40036  24.20243 12.40395  1.000 40.70159 ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.63347  25.63628 12.26733  1.000 40.74759 ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.42684  25.98718 11.00991  1.000 40.82017 ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.12642  27.00250 10.96812  1.000 42.64724 ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.33454  26.16530 13.51308  1.000 42.29466 ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.44784  26.08466 14.72414  1.000 42.85468 ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.45888  27.03203 14.93777  1.000 43.99315 ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.57206  25.04709 15.63449  1.000 42.67421 ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.63108  26.96375 16.03029  1.000 44.19048 ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.74685  24.96662 16.73646  1.000 43.45785 ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.77939  25.93289 16.93273  1.000 43.90812 ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.94409  25.87449 18.02379  1.000 43.26933 ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.30425  25.17676 9.96291   1.000 38.48166 ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.10995  25.40888 8.76924   1.000 40.57105 ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.74019  26.70224 8.04870   1.000 41.72429 ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.55437  27.21939 7.27768   1.000 42.74553 ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 8.98823  24.21604 7.82076   1.000 41.44549 ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.56515  23.87395 7.42842   1.000 44.63257 ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.44871  22.51561 6.76031   1.000 48.88782 ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.49356  21.90999 6.42764   1.000 48.44637 ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 6.30181  22.05257 6.56883   1.000 52.16620 ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.54419  27.24265 8.28243   1.000 44.28212 ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.15692  28.48651 7.63084   1.000 46.98701 ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.69556  29.72786 8.33189   1.000 46.92115 ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.60563  30.82064 7.76575   1.000 47.88291 ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.63236  28.58110 7.52567   1.000 51.95027 ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.01566  27.55754 6.58637   0.800 55.09402 ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 5.57784  27.64304 5.17875   0.700 58.56867 ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 5.83531  28.76977 4.69888   0.700 58.73947 ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 5.77215  26.57892 4.55400   0.700 60.47396 ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.25017  29.60099 9.53505   1.000 44.55226 ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.80478  30.74185 10.25519  1.000 44.14951 ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.25330 30.49257 10.65451  1.000 42.25613 ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.69615 30.88766 11.73589  1.000 41.73007 ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 7.95991  31.08208 11.48295  1.000 46.01809 ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.67312  31.82802 11.14720  1.000 49.60114 ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.91560  32.28449 12.38533  1.000 51.10443 ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.71766  33.15613 13.23650  1.000 52.66395 ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.28068  32.77530 14.37595  1.000 53.56992 ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.12580  31.54826 14.84709  1.000 52.43885 ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 8.02105  33.64575 15.05724  1.000 53.89602 ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.01570 29.85644 9.76295   1.000 42.34570 ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.38496 29.47481 10.09104  1.000 41.75484 ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.28593 30.67771 10.32117  1.000 42.72630 ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.22752 30.59495 11.11613  1.000 44.72254 ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 12.96604 28.60032 8.98504   1.000 40.81627 ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.41095 27.18295 8.91933   1.000 40.26698 ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.01083 26.45042 7.72450   1.000 38.19986 ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.68165 26.44124 10.22368  1.000 40.56404 ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.03877 31.79399 9.64299   1.000 43.95483 ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 13.94035 32.92006 9.83519   1.000 48.70640 ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.63800 33.70702 11.10136  1.000 48.60357 ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.43444 34.57314 11.47718  1.000 51.43232 ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.90956 33.85025 8.62156   1.000 54.47418 ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 15.29441 34.30286 8.21557   1.000 59.55227 ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 16.03841 33.48034 7.64108   1.000 60.59779 ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.64716 35.47065 8.49197   1.000 62.63180 ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.52621 33.42103 11.76985  1.000 47.26494 ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.17918 34.08555 13.01643  1.000 45.85515 ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.44612 33.22356 14.24341  1.000 43.02237 ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.12002 33.64501 15.35481  1.000 44.40251 ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 10.70206 34.50666 13.00145  1.000 48.52713 ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.35674 35.62564 12.02493  0.700 52.70267 ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 10.06381 35.12776 10.62093  0.600 56.04778 ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 10.23494 33.91848 10.36191  0.600 56.90695 ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 9.65381  35.95033 9.77491   0.600 57.24906 ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.03784 32.03993 14.07966  1.000 39.70135 ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.11656 31.04611 15.14725  1.000 39.35484 ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.55229 30.56983 15.31627  1.000 37.22120 ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.25633 30.31807 14.33195  1.000 38.59101 ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.18527 29.84788 14.85830  1.000 39.49830 ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.72137 30.27994 14.93432  1.000 40.02143 ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.46533 28.68723 15.81264  1.000 38.57046 ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.74970  29.17266 14.62808  1.000 41.70929 ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 14.98130 30.43792 16.56844  1.000 35.73514 ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.20308 29.72620 16.91557  1.000 35.18025 ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.82791 28.44493 17.64726  1.000 35.11619 ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.08987 28.48567 18.64101  1.000 36.11509 ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.12392 30.58491 17.78202  1.000 36.68504 ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.33898 27.31981 17.16382  1.000 32.41191 ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 16.01544 26.00417 17.69480  1.000 31.38653 ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.06189 25.54724 18.70278  1.000 30.42950 ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.24639 25.86799 18.58337  1.000 32.43123 ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.92917 24.96541 16.57460  1.000 30.88979 ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.72124 25.10263 15.69112  1.000 32.20655 ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 14.76892 25.89058 14.54972  1.000 32.97512 ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.56017 24.40148 15.96137  1.000 33.33020 ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.66934 26.00863 13.71543  1.000 34.74786 ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.45176 24.50547 15.11766  1.000 33.88962 ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.51158 25.31418 13.99333  1.000 36.05099 ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.60477 24.78722 19.70234  1.000 28.91038 ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.47447 24.13834 20.68036  1.000 30.87024 ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.93856 22.74016 20.93301  1.000 31.23897 ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.72958 22.54728 21.10122  1.000 33.52537 ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.55792 24.90790 22.02061  1.000 35.87349 ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 18.10103 26.31890 21.82645  1.000 42.13343 ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.42125 24.14406 23.02090  1.000 37.92324 ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.01747 27.35482 21.61925  1.000 46.75074 ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.83823 21.77047 20.98907  1.000 30.41903 ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.43705 20.41161 21.27128  1.000 32.52519 ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 18.07711 19.84986 22.52004  1.000 33.32130 ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.28315 19.99642 22.74605  1.000 36.90183 ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.25769 19.21880 23.35242  1.000 33.04885 ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.71572 18.50714 24.53442  1.000 33.91339 ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.46987 17.03231 24.29410  1.000 35.08900 ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.37232 16.64756 23.87521  1.000 36.71229 ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.97085 18.98140 25.79038  1.000 34.79019 ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 17.07322 20.49632 25.90387  1.000 37.81185 ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 17.51880 18.27622 27.01441  1.000 34.76135 ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.27346 21.06120 27.04083  1.000 39.73389 ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.47738 16.20420 24.54332  1.000 35.95991 ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.31781 14.77005 24.33946  1.000 39.83321 ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 18.07624 14.10727 25.68546  1.000 41.83843 ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.93829 14.14307 26.57469  1.000 46.07970 ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.50156 14.14145 23.59480  1.000 42.63485 ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.82870 14.28174 24.27498  1.000 43.76485 ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.34871 13.30761 25.09979  1.000 46.08250 ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.76480 15.25770 24.21039  1.000 43.24651 ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.53612 13.68980 25.53533  1.000 45.70146 ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.81497 14.86687 25.00373  1.000 44.84604 ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.88522 13.54645 25.84936  1.000 42.60804 ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.59614 12.80231 27.06682  1.000 45.49167 ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 17.05476 11.35580 26.96866  1.000 49.41901 ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 17.10190 10.66045 27.98892  1.000 52.13393 ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 15.09800 12.87547 27.41636  1.000 45.51839 ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.30053 12.88118 26.22879  1.000 47.45737 ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.80096 14.13408 28.21843  1.000 45.68059 ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 17.41506 10.90104 25.77833  1.000 50.71281 ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 18.14110 9.66263  25.58662  1.000 51.26790 ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 19.59652 9.92437  25.26193  1.000 51.35227 ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 20.23999 10.79782 25.85303  1.000 50.48101 ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 20.11486 9.17580  24.29762  1.000 53.15638 ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 21.48986 9.33054  23.85326  1.000 53.60075 ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.69023 10.66842 23.14156  1.000 49.04132 ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.74154 11.30396 22.67281  1.000 48.44432 ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.84567 8.21200  22.89038  1.000 56.33930 ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 20.98967 8.21643  21.66967  1.000 59.50615 ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 19.71722 7.69008  21.65920  1.000 60.98923 ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 21.19320 8.74085  20.43806  1.000 61.06701 ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 19.18578 7.86055  20.46259  1.000 62.10090 ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 20.06067 8.49400  19.70232  1.000 62.85899 ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.95747 11.07194 23.03406  1.000 44.44245 ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 23.30991 12.30787 22.34618  1.000 43.21365 ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.72722 12.33484 20.93850  1.000 44.34319 ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.74328 11.33170 20.22347  1.000 47.15204 ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.83210 12.45023 22.28466  1.000 42.43527 ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 25.42005 13.56552 21.42037  1.000 41.99259 ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 25.08934 14.93794 21.98064  1.000 41.19031 ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.91866 13.39518 21.28470  1.000 40.93033 ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 22.19897 13.49418 20.55143  1.000 41.83076 ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.67450 13.68276 19.21816  1.000 38.69429 ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.54744 14.62688 18.41889  1.000 40.93577 ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 23.35622 15.36449 18.98671  1.000 41.84063 ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.41276 14.61118 17.10024  1.000 36.70222 ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 23.13883 15.59657 16.31809  1.000 36.57603 ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.44584 16.93964 16.32647  1.000 38.72419 ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.10647 17.97199 16.16338  1.000 41.62999 ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.35049 15.09380 14.88568  1.000 34.59182 ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.57322 14.28548 14.75366  1.000 31.75544 ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.54162 12.93489 14.98640  1.000 33.50824 ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.78080 14.89056 14.45902  1.000 31.30828 ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.68063 12.19224 14.87989  1.000 37.07251 ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.92420 14.16253 14.37601  1.000 34.21110 ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 26.88092 12.80667 14.57895  1.000 37.14045 ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 21.13970 16.94417 16.55703  1.000 33.33944 ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.39742 18.17353 16.72680  1.000 32.71843 ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 20.06969 18.41220 18.18043  1.000 34.65008 ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.15448 19.53941 18.65917  1.000 37.97394 ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.10966 18.11967 15.92548  1.000 32.13714 ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.37050 17.93318 14.46450  1.000 31.85683 ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.23696 18.77591 13.78999  1.000 29.56167 ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.78262 16.88854 13.77177  1.000 31.08096 ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.48279 18.59874 12.42639  1.000 28.38233 ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 19.03223 16.69717 12.42702  1.000 29.27859 ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.88672 17.55110 11.76663  1.000 27.41881 ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.11084 17.36307 10.40964  1.000 26.46871 ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.69320 17.34615 18.87334  1.000 37.61081 ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.37637 17.40939 20.29516  1.000 39.02521 ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 20.68210 17.16706 21.03212  1.000 39.30480 ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 20.96226 16.07004 21.51172  1.000 40.53995 ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.31685 16.37883 20.65802  1.000 40.70741 ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.51477 18.20800 21.08303  1.000 37.96301 ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.86936 18.06066 21.59020  1.000 40.61462 ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 23.08473 18.68960 22.97222  1.000 43.11851 ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.23076 18.97311 23.32553  1.000 49.77282 ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.88404 18.62762 20.59806  1.000 41.49195 ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.63780 20.09507 20.25239  1.000 45.33367 ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.57140 20.64525 20.58026  1.000 49.15612 ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.52788 20.70172 19.61942  1.000 48.37125 ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 22.02177 18.89858 23.76184  1.000 44.71264 ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 22.10396 19.34989 25.15160  1.000 44.52146 ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.61148 18.26544 26.11255  1.000 41.24966 ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.64581 17.55681 25.82582  1.000 38.97423 ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 21.25377 20.60757 25.39957  1.000 51.16905 ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.78924 21.91191 24.88725  1.000 56.50796 ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.65732 22.41319 23.62273  1.000 58.04562 ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.49012 22.91179 25.64491  1.000 59.91078 ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.25409 23.64957 23.54007  1.000 60.89157 ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.77076 23.97852 24.76763  1.000 61.13375 ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.92073 23.00056 26.97535  1.000 60.46134 ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.46502 25.12038 25.17705  1.000 61.19120 ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.61110 24.13842 27.38025  1.000 59.90486 ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.87380 25.18007 26.48385  1.000 59.78974 ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 22.26934 18.16879 27.34260  1.000 43.20072 ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.82010 17.16345 28.30695  1.000 45.39021 ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.72940 17.72258 29.22228  1.000 45.62788 ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.70761 18.92194 29.50871  1.000 46.91272 ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.98579 16.67983 29.16946  1.000 48.48541 ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 24.17783 16.14160 28.40918  1.000 50.31022 ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 25.29236 15.70819 29.35789  0.800 52.83366 ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.79344 14.87335 30.44519  0.700 53.90962 ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 24.88210 15.18056 31.73249  0.700 55.86508 ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 25.49389 16.28115 32.14171  0.700 55.48696 ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 24.34786 14.36011 32.63286  0.700 56.38413 ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.82849 16.85849 29.70716  1.000 44.24210 ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.75829 17.32770 30.61272  1.000 47.22310 ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 19.25858 17.94168 31.90764  1.000 51.04484 ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.55669 18.77354 32.50684  1.000 51.68270 ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.95033 16.04979 30.88420  1.000 45.40518 ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 18.23281 15.16667 29.69051  1.000 45.43696 ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.67429 15.43495 29.35799  1.000 43.82543 ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.44011 17.54081 32.38033  1.000 52.71796 ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.96462 18.10507 33.61525  1.000 53.45501 ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 21.28856 19.58450 33.47525  1.000 54.19667 ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.45774 20.26917 34.49005  1.000 54.25968 ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 22.20943 17.33732 34.05975  1.000 54.15065 ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.37472 20.08767 32.24721  1.000 53.62216 ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.71650 21.47462 31.97419  1.000 55.12930 ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.50016 22.31180 31.60579  1.000 52.23764 ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.65594 23.46001 31.17381  1.000 50.92614 ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.76894 21.53139 30.86538  1.000 58.48453 ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 24.09156 20.90639 31.28950  1.000 60.31249 ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.88948 20.34195 30.13357  1.000 61.50447 ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 24.38960 19.42858 29.44170  1.000 62.19511 ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 26.02404 20.81235 29.92200  1.000 62.25652 ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.29420 21.76128 31.78018  1.000 51.81555 ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 18.07797 22.48493 31.42508  1.000 51.12044 ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 17.93829 23.77197 32.22408  1.000 49.63208 ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.50402 24.79780 31.68668  1.000 49.16717 ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.85697 21.59236 31.63653  1.000 53.25431 ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.29349 23.74088 33.51191  1.000 51.70892 ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.19982 24.95593 34.31547  1.000 53.42384 ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.18506 26.00809 33.82724  1.000 52.95961 ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.83884 27.19243 33.72828  1.000 52.21050 ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.43101 24.63950 35.79503  1.000 56.52138 ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.30256 23.82230 36.40071  1.000 60.23788 ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 16.19723 23.80708 35.81805  1.000 62.08272 ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.51539 23.19927 37.46161  1.000 62.08577 ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.41610 25.59282 33.50932  1.000 53.09613 ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.37306 26.51847 32.91479  1.000 54.51359 ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.88606 27.01247 31.56344  1.000 55.18655 ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.14247 28.16322 31.18924  1.000 56.52420 ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.73919 25.84557 32.77363  1.000 55.72238 ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.17490 26.15642 30.82670  1.000 54.01400 ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.64007 26.53696 29.52586  1.000 53.53313 ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.57447 27.61846 29.66276  1.000 53.08799 ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.62674 28.64186 28.97174  1.000 52.78846 ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.07652 25.30024 28.82822  1.000 54.06204 ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.90099 25.39953 27.32168  1.000 54.76502 ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.23016 25.74737 26.67566  1.000 55.56862 ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.36264 24.08774 26.77976  1.000 54.78770 ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.59424 27.40097 30.54717  1.000 52.34961 ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.57020 28.41190 30.81749  1.000 51.72172 ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.21785 29.75071 31.13943  1.000 54.62075 ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.82124 30.80139 30.61935  1.000 55.12310 ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.65624 27.95306 31.96770  1.000 49.68498 ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.83049 29.12695 32.49014  1.000 48.98388 ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.76272 26.81068 31.51980  1.000 50.68381 ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.23332 29.72267 32.00181  1.000 56.25134 ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.88801 30.94538 32.45072  1.000 59.08208 ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.50014 31.70555 31.27855  1.000 59.96660 ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 19.17314 32.87303 31.03525  1.000 60.10746 ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.94781 30.58534 33.49199  1.000 60.48308 ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 20.45356 31.73489 34.33373  1.000 61.36763 ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 21.24877 31.20065 35.51514  1.000 62.40391 ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 22.24092 32.22686 36.03055  1.000 62.64442 ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 22.79676 31.83234 37.35351  1.000 63.48346 ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.38219 31.04633 30.52343  1.000 61.14373 ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 21.06290 31.73250 29.43180  1.000 59.85457 ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 20.10027 32.09074 28.30566  1.000 60.27937 ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.30643 33.09212 27.61113  1.000 60.69145 ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.21185 30.86777 28.91823  1.000 61.68074 ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.33143 30.58835 29.92582  1.000 61.39363 ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 24.31692 29.56798 29.37573  1.000 61.82634 ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 24.04751 31.87470 30.30097  1.000 60.20946 ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 19.03871 31.30031 28.12766  1.000 60.45934 ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.06604 31.55939 27.06983  1.000 62.02255 ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.17935 32.75115 27.41078  1.000 65.54195 ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 16.80447 33.52969 26.52477  1.000 66.37206 ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.22049 30.30594 26.84733  1.000 62.13268 ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 16.63085 29.90974 25.49716  1.000 62.11370 ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 17.48997 30.38094 24.34349  1.000 60.50367 ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 16.50111 28.39348 25.46853  1.000 62.50029 ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 16.82415 32.90026 28.68899  1.000 66.40374 ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 15.98064 34.01532 29.10737  1.000 68.18658 ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 16.68667 35.34614 28.88899  1.000 69.92196 ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.13465 36.25995 28.26376  1.000 70.42238 ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 15.58812 33.84561 30.57210  1.000 68.18112 ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 17.90872 35.47437 29.41442  1.000 70.86855 ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 18.74090 36.63728 29.12156  1.000 71.48972 ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 18.80888 36.88931 27.62251  1.000 72.22755 ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 18.54318 38.00051 27.14916  1.000 72.28288 ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.14183 36.42290 29.69723  1.000 71.63754 ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 21.21572 37.36082 29.15851  1.000 72.23053 ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 22.59731 36.87669 29.58783  1.000 72.79774 ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 23.48542 38.01506 30.07255  1.000 72.97914 ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 24.15900 38.73790 28.95954  1.000 72.70619 ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 19.14125 35.85388 26.85840  1.000 72.31841 ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.19767 35.96717 25.41827  1.000 71.82673 ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 20.56028 36.39964 24.92850  1.000 70.34346 ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 21.58286 36.04588 25.52575  1.000 70.70142 ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 20.58387 37.14833 23.82697  1.000 68.61430 ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 21.79561 37.71213 23.23888  1.000 67.37916 ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 22.83589 36.64834 22.89862  1.000 68.06331 ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 23.99491 36.98064 22.61748  1.000 69.40438 ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 22.38337 38.78609 24.16008  1.000 66.56116 ? 94  GLU A CB  1 
ATOM   741  C CG  . GLU A 1 94  ? 21.33490 39.83203 24.53607  1.000 67.97243 ? 94  GLU A CG  1 
ATOM   742  C CD  . GLU A 1 94  ? 21.77094 40.75495 25.65191  1.000 66.96615 ? 94  GLU A CD  1 
ATOM   743  O OE1 . GLU A 1 94  ? 21.87209 40.28982 26.80740  1.000 66.39479 ? 94  GLU A OE1 1 
ATOM   744  O OE2 . GLU A 1 94  ? 22.00639 41.95019 25.37159  1.000 67.19345 ? 94  GLU A OE2 1 
ATOM   745  N N   . TYR A 1 95  ? 22.43849 35.37804 22.92717  1.000 66.76826 ? 95  TYR A N   1 
ATOM   746  C CA  . TYR A 1 95  ? 23.25099 34.26476 22.46819  1.000 64.94797 ? 95  TYR A CA  1 
ATOM   747  C C   . TYR A 1 95  ? 23.57951 34.42728 20.99128  1.000 64.02840 ? 95  TYR A C   1 
ATOM   748  O O   . TYR A 1 95  ? 22.92902 35.18117 20.26170  1.000 64.59939 ? 95  TYR A O   1 
ATOM   749  C CB  . TYR A 1 95  ? 22.49042 32.95707 22.67469  1.000 62.88452 ? 95  TYR A CB  1 
ATOM   750  C CG  . TYR A 1 95  ? 21.04718 33.09828 22.24709  1.000 61.04565 ? 95  TYR A CG  1 
ATOM   751  C CD1 . TYR A 1 95  ? 20.67977 32.96221 20.91535  1.000 60.95813 ? 95  TYR A CD1 1 
ATOM   752  C CD2 . TYR A 1 95  ? 20.05881 33.41422 23.16764  1.000 60.81337 ? 95  TYR A CD2 1 
ATOM   753  C CE1 . TYR A 1 95  ? 19.36824 33.11481 20.51804  1.000 60.85406 ? 95  TYR A CE1 1 
ATOM   754  C CE2 . TYR A 1 95  ? 18.74367 33.56763 22.77852  1.000 60.55872 ? 95  TYR A CE2 1 
ATOM   755  C CZ  . TYR A 1 95  ? 18.40485 33.41864 21.45390  1.000 61.11258 ? 95  TYR A CZ  1 
ATOM   756  O OH  . TYR A 1 95  ? 17.09458 33.56893 21.06662  1.000 62.42933 ? 95  TYR A OH  1 
ATOM   757  N N   . GLN A 1 96  ? 24.58112 33.68379 20.54024  1.000 61.81888 ? 96  GLN A N   1 
ATOM   758  C CA  . GLN A 1 96  ? 24.88265 33.65519 19.12029  1.000 58.68140 ? 96  GLN A CA  1 
ATOM   759  C C   . GLN A 1 96  ? 24.06614 32.56825 18.43164  1.000 53.82808 ? 96  GLN A C   1 
ATOM   760  O O   . GLN A 1 96  ? 23.65946 31.57542 19.04352  1.000 53.33217 ? 96  GLN A O   1 
ATOM   761  C CB  . GLN A 1 96  ? 26.37507 33.43439 18.87052  1.000 61.63551 ? 96  GLN A CB  1 
ATOM   762  C CG  . GLN A 1 96  ? 26.81431 33.89334 17.48572  0.800 64.38501 ? 96  GLN A CG  1 
ATOM   763  C CD  . GLN A 1 96  ? 26.12633 35.18412 17.06732  0.700 65.89771 ? 96  GLN A CD  1 
ATOM   764  O OE1 . GLN A 1 96  ? 25.19708 35.17455 16.25695  0.700 65.51511 ? 96  GLN A OE1 1 
ATOM   765  N NE2 . GLN A 1 96  ? 26.57515 36.30178 17.62872  0.700 66.59389 ? 96  GLN A NE2 1 
ATOM   766  N N   . LYS A 1 97  ? 23.81386 32.77592 17.14718  1.000 47.24161 ? 97  LYS A N   1 
ATOM   767  C CA  . LYS A 1 97  ? 23.05949 31.83171 16.34578  1.000 45.70144 ? 97  LYS A CA  1 
ATOM   768  C C   . LYS A 1 97  ? 23.98114 31.18833 15.32364  1.000 44.37426 ? 97  LYS A C   1 
ATOM   769  O O   . LYS A 1 97  ? 24.89435 31.83556 14.80289  1.000 45.84636 ? 97  LYS A O   1 
ATOM   770  C CB  . LYS A 1 97  ? 21.88026 32.51731 15.65522  1.000 46.09905 ? 97  LYS A CB  1 
ATOM   771  C CG  . LYS A 1 97  ? 20.76974 32.87649 16.62322  1.000 47.33748 ? 97  LYS A CG  1 
ATOM   772  C CD  . LYS A 1 97  ? 19.61939 33.58122 15.94259  1.000 49.63738 ? 97  LYS A CD  1 
ATOM   773  C CE  . LYS A 1 97  ? 19.79700 35.08440 15.98582  1.000 52.06482 ? 97  LYS A CE  1 
ATOM   774  N NZ  . LYS A 1 97  ? 18.57648 35.78674 15.50538  1.000 53.40319 ? 97  LYS A NZ  1 
ATOM   775  N N   . VAL A 1 98  ? 23.75052 29.90155 15.07823  1.000 42.28058 ? 98  VAL A N   1 
ATOM   776  C CA  . VAL A 1 98  ? 24.44452 29.12183 14.06269  1.000 40.30029 ? 98  VAL A CA  1 
ATOM   777  C C   . VAL A 1 98  ? 23.40367 28.64284 13.06401  1.000 36.87650 ? 98  VAL A C   1 
ATOM   778  O O   . VAL A 1 98  ? 22.30443 28.24017 13.45411  1.000 37.59155 ? 98  VAL A O   1 
ATOM   779  C CB  . VAL A 1 98  ? 25.19949 27.93357 14.69120  1.000 43.10351 ? 98  VAL A CB  1 
ATOM   780  C CG1 . VAL A 1 98  ? 25.76785 27.02061 13.62252  1.000 46.14818 ? 98  VAL A CG1 1 
ATOM   781  C CG2 . VAL A 1 98  ? 26.29796 28.44627 15.60534  1.000 44.52193 ? 98  VAL A CG2 1 
ATOM   782  N N   . SER A 1 99  ? 23.73692 28.69591 11.77584  1.000 36.37107 ? 99  SER A N   1 
ATOM   783  C CA  . SER A 1 99  ? 22.78525 28.35615 10.72926  1.000 36.29786 ? 99  SER A CA  1 
ATOM   784  C C   . SER A 1 99  ? 23.32388 27.21801 9.87410   1.000 35.21532 ? 99  SER A C   1 
ATOM   785  O O   . SER A 1 99  ? 24.49126 27.23434 9.47084   1.000 35.95115 ? 99  SER A O   1 
ATOM   786  C CB  . SER A 1 99  ? 22.47136 29.58064 9.87158   1.000 39.97377 ? 99  SER A CB  1 
ATOM   787  O OG  . SER A 1 99  ? 22.08820 30.66234 10.70146  1.000 42.95794 ? 99  SER A OG  1 
ATOM   788  N N   . TYR A 1 100 ? 22.46785 26.22747 9.60776   1.000 32.81552 ? 100 TYR A N   1 
ATOM   789  C CA  . TYR A 1 100 ? 22.79085 25.10183 8.74887   1.000 31.94730 ? 100 TYR A CA  1 
ATOM   790  C C   . TYR A 1 100 ? 22.01041 25.18608 7.44263   1.000 31.15766 ? 100 TYR A C   1 
ATOM   791  O O   . TYR A 1 100 ? 20.89238 25.70950 7.40567   1.000 31.85444 ? 100 TYR A O   1 
ATOM   792  C CB  . TYR A 1 100 ? 22.47755 23.75589 9.40985   1.000 32.49062 ? 100 TYR A CB  1 
ATOM   793  C CG  . TYR A 1 100 ? 23.44752 23.33036 10.48750  1.000 33.64525 ? 100 TYR A CG  1 
ATOM   794  C CD1 . TYR A 1 100 ? 24.53115 24.13141 10.84161  1.000 34.13381 ? 100 TYR A CD1 1 
ATOM   795  C CD2 . TYR A 1 100 ? 23.29455 22.10971 11.13602  1.000 34.23118 ? 100 TYR A CD2 1 
ATOM   796  C CE1 . TYR A 1 100 ? 25.42737 23.73573 11.84368  1.000 36.05251 ? 100 TYR A CE1 1 
ATOM   797  C CE2 . TYR A 1 100 ? 24.18127 21.70907 12.13096  1.000 36.06498 ? 100 TYR A CE2 1 
ATOM   798  C CZ  . TYR A 1 100 ? 25.24840 22.51977 12.46729  1.000 37.96695 ? 100 TYR A CZ  1 
ATOM   799  O OH  . TYR A 1 100 ? 26.13035 22.10755 13.44372  1.000 41.59237 ? 100 TYR A OH  1 
ATOM   800  N N   . PRO A 1 101 ? 22.56994 24.66923 6.35546   1.000 29.30284 ? 101 PRO A N   1 
ATOM   801  C CA  . PRO A 1 101 ? 21.85564 24.69957 5.07811   1.000 28.20350 ? 101 PRO A CA  1 
ATOM   802  C C   . PRO A 1 101 ? 20.71706 23.69351 5.04642   1.000 28.37551 ? 101 PRO A C   1 
ATOM   803  O O   . PRO A 1 101 ? 20.70315 22.69690 5.77087   1.000 29.72694 ? 101 PRO A O   1 
ATOM   804  C CB  . PRO A 1 101 ? 22.93709 24.33145 4.05314   1.000 29.39938 ? 101 PRO A CB  1 
ATOM   805  C CG  . PRO A 1 101 ? 24.24531 24.50075 4.76965   1.000 29.09301 ? 101 PRO A CG  1 
ATOM   806  C CD  . PRO A 1 101 ? 23.95689 24.20597 6.20519   1.000 29.29434 ? 101 PRO A CD  1 
ATOM   807  N N   . LEU A 1 102 ? 19.75917 23.95592 4.15835   1.000 28.70525 ? 102 LEU A N   1 
ATOM   808  C CA  . LEU A 1 102 ? 18.59876 23.09757 3.99127   1.000 26.94607 ? 102 LEU A CA  1 
ATOM   809  C C   . LEU A 1 102 ? 18.48683 22.68213 2.53356   1.000 28.42702 ? 102 LEU A C   1 
ATOM   810  O O   . LEU A 1 102 ? 19.11528 23.26083 1.64420   1.000 30.82327 ? 102 LEU A O   1 
ATOM   811  C CB  . LEU A 1 102 ? 17.30540 23.79333 4.43549   1.000 26.56582 ? 102 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 102 ? 17.29286 24.23106 5.90142   1.000 27.17623 ? 102 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 102 ? 16.06260 25.05846 6.18972   1.000 30.70726 ? 102 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 102 ? 17.35676 23.01492 6.81570   1.000 28.99726 ? 102 LEU A CD2 1 
ATOM   815  N N   . LEU A 1 103 ? 17.66191 21.67377 2.29734   1.000 27.15829 ? 103 LEU A N   1 
ATOM   816  C CA  . LEU A 1 103 ? 17.45108 21.13609 0.95727   1.000 28.02370 ? 103 LEU A CA  1 
ATOM   817  C C   . LEU A 1 103 ? 16.05141 21.48289 0.47884   1.000 30.14170 ? 103 LEU A C   1 
ATOM   818  O O   . LEU A 1 103 ? 15.07149 21.17839 1.16086   1.000 30.46463 ? 103 LEU A O   1 
ATOM   819  C CB  . LEU A 1 103 ? 17.63733 19.62143 0.95871   1.000 27.96252 ? 103 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 103 ? 17.24762 18.91443 -0.33854  1.000 23.80448 ? 103 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 103 ? 18.22568 19.26314 -1.46033  1.000 25.29400 ? 103 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 103 ? 17.19971 17.42665 -0.10771  1.000 25.98692 ? 103 LEU A CD2 1 
ATOM   823  N N   . LYS A 1 104 ? 15.95116 22.08823 -0.70867  1.000 31.02204 ? 104 LYS A N   1 
ATOM   824  C CA  . LYS A 1 104 ? 14.65382 22.33720 -1.32265  1.000 32.60919 ? 104 LYS A CA  1 
ATOM   825  C C   . LYS A 1 104 ? 14.31794 21.20127 -2.28002  1.000 32.77722 ? 104 LYS A C   1 
ATOM   826  O O   . LYS A 1 104 ? 15.13595 20.83148 -3.12595  1.000 32.72640 ? 104 LYS A O   1 
ATOM   827  C CB  . LYS A 1 104 ? 14.63379 23.66757 -2.07205  1.000 36.10895 ? 104 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 104 ? 13.36134 23.85541 -2.88748  0.900 38.72132 ? 104 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 104 ? 13.02137 25.31290 -3.06957  0.800 43.44658 ? 104 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 104 ? 13.14262 25.74557 -4.50846  0.700 44.58607 ? 104 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 104 ? 12.46388 27.05125 -4.73206  0.700 45.54012 ? 104 LYS A NZ  1 
ATOM   832  N N   . THR A 1 105 ? 13.12023 20.64858 -2.13599  1.000 34.23168 ? 105 THR A N   1 
ATOM   833  C CA  . THR A 1 105 ? 12.62528 19.58673 -3.00097  1.000 35.63407 ? 105 THR A CA  1 
ATOM   834  C C   . THR A 1 105 ? 11.38622 20.10654 -3.70397  1.000 34.92843 ? 105 THR A C   1 
ATOM   835  O O   . THR A 1 105 ? 10.43622 20.53219 -3.04526  1.000 36.99673 ? 105 THR A O   1 
ATOM   836  C CB  . THR A 1 105 ? 12.29542 18.32828 -2.19465  1.000 37.83939 ? 105 THR A CB  1 
ATOM   837  O OG1 . THR A 1 105 ? 13.48909 17.83560 -1.57886  1.000 37.65173 ? 105 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 105 ? 11.69912 17.24841 -3.08787  1.000 39.36716 ? 105 THR A CG2 1 
ATOM   839  N N   . THR A 1 106 ? 11.39626 20.09407 -5.03399  1.000 32.81602 ? 106 THR A N   1 
ATOM   840  C CA  . THR A 1 106 ? 10.23112 20.48815 -5.80929  1.000 35.31425 ? 106 THR A CA  1 
ATOM   841  C C   . THR A 1 106 ? 9.69510  19.27118 -6.54487  1.000 36.20778 ? 106 THR A C   1 
ATOM   842  O O   . THR A 1 106 ? 10.44452 18.58023 -7.24330  1.000 36.54606 ? 106 THR A O   1 
ATOM   843  C CB  . THR A 1 106 ? 10.56754 21.60191 -6.80223  1.000 35.60262 ? 106 THR A CB  1 
ATOM   844  O OG1 . THR A 1 106 ? 11.06951 22.73741 -6.09014  1.000 39.04448 ? 106 THR A OG1 1 
ATOM   845  C CG2 . THR A 1 106 ? 9.31658  22.01671 -7.58234  1.000 34.42323 ? 106 THR A CG2 1 
ATOM   846  N N   . VAL A 1 107 ? 8.40561  19.00816 -6.38057  1.000 36.32948 ? 107 VAL A N   1 
ATOM   847  C CA  . VAL A 1 107 ? 7.73903  17.90525 -7.05450  1.000 37.18844 ? 107 VAL A CA  1 
ATOM   848  C C   . VAL A 1 107 ? 6.77920  18.50211 -8.06929  1.000 38.08175 ? 107 VAL A C   1 
ATOM   849  O O   . VAL A 1 107 ? 5.89114  19.28403 -7.71322  1.000 39.21866 ? 107 VAL A O   1 
ATOM   850  C CB  . VAL A 1 107 ? 7.00693  16.98705 -6.06640  1.000 38.78563 ? 107 VAL A CB  1 
ATOM   851  C CG1 . VAL A 1 107 ? 6.42899  15.78716 -6.79521  1.000 38.20259 ? 107 VAL A CG1 1 
ATOM   852  C CG2 . VAL A 1 107 ? 7.95829  16.53546 -4.96805  1.000 41.27360 ? 107 VAL A CG2 1 
ATOM   853  N N   . LYS A 1 108 ? 6.97289  18.15088 -9.33150  1.000 36.17868 ? 108 LYS A N   1 
ATOM   854  C CA  . LYS A 1 108 ? 6.10176  18.58057 -10.40875 1.000 35.41441 ? 108 LYS A CA  1 
ATOM   855  C C   . LYS A 1 108 ? 5.17383  17.43165 -10.77612 1.000 38.97321 ? 108 LYS A C   1 
ATOM   856  O O   . LYS A 1 108 ? 5.63498  16.30200 -10.96547 1.000 38.68466 ? 108 LYS A O   1 
ATOM   857  C CB  . LYS A 1 108 ? 6.93020  19.01137 -11.61825 1.000 37.58701 ? 108 LYS A CB  1 
ATOM   858  N N   . TYR A 1 109 ? 3.86764  17.71027 -10.83162 1.000 42.94163 ? 109 TYR A N   1 
ATOM   859  C CA  . TYR A 1 109 ? 2.90789  16.81504 -11.46553 1.000 51.89047 ? 109 TYR A CA  1 
ATOM   860  C C   . TYR A 1 109 ? 1.94784  17.62645 -12.31352 1.000 57.50820 ? 109 TYR A C   1 
ATOM   861  O O   . TYR A 1 109 ? 1.44753  18.66317 -11.86610 1.000 60.61255 ? 109 TYR A O   1 
ATOM   862  C CB  . TYR A 1 109 ? 2.06736  15.97571 -10.49245 1.000 52.81117 ? 109 TYR A CB  1 
ATOM   863  C CG  . TYR A 1 109 ? 2.21369  16.15335 -8.99910  1.000 50.83140 ? 109 TYR A CG  1 
ATOM   864  C CD1 . TYR A 1 109 ? 2.27617  17.40834 -8.39597  1.000 49.20160 ? 109 TYR A CD1 1 
ATOM   865  C CD2 . TYR A 1 109 ? 2.19346  15.03697 -8.18057  1.000 53.23266 ? 109 TYR A CD2 1 
ATOM   866  C CE1 . TYR A 1 109 ? 2.37933  17.52918 -7.01662  1.000 52.32471 ? 109 TYR A CE1 1 
ATOM   867  C CE2 . TYR A 1 109 ? 2.28051  15.14508 -6.82103  1.000 55.31004 ? 109 TYR A CE2 1 
ATOM   868  C CZ  . TYR A 1 109 ? 2.37838  16.38562 -6.23380  1.000 56.31522 ? 109 TYR A CZ  1 
ATOM   869  O OH  . TYR A 1 109 ? 2.46970  16.45704 -4.85780  1.000 58.37232 ? 109 TYR A OH  1 
ATOM   870  N N   . GLY A 1 110 ? 1.67231  17.13279 -13.52022 1.000 59.41433 ? 110 GLY A N   1 
ATOM   871  C CA  . GLY A 1 110 ? 0.64819  17.70548 -14.37547 1.000 58.60326 ? 110 GLY A CA  1 
ATOM   872  C C   . GLY A 1 110 ? -0.66347 16.94448 -14.29745 1.000 58.98652 ? 110 GLY A C   1 
ATOM   873  O O   . GLY A 1 110 ? -1.56740 17.14488 -15.11434 1.000 58.14737 ? 110 GLY A O   1 
ATOM   874  N N   . LYS A 1 114 ? 1.31568  21.35929 -11.92676 1.000 58.23739 ? 114 LYS A N   1 
ATOM   875  C CA  . LYS A 1 114 ? 1.45093  21.96056 -10.60518 1.000 56.31481 ? 114 LYS A CA  1 
ATOM   876  C C   . LYS A 1 114 ? 2.76208  21.58035 -9.95216  1.000 55.12423 ? 114 LYS A C   1 
ATOM   877  O O   . LYS A 1 114 ? 3.48095  20.70240 -10.42936 1.000 56.04602 ? 114 LYS A O   1 
ATOM   878  C CB  . LYS A 1 114 ? 0.30804  21.53812 -9.68778  1.000 57.38386 ? 114 LYS A CB  1 
ATOM   879  C CG  . LYS A 1 114 ? -1.03407 22.09596 -10.04818 1.000 59.54562 ? 114 LYS A CG  1 
ATOM   880  C CD  . LYS A 1 114 ? -2.08611 21.52513 -9.12234  1.000 61.15245 ? 114 LYS A CD  1 
ATOM   881  C CE  . LYS A 1 114 ? -3.42432 21.40589 -9.82552  1.000 61.85638 ? 114 LYS A CE  1 
ATOM   882  N NZ  . LYS A 1 114 ? -4.44338 20.77120 -8.94740  1.000 62.48208 ? 114 LYS A NZ  1 
ATOM   883  N N   . GLU A 1 115 ? 3.05245  22.23304 -8.83367  1.000 51.93372 ? 115 GLU A N   1 
ATOM   884  C CA  . GLU A 1 115 ? 4.27295  21.97206 -8.09498  1.000 50.29141 ? 115 GLU A CA  1 
ATOM   885  C C   . GLU A 1 115 ? 3.99696  22.02079 -6.60228  1.000 50.12755 ? 115 GLU A C   1 
ATOM   886  O O   . GLU A 1 115 ? 3.20827  22.84317 -6.12818  1.000 52.64400 ? 115 GLU A O   1 
ATOM   887  C CB  . GLU A 1 115 ? 5.36456  22.97946 -8.44936  1.000 52.04230 ? 115 GLU A CB  1 
ATOM   888  C CG  . GLU A 1 115 ? 5.98222  22.76595 -9.81435  1.000 56.54608 ? 115 GLU A CG  1 
ATOM   889  C CD  . GLU A 1 115 ? 7.04876  23.79176 -10.12292 1.000 60.68228 ? 115 GLU A CD  1 
ATOM   890  O OE1 . GLU A 1 115 ? 7.19007  24.74764 -9.33073  1.000 63.64479 ? 115 GLU A OE1 1 
ATOM   891  O OE2 . GLU A 1 115 ? 7.74327  23.64313 -11.15185 1.000 60.88291 ? 115 GLU A OE2 1 
ATOM   892  N N   . ALA A 1 116 ? 4.64220  21.12373 -5.87473  1.000 47.77203 ? 116 ALA A N   1 
ATOM   893  C CA  . ALA A 1 116 ? 4.72233  21.18891 -4.42511  1.000 46.70277 ? 116 ALA A CA  1 
ATOM   894  C C   . ALA A 1 116 ? 6.18662  21.34214 -4.05362  1.000 45.09930 ? 116 ALA A C   1 
ATOM   895  O O   . ALA A 1 116 ? 7.05224  20.71504 -4.66929  1.000 44.77436 ? 116 ALA A O   1 
ATOM   896  C CB  . ALA A 1 116 ? 4.13813  19.93462 -3.77198  1.000 48.02649 ? 116 ALA A CB  1 
ATOM   897  N N   . THR A 1 117 ? 6.46947  22.18349 -3.06343  1.000 45.44691 ? 117 THR A N   1 
ATOM   898  C CA  . THR A 1 117 ? 7.83018  22.34781 -2.57621  1.000 43.31169 ? 117 THR A CA  1 
ATOM   899  C C   . THR A 1 117 ? 7.91107  21.95294 -1.11078  1.000 41.73533 ? 117 THR A C   1 
ATOM   900  O O   . THR A 1 117 ? 6.96790  22.15470 -0.34102  1.000 42.95004 ? 117 THR A O   1 
ATOM   901  C CB  . THR A 1 117 ? 8.34180  23.78583 -2.74277  1.000 48.26726 ? 117 THR A CB  1 
ATOM   902  O OG1 . THR A 1 117 ? 7.53241  24.68354 -1.97216  1.000 53.58312 ? 117 THR A OG1 1 
ATOM   903  C CG2 . THR A 1 117 ? 8.32208  24.19717 -4.20301  1.000 47.75325 ? 117 THR A CG2 1 
ATOM   904  N N   . TYR A 1 118 ? 9.05825  21.38891 -0.74367  1.000 39.73110 ? 118 TYR A N   1 
ATOM   905  C CA  . TYR A 1 118 ? 9.31256  20.91019 0.60484   1.000 38.81386 ? 118 TYR A CA  1 
ATOM   906  C C   . TYR A 1 118 ? 10.71137 21.32978 1.02072   1.000 38.83344 ? 118 TYR A C   1 
ATOM   907  O O   . TYR A 1 118 ? 11.60205 21.50321 0.18552   1.000 39.80307 ? 118 TYR A O   1 
ATOM   908  C CB  . TYR A 1 118 ? 9.19175  19.38389 0.70262   1.000 39.98567 ? 118 TYR A CB  1 
ATOM   909  C CG  . TYR A 1 118 ? 7.87471  18.83532 0.22431   1.000 40.93075 ? 118 TYR A CG  1 
ATOM   910  C CD1 . TYR A 1 118 ? 7.63869  18.61846 -1.12868  1.000 43.99440 ? 118 TYR A CD1 1 
ATOM   911  C CD2 . TYR A 1 118 ? 6.85680  18.54121 1.12389   1.000 42.88440 ? 118 TYR A CD2 1 
ATOM   912  C CE1 . TYR A 1 118 ? 6.42963  18.12457 -1.56784  1.000 45.63866 ? 118 TYR A CE1 1 
ATOM   913  C CE2 . TYR A 1 118 ? 5.65026  18.04555 0.69624   1.000 45.64648 ? 118 TYR A CE2 1 
ATOM   914  C CZ  . TYR A 1 118 ? 5.44046  17.83752 -0.65318  1.000 46.11904 ? 118 TYR A CZ  1 
ATOM   915  O OH  . TYR A 1 118 ? 4.23532  17.34027 -1.09241  1.000 50.32980 ? 118 TYR A OH  1 
ATOM   916  N N   . LEU A 1 119 ? 10.90165 21.47551 2.32538   1.000 37.38471 ? 119 LEU A N   1 
ATOM   917  C CA  . LEU A 1 119 ? 12.20716 21.75671 2.89834   1.000 35.40928 ? 119 LEU A CA  1 
ATOM   918  C C   . LEU A 1 119 ? 12.62874 20.55856 3.73119   1.000 30.76231 ? 119 LEU A C   1 
ATOM   919  O O   . LEU A 1 119 ? 11.81941 20.01152 4.48554   1.000 31.45240 ? 119 LEU A O   1 
ATOM   920  C CB  . LEU A 1 119 ? 12.15428 23.01223 3.76908   1.000 39.16828 ? 119 LEU A CB  1 
ATOM   921  C CG  . LEU A 1 119 ? 13.10704 24.17273 3.50148   1.000 42.07522 ? 119 LEU A CG  1 
ATOM   922  C CD1 . LEU A 1 119 ? 13.19662 24.49896 2.02275   1.000 43.29643 ? 119 LEU A CD1 1 
ATOM   923  C CD2 . LEU A 1 119 ? 12.63847 25.38800 4.29815   1.000 42.23695 ? 119 LEU A CD2 1 
ATOM   924  N N   . ALA A 1 120 ? 13.88345 20.14385 3.59082   1.000 28.96668 ? 120 ALA A N   1 
ATOM   925  C CA  . ALA A 1 120 ? 14.41772 19.02721 4.36068   1.000 26.79652 ? 120 ALA A CA  1 
ATOM   926  C C   . ALA A 1 120 ? 15.60743 19.47244 5.19960   1.000 26.26775 ? 120 ALA A C   1 
ATOM   927  O O   . ALA A 1 120 ? 16.45935 20.23283 4.73804   1.000 27.02991 ? 120 ALA A O   1 
ATOM   928  C CB  . ALA A 1 120 ? 14.84381 17.87411 3.45489   1.000 27.94211 ? 120 ALA A CB  1 
ATOM   929  N N   . LEU A 1 121 ? 15.64043 19.01188 6.45359   1.000 25.34913 ? 121 LEU A N   1 
ATOM   930  C CA  . LEU A 1 121 ? 16.78644 19.22445 7.32288   1.000 25.57725 ? 121 LEU A CA  1 
ATOM   931  C C   . LEU A 1 121 ? 17.76359 18.06016 7.27747   1.000 25.62992 ? 121 LEU A C   1 
ATOM   932  O O   . LEU A 1 121 ? 18.97794 18.25548 7.45016   1.000 27.08208 ? 121 LEU A O   1 
ATOM   933  C CB  . LEU A 1 121 ? 16.29924 19.44520 8.76444   1.000 26.45304 ? 121 LEU A CB  1 
ATOM   934  C CG  . LEU A 1 121 ? 17.37444 19.49547 9.85067   1.000 26.87635 ? 121 LEU A CG  1 
ATOM   935  C CD1 . LEU A 1 121 ? 18.35572 20.62241 9.62100   1.000 26.48260 ? 121 LEU A CD1 1 
ATOM   936  C CD2 . LEU A 1 121 ? 16.72543 19.62958 11.23140  1.000 26.86365 ? 121 LEU A CD2 1 
ATOM   937  N N   . ASN A 1 122 ? 17.26086 16.84963 7.06165   1.000 23.94628 ? 122 ASN A N   1 
ATOM   938  C CA  . ASN A 1 122 ? 18.12098 15.68927 6.89638   1.000 23.34215 ? 122 ASN A CA  1 
ATOM   939  C C   . ASN A 1 122 ? 18.27167 15.34437 5.42124   1.000 22.86603 ? 122 ASN A C   1 
ATOM   940  O O   . ASN A 1 122 ? 19.36223 15.45227 4.85541   1.000 23.24986 ? 122 ASN A O   1 
ATOM   941  C CB  . ASN A 1 122 ? 17.55001 14.48050 7.61758   1.000 23.30156 ? 122 ASN A CB  1 
ATOM   942  C CG  . ASN A 1 122 ? 18.09225 14.31234 9.01304   1.000 24.27253 ? 122 ASN A CG  1 
ATOM   943  O OD1 . ASN A 1 122 ? 18.93178 15.08142 9.48007   1.000 26.60096 ? 122 ASN A OD1 1 
ATOM   944  N ND2 . ASN A 1 122 ? 17.64608 13.26333 9.66456   1.000 23.74997 ? 122 ASN A ND2 1 
ATOM   945  N N   . GLU A 1 123 ? 17.19339 14.88704 4.80257   1.000 22.46937 ? 123 GLU A N   1 
ATOM   946  C CA  . GLU A 1 123 ? 17.31525 14.44085 3.41609   1.000 23.23754 ? 123 GLU A CA  1 
ATOM   947  C C   . GLU A 1 123 ? 15.93953 14.29386 2.81167   1.000 23.58054 ? 123 GLU A C   1 
ATOM   948  O O   . GLU A 1 123 ? 14.92085 14.28109 3.50377   1.000 26.83697 ? 123 GLU A O   1 
ATOM   949  C CB  . GLU A 1 123 ? 18.04868 13.10070 3.29291   1.000 24.28116 ? 123 GLU A CB  1 
ATOM   950  C CG  . GLU A 1 123 ? 17.20966 11.89262 3.71916   1.000 24.21087 ? 123 GLU A CG  1 
ATOM   951  C CD  . GLU A 1 123 ? 17.06062 11.79816 5.22601   1.000 24.00015 ? 123 GLU A CD  1 
ATOM   952  O OE1 . GLU A 1 123 ? 18.10451 11.76958 5.91210   1.000 24.48749 ? 123 GLU A OE1 1 
ATOM   953  O OE2 . GLU A 1 123 ? 15.90404 11.76265 5.70813   1.000 27.19327 ? 123 GLU A OE2 1 
ATOM   954  N N   . SER A 1 124 ? 15.93454 14.14816 1.49160   1.000 22.59473 ? 124 SER A N   1 
ATOM   955  C CA  . SER A 1 124 ? 14.76794 13.71055 0.74629   1.000 25.29499 ? 124 SER A CA  1 
ATOM   956  C C   . SER A 1 124 ? 15.16587 12.48921 -0.07123  1.000 25.55920 ? 124 SER A C   1 
ATOM   957  O O   . SER A 1 124 ? 16.26697 12.44435 -0.62669  1.000 26.21594 ? 124 SER A O   1 
ATOM   958  C CB  . SER A 1 124 ? 14.24410 14.84438 -0.14763  1.000 27.74655 ? 124 SER A CB  1 
ATOM   959  O OG  . SER A 1 124 ? 13.20072 14.41236 -1.00061  1.000 29.76144 ? 124 SER A OG  1 
ATOM   960  N N   . THR A 1 125 ? 14.30474 11.47307 -0.09890  1.000 23.73187 ? 125 THR A N   1 
ATOM   961  C CA  . THR A 1 125 ? 14.59497 10.26744 -0.87005  1.000 25.72251 ? 125 THR A CA  1 
ATOM   962  C C   . THR A 1 125 ? 13.44786 9.96167  -1.81889  1.000 27.15641 ? 125 THR A C   1 
ATOM   963  O O   . THR A 1 125 ? 12.30812 10.38407 -1.61303  1.000 26.93228 ? 125 THR A O   1 
ATOM   964  C CB  . THR A 1 125 ? 14.84453 9.03960  0.01784   1.000 26.30276 ? 125 THR A CB  1 
ATOM   965  O OG1 . THR A 1 125 ? 13.59758 8.56644  0.53553   1.000 31.34861 ? 125 THR A OG1 1 
ATOM   966  C CG2 . THR A 1 125 ? 15.78536 9.38009  1.18518   1.000 26.92662 ? 125 THR A CG2 1 
ATOM   967  N N   . VAL A 1 126 ? 13.78262 9.22787  -2.88155  1.000 28.11060 ? 126 VAL A N   1 
ATOM   968  C CA  . VAL A 1 126 ? 12.82288 8.76119  -3.87318  1.000 26.58978 ? 126 VAL A CA  1 
ATOM   969  C C   . VAL A 1 126 ? 12.99255 7.25612  -4.03115  1.000 25.88356 ? 126 VAL A C   1 
ATOM   970  O O   . VAL A 1 126 ? 14.10769 6.78271  -4.27293  1.000 27.56067 ? 126 VAL A O   1 
ATOM   971  C CB  . VAL A 1 126 ? 13.02276 9.46698  -5.22769  1.000 28.67101 ? 126 VAL A CB  1 
ATOM   972  C CG1 . VAL A 1 126 ? 11.90218 9.10391  -6.18299  1.000 28.63301 ? 126 VAL A CG1 1 
ATOM   973  C CG2 . VAL A 1 126 ? 13.08895 10.98017 -5.04396  1.000 32.81313 ? 126 VAL A CG2 1 
ATOM   974  N N   . LYS A 1 127 ? 11.89245 6.51329  -3.89656  1.000 29.24267 ? 127 LYS A N   1 
ATOM   975  C CA  . LYS A 1 127 ? 11.81679 5.07222  -4.14235  1.000 36.74457 ? 127 LYS A CA  1 
ATOM   976  C C   . LYS A 1 127 ? 10.57212 4.77871  -4.98078  1.000 41.41977 ? 127 LYS A C   1 
ATOM   977  O O   . LYS A 1 127 ? 9.73458  5.65455  -5.20478  1.000 39.56294 ? 127 LYS A O   1 
ATOM   978  C CB  . LYS A 1 127 ? 11.77009 4.27118  -2.82675  1.000 39.93761 ? 127 LYS A CB  1 
ATOM   979  C CG  . LYS A 1 127 ? 12.87297 4.61004  -1.81828  1.000 39.98717 ? 127 LYS A CG  1 
ATOM   980  C CD  . LYS A 1 127 ? 12.70963 3.82483  -0.51149  1.000 42.60248 ? 127 LYS A CD  1 
ATOM   981  C CE  . LYS A 1 127 ? 13.80006 4.18635  0.50912   1.000 42.09104 ? 127 LYS A CE  1 
ATOM   982  N NZ  . LYS A 1 127 ? 13.61407 3.59747  1.88565   1.000 42.65287 ? 127 LYS A NZ  1 
ATOM   983  N N   . SER A 1 128 ? 10.43733 3.53465  -5.45860  1.000 44.59160 ? 128 SER A N   1 
ATOM   984  C CA  . SER A 1 128 ? 9.27645  3.16002  -6.25774  1.000 51.00439 ? 128 SER A CA  1 
ATOM   985  C C   . SER A 1 128 ? 8.23043  2.43047  -5.42693  1.000 53.07936 ? 128 SER A C   1 
ATOM   986  O O   . SER A 1 128 ? 8.41771  2.13709  -4.24614  1.000 54.77800 ? 128 SER A O   1 
ATOM   987  C CB  . SER A 1 128 ? 9.65909  2.25848  -7.42551  1.000 53.23747 ? 128 SER A CB  1 
ATOM   988  O OG  . SER A 1 128 ? 9.97615  0.94675  -6.98533  1.000 53.97779 ? 128 SER A OG  1 
ATOM   989  N N   . SER A 1 129 ? 7.11885  2.09988  -6.08855  1.000 57.48905 ? 129 SER A N   1 
ATOM   990  C CA  . SER A 1 129 ? 6.10316  1.21085  -5.52725  1.000 60.49190 ? 129 SER A CA  1 
ATOM   991  C C   . SER A 1 129 ? 6.53838  -0.25175 -5.67914  1.000 62.76213 ? 129 SER A C   1 
ATOM   992  O O   . SER A 1 129 ? 5.90451  -1.05976 -6.35841  1.000 65.37463 ? 129 SER A O   1 
ATOM   993  C CB  . SER A 1 129 ? 4.75389  1.45666  -6.19340  1.000 61.02888 ? 129 SER A CB  1 
ATOM   994  O OG  . SER A 1 129 ? 4.73837  2.67455  -6.92209  1.000 61.30308 ? 129 SER A OG  1 
ATOM   995  N N   . GLY A 1 130 ? 7.65988  -0.58090 -5.03544  1.000 61.73787 ? 130 GLY A N   1 
ATOM   996  C CA  . GLY A 1 130 ? 8.14076  -1.95202 -4.99190  1.000 59.41663 ? 130 GLY A CA  1 
ATOM   997  C C   . GLY A 1 130 ? 9.08905  -2.34692 -6.11005  1.000 58.13638 ? 130 GLY A C   1 
ATOM   998  O O   . GLY A 1 130 ? 8.90651  -1.94874 -7.26400  1.000 59.55157 ? 130 GLY A O   1 
ATOM   999  N N   . GLY A 1 131 ? 10.10177 -3.14626 -5.77860  1.000 53.81522 ? 131 GLY A N   1 
ATOM   1000 C CA  . GLY A 1 131 ? 11.09411 -3.56261 -6.74133  1.000 50.54803 ? 131 GLY A CA  1 
ATOM   1001 C C   . GLY A 1 131 ? 11.99083 -2.40931 -7.14015  1.000 45.91869 ? 131 GLY A C   1 
ATOM   1002 O O   . GLY A 1 131 ? 11.99468 -1.35215 -6.50092  1.000 44.69342 ? 131 GLY A O   1 
ATOM   1003 N N   . PRO A 1 132 ? 12.77249 -2.58285 -8.20166  1.000 44.45394 ? 132 PRO A N   1 
ATOM   1004 C CA  . PRO A 1 132 ? 13.58055 -1.46696 -8.69813  1.000 41.56564 ? 132 PRO A CA  1 
ATOM   1005 C C   . PRO A 1 132 ? 12.76445 -0.53729 -9.58470  1.000 44.44790 ? 132 PRO A C   1 
ATOM   1006 O O   . PRO A 1 132 ? 11.82236 -0.94740 -10.26819 1.000 49.66599 ? 132 PRO A O   1 
ATOM   1007 C CB  . PRO A 1 132 ? 14.68332 -2.16559 -9.49893  1.000 41.76824 ? 132 PRO A CB  1 
ATOM   1008 C CG  . PRO A 1 132 ? 13.99776 -3.39691 -10.04083 1.000 42.49029 ? 132 PRO A CG  1 
ATOM   1009 C CD  . PRO A 1 132 ? 12.98245 -3.81444 -8.99018  1.000 44.18898 ? 132 PRO A CD  1 
ATOM   1010 N N   . PHE A 1 133 ? 13.12796 0.73787  -9.54354  1.000 39.08098 ? 133 PHE A N   1 
ATOM   1011 C CA  . PHE A 1 133 ? 12.56251 1.74172  -10.42060 1.000 35.05093 ? 133 PHE A CA  1 
ATOM   1012 C C   . PHE A 1 133 ? 13.67273 2.33709  -11.25748 1.000 29.55656 ? 133 PHE A C   1 
ATOM   1013 O O   . PHE A 1 133 ? 14.85487 2.08438  -11.03586 1.000 28.61855 ? 133 PHE A O   1 
ATOM   1014 C CB  . PHE A 1 133 ? 11.81446 2.84800  -9.66078  1.000 40.24072 ? 133 PHE A CB  1 
ATOM   1015 C CG  . PHE A 1 133 ? 12.69415 3.90602  -9.00546  1.000 45.58022 ? 133 PHE A CG  1 
ATOM   1016 C CD1 . PHE A 1 133 ? 13.99515 3.65875  -8.61110  1.000 45.80752 ? 133 PHE A CD1 1 
ATOM   1017 C CD2 . PHE A 1 133 ? 12.17361 5.16389  -8.76513  1.000 46.65060 ? 133 PHE A CD2 1 
ATOM   1018 C CE1 . PHE A 1 133 ? 14.75736 4.65612  -8.03586  1.000 47.05823 ? 133 PHE A CE1 1 
ATOM   1019 C CE2 . PHE A 1 133 ? 12.92930 6.14882  -8.16693  1.000 46.36583 ? 133 PHE A CE2 1 
ATOM   1020 C CZ  . PHE A 1 133 ? 14.21772 5.90013  -7.82103  1.000 49.04121 ? 133 PHE A CZ  1 
ATOM   1021 N N   . VAL A 1 134 ? 13.25993 3.14762  -12.21721 1.000 30.33257 ? 134 VAL A N   1 
ATOM   1022 C CA  . VAL A 1 134 ? 14.15091 3.72508  -13.20313 1.000 30.45819 ? 134 VAL A CA  1 
ATOM   1023 C C   . VAL A 1 134 ? 13.89461 5.21670  -13.23294 1.000 29.68910 ? 134 VAL A C   1 
ATOM   1024 O O   . VAL A 1 134 ? 12.74442 5.65122  -13.36593 1.000 33.42792 ? 134 VAL A O   1 
ATOM   1025 C CB  . VAL A 1 134 ? 13.92079 3.11708  -14.59680 1.000 31.44220 ? 134 VAL A CB  1 
ATOM   1026 C CG1 . VAL A 1 134 ? 14.94086 3.65345  -15.56879 1.000 30.94206 ? 134 VAL A CG1 1 
ATOM   1027 C CG2 . VAL A 1 134 ? 13.96509 1.60744  -14.52145 1.000 34.16030 ? 134 VAL A CG2 1 
ATOM   1028 N N   . VAL A 1 135 ? 14.95325 6.00160  -13.11331 1.000 28.88230 ? 135 VAL A N   1 
ATOM   1029 C CA  . VAL A 1 135 ? 14.81650 7.44523  -13.20809 1.000 31.43872 ? 135 VAL A CA  1 
ATOM   1030 C C   . VAL A 1 135 ? 15.99502 7.98832  -14.00208 1.000 30.48027 ? 135 VAL A C   1 
ATOM   1031 O O   . VAL A 1 135 ? 17.12195 7.49649  -13.87960 1.000 31.14521 ? 135 VAL A O   1 
ATOM   1032 C CB  . VAL A 1 135 ? 14.71465 8.08125  -11.80882 1.000 37.75777 ? 135 VAL A CB  1 
ATOM   1033 C CG1 . VAL A 1 135 ? 16.02964 8.02123  -11.11380 1.000 35.46564 ? 135 VAL A CG1 1 
ATOM   1034 C CG2 . VAL A 1 135 ? 14.22629 9.49516  -11.89615 1.000 43.09199 ? 135 VAL A CG2 1 
ATOM   1035 N N   . ASP A 1 136 ? 15.72658 8.97615  -14.84834 1.000 29.35183 ? 136 ASP A N   1 
ATOM   1036 C CA  . ASP A 1 136 ? 16.80340 9.71987  -15.48175 1.000 29.21474 ? 136 ASP A CA  1 
ATOM   1037 C C   . ASP A 1 136 ? 17.25509 10.82837 -14.54737 1.000 27.57400 ? 136 ASP A C   1 
ATOM   1038 O O   . ASP A 1 136 ? 16.42869 11.55520 -13.98841 1.000 29.51802 ? 136 ASP A O   1 
ATOM   1039 C CB  . ASP A 1 136 ? 16.35900 10.29402 -16.82413 1.000 33.64949 ? 136 ASP A CB  1 
ATOM   1040 C CG  . ASP A 1 136 ? 16.40122 9.26518  -17.92691 1.000 38.89047 ? 136 ASP A CG  1 
ATOM   1041 O OD1 . ASP A 1 136 ? 17.22575 8.33553  -17.83012 1.000 40.84468 ? 136 ASP A OD1 1 
ATOM   1042 O OD2 . ASP A 1 136 ? 15.61223 9.37171  -18.88427 1.000 41.74451 ? 136 ASP A OD2 1 
ATOM   1043 N N   . VAL A 1 137 ? 18.56356 10.92961 -14.35219 1.000 25.70972 ? 137 VAL A N   1 
ATOM   1044 C CA  . VAL A 1 137 ? 19.16044 11.93545 -13.48333 1.000 25.02529 ? 137 VAL A CA  1 
ATOM   1045 C C   . VAL A 1 137 ? 19.72301 13.03223 -14.37356 1.000 25.92523 ? 137 VAL A C   1 
ATOM   1046 O O   . VAL A 1 137 ? 20.60114 12.77448 -15.20421 1.000 27.06440 ? 137 VAL A O   1 
ATOM   1047 C CB  . VAL A 1 137 ? 20.25047 11.32245 -12.59228 1.000 24.07350 ? 137 VAL A CB  1 
ATOM   1048 C CG1 . VAL A 1 137 ? 20.85529 12.38164 -11.66567 1.000 25.61103 ? 137 VAL A CG1 1 
ATOM   1049 C CG2 . VAL A 1 137 ? 19.68251 10.14808 -11.81116 1.000 27.51059 ? 137 VAL A CG2 1 
ATOM   1050 N N   . VAL A 1 138 ? 19.20410 14.24693 -14.21659 1.000 25.25702 ? 138 VAL A N   1 
ATOM   1051 C CA  . VAL A 1 138 ? 19.56638 15.38841 -15.04903 1.000 26.06727 ? 138 VAL A CA  1 
ATOM   1052 C C   . VAL A 1 138 ? 20.17730 16.45025 -14.14771 1.000 26.80333 ? 138 VAL A C   1 
ATOM   1053 O O   . VAL A 1 138 ? 19.53810 16.90108 -13.18734 1.000 30.68877 ? 138 VAL A O   1 
ATOM   1054 C CB  . VAL A 1 138 ? 18.34853 15.94141 -15.80279 1.000 29.32758 ? 138 VAL A CB  1 
ATOM   1055 C CG1 . VAL A 1 138 ? 18.72618 17.18206 -16.57067 1.000 30.20010 ? 138 VAL A CG1 1 
ATOM   1056 C CG2 . VAL A 1 138 ? 17.77075 14.87833 -16.72330 1.000 29.73012 ? 138 VAL A CG2 1 
ATOM   1057 N N   . ILE A 1 139 ? 21.41187 16.84145 -14.44146 1.000 24.41566 ? 139 ILE A N   1 
ATOM   1058 C CA  . ILE A 1 139 ? 22.13849 17.81061 -13.62771 1.000 24.38404 ? 139 ILE A CA  1 
ATOM   1059 C C   . ILE A 1 139 ? 22.28214 19.08342 -14.43818 1.000 26.04899 ? 139 ILE A C   1 
ATOM   1060 O O   . ILE A 1 139 ? 22.94490 19.07838 -15.47916 1.000 26.05473 ? 139 ILE A O   1 
ATOM   1061 C CB  . ILE A 1 139 ? 23.51658 17.28370 -13.20640 1.000 24.86294 ? 139 ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 139 ? 23.39199 15.95856 -12.44635 1.000 24.44288 ? 139 ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 139 ? 24.24332 18.31984 -12.34993 1.000 27.04328 ? 139 ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 139 ? 24.74548 15.30668 -12.17856 1.000 27.01059 ? 139 ILE A CD1 1 
ATOM   1065 N N   . ASN A 1 140 ? 21.67731 20.17342 -13.96780 1.000 26.23341 ? 140 ASN A N   1 
ATOM   1066 C CA  . ASN A 1 140 ? 21.74690 21.45531 -14.67165 1.000 27.09916 ? 140 ASN A CA  1 
ATOM   1067 C C   . ASN A 1 140 ? 21.39224 21.28836 -16.14426 1.000 29.21601 ? 140 ASN A C   1 
ATOM   1068 O O   . ASN A 1 140 ? 22.09413 21.77260 -17.03531 1.000 29.91514 ? 140 ASN A O   1 
ATOM   1069 C CB  . ASN A 1 140 ? 23.12721 22.08803 -14.53543 1.000 29.17214 ? 140 ASN A CB  1 
ATOM   1070 C CG  . ASN A 1 140 ? 23.48000 22.36983 -13.11906 1.000 30.11550 ? 140 ASN A CG  1 
ATOM   1071 O OD1 . ASN A 1 140 ? 22.61993 22.75453 -12.33438 1.000 29.93791 ? 140 ASN A OD1 1 
ATOM   1072 N ND2 . ASN A 1 140 ? 24.74386 22.17382 -12.77290 1.000 30.73705 ? 140 ASN A ND2 1 
ATOM   1073 N N   . ASP A 1 141 ? 20.32060 20.54309 -16.39038 1.000 31.34196 ? 141 ASP A N   1 
ATOM   1074 C CA  . ASP A 1 141 ? 19.74469 20.32166 -17.71754 1.000 34.61054 ? 141 ASP A CA  1 
ATOM   1075 C C   . ASP A 1 141 ? 20.56775 19.40107 -18.60716 1.000 36.51673 ? 141 ASP A C   1 
ATOM   1076 O O   . ASP A 1 141 ? 20.24084 19.26801 -19.80620 1.000 39.60117 ? 141 ASP A O   1 
ATOM   1077 C CB  . ASP A 1 141 ? 19.50221 21.64201 -18.45838 1.000 39.57718 ? 141 ASP A CB  1 
ATOM   1078 C CG  . ASP A 1 141 ? 18.56734 22.56494 -17.71104 1.000 47.00175 ? 141 ASP A CG  1 
ATOM   1079 O OD1 . ASP A 1 141 ? 17.68512 22.06018 -16.98492 1.000 48.96603 ? 141 ASP A OD1 1 
ATOM   1080 O OD2 . ASP A 1 141 ? 18.71271 23.79732 -17.85669 1.000 51.18869 ? 141 ASP A OD2 1 
ATOM   1081 N N   . ILE A 1 142 ? 21.60982 18.74452 -18.09705 1.000 33.95542 ? 142 ILE A N   1 
ATOM   1082 C CA  . ILE A 1 142 ? 22.33758 17.75782 -18.89418 1.000 35.37065 ? 142 ILE A CA  1 
ATOM   1083 C C   . ILE A 1 142 ? 22.09271 16.36817 -18.32201 1.000 28.07028 ? 142 ILE A C   1 
ATOM   1084 O O   . ILE A 1 142 ? 22.21741 16.14415 -17.10616 1.000 27.37451 ? 142 ILE A O   1 
ATOM   1085 C CB  . ILE A 1 142 ? 23.84091 18.07912 -19.02067 1.000 42.00105 ? 142 ILE A CB  1 
ATOM   1086 C CG1 . ILE A 1 142 ? 24.59883 17.92027 -17.70482 0.700 43.57823 ? 142 ILE A CG1 1 
ATOM   1087 C CG2 . ILE A 1 142 ? 24.05432 19.47839 -19.60476 0.600 42.40666 ? 142 ILE A CG2 1 
ATOM   1088 C CD1 . ILE A 1 142 ? 25.36363 16.61132 -17.57872 0.600 47.36007 ? 142 ILE A CD1 1 
ATOM   1089 N N   . HIS A 1 143 ? 21.71243 15.44535 -19.20430 1.000 28.95224 ? 143 HIS A N   1 
ATOM   1090 C CA  A HIS A 1 143 ? 21.43059 14.07373 -18.80025 0.500 28.43282 ? 143 HIS A CA  1 
ATOM   1091 C CA  B HIS A 1 143 ? 21.42846 14.07789 -18.80556 0.500 28.42725 ? 143 HIS A CA  1 
ATOM   1092 C C   . HIS A 1 143 ? 22.70716 13.40851 -18.33128 1.000 28.18791 ? 143 HIS A C   1 
ATOM   1093 O O   . HIS A 1 143 ? 23.66804 13.26970 -19.09280 1.000 30.68685 ? 143 HIS A O   1 
ATOM   1094 C CB  A HIS A 1 143 ? 20.81323 13.25572 -19.93702 0.500 30.35555 ? 143 HIS A CB  1 
ATOM   1095 C CB  B HIS A 1 143 ? 20.79104 13.32671 -19.97822 0.500 30.57203 ? 143 HIS A CB  1 
ATOM   1096 C CG  A HIS A 1 143 ? 20.59343 11.81614 -19.57109 0.500 32.99403 ? 143 HIS A CG  1 
ATOM   1097 C CG  B HIS A 1 143 ? 19.42927 13.83648 -20.33955 0.500 33.99531 ? 143 HIS A CG  1 
ATOM   1098 N ND1 A HIS A 1 143 ? 21.58643 10.86340 -19.66183 0.500 35.08554 ? 143 HIS A ND1 1 
ATOM   1099 N ND1 B HIS A 1 143 ? 18.41992 13.01778 -20.79910 0.500 35.68273 ? 143 HIS A ND1 1 
ATOM   1100 C CD2 A HIS A 1 143 ? 19.50843 11.17786 -19.06922 0.500 33.48742 ? 143 HIS A CD2 1 
ATOM   1101 C CD2 B HIS A 1 143 ? 18.90903 15.08641 -20.30019 0.500 35.02139 ? 143 HIS A CD2 1 
ATOM   1102 C CE1 A HIS A 1 143 ? 21.11627 9.69702  -19.25479 0.500 33.25384 ? 143 HIS A CE1 1 
ATOM   1103 C CE1 B HIS A 1 143 ? 17.33712 13.74094 -21.02355 0.500 33.65666 ? 143 HIS A CE1 1 
ATOM   1104 N NE2 A HIS A 1 143 ? 19.85731 9.86030  -18.89022 0.500 32.59495 ? 143 HIS A NE2 1 
ATOM   1105 N NE2 B HIS A 1 143 ? 17.60761 14.99929 -20.72816 0.500 33.01730 ? 143 HIS A NE2 1 
ATOM   1106 N N   . PHE A 1 144 ? 22.71470 13.00220 -17.06796 1.000 24.49990 ? 144 PHE A N   1 
ATOM   1107 C CA  . PHE A 1 144 ? 23.91344 12.46573 -16.45033 1.000 25.06127 ? 144 PHE A CA  1 
ATOM   1108 C C   . PHE A 1 144 ? 23.92110 10.94875 -16.37238 1.000 26.47285 ? 144 PHE A C   1 
ATOM   1109 O O   . PHE A 1 144 ? 24.95029 10.32658 -16.65161 1.000 27.83327 ? 144 PHE A O   1 
ATOM   1110 C CB  . PHE A 1 144 ? 24.06702 13.05542 -15.04408 1.000 24.13354 ? 144 PHE A CB  1 
ATOM   1111 C CG  . PHE A 1 144 ? 25.27319 12.55488 -14.31374 1.000 24.56923 ? 144 PHE A CG  1 
ATOM   1112 C CD1 . PHE A 1 144 ? 26.53329 13.04532 -14.61955 1.000 25.27360 ? 144 PHE A CD1 1 
ATOM   1113 C CD2 . PHE A 1 144 ? 25.14801 11.59669 -13.32298 1.000 24.67723 ? 144 PHE A CD2 1 
ATOM   1114 C CE1 . PHE A 1 144 ? 27.65318 12.57980 -13.97001 1.000 25.12931 ? 144 PHE A CE1 1 
ATOM   1115 C CE2 . PHE A 1 144 ? 26.26163 11.12359 -12.65106 1.000 23.20284 ? 144 PHE A CE2 1 
ATOM   1116 C CZ  . PHE A 1 144 ? 27.51455 11.61715 -12.95901 1.000 24.55144 ? 144 PHE A CZ  1 
ATOM   1117 N N   . GLU A 1 145 ? 22.80849 10.33034 -15.98599 1.000 25.18765 ? 145 GLU A N   1 
ATOM   1118 C CA  . GLU A 1 145 ? 22.76542 8.87627  -15.92018 1.000 25.32780 ? 145 GLU A CA  1 
ATOM   1119 C C   . GLU A 1 145 ? 21.31574 8.44322  -15.90308 1.000 25.03326 ? 145 GLU A C   1 
ATOM   1120 O O   . GLU A 1 145 ? 20.42641 9.20913  -15.52477 1.000 27.33681 ? 145 GLU A O   1 
ATOM   1121 C CB  . GLU A 1 145 ? 23.49033 8.33960  -14.67951 1.000 26.97122 ? 145 GLU A CB  1 
ATOM   1122 C CG  . GLU A 1 145 ? 22.71117 8.60837  -13.40045 1.000 25.23815 ? 145 GLU A CG  1 
ATOM   1123 C CD  . GLU A 1 145 ? 23.50822 8.31986  -12.14086 1.000 26.23831 ? 145 GLU A CD  1 
ATOM   1124 O OE1 . GLU A 1 145 ? 24.65200 7.83624  -12.24162 1.000 28.33839 ? 145 GLU A OE1 1 
ATOM   1125 O OE2 . GLU A 1 145 ? 22.98225 8.58279  -11.03719 1.000 29.38609 ? 145 GLU A OE2 1 
ATOM   1126 N N   . ARG A 1 146 ? 21.08737 7.20024  -16.31277 1.000 25.26966 ? 146 ARG A N   1 
ATOM   1127 C CA  . ARG A 1 146 ? 19.80779 6.53275  -16.10102 1.000 25.70968 ? 146 ARG A CA  1 
ATOM   1128 C C   . ARG A 1 146 ? 19.99935 5.55910  -14.94954 1.000 26.64139 ? 146 ARG A C   1 
ATOM   1129 O O   . ARG A 1 146 ? 20.74680 4.58131  -15.06590 1.000 29.71132 ? 146 ARG A O   1 
ATOM   1130 C CB  . ARG A 1 146 ? 19.31509 5.81392  -17.35450 1.000 28.00675 ? 146 ARG A CB  1 
ATOM   1131 C CG  . ARG A 1 146 ? 18.08230 4.96498  -17.09549 1.000 30.06784 ? 146 ARG A CG  1 
ATOM   1132 C CD  . ARG A 1 146 ? 17.35778 4.59769  -18.38455 1.000 32.62802 ? 146 ARG A CD  1 
ATOM   1133 N NE  . ARG A 1 146 ? 16.72961 5.75665  -18.99918 0.800 33.10672 ? 146 ARG A NE  1 
ATOM   1134 C CZ  . ARG A 1 146 ? 15.97836 5.69237  -20.08877 0.700 36.76089 ? 146 ARG A CZ  1 
ATOM   1135 N NH1 . ARG A 1 146 ? 15.72976 4.53782  -20.68662 0.700 37.88842 ? 146 ARG A NH1 1 
ATOM   1136 N NH2 . ARG A 1 146 ? 15.46417 6.81161  -20.59037 0.700 37.90355 ? 146 ARG A NH2 1 
ATOM   1137 N N   . PHE A 1 147 ? 19.33499 5.84148  -13.83789 1.000 25.26196 ? 147 PHE A N   1 
ATOM   1138 C CA  . PHE A 1 147 ? 19.50200 5.07181  -12.62184 1.000 25.15458 ? 147 PHE A CA  1 
ATOM   1139 C C   . PHE A 1 147 ? 18.43806 3.98956  -12.54252 1.000 27.23664 ? 147 PHE A C   1 
ATOM   1140 O O   . PHE A 1 147 ? 17.24461 4.28251  -12.63800 1.000 28.15718 ? 147 PHE A O   1 
ATOM   1141 C CB  . PHE A 1 147 ? 19.38745 5.98142  -11.40318 1.000 24.19063 ? 147 PHE A CB  1 
ATOM   1142 C CG  . PHE A 1 147 ? 19.49100 5.24221  -10.09922 1.000 24.50300 ? 147 PHE A CG  1 
ATOM   1143 C CD1 . PHE A 1 147 ? 18.36607 4.70746  -9.49093  1.000 26.55318 ? 147 PHE A CD1 1 
ATOM   1144 C CD2 . PHE A 1 147 ? 20.72311 5.04966  -9.50473  1.000 26.09497 ? 147 PHE A CD2 1 
ATOM   1145 C CE1 . PHE A 1 147 ? 18.47160 4.00833  -8.30055  1.000 27.04219 ? 147 PHE A CE1 1 
ATOM   1146 C CE2 . PHE A 1 147 ? 20.83423 4.35642  -8.31121  1.000 27.19077 ? 147 PHE A CE2 1 
ATOM   1147 C CZ  . PHE A 1 147 ? 19.70596 3.83666  -7.71553  1.000 27.39636 ? 147 PHE A CZ  1 
ATOM   1148 N N   . ARG A 1 148 ? 18.87603 2.75146  -12.34673 1.000 27.79672 ? 148 ARG A N   1 
ATOM   1149 C CA  A ARG A 1 148 ? 18.01217 1.60973  -12.07013 0.500 30.08804 ? 148 ARG A CA  1 
ATOM   1150 C CA  B ARG A 1 148 ? 17.97607 1.65661  -12.02969 0.500 27.63652 ? 148 ARG A CA  1 
ATOM   1151 C C   . ARG A 1 148 ? 18.42281 1.03852  -10.71956 1.000 27.65344 ? 148 ARG A C   1 
ATOM   1152 O O   . ARG A 1 148 ? 19.59322 0.69808  -10.54358 1.000 28.89662 ? 148 ARG A O   1 
ATOM   1153 C CB  A ARG A 1 148 ? 18.17538 0.55081  -13.15972 0.500 35.42578 ? 148 ARG A CB  1 
ATOM   1154 C CB  B ARG A 1 148 ? 17.91551 0.57864  -13.10824 0.500 28.29113 ? 148 ARG A CB  1 
ATOM   1155 C CG  A ARG A 1 148 ? 16.91213 -0.07941 -13.68855 0.500 40.89951 ? 148 ARG A CG  1 
ATOM   1156 C CG  B ARG A 1 148 ? 16.74935 -0.38202 -12.86903 0.500 30.92014 ? 148 ARG A CG  1 
ATOM   1157 C CD  A ARG A 1 148 ? 17.24467 -0.76776 -14.99418 0.500 43.33779 ? 148 ARG A CD  1 
ATOM   1158 C CD  B ARG A 1 148 ? 16.50122 -1.34364 -14.03109 0.500 32.99861 ? 148 ARG A CD  1 
ATOM   1159 N NE  A ARG A 1 148 ? 18.16800 0.06002  -15.76058 0.500 45.63049 ? 148 ARG A NE  1 
ATOM   1160 N NE  B ARG A 1 148 ? 15.25389 -2.08284 -13.85765 0.500 35.74521 ? 148 ARG A NE  1 
ATOM   1161 C CZ  A ARG A 1 148 ? 17.88468 0.63927  -16.91904 0.500 44.95144 ? 148 ARG A CZ  1 
ATOM   1162 C CZ  B ARG A 1 148 ? 14.98378 -3.24543 -14.43514 0.500 38.06194 ? 148 ARG A CZ  1 
ATOM   1163 N NH1 A ARG A 1 148 ? 16.74275 0.41144  -17.54668 0.500 44.71141 ? 148 ARG A NH1 1 
ATOM   1164 N NH1 B ARG A 1 148 ? 15.86168 -3.84801 -15.21944 0.500 39.11892 ? 148 ARG A NH1 1 
ATOM   1165 N NH2 A ARG A 1 148 ? 18.77554 1.45958  -17.46606 0.500 46.37689 ? 148 ARG A NH2 1 
ATOM   1166 N NH2 B ARG A 1 148 ? 13.80359 -3.81960 -14.21872 0.500 39.83575 ? 148 ARG A NH2 1 
ATOM   1167 N N   . GLY A 1 149 ? 17.48232 0.92538  -9.79201  1.000 29.76000 ? 149 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 149 ? 17.83935 0.42196  -8.47250  1.000 28.02161 ? 149 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 149 ? 16.73991 0.68721  -7.47219  1.000 27.65815 ? 149 GLY A C   1 
ATOM   1170 O O   . GLY A 1 149 ? 15.57403 0.84240  -7.83709  1.000 30.47331 ? 149 GLY A O   1 
ATOM   1171 N N   . ASP A 1 150 ? 17.12594 0.73660  -6.19385  1.000 24.58155 ? 150 ASP A N   1 
ATOM   1172 C CA  . ASP A 1 150 ? 16.10060 0.85526  -5.16714  1.000 25.78859 ? 150 ASP A CA  1 
ATOM   1173 C C   . ASP A 1 150 ? 15.65531 2.29390  -4.94879  1.000 25.50415 ? 150 ASP A C   1 
ATOM   1174 O O   . ASP A 1 150 ? 14.49919 2.52620  -4.57855  1.000 28.43329 ? 150 ASP A O   1 
ATOM   1175 C CB  . ASP A 1 150 ? 16.60272 0.27729  -3.84809  1.000 25.51662 ? 150 ASP A CB  1 
ATOM   1176 C CG  . ASP A 1 150 ? 16.58007 -1.22341 -3.83788  1.000 27.64343 ? 150 ASP A CG  1 
ATOM   1177 O OD1 . ASP A 1 150 ? 16.07216 -1.80809 -4.81019  1.000 33.03798 ? 150 ASP A OD1 1 
ATOM   1178 O OD2 . ASP A 1 150 ? 17.05510 -1.82090 -2.85767  1.000 28.67700 ? 150 ASP A OD2 1 
ATOM   1179 N N   . GLY A 1 151 ? 16.54163 3.25979  -5.14167  1.000 24.24413 ? 151 GLY A N   1 
ATOM   1180 C CA  . GLY A 1 151 ? 16.18626 4.63071  -4.84552  1.000 25.41847 ? 151 GLY A CA  1 
ATOM   1181 C C   . GLY A 1 151 ? 17.40369 5.52586  -4.79567  1.000 23.14091 ? 151 GLY A C   1 
ATOM   1182 O O   . GLY A 1 151 ? 18.53941 5.09314  -4.99976  1.000 23.97527 ? 151 GLY A O   1 
ATOM   1183 N N   . LEU A 1 152 ? 17.13153 6.79708  -4.52065  1.000 23.00117 ? 152 LEU A N   1 
ATOM   1184 C CA  . LEU A 1 152 ? 18.14001 7.84124  -4.42703  1.000 21.31615 ? 152 LEU A CA  1 
ATOM   1185 C C   . LEU A 1 152 ? 17.88531 8.68864  -3.19125  1.000 22.54034 ? 152 LEU A C   1 
ATOM   1186 O O   . LEU A 1 152 ? 16.74022 8.89022  -2.78968  1.000 23.19074 ? 152 LEU A O   1 
ATOM   1187 C CB  . LEU A 1 152 ? 18.11614 8.73868  -5.65664  1.000 23.87579 ? 152 LEU A CB  1 
ATOM   1188 C CG  . LEU A 1 152 ? 18.62653 8.08184  -6.93192  1.000 25.91038 ? 152 LEU A CG  1 
ATOM   1189 C CD1 . LEU A 1 152 ? 18.13759 8.87755  -8.14181  1.000 28.04833 ? 152 LEU A CD1 1 
ATOM   1190 C CD2 . LEU A 1 152 ? 20.13494 8.00443  -6.92434  1.000 27.41612 ? 152 LEU A CD2 1 
ATOM   1191 N N   . CYS A 1 153 ? 18.96763 9.18975  -2.59892  1.000 21.47652 ? 153 CYS A N   1 
ATOM   1192 C CA  . CYS A 1 153 ? 18.90531 9.98768  -1.38031  1.000 20.62467 ? 153 CYS A CA  1 
ATOM   1193 C C   . CYS A 1 153 ? 19.66558 11.28483 -1.60387  1.000 22.27678 ? 153 CYS A C   1 
ATOM   1194 O O   . CYS A 1 153 ? 20.83440 11.25517 -2.00310  1.000 22.69968 ? 153 CYS A O   1 
ATOM   1195 C CB  . CYS A 1 153 ? 19.51587 9.21116  -0.20700  1.000 20.80191 ? 153 CYS A CB  1 
ATOM   1196 S SG  . CYS A 1 153 ? 19.60192 10.12680 1.38505   1.000 24.64599 ? 153 CYS A SG  1 
ATOM   1197 N N   . MET A 1 154 ? 19.02183 12.41704 -1.33216  1.000 22.08282 ? 154 MET A N   1 
ATOM   1198 C CA  . MET A 1 154 ? 19.67807 13.71809 -1.42219  1.000 21.83121 ? 154 MET A CA  1 
ATOM   1199 C C   . MET A 1 154 ? 19.69690 14.33714 -0.03500  1.000 22.17343 ? 154 MET A C   1 
ATOM   1200 O O   . MET A 1 154 ? 18.63659 14.59270 0.54033   1.000 21.79315 ? 154 MET A O   1 
ATOM   1201 C CB  . MET A 1 154 ? 18.97213 14.64353 -2.41238  1.000 22.95192 ? 154 MET A CB  1 
ATOM   1202 C CG  . MET A 1 154 ? 19.70780 15.95898 -2.63814  1.000 23.83987 ? 154 MET A CG  1 
ATOM   1203 S SD  . MET A 1 154 ? 21.27618 15.74578 -3.51996  1.000 23.60720 ? 154 MET A SD  1 
ATOM   1204 C CE  . MET A 1 154 ? 20.75694 15.99495 -5.23987  1.000 25.27395 ? 154 MET A CE  1 
ATOM   1205 N N   . SER A 1 155 ? 20.89430 14.59451 0.47853   1.000 22.06873 ? 155 SER A N   1 
ATOM   1206 C CA  . SER A 1 155 ? 21.09524 14.92652 1.88458   1.000 21.94095 ? 155 SER A CA  1 
ATOM   1207 C C   . SER A 1 155 ? 21.62139 16.34730 2.03095   1.000 23.47022 ? 155 SER A C   1 
ATOM   1208 O O   . SER A 1 155 ? 22.37900 16.83843 1.19457   1.000 24.97691 ? 155 SER A O   1 
ATOM   1209 C CB  . SER A 1 155 ? 22.07496 13.93997 2.52407   1.000 22.04508 ? 155 SER A CB  1 
ATOM   1210 O OG  . SER A 1 155 ? 22.38089 14.30582 3.87192   1.000 23.83552 ? 155 SER A OG  1 
ATOM   1211 N N   . THR A 1 156 ? 21.21593 17.00488 3.11275   1.000 22.23921 ? 156 THR A N   1 
ATOM   1212 C CA  . THR A 1 156 ? 21.84982 18.23366 3.54851   1.000 22.34790 ? 156 THR A CA  1 
ATOM   1213 C C   . THR A 1 156 ? 23.18436 17.91527 4.22112   1.000 22.85529 ? 156 THR A C   1 
ATOM   1214 O O   . THR A 1 156 ? 23.48864 16.75779 4.51253   1.000 25.57503 ? 156 THR A O   1 
ATOM   1215 C CB  . THR A 1 156 ? 20.95830 18.95168 4.55484   1.000 23.12934 ? 156 THR A CB  1 
ATOM   1216 O OG1 . THR A 1 156 ? 20.95682 18.16591 5.74291   1.000 24.22592 ? 156 THR A OG1 1 
ATOM   1217 C CG2 . THR A 1 156 ? 19.53048 19.10581 4.04263   1.000 25.33467 ? 156 THR A CG2 1 
ATOM   1218 N N   . PRO A 1 157 ? 24.00294 18.93035 4.50357   1.000 24.30913 ? 157 PRO A N   1 
ATOM   1219 C CA  . PRO A 1 157 ? 25.22234 18.66336 5.28414   1.000 24.45070 ? 157 PRO A CA  1 
ATOM   1220 C C   . PRO A 1 157 ? 24.95101 18.04116 6.64766   1.000 25.78353 ? 157 PRO A C   1 
ATOM   1221 O O   . PRO A 1 157 ? 25.57160 17.02848 6.99300   1.000 26.17828 ? 157 PRO A O   1 
ATOM   1222 C CB  . PRO A 1 157 ? 25.86262 20.05391 5.38389   1.000 24.79448 ? 157 PRO A CB  1 
ATOM   1223 C CG  . PRO A 1 157 ? 25.38945 20.74896 4.12043   1.000 25.20185 ? 157 PRO A CG  1 
ATOM   1224 C CD  . PRO A 1 157 ? 23.97160 20.31667 3.99942   1.000 24.28894 ? 157 PRO A CD  1 
ATOM   1225 N N   . SER A 1 158 ? 24.02382 18.59419 7.43151   1.000 25.66510 ? 158 SER A N   1 
ATOM   1226 C CA  . SER A 1 158 ? 23.75812 17.97852 8.72416   1.000 24.47564 ? 158 SER A CA  1 
ATOM   1227 C C   . SER A 1 158 ? 23.06287 16.62941 8.58571   1.000 22.89573 ? 158 SER A C   1 
ATOM   1228 O O   . SER A 1 158 ? 23.16641 15.79774 9.49599   1.000 24.37886 ? 158 SER A O   1 
ATOM   1229 C CB  . SER A 1 158 ? 22.95441 18.93312 9.62463   1.000 25.83440 ? 158 SER A CB  1 
ATOM   1230 O OG  . SER A 1 158 ? 21.67386 19.24306 9.09599   1.000 27.05160 ? 158 SER A OG  1 
ATOM   1231 N N   . GLY A 1 159 ? 22.37793 16.38196 7.46790   1.000 23.60652 ? 159 GLY A N   1 
ATOM   1232 C CA  . GLY A 1 159 ? 21.84888 15.05588 7.20333   1.000 23.08198 ? 159 GLY A CA  1 
ATOM   1233 C C   . GLY A 1 159 ? 22.88574 14.02363 6.79941   1.000 24.09890 ? 159 GLY A C   1 
ATOM   1234 O O   . GLY A 1 159 ? 22.55128 12.83445 6.73204   1.000 24.60012 ? 159 GLY A O   1 
ATOM   1235 N N   . THR A 1 160 ? 24.13354 14.42748 6.54261   1.000 22.31343 ? 160 THR A N   1 
ATOM   1236 C CA  . THR A 1 160 ? 25.07344 13.43558 6.02973   1.000 21.02750 ? 160 THR A CA  1 
ATOM   1237 C C   . THR A 1 160 ? 25.40748 12.37940 7.06475   1.000 21.19014 ? 160 THR A C   1 
ATOM   1238 O O   . THR A 1 160 ? 25.84634 11.28557 6.69071   1.000 21.35131 ? 160 THR A O   1 
ATOM   1239 C CB  . THR A 1 160 ? 26.37670 14.07062 5.50145   1.000 20.86260 ? 160 THR A CB  1 
ATOM   1240 O OG1 . THR A 1 160 ? 27.03686 14.82705 6.51700   1.000 21.50958 ? 160 THR A OG1 1 
ATOM   1241 C CG2 . THR A 1 160 ? 26.10730 14.98973 4.29118   1.000 22.17968 ? 160 THR A CG2 1 
ATOM   1242 N N   . THR A 1 161 ? 25.20305 12.67007 8.35159   1.000 22.44899 ? 161 THR A N   1 
ATOM   1243 C CA  . THR A 1 161 ? 25.42448 11.65645 9.37115   1.000 22.14615 ? 161 THR A CA  1 
ATOM   1244 C C   . THR A 1 161 ? 24.23226 10.72727 9.55505   1.000 22.74741 ? 161 THR A C   1 
ATOM   1245 O O   . THR A 1 161 ? 24.29393 9.84437  10.41731  1.000 23.85170 ? 161 THR A O   1 
ATOM   1246 C CB  . THR A 1 161 ? 25.77001 12.33135 10.70624  1.000 21.38520 ? 161 THR A CB  1 
ATOM   1247 O OG1 . THR A 1 161 ? 24.89252 13.44527 10.90100  1.000 23.68592 ? 161 THR A OG1 1 
ATOM   1248 C CG2 . THR A 1 161 ? 27.19909 12.82930 10.67115  1.000 25.44705 ? 161 THR A CG2 1 
ATOM   1249 N N   . ALA A 1 162 ? 23.17714 10.87620 8.76479   1.000 22.56811 ? 162 ALA A N   1 
ATOM   1250 C CA  . ALA A 1 162 ? 21.94631 10.09841 8.90996   1.000 23.67582 ? 162 ALA A CA  1 
ATOM   1251 C C   . ALA A 1 162 ? 21.86899 9.07724  7.78012   1.000 23.22029 ? 162 ALA A C   1 
ATOM   1252 O O   . ALA A 1 162 ? 22.83731 8.33214  7.58327   1.000 23.95212 ? 162 ALA A O   1 
ATOM   1253 C CB  . ALA A 1 162 ? 20.75627 11.04862 8.98076   1.000 25.36785 ? 162 ALA A CB  1 
ATOM   1254 N N   . TYR A 1 163 ? 20.75798 8.99229  7.04325   1.000 23.18102 ? 163 TYR A N   1 
ATOM   1255 C CA  . TYR A 1 163 ? 20.58889 7.99930  5.98161   1.000 20.35876 ? 163 TYR A CA  1 
ATOM   1256 C C   . TYR A 1 163 ? 21.77173 7.99880  5.02540   1.000 22.58619 ? 163 TYR A C   1 
ATOM   1257 O O   . TYR A 1 163 ? 22.28886 6.93743  4.66171   1.000 23.15401 ? 163 TYR A O   1 
ATOM   1258 C CB  . TYR A 1 163 ? 19.29463 8.31885  5.23480   1.000 20.44697 ? 163 TYR A CB  1 
ATOM   1259 C CG  . TYR A 1 163 ? 18.56145 7.17926  4.57271   1.000 21.37166 ? 163 TYR A CG  1 
ATOM   1260 C CD1 . TYR A 1 163 ? 19.14441 5.93480  4.39214   1.000 23.50082 ? 163 TYR A CD1 1 
ATOM   1261 C CD2 . TYR A 1 163 ? 17.26146 7.36348  4.13160   1.000 25.50151 ? 163 TYR A CD2 1 
ATOM   1262 C CE1 . TYR A 1 163 ? 18.44084 4.89834  3.75771   1.000 23.53424 ? 163 TYR A CE1 1 
ATOM   1263 C CE2 . TYR A 1 163 ? 16.55296 6.35100  3.50464   1.000 28.47765 ? 163 TYR A CE2 1 
ATOM   1264 C CZ  . TYR A 1 163 ? 17.14017 5.12228  3.30986   1.000 24.46541 ? 163 TYR A CZ  1 
ATOM   1265 O OH  . TYR A 1 163 ? 16.39282 4.13857  2.68228   1.000 27.70398 ? 163 TYR A OH  1 
ATOM   1266 N N   . ASN A 1 164 ? 22.23245 9.19224  4.65132   1.000 22.00896 ? 164 ASN A N   1 
ATOM   1267 C CA  . ASN A 1 164 ? 23.37844 9.35691  3.75547   1.000 21.19965 ? 164 ASN A CA  1 
ATOM   1268 C C   . ASN A 1 164 ? 24.57231 8.52773  4.20718   1.000 21.28715 ? 164 ASN A C   1 
ATOM   1269 O O   . ASN A 1 164 ? 25.25122 7.88604  3.39873   1.000 21.18774 ? 164 ASN A O   1 
ATOM   1270 C CB  . ASN A 1 164 ? 23.74009 10.84441 3.70768   1.000 20.39881 ? 164 ASN A CB  1 
ATOM   1271 C CG  . ASN A 1 164 ? 25.04623 11.11795 3.01404   1.000 21.68523 ? 164 ASN A CG  1 
ATOM   1272 O OD1 . ASN A 1 164 ? 25.08456 11.28422 1.79227   1.000 23.91094 ? 164 ASN A OD1 1 
ATOM   1273 N ND2 . ASN A 1 164 ? 26.13063 11.18927 3.78103   1.000 20.67448 ? 164 ASN A ND2 1 
ATOM   1274 N N   . LYS A 1 165 ? 24.85155 8.52838  5.50627   1.000 21.86618 ? 165 LYS A N   1 
ATOM   1275 C CA  . LYS A 1 165 ? 25.99833 7.77741  5.99360   1.000 18.56901 ? 165 LYS A CA  1 
ATOM   1276 C C   . LYS A 1 165 ? 25.81704 6.28729  5.76843   1.000 20.21658 ? 165 LYS A C   1 
ATOM   1277 O O   . LYS A 1 165 ? 26.75868 5.59210  5.37265   1.000 22.20509 ? 165 LYS A O   1 
ATOM   1278 C CB  . LYS A 1 165 ? 26.20275 8.06617  7.48569   1.000 21.56606 ? 165 LYS A CB  1 
ATOM   1279 C CG  . LYS A 1 165 ? 27.40668 7.38608  8.07172   1.000 23.27039 ? 165 LYS A CG  1 
ATOM   1280 C CD  . LYS A 1 165 ? 27.60756 7.83748  9.51414   1.000 24.57265 ? 165 LYS A CD  1 
ATOM   1281 C CE  . LYS A 1 165 ? 28.94774 7.40437  10.04637  1.000 29.94358 ? 165 LYS A CE  1 
ATOM   1282 N NZ  . LYS A 1 165 ? 29.01292 5.94278  10.26740  1.000 34.62866 ? 165 LYS A NZ  1 
ATOM   1283 N N   . SER A 1 166 ? 24.61443 5.77273  6.04253   1.000 21.36384 ? 166 SER A N   1 
ATOM   1284 C CA  . SER A 1 166 ? 24.34847 4.35189  5.87000   1.000 20.78554 ? 166 SER A CA  1 
ATOM   1285 C C   . SER A 1 166 ? 24.45666 3.91609  4.41301   1.000 22.00782 ? 166 SER A C   1 
ATOM   1286 O O   . SER A 1 166 ? 24.65176 2.72771  4.14462   1.000 23.17479 ? 166 SER A O   1 
ATOM   1287 C CB  . SER A 1 166 ? 22.95765 4.02551  6.39494   1.000 22.82596 ? 166 SER A CB  1 
ATOM   1288 O OG  . SER A 1 166 ? 22.91964 4.25924  7.79230   1.000 25.75128 ? 166 SER A OG  1 
ATOM   1289 N N   . LEU A 1 167 ? 24.28866 4.84377  3.48572   1.000 23.41518 ? 167 LEU A N   1 
ATOM   1290 C CA  . LEU A 1 167 ? 24.38792 4.58375  2.05570   1.000 22.65420 ? 167 LEU A CA  1 
ATOM   1291 C C   . LEU A 1 167 ? 25.79417 4.80320  1.50939   1.000 23.39507 ? 167 LEU A C   1 
ATOM   1292 O O   . LEU A 1 167 ? 25.99331 4.73748  0.28522   1.000 26.30898 ? 167 LEU A O   1 
ATOM   1293 C CB  . LEU A 1 167 ? 23.38443 5.46584  1.31095   1.000 22.20337 ? 167 LEU A CB  1 
ATOM   1294 C CG  . LEU A 1 167 ? 21.91862 5.16054  1.63818   1.000 22.91672 ? 167 LEU A CG  1 
ATOM   1295 C CD1 . LEU A 1 167 ? 20.98849 6.24139  1.09235   1.000 24.08793 ? 167 LEU A CD1 1 
ATOM   1296 C CD2 . LEU A 1 167 ? 21.52621 3.77643  1.12205   1.000 23.30973 ? 167 LEU A CD2 1 
ATOM   1297 N N   . GLY A 1 168 ? 26.77426 5.05805  2.37037   1.000 23.64121 ? 168 GLY A N   1 
ATOM   1298 C CA  . GLY A 1 168 ? 28.13906 5.24688  1.91586   1.000 22.76173 ? 168 GLY A CA  1 
ATOM   1299 C C   . GLY A 1 168 ? 28.52462 6.67815  1.61398   1.000 22.38377 ? 168 GLY A C   1 
ATOM   1300 O O   . GLY A 1 168 ? 29.63036 6.91400  1.10387   1.000 23.14408 ? 168 GLY A O   1 
ATOM   1301 N N   . GLY A 1 169 ? 27.66535 7.64149  1.93151   1.000 22.31657 ? 169 GLY A N   1 
ATOM   1302 C CA  . GLY A 1 169 ? 27.98030 9.02524  1.66275   1.000 21.77203 ? 169 GLY A CA  1 
ATOM   1303 C C   . GLY A 1 169 ? 29.07269 9.56936  2.56384   1.000 21.21021 ? 169 GLY A C   1 
ATOM   1304 O O   . GLY A 1 169 ? 29.37592 9.03440  3.63996   1.000 22.32993 ? 169 GLY A O   1 
ATOM   1305 N N   . ALA A 1 170 ? 29.65692 10.67438 2.12236   1.000 20.44247 ? 170 ALA A N   1 
ATOM   1306 C CA  . ALA A 1 170 ? 30.63955 11.40022 2.91700   1.000 20.61736 ? 170 ALA A CA  1 
ATOM   1307 C C   . ALA A 1 170 ? 29.94728 12.19515 4.01633   1.000 23.03207 ? 170 ALA A C   1 
ATOM   1308 O O   . ALA A 1 170 ? 28.80963 12.64098 3.86054   1.000 23.15562 ? 170 ALA A O   1 
ATOM   1309 C CB  . ALA A 1 170 ? 31.44512 12.35670 2.03636   1.000 22.23275 ? 170 ALA A CB  1 
ATOM   1310 N N   . LEU A 1 171 ? 30.64195 12.37081 5.14323   1.000 21.16946 ? 171 LEU A N   1 
ATOM   1311 C CA  . LEU A 1 171 ? 30.18034 13.29333 6.17309   1.000 22.04493 ? 171 LEU A CA  1 
ATOM   1312 C C   . LEU A 1 171 ? 30.73426 14.67683 5.86383   1.000 23.50184 ? 171 LEU A C   1 
ATOM   1313 O O   . LEU A 1 171 ? 31.95057 14.84881 5.72528   1.000 26.07494 ? 171 LEU A O   1 
ATOM   1314 C CB  . LEU A 1 171 ? 30.62323 12.83461 7.55865   1.000 22.21234 ? 171 LEU A CB  1 
ATOM   1315 C CG  . LEU A 1 171 ? 30.37583 11.35950 7.86479   1.000 22.37957 ? 171 LEU A CG  1 
ATOM   1316 C CD1 . LEU A 1 171 ? 30.77067 11.07023 9.32099   1.000 24.05305 ? 171 LEU A CD1 1 
ATOM   1317 C CD2 . LEU A 1 171 ? 28.91931 10.97777 7.60963   1.000 24.12850 ? 171 LEU A CD2 1 
ATOM   1318 N N   . MET A 1 172 ? 29.84721 15.65590 5.74798   1.000 22.62155 ? 172 MET A N   1 
ATOM   1319 C CA  A MET A 1 172 ? 30.20390 17.00226 5.31903   0.500 24.64625 ? 172 MET A CA  1 
ATOM   1320 C CA  B MET A 1 172 ? 30.20038 16.99817 5.31409   0.500 25.91420 ? 172 MET A CA  1 
ATOM   1321 C C   . MET A 1 172 ? 29.94022 17.98518 6.44497   1.000 26.23614 ? 172 MET A C   1 
ATOM   1322 O O   . MET A 1 172 ? 28.85218 17.98310 7.03549   1.000 26.23529 ? 172 MET A O   1 
ATOM   1323 C CB  A MET A 1 172 ? 29.40261 17.44448 4.09562   0.500 26.74274 ? 172 MET A CB  1 
ATOM   1324 C CB  B MET A 1 172 ? 29.39356 17.36113 4.06389   0.500 30.80955 ? 172 MET A CB  1 
ATOM   1325 C CG  A MET A 1 172 ? 29.30517 16.45927 2.97864   0.500 28.98532 ? 172 MET A CG  1 
ATOM   1326 C CG  B MET A 1 172 ? 29.84390 18.58986 3.33512   0.500 35.11368 ? 172 MET A CG  1 
ATOM   1327 S SD  A MET A 1 172 ? 28.37930 17.29502 1.67466   0.500 28.99623 ? 172 MET A SD  1 
ATOM   1328 S SD  B MET A 1 172 ? 29.29598 18.49848 1.61997   0.500 41.41053 ? 172 MET A SD  1 
ATOM   1329 C CE  A MET A 1 172 ? 29.43740 18.71646 1.41813   0.500 29.22087 ? 172 MET A CE  1 
ATOM   1330 C CE  B MET A 1 172 ? 27.91599 17.35825 1.72852   0.500 43.05596 ? 172 MET A CE  1 
ATOM   1331 N N   . HIS A 1 173 ? 30.92458 18.83320 6.72333   1.000 25.02821 ? 173 HIS A N   1 
ATOM   1332 C CA  . HIS A 1 173 ? 30.75647 19.86635 7.73814   1.000 25.23519 ? 173 HIS A CA  1 
ATOM   1333 C C   . HIS A 1 173 ? 29.62912 20.81133 7.33286   1.000 27.25666 ? 173 HIS A C   1 
ATOM   1334 O O   . HIS A 1 173 ? 29.57146 21.24236 6.17505   1.000 27.73394 ? 173 HIS A O   1 
ATOM   1335 C CB  . HIS A 1 173 ? 32.03689 20.66476 7.94789   1.000 26.94164 ? 173 HIS A CB  1 
ATOM   1336 C CG  . HIS A 1 173 ? 31.96218 21.57592 9.13168   1.000 28.71800 ? 173 HIS A CG  1 
ATOM   1337 N ND1 . HIS A 1 173 ? 31.53322 22.88190 9.03953   1.000 31.32070 ? 173 HIS A ND1 1 
ATOM   1338 C CD2 . HIS A 1 173 ? 32.21975 21.35489 10.44394  1.000 28.35464 ? 173 HIS A CD2 1 
ATOM   1339 C CE1 . HIS A 1 173 ? 31.54896 23.43246 10.24234  1.000 31.28727 ? 173 HIS A CE1 1 
ATOM   1340 N NE2 . HIS A 1 173 ? 31.95830 22.52553 11.11135  1.000 29.70643 ? 173 HIS A NE2 1 
ATOM   1341 N N   . PRO A 1 174 ? 28.71811 21.15628 8.24396   1.000 27.04018 ? 174 PRO A N   1 
ATOM   1342 C CA  . PRO A 1 174 ? 27.52466 21.91284 7.84388   1.000 29.35046 ? 174 PRO A CA  1 
ATOM   1343 C C   . PRO A 1 174 ? 27.78231 23.36652 7.48961   1.000 32.90914 ? 174 PRO A C   1 
ATOM   1344 O O   . PRO A 1 174 ? 26.84410 24.05610 7.08316   1.000 36.05042 ? 174 PRO A O   1 
ATOM   1345 C CB  . PRO A 1 174 ? 26.60531 21.78124 9.06590   1.000 32.64603 ? 174 PRO A CB  1 
ATOM   1346 C CG  . PRO A 1 174 ? 27.51976 21.48816 10.19226  1.000 31.93174 ? 174 PRO A CG  1 
ATOM   1347 C CD  . PRO A 1 174 ? 28.65052 20.69880 9.64149   1.000 26.25215 ? 174 PRO A CD  1 
ATOM   1348 N N   . SER A 1 175 ? 29.00885 23.86892 7.59861   1.000 32.62758 ? 175 SER A N   1 
ATOM   1349 C CA  . SER A 1 175 ? 29.28096 25.19243 7.05246   1.000 33.38076 ? 175 SER A CA  1 
ATOM   1350 C C   . SER A 1 175 ? 29.36338 25.18006 5.52898   1.000 34.17273 ? 175 SER A C   1 
ATOM   1351 O O   . SER A 1 175 ? 29.39072 26.25329 4.91221   1.000 35.16303 ? 175 SER A O   1 
ATOM   1352 C CB  . SER A 1 175 ? 30.57636 25.74672 7.64052   1.000 35.13843 ? 175 SER A CB  1 
ATOM   1353 O OG  . SER A 1 175 ? 31.68196 24.95609 7.24964   1.000 37.90248 ? 175 SER A OG  1 
ATOM   1354 N N   . ILE A 1 176 ? 29.38675 24.00111 4.91804   1.000 32.10159 ? 176 ILE A N   1 
ATOM   1355 C CA  . ILE A 1 176 ? 29.48952 23.86474 3.46922   1.000 29.15462 ? 176 ILE A CA  1 
ATOM   1356 C C   . ILE A 1 176 ? 28.08624 23.90644 2.87942   1.000 28.99384 ? 176 ILE A C   1 
ATOM   1357 O O   . ILE A 1 176 ? 27.22305 23.10833 3.25478   1.000 30.48149 ? 176 ILE A O   1 
ATOM   1358 C CB  . ILE A 1 176 ? 30.20369 22.56179 3.08720   1.000 28.68622 ? 176 ILE A CB  1 
ATOM   1359 C CG1 . ILE A 1 176 ? 31.61898 22.54818 3.66196   1.000 28.57801 ? 176 ILE A CG1 1 
ATOM   1360 C CG2 . ILE A 1 176 ? 30.21189 22.38236 1.56506   1.000 27.50394 ? 176 ILE A CG2 1 
ATOM   1361 C CD1 . ILE A 1 176 ? 32.28107 21.20633 3.57804   1.000 29.71920 ? 176 ILE A CD1 1 
ATOM   1362 N N   . GLU A 1 177 ? 27.85015 24.83642 1.95853   1.000 26.72289 ? 177 GLU A N   1 
ATOM   1363 C CA  . GLU A 1 177 ? 26.51182 25.00956 1.39852   1.000 26.19561 ? 177 GLU A CA  1 
ATOM   1364 C C   . GLU A 1 177 ? 26.39712 24.06833 0.21107   1.000 28.06156 ? 177 GLU A C   1 
ATOM   1365 O O   . GLU A 1 177 ? 26.78675 24.39794 -0.90833  1.000 29.71325 ? 177 GLU A O   1 
ATOM   1366 C CB  . GLU A 1 177 ? 26.26744 26.46184 1.01428   1.000 31.32439 ? 177 GLU A CB  1 
ATOM   1367 C CG  . GLU A 1 177 ? 26.06949 27.36471 2.21633   1.000 37.15431 ? 177 GLU A CG  1 
ATOM   1368 C CD  . GLU A 1 177 ? 25.66828 28.77225 1.83790   0.800 42.99674 ? 177 GLU A CD  1 
ATOM   1369 O OE1 . GLU A 1 177 ? 26.49458 29.48172 1.22990   0.800 44.38911 ? 177 GLU A OE1 1 
ATOM   1370 O OE2 . GLU A 1 177 ? 24.51948 29.16627 2.13999   0.800 45.96445 ? 177 GLU A OE2 1 
ATOM   1371 N N   . ALA A 1 178 ? 25.85957 22.87832 0.46378   1.000 26.61240 ? 178 ALA A N   1 
ATOM   1372 C CA  . ALA A 1 178 ? 25.88536 21.81088 -0.52630  1.000 23.28406 ? 178 ALA A CA  1 
ATOM   1373 C C   . ALA A 1 178 ? 24.80410 20.79087 -0.20583  1.000 25.66569 ? 178 ALA A C   1 
ATOM   1374 O O   . ALA A 1 178 ? 24.19035 20.81031 0.86609   1.000 26.84981 ? 178 ALA A O   1 
ATOM   1375 C CB  . ALA A 1 178 ? 27.26042 21.13439 -0.59252  1.000 25.28093 ? 178 ALA A CB  1 
ATOM   1376 N N   . MET A 1 179 ? 24.57064 19.90327 -1.17023  1.000 23.51227 ? 179 MET A N   1 
ATOM   1377 C CA  . MET A 1 179 ? 23.73236 18.72846 -0.99571  1.000 22.72042 ? 179 MET A CA  1 
ATOM   1378 C C   . MET A 1 179 ? 24.46390 17.53144 -1.58428  1.000 21.68608 ? 179 MET A C   1 
ATOM   1379 O O   . MET A 1 179 ? 25.29977 17.68445 -2.48462  1.000 23.65877 ? 179 MET A O   1 
ATOM   1380 C CB  . MET A 1 179 ? 22.36324 18.90654 -1.66909  1.000 21.12370 ? 179 MET A CB  1 
ATOM   1381 C CG  . MET A 1 179 ? 22.46564 19.20654 -3.17990  1.000 21.53951 ? 179 MET A CG  1 
ATOM   1382 S SD  . MET A 1 179 ? 20.87812 19.56626 -3.94254  1.000 24.93383 ? 179 MET A SD  1 
ATOM   1383 C CE  . MET A 1 179 ? 21.39916 19.76773 -5.65299  1.000 24.23713 ? 179 MET A CE  1 
ATOM   1384 N N   . GLN A 1 180 ? 24.14735 16.33390 -1.08618  1.000 22.00389 ? 180 GLN A N   1 
ATOM   1385 C CA  . GLN A 1 180 ? 24.87603 15.13349 -1.48476  1.000 21.74687 ? 180 GLN A CA  1 
ATOM   1386 C C   . GLN A 1 180 ? 23.90520 14.04662 -1.91787  1.000 22.75990 ? 180 GLN A C   1 
ATOM   1387 O O   . GLN A 1 180 ? 23.00373 13.67732 -1.16418  1.000 22.35329 ? 180 GLN A O   1 
ATOM   1388 C CB  . GLN A 1 180 ? 25.78478 14.63409 -0.35717  1.000 21.99678 ? 180 GLN A CB  1 
ATOM   1389 C CG  . GLN A 1 180 ? 26.50834 13.36217 -0.70610  1.000 20.53511 ? 180 GLN A CG  1 
ATOM   1390 C CD  . GLN A 1 180 ? 27.55172 12.98302 0.31115   1.000 21.72524 ? 180 GLN A CD  1 
ATOM   1391 O OE1 . GLN A 1 180 ? 28.31164 12.04171 0.10495   1.000 22.95445 ? 180 GLN A OE1 1 
ATOM   1392 N NE2 . GLN A 1 180 ? 27.57802 13.69884 1.43517   1.000 21.79523 ? 180 GLN A NE2 1 
ATOM   1393 N N   . LEU A 1 181 ? 24.09013 13.53645 -3.14150  1.000 22.46656 ? 181 LEU A N   1 
ATOM   1394 C CA  . LEU A 1 181 ? 23.23911 12.50053 -3.70569  1.000 23.46367 ? 181 LEU A CA  1 
ATOM   1395 C C   . LEU A 1 181 ? 23.90877 11.13676 -3.57158  1.000 21.95885 ? 181 LEU A C   1 
ATOM   1396 O O   . LEU A 1 181 ? 25.02299 10.93965 -4.07179  1.000 22.42418 ? 181 LEU A O   1 
ATOM   1397 C CB  . LEU A 1 181 ? 22.96427 12.80216 -5.18440  1.000 23.55471 ? 181 LEU A CB  1 
ATOM   1398 C CG  . LEU A 1 181 ? 22.05741 11.81197 -5.90492  1.000 23.87559 ? 181 LEU A CG  1 
ATOM   1399 C CD1 . LEU A 1 181 ? 20.60488 12.01248 -5.47781  1.000 22.75781 ? 181 LEU A CD1 1 
ATOM   1400 C CD2 . LEU A 1 181 ? 22.21020 11.96265 -7.43551  1.000 24.93062 ? 181 LEU A CD2 1 
ATOM   1401 N N   . THR A 1 182 ? 23.22472 10.18715 -2.92357  1.000 20.99121 ? 182 THR A N   1 
ATOM   1402 C CA  . THR A 1 182 ? 23.72061 8.82415  -2.80758  1.000 20.76361 ? 182 THR A CA  1 
ATOM   1403 C C   . THR A 1 182 ? 22.74177 7.83804  -3.43625  1.000 20.83669 ? 182 THR A C   1 
ATOM   1404 O O   . THR A 1 182 ? 21.52970 8.07742  -3.49815  1.000 21.14324 ? 182 THR A O   1 
ATOM   1405 C CB  . THR A 1 182 ? 23.98007 8.42251  -1.33379  1.000 21.52250 ? 182 THR A CB  1 
ATOM   1406 O OG1 . THR A 1 182 ? 22.82387 8.71275  -0.54538  1.000 23.72329 ? 182 THR A OG1 1 
ATOM   1407 C CG2 . THR A 1 182 ? 25.18629 9.17436  -0.76814  1.000 23.48793 ? 182 THR A CG2 1 
ATOM   1408 N N   . GLU A 1 183 ? 23.28748 6.71643  -3.89165  1.000 23.13976 ? 183 GLU A N   1 
ATOM   1409 C CA  . GLU A 1 183 ? 22.52038 5.65273  -4.52127  1.000 23.69829 ? 183 GLU A CA  1 
ATOM   1410 C C   . GLU A 1 183 ? 22.07818 4.61738  -3.49966  1.000 21.79104 ? 183 GLU A C   1 
ATOM   1411 O O   . GLU A 1 183 ? 22.79872 4.32253  -2.54389  1.000 23.93589 ? 183 GLU A O   1 
ATOM   1412 C CB  . GLU A 1 183 ? 23.35673 4.94143  -5.57981  1.000 24.21359 ? 183 GLU A CB  1 
ATOM   1413 C CG  . GLU A 1 183 ? 23.88013 5.82615  -6.67930  1.000 25.94732 ? 183 GLU A CG  1 
ATOM   1414 C CD  . GLU A 1 183 ? 24.69880 5.05698  -7.68636  1.000 30.13100 ? 183 GLU A CD  1 
ATOM   1415 O OE1 . GLU A 1 183 ? 24.97116 3.85230  -7.45345  1.000 33.80735 ? 183 GLU A OE1 1 
ATOM   1416 O OE2 . GLU A 1 183 ? 25.08168 5.66353  -8.70532  1.000 29.85604 ? 183 GLU A OE2 1 
ATOM   1417 N N   . MET A 1 184 ? 20.90257 4.03020  -3.73823  1.000 21.78046 ? 184 MET A N   1 
ATOM   1418 C CA  . MET A 1 184 ? 20.45827 2.83173  -3.02921  1.000 22.51063 ? 184 MET A CA  1 
ATOM   1419 C C   . MET A 1 184 ? 20.43926 1.65514  -3.99469  1.000 24.82647 ? 184 MET A C   1 
ATOM   1420 O O   . MET A 1 184 ? 19.53123 1.55655  -4.82695  1.000 26.86875 ? 184 MET A O   1 
ATOM   1421 C CB  . MET A 1 184 ? 19.07308 3.01480  -2.43108  1.000 22.95183 ? 184 MET A CB  1 
ATOM   1422 C CG  . MET A 1 184 ? 18.89190 4.27057  -1.61947  1.000 25.98326 ? 184 MET A CG  1 
ATOM   1423 S SD  . MET A 1 184 ? 17.16539 4.37495  -1.15778  1.000 35.10638 ? 184 MET A SD  1 
ATOM   1424 C CE  . MET A 1 184 ? 17.14660 5.94143  -0.28636  1.000 33.23331 ? 184 MET A CE  1 
ATOM   1425 N N   . ALA A 1 185 ? 21.38823 0.73771  -3.82691  1.000 24.19540 ? 185 ALA A N   1 
ATOM   1426 C CA  . ALA A 1 185 ? 21.48639 -0.50950 -4.58673  1.000 24.81830 ? 185 ALA A CA  1 
ATOM   1427 C C   . ALA A 1 185 ? 21.23550 -0.29040 -6.07245  1.000 27.89088 ? 185 ALA A C   1 
ATOM   1428 O O   . ALA A 1 185 ? 20.19158 -0.67958 -6.59262  1.000 32.62644 ? 185 ALA A O   1 
ATOM   1429 C CB  . ALA A 1 185 ? 20.51603 -1.56687 -4.05512  1.000 24.36802 ? 185 ALA A CB  1 
ATOM   1430 N N   . SER A 1 186 ? 22.17726 0.34225  -6.74409  1.000 28.33332 ? 186 SER A N   1 
ATOM   1431 C CA  . SER A 1 186 ? 22.06215 0.52559  -8.18568  1.000 29.60036 ? 186 SER A CA  1 
ATOM   1432 C C   . SER A 1 186 ? 22.43930 -0.75366 -8.91857  1.000 31.03943 ? 186 SER A C   1 
ATOM   1433 O O   . SER A 1 186 ? 23.31050 -1.51173 -8.48405  1.000 32.73104 ? 186 SER A O   1 
ATOM   1434 C CB  . SER A 1 186 ? 22.96071 1.66733  -8.64468  1.000 32.44541 ? 186 SER A CB  1 
ATOM   1435 O OG  . SER A 1 186 ? 24.29098 1.43403  -8.23700  1.000 37.41387 ? 186 SER A OG  1 
ATOM   1436 N N   . ILE A 1 187 ? 21.77810 -0.98673 -10.05255 1.000 30.31228 ? 187 ILE A N   1 
ATOM   1437 C CA  . ILE A 1 187 ? 22.15878 -2.08938 -10.92417 1.000 30.19206 ? 187 ILE A CA  1 
ATOM   1438 C C   . ILE A 1 187 ? 23.27382 -1.60775 -11.83340 1.000 31.54067 ? 187 ILE A C   1 
ATOM   1439 O O   . ILE A 1 187 ? 23.16024 -0.54793 -12.45932 1.000 33.35495 ? 187 ILE A O   1 
ATOM   1440 C CB  . ILE A 1 187 ? 20.96463 -2.58904 -11.75057 1.000 33.49405 ? 187 ILE A CB  1 
ATOM   1441 C CG1 . ILE A 1 187 ? 19.75889 -2.86950 -10.85565 1.000 37.12263 ? 187 ILE A CG1 1 
ATOM   1442 C CG2 . ILE A 1 187 ? 21.36685 -3.83520 -12.53795 1.000 35.72110 ? 187 ILE A CG2 1 
ATOM   1443 C CD1 . ILE A 1 187 ? 18.60074 -3.50063 -11.58360 1.000 40.39477 ? 187 ILE A CD1 1 
ATOM   1444 N N   . ASN A 1 188 ? 24.36041 -2.36697 -11.89195 1.000 31.22621 ? 188 ASN A N   1 
ATOM   1445 C CA  . ASN A 1 188 ? 25.44164 -2.07713 -12.82750 1.000 34.75771 ? 188 ASN A CA  1 
ATOM   1446 C C   . ASN A 1 188 ? 25.84953 -3.35795 -13.52933 1.000 35.45043 ? 188 ASN A C   1 
ATOM   1447 O O   . ASN A 1 188 ? 26.30107 -4.31019 -12.88522 1.000 34.77561 ? 188 ASN A O   1 
ATOM   1448 C CB  . ASN A 1 188 ? 26.63669 -1.43478 -12.12083 1.000 36.62387 ? 188 ASN A CB  1 
ATOM   1449 C CG  . ASN A 1 188 ? 26.45595 0.05817  -11.93398 1.000 36.38918 ? 188 ASN A CG  1 
ATOM   1450 O OD1 . ASN A 1 188 ? 26.80817 0.85684  -12.81217 1.000 35.34016 ? 188 ASN A OD1 1 
ATOM   1451 N ND2 . ASN A 1 188 ? 25.88007 0.44468  -10.80302 1.000 34.77588 ? 188 ASN A ND2 1 
ATOM   1452 N N   . ASN A 1 189 ? 25.68236 -3.37815 -14.84535 1.000 36.65200 ? 189 ASN A N   1 
ATOM   1453 C CA  . ASN A 1 189 ? 26.14390 -4.48306 -15.66544 1.000 38.71982 ? 189 ASN A CA  1 
ATOM   1454 C C   . ASN A 1 189 ? 26.50620 -3.90611 -17.02537 1.000 43.41738 ? 189 ASN A C   1 
ATOM   1455 O O   . ASN A 1 189 ? 26.55913 -2.68572 -17.19922 1.000 46.71551 ? 189 ASN A O   1 
ATOM   1456 C CB  . ASN A 1 189 ? 25.08270 -5.59047 -15.73100 1.000 40.16756 ? 189 ASN A CB  1 
ATOM   1457 C CG  . ASN A 1 189 ? 23.70772 -5.06398 -16.09274 1.000 43.04237 ? 189 ASN A CG  1 
ATOM   1458 O OD1 . ASN A 1 189 ? 23.57560 -4.16553 -16.91887 1.000 45.80797 ? 189 ASN A OD1 1 
ATOM   1459 N ND2 . ASN A 1 189 ? 22.67491 -5.62011 -15.46883 1.000 44.35914 ? 189 ASN A ND2 1 
ATOM   1460 N N   . ARG A 1 190 ? 26.74375 -4.78572 -17.99793 1.000 47.58012 ? 190 ARG A N   1 
ATOM   1461 C CA  . ARG A 1 190 ? 27.10486 -4.33147 -19.33787 1.000 51.00033 ? 190 ARG A CA  1 
ATOM   1462 C C   . ARG A 1 190 ? 26.07934 -3.35882 -19.91444 1.000 51.72259 ? 190 ARG A C   1 
ATOM   1463 O O   . ARG A 1 190 ? 26.43194 -2.49103 -20.72068 1.000 54.30766 ? 190 ARG A O   1 
ATOM   1464 C CB  . ARG A 1 190 ? 27.26838 -5.54177 -20.26168 1.000 53.74198 ? 190 ARG A CB  1 
ATOM   1465 C CG  . ARG A 1 190 ? 27.64062 -5.21595 -21.69613 1.000 56.55805 ? 190 ARG A CG  1 
ATOM   1466 C CD  . ARG A 1 190 ? 27.03355 -6.24941 -22.62269 1.000 58.60768 ? 190 ARG A CD  1 
ATOM   1467 N NE  . ARG A 1 190 ? 26.94111 -7.53908 -21.95075 1.000 59.72037 ? 190 ARG A NE  1 
ATOM   1468 C CZ  . ARG A 1 190 ? 25.99626 -8.43937 -22.18031 1.000 60.44721 ? 190 ARG A CZ  1 
ATOM   1469 N NH1 . ARG A 1 190 ? 25.04617 -8.23187 -23.07800 1.000 60.70313 ? 190 ARG A NH1 1 
ATOM   1470 N NH2 . ARG A 1 190 ? 25.99867 -9.57186 -21.48422 1.000 60.92713 ? 190 ARG A NH2 1 
ATOM   1471 N N   . VAL A 1 191 ? 24.82098 -3.46591 -19.49945 1.000 50.98909 ? 191 VAL A N   1 
ATOM   1472 C CA  . VAL A 1 191 ? 23.74001 -2.67535 -20.07266 1.000 50.82040 ? 191 VAL A CA  1 
ATOM   1473 C C   . VAL A 1 191 ? 23.39830 -1.45615 -19.21722 1.000 47.58907 ? 191 VAL A C   1 
ATOM   1474 O O   . VAL A 1 191 ? 23.07151 -0.39346 -19.74460 1.000 49.08468 ? 191 VAL A O   1 
ATOM   1475 C CB  . VAL A 1 191 ? 22.50332 -3.57314 -20.28878 1.000 54.10138 ? 191 VAL A CB  1 
ATOM   1476 C CG1 . VAL A 1 191 ? 21.44175 -2.83000 -21.06630 1.000 55.32050 ? 191 VAL A CG1 1 
ATOM   1477 C CG2 . VAL A 1 191 ? 22.90000 -4.85878 -21.02031 1.000 56.62698 ? 191 VAL A CG2 1 
ATOM   1478 N N   . TYR A 1 192 ? 23.45091 -1.57119 -17.89580 1.000 42.89494 ? 192 TYR A N   1 
ATOM   1479 C CA  . TYR A 1 192 ? 23.01973 -0.49447 -17.01567 1.000 40.21983 ? 192 TYR A CA  1 
ATOM   1480 C C   . TYR A 1 192 ? 24.22952 0.07795  -16.29036 1.000 38.45683 ? 192 TYR A C   1 
ATOM   1481 O O   . TYR A 1 192 ? 25.08848 -0.67772 -15.82816 1.000 40.81898 ? 192 TYR A O   1 
ATOM   1482 C CB  . TYR A 1 192 ? 21.97357 -1.00944 -16.02283 1.000 43.16051 ? 192 TYR A CB  1 
ATOM   1483 C CG  . TYR A 1 192 ? 20.83347 -1.75125 -16.69801 0.700 44.94760 ? 192 TYR A CG  1 
ATOM   1484 C CD1 . TYR A 1 192 ? 20.31073 -1.30815 -17.90573 0.700 46.26018 ? 192 TYR A CD1 1 
ATOM   1485 C CD2 . TYR A 1 192 ? 20.29710 -2.90594 -16.13913 0.700 45.50152 ? 192 TYR A CD2 1 
ATOM   1486 C CE1 . TYR A 1 192 ? 19.26754 -1.98403 -18.53477 0.700 46.91341 ? 192 TYR A CE1 1 
ATOM   1487 C CE2 . TYR A 1 192 ? 19.25717 -3.59102 -16.75924 0.700 46.59554 ? 192 TYR A CE2 1 
ATOM   1488 C CZ  . TYR A 1 192 ? 18.74685 -3.12406 -17.95762 0.700 47.53432 ? 192 TYR A CZ  1 
ATOM   1489 O OH  . TYR A 1 192 ? 17.71623 -3.79687 -18.58290 0.700 48.86326 ? 192 TYR A OH  1 
ATOM   1490 N N   . ARG A 1 193 ? 24.30192 1.41195  -16.19611 1.000 35.36726 ? 193 ARG A N   1 
ATOM   1491 C CA  . ARG A 1 193 ? 25.51173 2.08731  -15.72031 1.000 34.29944 ? 193 ARG A CA  1 
ATOM   1492 C C   . ARG A 1 193 ? 25.15772 3.30675  -14.87910 1.000 32.78139 ? 193 ARG A C   1 
ATOM   1493 O O   . ARG A 1 193 ? 24.47403 4.21415  -15.35861 1.000 37.29875 ? 193 ARG A O   1 
ATOM   1494 C CB  . ARG A 1 193 ? 26.38126 2.50997  -16.90852 1.000 38.52459 ? 193 ARG A CB  1 
ATOM   1495 C CG  . ARG A 1 193 ? 27.77369 2.97527  -16.55052 1.000 43.56644 ? 193 ARG A CG  1 
ATOM   1496 C CD  . ARG A 1 193 ? 28.79444 1.85797  -16.73862 0.800 47.95017 ? 193 ARG A CD  1 
ATOM   1497 N NE  . ARG A 1 193 ? 30.14963 2.38095  -16.87564 0.700 52.56221 ? 193 ARG A NE  1 
ATOM   1498 C CZ  . ARG A 1 193 ? 30.85000 2.36933  -18.00213 0.600 55.85596 ? 193 ARG A CZ  1 
ATOM   1499 N NH1 . ARG A 1 193 ? 30.36713 1.83338  -19.11172 0.600 56.73731 ? 193 ARG A NH1 1 
ATOM   1500 N NH2 . ARG A 1 193 ? 32.06960 2.90020  -18.01332 0.600 56.32566 ? 193 ARG A NH2 1 
ATOM   1501 N N   . THR A 1 194 ? 25.64683 3.35612  -13.63607 1.000 26.65596 ? 194 THR A N   1 
ATOM   1502 C CA  . THR A 1 194 ? 25.54787 4.56869  -12.83816 1.000 24.40768 ? 194 THR A CA  1 
ATOM   1503 C C   . THR A 1 194 ? 26.93443 4.96237  -12.34759 1.000 22.08350 ? 194 THR A C   1 
ATOM   1504 O O   . THR A 1 194 ? 27.91113 4.22325  -12.50751 1.000 24.63212 ? 194 THR A O   1 
ATOM   1505 C CB  . THR A 1 194 ? 24.60115 4.40420  -11.64143 1.000 26.75541 ? 194 THR A CB  1 
ATOM   1506 O OG1 . THR A 1 194 ? 25.21773 3.55042  -10.67274 1.000 28.26391 ? 194 THR A OG1 1 
ATOM   1507 C CG2 . THR A 1 194 ? 23.27735 3.80174  -12.08183 1.000 32.14250 ? 194 THR A CG2 1 
ATOM   1508 N N   . ILE A 1 195 ? 27.01359 6.14803  -11.74142 1.000 21.99696 ? 195 ILE A N   1 
ATOM   1509 C CA  . ILE A 1 195 ? 28.30872 6.64387  -11.29634 1.000 23.16665 ? 195 ILE A CA  1 
ATOM   1510 C C   . ILE A 1 195 ? 28.79276 5.87491  -10.07085 1.000 25.15870 ? 195 ILE A C   1 
ATOM   1511 O O   . ILE A 1 195 ? 30.00097 5.68170  -9.89278  1.000 27.82780 ? 195 ILE A O   1 
ATOM   1512 C CB  . ILE A 1 195 ? 28.23414 8.16175  -11.03415 1.000 23.89837 ? 195 ILE A CB  1 
ATOM   1513 C CG1 . ILE A 1 195 ? 29.62764 8.72745  -10.76494 1.000 24.20918 ? 195 ILE A CG1 1 
ATOM   1514 C CG2 . ILE A 1 195 ? 27.26871 8.48137  -9.87919  1.000 23.49663 ? 195 ILE A CG2 1 
ATOM   1515 C CD1 . ILE A 1 195 ? 30.57309 8.58575  -11.93873 1.000 26.41565 ? 195 ILE A CD1 1 
ATOM   1516 N N   . GLY A 1 196 ? 27.86966 5.41460  -9.22107  1.000 25.32760 ? 196 GLY A N   1 
ATOM   1517 C CA  . GLY A 1 196 ? 28.21535 4.65581  -8.03323  1.000 26.42185 ? 196 GLY A CA  1 
ATOM   1518 C C   . GLY A 1 196 ? 28.54398 5.56142  -6.87164  1.000 24.84061 ? 196 GLY A C   1 
ATOM   1519 O O   . GLY A 1 196 ? 27.92734 5.49745  -5.78831  1.000 27.47035 ? 196 GLY A O   1 
ATOM   1520 N N   . SER A 1 197 ? 29.50304 6.44792  -7.09978  1.000 20.69771 ? 197 SER A N   1 
ATOM   1521 C CA  . SER A 1 197 ? 30.00214 7.33611  -6.05772  1.000 21.61332 ? 197 SER A CA  1 
ATOM   1522 C C   . SER A 1 197 ? 28.93673 8.33642  -5.61279  1.000 20.89634 ? 197 SER A C   1 
ATOM   1523 O O   . SER A 1 197 ? 28.11838 8.79011  -6.40775  1.000 23.66391 ? 197 SER A O   1 
ATOM   1524 C CB  . SER A 1 197 ? 31.21979 8.10533  -6.57342  1.000 24.01692 ? 197 SER A CB  1 
ATOM   1525 O OG  . SER A 1 197 ? 32.20502 7.22201  -7.04975  1.000 24.98584 ? 197 SER A OG  1 
ATOM   1526 N N   . PRO A 1 198 ? 28.93132 8.71253  -4.33462  1.000 20.14646 ? 198 PRO A N   1 
ATOM   1527 C CA  . PRO A 1 198 ? 28.14046 9.87733  -3.93073  1.000 20.12124 ? 198 PRO A CA  1 
ATOM   1528 C C   . PRO A 1 198 ? 28.58455 11.11347 -4.70023  1.000 21.97630 ? 198 PRO A C   1 
ATOM   1529 O O   . PRO A 1 198 ? 29.75629 11.25962 -5.05796  1.000 22.74201 ? 198 PRO A O   1 
ATOM   1530 C CB  . PRO A 1 198 ? 28.43987 10.01524 -2.42451  1.000 23.51043 ? 198 PRO A CB  1 
ATOM   1531 C CG  . PRO A 1 198 ? 29.01037 8.67617  -2.01938  1.000 23.38979 ? 198 PRO A CG  1 
ATOM   1532 C CD  . PRO A 1 198 ? 29.72870 8.15416  -3.23609  1.000 22.70366 ? 198 PRO A CD  1 
ATOM   1533 N N   . LEU A 1 199 ? 27.62613 12.00541 -4.96016  1.000 22.10651 ? 199 LEU A N   1 
ATOM   1534 C CA  . LEU A 1 199 ? 27.86232 13.26495 -5.65798  1.000 20.76944 ? 199 LEU A CA  1 
ATOM   1535 C C   . LEU A 1 199 ? 27.52977 14.43338 -4.74056  1.000 21.16174 ? 199 LEU A C   1 
ATOM   1536 O O   . LEU A 1 199 ? 26.45536 14.46041 -4.12784  1.000 21.39752 ? 199 LEU A O   1 
ATOM   1537 C CB  . LEU A 1 199 ? 27.01648 13.34304 -6.93535  1.000 21.72111 ? 199 LEU A CB  1 
ATOM   1538 C CG  . LEU A 1 199 ? 27.19678 12.20982 -7.94080  1.000 21.71232 ? 199 LEU A CG  1 
ATOM   1539 C CD1 . LEU A 1 199 ? 26.28558 12.46913 -9.16613  1.000 25.29294 ? 199 LEU A CD1 1 
ATOM   1540 C CD2 . LEU A 1 199 ? 28.68399 12.04037 -8.33605  1.000 21.89531 ? 199 LEU A CD2 1 
ATOM   1541 N N   . VAL A 1 200 ? 28.43193 15.40946 -4.66879  1.000 21.26880 ? 200 VAL A N   1 
ATOM   1542 C CA  . VAL A 1 200 ? 28.25037 16.59232 -3.83052  1.000 22.02868 ? 200 VAL A CA  1 
ATOM   1543 C C   . VAL A 1 200 ? 28.11933 17.80747 -4.73667  1.000 22.55181 ? 200 VAL A C   1 
ATOM   1544 O O   . VAL A 1 200 ? 29.03314 18.10755 -5.51839  1.000 23.55967 ? 200 VAL A O   1 
ATOM   1545 C CB  . VAL A 1 200 ? 29.41046 16.77156 -2.84064  1.000 22.33369 ? 200 VAL A CB  1 
ATOM   1546 C CG1 . VAL A 1 200 ? 29.24048 18.06850 -2.07163  1.000 24.09383 ? 200 VAL A CG1 1 
ATOM   1547 C CG2 . VAL A 1 200 ? 29.51240 15.57481 -1.88392  1.000 23.54432 ? 200 VAL A CG2 1 
ATOM   1548 N N   . PHE A 1 201 ? 26.99058 18.51534 -4.61721  1.000 22.37157 ? 201 PHE A N   1 
ATOM   1549 C CA  . PHE A 1 201 ? 26.58707 19.64869 -5.43555  1.000 23.62863 ? 201 PHE A CA  1 
ATOM   1550 C C   . PHE A 1 201 ? 26.64552 20.94229 -4.64851  1.000 25.12978 ? 201 PHE A C   1 
ATOM   1551 O O   . PHE A 1 201 ? 26.20631 20.98159 -3.49460  1.000 27.08348 ? 201 PHE A O   1 
ATOM   1552 C CB  . PHE A 1 201 ? 25.16362 19.45427 -5.95953  1.000 23.32184 ? 201 PHE A CB  1 
ATOM   1553 C CG  . PHE A 1 201 ? 25.00639 18.21810 -6.77965  1.000 23.62484 ? 201 PHE A CG  1 
ATOM   1554 C CD1 . PHE A 1 201 ? 25.30434 18.23221 -8.13198  1.000 24.05625 ? 201 PHE A CD1 1 
ATOM   1555 C CD2 . PHE A 1 201 ? 24.59308 17.03259 -6.19929  1.000 25.36448 ? 201 PHE A CD2 1 
ATOM   1556 C CE1 . PHE A 1 201 ? 25.18261 17.08420 -8.89340  1.000 24.40031 ? 201 PHE A CE1 1 
ATOM   1557 C CE2 . PHE A 1 201 ? 24.46278 15.88300 -6.95167  1.000 23.98496 ? 201 PHE A CE2 1 
ATOM   1558 C CZ  . PHE A 1 201 ? 24.76198 15.90808 -8.31450  1.000 24.01677 ? 201 PHE A CZ  1 
ATOM   1559 N N   . PRO A 1 202 ? 27.15814 22.00793 -5.24589  1.000 25.66508 ? 202 PRO A N   1 
ATOM   1560 C CA  . PRO A 1 202 ? 27.11910 23.32131 -4.60452  1.000 27.02744 ? 202 PRO A CA  1 
ATOM   1561 C C   . PRO A 1 202 ? 25.74546 23.95724 -4.74784  1.000 29.02473 ? 202 PRO A C   1 
ATOM   1562 O O   . PRO A 1 202 ? 24.84202 23.42827 -5.39755  1.000 27.15773 ? 202 PRO A O   1 
ATOM   1563 C CB  . PRO A 1 202 ? 28.17365 24.11304 -5.37927  1.000 26.99895 ? 202 PRO A CB  1 
ATOM   1564 C CG  . PRO A 1 202 ? 28.04716 23.55600 -6.75571  1.000 27.15677 ? 202 PRO A CG  1 
ATOM   1565 C CD  . PRO A 1 202 ? 27.74147 22.07895 -6.59920  1.000 25.38705 ? 202 PRO A CD  1 
ATOM   1566 N N   . LYS A 1 203 ? 25.60160 25.10419 -4.08973  1.000 32.04373 ? 203 LYS A N   1 
ATOM   1567 C CA  . LYS A 1 203 ? 24.43595 25.94978 -4.27576  1.000 33.33831 ? 203 LYS A CA  1 
ATOM   1568 C C   . LYS A 1 203 ? 24.27239 26.27251 -5.74950  1.000 30.83557 ? 203 LYS A C   1 
ATOM   1569 O O   . LYS A 1 203 ? 25.25377 26.37769 -6.48870  1.000 29.72097 ? 203 LYS A O   1 
ATOM   1570 C CB  . LYS A 1 203 ? 24.59879 27.24853 -3.48983  1.000 39.38005 ? 203 LYS A CB  1 
ATOM   1571 C CG  . LYS A 1 203 ? 23.43841 27.62308 -2.59522  0.800 43.10544 ? 203 LYS A CG  1 
ATOM   1572 C CD  . LYS A 1 203 ? 23.51919 29.09538 -2.20073  0.700 44.69660 ? 203 LYS A CD  1 
ATOM   1573 C CE  . LYS A 1 203 ? 24.72296 29.39457 -1.31802  0.700 47.48078 ? 203 LYS A CE  1 
ATOM   1574 N NZ  . LYS A 1 203 ? 26.04013 29.51002 -2.01437  0.600 48.24624 ? 203 LYS A NZ  1 
ATOM   1575 N N   . HIS A 1 204 ? 23.01985 26.42005 -6.17033  1.000 30.40391 ? 204 HIS A N   1 
ATOM   1576 C CA  . HIS A 1 204 ? 22.57751 26.83083 -7.49658  1.000 32.00111 ? 204 HIS A CA  1 
ATOM   1577 C C   . HIS A 1 204 ? 22.62422 25.69991 -8.51927  1.000 30.36468 ? 204 HIS A C   1 
ATOM   1578 O O   . HIS A 1 204 ? 22.10186 25.87870 -9.62518  1.000 34.90313 ? 204 HIS A O   1 
ATOM   1579 C CB  . HIS A 1 204 ? 23.36481 28.02962 -8.05710  1.000 34.75316 ? 204 HIS A CB  1 
ATOM   1580 C CG  . HIS A 1 204 ? 23.42835 29.19033 -7.12149  1.000 37.80995 ? 204 HIS A CG  1 
ATOM   1581 N ND1 . HIS A 1 204 ? 22.30552 29.87157 -6.70469  1.000 40.27378 ? 204 HIS A ND1 1 
ATOM   1582 C CD2 . HIS A 1 204 ? 24.47856 29.78109 -6.50742  1.000 40.59153 ? 204 HIS A CD2 1 
ATOM   1583 C CE1 . HIS A 1 204 ? 22.66391 30.83999 -5.88220  1.000 41.09721 ? 204 HIS A CE1 1 
ATOM   1584 N NE2 . HIS A 1 204 ? 23.97748 30.80902 -5.74997  1.000 41.82207 ? 204 HIS A NE2 1 
ATOM   1585 N N   . HIS A 1 205 ? 23.23213 24.55659 -8.21739  1.000 27.41293 ? 205 HIS A N   1 
ATOM   1586 C CA  . HIS A 1 205 ? 23.05818 23.39195 -9.07024  1.000 26.99220 ? 205 HIS A CA  1 
ATOM   1587 C C   . HIS A 1 205 ? 21.70274 22.75724 -8.79776  1.000 27.50610 ? 205 HIS A C   1 
ATOM   1588 O O   . HIS A 1 205 ? 21.24700 22.68267 -7.65171  1.000 30.37784 ? 205 HIS A O   1 
ATOM   1589 C CB  . HIS A 1 205 ? 24.16905 22.36657 -8.85550  1.000 26.51019 ? 205 HIS A CB  1 
ATOM   1590 C CG  . HIS A 1 205 ? 25.47818 22.76914 -9.44872  1.000 26.43306 ? 205 HIS A CG  1 
ATOM   1591 N ND1 . HIS A 1 205 ? 26.39364 21.85446 -9.92412  1.000 26.96625 ? 205 HIS A ND1 1 
ATOM   1592 C CD2 . HIS A 1 205 ? 26.01850 23.99216 -9.66457  1.000 29.29740 ? 205 HIS A CD2 1 
ATOM   1593 C CE1 . HIS A 1 205 ? 27.44663 22.49769 -10.39932 1.000 30.75246 ? 205 HIS A CE1 1 
ATOM   1594 N NE2 . HIS A 1 205 ? 27.24502 23.79570 -10.25288 1.000 31.74858 ? 205 HIS A NE2 1 
ATOM   1595 N N   . VAL A 1 206 ? 21.06288 22.29664 -9.86409  1.000 25.78183 ? 206 VAL A N   1 
ATOM   1596 C CA  . VAL A 1 206 ? 19.74979 21.67464 -9.80068  1.000 26.83464 ? 206 VAL A CA  1 
ATOM   1597 C C   . VAL A 1 206 ? 19.87579 20.25239 -10.31822 1.000 25.51440 ? 206 VAL A C   1 
ATOM   1598 O O   . VAL A 1 206 ? 20.37087 20.03052 -11.42699 1.000 30.02023 ? 206 VAL A O   1 
ATOM   1599 C CB  . VAL A 1 206 ? 18.70931 22.45666 -10.61510 1.000 31.55283 ? 206 VAL A CB  1 
ATOM   1600 C CG1 . VAL A 1 206 ? 17.38272 21.73672 -10.59461 1.000 32.87230 ? 206 VAL A CG1 1 
ATOM   1601 C CG2 . VAL A 1 206 ? 18.57725 23.87040 -10.08256 1.000 32.31616 ? 206 VAL A CG2 1 
ATOM   1602 N N   . VAL A 1 207 ? 19.44248 19.29449 -9.51293  1.000 23.91355 ? 207 VAL A N   1 
ATOM   1603 C CA  . VAL A 1 207 ? 19.42649 17.89025 -9.88096  1.000 24.37642 ? 207 VAL A CA  1 
ATOM   1604 C C   . VAL A 1 207 ? 17.97035 17.50920 -10.05647 1.000 25.06119 ? 207 VAL A C   1 
ATOM   1605 O O   . VAL A 1 207 ? 17.15913 17.68208 -9.13721  1.000 27.58325 ? 207 VAL A O   1 
ATOM   1606 C CB  . VAL A 1 207 ? 20.11624 17.02369 -8.81686  1.000 26.00014 ? 207 VAL A CB  1 
ATOM   1607 C CG1 . VAL A 1 207 ? 20.04650 15.55306 -9.19138  1.000 29.47417 ? 207 VAL A CG1 1 
ATOM   1608 C CG2 . VAL A 1 207 ? 21.54444 17.46582 -8.67910  1.000 28.09953 ? 207 VAL A CG2 1 
ATOM   1609 N N   . SER A 1 208 ? 17.63140 17.04291 -11.25429 1.000 25.84361 ? 208 SER A N   1 
ATOM   1610 C CA  . SER A 1 208 ? 16.26742 16.70693 -11.62537 1.000 26.54888 ? 208 SER A CA  1 
ATOM   1611 C C   . SER A 1 208 ? 16.16787 15.20094 -11.81355 1.000 28.74112 ? 208 SER A C   1 
ATOM   1612 O O   . SER A 1 208 ? 16.97696 14.61153 -12.53279 1.000 28.88458 ? 208 SER A O   1 
ATOM   1613 C CB  . SER A 1 208 ? 15.87053 17.44815 -12.90796 1.000 30.88926 ? 208 SER A CB  1 
ATOM   1614 O OG  . SER A 1 208 ? 14.72072 16.88118 -13.49503 1.000 36.76791 ? 208 SER A OG  1 
ATOM   1615 N N   . LEU A 1 209 ? 15.19815 14.57841 -11.14834 1.000 29.25508 ? 209 LEU A N   1 
ATOM   1616 C CA  . LEU A 1 209 ? 14.90433 13.16186 -11.33713 1.000 33.86346 ? 209 LEU A CA  1 
ATOM   1617 C C   . LEU A 1 209 ? 13.63526 13.03237 -12.16891 1.000 35.27932 ? 209 LEU A C   1 
ATOM   1618 O O   . LEU A 1 209 ? 12.59680 13.58701 -11.79902 1.000 37.46169 ? 209 LEU A O   1 
ATOM   1619 C CB  . LEU A 1 209 ? 14.73130 12.44757 -9.99523  1.000 34.09849 ? 209 LEU A CB  1 
ATOM   1620 C CG  . LEU A 1 209 ? 15.92208 12.50025 -9.03643  1.000 33.86857 ? 209 LEU A CG  1 
ATOM   1621 C CD1 . LEU A 1 209 ? 15.66577 11.65498 -7.78314  1.000 34.68007 ? 209 LEU A CD1 1 
ATOM   1622 C CD2 . LEU A 1 209 ? 17.20088 12.06702 -9.73087  1.000 33.43089 ? 209 LEU A CD2 1 
ATOM   1623 N N   . GLN A 1 210 ? 13.71544 12.29254 -13.27861 1.000 36.22654 ? 210 GLN A N   1 
ATOM   1624 C CA  . GLN A 1 210 ? 12.62351 12.22858 -14.24092 1.000 37.85403 ? 210 GLN A CA  1 
ATOM   1625 C C   . GLN A 1 210 ? 12.23207 10.79683 -14.58748 1.000 37.66573 ? 210 GLN A C   1 
ATOM   1626 O O   . GLN A 1 210 ? 13.09356 9.95013  -14.84333 1.000 37.14200 ? 210 GLN A O   1 
ATOM   1627 C CB  . GLN A 1 210 ? 13.00782 12.97534 -15.52219 1.000 42.75897 ? 210 GLN A CB  1 
ATOM   1628 C CG  . GLN A 1 210 ? 13.27549 14.44906 -15.29685 1.000 45.21773 ? 210 GLN A CG  1 
ATOM   1629 C CD  . GLN A 1 210 ? 14.04373 15.07902 -16.43158 1.000 48.05775 ? 210 GLN A CD  1 
ATOM   1630 O OE1 . GLN A 1 210 ? 14.07816 14.54664 -17.54206 1.000 48.14655 ? 210 GLN A OE1 1 
ATOM   1631 N NE2 . GLN A 1 210 ? 14.67177 16.22041 -16.16006 1.000 50.29501 ? 210 GLN A NE2 1 
ATOM   1632 N N   . PRO A 1 211 ? 10.93439 10.51660 -14.66877 1.000 41.67066 ? 211 PRO A N   1 
ATOM   1633 C CA  . PRO A 1 211 ? 10.49223 9.13396  -14.85256 1.000 43.07388 ? 211 PRO A CA  1 
ATOM   1634 C C   . PRO A 1 211 ? 10.83548 8.61598  -16.23602 1.000 46.63158 ? 211 PRO A C   1 
ATOM   1635 O O   . PRO A 1 211 ? 10.97214 9.37558  -17.19965 1.000 46.62244 ? 211 PRO A O   1 
ATOM   1636 C CB  . PRO A 1 211 ? 8.97336  9.21198  -14.66007 1.000 43.37401 ? 211 PRO A CB  1 
ATOM   1637 C CG  . PRO A 1 211 ? 8.69547  10.59140 -14.11734 1.000 44.39212 ? 211 PRO A CG  1 
ATOM   1638 C CD  . PRO A 1 211 ? 9.80291  11.45432 -14.62785 1.000 42.91124 ? 211 PRO A CD  1 
ATOM   1639 N N   . VAL A 1 212 ? 10.96938 7.29745  -16.31757 1.000 48.23567 ? 212 VAL A N   1 
ATOM   1640 C CA  . VAL A 1 212 ? 11.23749 6.59645  -17.56305 1.000 49.62151 ? 212 VAL A CA  1 
ATOM   1641 C C   . VAL A 1 212 ? 10.03342 5.76764  -17.99558 1.000 53.62321 ? 212 VAL A C   1 
ATOM   1642 O O   . VAL A 1 212 ? 9.59951  5.83838  -19.14665 1.000 54.99017 ? 212 VAL A O   1 
ATOM   1643 C CB  . VAL A 1 212 ? 12.50385 5.72096  -17.43637 1.000 47.45849 ? 212 VAL A CB  1 
ATOM   1644 C CG1 . VAL A 1 212 ? 12.63153 4.78517  -18.63060 1.000 49.25130 ? 212 VAL A CG1 1 
ATOM   1645 C CG2 . VAL A 1 212 ? 13.73810 6.60410  -17.31080 1.000 46.44292 ? 212 VAL A CG2 1 
ATOM   1646 N N   . ASN A 1 213 ? 9.47135  4.98540  -17.07556 1.000 55.57620 ? 213 ASN A N   1 
ATOM   1647 C CA  . ASN A 1 213 ? 8.24122  4.24887  -17.33651 1.000 57.96496 ? 213 ASN A CA  1 
ATOM   1648 C C   . ASN A 1 213 ? 7.19621  4.57013  -16.27744 1.000 59.21249 ? 213 ASN A C   1 
ATOM   1649 O O   . ASN A 1 213 ? 6.32422  5.41516  -16.49801 1.000 61.00613 ? 213 ASN A O   1 
ATOM   1650 C CB  . ASN A 1 213 ? 8.50831  2.74336  -17.38990 1.000 59.78243 ? 213 ASN A CB  1 
ATOM   1651 C CG  . ASN A 1 213 ? 8.69842  2.23879  -18.80730 1.000 62.95710 ? 213 ASN A CG  1 
ATOM   1652 O OD1 . ASN A 1 213 ? 8.16666  2.81400  -19.75995 1.000 65.09436 ? 213 ASN A OD1 1 
ATOM   1653 N ND2 . ASN A 1 213 ? 9.45761  1.15960  -18.95586 1.000 63.87579 ? 213 ASN A ND2 1 
ATOM   1654 N N   . ASP A 1 214 ? 7.27730  3.90325  -15.12929 1.000 60.37960 ? 214 ASP A N   1 
ATOM   1655 C CA  . ASP A 1 214 ? 6.36087  4.18393  -14.03315 1.000 61.57028 ? 214 ASP A CA  1 
ATOM   1656 C C   . ASP A 1 214 ? 6.49431  5.63530  -13.58539 1.000 60.80115 ? 214 ASP A C   1 
ATOM   1657 O O   . ASP A 1 214 ? 7.59693  6.18680  -13.52433 1.000 61.05053 ? 214 ASP A O   1 
ATOM   1658 C CB  . ASP A 1 214 ? 6.63503  3.23301  -12.86481 1.000 62.75591 ? 214 ASP A CB  1 
ATOM   1659 C CG  . ASP A 1 214 ? 5.83576  3.58145  -11.62485 1.000 64.79893 ? 214 ASP A CG  1 
ATOM   1660 O OD1 . ASP A 1 214 ? 4.63516  3.89788  -11.76151 1.000 65.82788 ? 214 ASP A OD1 1 
ATOM   1661 O OD2 . ASP A 1 214 ? 6.40449  3.52492  -10.51235 1.000 65.39524 ? 214 ASP A OD2 1 
ATOM   1662 N N   . LYS A 1 215 ? 5.35532  6.25832  -13.28156 1.000 58.92743 ? 215 LYS A N   1 
ATOM   1663 C CA  . LYS A 1 215 ? 5.30882  7.65670  -12.87568 1.000 57.60976 ? 215 LYS A CA  1 
ATOM   1664 C C   . LYS A 1 215 ? 4.91591  7.83498  -11.41225 1.000 53.92418 ? 215 LYS A C   1 
ATOM   1665 O O   . LYS A 1 215 ? 4.75134  8.97303  -10.96133 1.000 53.59668 ? 215 LYS A O   1 
ATOM   1666 C CB  . LYS A 1 215 ? 4.34453  8.43503  -13.77266 1.000 60.86737 ? 215 LYS A CB  1 
ATOM   1667 C CG  . LYS A 1 215 ? 4.42748  8.08982  -15.25541 1.000 63.24329 ? 215 LYS A CG  1 
ATOM   1668 C CD  . LYS A 1 215 ? 5.68047  8.64806  -15.92153 1.000 64.32412 ? 215 LYS A CD  1 
ATOM   1669 C CE  . LYS A 1 215 ? 5.61371  8.47652  -17.43827 1.000 65.15145 ? 215 LYS A CE  1 
ATOM   1670 N NZ  . LYS A 1 215 ? 6.85060  8.94651  -18.13000 1.000 65.88039 ? 215 LYS A NZ  1 
ATOM   1671 N N   . ASP A 1 216 ? 4.75439  6.74642  -10.66408 1.000 52.66206 ? 216 ASP A N   1 
ATOM   1672 C CA  . ASP A 1 216 ? 4.40078  6.79963  -9.25037  1.000 52.53398 ? 216 ASP A CA  1 
ATOM   1673 C C   . ASP A 1 216 ? 5.63011  6.48100  -8.40739  1.000 49.88371 ? 216 ASP A C   1 
ATOM   1674 O O   . ASP A 1 216 ? 6.33339  5.50030  -8.66889  1.000 51.09487 ? 216 ASP A O   1 
ATOM   1675 C CB  . ASP A 1 216 ? 3.27121  5.82041  -8.92875  1.000 54.20184 ? 216 ASP A CB  1 
ATOM   1676 C CG  . ASP A 1 216 ? 2.04723  6.02913  -9.79990  1.000 56.42113 ? 216 ASP A CG  1 
ATOM   1677 O OD1 . ASP A 1 216 ? 1.82746  7.16260  -10.28024 1.000 55.94519 ? 216 ASP A OD1 1 
ATOM   1678 O OD2 . ASP A 1 216 ? 1.30007  5.05197  -10.00301 1.000 57.76611 ? 216 ASP A OD2 1 
ATOM   1679 N N   . PHE A 1 217 ? 5.88343  7.30142  -7.39322  1.000 46.46527 ? 217 PHE A N   1 
ATOM   1680 C CA  . PHE A 1 217 ? 7.06757  7.14353  -6.56246  1.000 43.15853 ? 217 PHE A CA  1 
ATOM   1681 C C   . PHE A 1 217 ? 6.68734  7.35817  -5.11058  1.000 39.61938 ? 217 PHE A C   1 
ATOM   1682 O O   . PHE A 1 217 ? 5.72225  8.05389  -4.80331  1.000 41.71336 ? 217 PHE A O   1 
ATOM   1683 C CB  . PHE A 1 217 ? 8.16834  8.14285  -6.94139  1.000 41.54181 ? 217 PHE A CB  1 
ATOM   1684 C CG  . PHE A 1 217 ? 8.54195  8.11465  -8.39141  1.000 44.35032 ? 217 PHE A CG  1 
ATOM   1685 C CD1 . PHE A 1 217 ? 7.82549  8.84406  -9.32353  1.000 43.21135 ? 217 PHE A CD1 1 
ATOM   1686 C CD2 . PHE A 1 217 ? 9.63017  7.37114  -8.82039  1.000 44.32916 ? 217 PHE A CD2 1 
ATOM   1687 C CE1 . PHE A 1 217 ? 8.18341  8.81899  -10.66797 1.000 44.08417 ? 217 PHE A CE1 1 
ATOM   1688 C CE2 . PHE A 1 217 ? 9.99523  7.34144  -10.15249 1.000 43.51876 ? 217 PHE A CE2 1 
ATOM   1689 C CZ  . PHE A 1 217 ? 9.27188  8.06605  -11.07999 1.000 42.59961 ? 217 PHE A CZ  1 
ATOM   1690 N N   . GLN A 1 218 ? 7.48165  6.78653  -4.21231  1.000 35.22853 ? 218 GLN A N   1 
ATOM   1691 C CA  . GLN A 1 218 ? 7.41945  7.14741  -2.80695  1.000 34.11199 ? 218 GLN A CA  1 
ATOM   1692 C C   . GLN A 1 218 ? 8.48608  8.20760  -2.56620  1.000 30.16471 ? 218 GLN A C   1 
ATOM   1693 O O   . GLN A 1 218 ? 9.66955  7.96200  -2.80749  1.000 31.10325 ? 218 GLN A O   1 
ATOM   1694 C CB  . GLN A 1 218 ? 7.64344  5.92517  -1.91828  1.000 41.54408 ? 218 GLN A CB  1 
ATOM   1695 C CG  . GLN A 1 218 ? 7.17729  6.08881  -0.48055  1.000 44.71472 ? 218 GLN A CG  1 
ATOM   1696 C CD  . GLN A 1 218 ? 5.67354  5.88723  -0.32243  0.700 45.61007 ? 218 GLN A CD  1 
ATOM   1697 O OE1 . GLN A 1 218 ? 5.03877  5.21004  -1.13032  0.600 47.67776 ? 218 GLN A OE1 1 
ATOM   1698 N NE2 . GLN A 1 218 ? 5.10145  6.48011  0.71784   0.600 44.30751 ? 218 GLN A NE2 1 
ATOM   1699 N N   . ILE A 1 219 ? 8.07191  9.39200  -2.12624  1.000 29.66141 ? 219 ILE A N   1 
ATOM   1700 C CA  . ILE A 1 219 ? 8.99665  10.48774 -1.86200  1.000 30.95270 ? 219 ILE A CA  1 
ATOM   1701 C C   . ILE A 1 219 ? 8.97502  10.78117 -0.37144  1.000 34.16473 ? 219 ILE A C   1 
ATOM   1702 O O   . ILE A 1 219 ? 7.90356  10.96677 0.21860   1.000 35.31070 ? 219 ILE A O   1 
ATOM   1703 C CB  . ILE A 1 219 ? 8.65131  11.74501 -2.67590  1.000 32.05562 ? 219 ILE A CB  1 
ATOM   1704 C CG1 . ILE A 1 219 ? 8.67033  11.42306 -4.17311  1.000 32.42664 ? 219 ILE A CG1 1 
ATOM   1705 C CG2 . ILE A 1 219 ? 9.62899  12.85553 -2.36112  1.000 34.89417 ? 219 ILE A CG2 1 
ATOM   1706 C CD1 . ILE A 1 219 ? 8.05395  12.50240 -5.05210  1.000 32.78085 ? 219 ILE A CD1 1 
ATOM   1707 N N   . SER A 1 220 ? 10.15285 10.81470 0.23445   1.000 33.35547 ? 220 SER A N   1 
ATOM   1708 C CA  . SER A 1 220 ? 10.28018 11.16838 1.63767   1.000 34.64280 ? 220 SER A CA  1 
ATOM   1709 C C   . SER A 1 220 ? 10.96190 12.52405 1.75904   1.000 33.28740 ? 220 SER A C   1 
ATOM   1710 O O   . SER A 1 220 ? 11.80426 12.89430 0.93434   1.000 35.04447 ? 220 SER A O   1 
ATOM   1711 C CB  . SER A 1 220 ? 11.08667 10.12042 2.40025   1.000 37.92962 ? 220 SER A CB  1 
ATOM   1712 O OG  . SER A 1 220 ? 12.48099 10.32352 2.20392   1.000 39.38076 ? 220 SER A OG  1 
ATOM   1713 N N   . VAL A 1 221 ? 10.57599 13.26812 2.78563   1.000 30.68107 ? 221 VAL A N   1 
ATOM   1714 C CA  . VAL A 1 221 ? 11.26148 14.48097 3.18879   1.000 31.29725 ? 221 VAL A CA  1 
ATOM   1715 C C   . VAL A 1 221 ? 11.42115 14.34939 4.69065   1.000 30.68066 ? 221 VAL A C   1 
ATOM   1716 O O   . VAL A 1 221 ? 10.43314 14.44006 5.42240   1.000 32.40633 ? 221 VAL A O   1 
ATOM   1717 C CB  . VAL A 1 221 ? 10.48588 15.75182 2.83767   1.000 34.53650 ? 221 VAL A CB  1 
ATOM   1718 C CG1 . VAL A 1 221 ? 11.14428 16.96477 3.49306   1.000 35.16097 ? 221 VAL A CG1 1 
ATOM   1719 C CG2 . VAL A 1 221 ? 10.40684 15.92392 1.32035   1.000 34.81904 ? 221 VAL A CG2 1 
ATOM   1720 N N   . ASP A 1 222 ? 12.64470 14.09073 5.15145   1.000 29.07973 ? 222 ASP A N   1 
ATOM   1721 C CA  . ASP A 1 222 ? 12.88894 13.80205 6.57987   1.000 31.28986 ? 222 ASP A CA  1 
ATOM   1722 C C   . ASP A 1 222 ? 12.00257 12.61108 6.95434   1.000 33.34315 ? 222 ASP A C   1 
ATOM   1723 O O   . ASP A 1 222 ? 12.02821 11.58001 6.26453   1.000 35.91180 ? 222 ASP A O   1 
ATOM   1724 C CB  . ASP A 1 222 ? 12.69291 15.08104 7.37843   1.000 31.71673 ? 222 ASP A CB  1 
ATOM   1725 C CG  . ASP A 1 222 ? 13.76022 16.11168 7.06662   1.000 28.67339 ? 222 ASP A CG  1 
ATOM   1726 O OD1 . ASP A 1 222 ? 14.84759 15.70135 6.64250   1.000 27.92535 ? 222 ASP A OD1 1 
ATOM   1727 O OD2 . ASP A 1 222 ? 13.52040 17.31818 7.23829   1.000 29.71896 ? 222 ASP A OD2 1 
ATOM   1728 N N   . HIS A 1 223 ? 11.22169 12.65802 8.04106   1.000 35.91221 ? 223 HIS A N   1 
ATOM   1729 C CA  . HIS A 1 223 ? 10.49045 11.42212 8.29872   1.000 43.91542 ? 223 HIS A CA  1 
ATOM   1730 C C   . HIS A 1 223 ? 9.24588  11.23121 7.42816   1.000 45.33272 ? 223 HIS A C   1 
ATOM   1731 O O   . HIS A 1 223 ? 8.69414  10.12258 7.40103   1.000 48.28244 ? 223 HIS A O   1 
ATOM   1732 C CB  . HIS A 1 223 ? 10.06706 11.30947 9.76201   1.000 48.25799 ? 223 HIS A CB  1 
ATOM   1733 C CG  . HIS A 1 223 ? 9.46177  9.98265  10.08157  0.700 51.74001 ? 223 HIS A CG  1 
ATOM   1734 N ND1 . HIS A 1 223 ? 10.05669 8.79835  9.70386   0.700 52.66569 ? 223 HIS A ND1 1 
ATOM   1735 C CD2 . HIS A 1 223 ? 8.28866  9.64769  10.66610  0.700 53.72013 ? 223 HIS A CD2 1 
ATOM   1736 C CE1 . HIS A 1 223 ? 9.29429  7.78864  10.07942  0.700 52.57343 ? 223 HIS A CE1 1 
ATOM   1737 N NE2 . HIS A 1 223 ? 8.21533  8.27647  10.66521  0.700 53.36581 ? 223 HIS A NE2 1 
ATOM   1738 N N   . LEU A 1 224 ? 8.80428  12.24145 6.69471   1.000 43.55207 ? 224 LEU A N   1 
ATOM   1739 C CA  . LEU A 1 224 ? 7.47289  12.23249 6.09911   1.000 42.69261 ? 224 LEU A CA  1 
ATOM   1740 C C   . LEU A 1 224 ? 7.53817  11.62932 4.70237   1.000 44.79933 ? 224 LEU A C   1 
ATOM   1741 O O   . LEU A 1 224 ? 8.19910  12.18302 3.81857   1.000 48.35166 ? 224 LEU A O   1 
ATOM   1742 C CB  . LEU A 1 224 ? 6.92425  13.65584 6.07239   1.000 43.90907 ? 224 LEU A CB  1 
ATOM   1743 C CG  . LEU A 1 224 ? 7.09501  14.25821 7.47300   1.000 47.24065 ? 224 LEU A CG  1 
ATOM   1744 C CD1 . LEU A 1 224 ? 6.86027  15.76392 7.50564   1.000 47.93217 ? 224 LEU A CD1 1 
ATOM   1745 C CD2 . LEU A 1 224 ? 6.18657  13.54455 8.47864   1.000 47.76013 ? 224 LEU A CD2 1 
ATOM   1746 N N   . SER A 1 225 ? 6.86898  10.48998 4.51681   1.000 44.09550 ? 225 SER A N   1 
ATOM   1747 C CA  . SER A 1 225 ? 6.91721  9.72028  3.27851   1.000 48.12710 ? 225 SER A CA  1 
ATOM   1748 C C   . SER A 1 225 ? 5.51342  9.59302  2.71059   1.000 49.21552 ? 225 SER A C   1 
ATOM   1749 O O   . SER A 1 225 ? 4.59871  9.12993  3.40212   1.000 50.01200 ? 225 SER A O   1 
ATOM   1750 C CB  . SER A 1 225 ? 7.51185  8.32771  3.51217   1.000 50.98068 ? 225 SER A CB  1 
ATOM   1751 O OG  . SER A 1 225 ? 7.67324  7.62980  2.28388   1.000 52.75130 ? 225 SER A OG  1 
ATOM   1752 N N   . ILE A 1 226 ? 5.34559  9.99269  1.45282   1.000 50.29425 ? 226 ILE A N   1 
ATOM   1753 C CA  . ILE A 1 226 ? 4.03039  10.03246 0.82653   1.000 52.19755 ? 226 ILE A CA  1 
ATOM   1754 C C   . ILE A 1 226 ? 4.12973  9.47817  -0.59018  1.000 52.06942 ? 226 ILE A C   1 
ATOM   1755 O O   . ILE A 1 226 ? 5.09818  9.74027  -1.31518  1.000 49.72689 ? 226 ILE A O   1 
ATOM   1756 C CB  . ILE A 1 226 ? 3.43406  11.46092 0.82964   1.000 54.73089 ? 226 ILE A CB  1 
ATOM   1757 C CG1 . ILE A 1 226 ? 4.28544  12.42211 -0.00286  1.000 55.47772 ? 226 ILE A CG1 1 
ATOM   1758 C CG2 . ILE A 1 226 ? 3.28263  11.98978 2.25951   1.000 55.04337 ? 226 ILE A CG2 1 
ATOM   1759 C CD1 . ILE A 1 226 ? 5.45360  13.07032 0.74511   1.000 54.89748 ? 226 ILE A CD1 1 
ATOM   1760 N N   . LEU A 1 227 ? 3.12888  8.69320  -0.97528  1.000 51.84459 ? 227 LEU A N   1 
ATOM   1761 C CA  . LEU A 1 227 ? 3.06593  8.18184  -2.33523  1.000 52.73726 ? 227 LEU A CA  1 
ATOM   1762 C C   . LEU A 1 227 ? 2.66470  9.30429  -3.27918  1.000 54.14753 ? 227 LEU A C   1 
ATOM   1763 O O   . LEU A 1 227 ? 1.62363  9.94386  -3.09250  1.000 54.31065 ? 227 LEU A O   1 
ATOM   1764 C CB  . LEU A 1 227 ? 2.07473  7.02805  -2.43693  1.000 53.17557 ? 227 LEU A CB  1 
ATOM   1765 C CG  . LEU A 1 227 ? 1.89358  6.58913  -3.89125  1.000 53.40791 ? 227 LEU A CG  1 
ATOM   1766 C CD1 . LEU A 1 227 ? 3.10783  5.79776  -4.36930  1.000 53.13969 ? 227 LEU A CD1 1 
ATOM   1767 C CD2 . LEU A 1 227 ? 0.61079  5.80371  -4.08506  1.000 53.16150 ? 227 LEU A CD2 1 
ATOM   1768 N N   . HIS A 1 228 ? 3.48207  9.53433  -4.29923  1.000 53.45604 ? 228 HIS A N   1 
ATOM   1769 C CA  . HIS A 1 228 ? 3.25838  10.59459 -5.27145  1.000 54.52856 ? 228 HIS A CA  1 
ATOM   1770 C C   . HIS A 1 228 ? 2.85619  9.97140  -6.60097  1.000 53.06509 ? 228 HIS A C   1 
ATOM   1771 O O   . HIS A 1 228 ? 3.59559  9.15026  -7.15444  1.000 50.44115 ? 228 HIS A O   1 
ATOM   1772 C CB  . HIS A 1 228 ? 4.51319  11.44713 -5.42706  1.000 55.87662 ? 228 HIS A CB  1 
ATOM   1773 C CG  . HIS A 1 228 ? 4.56178  12.62983 -4.51316  1.000 56.59445 ? 228 HIS A CG  1 
ATOM   1774 N ND1 . HIS A 1 228 ? 5.19933  12.60671 -3.29168  1.000 58.35331 ? 228 HIS A ND1 1 
ATOM   1775 C CD2 . HIS A 1 228 ? 4.06006  13.87830 -4.65069  1.000 56.50792 ? 228 HIS A CD2 1 
ATOM   1776 C CE1 . HIS A 1 228 ? 5.08912  13.79307 -2.71896  1.000 58.54940 ? 228 HIS A CE1 1 
ATOM   1777 N NE2 . HIS A 1 228 ? 4.39578  14.58042 -3.51994  1.000 58.05700 ? 228 HIS A NE2 1 
ATOM   1778 N N   . ARG A 1 229 ? 1.69201  10.36298 -7.11145  1.000 53.84901 ? 229 ARG A N   1 
ATOM   1779 C CA  . ARG A 1 229 ? 1.16712  9.82300  -8.35359  1.000 52.83362 ? 229 ARG A CA  1 
ATOM   1780 C C   . ARG A 1 229 ? 1.21844  10.87440 -9.45367  1.000 51.09456 ? 229 ARG A C   1 
ATOM   1781 O O   . ARG A 1 229 ? 1.04601  12.07297 -9.20534  1.000 48.63822 ? 229 ARG A O   1 
ATOM   1782 C CB  . ARG A 1 229 ? -0.27130 9.32314  -8.17709  1.000 55.27049 ? 229 ARG A CB  1 
ATOM   1783 C CG  . ARG A 1 229 ? -0.40661 8.09275  -7.28892  0.800 56.80594 ? 229 ARG A CG  1 
ATOM   1784 C CD  . ARG A 1 229 ? -1.86966 7.75620  -7.06053  0.700 59.50533 ? 229 ARG A CD  1 
ATOM   1785 N NE  . ARG A 1 229 ? -2.13573 6.33222  -7.22051  0.600 62.58943 ? 229 ARG A NE  1 
ATOM   1786 C CZ  . ARG A 1 229 ? -2.45567 5.51115  -6.23019  0.600 64.59133 ? 229 ARG A CZ  1 
ATOM   1787 N NH1 . ARG A 1 229 ? -2.57848 5.94341  -4.98631  0.600 65.76671 ? 229 ARG A NH1 1 
ATOM   1788 N NH2 . ARG A 1 229 ? -2.66786 4.22556  -6.49667  0.600 65.11211 ? 229 ARG A NH2 1 
ATOM   1789 N N   . ASP A 1 230 ? 1.46048  10.39793 -10.67664 1.000 51.70036 ? 230 ASP A N   1 
ATOM   1790 C CA  . ASP A 1 230 ? 1.54691  11.24414 -11.86495 1.000 53.08533 ? 230 ASP A CA  1 
ATOM   1791 C C   . ASP A 1 230 ? 2.66741  12.27069 -11.73116 1.000 51.26901 ? 230 ASP A C   1 
ATOM   1792 O O   . ASP A 1 230 ? 2.52292  13.43162 -12.11798 1.000 50.20046 ? 230 ASP A O   1 
ATOM   1793 C CB  . ASP A 1 230 ? 0.21153  11.92942 -12.16007 1.000 55.39792 ? 230 ASP A CB  1 
ATOM   1794 C CG  . ASP A 1 230 ? 0.14033  12.46737 -13.57010 1.000 60.01340 ? 230 ASP A CG  1 
ATOM   1795 O OD1 . ASP A 1 230 ? 0.28603  11.65856 -14.51125 1.000 62.02174 ? 230 ASP A OD1 1 
ATOM   1796 O OD2 . ASP A 1 230 ? -0.05543 13.69121 -13.73645 1.000 62.06044 ? 230 ASP A OD2 1 
ATOM   1797 N N   . VAL A 1 231 ? 3.79694  11.83699 -11.18223 1.000 49.49878 ? 231 VAL A N   1 
ATOM   1798 C CA  . VAL A 1 231 ? 4.94833  12.71395 -11.01777 1.000 48.71729 ? 231 VAL A CA  1 
ATOM   1799 C C   . VAL A 1 231 ? 5.65463  12.86785 -12.35417 1.000 47.70313 ? 231 VAL A C   1 
ATOM   1800 O O   . VAL A 1 231 ? 5.88186  11.88621 -13.07109 1.000 51.04619 ? 231 VAL A O   1 
ATOM   1801 C CB  . VAL A 1 231 ? 5.89857  12.16400 -9.94831  1.000 48.42186 ? 231 VAL A CB  1 
ATOM   1802 C CG1 . VAL A 1 231 ? 7.27225  12.80056 -10.07694 1.000 49.12831 ? 231 VAL A CG1 1 
ATOM   1803 C CG2 . VAL A 1 231 ? 5.32681  12.43364 -8.58161  1.000 47.59567 ? 231 VAL A CG2 1 
ATOM   1804 N N   . GLN A 1 232 ? 5.98831  14.10661 -12.70033 1.000 44.53250 ? 232 GLN A N   1 
ATOM   1805 C CA  . GLN A 1 232 ? 6.78587  14.37423 -13.88313 1.000 42.85367 ? 232 GLN A CA  1 
ATOM   1806 C C   . GLN A 1 232 ? 8.24376  14.65771 -13.56068 1.000 42.66831 ? 232 GLN A C   1 
ATOM   1807 O O   . GLN A 1 232 ? 9.10034  14.44052 -14.42385 1.000 43.92856 ? 232 GLN A O   1 
ATOM   1808 C CB  . GLN A 1 232 ? 6.20319  15.55954 -14.66460 1.000 43.45351 ? 232 GLN A CB  1 
ATOM   1809 N N   . GLU A 1 233 ? 8.54918  15.11277 -12.34429 1.000 38.53962 ? 233 GLU A N   1 
ATOM   1810 C CA  . GLU A 1 233 ? 9.90424  15.55318 -12.04443 1.000 38.87191 ? 233 GLU A CA  1 
ATOM   1811 C C   . GLU A 1 233 ? 10.05061 15.79789 -10.54888 1.000 37.48288 ? 233 GLU A C   1 
ATOM   1812 O O   . GLU A 1 233 ? 9.11996  16.28169 -9.90075  1.000 37.48272 ? 233 GLU A O   1 
ATOM   1813 C CB  . GLU A 1 233 ? 10.23271 16.83363 -12.81956 1.000 39.86026 ? 233 GLU A CB  1 
ATOM   1814 C CG  . GLU A 1 233 ? 11.66505 17.27732 -12.71907 1.000 42.56173 ? 233 GLU A CG  1 
ATOM   1815 C CD  . GLU A 1 233 ? 11.88995 18.62171 -13.37435 1.000 44.07254 ? 233 GLU A CD  1 
ATOM   1816 O OE1 . GLU A 1 233 ? 10.94758 19.43515 -13.40199 1.000 43.90157 ? 233 GLU A OE1 1 
ATOM   1817 O OE2 . GLU A 1 233 ? 13.01152 18.87445 -13.85218 1.000 47.44429 ? 233 GLU A OE2 1 
ATOM   1818 N N   . ILE A 1 234 ? 11.22010 15.45637 -10.01417 1.000 36.77377 ? 234 ILE A N   1 
ATOM   1819 C CA  . ILE A 1 234 ? 11.62145 15.81503 -8.65754  1.000 35.04135 ? 234 ILE A CA  1 
ATOM   1820 C C   . ILE A 1 234 ? 12.91141 16.61680 -8.77589  1.000 33.87353 ? 234 ILE A C   1 
ATOM   1821 O O   . ILE A 1 234 ? 13.91382 16.10573 -9.28891  1.000 37.84341 ? 234 ILE A O   1 
ATOM   1822 C CB  . ILE A 1 234 ? 11.81386 14.57535 -7.76954  1.000 35.94381 ? 234 ILE A CB  1 
ATOM   1823 C CG1 . ILE A 1 234 ? 10.53511 13.73542 -7.74960  1.000 34.60650 ? 234 ILE A CG1 1 
ATOM   1824 C CG2 . ILE A 1 234 ? 12.19841 14.98849 -6.36090  1.000 39.27984 ? 234 ILE A CG2 1 
ATOM   1825 C CD1 . ILE A 1 234 ? 10.76633 12.25673 -7.96159  1.000 33.84852 ? 234 ILE A CD1 1 
ATOM   1826 N N   . ARG A 1 235 ? 12.88512 17.87465 -8.33367  1.000 29.06453 ? 235 ARG A N   1 
ATOM   1827 C CA  A ARG A 1 235 ? 14.02384 18.77336 -8.46688  0.500 29.09672 ? 235 ARG A CA  1 
ATOM   1828 C CA  B ARG A 1 235 ? 14.01855 18.78317 -8.46794  0.500 29.18476 ? 235 ARG A CA  1 
ATOM   1829 C C   . ARG A 1 235 ? 14.61502 19.06178 -7.09664  1.000 28.59180 ? 235 ARG A C   1 
ATOM   1830 O O   . ARG A 1 235 ? 13.88566 19.39472 -6.15892  1.000 31.10980 ? 235 ARG A O   1 
ATOM   1831 C CB  A ARG A 1 235 ? 13.62534 20.08379 -9.14670  0.500 30.92584 ? 235 ARG A CB  1 
ATOM   1832 C CB  B ARG A 1 235 ? 13.60297 20.10118 -9.12960  0.500 31.29409 ? 235 ARG A CB  1 
ATOM   1833 C CG  A ARG A 1 235 ? 13.00154 19.89560 -10.50336 0.500 35.46118 ? 235 ARG A CG  1 
ATOM   1834 C CG  B ARG A 1 235 ? 13.13606 19.96050 -10.56101 0.500 36.04196 ? 235 ARG A CG  1 
ATOM   1835 C CD  A ARG A 1 235 ? 13.28336 21.08009 -11.41489 0.500 38.55118 ? 235 ARG A CD  1 
ATOM   1836 C CD  B ARG A 1 235 ? 12.56189 21.26591 -11.10805 0.500 39.15785 ? 235 ARG A CD  1 
ATOM   1837 N NE  A ARG A 1 235 ? 12.78425 22.33699 -10.87085 0.500 39.96693 ? 235 ARG A NE  1 
ATOM   1838 N NE  B ARG A 1 235 ? 13.58310 22.26765 -11.39619 0.500 42.94786 ? 235 ARG A NE  1 
ATOM   1839 C CZ  A ARG A 1 235 ? 11.52440 22.74064 -10.95766 0.500 42.27771 ? 235 ARG A CZ  1 
ATOM   1840 C CZ  B ARG A 1 235 ? 14.25123 22.35077 -12.53959 0.500 44.56923 ? 235 ARG A CZ  1 
ATOM   1841 N NH1 A ARG A 1 235 ? 10.59401 21.98587 -11.51851 0.500 43.84642 ? 235 ARG A NH1 1 
ATOM   1842 N NH1 B ARG A 1 235 ? 14.06071 21.47963 -13.51784 0.500 44.09366 ? 235 ARG A NH1 1 
ATOM   1843 N NH2 A ARG A 1 235 ? 11.18888 23.92983 -10.46719 0.500 42.23871 ? 235 ARG A NH2 1 
ATOM   1844 N NH2 B ARG A 1 235 ? 15.13334 23.33250 -12.70625 0.500 45.44525 ? 235 ARG A NH2 1 
ATOM   1845 N N   . TYR A 1 236 ? 15.93358 18.94880 -6.99965  1.000 26.35976 ? 236 TYR A N   1 
ATOM   1846 C CA  . TYR A 1 236 ? 16.68419 19.18478 -5.77556  1.000 27.71715 ? 236 TYR A CA  1 
ATOM   1847 C C   . TYR A 1 236 ? 17.63568 20.35949 -5.95247  1.000 29.68725 ? 236 TYR A C   1 
ATOM   1848 O O   . TYR A 1 236 ? 18.32752 20.46035 -6.96838  1.000 29.60665 ? 236 TYR A O   1 
ATOM   1849 C CB  . TYR A 1 236 ? 17.48816 17.95016 -5.40505  1.000 29.40405 ? 236 TYR A CB  1 
ATOM   1850 C CG  . TYR A 1 236 ? 16.64744 16.80325 -4.93260  1.000 30.09437 ? 236 TYR A CG  1 
ATOM   1851 C CD1 . TYR A 1 236 ? 15.78507 16.96448 -3.85667  1.000 31.44147 ? 236 TYR A CD1 1 
ATOM   1852 C CD2 . TYR A 1 236 ? 16.73509 15.54764 -5.52565  1.000 32.12543 ? 236 TYR A CD2 1 
ATOM   1853 C CE1 . TYR A 1 236 ? 15.01825 15.92867 -3.39941  1.000 31.34581 ? 236 TYR A CE1 1 
ATOM   1854 C CE2 . TYR A 1 236 ? 15.96370 14.48815 -5.05675  1.000 33.33861 ? 236 TYR A CE2 1 
ATOM   1855 C CZ  . TYR A 1 236 ? 15.11038 14.69710 -3.98357  1.000 34.51801 ? 236 TYR A CZ  1 
ATOM   1856 O OH  . TYR A 1 236 ? 14.33284 13.68033 -3.48349  1.000 40.07259 ? 236 TYR A OH  1 
ATOM   1857 N N   . GLU A 1 237 ? 17.68233 21.23881 -4.95604  1.000 29.43113 ? 237 GLU A N   1 
ATOM   1858 C CA  . GLU A 1 237 ? 18.66767 22.31006 -4.93057  1.000 28.02712 ? 237 GLU A CA  1 
ATOM   1859 C C   . GLU A 1 237 ? 18.85210 22.74386 -3.49018  1.000 29.05878 ? 237 GLU A C   1 
ATOM   1860 O O   . GLU A 1 237 ? 17.94069 22.60379 -2.67294  1.000 29.22276 ? 237 GLU A O   1 
ATOM   1861 C CB  . GLU A 1 237 ? 18.24979 23.50595 -5.79255  1.000 32.02115 ? 237 GLU A CB  1 
ATOM   1862 C CG  . GLU A 1 237 ? 16.80656 23.92164 -5.62857  0.800 34.76833 ? 237 GLU A CG  1 
ATOM   1863 C CD  . GLU A 1 237 ? 16.27346 24.66676 -6.84622  0.700 37.52534 ? 237 GLU A CD  1 
ATOM   1864 O OE1 . GLU A 1 237 ? 16.88930 25.67505 -7.25600  0.700 35.75753 ? 237 GLU A OE1 1 
ATOM   1865 O OE2 . GLU A 1 237 ? 15.24444 24.22723 -7.40060  0.700 40.13372 ? 237 GLU A OE2 1 
ATOM   1866 N N   . VAL A 1 238 ? 20.03422 23.28215 -3.19252  1.000 28.44397 ? 238 VAL A N   1 
ATOM   1867 C CA  . VAL A 1 238 ? 20.25527 23.84316 -1.86364  1.000 28.81601 ? 238 VAL A CA  1 
ATOM   1868 C C   . VAL A 1 238 ? 19.31492 25.02196 -1.66636  1.000 30.69475 ? 238 VAL A C   1 
ATOM   1869 O O   . VAL A 1 238 ? 19.22654 25.92410 -2.51069  1.000 33.95829 ? 238 VAL A O   1 
ATOM   1870 C CB  . VAL A 1 238 ? 21.72714 24.24285 -1.67911  1.000 26.91002 ? 238 VAL A CB  1 
ATOM   1871 C CG1 . VAL A 1 238 ? 21.93707 24.90592 -0.31658  1.000 28.20818 ? 238 VAL A CG1 1 
ATOM   1872 C CG2 . VAL A 1 238 ? 22.62823 23.02976 -1.81170  1.000 27.37954 ? 238 VAL A CG2 1 
ATOM   1873 N N   . SER A 1 239 ? 18.59230 25.01334 -0.54884  1.000 30.36469 ? 239 SER A N   1 
ATOM   1874 C CA  . SER A 1 239 ? 17.61651 26.05340 -0.28257  1.000 31.43199 ? 239 SER A CA  1 
ATOM   1875 C C   . SER A 1 239 ? 18.30394 27.37921 0.01399   1.000 36.21285 ? 239 SER A C   1 
ATOM   1876 O O   . SER A 1 239 ? 19.43816 27.42841 0.50011   1.000 36.73773 ? 239 SER A O   1 
ATOM   1877 C CB  . SER A 1 239 ? 16.72596 25.66329 0.90121   1.000 33.51928 ? 239 SER A CB  1 
ATOM   1878 O OG  . SER A 1 239 ? 15.85761 26.73507 1.24136   1.000 35.32698 ? 239 SER A OG  1 
ATOM   1879 N N   . ALA A 1 240 ? 17.59532 28.46585 -0.28241  1.000 37.97348 ? 240 ALA A N   1 
ATOM   1880 C CA  . ALA A 1 240 ? 18.01921 29.77595 0.18276   1.000 39.46913 ? 240 ALA A CA  1 
ATOM   1881 C C   . ALA A 1 240 ? 17.70790 29.97677 1.65765   1.000 39.92809 ? 240 ALA A C   1 
ATOM   1882 O O   . ALA A 1 240 ? 18.26249 30.88834 2.27834   1.000 41.77510 ? 240 ALA A O   1 
ATOM   1883 C CB  . ALA A 1 240 ? 17.34936 30.87254 -0.64294  1.000 40.13835 ? 240 ALA A CB  1 
ATOM   1884 N N   . LYS A 1 241 ? 16.83491 29.14952 2.21942   1.000 39.20732 ? 241 LYS A N   1 
ATOM   1885 C CA  . LYS A 1 241 ? 16.49103 29.20374 3.63402   1.000 37.33151 ? 241 LYS A CA  1 
ATOM   1886 C C   . LYS A 1 241 ? 17.47267 28.37785 4.45787   1.000 35.97203 ? 241 LYS A C   1 
ATOM   1887 O O   . LYS A 1 241 ? 18.03577 27.39217 3.98341   1.000 35.09633 ? 241 LYS A O   1 
ATOM   1888 C CB  . LYS A 1 241 ? 15.06768 28.68673 3.85918   1.000 36.88429 ? 241 LYS A CB  1 
ATOM   1889 C CG  . LYS A 1 241 ? 13.97580 29.48732 3.15521   1.000 41.50087 ? 241 LYS A CG  1 
ATOM   1890 C CD  . LYS A 1 241 ? 12.63513 28.75726 3.23171   1.000 46.85098 ? 241 LYS A CD  1 
ATOM   1891 C CE  . LYS A 1 241 ? 11.56111 29.40919 2.36591   1.000 51.12504 ? 241 LYS A CE  1 
ATOM   1892 N NZ  . LYS A 1 241 ? 10.36625 28.52016 2.20988   1.000 53.47952 ? 241 LYS A NZ  1 
ATOM   1893 N N   . LYS A 1 242 ? 17.65545 28.77867 5.71635   1.000 36.66824 ? 242 LYS A N   1 
ATOM   1894 C CA  . LYS A 1 242 ? 18.52930 28.07023 6.64067   1.000 36.21988 ? 242 LYS A CA  1 
ATOM   1895 C C   . LYS A 1 242 ? 17.80793 27.85832 7.95889   1.000 35.48373 ? 242 LYS A C   1 
ATOM   1896 O O   . LYS A 1 242 ? 16.89001 28.60360 8.30776   1.000 36.20509 ? 242 LYS A O   1 
ATOM   1897 C CB  . LYS A 1 242 ? 19.83626 28.83067 6.90009   1.000 38.37024 ? 242 LYS A CB  1 
ATOM   1898 C CG  . LYS A 1 242 ? 20.61467 29.17521 5.63922   0.800 39.85856 ? 242 LYS A CG  1 
ATOM   1899 C CD  . LYS A 1 242 ? 22.04223 29.61168 5.95021   0.700 44.13815 ? 242 LYS A CD  1 
ATOM   1900 C CE  . LYS A 1 242 ? 22.94552 28.41348 6.22491   0.600 47.87147 ? 242 LYS A CE  1 
ATOM   1901 N NZ  . LYS A 1 242 ? 24.37102 28.81579 6.40445   0.600 50.04749 ? 242 LYS A NZ  1 
ATOM   1902 N N   . ILE A 1 243 ? 18.22169 26.83043 8.68003   1.000 32.73002 ? 243 ILE A N   1 
ATOM   1903 C CA  . ILE A 1 243 ? 17.75871 26.62422 10.04746  1.000 30.89778 ? 243 ILE A CA  1 
ATOM   1904 C C   . ILE A 1 243 ? 18.73677 27.30529 10.98758  1.000 31.69636 ? 243 ILE A C   1 
ATOM   1905 O O   . ILE A 1 243 ? 19.95301 27.25239 10.78726  1.000 30.45114 ? 243 ILE A O   1 
ATOM   1906 C CB  . ILE A 1 243 ? 17.61309 25.12303 10.37119  1.000 30.77993 ? 243 ILE A CB  1 
ATOM   1907 C CG1 . ILE A 1 243 ? 17.01963 24.93269 11.77781  1.000 33.14928 ? 243 ILE A CG1 1 
ATOM   1908 C CG2 . ILE A 1 243 ? 18.94228 24.39324 10.24176  1.000 29.65658 ? 243 ILE A CG2 1 
ATOM   1909 C CD1 . ILE A 1 243 ? 16.89261 23.47876 12.18757  1.000 34.04708 ? 243 ILE A CD1 1 
ATOM   1910 N N   . HIS A 1 244 ? 18.21096 27.95087 12.02304  1.000 33.11497 ? 244 HIS A N   1 
ATOM   1911 C CA  . HIS A 1 244 ? 19.03692 28.67185 12.98035  1.000 33.26550 ? 244 HIS A CA  1 
ATOM   1912 C C   . HIS A 1 244 ? 18.99428 27.96444 14.32569  1.000 33.54231 ? 244 HIS A C   1 
ATOM   1913 O O   . HIS A 1 244 ? 17.91779 27.60472 14.81025  1.000 34.84528 ? 244 HIS A O   1 
ATOM   1914 C CB  . HIS A 1 244 ? 18.57200 30.12409 13.11084  1.000 36.44226 ? 244 HIS A CB  1 
ATOM   1915 C CG  . HIS A 1 244 ? 18.50938 30.84701 11.80022  1.000 40.95459 ? 244 HIS A CG  1 
ATOM   1916 N ND1 . HIS A 1 244 ? 19.63144 31.33417 11.16415  1.000 42.79303 ? 244 HIS A ND1 1 
ATOM   1917 C CD2 . HIS A 1 244 ? 17.46240 31.14566 10.99523  1.000 42.90876 ? 244 HIS A CD2 1 
ATOM   1918 C CE1 . HIS A 1 244 ? 19.27730 31.90982 10.02818  1.000 43.18989 ? 244 HIS A CE1 1 
ATOM   1919 N NE2 . HIS A 1 244 ? 17.96670 31.80652 9.90061   1.000 42.78672 ? 244 HIS A NE2 1 
ATOM   1920 N N   . PHE A 1 245 ? 20.16657 27.74496 14.90519  1.000 31.28227 ? 245 PHE A N   1 
ATOM   1921 C CA  . PHE A 1 245 ? 20.29943 27.15734 16.23243  1.000 32.70703 ? 245 PHE A CA  1 
ATOM   1922 C C   . PHE A 1 245 ? 20.74888 28.22310 17.21409  1.000 35.51628 ? 245 PHE A C   1 
ATOM   1923 O O   . PHE A 1 245 ? 21.59664 29.05610 16.89090  1.000 38.30593 ? 245 PHE A O   1 
ATOM   1924 C CB  . PHE A 1 245 ? 21.32112 26.01911 16.24561  1.000 34.10268 ? 245 PHE A CB  1 
ATOM   1925 C CG  . PHE A 1 245 ? 20.94666 24.85038 15.38933  1.000 35.73547 ? 245 PHE A CG  1 
ATOM   1926 C CD1 . PHE A 1 245 ? 21.30482 24.81325 14.04980  1.000 36.72040 ? 245 PHE A CD1 1 
ATOM   1927 C CD2 . PHE A 1 245 ? 20.25817 23.77882 15.92243  1.000 36.67823 ? 245 PHE A CD2 1 
ATOM   1928 C CE1 . PHE A 1 245 ? 20.96931 23.73252 13.25689  1.000 37.37268 ? 245 PHE A CE1 1 
ATOM   1929 C CE2 . PHE A 1 245 ? 19.92400 22.69520 15.13466  1.000 36.68036 ? 245 PHE A CE2 1 
ATOM   1930 C CZ  . PHE A 1 245 ? 20.28181 22.67166 13.79768  1.000 36.23568 ? 245 PHE A CZ  1 
ATOM   1931 N N   . ALA A 1 246 ? 20.19449 28.19199 18.41759  1.000 37.61190 ? 246 ALA A N   1 
ATOM   1932 C CA  . ALA A 1 246 ? 20.79885 28.94547 19.50303  1.000 38.33882 ? 246 ALA A CA  1 
ATOM   1933 C C   . ALA A 1 246 ? 21.93910 28.11986 20.07949  1.000 43.25391 ? 246 ALA A C   1 
ATOM   1934 O O   . ALA A 1 246 ? 21.75597 26.94766 20.42082  1.000 44.92692 ? 246 ALA A O   1 
ATOM   1935 C CB  . ALA A 1 246 ? 19.76863 29.27918 20.57980  1.000 38.95977 ? 246 ALA A CB  1 
ATOM   1936 N N   . ARG A 1 247 ? 23.12257 28.71374 20.15963  1.000 45.63233 ? 247 ARG A N   1 
ATOM   1937 C CA  . ARG A 1 247 ? 24.27473 28.03445 20.72704  1.000 49.81723 ? 247 ARG A CA  1 
ATOM   1938 C C   . ARG A 1 247 ? 24.76664 28.81403 21.93861  1.000 50.60362 ? 247 ARG A C   1 
ATOM   1939 O O   . ARG A 1 247 ? 24.82571 30.04813 21.92007  1.000 51.32762 ? 247 ARG A O   1 
ATOM   1940 C CB  . ARG A 1 247 ? 25.38742 27.85745 19.68567  1.000 52.89851 ? 247 ARG A CB  1 
ATOM   1941 C CG  . ARG A 1 247 ? 25.01279 26.92524 18.51573  1.000 55.82729 ? 247 ARG A CG  1 
ATOM   1942 C CD  . ARG A 1 247 ? 25.29302 25.44166 18.80718  1.000 57.64188 ? 247 ARG A CD  1 
ATOM   1943 N NE  . ARG A 1 247 ? 25.35848 24.64340 17.58383  1.000 58.80249 ? 247 ARG A NE  1 
ATOM   1944 C CZ  . ARG A 1 247 ? 24.52336 23.66040 17.26868  1.000 58.67980 ? 247 ARG A CZ  1 
ATOM   1945 N NH1 . ARG A 1 247 ? 23.55646 23.28281 18.08773  1.000 59.12602 ? 247 ARG A NH1 1 
ATOM   1946 N NH2 . ARG A 1 247 ? 24.66916 23.03343 16.10433  1.000 56.92673 ? 247 ARG A NH2 1 
ATOM   1947 N N   . PHE A 1 248 ? 25.08244 28.08868 23.00476  1.000 52.21949 ? 248 PHE A N   1 
ATOM   1948 C CA  . PHE A 1 248 ? 25.54779 28.69808 24.23874  1.000 52.96637 ? 248 PHE A CA  1 
ATOM   1949 C C   . PHE A 1 248 ? 26.95175 28.28025 24.62278  1.000 50.17541 ? 248 PHE A C   1 
ATOM   1950 O O   . PHE A 1 248 ? 27.52679 28.87654 25.53941  1.000 50.82009 ? 248 PHE A O   1 
ATOM   1951 C CB  . PHE A 1 248 ? 24.59778 28.36089 25.39112  1.000 57.10984 ? 248 PHE A CB  1 
ATOM   1952 C CG  . PHE A 1 248 ? 23.24306 28.95173 25.22556  1.000 59.24390 ? 248 PHE A CG  1 
ATOM   1953 C CD1 . PHE A 1 248 ? 22.99617 30.24517 25.64116  1.000 59.29141 ? 248 PHE A CD1 1 
ATOM   1954 C CD2 . PHE A 1 248 ? 22.22353 28.23160 24.62929  1.000 60.46262 ? 248 PHE A CD2 1 
ATOM   1955 C CE1 . PHE A 1 248 ? 21.75794 30.80792 25.48681  1.000 59.46138 ? 248 PHE A CE1 1 
ATOM   1956 C CE2 . PHE A 1 248 ? 20.97837 28.79187 24.47217  1.000 61.32933 ? 248 PHE A CE2 1 
ATOM   1957 C CZ  . PHE A 1 248 ? 20.74934 30.08414 24.90564  1.000 60.64158 ? 248 PHE A CZ  1 
ATOM   1958 N N   . ARG A 1 249 ? 27.51031 27.28085 23.95476  1.000 45.01654 ? 249 ARG A N   1 
ATOM   1959 C CA  . ARG A 1 249 ? 28.85820 26.81326 24.21816  1.000 47.20435 ? 249 ARG A CA  1 
ATOM   1960 C C   . ARG A 1 249 ? 29.35896 26.15811 22.94364  1.000 45.94731 ? 249 ARG A C   1 
ATOM   1961 O O   . ARG A 1 249 ? 28.58845 25.88666 22.01878  1.000 46.47463 ? 249 ARG A O   1 
ATOM   1962 C CB  . ARG A 1 249 ? 28.89505 25.84042 25.40029  1.000 48.68796 ? 249 ARG A CB  1 
ATOM   1963 C CG  . ARG A 1 249 ? 27.88002 24.71724 25.27837  1.000 52.14758 ? 249 ARG A CG  1 
ATOM   1964 C CD  . ARG A 1 249 ? 27.90456 23.78631 26.47856  0.800 54.24283 ? 249 ARG A CD  1 
ATOM   1965 N NE  . ARG A 1 249 ? 26.99489 22.66258 26.29082  0.700 57.16424 ? 249 ARG A NE  1 
ATOM   1966 C CZ  . ARG A 1 249 ? 26.75391 21.73207 27.20308  0.700 59.41881 ? 249 ARG A CZ  1 
ATOM   1967 N NH1 . ARG A 1 249 ? 27.33406 21.76410 28.39174  0.700 60.92925 ? 249 ARG A NH1 1 
ATOM   1968 N NH2 . ARG A 1 249 ? 25.90638 20.74671 26.91788  0.700 59.16011 ? 249 ARG A NH2 1 
ATOM   1969 N N   . SER A 1 250 ? 30.66236 25.90886 22.90021  1.000 44.41818 ? 250 SER A N   1 
ATOM   1970 C CA  . SER A 1 250 ? 31.24890 25.23141 21.75366  1.000 43.28375 ? 250 SER A CA  1 
ATOM   1971 C C   . SER A 1 250 ? 30.95911 23.73906 21.83750  1.000 41.81723 ? 250 SER A C   1 
ATOM   1972 O O   . SER A 1 250 ? 31.31119 23.08345 22.82107  1.000 44.50156 ? 250 SER A O   1 
ATOM   1973 C CB  . SER A 1 250 ? 32.75438 25.48048 21.69076  1.000 45.90207 ? 250 SER A CB  1 
ATOM   1974 O OG  . SER A 1 250 ? 33.34149 24.77785 20.60254  1.000 47.60289 ? 250 SER A OG  1 
ATOM   1975 N N   . PHE A 1 251 ? 30.31813 23.20161 20.80624  1.000 38.71761 ? 251 PHE A N   1 
ATOM   1976 C CA  . PHE A 1 251 ? 30.17107 21.75759 20.63313  1.000 35.46933 ? 251 PHE A CA  1 
ATOM   1977 C C   . PHE A 1 251 ? 30.39643 21.51928 19.15332  1.000 33.88735 ? 251 PHE A C   1 
ATOM   1978 O O   . PHE A 1 251 ? 29.44497 21.44883 18.36860  1.000 34.76223 ? 251 PHE A O   1 
ATOM   1979 C CB  . PHE A 1 251 ? 28.79418 21.26303 21.08703  1.000 37.02842 ? 251 PHE A CB  1 
ATOM   1980 C CG  . PHE A 1 251 ? 28.71268 19.76492 21.30138  1.000 37.85152 ? 251 PHE A CG  1 
ATOM   1981 C CD1 . PHE A 1 251 ? 29.79400 18.93971 21.02935  1.000 39.09935 ? 251 PHE A CD1 1 
ATOM   1982 C CD2 . PHE A 1 251 ? 27.54742 19.18859 21.78793  1.000 38.22343 ? 251 PHE A CD2 1 
ATOM   1983 C CE1 . PHE A 1 251 ? 29.71343 17.56774 21.23077  1.000 38.59078 ? 251 PHE A CE1 1 
ATOM   1984 C CE2 . PHE A 1 251 ? 27.45704 17.81903 21.99668  1.000 39.78512 ? 251 PHE A CE2 1 
ATOM   1985 C CZ  . PHE A 1 251 ? 28.54156 17.00744 21.71544  1.000 40.15851 ? 251 PHE A CZ  1 
ATOM   1986 N N   . PRO A 1 252 ? 31.65687 21.42739 18.73320  1.000 31.41435 ? 252 PRO A N   1 
ATOM   1987 C CA  . PRO A 1 252 ? 31.96207 21.35371 17.30272  1.000 30.31564 ? 252 PRO A CA  1 
ATOM   1988 C C   . PRO A 1 252 ? 31.32402 20.15294 16.63257  1.000 30.26221 ? 252 PRO A C   1 
ATOM   1989 O O   . PRO A 1 252 ? 31.20593 19.07391 17.21422  1.000 31.19821 ? 252 PRO A O   1 
ATOM   1990 C CB  . PRO A 1 252 ? 33.49137 21.24745 17.27879  1.000 31.63729 ? 252 PRO A CB  1 
ATOM   1991 C CG  . PRO A 1 252 ? 33.92219 21.89863 18.54060  1.000 30.93007 ? 252 PRO A CG  1 
ATOM   1992 C CD  . PRO A 1 252 ? 32.88321 21.50454 19.54580  1.000 29.60312 ? 252 PRO A CD  1 
ATOM   1993 N N   . PHE A 1 253 ? 30.93913 20.35240 15.36756  1.000 29.97617 ? 253 PHE A N   1 
ATOM   1994 C CA  . PHE A 1 253 ? 30.37460 19.27062 14.57265  1.000 29.46865 ? 253 PHE A CA  1 
ATOM   1995 C C   . PHE A 1 253 ? 31.25581 18.02919 14.61117  1.000 27.42464 ? 253 PHE A C   1 
ATOM   1996 O O   . PHE A 1 253 ? 30.76504 16.90945 14.77422  1.000 27.55277 ? 253 PHE A O   1 
ATOM   1997 C CB  . PHE A 1 253 ? 30.18720 19.74962 13.13466  1.000 29.65066 ? 253 PHE A CB  1 
ATOM   1998 C CG  . PHE A 1 253 ? 29.62029 18.71332 12.22026  1.000 28.07484 ? 253 PHE A CG  1 
ATOM   1999 C CD1 . PHE A 1 253 ? 28.27150 18.38316 12.26574  1.000 29.02517 ? 253 PHE A CD1 1 
ATOM   2000 C CD2 . PHE A 1 253 ? 30.43206 18.07569 11.29752  1.000 29.85784 ? 253 PHE A CD2 1 
ATOM   2001 C CE1 . PHE A 1 253 ? 27.74749 17.43107 11.40175  1.000 31.59449 ? 253 PHE A CE1 1 
ATOM   2002 C CE2 . PHE A 1 253 ? 29.91570 17.13065 10.43883  1.000 30.73349 ? 253 PHE A CE2 1 
ATOM   2003 C CZ  . PHE A 1 253 ? 28.56984 16.81106 10.48519  1.000 32.53527 ? 253 PHE A CZ  1 
ATOM   2004 N N   . TRP A 1 254 ? 32.56806 18.20395 14.44205  1.000 27.20751 ? 254 TRP A N   1 
ATOM   2005 C CA  . TRP A 1 254 ? 33.42325 17.02788 14.39283  1.000 25.01606 ? 254 TRP A CA  1 
ATOM   2006 C C   . TRP A 1 254 ? 33.50424 16.34233 15.74798  1.000 25.64868 ? 254 TRP A C   1 
ATOM   2007 O O   . TRP A 1 254 ? 33.71416 15.12485 15.80926  1.000 26.15170 ? 254 TRP A O   1 
ATOM   2008 C CB  . TRP A 1 254 ? 34.81504 17.39769 13.88230  1.000 25.52744 ? 254 TRP A CB  1 
ATOM   2009 C CG  . TRP A 1 254 ? 34.82142 17.86329 12.43875  1.000 25.46613 ? 254 TRP A CG  1 
ATOM   2010 C CD1 . TRP A 1 254 ? 35.31570 19.04361 11.96846  1.000 28.59197 ? 254 TRP A CD1 1 
ATOM   2011 C CD2 . TRP A 1 254 ? 34.30694 17.16065 11.29302  1.000 27.21177 ? 254 TRP A CD2 1 
ATOM   2012 N NE1 . TRP A 1 254 ? 35.14132 19.12419 10.60540  1.000 27.96597 ? 254 TRP A NE1 1 
ATOM   2013 C CE2 . TRP A 1 254 ? 34.52688 17.98122 10.16786  1.000 26.35226 ? 254 TRP A CE2 1 
ATOM   2014 C CE3 . TRP A 1 254 ? 33.68019 15.92192 11.11211  1.000 27.58750 ? 254 TRP A CE3 1 
ATOM   2015 C CZ2 . TRP A 1 254 ? 34.15456 17.59920 8.87261   1.000 26.21668 ? 254 TRP A CZ2 1 
ATOM   2016 C CZ3 . TRP A 1 254 ? 33.31260 15.54396 9.82326   1.000 28.07577 ? 254 TRP A CZ3 1 
ATOM   2017 C CH2 . TRP A 1 254 ? 33.55234 16.38228 8.72490   1.000 28.49174 ? 254 TRP A CH2 1 
ATOM   2018 N N   . ARG A 1 255 ? 33.33350 17.09550 16.84128  1.000 27.10903 ? 255 ARG A N   1 
ATOM   2019 C CA  . ARG A 1 255 ? 33.24098 16.44919 18.14701  1.000 28.84567 ? 255 ARG A CA  1 
ATOM   2020 C C   . ARG A 1 255 ? 31.91734 15.70632 18.28921  1.000 29.99629 ? 255 ARG A C   1 
ATOM   2021 O O   . ARG A 1 255 ? 31.87212 14.60438 18.84896  1.000 29.76880 ? 255 ARG A O   1 
ATOM   2022 C CB  . ARG A 1 255 ? 33.41450 17.48175 19.26947  1.000 31.93637 ? 255 ARG A CB  1 
ATOM   2023 C CG  . ARG A 1 255 ? 33.24131 16.90619 20.67677  0.900 35.32787 ? 255 ARG A CG  1 
ATOM   2024 C CD  . ARG A 1 255 ? 34.15701 17.59635 21.68688  0.800 39.86458 ? 255 ARG A CD  1 
ATOM   2025 N NE  . ARG A 1 255 ? 35.50020 17.03267 21.63667  0.700 44.82412 ? 255 ARG A NE  1 
ATOM   2026 C CZ  . ARG A 1 255 ? 36.60036 17.65671 22.03346  0.700 47.39416 ? 255 ARG A CZ  1 
ATOM   2027 N NH1 . ARG A 1 255 ? 36.56194 18.88853 22.51679  0.700 47.95246 ? 255 ARG A NH1 1 
ATOM   2028 N NH2 . ARG A 1 255 ? 37.77053 17.02984 21.93895  0.700 47.68541 ? 255 ARG A NH2 1 
ATOM   2029 N N   . ARG A 1 256 ? 30.83185 16.28617 17.76834  1.000 28.19110 ? 256 ARG A N   1 
ATOM   2030 C CA  . ARG A 1 256 ? 29.54819 15.59255 17.77357  1.000 29.66750 ? 256 ARG A CA  1 
ATOM   2031 C C   . ARG A 1 256 ? 29.62552 14.30151 16.97331  1.000 27.75950 ? 256 ARG A C   1 
ATOM   2032 O O   . ARG A 1 256 ? 29.06696 13.27608 17.37502  1.000 28.62779 ? 256 ARG A O   1 
ATOM   2033 C CB  . ARG A 1 256 ? 28.44987 16.51054 17.22762  1.000 35.49049 ? 256 ARG A CB  1 
ATOM   2034 C CG  . ARG A 1 256 ? 27.29696 16.72088 18.20469  1.000 41.19367 ? 256 ARG A CG  1 
ATOM   2035 C CD  . ARG A 1 256 ? 26.61804 18.08369 18.05939  1.000 39.17365 ? 256 ARG A CD  1 
ATOM   2036 N NE  . ARG A 1 256 ? 26.26033 18.39666 16.67947  1.000 32.77508 ? 256 ARG A NE  1 
ATOM   2037 C CZ  . ARG A 1 256 ? 26.74260 19.43323 16.00394  1.000 37.29753 ? 256 ARG A CZ  1 
ATOM   2038 N NH1 . ARG A 1 256 ? 27.60652 20.27757 16.55229  1.000 37.58525 ? 256 ARG A NH1 1 
ATOM   2039 N NH2 . ARG A 1 256 ? 26.34740 19.63205 14.74893  1.000 41.27407 ? 256 ARG A NH2 1 
ATOM   2040 N N   . VAL A 1 257 ? 30.32467 14.33146 15.83539  1.000 26.97409 ? 257 VAL A N   1 
ATOM   2041 C CA  . VAL A 1 257 ? 30.53387 13.11214 15.06377  1.000 26.30675 ? 257 VAL A CA  1 
ATOM   2042 C C   . VAL A 1 257 ? 31.33597 12.10161 15.86788  1.000 27.46828 ? 257 VAL A C   1 
ATOM   2043 O O   . VAL A 1 257 ? 30.99335 10.91237 15.91805  1.000 26.68883 ? 257 VAL A O   1 
ATOM   2044 C CB  . VAL A 1 257 ? 31.22339 13.43539 13.72648  1.000 25.05006 ? 257 VAL A CB  1 
ATOM   2045 C CG1 . VAL A 1 257 ? 31.68572 12.15081 13.03849  1.000 24.82253 ? 257 VAL A CG1 1 
ATOM   2046 C CG2 . VAL A 1 257 ? 30.28131 14.23404 12.85037  1.000 24.58474 ? 257 VAL A CG2 1 
ATOM   2047 N N   . HIS A 1 258 ? 32.42966 12.55759 16.49199  1.000 27.20358 ? 258 HIS A N   1 
ATOM   2048 C CA  . HIS A 1 258 ? 33.24563 11.67269 17.31577  1.000 26.45066 ? 258 HIS A CA  1 
ATOM   2049 C C   . HIS A 1 258 ? 32.40551 11.04147 18.41075  1.000 27.48035 ? 258 HIS A C   1 
ATOM   2050 O O   . HIS A 1 258 ? 32.44642 9.82599  18.62249  1.000 28.46314 ? 258 HIS A O   1 
ATOM   2051 C CB  . HIS A 1 258 ? 34.40716 12.45209 17.93723  1.000 27.08508 ? 258 HIS A CB  1 
ATOM   2052 C CG  . HIS A 1 258 ? 35.19953 11.66673 18.93224  1.000 28.58483 ? 258 HIS A CG  1 
ATOM   2053 N ND1 . HIS A 1 258 ? 34.89132 11.64446 20.27862  1.000 32.69221 ? 258 HIS A ND1 1 
ATOM   2054 C CD2 . HIS A 1 258 ? 36.29917 10.89191 18.78679  1.000 29.19269 ? 258 HIS A CD2 1 
ATOM   2055 C CE1 . HIS A 1 258 ? 35.77068 10.88997 20.91714  1.000 31.75961 ? 258 HIS A CE1 1 
ATOM   2056 N NE2 . HIS A 1 258 ? 36.63276 10.41666 20.03416  1.000 34.27457 ? 258 HIS A NE2 1 
ATOM   2057 N N   . ASP A 1 259 ? 31.61642 11.86095 19.10119  1.000 28.21773 ? 259 ASP A N   1 
ATOM   2058 C CA  . ASP A 1 259 ? 30.87595 11.37813 20.25881  1.000 29.62762 ? 259 ASP A CA  1 
ATOM   2059 C C   . ASP A 1 259 ? 29.77421 10.40384 19.86009  1.000 31.98398 ? 259 ASP A C   1 
ATOM   2060 O O   . ASP A 1 259 ? 29.43387 9.49979  20.63276  1.000 34.81459 ? 259 ASP A O   1 
ATOM   2061 C CB  . ASP A 1 259 ? 30.28902 12.56462 21.02218  1.000 30.94625 ? 259 ASP A CB  1 
ATOM   2062 C CG  . ASP A 1 259 ? 31.34027 13.37471 21.76667  1.000 31.64725 ? 259 ASP A CG  1 
ATOM   2063 O OD1 . ASP A 1 259 ? 32.52920 12.98186 21.79045  1.000 32.54277 ? 259 ASP A OD1 1 
ATOM   2064 O OD2 . ASP A 1 259 ? 30.96303 14.42063 22.33400  1.000 34.73248 ? 259 ASP A OD2 1 
ATOM   2065 N N   . SER A 1 260 ? 29.21260 10.55751 18.66307  1.000 30.69116 ? 260 SER A N   1 
ATOM   2066 C CA  . SER A 1 260 ? 28.10821 9.70598  18.24490  1.000 31.48761 ? 260 SER A CA  1 
ATOM   2067 C C   . SER A 1 260 ? 28.56311 8.41010  17.59411  1.000 31.18376 ? 260 SER A C   1 
ATOM   2068 O O   . SER A 1 260 ? 27.84627 7.40330  17.67837  1.000 33.45370 ? 260 SER A O   1 
ATOM   2069 C CB  . SER A 1 260 ? 27.20707 10.44511 17.25353  1.000 36.05429 ? 260 SER A CB  1 
ATOM   2070 O OG  . SER A 1 260 ? 26.77387 11.69481 17.75670  1.000 37.02025 ? 260 SER A OG  1 
ATOM   2071 N N   . PHE A 1 261 ? 29.71727 8.41242  16.91112  1.000 27.68052 ? 261 PHE A N   1 
ATOM   2072 C CA  . PHE A 1 261 ? 30.13909 7.24785  16.14636  1.000 28.12342 ? 261 PHE A CA  1 
ATOM   2073 C C   . PHE A 1 261 ? 31.43090 6.60599  16.62132  1.000 31.49938 ? 261 PHE A C   1 
ATOM   2074 O O   . PHE A 1 261 ? 31.65154 5.43047  16.31480  1.000 33.82254 ? 261 PHE A O   1 
ATOM   2075 C CB  . PHE A 1 261 ? 30.29478 7.60817  14.65242  1.000 27.58671 ? 261 PHE A CB  1 
ATOM   2076 C CG  . PHE A 1 261 ? 29.01251 8.05757  14.01360  1.000 26.72361 ? 261 PHE A CG  1 
ATOM   2077 C CD1 . PHE A 1 261 ? 28.01908 7.14412  13.71409  1.000 28.52596 ? 261 PHE A CD1 1 
ATOM   2078 C CD2 . PHE A 1 261 ? 28.78073 9.39468  13.76207  1.000 24.40803 ? 261 PHE A CD2 1 
ATOM   2079 C CE1 . PHE A 1 261 ? 26.82719 7.55259  13.14656  1.000 27.90677 ? 261 PHE A CE1 1 
ATOM   2080 C CE2 . PHE A 1 261 ? 27.58853 9.81113  13.19480  1.000 28.34872 ? 261 PHE A CE2 1 
ATOM   2081 C CZ  . PHE A 1 261 ? 26.61193 8.88892  12.88906  1.000 28.27829 ? 261 PHE A CZ  1 
ATOM   2082 N N   . ILE A 1 262 ? 32.28199 7.31753  17.35563  1.000 31.19252 ? 262 ILE A N   1 
ATOM   2083 C CA  . ILE A 1 262 ? 33.59151 6.80205  17.72248  1.000 32.36020 ? 262 ILE A CA  1 
ATOM   2084 C C   . ILE A 1 262 ? 33.61097 6.33903  19.16794  1.000 33.89362 ? 262 ILE A C   1 
ATOM   2085 O O   . ILE A 1 262 ? 33.92512 5.18230  19.44996  1.000 37.44672 ? 262 ILE A O   1 
ATOM   2086 C CB  . ILE A 1 262 ? 34.68840 7.85950  17.45426  1.000 32.51566 ? 262 ILE A CB  1 
ATOM   2087 C CG1 . ILE A 1 262 ? 34.70790 8.25997  15.97517  1.000 33.44152 ? 262 ILE A CG1 1 
ATOM   2088 C CG2 . ILE A 1 262 ? 36.06024 7.32677  17.84857  1.000 33.57284 ? 262 ILE A CG2 1 
ATOM   2089 C CD1 . ILE A 1 262 ? 35.06523 7.13179  15.04415  1.000 33.33914 ? 262 ILE A CD1 1 
ATOM   2090 N N   . GLU A 1 263 ? 33.24045 7.23371  20.08358  1.000 33.25878 ? 263 GLU A N   1 
ATOM   2091 C CA  . GLU A 1 263 ? 33.22707 6.95212  21.51722  1.000 42.09817 ? 263 GLU A CA  1 
ATOM   2092 C C   . GLU A 1 263 ? 32.69199 8.15729  22.27852  1.000 47.38921 ? 263 GLU A C   1 
ATOM   2093 O O   . GLU A 1 263 ? 32.85141 9.29607  21.83470  1.000 48.96148 ? 263 GLU A O   1 
ATOM   2094 C CB  . GLU A 1 263 ? 34.63376 6.60078  22.01114  1.000 47.87225 ? 263 GLU A CB  1 
ATOM   2095 C CG  . GLU A 1 263 ? 35.67809 7.64997  21.65441  1.000 51.93700 ? 263 GLU A CG  1 
ATOM   2096 C CD  . GLU A 1 263 ? 37.09302 7.23783  22.01200  0.700 54.18715 ? 263 GLU A CD  1 
ATOM   2097 O OE1 . GLU A 1 263 ? 37.25127 6.25651  22.76762  0.700 58.26494 ? 263 GLU A OE1 1 
ATOM   2098 O OE2 . GLU A 1 263 ? 38.04658 7.89698  21.53623  0.700 52.43737 ? 263 GLU A OE2 1 
ATOM   2099 N N   . ASP A 1 264 ? 32.07793 7.92987  23.43370  1.000 54.53837 ? 264 ASP A N   1 
ATOM   2100 C CA  . ASP A 1 264 ? 31.58237 9.03720  24.24788  1.000 58.79695 ? 264 ASP A CA  1 
ATOM   2101 C C   . ASP A 1 264 ? 31.65088 8.67948  25.72792  1.000 61.29661 ? 264 ASP A C   1 
ATOM   2102 O O   . ASP A 1 264 ? 32.49966 7.89012  26.14521  1.000 64.11089 ? 264 ASP A O   1 
ATOM   2103 C CB  . ASP A 1 264 ? 30.14644 9.40428  23.85487  1.000 59.21300 ? 264 ASP A CB  1 
ATOM   2104 C CG  . ASP A 1 264 ? 29.70523 10.74514 24.42509  0.800 60.54465 ? 264 ASP A CG  1 
ATOM   2105 O OD1 . ASP A 1 264 ? 30.52840 11.41985 25.08065  0.800 60.99110 ? 264 ASP A OD1 1 
ATOM   2106 O OD2 . ASP A 1 264 ? 28.53339 11.12623 24.21228  0.800 60.04048 ? 264 ASP A OD2 1 
HETATM 2107 C C1  . CIT B 2 .   ? 31.84356 23.93928 14.30110  1.000 44.96992 ? 301 CIT A C1  1 
HETATM 2108 O O1  . CIT B 2 .   ? 31.62361 22.74593 14.02732  1.000 40.06161 ? 301 CIT A O1  1 
HETATM 2109 O O2  . CIT B 2 .   ? 33.01883 24.27040 14.57648  1.000 49.58287 ? 301 CIT A O2  1 
HETATM 2110 C C2  . CIT B 2 .   ? 30.73576 24.97088 14.31723  1.000 47.66972 ? 301 CIT A C2  1 
HETATM 2111 C C3  . CIT B 2 .   ? 29.57950 24.57681 15.23981  1.000 50.11579 ? 301 CIT A C3  1 
HETATM 2112 O O7  . CIT B 2 .   ? 30.12260 24.12411 16.50970  1.000 50.64430 ? 301 CIT A O7  1 
HETATM 2113 C C4  . CIT B 2 .   ? 28.65088 25.76079 15.48025  1.000 53.44036 ? 301 CIT A C4  1 
HETATM 2114 C C5  . CIT B 2 .   ? 29.11467 26.57727 16.66362  1.000 57.80196 ? 301 CIT A C5  1 
HETATM 2115 O O3  . CIT B 2 .   ? 29.47326 27.76506 16.50626  1.000 60.36765 ? 301 CIT A O3  1 
HETATM 2116 O O4  . CIT B 2 .   ? 29.13534 26.08168 17.81265  1.000 58.34629 ? 301 CIT A O4  1 
HETATM 2117 C C6  . CIT B 2 .   ? 28.75661 23.45418 14.62367  1.000 49.12970 ? 301 CIT A C6  1 
HETATM 2118 O O5  . CIT B 2 .   ? 28.27488 23.57889 13.47666  1.000 46.92063 ? 301 CIT A O5  1 
HETATM 2119 O O6  . CIT B 2 .   ? 28.55926 22.38572 15.23893  1.000 50.82400 ? 301 CIT A O6  1 
HETATM 2120 C C1  . GOL C 3 .   ? 13.83948 9.08581  17.68484  1.000 59.59396 ? 302 GOL A C1  1 
HETATM 2121 O O1  . GOL C 3 .   ? 14.89216 9.92334  17.29956  1.000 59.43132 ? 302 GOL A O1  1 
HETATM 2122 C C2  . GOL C 3 .   ? 13.59376 9.35122  19.18661  1.000 59.58662 ? 302 GOL A C2  1 
HETATM 2123 O O2  . GOL C 3 .   ? 14.73316 9.08662  19.95188  1.000 59.18518 ? 302 GOL A O2  1 
HETATM 2124 C C3  . GOL C 3 .   ? 13.16749 10.84232 19.26233  1.000 58.73770 ? 302 GOL A C3  1 
HETATM 2125 O O3  . GOL C 3 .   ? 12.05040 11.00501 18.46194  1.000 59.69453 ? 302 GOL A O3  1 
HETATM 2126 N N1  . UJT D 4 .   ? 19.69507 4.08030  7.69871   1.000 26.82567 ? 303 UJT A N1  1 
HETATM 2127 C C7  . UJT D 4 .   ? 14.06678 9.74666  10.51300  1.000 29.12999 ? 303 UJT A C7  1 
HETATM 2128 C C8  . UJT D 4 .   ? 13.03509 8.45950  12.30637  1.000 39.47271 ? 303 UJT A C8  1 
HETATM 2129 N N2  . UJT D 4 .   ? 19.21430 6.22819  8.67445   1.000 26.07415 ? 303 UJT A N2  1 
HETATM 2130 C C9  . UJT D 4 .   ? 13.05150 7.14104  11.54819  1.000 43.24382 ? 303 UJT A C9  1 
HETATM 2131 O O1  . UJT D 4 .   ? 10.91114 6.38562  12.38820  0.600 48.66275 ? 303 UJT A O1  1 
HETATM 2132 C C1  . UJT D 4 .   ? 19.99934 5.19529  8.36786   1.000 26.36410 ? 303 UJT A C1  1 
HETATM 2133 O O5  . UJT D 4 .   ? 18.95949 9.42512  16.17067  1.000 38.38011 ? 303 UJT A O5  1 
HETATM 2134 C C5  . UJT D 4 .   ? 16.93586 8.23353  8.90154   1.000 26.13684 ? 303 UJT A C5  1 
HETATM 2135 C C6  . UJT D 4 .   ? 15.43968 9.66850  9.87981   1.000 27.76104 ? 303 UJT A C6  1 
HETATM 2136 N N3  . UJT D 4 .   ? 16.91924 6.91695  8.28469   1.000 25.17449 ? 303 UJT A N3  1 
HETATM 2137 C C4  . UJT D 4 .   ? 17.51809 4.95521  7.48394   1.000 24.94275 ? 303 UJT A C4  1 
HETATM 2138 O O4  . UJT D 4 .   ? 19.32656 6.85091  15.71612  1.000 42.25321 ? 303 UJT A O4  1 
HETATM 2139 C C3  . UJT D 4 .   ? 15.88121 6.30478  7.62821   1.000 26.44926 ? 303 UJT A C3  1 
HETATM 2140 O O3  . UJT D 4 .   ? 15.94533 7.47927  13.20911  1.000 42.20477 ? 303 UJT A O3  1 
HETATM 2141 C C2  . UJT D 4 .   ? 17.97492 6.05047  8.19726   1.000 25.11054 ? 303 UJT A C2  1 
HETATM 2142 N N4  . UJT D 4 .   ? 16.18448 5.13259  7.12789   1.000 26.32963 ? 303 UJT A N4  1 
HETATM 2143 N N   . UJT D 4 .   ? 18.12498 2.77347  6.62320   1.000 28.43086 ? 303 UJT A N   1 
HETATM 2144 C C   . UJT D 4 .   ? 18.43491 3.91960  7.23985   1.000 26.13178 ? 303 UJT A C   1 
HETATM 2145 O O   . UJT D 4 .   ? 15.89012 8.30442  9.85188   1.000 28.03925 ? 303 UJT A O   1 
HETATM 2146 C C10 . UJT D 4 .   ? 12.27461 6.04388  12.22690  0.700 46.06598 ? 303 UJT A C10 1 
HETATM 2147 C C11 . UJT D 4 .   ? 14.47269 10.40125 12.88030  1.000 34.02423 ? 303 UJT A C11 1 
HETATM 2148 C C12 . UJT D 4 .   ? 15.88647 10.79894 12.88215  1.000 32.79294 ? 303 UJT A C12 1 
HETATM 2149 C C13 . UJT D 4 .   ? 17.06890 11.01042 12.86694  1.000 29.71916 ? 303 UJT A C13 1 
HETATM 2150 C C14 . UJT D 4 .   ? 18.45663 11.31423 12.82639  1.000 27.87176 ? 303 UJT A C14 1 
HETATM 2151 C C15 . UJT D 4 .   ? 20.33094 12.23922 12.39047  1.000 24.26139 ? 303 UJT A C15 1 
HETATM 2152 C C16 . UJT D 4 .   ? 21.40457 13.00209 11.89835  1.000 23.40077 ? 303 UJT A C16 1 
HETATM 2153 C C17 . UJT D 4 .   ? 22.80152 11.34291 12.69760  1.000 26.01898 ? 303 UJT A C17 1 
HETATM 2154 C C18 . UJT D 4 .   ? 20.64315 11.03309 12.99182  1.000 25.08665 ? 303 UJT A C18 1 
HETATM 2155 C C19 . UJT D 4 .   ? 19.29176 9.09348  13.81726  1.000 32.01518 ? 303 UJT A C19 1 
HETATM 2156 C C20 . UJT D 4 .   ? 18.31486 7.02827  13.51492  1.000 36.93765 ? 303 UJT A C20 1 
HETATM 2157 C C21 . UJT D 4 .   ? 17.01154 6.59400  12.88404  1.000 40.86715 ? 303 UJT A C21 1 
HETATM 2158 C C22 . UJT D 4 .   ? 18.22682 7.40125  15.00319  1.000 38.67042 ? 303 UJT A C22 1 
HETATM 2159 C C23 . UJT D 4 .   ? 18.34520 8.92570  14.98762  1.000 35.70155 ? 303 UJT A C23 1 
HETATM 2160 C C24 . UJT D 4 .   ? 15.47145 10.08423 8.41940   1.000 26.30902 ? 303 UJT A C24 1 
HETATM 2161 C C25 . UJT D 4 .   ? 16.74483 9.39439  7.90980   1.000 26.32328 ? 303 UJT A C25 1 
HETATM 2162 N N10 . UJT D 4 .   ? 19.43604 10.42881 13.26240  1.000 29.55130 ? 303 UJT A N10 1 
HETATM 2163 N N5  . UJT D 4 .   ? 14.14080 9.34529  11.92343  1.000 34.22180 ? 303 UJT A N5  1 
HETATM 2164 N N6  . UJT D 4 .   ? 18.95793 12.41694 12.31374  1.000 26.35385 ? 303 UJT A N6  1 
HETATM 2165 N N7  . UJT D 4 .   ? 21.25333 14.11385 11.16818  1.000 24.96807 ? 303 UJT A N7  1 
HETATM 2166 N N8  . UJT D 4 .   ? 22.65126 12.52155 12.08720  1.000 26.27479 ? 303 UJT A N8  1 
HETATM 2167 N N9  . UJT D 4 .   ? 21.86513 10.52853 13.18743  1.000 26.47390 ? 303 UJT A N9  1 
HETATM 2168 O O2  . UJT D 4 .   ? 18.82634 8.19718  12.83241  1.000 33.81032 ? 303 UJT A O2  1 
HETATM 2169 O O6  . UJT D 4 .   ? 15.54891 11.49998 8.32529   1.000 26.61632 ? 303 UJT A O6  1 
HETATM 2170 O O7  . UJT D 4 .   ? 17.87792 10.25156 7.97084   1.000 27.20509 ? 303 UJT A O7  1 
HETATM 2171 O O   . HOH E 5 .   ? 8.14746  31.51444 41.81354  1.000 30.98935 ? 401 HOH A O   1 
HETATM 2172 O O   . HOH E 5 .   ? 27.12591 -4.33839 -10.64128 1.000 53.68109 ? 402 HOH A O   1 
HETATM 2173 O O   . HOH E 5 .   ? 9.74531  6.66297  1.54919   1.000 49.69660 ? 403 HOH A O   1 
HETATM 2174 O O   . HOH E 5 .   ? 11.91507 1.57220  -5.34670  1.000 48.52492 ? 404 HOH A O   1 
HETATM 2175 O O   . HOH E 5 .   ? 24.02336 8.14581  -8.84691  1.000 31.27303 ? 405 HOH A O   1 
HETATM 2176 O O   . HOH E 5 .   ? 18.95783 26.85945 -6.57712  1.000 48.45816 ? 406 HOH A O   1 
HETATM 2177 O O   . HOH E 5 .   ? 18.52607 6.50414  18.06951  1.000 54.84979 ? 407 HOH A O   1 
HETATM 2178 O O   . HOH E 5 .   ? 24.37598 16.23066 11.66074  1.000 34.84753 ? 408 HOH A O   1 
HETATM 2179 O O   . HOH E 5 .   ? 9.52582  12.39622 18.92798  1.000 59.43587 ? 409 HOH A O   1 
HETATM 2180 O O   . HOH E 5 .   ? 22.40176 27.84325 2.51347   1.000 58.39750 ? 410 HOH A O   1 
HETATM 2181 O O   . HOH E 5 .   ? 35.28998 23.39122 21.44209  1.000 56.06004 ? 411 HOH A O   1 
HETATM 2182 O O   . HOH E 5 .   ? 18.85887 35.50952 12.98984  1.000 56.50051 ? 412 HOH A O   1 
HETATM 2183 O O   . HOH E 5 .   ? 2.73367  23.82943 22.90550  1.000 54.31555 ? 413 HOH A O   1 
HETATM 2184 O O   . HOH E 5 .   ? 15.00405 16.90340 20.57519  1.000 36.25965 ? 414 HOH A O   1 
HETATM 2185 O O   . HOH E 5 .   ? 2.28936  17.08899 0.56687   1.000 49.98133 ? 415 HOH A O   1 
HETATM 2186 O O   . HOH E 5 .   ? 6.63139  19.12626 16.67188  1.000 49.56887 ? 416 HOH A O   1 
HETATM 2187 O O   . HOH E 5 .   ? 8.79445  20.85085 4.09455   1.000 50.85063 ? 417 HOH A O   1 
HETATM 2188 O O   . HOH E 5 .   ? 13.33454 18.93171 0.75278   1.000 42.22928 ? 418 HOH A O   1 
HETATM 2189 O O   . HOH E 5 .   ? 13.69803 10.76952 4.46837   1.000 29.25436 ? 419 HOH A O   1 
HETATM 2190 O O   . HOH E 5 .   ? 34.22234 7.25734  27.97424  1.000 61.91010 ? 420 HOH A O   1 
HETATM 2191 O O   . HOH E 5 .   ? 16.62905 2.10987  -20.55116 1.000 61.56809 ? 421 HOH A O   1 
HETATM 2192 O O   . HOH E 5 .   ? 20.42036 21.92917 19.69565  1.000 44.38583 ? 422 HOH A O   1 
HETATM 2193 O O   . HOH E 5 .   ? 25.26602 3.51092  -1.91219  1.000 40.61368 ? 423 HOH A O   1 
HETATM 2194 O O   . HOH E 5 .   ? 3.60719  15.90398 25.78344  1.000 60.00524 ? 424 HOH A O   1 
HETATM 2195 O O   . HOH E 5 .   ? 27.89779 26.14531 -2.51766  1.000 36.47281 ? 425 HOH A O   1 
HETATM 2196 O O   . HOH E 5 .   ? 22.01719 23.28280 -5.20604  1.000 29.49088 ? 426 HOH A O   1 
HETATM 2197 O O   . HOH E 5 .   ? 25.91006 -1.24627 -8.09814  1.000 46.59557 ? 427 HOH A O   1 
HETATM 2198 O O   . HOH E 5 .   ? 6.60279  30.73404 30.66326  1.000 56.15654 ? 428 HOH A O   1 
HETATM 2199 O O   . HOH E 5 .   ? 15.50738 28.51217 12.15836  1.000 37.84328 ? 430 HOH A O   1 
HETATM 2200 O O   . HOH E 5 .   ? 22.78038 11.29376 0.45346   1.000 21.18749 ? 431 HOH A O   1 
HETATM 2201 O O   . HOH E 5 .   ? 15.66252 30.61480 7.06092   1.000 49.21992 ? 432 HOH A O   1 
HETATM 2202 O O   . HOH E 5 .   ? 20.24323 26.40153 2.86021   1.000 32.82936 ? 433 HOH A O   1 
HETATM 2203 O O   . HOH E 5 .   ? 31.82008 5.23241  -11.80186 1.000 34.29250 ? 434 HOH A O   1 
HETATM 2204 O O   . HOH E 5 .   ? 32.40049 15.76026 24.15485  1.000 43.79051 ? 435 HOH A O   1 
HETATM 2205 O O   . HOH E 5 .   ? 33.57773 20.94377 13.67423  1.000 30.83774 ? 436 HOH A O   1 
HETATM 2206 O O   . HOH E 5 .   ? 24.32889 5.04615  9.93382   1.000 31.53060 ? 437 HOH A O   1 
HETATM 2207 O O   . HOH E 5 .   ? 29.28553 6.66172  4.88819   1.000 22.46546 ? 438 HOH A O   1 
HETATM 2208 O O   . HOH E 5 .   ? 9.88702  34.36977 42.12364  1.000 48.55055 ? 439 HOH A O   1 
HETATM 2209 O O   . HOH E 5 .   ? 27.49507 5.61279  -1.77585  1.000 39.60241 ? 440 HOH A O   1 
HETATM 2210 O O   . HOH E 5 .   ? 20.61017 26.73368 -4.68092  1.000 40.03667 ? 441 HOH A O   1 
HETATM 2211 O O   . HOH E 5 .   ? 10.99764 32.96156 7.95715   1.000 59.13411 ? 442 HOH A O   1 
HETATM 2212 O O   . HOH E 5 .   ? 24.98597 14.05645 -21.32351 1.000 56.23237 ? 443 HOH A O   1 
HETATM 2213 O O   . HOH E 5 .   ? 24.28719 18.43533 13.44533  1.000 41.31191 ? 444 HOH A O   1 
HETATM 2214 O O   . HOH E 5 .   ? 13.74403 22.28058 -5.88635  1.000 37.10215 ? 445 HOH A O   1 
HETATM 2215 O O   . HOH E 5 .   ? 21.33532 1.39686  -13.09049 1.000 38.22660 ? 446 HOH A O   1 
HETATM 2216 O O   . HOH E 5 .   ? 22.40045 21.03231 7.14792   1.000 27.98158 ? 447 HOH A O   1 
HETATM 2217 O O   . HOH E 5 .   ? 14.37681 3.99061  5.40411   1.000 34.75004 ? 448 HOH A O   1 
HETATM 2218 O O   . HOH E 5 .   ? 13.69777 26.99735 -0.44898  1.000 50.83062 ? 449 HOH A O   1 
HETATM 2219 O O   . HOH E 5 .   ? 17.89159 10.42411 18.51005  1.000 52.86097 ? 450 HOH A O   1 
HETATM 2220 O O   . HOH E 5 .   ? 7.11304  11.24278 19.92467  1.000 53.70580 ? 451 HOH A O   1 
HETATM 2221 O O   . HOH E 5 .   ? 20.54370 7.69350  10.61509  1.000 28.99172 ? 452 HOH A O   1 
HETATM 2222 O O   . HOH E 5 .   ? 17.17909 8.17947  22.67409  1.000 60.16793 ? 453 HOH A O   1 
HETATM 2223 O O   . HOH E 5 .   ? 2.76940  5.49722  -13.95960 1.000 57.25987 ? 454 HOH A O   1 
HETATM 2224 O O   . HOH E 5 .   ? 20.72864 11.56179 4.99903   1.000 22.92588 ? 455 HOH A O   1 
HETATM 2225 O O   . HOH E 5 .   ? 11.22401 7.48219  -0.44319  1.000 37.08004 ? 456 HOH A O   1 
HETATM 2226 O O   . HOH E 5 .   ? 17.76596 11.40313 22.81111  1.000 54.09150 ? 457 HOH A O   1 
HETATM 2227 O O   . HOH E 5 .   ? 25.35051 9.20669  -6.55164  1.000 23.85380 ? 458 HOH A O   1 
HETATM 2228 O O   . HOH E 5 .   ? 28.77176 25.55530 11.53295  1.000 48.26959 ? 459 HOH A O   1 
HETATM 2229 O O   . HOH E 5 .   ? 4.89758  18.61654 29.23686  1.000 44.41134 ? 460 HOH A O   1 
HETATM 2230 O O   . HOH E 5 .   ? 27.04050 3.42812  -4.07103  1.000 40.03264 ? 461 HOH A O   1 
HETATM 2231 O O   . HOH E 5 .   ? 25.12489 16.49163 25.22122  1.000 55.45493 ? 462 HOH A O   1 
HETATM 2232 O O   . HOH E 5 .   ? 8.60353  17.89560 18.28526  1.000 46.49202 ? 463 HOH A O   1 
HETATM 2233 O O   . HOH E 5 .   ? 27.32029 26.96412 9.59426   1.000 50.98642 ? 464 HOH A O   1 
HETATM 2234 O O   . HOH E 5 .   ? 11.32861 26.83984 0.12591   1.000 61.39425 ? 465 HOH A O   1 
HETATM 2235 O O   . HOH E 5 .   ? 23.20404 7.28783  11.05276  1.000 32.18421 ? 466 HOH A O   1 
HETATM 2236 O O   . HOH E 5 .   ? 24.43338 1.54314  -5.38850  1.000 41.70696 ? 467 HOH A O   1 
HETATM 2237 O O   . HOH E 5 .   ? 23.03659 -7.77827 -13.61830 1.000 39.40613 ? 468 HOH A O   1 
HETATM 2238 O O   . HOH E 5 .   ? 28.88528 2.34323  -10.54309 1.000 48.84231 ? 469 HOH A O   1 
HETATM 2239 O O   . HOH E 5 .   ? 30.00996 26.51903 1.01609   1.000 43.44039 ? 470 HOH A O   1 
HETATM 2240 O O   . HOH E 5 .   ? 21.33972 21.08438 1.36605   1.000 32.02867 ? 471 HOH A O   1 
HETATM 2241 O O   . HOH E 5 .   ? 31.98027 23.70207 25.58521  1.000 54.76650 ? 472 HOH A O   1 
HETATM 2242 O O   . HOH E 5 .   ? 26.20144 6.79333  -3.77409  1.000 24.59745 ? 473 HOH A O   1 
HETATM 2243 O O   . HOH E 5 .   ? 26.78596 21.43922 -14.72781 1.000 40.57755 ? 474 HOH A O   1 
HETATM 2244 O O   . HOH E 5 .   ? 34.74188 21.17285 22.71859  1.000 60.38686 ? 475 HOH A O   1 
HETATM 2245 O O   . HOH E 5 .   ? 23.70192 0.74154  -2.01538  1.000 48.19156 ? 476 HOH A O   1 
HETATM 2246 O O   . HOH E 5 .   ? 0.60707  26.13787 17.02046  1.000 55.58325 ? 477 HOH A O   1 
HETATM 2247 O O   . HOH E 5 .   ? 30.05954 4.40773  7.98624   1.000 43.39859 ? 478 HOH A O   1 
HETATM 2248 O O   . HOH E 5 .   ? 10.27177 14.36119 10.25752  1.000 44.57877 ? 479 HOH A O   1 
HETATM 2249 O O   . HOH E 5 .   ? 16.80882 34.30953 13.64130  1.000 64.05428 ? 480 HOH A O   1 
HETATM 2250 O O   . HOH E 5 .   ? 29.35718 28.74073 0.85807   1.000 58.68037 ? 481 HOH A O   1 
HETATM 2251 O O   . HOH E 5 .   ? 5.21602  26.77048 10.09557  1.000 44.33326 ? 482 HOH A O   1 
HETATM 2252 O O   . HOH E 5 .   ? 18.49940 19.72553 -14.09168 1.000 36.40231 ? 483 HOH A O   1 
HETATM 2253 O O   . HOH E 5 .   ? 32.34050 26.10475 25.49569  1.000 55.54112 ? 484 HOH A O   1 
HETATM 2254 O O   . HOH E 5 .   ? 5.75301  17.94100 12.57224  1.000 49.47312 ? 485 HOH A O   1 
HETATM 2255 O O   . HOH E 5 .   ? 33.62577 25.98676 11.99379  1.000 62.78437 ? 486 HOH A O   1 
HETATM 2256 O O   . HOH E 5 .   ? 10.19485 3.94518  -12.24006 1.000 49.72814 ? 487 HOH A O   1 
HETATM 2257 O O   . HOH E 5 .   ? 16.20292 19.30117 -15.97980 1.000 58.73158 ? 488 HOH A O   1 
HETATM 2258 O O   . HOH E 5 .   ? 31.08560 29.19456 23.34646  1.000 59.35303 ? 489 HOH A O   1 
HETATM 2259 O O   . HOH E 5 .   ? 12.39528 7.51039  7.66746   1.000 44.85729 ? 490 HOH A O   1 
HETATM 2260 O O   . HOH E 5 .   ? 13.04011 5.90798  4.30398   1.000 58.03583 ? 491 HOH A O   1 
HETATM 2261 O O   . HOH E 5 .   ? 27.79763 1.72810  1.01632   1.000 52.60201 ? 492 HOH A O   1 
HETATM 2262 O O   . HOH E 5 .   ? 0.93307  14.06644 -2.55897  1.000 55.97405 ? 493 HOH A O   1 
HETATM 2263 O O   . HOH E 5 .   ? 30.05413 4.78155  -1.84619  1.000 42.49636 ? 494 HOH A O   1 
HETATM 2264 O O   . HOH E 5 .   ? 35.94309 10.28490 23.81373  1.000 50.37918 ? 495 HOH A O   1 
HETATM 2265 O O   . HOH E 5 .   ? 13.50544 8.09552  5.67361   1.000 39.98855 ? 496 HOH A O   1 
HETATM 2266 O O   . HOH E 5 .   ? 31.67670 4.73473  -4.04837  1.000 36.09041 ? 497 HOH A O   1 
HETATM 2267 O O   . HOH E 5 .   ? 26.95768 -3.40342 -8.64518  1.000 44.03712 ? 498 HOH A O   1 
HETATM 2268 O O   . HOH E 5 .   ? 28.59167 28.97663 8.25123   1.000 57.66672 ? 499 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   ? 0.88321 0.69767 0.68275 0.00050  -0.03885 -0.00748 1   MET A N   
2    C CA  . MET A 1   ? 0.84050 0.68091 0.69680 0.02697  0.00137  -0.02264 1   MET A CA  
3    C C   . MET A 1   ? 0.84684 0.63459 0.62680 0.05822  0.00947  -0.05177 1   MET A C   
4    O O   . MET A 1   ? 0.88652 0.63659 0.58320 0.05166  0.03794  -0.07339 1   MET A O   
5    C CB  . MET A 1   ? 0.93500 0.82095 0.78841 0.03400  0.05417  -0.01909 1   MET A CB  
6    C CG  . MET A 1   ? 0.95302 0.87162 0.88906 0.00857  0.09143  -0.00301 1   MET A CG  
7    S SD  . MET A 1   ? 0.83963 0.80511 0.92331 -0.02530 0.09507  0.04187  1   MET A SD  
8    C CE  . MET A 1   ? 0.90169 0.84525 0.95333 -0.03987 0.08533  0.07514  1   MET A CE  
9    N N   . LYS A 2   ? 0.81469 0.60188 0.53770 0.10329  0.01531  -0.03259 2   LYS A N   
10   C CA  . LYS A 2   ? 0.76319 0.55090 0.47829 0.16565  0.02519  -0.05883 2   LYS A CA  
11   C C   . LYS A 2   ? 0.71931 0.50206 0.42382 0.16282  0.08204  -0.07321 2   LYS A C   
12   O O   . LYS A 2   ? 0.76265 0.47406 0.39653 0.15369  0.11485  -0.10279 2   LYS A O   
13   C CB  . LYS A 2   ? 0.75699 0.56585 0.50956 0.21048  -0.01750 -0.05202 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.76868 0.57117 0.54549 0.23347  -0.05399 -0.04429 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.78608 0.60831 0.59429 0.21192  -0.05500 -0.04641 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.84180 0.66094 0.62836 0.14190  -0.08836 -0.03021 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.88507 0.70165 0.65084 0.10399  -0.09826 -0.01558 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.65914 0.48829 0.37511 0.13606  0.10242  -0.06832 3   TYR A N   
19   C CA  . TYR A 3   ? 0.62334 0.49993 0.35327 0.09741  0.07794  -0.05088 3   TYR A CA  
20   C C   . TYR A 3   ? 0.58773 0.52811 0.34049 0.15232  0.04536  -0.07158 3   TYR A C   
21   O O   . TYR A 3   ? 0.57290 0.54463 0.36128 0.20574  0.02403  -0.09320 3   TYR A O   
22   C CB  . TYR A 3   ? 0.61955 0.51203 0.32755 0.04781  0.07788  -0.04922 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.62257 0.49770 0.32773 0.04538  0.08325  -0.04316 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.59642 0.50916 0.31218 0.03976  0.08880  -0.08764 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.61470 0.50603 0.33763 0.04907  0.05179  -0.05360 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.65423 0.54363 0.32817 0.01585  0.05551  -0.06199 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.63998 0.54090 0.32833 0.03752  0.03910  -0.05896 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.65547 0.57445 0.32126 0.02441  0.04953  -0.07062 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.67168 0.63583 0.29631 0.05039  0.08411  -0.10120 3   TYR A OH  
30   N N   . MET A 4   ? 0.58494 0.54007 0.32633 0.13347  0.04345  -0.05913 4   MET A N   
31   C CA  . MET A 4   ? 0.58021 0.55484 0.31989 0.15228  0.01829  -0.06369 4   MET A CA  
32   C C   . MET A 4   ? 0.48962 0.51619 0.29010 0.12816  0.02668  -0.06333 4   MET A C   
33   O O   . MET A 4   ? 0.48739 0.49522 0.30284 0.08233  0.03481  -0.04225 4   MET A O   
34   C CB  . MET A 4   ? 0.59037 0.63120 0.34410 0.20160  -0.00438 -0.04435 4   MET A CB  
35   C CG  . MET A 4   ? 0.57507 0.67483 0.34240 0.20015  -0.00747 -0.05780 4   MET A CG  
36   S SD  . MET A 4   ? 0.55629 0.71338 0.34565 0.19541  0.02449  -0.05009 4   MET A SD  
37   C CE  . MET A 4   ? 0.52307 0.73053 0.33549 0.21110  0.11391  -0.04813 4   MET A CE  
38   N N   . ILE A 5   ? 0.46815 0.50967 0.27042 0.13260  0.02706  -0.07254 5   ILE A N   
39   C CA  . ILE A 5   ? 0.43984 0.51328 0.27513 0.11812  0.01886  -0.02022 5   ILE A CA  
40   C C   . ILE A 5   ? 0.42210 0.55507 0.29206 0.07695  0.05845  -0.07268 5   ILE A C   
41   O O   . ILE A 5   ? 0.38668 0.60381 0.30048 0.06398  0.05204  -0.12372 5   ILE A O   
42   C CB  . ILE A 5   ? 0.40010 0.50723 0.28707 0.13873  0.01770  0.04695  5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.38838 0.50758 0.28962 0.09836  0.00765  0.03868  5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.38761 0.52554 0.33206 0.15898  0.06599  0.06673  5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.39182 0.47782 0.32036 0.07041  0.02537  0.04402  5   ILE A CD1 
46   N N   . THR A 6   ? 0.42932 0.54697 0.29564 0.05406  0.05332  -0.10761 6   THR A N   
47   C CA  . THR A 6   ? 0.45104 0.54951 0.31650 0.04026  0.04258  -0.12600 6   THR A CA  
48   C C   . THR A 6   ? 0.46368 0.56162 0.39198 -0.04285 0.05686  -0.13122 6   THR A C   
49   O O   . THR A 6   ? 0.50093 0.61099 0.45058 -0.03255 0.07282  -0.07197 6   THR A O   
50   C CB  . THR A 6   ? 0.52038 0.61165 0.36548 0.11105  0.08422  -0.08370 6   THR A CB  
51   O OG1 . THR A 6   ? 0.54523 0.64035 0.40081 0.01891  0.05260  -0.08025 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.61555 0.64972 0.39658 0.12211  0.07545  -0.06204 6   THR A CG2 
53   N N   . SER A 7   ? 0.48342 0.53045 0.38327 -0.05488 0.05400  -0.13242 7   SER A N   
54   C CA  . SER A 7   ? 0.52232 0.51857 0.38205 -0.04137 0.08225  -0.07105 7   SER A CA  
55   C C   . SER A 7   ? 0.53811 0.50917 0.40278 -0.02764 0.09036  -0.06088 7   SER A C   
56   O O   . SER A 7   ? 0.53799 0.52540 0.44758 0.00874  0.07913  -0.07903 7   SER A O   
57   C CB  . SER A 7   ? 0.50705 0.51867 0.37646 -0.01819 0.11755  -0.04900 7   SER A CB  
58   O OG  . SER A 7   ? 0.47391 0.54323 0.39332 0.01705  0.10141  -0.03207 7   SER A OG  
59   N N   . LYS A 8   ? 0.54821 0.51890 0.41624 -0.04932 0.12544  -0.04319 8   LYS A N   
60   C CA  . LYS A 8   ? 0.57192 0.53345 0.45680 -0.07795 0.13544  -0.05211 8   LYS A CA  
61   C C   . LYS A 8   ? 0.58845 0.55400 0.46916 -0.06679 0.15855  -0.04648 8   LYS A C   
62   O O   . LYS A 8   ? 0.62305 0.56513 0.48655 -0.09528 0.15665  -0.04351 8   LYS A O   
63   C CB  . LYS A 8   ? 0.55227 0.52496 0.46974 -0.04900 0.14397  -0.10174 8   LYS A CB  
64   C CG  . LYS A 8   ? 0.61335 0.54994 0.50501 -0.05906 0.11482  -0.11386 8   LYS A CG  
65   C CD  . LYS A 8   ? 0.71126 0.57717 0.54401 -0.06177 0.06966  -0.11632 8   LYS A CD  
66   C CE  . LYS A 8   ? 0.78649 0.60921 0.58004 -0.06797 0.05528  -0.09358 8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.83872 0.65184 0.61937 -0.05731 0.05230  -0.09256 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.59669 0.56603 0.46506 -0.04080 0.17208  -0.01561 9   GLY A N   
69   C CA  . GLY A 9   ? 0.56531 0.56448 0.48933 -0.04738 0.18551  -0.01369 9   GLY A CA  
70   C C   . GLY A 9   ? 0.63334 0.59068 0.50578 -0.00317 0.18544  -0.04971 9   GLY A C   
71   O O   . GLY A 9   ? 0.66808 0.57653 0.52668 -0.03374 0.16231  -0.04893 9   GLY A O   
72   N N   . ASP A 10  ? 0.67474 0.61153 0.50020 0.03006  0.20553  -0.06845 10  ASP A N   
73   C CA  . ASP A 10  ? 0.74892 0.59952 0.50958 0.03046  0.19986  -0.05567 10  ASP A CA  
74   C C   . ASP A 10  ? 0.75786 0.59530 0.50056 0.03347  0.21825  -0.03095 10  ASP A C   
75   O O   . ASP A 10  ? 0.75623 0.60445 0.49125 0.04625  0.24365  -0.00964 10  ASP A O   
76   C CB  . ASP A 10  ? 0.78271 0.61142 0.55499 0.03803  0.18732  -0.07115 10  ASP A CB  
77   C CG  . ASP A 10  ? 0.83649 0.62548 0.58188 0.05625  0.15473  -0.07930 10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.85515 0.61808 0.56641 0.07417  0.16235  -0.08982 10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.87888 0.65013 0.60746 0.03733  0.12640  -0.07884 10  ASP A OD2 
80   N N   . GLU A 11  ? 0.75994 0.58816 0.49056 0.01382  0.17452  0.00905  11  GLU A N   
81   C CA  . GLU A 11  ? 0.75556 0.62034 0.51377 0.02183  0.16297  0.02635  11  GLU A CA  
82   C C   . GLU A 11  ? 0.73186 0.61560 0.49359 0.03806  0.15100  0.01382  11  GLU A C   
83   O O   . GLU A 11  ? 0.72169 0.63493 0.50793 0.05429  0.14041  0.04824  11  GLU A O   
84   C CB  . GLU A 11  ? 0.77781 0.66140 0.56967 0.02027  0.12061  0.05619  11  GLU A CB  
85   C CG  . GLU A 11  ? 0.81464 0.72081 0.61960 -0.01310 0.09478  0.07540  11  GLU A CG  
86   C CD  . GLU A 11  ? 0.85673 0.77786 0.67670 -0.03325 0.06292  0.06630  11  GLU A CD  
87   O OE1 . GLU A 11  ? 0.87846 0.79665 0.68221 -0.01443 0.04306  0.06124  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 0.85316 0.79896 0.70328 -0.06598 0.06558  0.06513  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.72107 0.59376 0.47047 0.06229  0.15354  -0.01355 12  LYS A N   
90   C CA  . LYS A 12  ? 0.71673 0.60066 0.46079 0.04743  0.16688  -0.03156 12  LYS A CA  
91   C C   . LYS A 12  ? 0.71829 0.59593 0.40269 0.04641  0.17395  -0.02153 12  LYS A C   
92   O O   . LYS A 12  ? 0.74618 0.59512 0.37115 0.08032  0.20458  0.00829  12  LYS A O   
93   C CB  . LYS A 12  ? 0.74785 0.64355 0.52656 0.03808  0.14700  -0.01442 12  LYS A CB  
94   C CG  . LYS A 12  ? 0.75798 0.66950 0.56134 0.03729  0.17489  0.00337  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.74765 0.69850 0.58069 0.04944  0.20515  0.01159  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.74558 0.73707 0.60937 0.07475  0.19358  0.01595  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.75680 0.73091 0.61938 0.10935  0.18698  0.00698  12  LYS A NZ  
98   N N   . SER A 13  ? 0.71619 0.58917 0.40171 0.08693  0.17368  -0.04623 13  SER A N   
99   C CA  . SER A 13  ? 0.65563 0.53890 0.38604 0.11674  0.16303  -0.05080 13  SER A CA  
100  C C   . SER A 13  ? 0.60867 0.54509 0.40220 0.08522  0.17012  -0.00900 13  SER A C   
101  O O   . SER A 13  ? 0.59302 0.55018 0.39537 0.06509  0.15585  0.00703  13  SER A O   
102  C CB  . SER A 13  ? 0.65594 0.52351 0.39828 0.10201  0.10250  -0.06722 13  SER A CB  
103  O OG  . SER A 13  ? 0.66287 0.52034 0.40605 0.07405  0.06953  -0.08819 13  SER A OG  
104  N N   . ASP A 14  ? 0.63263 0.57891 0.40965 0.08749  0.19444  -0.00396 14  ASP A N   
105  C CA  . ASP A 14  ? 0.64138 0.61068 0.38969 0.05076  0.20522  -0.03346 14  ASP A CA  
106  C C   . ASP A 14  ? 0.66546 0.60039 0.36125 0.05654  0.16874  0.00618  14  ASP A C   
107  O O   . ASP A 14  ? 0.66395 0.60859 0.33181 0.08882  0.17826  0.00064  14  ASP A O   
108  C CB  . ASP A 14  ? 0.67583 0.66259 0.40665 -0.03908 0.20305  -0.04732 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.69824 0.71352 0.43725 -0.07929 0.20448  -0.10771 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.71307 0.73273 0.43204 -0.06090 0.19762  -0.13024 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.74120 0.74247 0.47533 -0.10289 0.19844  -0.12992 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.71025 0.58825 0.37804 0.06328  0.11197  -0.01419 15  LEU A N   
113  C CA  . LEU A 15  ? 0.70100 0.58073 0.37366 0.05648  0.10201  0.01205  15  LEU A CA  
114  C C   . LEU A 15  ? 0.62845 0.56437 0.35158 0.08214  0.10299  -0.00773 15  LEU A C   
115  O O   . LEU A 15  ? 0.61989 0.56871 0.36709 0.07758  0.06896  -0.01909 15  LEU A O   
116  C CB  . LEU A 15  ? 0.75588 0.59566 0.37888 0.01323  0.12282  0.02853  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.75861 0.60266 0.43027 0.01796  0.15098  0.03171  15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.76816 0.59461 0.46497 0.01209  0.12662  0.04864  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.74564 0.60871 0.44470 0.02243  0.18734  0.01929  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.59303 0.54827 0.33819 0.10554  0.10935  -0.00470 16  LEU A N   
121  C CA  . LEU A 16  ? 0.53737 0.57110 0.30604 0.08717  0.10610  -0.03443 16  LEU A CA  
122  C C   . LEU A 16  ? 0.51776 0.53359 0.31364 0.06496  0.06388  -0.03956 16  LEU A C   
123  O O   . LEU A 16  ? 0.57986 0.51053 0.31257 0.09362  0.02329  -0.03205 16  LEU A O   
124  C CB  . LEU A 16  ? 0.54576 0.64468 0.31179 0.10228  0.10180  -0.03534 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.58158 0.67311 0.30499 0.12711  0.08672  -0.04288 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.63308 0.68187 0.35421 0.14810  0.05244  -0.05232 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.57957 0.69063 0.28895 0.18836  0.08976  -0.07806 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.49947 0.54507 0.31495 0.08407  0.07772  -0.03124 17  ARG A N   
129  C CA  . ARG A 17  ? 0.48320 0.52936 0.30356 0.09142  0.08582  -0.06032 17  ARG A CA  
130  C C   . ARG A 17  ? 0.53882 0.52460 0.31121 0.11787  0.07693  -0.07094 17  ARG A C   
131  O O   . ARG A 17  ? 0.56398 0.50968 0.31655 0.15668  0.06471  -0.06839 17  ARG A O   
132  C CB  . ARG A 17  ? 0.44649 0.53521 0.30132 0.06227  0.06926  -0.06821 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.45822 0.54855 0.31770 0.05732  0.02991  -0.07505 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.48099 0.56093 0.31657 0.08694  0.04422  -0.09017 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.45136 0.57570 0.34699 0.09008  0.04869  -0.07210 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.46975 0.56559 0.37691 0.08328  0.07637  -0.07177 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.50624 0.57091 0.39804 0.04971  0.08858  -0.08198 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.51763 0.58162 0.41592 0.05034  0.06945  -0.06152 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.53481 0.53962 0.30518 0.09283  0.09968  -0.06719 18  LEU A N   
140  C CA  . LEU A 18  ? 0.55050 0.55135 0.29524 0.06692  0.09576  -0.04808 18  LEU A CA  
141  C C   . LEU A 18  ? 0.56066 0.53745 0.29855 0.10038  0.06350  -0.02596 18  LEU A C   
142  O O   . LEU A 18  ? 0.55792 0.53202 0.30187 0.11060  0.05296  0.00015  18  LEU A O   
143  C CB  . LEU A 18  ? 0.58281 0.58332 0.30336 0.00675  0.05870  -0.01347 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.54218 0.57484 0.34604 -0.02180 0.06129  0.02410  18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.54186 0.58940 0.32380 -0.02234 0.03361  0.02525  18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.53972 0.54615 0.36757 -0.00764 0.07881  0.04613  18  LEU A CD2 
147  N N   . ASN A 19  ? 0.60212 0.52034 0.29105 0.09626  0.05388  -0.03145 19  ASN A N   
148  C CA  . ASN A 19  ? 0.61031 0.54854 0.28980 0.12432  0.04957  -0.05456 19  ASN A CA  
149  C C   . ASN A 19  ? 0.58284 0.59452 0.30328 0.11254  0.01957  -0.09066 19  ASN A C   
150  O O   . ASN A 19  ? 0.63579 0.64057 0.28495 0.13922  -0.00781 -0.08844 19  ASN A O   
151  C CB  . ASN A 19  ? 0.63463 0.55246 0.32097 0.16287  0.05415  -0.04057 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.68203 0.54214 0.34960 0.16527  0.06623  -0.01700 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.77996 0.52986 0.30456 0.12521  0.08594  -0.02266 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.67214 0.56616 0.39108 0.22011  0.06121  -0.03864 19  ASN A ND2 
155  N N   . MET A 20  ? 0.48130 0.58696 0.28333 0.10006  0.04527  -0.08553 20  MET A N   
156  C CA  . MET A 20  ? 0.50161 0.60588 0.28826 0.13702  0.06950  -0.09122 20  MET A CA  
157  C C   . MET A 20  ? 0.55983 0.61184 0.28881 0.06337  0.06804  -0.06445 20  MET A C   
158  O O   . MET A 20  ? 0.62791 0.65275 0.30906 0.05560  0.07989  -0.06584 20  MET A O   
159  C CB  . MET A 20  ? 0.50546 0.60097 0.30490 0.13454  0.05235  -0.09532 20  MET A CB  
160  C CG  . MET A 20  ? 0.52693 0.61427 0.30333 0.18610  0.06598  -0.13221 20  MET A CG  
161  S SD  . MET A 20  ? 0.58146 0.62653 0.33353 0.15376  0.04352  -0.11037 20  MET A SD  
162  C CE  . MET A 20  ? 0.59663 0.62389 0.33931 0.06788  0.06417  -0.13054 20  MET A CE  
163  N N   . ILE A 21  ? 0.60412 0.59229 0.29017 0.08759  0.06903  -0.05850 21  ILE A N   
164  C CA  . ILE A 21  ? 0.54499 0.54539 0.28645 0.08724  0.02405  -0.05771 21  ILE A CA  
165  C C   . ILE A 21  ? 0.53241 0.51111 0.27526 0.11867  0.00603  -0.04543 21  ILE A C   
166  O O   . ILE A 21  ? 0.53583 0.54146 0.27604 0.11052  -0.00527 -0.01419 21  ILE A O   
167  C CB  . ILE A 21  ? 0.50879 0.56886 0.30748 0.04050  0.00651  -0.07366 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.47540 0.53049 0.28078 -0.03007 -0.02854 -0.06949 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.50669 0.59508 0.32227 0.06661  0.01742  -0.09395 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.51460 0.53231 0.30119 -0.00578 -0.00588 -0.08485 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.54206 0.50467 0.29088 0.08931  0.03150  -0.03446 22  ALA A N   
172  C CA  . ALA A 22  ? 0.59497 0.52228 0.32197 0.12725  0.03856  -0.04910 22  ALA A CA  
173  C C   . ALA A 22  ? 0.58805 0.55604 0.34573 0.14094  0.01235  -0.07826 22  ALA A C   
174  O O   . ALA A 22  ? 0.59021 0.56008 0.35870 0.17155  0.01297  -0.08575 22  ALA A O   
175  C CB  . ALA A 22  ? 0.63973 0.50680 0.32090 0.14821  0.06416  -0.02539 22  ALA A CB  
176  N N   . GLY A 23  ? 0.60562 0.58567 0.32052 0.11653  0.00268  -0.09673 23  GLY A N   
177  C CA  . GLY A 23  ? 0.59472 0.59314 0.29730 0.07651  -0.05143 -0.09828 23  GLY A CA  
178  C C   . GLY A 23  ? 0.59757 0.60489 0.35481 0.09341  -0.01842 -0.12200 23  GLY A C   
179  O O   . GLY A 23  ? 0.63537 0.62663 0.39037 0.11197  -0.00325 -0.11374 23  GLY A O   
180  N N   . PHE A 24  ? 0.55063 0.57054 0.32610 0.09090  -0.01318 -0.10786 24  PHE A N   
181  C CA  . PHE A 24  ? 0.58859 0.58449 0.38456 0.08773  -0.00026 -0.12241 24  PHE A CA  
182  C C   . PHE A 24  ? 0.63524 0.60046 0.40497 0.08680  0.01942  -0.12172 24  PHE A C   
183  O O   . PHE A 24  ? 0.70594 0.55665 0.40220 0.07648  0.01731  -0.17380 24  PHE A O   
184  C CB  . PHE A 24  ? 0.55311 0.57512 0.39165 0.07811  0.03395  -0.15676 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.55929 0.59246 0.42805 0.02936  0.06473  -0.14946 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.58396 0.60728 0.46080 -0.00379 0.07705  -0.15660 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.53967 0.56555 0.45404 0.02240  0.07150  -0.16830 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.58741 0.60755 0.45866 0.01483  0.10709  -0.17903 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.55715 0.59273 0.45613 -0.01522 0.09971  -0.17357 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.57730 0.59988 0.47345 0.00832  0.11063  -0.18047 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.61439 0.64305 0.42908 0.07554  0.01673  -0.09789 25  GLY A N   
192  C CA  . GLY A 25  ? 0.63712 0.67084 0.44264 0.10488  0.06005  -0.10730 25  GLY A CA  
193  C C   . GLY A 25  ? 0.68110 0.68888 0.43141 0.13051  0.06280  -0.11707 25  GLY A C   
194  O O   . GLY A 25  ? 0.69199 0.72460 0.41400 0.14732  0.08986  -0.11570 25  GLY A O   
195  N N   . GLU A 26  ? 0.71196 0.69491 0.44154 0.10635  0.07270  -0.12270 26  GLU A N   
196  C CA  . GLU A 26  ? 0.75309 0.71619 0.45472 0.09713  0.04067  -0.12033 26  GLU A CA  
197  C C   . GLU A 26  ? 0.77845 0.70100 0.49722 0.08952  0.02207  -0.16548 26  GLU A C   
198  O O   . GLU A 26  ? 0.80791 0.72264 0.53414 0.08973  -0.01230 -0.17211 26  GLU A O   
199  C CB  . GLU A 26  ? 0.78264 0.76301 0.42942 0.10362  0.04080  -0.08378 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.79712 0.78333 0.38668 0.12762  0.04106  -0.07384 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.85270 0.79652 0.41496 0.15319  0.04145  -0.07488 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.87011 0.80274 0.41827 0.20402  0.00336  0.00397  26  GLU A OE1 
203  O OE2 . GLU A 26  ? 0.88392 0.79318 0.40706 0.15561  0.09214  -0.13741 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.79549 0.66153 0.50033 0.11059  0.07576  -0.21823 27  TYR A N   
205  C CA  . TYR A 27  ? 0.79236 0.66030 0.56254 0.09096  0.10549  -0.19162 27  TYR A CA  
206  C C   . TYR A 27  ? 0.82117 0.65380 0.61423 0.07057  0.09789  -0.18496 27  TYR A C   
207  O O   . TYR A 27  ? 0.79637 0.62562 0.62879 0.09352  0.10877  -0.21266 27  TYR A O   
208  C CB  . TYR A 27  ? 0.75109 0.68847 0.57326 0.07800  0.14406  -0.14848 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.71040 0.69635 0.58975 0.06998  0.16133  -0.12900 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.69864 0.68868 0.59300 0.05948  0.18186  -0.13302 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.73852 0.71825 0.60907 0.06571  0.15195  -0.09348 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.67970 0.70765 0.59353 0.06137  0.19207  -0.10928 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.72336 0.73511 0.62346 0.07447  0.15469  -0.07496 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.69680 0.75515 0.61032 0.05831  0.20852  -0.05685 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.69222 0.82764 0.60483 0.01640  0.29924  -0.03201 27  TYR A OH  
216  N N   . ASP A 28  ? 0.85958 0.67994 0.62623 0.05778  0.09145  -0.18753 28  ASP A N   
217  C CA  . ASP A 28  ? 0.89338 0.70151 0.63437 0.04488  0.06270  -0.19450 28  ASP A CA  
218  C C   . ASP A 28  ? 0.92366 0.70926 0.61171 0.01981  0.07537  -0.20631 28  ASP A C   
219  O O   . ASP A 28  ? 0.96404 0.72150 0.63785 -0.00516 0.06350  -0.17621 28  ASP A O   
220  C CB  . ASP A 28  ? 0.89515 0.75145 0.68856 0.04539  0.04041  -0.16639 28  ASP A CB  
221  C CG  . ASP A 28  ? 0.91138 0.81481 0.74092 0.02431  0.03414  -0.12208 28  ASP A CG  
222  O OD1 . ASP A 28  ? 0.92303 0.83644 0.76710 0.03748  0.02045  -0.12327 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 0.91264 0.84922 0.75265 0.01234  0.04484  -0.09028 28  ASP A OD2 
224  N N   . MET A 29  ? 0.90564 0.71712 0.58327 0.01192  0.08556  -0.22733 29  MET A N   
225  C CA  . MET A 29  ? 0.88557 0.72561 0.58595 0.01298  0.08649  -0.21490 29  MET A CA  
226  C C   . MET A 29  ? 0.85928 0.73618 0.58355 0.02293  0.08251  -0.19686 29  MET A C   
227  O O   . MET A 29  ? 0.87343 0.78176 0.59449 0.02067  0.10633  -0.19344 29  MET A O   
228  C CB  . MET A 29  ? 0.89776 0.76094 0.58722 -0.01849 0.07324  -0.19727 29  MET A CB  
229  C CG  . MET A 29  ? 0.92734 0.79167 0.60323 -0.04479 0.06411  -0.19430 29  MET A CG  
230  S SD  . MET A 29  ? 0.94527 0.80228 0.61938 -0.06395 0.07587  -0.20863 29  MET A SD  
231  C CE  . MET A 29  ? 0.94267 0.78885 0.60911 -0.06219 0.05791  -0.21879 29  MET A CE  
232  N N   . GLU A 30  ? 0.82650 0.68376 0.56621 0.07579  0.06174  -0.20479 30  GLU A N   
233  C CA  . GLU A 30  ? 0.79337 0.65116 0.56532 0.11624  0.02791  -0.20022 30  GLU A CA  
234  C C   . GLU A 30  ? 0.74742 0.62346 0.51480 0.10811  0.04282  -0.20557 30  GLU A C   
235  O O   . GLU A 30  ? 0.77276 0.63289 0.46650 0.11017  0.04219  -0.22802 30  GLU A O   
236  C CB  . GLU A 30  ? 0.82834 0.70809 0.63599 0.12326  0.02009  -0.17987 30  GLU A CB  
237  C CG  . GLU A 30  ? 0.83899 0.75257 0.68909 0.12398  0.01043  -0.14049 30  GLU A CG  
238  C CD  . GLU A 30  ? 0.88375 0.79443 0.73598 0.12087  0.01723  -0.09457 30  GLU A CD  
239  O OE1 . GLU A 30  ? 0.89736 0.79246 0.74350 0.14111  0.03922  -0.09226 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 0.90841 0.82490 0.75848 0.10976  0.00669  -0.06834 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.67696 0.60737 0.48229 0.12948  0.05115  -0.19431 31  TYR A N   
242  C CA  . TYR A 31  ? 0.63859 0.62384 0.45257 0.16248  0.04198  -0.13723 31  TYR A CA  
243  C C   . TYR A 31  ? 0.63885 0.65234 0.44490 0.21795  0.05941  -0.11563 31  TYR A C   
244  O O   . TYR A 31  ? 0.64244 0.69716 0.45597 0.21932  0.06219  -0.06512 31  TYR A O   
245  C CB  . TYR A 31  ? 0.56317 0.62837 0.44430 0.16936  0.02088  -0.10166 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.50598 0.60452 0.40396 0.19267  0.04177  -0.11111 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.52823 0.62671 0.40038 0.18110  -0.02044 -0.09678 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.50453 0.60735 0.37847 0.13185  0.08074  -0.08722 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.52188 0.62855 0.40658 0.18241  0.00119  -0.09805 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.49743 0.59758 0.37696 0.13416  0.07696  -0.10586 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.51085 0.63399 0.38599 0.17165  0.03399  -0.09368 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.55850 0.67077 0.37191 0.17601  0.04301  -0.09316 31  TYR A OH  
253  N N   . ASP A 32  ? 0.66383 0.64470 0.43748 0.22734  0.03594  -0.11329 32  ASP A N   
254  C CA  . ASP A 32  ? 0.71089 0.65007 0.44711 0.21698  0.03083  -0.13787 32  ASP A CA  
255  C C   . ASP A 32  ? 0.69000 0.65545 0.44213 0.23423  0.02308  -0.14815 32  ASP A C   
256  O O   . ASP A 32  ? 0.72225 0.66409 0.41903 0.20436  0.03592  -0.16230 32  ASP A O   
257  C CB  . ASP A 32  ? 0.76879 0.69226 0.48265 0.21947  0.00044  -0.11910 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.80734 0.70769 0.51372 0.22581  -0.04959 -0.10732 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.79264 0.70572 0.51238 0.28597  -0.02363 -0.11326 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.86623 0.74142 0.53671 0.17751  -0.09004 -0.06845 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.64805 0.67671 0.46548 0.25212  0.01781  -0.13874 33  ASP A N   
262  C CA  . ASP A 33  ? 0.63437 0.69651 0.49158 0.24383  0.02919  -0.11517 33  ASP A CA  
263  C C   . ASP A 33  ? 0.62224 0.72802 0.49222 0.24495  0.01675  -0.07694 33  ASP A C   
264  O O   . ASP A 33  ? 0.61771 0.76769 0.45211 0.25782  0.00682  -0.08003 33  ASP A O   
265  C CB  . ASP A 33  ? 0.62587 0.70401 0.53400 0.23396  0.06164  -0.11556 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.65421 0.71595 0.59696 0.22040  0.04781  -0.09962 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.64321 0.71231 0.60878 0.27769  0.06144  -0.09471 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.66786 0.70925 0.62729 0.15940  0.03580  -0.10403 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.60853 0.71735 0.51334 0.23064  0.02179  -0.04937 34  VAL A N   
270  C CA  . VAL A 34  ? 0.61357 0.69844 0.54437 0.22914  -0.02072 -0.05764 34  VAL A CA  
271  C C   . VAL A 34  ? 0.65553 0.66757 0.52905 0.24056  -0.04363 -0.06259 34  VAL A C   
272  O O   . VAL A 34  ? 0.66821 0.67488 0.49843 0.23650  -0.05698 -0.12216 34  VAL A O   
273  C CB  . VAL A 34  ? 0.60933 0.72073 0.57957 0.19178  -0.01890 -0.07340 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.60589 0.73792 0.58683 0.16517  -0.04166 -0.08310 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.58668 0.74078 0.60357 0.19639  -0.01975 -0.08959 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.70916 0.64133 0.54883 0.24819  -0.02683 -0.03481 35  GLU A N   
277  C CA  . GLU A 35  ? 0.73740 0.64654 0.57452 0.24267  -0.02300 -0.03399 35  GLU A CA  
278  C C   . GLU A 35  ? 0.73387 0.62551 0.53907 0.23806  0.02744  -0.07648 35  GLU A C   
279  O O   . GLU A 35  ? 0.73596 0.67593 0.55296 0.23466  0.06452  -0.08128 35  GLU A O   
280  C CB  . GLU A 35  ? 0.79238 0.69048 0.62438 0.18907  -0.05704 -0.02570 35  GLU A CB  
281  C CG  . GLU A 35  ? 0.82421 0.73109 0.67033 0.14101  -0.09788 -0.01087 35  GLU A CG  
282  C CD  . GLU A 35  ? 0.83187 0.74903 0.69876 0.09211  -0.12829 0.01025  35  GLU A CD  
283  O OE1 . GLU A 35  ? 0.81200 0.73383 0.70836 0.07466  -0.14322 0.00298  35  GLU A OE1 
284  O OE2 . GLU A 35  ? 0.84914 0.77677 0.70699 0.06394  -0.13536 0.02403  35  GLU A OE2 
285  N N   . PRO A 36  ? 0.70142 0.58790 0.48694 0.23944  0.03192  -0.07337 36  PRO A N   
286  C CA  . PRO A 36  ? 0.71375 0.55882 0.46181 0.21240  0.05863  -0.09586 36  PRO A CA  
287  C C   . PRO A 36  ? 0.72577 0.53248 0.45717 0.19468  0.09632  -0.11168 36  PRO A C   
288  O O   . PRO A 36  ? 0.76932 0.56991 0.46141 0.17331  0.12322  -0.13168 36  PRO A O   
289  C CB  . PRO A 36  ? 0.70029 0.52683 0.43153 0.21315  0.03622  -0.09216 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.65508 0.53573 0.44521 0.23414  0.04680  -0.08902 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.66460 0.54655 0.45943 0.25613  0.03924  -0.07364 36  PRO A CD  
292  N N   . GLU A 37  ? 0.70733 0.52646 0.46828 0.18424  0.10038  -0.07786 37  GLU A N   
293  C CA  . GLU A 37  ? 0.70591 0.53957 0.47165 0.09747  0.08975  -0.05383 37  GLU A CA  
294  C C   . GLU A 37  ? 0.66110 0.49105 0.40459 0.05263  0.05511  -0.06906 37  GLU A C   
295  O O   . GLU A 37  ? 0.63975 0.48571 0.36916 -0.00688 0.03026  -0.07754 37  GLU A O   
296  C CB  . GLU A 37  ? 0.73454 0.59390 0.52183 0.07750  0.09214  -0.05204 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.75559 0.63870 0.57837 0.07380  0.06897  -0.04702 37  GLU A CG  
298  C CD  . GLU A 37  ? 0.78747 0.66343 0.62198 0.06321  0.03758  -0.05991 37  GLU A CD  
299  O OE1 . GLU A 37  ? 0.81928 0.65699 0.64244 0.06129  0.02079  -0.07590 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 0.77111 0.66083 0.63847 0.07095  0.03864  -0.05984 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.65309 0.46653 0.36730 0.06298  0.04318  -0.08833 38  ILE A N   
302  C CA  . ILE A 38  ? 0.63689 0.47778 0.36309 0.04530  0.01964  -0.07958 38  ILE A CA  
303  C C   . ILE A 38  ? 0.59713 0.44027 0.36111 0.08061  0.02378  -0.05075 38  ILE A C   
304  O O   . ILE A 38  ? 0.57630 0.41866 0.38228 0.08561  0.04740  -0.03615 38  ILE A O   
305  C CB  . ILE A 38  ? 0.65154 0.53888 0.35790 -0.01111 0.03462  -0.09268 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.68829 0.58130 0.36889 -0.06347 0.03220  -0.12055 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.66132 0.56767 0.37723 -0.01211 0.03390  -0.08769 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.69051 0.63362 0.38792 -0.08762 0.04064  -0.08552 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.57952 0.42570 0.31340 0.07432  0.02311  -0.06132 39  VAL A N   
310  C CA  . VAL A 39  ? 0.51710 0.41432 0.31314 0.06706  0.03675  -0.04999 39  VAL A CA  
311  C C   . VAL A 39  ? 0.46517 0.41817 0.29570 0.06963  0.06129  -0.05054 39  VAL A C   
312  O O   . VAL A 39  ? 0.49746 0.45523 0.31179 0.04946  0.08186  -0.00746 39  VAL A O   
313  C CB  . VAL A 39  ? 0.52959 0.39842 0.33640 0.05670  0.02103  -0.04205 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.53123 0.39017 0.36408 0.04311  0.05958  -0.03929 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.53428 0.40020 0.33938 0.06213  -0.00464 -0.01212 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.47852 0.42763 0.29552 0.06057  0.04608  -0.05434 40  ILE A N   
317  C CA  . ILE A 40  ? 0.49472 0.45648 0.29202 0.05965  0.06533  -0.05282 40  ILE A CA  
318  C C   . ILE A 40  ? 0.44025 0.43982 0.29141 0.07795  0.06921  -0.06115 40  ILE A C   
319  O O   . ILE A 40  ? 0.43165 0.42472 0.32915 0.08452  0.09031  -0.05686 40  ILE A O   
320  C CB  . ILE A 40  ? 0.54104 0.48006 0.30460 0.06177  0.06868  -0.06606 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.55357 0.49806 0.30811 0.04487  0.07002  -0.04854 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.54563 0.50014 0.29730 0.05558  0.07767  -0.06401 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.59409 0.49810 0.28382 0.04318  0.13181  -0.03990 40  ILE A CD1 
324  N N   . SER A 41  ? 0.41968 0.43603 0.27196 0.07079  0.03981  -0.08017 41  SER A N   
325  C CA  . SER A 41  ? 0.45956 0.46203 0.25837 0.05896  0.01252  -0.07175 41  SER A CA  
326  C C   . SER A 41  ? 0.47694 0.49399 0.26814 0.02931  0.05094  -0.06047 41  SER A C   
327  O O   . SER A 41  ? 0.46487 0.49039 0.32701 -0.01145 0.02209  -0.02472 41  SER A O   
328  C CB  . SER A 41  ? 0.58499 0.42643 0.25675 0.03920  0.02149  -0.14127 41  SER A CB  
329  O OG  . SER A 41  ? 0.64869 0.53757 0.29035 0.07972  0.08277  -0.10209 41  SER A OG  
330  N N   . ILE A 42  ? 0.45977 0.50921 0.24638 0.06024  0.09416  -0.04621 42  ILE A N   
331  C CA  . ILE A 42  ? 0.50814 0.48790 0.24154 0.06223  0.11616  -0.01688 42  ILE A CA  
332  C C   . ILE A 42  ? 0.53543 0.43331 0.24974 0.03834  0.14973  -0.03864 42  ILE A C   
333  O O   . ILE A 42  ? 0.56030 0.42491 0.26802 0.01646  0.14770  -0.04193 42  ILE A O   
334  C CB  . ILE A 42  ? 0.53694 0.49766 0.22451 0.08594  0.05530  -0.04097 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.47697 0.47673 0.25072 0.12724  0.06209  -0.06918 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.61245 0.55932 0.18590 0.07385  0.07697  0.00568  42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.45002 0.48997 0.25352 0.12062  0.02565  -0.04135 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.56368 0.39680 0.29728 0.11250  0.13612  -0.05763 43  GLY A N   
339  C CA  . GLY A 43  ? 0.58510 0.43828 0.33507 0.13155  0.17795  -0.07599 43  GLY A CA  
340  C C   . GLY A 43  ? 0.61645 0.52428 0.36744 0.13696  0.17808  -0.06629 43  GLY A C   
341  O O   . GLY A 43  ? 0.66767 0.60690 0.43271 0.06428  0.17353  -0.08073 43  GLY A O   
342  N N   . GLY A 44  ? 0.57818 0.51565 0.30838 0.10472  0.21103  -0.00700 44  GLY A N   
343  C CA  . GLY A 44  ? 0.54108 0.49377 0.27038 0.08666  0.14977  -0.04713 44  GLY A CA  
344  C C   . GLY A 44  ? 0.49666 0.51833 0.29308 0.05521  0.13284  -0.00332 44  GLY A C   
345  O O   . GLY A 44  ? 0.48871 0.49007 0.29358 0.06369  0.11466  -0.00830 44  GLY A O   
346  N N   . ASP A 45  ? 0.49667 0.60021 0.26816 0.08967  0.09002  0.00136  45  ASP A N   
347  C CA  . ASP A 45  ? 0.42894 0.62494 0.28367 0.07857  0.11589  0.02882  45  ASP A CA  
348  C C   . ASP A 45  ? 0.41806 0.61620 0.34510 0.04735  0.11392  -0.01205 45  ASP A C   
349  O O   . ASP A 45  ? 0.37080 0.61725 0.32736 0.04176  0.09844  -0.05055 45  ASP A O   
350  C CB  . ASP A 45  ? 0.42861 0.63881 0.28371 0.17432  0.11174  0.00357  45  ASP A CB  
351  C CG  . ASP A 45  ? 0.43495 0.66602 0.28630 0.20831  0.09457  -0.02977 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.44712 0.69813 0.30816 0.14485  0.09146  -0.02887 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.52414 0.72172 0.28673 0.23025  0.04133  -0.02928 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.43263 0.57170 0.35992 0.07307  0.13007  -0.05848 46  GLY A N   
355  C CA  . GLY A 46  ? 0.41047 0.53600 0.34779 0.02230  0.12726  -0.08441 46  GLY A CA  
356  C C   . GLY A 46  ? 0.43178 0.54914 0.33756 0.00144  0.12511  -0.05876 46  GLY A C   
357  O O   . GLY A 46  ? 0.43339 0.58362 0.33297 -0.00642 0.10494  -0.06908 46  GLY A O   
358  N N   . THR A 47  ? 0.43391 0.52015 0.31613 -0.00253 0.12893  -0.06854 47  THR A N   
359  C CA  . THR A 47  ? 0.42769 0.48839 0.28774 0.02049  0.10079  -0.08235 47  THR A CA  
360  C C   . THR A 47  ? 0.37365 0.46606 0.26737 0.02510  0.08357  -0.07201 47  THR A C   
361  O O   . THR A 47  ? 0.42397 0.43724 0.30817 -0.02043 0.08503  -0.04612 47  THR A O   
362  C CB  . THR A 47  ? 0.49694 0.50833 0.31099 0.02675  0.10420  -0.08100 47  THR A CB  
363  O OG1 . THR A 47  ? 0.63864 0.53926 0.34033 0.04043  0.12270  -0.06048 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.40410 0.50982 0.31550 0.01773  0.05841  -0.10371 47  THR A CG2 
365  N N   . PHE A 48  ? 0.36330 0.47983 0.23906 0.00218  0.07124  -0.05633 48  PHE A N   
366  C CA  . PHE A 48  ? 0.33369 0.47315 0.27747 -0.04551 0.04631  -0.04250 48  PHE A CA  
367  C C   . PHE A 48  ? 0.36770 0.47227 0.26552 -0.01628 0.04432  -0.02573 48  PHE A C   
368  O O   . PHE A 48  ? 0.40364 0.43936 0.27890 -0.02408 0.03947  -0.04529 48  PHE A O   
369  C CB  . PHE A 48  ? 0.36402 0.51696 0.30760 -0.02275 0.07094  -0.05896 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.37029 0.54226 0.29195 -0.02529 0.08094  -0.06445 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.38985 0.53183 0.26758 -0.06208 0.06709  -0.05187 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.41092 0.55421 0.32038 -0.02327 0.10053  -0.11094 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.43489 0.58636 0.28470 -0.03084 0.07716  -0.08045 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.46367 0.54747 0.30701 -0.02281 0.11628  -0.08289 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.45364 0.55768 0.26952 -0.00274 0.11446  -0.12289 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.33310 0.46259 0.23958 0.00382  0.05646  -0.03396 49  LEU A N   
377  C CA  . LEU A 49  ? 0.31152 0.49641 0.26496 0.06819  0.07473  -0.04998 49  LEU A CA  
378  C C   . LEU A 49  ? 0.33993 0.48797 0.29118 0.06156  0.08564  -0.06598 49  LEU A C   
379  O O   . LEU A 49  ? 0.33846 0.50852 0.31024 0.04103  0.03215  -0.06454 49  LEU A O   
380  C CB  . LEU A 49  ? 0.38977 0.52507 0.27157 0.09815  0.07597  -0.05169 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.41528 0.59435 0.33645 0.04680  0.08705  0.07742  49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.37928 0.53931 0.34472 0.02770  0.09253  0.11467  49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.56973 0.65822 0.39131 0.01652  0.06808  0.06034  49  LEU A CD2 
384  N N   . SER A 50  ? 0.34149 0.48068 0.29949 0.02687  0.09448  -0.06628 50  SER A N   
385  C CA  . SER A 50  ? 0.41441 0.47871 0.35547 -0.03256 0.08539  -0.08434 50  SER A CA  
386  C C   . SER A 50  ? 0.39982 0.49215 0.34402 -0.00785 0.08066  -0.09549 50  SER A C   
387  O O   . SER A 50  ? 0.43444 0.48265 0.35246 -0.00217 0.04486  -0.09327 50  SER A O   
388  C CB  . SER A 50  ? 0.52114 0.45941 0.43706 -0.09709 0.04104  -0.10413 50  SER A CB  
389  O OG  . SER A 50  ? 0.54127 0.47833 0.52611 -0.12672 0.08412  -0.06682 50  SER A OG  
390  N N   . ALA A 51  ? 0.38931 0.50221 0.30571 -0.03596 0.02829  -0.08819 51  ALA A N   
391  C CA  . ALA A 51  ? 0.40671 0.50252 0.30121 -0.01781 0.03064  -0.07199 51  ALA A CA  
392  C C   . ALA A 51  ? 0.36159 0.54309 0.29818 0.03116  0.01295  -0.06004 51  ALA A C   
393  O O   . ALA A 51  ? 0.38709 0.56471 0.33862 0.02640  -0.00293 -0.06246 51  ALA A O   
394  C CB  . ALA A 51  ? 0.42054 0.49236 0.30770 0.00425  0.02605  -0.08499 51  ALA A CB  
395  N N   . PHE A 52  ? 0.32580 0.54738 0.26946 0.05295  0.05434  -0.05874 52  PHE A N   
396  C CA  . PHE A 52  ? 0.33176 0.56665 0.29361 0.04083  0.04232  -0.01674 52  PHE A CA  
397  C C   . PHE A 52  ? 0.36371 0.59443 0.33031 0.03920  0.03311  -0.02290 52  PHE A C   
398  O O   . PHE A 52  ? 0.44575 0.60936 0.32006 0.04769  0.01346  -0.06348 52  PHE A O   
399  C CB  . PHE A 52  ? 0.32102 0.50011 0.27755 0.06642  0.06818  -0.00697 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.41468 0.47523 0.28520 0.08581  0.02964  0.01683  52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.47603 0.49631 0.30997 0.10445  0.00702  0.01693  52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.42121 0.44820 0.27059 0.09212  0.03747  -0.01973 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.52851 0.49326 0.31278 0.11593  0.04265  0.00549  52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.46000 0.46640 0.33782 0.08318  0.05079  -0.02555 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.49391 0.47960 0.34919 0.10510  0.03516  0.00239  52  PHE A CZ  
406  N N   . HIS A 53  ? 0.33222 0.61932 0.33450 0.07060  0.04675  -0.03060 53  HIS A N   
407  C CA  . HIS A 53  ? 0.29681 0.63042 0.32450 0.13579  0.04085  -0.07341 53  HIS A CA  
408  C C   . HIS A 53  ? 0.37297 0.66714 0.34436 0.16552  0.04176  -0.07375 53  HIS A C   
409  O O   . HIS A 53  ? 0.43539 0.68351 0.38513 0.19356  0.03765  -0.05894 53  HIS A O   
410  C CB  . HIS A 53  ? 0.27453 0.63990 0.30954 0.12491  0.05215  -0.08103 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.30703 0.63027 0.30457 0.10016  0.04821  -0.06955 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.34589 0.62632 0.30517 0.13019  0.04208  -0.07396 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.29085 0.62629 0.29737 0.10720  0.01324  -0.07429 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.30896 0.61784 0.33015 0.11732  0.04953  -0.05445 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.30620 0.61409 0.31173 0.07885  0.03612  -0.04212 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.37834 0.68762 0.35374 0.12478  0.05514  -0.11317 54  GLN A N   
417  C CA  . GLN A 54  ? 0.38714 0.70857 0.37148 0.13804  0.04959  -0.13769 54  GLN A CA  
418  C C   . GLN A 54  ? 0.44990 0.70476 0.40083 0.15639  0.05160  -0.10276 54  GLN A C   
419  O O   . GLN A 54  ? 0.51636 0.70970 0.44445 0.14488  0.03419  -0.07357 54  GLN A O   
420  C CB  . GLN A 54  ? 0.42345 0.74123 0.37990 0.12732  0.09956  -0.18078 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.44496 0.81096 0.40209 0.10701  0.11997  -0.16581 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.50529 0.84253 0.41639 0.10767  0.07386  -0.15229 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.50749 0.87334 0.39967 0.13827  0.06617  -0.11789 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.54270 0.83897 0.44829 0.07622  0.03201  -0.16406 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.48241 0.68566 0.37840 0.13271  0.05461  -0.10533 55  TYR A N   
426  C CA  . TYR A 55  ? 0.52487 0.64637 0.37698 0.11600  0.00918  -0.13032 55  TYR A CA  
427  C C   . TYR A 55  ? 0.51374 0.63268 0.40456 0.12021  0.01177  -0.08387 55  TYR A C   
428  O O   . TYR A 55  ? 0.57818 0.63955 0.40268 0.13411  0.00578  -0.03918 55  TYR A O   
429  C CB  . TYR A 55  ? 0.57274 0.65042 0.38385 0.12608  -0.00168 -0.13908 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.58835 0.65299 0.38694 0.14209  -0.00923 -0.14772 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.60644 0.67754 0.38756 0.17455  -0.00681 -0.13320 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.59014 0.63811 0.39317 0.11719  -0.02806 -0.15851 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.61783 0.68573 0.37547 0.17320  -0.02008 -0.11440 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.58408 0.66973 0.39739 0.13157  -0.03622 -0.13412 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.58808 0.69739 0.38284 0.17685  -0.02429 -0.12116 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.56161 0.73266 0.34976 0.21770  0.00404  -0.13608 55  TYR A OH  
437  N N   . GLU A 56  ? 0.46702 0.60232 0.39279 0.12108  0.01576  -0.11011 56  GLU A N   
438  C CA  . GLU A 56  ? 0.46881 0.62343 0.44927 0.10547  0.01159  -0.08118 56  GLU A CA  
439  C C   . GLU A 56  ? 0.47506 0.63380 0.47647 0.13108  -0.02929 -0.04921 56  GLU A C   
440  O O   . GLU A 56  ? 0.46876 0.64601 0.50937 0.13022  -0.10419 -0.00972 56  GLU A O   
441  C CB  . GLU A 56  ? 0.48995 0.63431 0.45048 0.09756  0.03146  -0.10140 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.55470 0.66932 0.47181 0.09063  0.01461  -0.12469 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.60668 0.73197 0.51886 0.11830  -0.00473 -0.12317 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.56628 0.74405 0.53041 0.23366  -0.03537 -0.12098 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.68071 0.76459 0.53677 0.09824  -0.01163 -0.14690 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.56505 0.62427 0.49319 0.13832  -0.00411 -0.07962 57  GLU A N   
447  C CA  . GLU A 57  ? 0.62076 0.64933 0.51520 0.15565  0.00220  -0.06084 57  GLU A CA  
448  C C   . GLU A 57  ? 0.65850 0.62984 0.49445 0.19052  0.01108  -0.02233 57  GLU A C   
449  O O   . GLU A 57  ? 0.70416 0.61264 0.50254 0.25159  -0.01898 0.02178  57  GLU A O   
450  C CB  . GLU A 57  ? 0.69977 0.70505 0.56905 0.11644  -0.02734 -0.07107 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.73440 0.74255 0.61638 0.10253  -0.05011 -0.08064 57  GLU A CG  
452  C CD  . GLU A 57  ? 0.77210 0.77247 0.68077 0.10778  -0.08113 -0.09444 57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.76028 0.77738 0.69417 0.12523  -0.09570 -0.07931 57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.80829 0.78237 0.70707 0.10036  -0.07854 -0.12129 57  GLU A OE2 
455  N N   . ARG A 58  ? 0.63448 0.59980 0.45850 0.20450  0.05246  -0.04859 58  ARG A N   
456  C CA  . ARG A 58  ? 0.61956 0.60375 0.45418 0.17725  0.06205  -0.04993 58  ARG A CA  
457  C C   . ARG A 58  ? 0.62756 0.54864 0.42935 0.18691  0.06673  -0.01830 58  ARG A C   
458  O O   . ARG A 58  ? 0.65192 0.54301 0.39062 0.16155  0.06908  -0.00134 58  ARG A O   
459  C CB  . ARG A 58  ? 0.62578 0.65120 0.47150 0.18934  0.08646  -0.07479 58  ARG A CB  
460  C CG  . ARG A 58  ? 0.66266 0.72175 0.50021 0.14698  0.05779  -0.05899 58  ARG A CG  
461  C CD  . ARG A 58  ? 0.67237 0.76010 0.50926 0.10414  0.05041  -0.06070 58  ARG A CD  
462  N NE  . ARG A 58  ? 0.70022 0.77060 0.53017 0.06716  0.03646  -0.04393 58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.73138 0.76232 0.54171 0.05871  0.06711  -0.01990 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.70330 0.74449 0.54465 0.05235  0.11582  0.01946  58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.74714 0.76215 0.53851 0.07730  0.04598  -0.03801 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.63289 0.53072 0.44533 0.21041  0.04445  -0.04581 59  LEU A N   
467  C CA  . LEU A 59  ? 0.61737 0.53546 0.43367 0.17294  0.00963  -0.04288 59  LEU A CA  
468  C C   . LEU A 59  ? 0.63564 0.53858 0.44918 0.16683  0.03022  -0.00721 59  LEU A C   
469  O O   . LEU A 59  ? 0.63463 0.57365 0.49096 0.15024  0.00532  -0.01942 59  LEU A O   
470  C CB  . LEU A 59  ? 0.60837 0.53558 0.40689 0.12851  0.05205  -0.06663 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.59504 0.54440 0.39053 0.08678  0.06574  -0.08911 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.55489 0.52225 0.37429 0.14083  0.10852  -0.12397 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.61303 0.52938 0.39883 0.02660  0.06895  -0.07416 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.66666 0.55271 0.45071 0.14883  0.05917  0.01393  60  ASP A N   
475  C CA  . ASP A 60  ? 0.75853 0.60270 0.48939 0.10183  0.06794  0.02734  60  ASP A CA  
476  C C   . ASP A 60  ? 0.75830 0.60720 0.48122 0.09555  0.05726  0.01649  60  ASP A C   
477  O O   . ASP A 60  ? 0.81494 0.65456 0.48470 0.09250  0.01806  0.03862  60  ASP A O   
478  C CB  . ASP A 60  ? 0.84935 0.66217 0.55825 0.04172  0.09504  0.00663  60  ASP A CB  
479  C CG  . ASP A 60  ? 0.92774 0.71937 0.61560 0.02552  0.10027  -0.05635 60  ASP A CG  
480  O OD1 . ASP A 60  ? 0.95901 0.72833 0.61510 0.03763  0.11296  -0.10345 60  ASP A OD1 
481  O OD2 . ASP A 60  ? 0.96615 0.76024 0.65334 0.00066  0.07896  -0.08942 60  ASP A OD2 
482  N N   . GLU A 61  ? 0.72074 0.60040 0.47471 0.11265  0.06043  -0.00084 61  GLU A N   
483  C CA  . GLU A 61  ? 0.71464 0.56195 0.46569 0.09664  0.06499  -0.01679 61  GLU A CA  
484  C C   . GLU A 61  ? 0.70993 0.50195 0.42277 0.09499  0.05591  -0.00906 61  GLU A C   
485  O O   . GLU A 61  ? 0.77444 0.48923 0.42342 0.08865  0.01759  -0.04305 61  GLU A O   
486  C CB  . GLU A 61  ? 0.75569 0.59160 0.49652 0.07494  0.09005  -0.02284 61  GLU A CB  
487  C CG  . GLU A 61  ? 0.81255 0.64964 0.54027 0.04172  0.08760  -0.02339 61  GLU A CG  
488  C CD  . GLU A 61  ? 0.84993 0.69396 0.58567 0.01530  0.08804  -0.01525 61  GLU A CD  
489  O OE1 . GLU A 61  ? 0.86095 0.69778 0.60347 0.01544  0.09409  -0.02529 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 0.85960 0.71763 0.59797 0.00150  0.09589  -0.00424 61  GLU A OE2 
491  N N   . ILE A 62  ? 0.67063 0.43892 0.39892 0.08719  0.04746  0.01383  62  ILE A N   
492  C CA  . ILE A 62  ? 0.64527 0.43152 0.41852 0.08021  0.05109  0.00185  62  ILE A CA  
493  C C   . ILE A 62  ? 0.61840 0.42743 0.36841 0.08976  0.00918  -0.01031 62  ILE A C   
494  O O   . ILE A 62  ? 0.66247 0.47475 0.32906 0.14179  0.03587  -0.04809 62  ILE A O   
495  C CB  . ILE A 62  ? 0.65326 0.40609 0.44140 0.07702  0.06199  0.00304  62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.63906 0.41376 0.46782 0.04293  0.06865  -0.02394 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.65506 0.39660 0.41385 0.10650  0.07767  0.00801  62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.66987 0.43243 0.48246 0.04358  0.06765  -0.00983 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.58843 0.40031 0.36903 0.02148  0.00027  -0.04545 63  ALA A N   
500  C CA  . ALA A 63  ? 0.57234 0.41122 0.35313 0.01968  -0.00942 -0.04570 63  ALA A CA  
501  C C   . ALA A 63  ? 0.58071 0.41238 0.34116 -0.00856 0.02428  -0.04914 63  ALA A C   
502  O O   . ALA A 63  ? 0.61664 0.41878 0.33679 -0.01397 0.03449  -0.05539 63  ALA A O   
503  C CB  . ALA A 63  ? 0.59901 0.41836 0.37649 0.02363  -0.05066 -0.04065 63  ALA A CB  
504  N N   . PHE A 64  ? 0.50430 0.40801 0.31919 -0.04013 0.04034  -0.07564 64  PHE A N   
505  C CA  . PHE A 64  ? 0.45542 0.46072 0.27641 -0.02031 0.05887  -0.06314 64  PHE A CA  
506  C C   . PHE A 64  ? 0.38574 0.48843 0.28201 -0.01489 0.05930  -0.07519 64  PHE A C   
507  O O   . PHE A 64  ? 0.40186 0.51864 0.31174 -0.08228 0.06417  -0.05752 64  PHE A O   
508  C CB  . PHE A 64  ? 0.45613 0.45871 0.25883 -0.00736 0.05547  -0.09344 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.45042 0.48067 0.29261 0.01489  0.05165  -0.07418 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.47388 0.46947 0.30956 0.02337  0.04855  -0.05446 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.44784 0.50824 0.31031 0.01602  0.02715  -0.07174 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.50993 0.47839 0.33194 -0.02298 0.08088  -0.07255 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.48961 0.51430 0.28374 -0.01014 0.04100  -0.06282 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.52642 0.51406 0.32930 -0.01680 0.09256  -0.08426 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.39989 0.45713 0.24144 -0.02437 0.01691  -0.04984 65  ILE A N   
516  C CA  . ILE A 65  ? 0.43056 0.44308 0.29928 0.00538  -0.01372 -0.06860 65  ILE A CA  
517  C C   . ILE A 65  ? 0.41619 0.45567 0.31508 0.02954  -0.00921 -0.08033 65  ILE A C   
518  O O   . ILE A 65  ? 0.40970 0.49993 0.36418 0.03642  0.02613  -0.06430 65  ILE A O   
519  C CB  . ILE A 65  ? 0.56280 0.46481 0.33542 0.00643  -0.07806 -0.08943 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.65410 0.52630 0.42048 0.04599  -0.04613 -0.04572 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.61434 0.48824 0.33833 0.03794  -0.08752 -0.09706 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.71734 0.58092 0.47805 0.04350  -0.03503 -0.03362 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.44127 0.41810 0.29641 0.06518  0.00718  -0.09147 66  GLY A N   
524  C CA  . GLY A 66  ? 0.48904 0.45351 0.29326 0.08712  0.04747  -0.05848 66  GLY A CA  
525  C C   . GLY A 66  ? 0.48898 0.48624 0.29084 0.13611  0.09471  -0.09185 66  GLY A C   
526  O O   . GLY A 66  ? 0.55663 0.50980 0.33567 0.14464  0.06424  -0.02821 66  GLY A O   
527  N N   . ILE A 67  ? 0.50574 0.49910 0.25086 0.10067  0.05682  -0.06584 67  ILE A N   
528  C CA  . ILE A 67  ? 0.48873 0.52983 0.26999 0.10876  0.06122  -0.06160 67  ILE A CA  
529  C C   . ILE A 67  ? 0.47446 0.53770 0.32106 0.11196  0.08550  -0.07961 67  ILE A C   
530  O O   . ILE A 67  ? 0.45756 0.59286 0.34447 0.08941  0.07076  -0.06805 67  ILE A O   
531  C CB  . ILE A 67  ? 0.50261 0.55324 0.26602 0.09839  0.02480  -0.09504 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.55178 0.59209 0.29281 0.13870  0.03250  -0.09618 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.50989 0.56578 0.24510 0.08432  0.01631  -0.06634 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.53092 0.65390 0.32489 0.14921  0.03407  -0.07483 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.48128 0.54567 0.33937 0.11742  0.09995  -0.06292 68  HIS A N   
536  C CA  . HIS A 68  ? 0.55636 0.54870 0.40842 0.10378  0.13168  0.01851  68  HIS A CA  
537  C C   . HIS A 68  ? 0.59036 0.57501 0.42430 0.15568  0.15197  0.06304  68  HIS A C   
538  O O   . HIS A 68  ? 0.66024 0.62693 0.46365 0.16630  0.10400  0.07225  68  HIS A O   
539  C CB  . HIS A 68  ? 0.60907 0.55845 0.45242 0.08899  0.10311  0.03920  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.63278 0.56625 0.46384 0.07132  0.11992  0.05030  68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.67704 0.57466 0.49922 0.00204  0.14124  0.05743  68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.63699 0.56980 0.43639 0.10355  0.18514  0.03488  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.68461 0.57304 0.47879 0.03048  0.19360  0.03553  68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.67726 0.58324 0.44344 0.09024  0.21850  0.01871  68  HIS A NE2 
545  N N   . THR A 69  ? 0.61579 0.56726 0.43587 0.17938  0.20794  0.07423  69  THR A N   
546  C CA  . THR A 69  ? 0.68854 0.58257 0.45737 0.14556  0.25138  0.07621  69  THR A CA  
547  C C   . THR A 69  ? 0.74938 0.64334 0.48498 0.13003  0.23379  0.06659  69  THR A C   
548  O O   . THR A 69  ? 0.80900 0.66572 0.50613 0.14484  0.19049  0.08599  69  THR A O   
549  C CB  . THR A 69  ? 0.67312 0.57382 0.48255 0.12852  0.25768  0.02378  69  THR A CB  
550  O OG1 . THR A 69  ? 0.68346 0.60425 0.51544 0.05971  0.27096  0.01251  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.66344 0.56778 0.50444 0.11941  0.25151  0.01559  69  THR A CG2 
552  N N   . GLY A 70  ? 0.76446 0.67241 0.48999 0.10055  0.18733  0.04495  70  GLY A N   
553  C CA  . GLY A 70  ? 0.77137 0.67226 0.50432 0.06392  0.16377  0.05094  70  GLY A CA  
554  C C   . GLY A 70  ? 0.76069 0.68523 0.50523 0.06396  0.16443  0.03479  70  GLY A C   
555  O O   . GLY A 70  ? 0.75628 0.67764 0.48412 0.05637  0.14115  0.04707  70  GLY A O   
556  N N   . HIS A 71  ? 0.77348 0.70373 0.54248 0.03903  0.18217  0.03193  71  HIS A N   
557  C CA  . HIS A 71  ? 0.77829 0.68953 0.56876 0.00914  0.14194  0.04074  71  HIS A CA  
558  C C   . HIS A 71  ? 0.72442 0.62292 0.51601 0.05586  0.13283  0.03346  71  HIS A C   
559  O O   . HIS A 71  ? 0.70087 0.61164 0.52815 0.09032  0.14647  0.04079  71  HIS A O   
560  C CB  . HIS A 71  ? 0.79669 0.72608 0.61787 -0.01025 0.10490  0.05023  71  HIS A CB  
561  C CG  . HIS A 71  ? 0.80447 0.78746 0.66902 -0.03062 0.04113  0.08806  71  HIS A CG  
562  N ND1 . HIS A 71  ? 0.81478 0.80965 0.69289 -0.04351 0.01770  0.09959  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 0.82152 0.81377 0.68498 -0.00794 0.00238  0.09820  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 0.83246 0.82397 0.70312 -0.04780 0.01445  0.09181  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 0.85375 0.82876 0.70584 -0.02022 0.00386  0.09312  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.66800 0.57534 0.44527 0.08857  0.11185  0.02019  72  LEU A N   
567  C CA  . LEU A 72  ? 0.66066 0.57248 0.40878 0.07345  0.06639  -0.00206 72  LEU A CA  
568  C C   . LEU A 72  ? 0.69761 0.57331 0.41392 0.11653  0.04792  -0.02025 72  LEU A C   
569  O O   . LEU A 72  ? 0.77889 0.57796 0.43470 0.13514  0.02574  -0.02225 72  LEU A O   
570  C CB  . LEU A 72  ? 0.63879 0.56937 0.40419 0.07856  0.05169  -0.01782 72  LEU A CB  
571  C CG  . LEU A 72  ? 0.58700 0.57181 0.43672 0.06826  0.05280  -0.04160 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.57546 0.57573 0.41386 0.06093  0.07088  -0.03154 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.55047 0.55266 0.45204 0.08527  0.00165  -0.08639 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.61968 0.58483 0.38486 0.11617  0.04213  -0.00060 73  GLY A N   
575  C CA  . GLY A 73  ? 0.53435 0.56425 0.37161 0.06209  0.05991  0.04428  73  GLY A CA  
576  C C   . GLY A 73  ? 0.58094 0.56019 0.41425 0.06709  0.00651  0.00047  73  GLY A C   
577  O O   . GLY A 73  ? 0.62021 0.51602 0.45353 0.01919  0.00100  0.03351  73  GLY A O   
578  N N   . PHE A 74  ? 0.51189 0.54925 0.33337 0.05480  0.00355  -0.03758 74  PHE A N   
579  C CA  . PHE A 74  ? 0.45852 0.55011 0.38110 0.06406  0.05545  -0.09922 74  PHE A CA  
580  C C   . PHE A 74  ? 0.48308 0.56323 0.42503 0.00189  0.06321  -0.11026 74  PHE A C   
581  O O   . PHE A 74  ? 0.57507 0.53463 0.47205 -0.00868 0.00398  -0.09368 74  PHE A O   
582  C CB  . PHE A 74  ? 0.42324 0.54154 0.34955 0.04297  0.04264  -0.08960 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.42636 0.49271 0.28749 -0.00210 0.01961  -0.10156 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.44787 0.52774 0.29756 -0.00709 -0.00398 -0.06032 74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.37625 0.50708 0.30624 0.02673  -0.02095 -0.06727 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.49320 0.56881 0.34657 -0.01879 0.04095  -0.01848 74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.44390 0.53216 0.32381 0.01763  0.03283  -0.05582 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.47111 0.57261 0.36745 -0.04352 0.02629  -0.02593 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.38073 0.55984 0.32617 -0.00334 0.06425  -0.18186 75  TYR A N   
590  C CA  . TYR A 75  ? 0.43845 0.54429 0.26041 -0.05749 0.09289  -0.12885 75  TYR A CA  
591  C C   . TYR A 75  ? 0.53783 0.52849 0.25022 -0.04703 0.09202  -0.12888 75  TYR A C   
592  O O   . TYR A 75  ? 0.57501 0.55806 0.30976 -0.08839 -0.05692 -0.09216 75  TYR A O   
593  C CB  . TYR A 75  ? 0.44347 0.52952 0.24807 -0.10095 0.05919  -0.06761 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.43723 0.51821 0.25498 -0.08415 0.04944  -0.09442 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.39914 0.47994 0.24412 -0.06237 0.02776  -0.11428 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.42196 0.48162 0.27736 -0.06052 0.06838  -0.07452 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.36450 0.46730 0.24660 -0.02488 0.00166  -0.12360 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.37621 0.47250 0.26374 -0.00411 0.06035  -0.05188 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.33006 0.44892 0.26281 0.01870  0.04513  -0.07835 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.30657 0.43597 0.26315 0.03431  0.03421  -0.03348 75  TYR A OH  
601  N N   . ALA A 76  ? 0.63638 0.53178 0.26087 -0.07155 0.13933  -0.05807 76  ALA A N   
602  C CA  . ALA A 76  ? 0.64898 0.53877 0.29503 -0.01514 0.09730  -0.04738 76  ALA A CA  
603  C C   . ALA A 76  ? 0.62664 0.54971 0.31706 0.01053  0.01379  -0.02422 76  ALA A C   
604  O O   . ALA A 76  ? 0.61074 0.57448 0.35511 -0.01956 0.00695  0.01713  76  ALA A O   
605  C CB  . ALA A 76  ? 0.67786 0.53827 0.33057 -0.06350 0.03344  -0.01096 76  ALA A CB  
606  N N   . ASP A 77  ? 0.64487 0.51817 0.27939 0.00059  0.01075  -0.02491 77  ASP A N   
607  C CA  . ASP A 77  ? 0.62254 0.59387 0.32676 0.02632  -0.08410 -0.01588 77  ASP A CA  
608  C C   . ASP A 77  ? 0.63364 0.63147 0.37319 -0.01999 -0.06423 -0.08521 77  ASP A C   
609  O O   . ASP A 77  ? 0.75343 0.69096 0.44676 -0.02266 -0.01984 -0.04931 77  ASP A O   
610  C CB  . ASP A 77  ? 0.64438 0.63254 0.29958 0.12769  -0.09536 -0.00002 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.67628 0.69140 0.35479 0.15047  -0.03379 0.04144  77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.75034 0.75721 0.36016 0.15664  -0.05617 0.07426  77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.72118 0.67597 0.44074 0.13664  -0.04298 0.05042  77  ASP A OD2 
614  N N   . TRP A 78  ? 0.60424 0.61351 0.48112 0.05765  -0.03732 -0.03384 78  TRP A N   
615  C CA  . TRP A 78  ? 0.57240 0.60665 0.51257 0.06669  -0.06675 -0.06400 78  TRP A CA  
616  C C   . TRP A 78  ? 0.51685 0.60246 0.44799 0.10338  -0.02500 -0.07871 78  TRP A C   
617  O O   . TRP A 78  ? 0.50755 0.57170 0.40159 0.10475  0.03661  -0.06182 78  TRP A O   
618  C CB  . TRP A 78  ? 0.65855 0.65976 0.62588 0.01819  -0.08837 -0.01464 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.73192 0.70411 0.71102 -0.01552 -0.10213 -0.02458 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.74831 0.71163 0.74553 -0.02362 -0.10543 -0.00511 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.78043 0.74713 0.74878 -0.00338 -0.06662 -0.05436 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.77787 0.76289 0.77284 -0.03588 -0.09883 -0.01888 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.80001 0.76158 0.76121 -0.01984 -0.07618 -0.05844 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.79586 0.73873 0.76267 0.01386  -0.02486 -0.08683 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.79996 0.75380 0.77123 -0.00202 -0.05004 -0.09132 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.79916 0.71568 0.76128 0.02469  -0.00439 -0.10645 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.78999 0.71385 0.76789 0.01195  -0.02044 -0.11072 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.52564 0.67103 0.44476 0.09110  -0.07642 -0.13361 79  ARG A N   
629  C CA  . ARG A 79  ? 0.55468 0.71487 0.45507 0.18336  -0.02616 -0.12072 79  ARG A CA  
630  C C   . ARG A 79  ? 0.57969 0.69717 0.45680 0.25028  -0.01084 -0.12837 79  ARG A C   
631  O O   . ARG A 79  ? 0.59074 0.70350 0.48823 0.31301  -0.05494 -0.12025 79  ARG A O   
632  C CB  . ARG A 79  ? 0.61185 0.74518 0.48519 0.19066  -0.01526 -0.09980 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.64532 0.74062 0.52562 0.20589  -0.04494 -0.10094 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.69522 0.75208 0.56014 0.16762  -0.04561 -0.06846 79  ARG A CD  
635  N NE  . ARG A 79  ? 0.71333 0.74972 0.58527 0.14303  -0.04921 -0.05777 79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.74446 0.75928 0.61887 0.10605  -0.05724 -0.03220 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.73800 0.74858 0.62167 0.09010  -0.06000 -0.04780 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.75683 0.76274 0.62277 0.09923  -0.07297 0.00062  79  ARG A NH2 
639  N N   . PRO A 80  ? 0.56189 0.70259 0.41652 0.21380  0.03626  -0.10899 80  PRO A N   
640  C CA  . PRO A 80  ? 0.60545 0.74725 0.44157 0.21678  -0.05326 -0.09991 80  PRO A CA  
641  C C   . PRO A 80  ? 0.66169 0.78221 0.49557 0.23357  -0.07491 -0.14360 80  PRO A C   
642  O O   . PRO A 80  ? 0.67367 0.81673 0.47331 0.23203  -0.07154 -0.19772 80  PRO A O   
643  C CB  . PRO A 80  ? 0.58453 0.74362 0.39704 0.20770  -0.03664 -0.06665 80  PRO A CB  
644  C CG  . PRO A 80  ? 0.57402 0.73143 0.42094 0.24053  -0.00523 -0.08168 80  PRO A CG  
645  C CD  . PRO A 80  ? 0.54679 0.71690 0.40148 0.18957  0.04005  -0.07441 80  PRO A CD  
646  N N   . ALA A 81  ? 0.67786 0.78172 0.54347 0.24556  -0.12015 -0.15236 81  ALA A N   
647  C CA  . ALA A 81  ? 0.67545 0.77766 0.57794 0.21124  -0.16656 -0.17583 81  ALA A CA  
648  C C   . ALA A 81  ? 0.68913 0.78340 0.58670 0.16554  -0.16268 -0.20905 81  ALA A C   
649  O O   . ALA A 81  ? 0.68993 0.80408 0.56761 0.19288  -0.16478 -0.25357 81  ALA A O   
650  C CB  . ALA A 81  ? 0.68111 0.78318 0.59319 0.23976  -0.15638 -0.16497 81  ALA A CB  
651  N N   . GLU A 82  ? 0.65660 0.77833 0.60247 0.11135  -0.15851 -0.20134 82  GLU A N   
652  C CA  . GLU A 82  ? 0.68764 0.78612 0.62091 0.09324  -0.12124 -0.18749 82  GLU A CA  
653  C C   . GLU A 82  ? 0.62914 0.77089 0.58477 0.10752  -0.08927 -0.20066 82  GLU A C   
654  O O   . GLU A 82  ? 0.58849 0.77114 0.57533 0.09613  -0.08740 -0.20539 82  GLU A O   
655  C CB  . GLU A 82  ? 0.75932 0.81091 0.65191 0.07344  -0.10024 -0.15804 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.78287 0.83420 0.67453 0.06322  -0.06900 -0.13922 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.80419 0.85419 0.67850 0.00798  -0.03641 -0.12050 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.81236 0.86306 0.68771 -0.00977 0.02010  -0.08468 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.82376 0.85544 0.68627 -0.00063 -0.05576 -0.12932 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.64300 0.77010 0.55566 0.10992  -0.04698 -0.21382 83  ALA A N   
661  C CA  . ALA A 83  ? 0.61785 0.76455 0.55994 0.07764  -0.02842 -0.19162 83  ALA A CA  
662  C C   . ALA A 83  ? 0.58755 0.75698 0.54127 0.09497  0.03106  -0.21672 83  ALA A C   
663  O O   . ALA A 83  ? 0.58420 0.77112 0.51281 0.07018  0.04696  -0.25082 83  ALA A O   
664  C CB  . ALA A 83  ? 0.65554 0.77956 0.58831 0.07198  -0.00095 -0.14311 83  ALA A CB  
665  N N   . ASP A 84  ? 0.62469 0.76313 0.57688 0.08426  0.01749  -0.20647 84  ASP A N   
666  C CA  . ASP A 84  ? 0.65543 0.78237 0.59206 0.08916  0.01579  -0.20345 84  ASP A CA  
667  C C   . ASP A 84  ? 0.64074 0.78767 0.58381 0.05233  0.02835  -0.23937 84  ASP A C   
668  O O   . ASP A 84  ? 0.61752 0.82470 0.54154 0.06227  0.02811  -0.27985 84  ASP A O   
669  C CB  . ASP A 84  ? 0.69942 0.81600 0.63214 0.10961  -0.00320 -0.15689 84  ASP A CB  
670  C CG  . ASP A 84  ? 0.76802 0.84870 0.67205 0.09771  -0.01420 -0.11288 84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.79122 0.86297 0.70467 0.09917  0.01089  -0.10433 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.80860 0.86541 0.68497 0.07812  -0.01617 -0.10077 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.64535 0.76342 0.60864 0.01363  0.06324  -0.25072 85  LYS A N   
674  C CA  . LYS A 85  ? 0.66209 0.74370 0.66548 -0.02905 0.06339  -0.23903 85  LYS A CA  
675  C C   . LYS A 85  ? 0.66752 0.71716 0.71215 -0.07708 0.06742  -0.21643 85  LYS A C   
676  O O   . LYS A 85  ? 0.68896 0.71282 0.74588 -0.11934 0.07562  -0.20273 85  LYS A O   
677  C CB  . LYS A 85  ? 0.68874 0.75733 0.67113 -0.01189 0.06273  -0.23953 85  LYS A CB  
678  N N   . LEU A 86  ? 0.64472 0.70573 0.70183 -0.05514 0.05421  -0.22073 86  LEU A N   
679  C CA  . LEU A 86  ? 0.66266 0.67709 0.69426 -0.01958 0.05604  -0.20450 86  LEU A CA  
680  C C   . LEU A 86  ? 0.68855 0.65231 0.67624 0.01124  0.06678  -0.22197 86  LEU A C   
681  O O   . LEU A 86  ? 0.71172 0.61754 0.67646 0.01033  0.06086  -0.24528 86  LEU A O   
682  C CB  . LEU A 86  ? 0.68007 0.67929 0.69475 -0.01544 0.02715  -0.18402 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.70350 0.67947 0.69785 -0.04161 0.00152  -0.14328 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.69750 0.70160 0.71225 -0.05839 -0.03859 -0.13139 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.74065 0.64852 0.69251 -0.07144 0.00226  -0.13797 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.66914 0.66183 0.65807 0.05273  0.10171  -0.22042 87  VAL A N   
687  C CA  . VAL A 87  ? 0.64201 0.66466 0.65851 0.06144  0.13188  -0.22023 87  VAL A CA  
688  C C   . VAL A 87  ? 0.67748 0.70174 0.69611 0.06654  0.14789  -0.21691 87  VAL A C   
689  O O   . VAL A 87  ? 0.69562 0.69838 0.70042 0.05237  0.14263  -0.22633 87  VAL A O   
690  C CB  . VAL A 87  ? 0.60504 0.65379 0.62898 0.06491  0.16570  -0.22923 87  VAL A CB  
691  C CG1 . VAL A 87  ? 0.60006 0.66276 0.59835 0.08030  0.16152  -0.23983 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.63328 0.65880 0.63367 0.04373  0.17136  -0.21873 87  VAL A CG2 
693  N N   . LYS A 88  ? 0.69745 0.72453 0.71531 0.06350  0.18299  -0.22225 88  LYS A N   
694  C CA  . LYS A 88  ? 0.73239 0.76092 0.75154 0.04450  0.16870  -0.18136 88  LYS A CA  
695  C C   . LYS A 88  ? 0.75672 0.73860 0.78313 0.04891  0.18591  -0.21683 88  LYS A C   
696  O O   . LYS A 88  ? 0.78517 0.69586 0.80278 0.02300  0.16853  -0.24232 88  LYS A O   
697  C CB  . LYS A 88  ? 0.73531 0.79567 0.76709 0.04662  0.13538  -0.13037 88  LYS A CB  
698  C CG  . LYS A 88  ? 0.75808 0.80687 0.76674 0.06796  0.10135  -0.10181 88  LYS A CG  
699  C CD  . LYS A 88  ? 0.77258 0.82003 0.77845 0.07343  0.05985  -0.07168 88  LYS A CD  
700  C CE  . LYS A 88  ? 0.77588 0.82675 0.77757 0.09401  0.03661  -0.06980 88  LYS A CE  
701  N NZ  . LYS A 88  ? 0.77905 0.84286 0.79016 0.11459  0.02158  -0.06667 88  LYS A NZ  
702  N N   . LEU A 89  ? 0.78818 0.74646 0.78854 0.02858  0.16685  -0.21583 89  LEU A N   
703  C CA  . LEU A 89  ? 0.76170 0.73152 0.78098 0.06204  0.20886  -0.21772 89  LEU A CA  
704  C C   . LEU A 89  ? 0.76253 0.72624 0.80157 0.06858  0.27436  -0.20638 89  LEU A C   
705  O O   . LEU A 89  ? 0.77270 0.71706 0.81624 0.03901  0.30513  -0.18707 89  LEU A O   
706  C CB  . LEU A 89  ? 0.78326 0.76828 0.79204 0.03361  0.14909  -0.17538 89  LEU A CB  
707  C CG  . LEU A 89  ? 0.76579 0.77350 0.79339 0.02969  0.11173  -0.15242 89  LEU A CG  
708  C CD1 . LEU A 89  ? 0.76774 0.78230 0.79908 0.03441  0.09081  -0.13377 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 0.74456 0.75909 0.78404 0.00547  0.10457  -0.16232 89  LEU A CD2 
710  N N   . LEU A 90  ? 0.73152 0.74639 0.81927 0.06366  0.29024  -0.18411 90  LEU A N   
711  C CA  . LEU A 90  ? 0.75399 0.75574 0.84684 0.06898  0.24728  -0.16174 90  LEU A CA  
712  C C   . LEU A 90  ? 0.84707 0.76554 0.87768 0.06131  0.23915  -0.14400 90  LEU A C   
713  O O   . LEU A 90  ? 0.88948 0.74827 0.88409 0.08431  0.26093  -0.13839 90  LEU A O   
714  C CB  . LEU A 90  ? 0.73234 0.78124 0.84719 0.04284  0.19779  -0.13359 90  LEU A CB  
715  C CG  . LEU A 90  ? 0.72515 0.79211 0.84278 0.02127  0.13342  -0.10938 90  LEU A CG  
716  C CD1 . LEU A 90  ? 0.66089 0.79584 0.84214 0.02069  0.13755  -0.09787 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 0.74411 0.78639 0.84423 0.03421  0.11048  -0.09579 90  LEU A CD2 
718  N N   . ALA A 91  ? 0.85448 0.77495 0.89361 0.03961  0.23398  -0.15849 91  ALA A N   
719  C CA  . ALA A 91  ? 0.88264 0.79870 0.90944 0.02045  0.20064  -0.15555 91  ALA A CA  
720  C C   . ALA A 91  ? 0.91088 0.82919 0.91665 0.01745  0.17218  -0.15862 91  ALA A C   
721  O O   . ALA A 91  ? 0.91527 0.84909 0.91136 0.01064  0.17421  -0.14795 91  ALA A O   
722  C CB  . ALA A 91  ? 0.88233 0.79915 0.90909 0.02469  0.21009  -0.15737 91  ALA A CB  
723  N N   . LYS A 92  ? 0.92695 0.84563 0.92010 0.01184  0.15195  -0.17485 92  LYS A N   
724  C CA  . LYS A 92  ? 0.93727 0.86237 0.91664 0.02296  0.14079  -0.17859 92  LYS A CA  
725  C C   . LYS A 92  ? 0.98110 0.85934 0.90387 0.04006  0.14839  -0.18877 92  LYS A C   
726  O O   . LYS A 92  ? 0.99726 0.84790 0.90126 0.09079  0.16751  -0.21575 92  LYS A O   
727  C CB  . LYS A 92  ? 0.91153 0.87872 0.93165 0.02961  0.12349  -0.16697 92  LYS A CB  
728  C CG  . LYS A 92  ? 0.90778 0.89527 0.94139 0.01830  0.10579  -0.14954 92  LYS A CG  
729  C CD  . LYS A 92  ? 0.91354 0.90668 0.94577 0.00616  0.09049  -0.14550 92  LYS A CD  
730  C CE  . LYS A 92  ? 0.90898 0.92029 0.94360 -0.00346 0.07339  -0.14130 92  LYS A CE  
731  N NZ  . LYS A 92  ? 0.89416 0.92397 0.94438 -0.01394 0.06805  -0.13610 92  LYS A NZ  
732  N N   . GLY A 93  ? 0.98537 0.86906 0.89334 0.00244  0.14055  -0.17910 93  GLY A N   
733  C CA  . GLY A 93  ? 0.96672 0.87130 0.89107 -0.03771 0.12323  -0.17293 93  GLY A CA  
734  C C   . GLY A 93  ? 0.93429 0.85780 0.88064 -0.04488 0.10883  -0.16962 93  GLY A C   
735  O O   . GLY A 93  ? 0.94789 0.86903 0.86941 -0.04649 0.08601  -0.19120 93  GLY A O   
736  N N   . GLU A 94  ? 0.89828 0.81585 0.89290 -0.03887 0.10352  -0.11511 94  GLU A N   
737  C CA  . GLU A 94  ? 0.86463 0.78411 0.91136 -0.02978 0.07771  -0.05658 94  GLU A CA  
738  C C   . GLU A 94  ? 0.87049 0.81542 0.90019 -0.03547 0.09076  -0.05550 94  GLU A C   
739  O O   . GLU A 94  ? 0.89295 0.83859 0.90551 -0.04955 0.11126  -0.05226 94  GLU A O   
740  C CB  . GLU A 94  ? 0.84751 0.76506 0.91646 -0.02928 0.05832  -0.01692 94  GLU A CB  
741  C CG  . GLU A 94  ? 0.87474 0.76588 0.94203 -0.01344 0.04576  0.01094  94  GLU A CG  
742  C CD  . GLU A 94  ? 0.85219 0.73911 0.95311 -0.00933 0.05071  0.03334  94  GLU A CD  
743  O OE1 . GLU A 94  ? 0.83567 0.71220 0.97483 0.01320  0.07497  0.05237  94  GLU A OE1 
744  O OE2 . GLU A 94  ? 0.83020 0.75530 0.96755 -0.01750 0.04896  0.04947  94  GLU A OE2 
745  N N   . TYR A 95  ? 0.85931 0.80829 0.86929 -0.04224 0.08577  -0.06356 95  TYR A N   
746  C CA  . TYR A 95  ? 0.84727 0.78884 0.83162 -0.04945 0.06784  -0.06478 95  TYR A CA  
747  C C   . TYR A 95  ? 0.83195 0.79762 0.80322 -0.06344 0.05158  -0.07022 95  TYR A C   
748  O O   . TYR A 95  ? 0.84800 0.79381 0.81267 -0.05374 0.05551  -0.05783 95  TYR A O   
749  C CB  . TYR A 95  ? 0.82586 0.74611 0.81735 -0.05223 0.06060  -0.05273 95  TYR A CB  
750  C CG  . TYR A 95  ? 0.79971 0.71002 0.80972 -0.06757 0.03733  -0.03504 95  TYR A CG  
751  C CD1 . TYR A 95  ? 0.79746 0.69960 0.81908 -0.07929 0.01726  -0.02052 95  TYR A CD1 
752  C CD2 . TYR A 95  ? 0.79964 0.69591 0.81508 -0.04462 0.02300  -0.02700 95  TYR A CD2 
753  C CE1 . TYR A 95  ? 0.79257 0.70111 0.81850 -0.06875 -0.00164 -0.01609 95  TYR A CE1 
754  C CE2 . TYR A 95  ? 0.79789 0.68310 0.81997 -0.02815 0.00115  -0.03339 95  TYR A CE2 
755  C CZ  . TYR A 95  ? 0.79766 0.70043 0.82391 -0.02420 -0.00952 -0.02901 95  TYR A CZ  
756  O OH  . TYR A 95  ? 0.82361 0.71895 0.82947 0.00929  -0.02288 -0.02761 95  TYR A OH  
757  N N   . GLN A 96  ? 0.78734 0.79816 0.76333 -0.07994 0.02515  -0.08423 96  GLN A N   
758  C CA  . GLN A 96  ? 0.76881 0.76387 0.69695 -0.10371 0.01776  -0.09172 96  GLN A CA  
759  C C   . GLN A 96  ? 0.71389 0.69554 0.63579 -0.12876 0.02387  -0.09904 96  GLN A C   
760  O O   . GLN A 96  ? 0.70809 0.70919 0.60910 -0.16451 -0.00957 -0.10935 96  GLN A O   
761  C CB  . GLN A 96  ? 0.81864 0.80484 0.71838 -0.07740 0.01603  -0.07020 96  GLN A CB  
762  C CG  . GLN A 96  ? 0.86488 0.83294 0.74852 -0.06784 0.01882  -0.06083 96  GLN A CG  
763  C CD  . GLN A 96  ? 0.88155 0.85104 0.77122 -0.06808 0.02511  -0.05238 96  GLN A CD  
764  O OE1 . GLN A 96  ? 0.85723 0.85567 0.77638 -0.06574 0.03331  -0.05531 96  GLN A OE1 
765  N NE2 . GLN A 96  ? 0.89396 0.85298 0.78332 -0.08044 0.02055  -0.04463 96  GLN A NE2 
766  N N   . LYS A 97  ? 0.62103 0.59769 0.57625 -0.10254 0.07884  -0.13713 97  LYS A N   
767  C CA  . LYS A 97  ? 0.59381 0.57817 0.56447 -0.08536 0.10739  -0.09844 97  LYS A CA  
768  C C   . LYS A 97  ? 0.58444 0.58140 0.52018 -0.08013 0.12878  -0.10797 97  LYS A C   
769  O O   . LYS A 97  ? 0.60470 0.58573 0.55152 -0.09333 0.10821  -0.08329 97  LYS A O   
770  C CB  . LYS A 97  ? 0.59264 0.56254 0.59637 -0.07866 0.12825  -0.04796 97  LYS A CB  
771  C CG  . LYS A 97  ? 0.60415 0.57893 0.61553 -0.05936 0.12932  -0.01470 97  LYS A CG  
772  C CD  . LYS A 97  ? 0.63016 0.60928 0.64656 -0.03035 0.09422  -0.01011 97  LYS A CD  
773  C CE  . LYS A 97  ? 0.65361 0.65193 0.67269 -0.02230 0.08121  -0.01326 97  LYS A CE  
774  N NZ  . LYS A 97  ? 0.67159 0.67016 0.68732 0.02427  0.10768  -0.01575 97  LYS A NZ  
775  N N   . VAL A 98  ? 0.55442 0.57053 0.48152 -0.07700 0.09458  -0.11413 98  VAL A N   
776  C CA  . VAL A 98  ? 0.51066 0.57075 0.44982 -0.04377 0.08041  -0.13428 98  VAL A CA  
777  C C   . VAL A 98  ? 0.47355 0.52575 0.40185 -0.03591 0.07888  -0.11445 98  VAL A C   
778  O O   . VAL A 98  ? 0.49076 0.54926 0.38829 -0.05662 0.01599  -0.10662 98  VAL A O   
779  C CB  . VAL A 98  ? 0.53933 0.62412 0.47428 0.00156  0.02029  -0.16634 98  VAL A CB  
780  C CG1 . VAL A 98  ? 0.59023 0.65334 0.50984 0.02301  -0.00699 -0.15914 98  VAL A CG1 
781  C CG2 . VAL A 98  ? 0.56445 0.64454 0.48264 0.01544  -0.03623 -0.18730 98  VAL A CG2 
782  N N   . SER A 99  ? 0.49582 0.49187 0.39424 -0.04787 0.10708  -0.11361 99  SER A N   
783  C CA  . SER A 99  ? 0.52903 0.45496 0.39516 -0.06754 0.07913  -0.10548 99  SER A CA  
784  C C   . SER A 99  ? 0.48120 0.46660 0.39023 -0.03278 0.06802  -0.06490 99  SER A C   
785  O O   . SER A 99  ? 0.46875 0.47866 0.41856 -0.03807 0.05267  -0.05967 99  SER A O   
786  C CB  . SER A 99  ? 0.61911 0.43739 0.46232 -0.10275 0.04154  -0.15892 99  SER A CB  
787  O OG  . SER A 99  ? 0.64724 0.46867 0.51630 -0.10482 0.05511  -0.13848 99  SER A OG  
788  N N   . TYR A 100 ? 0.43906 0.46737 0.34042 -0.00164 0.04550  -0.10245 100 TYR A N   
789  C CA  . TYR A 100 ? 0.44128 0.46385 0.30871 0.04462  0.04546  -0.07933 100 TYR A CA  
790  C C   . TYR A 100 ? 0.44035 0.43161 0.31189 0.08218  0.04378  -0.03693 100 TYR A C   
791  O O   . TYR A 100 ? 0.46655 0.42256 0.32122 0.09973  0.05347  0.00722  100 TYR A O   
792  C CB  . TYR A 100 ? 0.45765 0.46589 0.31095 0.00899  0.03338  -0.06267 100 TYR A CB  
793  C CG  . TYR A 100 ? 0.47158 0.50025 0.30653 0.04098  -0.01075 -0.09361 100 TYR A CG  
794  C CD1 . TYR A 100 ? 0.49624 0.50842 0.29226 0.03504  -0.05450 -0.11350 100 TYR A CD1 
795  C CD2 . TYR A 100 ? 0.48148 0.53166 0.28748 0.06924  0.02348  -0.10228 100 TYR A CD2 
796  C CE1 . TYR A 100 ? 0.54059 0.52230 0.30694 0.03846  -0.05419 -0.09449 100 TYR A CE1 
797  C CE2 . TYR A 100 ? 0.51514 0.54438 0.31078 0.08237  -0.01186 -0.08214 100 TYR A CE2 
798  C CZ  . TYR A 100 ? 0.58072 0.55824 0.30361 0.06901  -0.03035 -0.09368 100 TYR A CZ  
799  O OH  . TYR A 100 ? 0.59699 0.61090 0.37242 0.07992  -0.04707 -0.10235 100 TYR A OH  
800  N N   . PRO A 101 ? 0.41093 0.40280 0.29964 0.05120  0.05531  -0.03274 101 PRO A N   
801  C CA  . PRO A 101 ? 0.37581 0.43380 0.26199 0.02454  0.03818  -0.00343 101 PRO A CA  
802  C C   . PRO A 101 ? 0.35188 0.45777 0.26849 0.07136  0.02915  -0.01324 101 PRO A C   
803  O O   . PRO A 101 ? 0.38372 0.45763 0.28814 0.03100  0.00467  0.00494  101 PRO A O   
804  C CB  . PRO A 101 ? 0.35637 0.45499 0.30568 0.01527  0.04075  -0.01050 101 PRO A CB  
805  C CG  . PRO A 101 ? 0.36106 0.44274 0.30160 0.01915  -0.00584 0.00230  101 PRO A CG  
806  C CD  . PRO A 101 ? 0.38524 0.41732 0.31049 -0.00755 0.00482  -0.02979 101 PRO A CD  
807  N N   . LEU A 102 ? 0.34666 0.46840 0.27561 0.06965  0.00747  -0.05944 102 LEU A N   
808  C CA  . LEU A 102 ? 0.34888 0.41203 0.26291 0.09804  0.02184  -0.08763 102 LEU A CA  
809  C C   . LEU A 102 ? 0.37092 0.43925 0.26993 0.09977  -0.00510 -0.05599 102 LEU A C   
810  O O   . LEU A 102 ? 0.39832 0.46765 0.30518 0.10996  0.00603  -0.01035 102 LEU A O   
811  C CB  . LEU A 102 ? 0.36219 0.36066 0.28653 0.10071  0.03676  -0.06770 102 LEU A CB  
812  C CG  . LEU A 102 ? 0.41084 0.33339 0.28834 0.12008  0.02953  -0.01267 102 LEU A CG  
813  C CD1 . LEU A 102 ? 0.44808 0.39210 0.32655 0.08556  0.02843  -0.00511 102 LEU A CD1 
814  C CD2 . LEU A 102 ? 0.48732 0.27513 0.33931 0.09504  0.01210  0.00141  102 LEU A CD2 
815  N N   . LEU A 103 ? 0.37496 0.38883 0.26810 0.09011  -0.01246 -0.05380 103 LEU A N   
816  C CA  . LEU A 103 ? 0.39455 0.42010 0.25012 0.09309  -0.00325 -0.03200 103 LEU A CA  
817  C C   . LEU A 103 ? 0.41419 0.47757 0.25349 0.11876  0.00789  0.01004  103 LEU A C   
818  O O   . LEU A 103 ? 0.39383 0.51164 0.25204 0.08274  0.03284  0.01343  103 LEU A O   
819  C CB  . LEU A 103 ? 0.39253 0.38959 0.28033 0.07511  -0.02883 -0.01687 103 LEU A CB  
820  C CG  . LEU A 103 ? 0.31069 0.32939 0.26438 0.07402  0.03252  0.00715  103 LEU A CG  
821  C CD1 . LEU A 103 ? 0.32366 0.33977 0.29762 0.07461  0.01054  0.04090  103 LEU A CD1 
822  C CD2 . LEU A 103 ? 0.36488 0.34077 0.28173 0.07018  -0.01287 0.03185  103 LEU A CD2 
823  N N   . LYS A 104 ? 0.37192 0.52222 0.28456 0.16184  -0.00547 0.04606  104 LYS A N   
824  C CA  . LYS A 104 ? 0.38817 0.56225 0.28858 0.19625  -0.05622 0.04582  104 LYS A CA  
825  C C   . LYS A 104 ? 0.36709 0.57701 0.30128 0.14619  -0.02104 0.01249  104 LYS A C   
826  O O   . LYS A 104 ? 0.37791 0.57018 0.29537 0.13387  0.01459  -0.00661 104 LYS A O   
827  C CB  . LYS A 104 ? 0.42316 0.60026 0.34856 0.26418  -0.04932 0.00431  104 LYS A CB  
828  C CG  . LYS A 104 ? 0.47043 0.62587 0.37494 0.27334  -0.08286 -0.07338 104 LYS A CG  
829  C CD  . LYS A 104 ? 0.57022 0.63488 0.44566 0.23913  -0.07723 -0.12119 104 LYS A CD  
830  C CE  . LYS A 104 ? 0.59157 0.62183 0.48068 0.27628  -0.02468 -0.16588 104 LYS A CE  
831  N NZ  . LYS A 104 ? 0.58627 0.64787 0.49617 0.29476  -0.03178 -0.18004 104 LYS A NZ  
832  N N   . THR A 105 ? 0.37029 0.61675 0.31361 0.17323  0.01110  0.00675  105 THR A N   
833  C CA  . THR A 105 ? 0.36632 0.65893 0.32869 0.15930  0.01025  0.05070  105 THR A CA  
834  C C   . THR A 105 ? 0.35095 0.64914 0.32703 0.20507  0.01693  0.04211  105 THR A C   
835  O O   . THR A 105 ? 0.37880 0.69188 0.33503 0.24009  0.05121  0.03880  105 THR A O   
836  C CB  . THR A 105 ? 0.37913 0.70238 0.35621 0.14408  -0.01475 0.10089  105 THR A CB  
837  O OG1 . THR A 105 ? 0.35464 0.73149 0.34447 0.12719  -0.01341 0.14408  105 THR A OG1 
838  C CG2 . THR A 105 ? 0.38953 0.72414 0.38210 0.11212  -0.01722 0.09259  105 THR A CG2 
839  N N   . THR A 106 ? 0.33124 0.58932 0.32630 0.18149  -0.03500 0.03294  106 THR A N   
840  C CA  . THR A 106 ? 0.39171 0.60526 0.34482 0.16986  -0.02482 0.04980  106 THR A CA  
841  C C   . THR A 106 ? 0.36306 0.65094 0.36172 0.15530  -0.01589 0.04638  106 THR A C   
842  O O   . THR A 106 ? 0.33100 0.67344 0.38414 0.14241  0.00261  0.01983  106 THR A O   
843  C CB  . THR A 106 ? 0.40353 0.58906 0.36015 0.16395  -0.02526 0.04443  106 THR A CB  
844  O OG1 . THR A 106 ? 0.49809 0.58892 0.39650 0.17626  -0.00988 0.02169  106 THR A OG1 
845  C CG2 . THR A 106 ? 0.36936 0.59874 0.33983 0.17719  -0.00811 0.00765  106 THR A CG2 
846  N N   . VAL A 107 ? 0.34817 0.67131 0.36088 0.17116  -0.00451 0.04733  107 VAL A N   
847  C CA  . VAL A 107 ? 0.34572 0.68180 0.38547 0.16569  -0.01529 0.05369  107 VAL A CA  
848  C C   . VAL A 107 ? 0.37645 0.67880 0.39168 0.16602  0.02019  0.07111  107 VAL A C   
849  O O   . VAL A 107 ? 0.39679 0.70024 0.39310 0.20001  0.01131  0.07476  107 VAL A O   
850  C CB  . VAL A 107 ? 0.36730 0.70820 0.39818 0.10368  -0.02949 0.06206  107 VAL A CB  
851  C CG1 . VAL A 107 ? 0.32077 0.73018 0.40058 0.03681  -0.02805 0.04555  107 VAL A CG1 
852  C CG2 . VAL A 107 ? 0.43022 0.71817 0.41982 0.10334  -0.04977 0.08919  107 VAL A CG2 
853  N N   . LYS A 108 ? 0.34062 0.64491 0.38909 0.11344  -0.02844 0.07420  108 LYS A N   
854  C CA  . LYS A 108 ? 0.32663 0.61449 0.40447 0.12398  0.00254  0.09649  108 LYS A CA  
855  C C   . LYS A 108 ? 0.36208 0.63363 0.48509 0.11180  -0.03686 0.09872  108 LYS A C   
856  O O   . LYS A 108 ? 0.34420 0.62409 0.50155 0.09923  -0.07395 0.11218  108 LYS A O   
857  C CB  . LYS A 108 ? 0.40181 0.61772 0.40861 0.15292  -0.01445 0.12302  108 LYS A CB  
858  N N   . TYR A 109 ? 0.41150 0.66420 0.55588 0.11568  -0.05716 0.08525  109 TYR A N   
859  C CA  . TYR A 109 ? 0.59566 0.73408 0.64186 0.06701  -0.04762 0.05587  109 TYR A CA  
860  C C   . TYR A 109 ? 0.64898 0.81422 0.72185 0.06226  -0.08845 -0.00975 109 TYR A C   
861  O O   . TYR A 109 ? 0.68497 0.85927 0.75876 0.06288  -0.06013 -0.04311 109 TYR A O   
862  C CB  . TYR A 109 ? 0.60904 0.73666 0.66088 0.01293  0.00026  0.04267  109 TYR A CB  
863  C CG  . TYR A 109 ? 0.56477 0.73217 0.63443 0.03422  -0.02932 0.06947  109 TYR A CG  
864  C CD1 . TYR A 109 ? 0.51576 0.73040 0.62327 0.03738  -0.03732 0.09188  109 TYR A CD1 
865  C CD2 . TYR A 109 ? 0.62180 0.74830 0.65249 0.05881  -0.03613 0.05200  109 TYR A CD2 
866  C CE1 . TYR A 109 ? 0.58500 0.76192 0.64118 0.02787  -0.08610 0.06113  109 TYR A CE1 
867  C CE2 . TYR A 109 ? 0.66948 0.76791 0.66414 0.04677  -0.07605 0.03010  109 TYR A CE2 
868  C CZ  . TYR A 109 ? 0.69883 0.78403 0.65686 0.03726  -0.10674 0.04783  109 TYR A CZ  
869  O OH  . TYR A 109 ? 0.77491 0.80173 0.64125 0.03970  -0.17055 0.08875  109 TYR A OH  
870  N N   . GLY A 110 ? 0.69541 0.83746 0.72460 0.03943  -0.09572 -0.00815 110 GLY A N   
871  C CA  . GLY A 110 ? 0.65671 0.84283 0.72711 0.02213  -0.13066 -0.01141 110 GLY A CA  
872  C C   . GLY A 110 ? 0.65156 0.84531 0.74435 0.00166  -0.14784 -0.02291 110 GLY A C   
873  O O   . GLY A 110 ? 0.57863 0.85962 0.77108 -0.00387 -0.16963 -0.03879 110 GLY A O   
874  N N   . LYS A 114 ? 0.76033 0.77520 0.67722 0.20603  -0.12944 0.08380  114 LYS A N   
875  C CA  . LYS A 114 ? 0.68459 0.78238 0.67274 0.22095  -0.12467 0.10758  114 LYS A CA  
876  C C   . LYS A 114 ? 0.62698 0.80470 0.66278 0.22856  -0.08756 0.08528  114 LYS A C   
877  O O   . LYS A 114 ? 0.63023 0.80304 0.69622 0.20257  -0.04091 0.11598  114 LYS A O   
878  C CB  . LYS A 114 ? 0.70793 0.78333 0.68906 0.19512  -0.10874 0.13205  114 LYS A CB  
879  C CG  . LYS A 114 ? 0.75776 0.80147 0.70324 0.12102  -0.08127 0.10382  114 LYS A CG  
880  C CD  . LYS A 114 ? 0.79099 0.82347 0.70906 0.06824  -0.06414 0.09969  114 LYS A CD  
881  C CE  . LYS A 114 ? 0.78578 0.85505 0.70942 0.04422  -0.06454 0.10855  114 LYS A CE  
882  N NZ  . LYS A 114 ? 0.77507 0.88750 0.71146 0.04907  -0.04744 0.10690  114 LYS A NZ  
883  N N   . GLU A 115 ? 0.56006 0.80612 0.60706 0.26335  -0.13600 0.03640  115 GLU A N   
884  C CA  . GLU A 115 ? 0.53741 0.79788 0.57555 0.31068  -0.14512 -0.01203 115 GLU A CA  
885  C C   . GLU A 115 ? 0.51338 0.85153 0.53971 0.33712  -0.12110 -0.06128 115 GLU A C   
886  O O   . GLU A 115 ? 0.52871 0.90098 0.57054 0.33602  -0.13520 -0.09503 115 GLU A O   
887  C CB  . GLU A 115 ? 0.60310 0.77158 0.60269 0.28616  -0.11792 0.01435  115 GLU A CB  
888  C CG  . GLU A 115 ? 0.68540 0.77506 0.68803 0.25084  -0.11326 0.03898  115 GLU A CG  
889  C CD  . GLU A 115 ? 0.77684 0.78167 0.74713 0.21547  -0.10233 0.06039  115 GLU A CD  
890  O OE1 . GLU A 115 ? 0.83373 0.80511 0.77937 0.18744  -0.13693 0.04751  115 GLU A OE1 
891  O OE2 . GLU A 115 ? 0.77407 0.77263 0.76657 0.21344  -0.06761 0.09768  115 GLU A OE2 
892  N N   . ALA A 116 ? 0.46307 0.86495 0.48710 0.31764  -0.11284 -0.06210 116 ALA A N   
893  C CA  . ALA A 116 ? 0.43409 0.90321 0.43719 0.25832  -0.08388 -0.03933 116 ALA A CA  
894  C C   . ALA A 116 ? 0.38976 0.91601 0.40780 0.25560  -0.05198 -0.03578 116 ALA A C   
895  O O   . ALA A 116 ? 0.34555 0.96493 0.39074 0.19535  0.01101  -0.00450 116 ALA A O   
896  C CB  . ALA A 116 ? 0.43970 0.91078 0.47430 0.23387  -0.07905 -0.04438 116 ALA A CB  
897  N N   . THR A 117 ? 0.43266 0.90503 0.38908 0.26180  -0.04089 -0.06113 117 THR A N   
898  C CA  . THR A 117 ? 0.43483 0.86314 0.34768 0.25254  -0.01722 -0.07258 117 THR A CA  
899  C C   . THR A 117 ? 0.37157 0.85037 0.36381 0.26492  0.02173  -0.04273 117 THR A C   
900  O O   . THR A 117 ? 0.37119 0.87858 0.38214 0.20693  0.05559  -0.08743 117 THR A O   
901  C CB  . THR A 117 ? 0.60901 0.86361 0.36131 0.20666  -0.00372 -0.06981 117 THR A CB  
902  O OG1 . THR A 117 ? 0.69431 0.90739 0.43421 0.18913  0.00846  -0.02910 117 THR A OG1 
903  C CG2 . THR A 117 ? 0.63010 0.86023 0.32407 0.19232  -0.04767 -0.04936 117 THR A CG2 
904  N N   . TYR A 118 ? 0.33181 0.82617 0.35162 0.23048  -0.03173 0.02281  118 TYR A N   
905  C CA  . TYR A 118 ? 0.30438 0.80458 0.36578 0.19999  -0.00290 0.02963  118 TYR A CA  
906  C C   . TYR A 118 ? 0.36142 0.76780 0.34628 0.17777  0.00242  0.00945  118 TYR A C   
907  O O   . TYR A 118 ? 0.40108 0.78170 0.32956 0.17558  0.01524  -0.00412 118 TYR A O   
908  C CB  . TYR A 118 ? 0.28805 0.82237 0.40886 0.12526  0.02074  0.02025  118 TYR A CB  
909  C CG  . TYR A 118 ? 0.24981 0.86974 0.43563 0.08304  -0.01782 0.02065  118 TYR A CG  
910  C CD1 . TYR A 118 ? 0.28147 0.91456 0.47556 -0.00616 -0.01170 -0.02220 118 TYR A CD1 
911  C CD2 . TYR A 118 ? 0.28198 0.89331 0.45413 0.04211  -0.00617 -0.02184 118 TYR A CD2 
912  C CE1 . TYR A 118 ? 0.31867 0.92894 0.48644 0.02567  -0.03170 -0.00633 118 TYR A CE1 
913  C CE2 . TYR A 118 ? 0.33468 0.91534 0.48434 0.03704  -0.01840 -0.02435 118 TYR A CE2 
914  C CZ  . TYR A 118 ? 0.33612 0.93919 0.47701 0.02050  -0.01472 -0.00111 118 TYR A CZ  
915  O OH  . TYR A 118 ? 0.40746 0.98046 0.52438 0.00948  0.02550  0.01632  118 TYR A OH  
916  N N   . LEU A 119 ? 0.38707 0.69858 0.33479 0.17097  0.05128  -0.00794 119 LEU A N   
917  C CA  . LEU A 119 ? 0.39335 0.61134 0.34070 0.13989  0.05176  -0.05631 119 LEU A CA  
918  C C   . LEU A 119 ? 0.32085 0.54291 0.30506 0.11393  0.00634  -0.03192 119 LEU A C   
919  O O   . LEU A 119 ? 0.33753 0.55123 0.30629 0.11420  0.00622  -0.04350 119 LEU A O   
920  C CB  . LEU A 119 ? 0.50131 0.58353 0.40337 0.09106  0.06683  -0.11740 119 LEU A CB  
921  C CG  . LEU A 119 ? 0.55366 0.60116 0.44385 0.08575  0.06787  -0.15598 119 LEU A CG  
922  C CD1 . LEU A 119 ? 0.57608 0.61125 0.45773 0.09127  0.04076  -0.11352 119 LEU A CD1 
923  C CD2 . LEU A 119 ? 0.55408 0.59161 0.45912 0.09948  0.07457  -0.19877 119 LEU A CD2 
924  N N   . ALA A 120 ? 0.31627 0.48963 0.29470 0.08034  -0.00689 -0.01525 120 ALA A N   
925  C CA  . ALA A 120 ? 0.29481 0.45441 0.26892 0.08065  -0.01795 -0.01185 120 ALA A CA  
926  C C   . ALA A 120 ? 0.30340 0.44938 0.24527 0.04540  0.01890  -0.03931 120 ALA A C   
927  O O   . ALA A 120 ? 0.32815 0.40763 0.29123 0.06991  0.03129  -0.01823 120 ALA A O   
928  C CB  . ALA A 120 ? 0.34087 0.45556 0.26524 0.10254  0.01472  -0.06431 120 ALA A CB  
929  N N   . LEU A 121 ? 0.27746 0.45893 0.22677 0.05863  0.02053  -0.04307 121 LEU A N   
930  C CA  . LEU A 121 ? 0.28863 0.44896 0.23423 0.03963  0.03315  -0.03027 121 LEU A CA  
931  C C   . LEU A 121 ? 0.29269 0.42641 0.25472 0.02843  -0.00749 -0.03294 121 LEU A C   
932  O O   . LEU A 121 ? 0.31011 0.44530 0.27359 0.07723  -0.02404 -0.01845 121 LEU A O   
933  C CB  . LEU A 121 ? 0.32300 0.46231 0.21978 0.02338  0.02527  -0.03493 121 LEU A CB  
934  C CG  . LEU A 121 ? 0.30879 0.47444 0.23795 -0.00424 0.03112  -0.01131 121 LEU A CG  
935  C CD1 . LEU A 121 ? 0.28026 0.42054 0.30542 -0.01142 -0.00132 -0.01854 121 LEU A CD1 
936  C CD2 . LEU A 121 ? 0.32413 0.47182 0.22475 0.04245  0.03115  -0.05997 121 LEU A CD2 
937  N N   . ASN A 122 ? 0.30215 0.39337 0.21432 0.00780  0.00157  -0.05488 122 ASN A N   
938  C CA  . ASN A 122 ? 0.32972 0.32741 0.22976 -0.00514 -0.01545 -0.02911 122 ASN A CA  
939  C C   . ASN A 122 ? 0.30570 0.32199 0.24112 0.01229  -0.02409 -0.01503 122 ASN A C   
940  O O   . ASN A 122 ? 0.32694 0.29120 0.26525 0.04106  -0.03068 -0.01490 122 ASN A O   
941  C CB  . ASN A 122 ? 0.33719 0.32268 0.22548 -0.02984 -0.00526 -0.00685 122 ASN A CB  
942  C CG  . ASN A 122 ? 0.29874 0.37368 0.24983 -0.02013 0.03697  -0.01868 122 ASN A CG  
943  O OD1 . ASN A 122 ? 0.32988 0.43915 0.24169 0.05373  0.00487  -0.00042 122 ASN A OD1 
944  N ND2 . ASN A 122 ? 0.28024 0.37746 0.24469 -0.02507 0.02024  0.01640  122 ASN A ND2 
945  N N   . GLU A 123 ? 0.31191 0.33513 0.20669 0.06358  -0.00815 -0.02526 123 GLU A N   
946  C CA  . GLU A 123 ? 0.27857 0.38240 0.22195 0.05512  -0.00448 -0.01696 123 GLU A CA  
947  C C   . GLU A 123 ? 0.28397 0.39765 0.21433 0.03390  0.01636  -0.03625 123 GLU A C   
948  O O   . GLU A 123 ? 0.33053 0.45731 0.23185 0.02028  0.03820  -0.02431 123 GLU A O   
949  C CB  . GLU A 123 ? 0.28503 0.37451 0.26304 -0.01125 -0.00383 -0.02917 123 GLU A CB  
950  C CG  . GLU A 123 ? 0.26162 0.40757 0.25071 -0.00840 -0.01552 0.01060  123 GLU A CG  
951  C CD  . GLU A 123 ? 0.23689 0.42415 0.25085 0.01514  0.01942  0.00026  123 GLU A CD  
952  O OE1 . GLU A 123 ? 0.28705 0.36240 0.28097 0.01132  -0.00103 -0.03799 123 GLU A OE1 
953  O OE2 . GLU A 123 ? 0.27399 0.47238 0.28685 -0.00339 0.04001  -0.00820 123 GLU A OE2 
954  N N   . SER A 124 ? 0.23043 0.42755 0.20052 0.02744  -0.03187 -0.01807 124 SER A N   
955  C CA  . SER A 124 ? 0.25035 0.46500 0.24574 0.05370  -0.02290 -0.03310 124 SER A CA  
956  C C   . SER A 124 ? 0.26587 0.45445 0.25081 0.03083  -0.01703 -0.02532 124 SER A C   
957  O O   . SER A 124 ? 0.26022 0.45337 0.28250 0.04818  0.02489  -0.02238 124 SER A O   
958  C CB  . SER A 124 ? 0.26393 0.53711 0.25320 0.04678  -0.06570 -0.02875 124 SER A CB  
959  O OG  . SER A 124 ? 0.26329 0.59111 0.27641 0.04749  -0.04437 -0.04852 124 SER A OG  
960  N N   . THR A 125 ? 0.23982 0.41722 0.24466 0.00072  -0.02610 -0.05913 125 THR A N   
961  C CA  . THR A 125 ? 0.24853 0.47197 0.25684 -0.00815 -0.01412 -0.05800 125 THR A CA  
962  C C   . THR A 125 ? 0.25903 0.49430 0.27849 0.02290  0.01719  -0.06637 125 THR A C   
963  O O   . THR A 125 ? 0.22901 0.52082 0.27347 0.01165  0.00165  -0.04204 125 THR A O   
964  C CB  . THR A 125 ? 0.24544 0.50359 0.25036 -0.05314 0.00922  0.00756  125 THR A CB  
965  O OG1 . THR A 125 ? 0.29216 0.58079 0.31816 -0.04281 0.04063  0.02071  125 THR A OG1 
966  C CG2 . THR A 125 ? 0.27104 0.51384 0.23821 -0.06046 -0.03237 -0.00948 125 THR A CG2 
967  N N   . VAL A 126 ? 0.30467 0.47947 0.28393 0.00526  -0.00840 -0.06134 126 VAL A N   
968  C CA  . VAL A 126 ? 0.26872 0.43769 0.30387 -0.00503 -0.08212 -0.04711 126 VAL A CA  
969  C C   . VAL A 126 ? 0.25847 0.40117 0.32381 0.08097  -0.04762 -0.03712 126 VAL A C   
970  O O   . VAL A 126 ? 0.26092 0.44010 0.34617 0.07456  -0.03723 -0.06075 126 VAL A O   
971  C CB  . VAL A 126 ? 0.35058 0.42602 0.31276 0.01215  -0.09499 -0.04183 126 VAL A CB  
972  C CG1 . VAL A 126 ? 0.31909 0.44753 0.32130 0.01292  -0.10846 -0.03230 126 VAL A CG1 
973  C CG2 . VAL A 126 ? 0.38621 0.49877 0.36177 -0.03381 -0.08713 -0.00731 126 VAL A CG2 
974  N N   . LYS A 127 ? 0.30793 0.43718 0.36598 0.00683  0.00498  -0.00122 127 LYS A N   
975  C CA  . LYS A 127 ? 0.41404 0.52012 0.46196 0.05125  0.01777  0.01859  127 LYS A CA  
976  C C   . LYS A 127 ? 0.45240 0.52792 0.59344 -0.07832 0.02810  -0.07751 127 LYS A C   
977  O O   . LYS A 127 ? 0.36566 0.50197 0.63558 -0.08830 0.01634  -0.13374 127 LYS A O   
978  C CB  . LYS A 127 ? 0.48340 0.58841 0.44565 0.10478  -0.00293 0.07336  127 LYS A CB  
979  C CG  . LYS A 127 ? 0.45718 0.63197 0.43018 0.10124  0.04951  0.09398  127 LYS A CG  
980  C CD  . LYS A 127 ? 0.48385 0.68848 0.44637 0.03827  0.07099  0.10999  127 LYS A CD  
981  C CE  . LYS A 127 ? 0.49204 0.71411 0.39312 0.02051  0.02913  0.09616  127 LYS A CE  
982  N NZ  . LYS A 127 ? 0.48845 0.72443 0.40773 0.01828  0.05330  0.11227  127 LYS A NZ  
983  N N   . SER A 128 ? 0.46345 0.59621 0.63462 -0.13728 0.06769  -0.07512 128 SER A N   
984  C CA  . SER A 128 ? 0.61358 0.64064 0.68372 -0.13111 0.06654  -0.12356 128 SER A CA  
985  C C   . SER A 128 ? 0.60740 0.69831 0.71106 -0.18208 0.06177  -0.11094 128 SER A C   
986  O O   . SER A 128 ? 0.65569 0.71151 0.71412 -0.16432 0.03824  -0.10669 128 SER A O   
987  C CB  . SER A 128 ? 0.68379 0.63293 0.70606 -0.09575 0.06878  -0.15144 128 SER A CB  
988  O OG  . SER A 128 ? 0.73268 0.60095 0.71728 -0.08159 0.06336  -0.18626 128 SER A OG  
989  N N   . SER A 129 ? 0.68074 0.76166 0.74192 -0.13985 0.03718  -0.11314 129 SER A N   
990  C CA  . SER A 129 ? 0.72968 0.79781 0.77093 -0.08208 0.01638  -0.06551 129 SER A CA  
991  C C   . SER A 129 ? 0.79119 0.81678 0.77670 -0.05871 0.01658  -0.05197 129 SER A C   
992  O O   . SER A 129 ? 0.84137 0.83912 0.80345 -0.07338 -0.01325 -0.01804 129 SER A O   
993  C CB  . SER A 129 ? 0.72595 0.80486 0.78801 -0.05839 -0.00469 -0.05559 129 SER A CB  
994  O OG  . SER A 129 ? 0.72310 0.80225 0.80389 -0.02278 -0.02808 -0.03990 129 SER A OG  
995  N N   . GLY A 130 ? 0.77455 0.81017 0.76104 -0.02564 0.06259  -0.05798 130 GLY A N   
996  C CA  . GLY A 130 ? 0.75150 0.78900 0.71706 -0.00242 0.09646  -0.06878 130 GLY A CA  
997  C C   . GLY A 130 ? 0.77706 0.77039 0.66146 0.02550  0.08498  -0.07202 130 GLY A C   
998  O O   . GLY A 130 ? 0.83057 0.77876 0.65335 0.06015  0.04466  -0.08705 130 GLY A O   
999  N N   . GLY A 131 ? 0.71306 0.73270 0.59897 0.00290  0.12133  -0.07822 131 GLY A N   
1000 C CA  . GLY A 131 ? 0.69520 0.67882 0.54658 -0.02685 0.09053  -0.07678 131 GLY A CA  
1001 C C   . GLY A 131 ? 0.62556 0.63793 0.48121 -0.06614 0.04812  -0.07748 131 GLY A C   
1002 O O   . GLY A 131 ? 0.63070 0.58601 0.48144 -0.05580 0.03196  -0.09693 131 GLY A O   
1003 N N   . PRO A 132 ? 0.62315 0.63481 0.43109 -0.04206 -0.02181 -0.07816 132 PRO A N   
1004 C CA  . PRO A 132 ? 0.57818 0.62056 0.38056 -0.01619 -0.05556 -0.04159 132 PRO A CA  
1005 C C   . PRO A 132 ? 0.65983 0.67003 0.35896 -0.00609 -0.03290 -0.06894 132 PRO A C   
1006 O O   . PRO A 132 ? 0.74647 0.76869 0.37193 0.03473  -0.02886 -0.03432 132 PRO A O   
1007 C CB  . PRO A 132 ? 0.55230 0.62646 0.40824 -0.05125 -0.06663 -0.03068 132 PRO A CB  
1008 C CG  . PRO A 132 ? 0.60033 0.61202 0.40208 -0.07806 -0.07197 -0.07599 132 PRO A CG  
1009 C CD  . PRO A 132 ? 0.62758 0.63193 0.41947 -0.06308 -0.04862 -0.07256 132 PRO A CD  
1010 N N   . PHE A 133 ? 0.58285 0.58688 0.31517 -0.03219 -0.00921 -0.04126 133 PHE A N   
1011 C CA  . PHE A 133 ? 0.46420 0.58243 0.28515 -0.02568 -0.08856 -0.05286 133 PHE A CA  
1012 C C   . PHE A 133 ? 0.33860 0.48554 0.29888 -0.02320 -0.03649 -0.01486 133 PHE A C   
1013 O O   . PHE A 133 ? 0.31305 0.45065 0.32367 -0.02594 -0.04386 0.02117  133 PHE A O   
1014 C CB  . PHE A 133 ? 0.55323 0.65963 0.31611 0.01195  -0.07312 -0.01947 133 PHE A CB  
1015 C CG  . PHE A 133 ? 0.68559 0.68692 0.35933 0.09669  -0.03476 -0.04926 133 PHE A CG  
1016 C CD1 . PHE A 133 ? 0.72174 0.69952 0.31922 0.18158  -0.14863 -0.04234 133 PHE A CD1 
1017 C CD2 . PHE A 133 ? 0.72867 0.66894 0.37491 0.17549  -0.00363 -0.07063 133 PHE A CD2 
1018 C CE1 . PHE A 133 ? 0.79745 0.66885 0.32170 0.22567  -0.11159 -0.14069 133 PHE A CE1 
1019 C CE2 . PHE A 133 ? 0.75465 0.68191 0.32513 0.20900  -0.10179 -0.09584 133 PHE A CE2 
1020 C CZ  . PHE A 133 ? 0.81818 0.70678 0.33839 0.20519  -0.12640 -0.10048 133 PHE A CZ  
1021 N N   . VAL A 134 ? 0.35800 0.47427 0.32023 0.01214  -0.04159 0.00457  134 VAL A N   
1022 C CA  . VAL A 134 ? 0.37119 0.45944 0.32664 -0.02028 -0.02365 0.01329  134 VAL A CA  
1023 C C   . VAL A 134 ? 0.33676 0.45610 0.33519 -0.03268 -0.03362 0.02412  134 VAL A C   
1024 O O   . VAL A 134 ? 0.38696 0.50826 0.37489 -0.01363 -0.04909 0.04312  134 VAL A O   
1025 C CB  . VAL A 134 ? 0.44520 0.42491 0.32455 -0.02581 -0.03544 -0.02874 134 VAL A CB  
1026 C CG1 . VAL A 134 ? 0.40378 0.46886 0.30301 -0.02292 -0.02509 -0.01540 134 VAL A CG1 
1027 C CG2 . VAL A 134 ? 0.49389 0.44662 0.35742 -0.00485 -0.05428 -0.07191 134 VAL A CG2 
1028 N N   . VAL A 135 ? 0.34134 0.44792 0.30813 -0.05486 -0.03167 0.01649  135 VAL A N   
1029 C CA  . VAL A 135 ? 0.35783 0.47457 0.36212 -0.04627 -0.02917 0.03804  135 VAL A CA  
1030 C C   . VAL A 135 ? 0.36591 0.43050 0.36170 -0.00273 -0.02450 0.03611  135 VAL A C   
1031 O O   . VAL A 135 ? 0.37445 0.41078 0.39815 0.04583  -0.04059 0.05463  135 VAL A O   
1032 C CB  . VAL A 135 ? 0.50642 0.52130 0.40691 -0.01659 -0.04560 0.03864  135 VAL A CB  
1033 C CG1 . VAL A 135 ? 0.42227 0.56948 0.35578 -0.07637 -0.14814 0.03398  135 VAL A CG1 
1034 C CG2 . VAL A 135 ? 0.63631 0.53067 0.47032 0.01173  -0.02767 0.04247  135 VAL A CG2 
1035 N N   . ASP A 136 ? 0.36229 0.41365 0.33929 0.02004  -0.03876 -0.00572 136 ASP A N   
1036 C CA  . ASP A 136 ? 0.36674 0.41552 0.32777 0.07834  -0.06354 0.01697  136 ASP A CA  
1037 C C   . ASP A 136 ? 0.30545 0.42316 0.31908 0.03846  -0.07444 -0.02302 136 ASP A C   
1038 O O   . ASP A 136 ? 0.27947 0.45903 0.38306 0.03309  -0.06291 -0.02216 136 ASP A O   
1039 C CB  . ASP A 136 ? 0.45315 0.48209 0.34329 0.10606  -0.11190 0.01710  136 ASP A CB  
1040 C CG  . ASP A 136 ? 0.55167 0.54264 0.38336 0.15237  -0.12855 0.00043  136 ASP A CG  
1041 O OD1 . ASP A 136 ? 0.57178 0.57273 0.40741 0.12910  -0.12577 -0.05136 136 ASP A OD1 
1042 O OD2 . ASP A 136 ? 0.56489 0.59202 0.42918 0.18540  -0.14458 -0.01562 136 ASP A OD2 
1043 N N   . VAL A 137 ? 0.31213 0.38307 0.28166 -0.02977 -0.05836 0.00185  137 VAL A N   
1044 C CA  . VAL A 137 ? 0.30095 0.37313 0.27677 0.01463  -0.04038 0.04127  137 VAL A CA  
1045 C C   . VAL A 137 ? 0.32418 0.37282 0.28805 0.02134  -0.00320 0.05121  137 VAL A C   
1046 O O   . VAL A 137 ? 0.30938 0.42964 0.28931 0.01277  0.01436  0.04253  137 VAL A O   
1047 C CB  . VAL A 137 ? 0.27444 0.35496 0.28529 0.04335  -0.01484 0.03268  137 VAL A CB  
1048 C CG1 . VAL A 137 ? 0.30381 0.37572 0.29357 0.01522  0.00288  -0.00446 137 VAL A CG1 
1049 C CG2 . VAL A 137 ? 0.34915 0.38401 0.31212 0.01532  0.01713  0.05282  137 VAL A CG2 
1050 N N   . VAL A 138 ? 0.33271 0.33794 0.28901 0.01348  -0.01833 0.02156  138 VAL A N   
1051 C CA  . VAL A 138 ? 0.31430 0.39465 0.28149 0.02010  -0.04678 0.01873  138 VAL A CA  
1052 C C   . VAL A 138 ? 0.30466 0.41003 0.30372 0.01066  -0.01159 -0.00128 138 VAL A C   
1053 O O   . VAL A 138 ? 0.35186 0.46015 0.35403 -0.02566 0.04356  -0.08532 138 VAL A O   
1054 C CB  . VAL A 138 ? 0.36220 0.43412 0.31799 -0.02013 -0.04093 0.01598  138 VAL A CB  
1055 C CG1 . VAL A 138 ? 0.36125 0.41433 0.37188 -0.02868 -0.07976 0.06711  138 VAL A CG1 
1056 C CG2 . VAL A 138 ? 0.34288 0.48526 0.30147 0.00659  -0.08659 -0.00708 138 VAL A CG2 
1057 N N   . ILE A 139 ? 0.26289 0.39794 0.26685 0.01593  -0.02181 0.04942  139 ILE A N   
1058 C CA  . ILE A 139 ? 0.28705 0.36681 0.27263 -0.01204 -0.00810 0.05455  139 ILE A CA  
1059 C C   . ILE A 139 ? 0.34376 0.34219 0.30379 0.00931  -0.01168 0.06824  139 ILE A C   
1060 O O   . ILE A 139 ? 0.33629 0.34513 0.30854 -0.01230 0.02240  0.06116  139 ILE A O   
1061 C CB  . ILE A 139 ? 0.31251 0.34280 0.28937 0.02134  -0.01319 0.00997  139 ILE A CB  
1062 C CG1 . ILE A 139 ? 0.31377 0.32101 0.29394 0.09561  -0.02569 -0.01556 139 ILE A CG1 
1063 C CG2 . ILE A 139 ? 0.36118 0.38024 0.28611 -0.04748 0.00394  0.03376  139 ILE A CG2 
1064 C CD1 . ILE A 139 ? 0.31370 0.38091 0.33167 0.08429  -0.01996 -0.02538 139 ILE A CD1 
1065 N N   . ASN A 140 ? 0.35684 0.36425 0.27565 -0.01011 -0.00483 0.02258  140 ASN A N   
1066 C CA  . ASN A 140 ? 0.38707 0.34942 0.29316 -0.02781 -0.01703 -0.00008 140 ASN A CA  
1067 C C   . ASN A 140 ? 0.46768 0.35436 0.28803 0.00320  -0.03214 0.01511  140 ASN A C   
1068 O O   . ASN A 140 ? 0.47628 0.37877 0.28159 0.00408  0.00370  0.04710  140 ASN A O   
1069 C CB  . ASN A 140 ? 0.40813 0.40462 0.29566 -0.01837 -0.00699 0.00822  140 ASN A CB  
1070 C CG  . ASN A 140 ? 0.41881 0.41619 0.30925 -0.04944 0.01029  0.04380  140 ASN A CG  
1071 O OD1 . ASN A 140 ? 0.38664 0.43120 0.31966 -0.05249 0.00816  0.01695  140 ASN A OD1 
1072 N ND2 . ASN A 140 ? 0.41180 0.45682 0.29925 -0.03574 -0.02405 0.06859  140 ASN A ND2 
1073 N N   . ASP A 141 ? 0.53420 0.35526 0.30139 0.02971  -0.09807 0.00693  141 ASP A N   
1074 C CA  . ASP A 141 ? 0.60463 0.41640 0.29401 0.03418  -0.07148 0.01207  141 ASP A CA  
1075 C C   . ASP A 141 ? 0.63439 0.47815 0.27493 0.01581  -0.01026 0.01450  141 ASP A C   
1076 O O   . ASP A 141 ? 0.73030 0.50535 0.26902 -0.00228 -0.02144 -0.02597 141 ASP A O   
1077 C CB  . ASP A 141 ? 0.65652 0.48685 0.36038 0.04671  -0.02666 0.05503  141 ASP A CB  
1078 C CG  . ASP A 141 ? 0.76698 0.56234 0.45653 0.08371  -0.01127 0.08612  141 ASP A CG  
1079 O OD1 . ASP A 141 ? 0.76165 0.62575 0.47309 0.12695  -0.00757 0.12011  141 ASP A OD1 
1080 O OD2 . ASP A 141 ? 0.83392 0.59479 0.51623 0.08990  -0.00887 0.04729  141 ASP A OD2 
1081 N N   . ILE A 142 ? 0.57440 0.44779 0.26796 0.00862  0.02022  0.03032  142 ILE A N   
1082 C CA  . ILE A 142 ? 0.55397 0.45567 0.33429 0.01909  0.03832  0.06026  142 ILE A CA  
1083 C C   . ILE A 142 ? 0.42571 0.38250 0.25833 0.05039  -0.02142 0.05747  142 ILE A C   
1084 O O   . ILE A 142 ? 0.37757 0.41530 0.24724 0.02926  -0.02088 0.05489  142 ILE A O   
1085 C CB  . ILE A 142 ? 0.61570 0.52548 0.45467 -0.04401 0.02096  0.07756  142 ILE A CB  
1086 C CG1 . ILE A 142 ? 0.63397 0.52912 0.49268 -0.05838 0.00179  0.08148  142 ILE A CG1 
1087 C CG2 . ILE A 142 ? 0.63893 0.52680 0.44553 -0.05264 0.02905  0.10206  142 ILE A CG2 
1088 C CD1 . ILE A 142 ? 0.68087 0.54063 0.57796 -0.07027 0.00799  0.00672  142 ILE A CD1 
1089 N N   . HIS A 143 ? 0.46134 0.37802 0.26069 0.00928  -0.03241 0.00312  143 HIS A N   
1090 C CA  A HIS A 143 ? 0.44014 0.37319 0.26699 0.01206  -0.04917 -0.02162 143 HIS A CA  
1091 C CA  B HIS A 143 ? 0.44481 0.36873 0.26657 0.02244  -0.07557 -0.02033 143 HIS A CA  
1092 C C   . HIS A 143 ? 0.42833 0.38867 0.25401 0.03695  -0.03649 0.00214  143 HIS A C   
1093 O O   . HIS A 143 ? 0.42761 0.45371 0.28465 0.11277  -0.03487 0.07523  143 HIS A O   
1094 C CB  A HIS A 143 ? 0.44516 0.40648 0.30173 0.00059  -0.03195 -0.01571 143 HIS A CB  
1095 C CB  B HIS A 143 ? 0.46291 0.39304 0.30565 0.02571  -0.11238 -0.01615 143 HIS A CB  
1096 C CG  A HIS A 143 ? 0.48685 0.42184 0.34493 0.00931  -0.02802 0.02385  143 HIS A CG  
1097 C CG  B HIS A 143 ? 0.51488 0.40940 0.36738 0.04374  -0.13284 0.00126  143 HIS A CG  
1098 N ND1 A HIS A 143 ? 0.53766 0.44295 0.35247 0.00950  -0.03487 0.05308  143 HIS A ND1 
1099 N ND1 B HIS A 143 ? 0.52608 0.41531 0.41439 0.03637  -0.14820 0.00202  143 HIS A ND1 
1100 C CD2 A HIS A 143 ? 0.47545 0.42391 0.37301 -0.01120 -0.05575 0.04773  143 HIS A CD2 
1101 C CD2 B HIS A 143 ? 0.53813 0.41457 0.37795 0.06082  -0.15106 0.03904  143 HIS A CD2 
1102 C CE1 A HIS A 143 ? 0.50503 0.41802 0.34045 0.03132  -0.07786 0.09773  143 HIS A CE1 
1103 C CE1 B HIS A 143 ? 0.49548 0.39449 0.38883 0.08117  -0.18731 0.07182  143 HIS A CE1 
1104 N NE2 A HIS A 143 ? 0.47736 0.42490 0.33620 -0.00547 -0.09779 0.09368  143 HIS A NE2 
1105 N NE2 B HIS A 143 ? 0.47911 0.39750 0.37789 0.09344  -0.19505 0.07648  143 HIS A NE2 
1106 N N   . PHE A 144 ? 0.34746 0.37661 0.20681 -0.02751 -0.05575 0.00836  144 PHE A N   
1107 C CA  . PHE A 144 ? 0.33491 0.40003 0.21728 0.03340  -0.05402 0.03488  144 PHE A CA  
1108 C C   . PHE A 144 ? 0.36463 0.40367 0.23754 0.00551  -0.02723 0.01527  144 PHE A C   
1109 O O   . PHE A 144 ? 0.36218 0.46665 0.22871 -0.01966 0.01317  0.03019  144 PHE A O   
1110 C CB  . PHE A 144 ? 0.30091 0.40536 0.21069 0.01253  -0.00240 0.03229  144 PHE A CB  
1111 C CG  . PHE A 144 ? 0.29554 0.40844 0.22954 0.04117  -0.00419 0.01681  144 PHE A CG  
1112 C CD1 . PHE A 144 ? 0.32101 0.40285 0.23643 0.02690  0.01021  -0.00286 144 PHE A CD1 
1113 C CD2 . PHE A 144 ? 0.29610 0.41192 0.22960 0.03297  0.00182  0.03103  144 PHE A CD2 
1114 C CE1 . PHE A 144 ? 0.32631 0.41938 0.20911 0.01397  -0.01601 -0.01459 144 PHE A CE1 
1115 C CE2 . PHE A 144 ? 0.23211 0.42302 0.22647 0.03589  -0.01054 0.02454  144 PHE A CE2 
1116 C CZ  . PHE A 144 ? 0.27622 0.43761 0.21902 -0.00535 0.02954  0.00299  144 PHE A CZ  
1117 N N   . GLU A 145 ? 0.36060 0.35346 0.24296 0.00202  -0.03299 0.00847  145 GLU A N   
1118 C CA  . GLU A 145 ? 0.34845 0.39099 0.22290 0.01911  -0.03344 0.02278  145 GLU A CA  
1119 C C   . GLU A 145 ? 0.34851 0.37645 0.22619 -0.00061 -0.01727 0.00403  145 GLU A C   
1120 O O   . GLU A 145 ? 0.34717 0.38558 0.30592 0.03631  -0.03315 0.00242  145 GLU A O   
1121 C CB  . GLU A 145 ? 0.37595 0.45339 0.19545 0.00078  -0.04733 0.03418  145 GLU A CB  
1122 C CG  . GLU A 145 ? 0.34386 0.45583 0.15924 0.00819  0.00099  -0.00464 145 GLU A CG  
1123 C CD  . GLU A 145 ? 0.35534 0.43025 0.21134 0.04292  0.05354  0.00425  145 GLU A CD  
1124 O OE1 . GLU A 145 ? 0.39868 0.41820 0.25985 0.06451  0.02118  0.00455  145 GLU A OE1 
1125 O OE2 . GLU A 145 ? 0.36183 0.48907 0.26563 0.07375  0.01858  0.01112  145 GLU A OE2 
1126 N N   . ARG A 146 ? 0.33398 0.40780 0.21836 -0.03840 -0.01476 -0.00496 146 ARG A N   
1127 C CA  . ARG A 146 ? 0.36244 0.40234 0.21208 -0.07040 -0.04291 0.00377  146 ARG A CA  
1128 C C   . ARG A 146 ? 0.41487 0.37066 0.22672 -0.01460 -0.02278 -0.00941 146 ARG A C   
1129 O O   . ARG A 146 ? 0.49108 0.37906 0.25875 0.02455  -0.01932 0.01857  146 ARG A O   
1130 C CB  . ARG A 146 ? 0.39907 0.43213 0.23294 -0.10612 -0.03911 -0.01435 146 ARG A CB  
1131 C CG  . ARG A 146 ? 0.39602 0.47224 0.27418 -0.09381 -0.07862 -0.02782 146 ARG A CG  
1132 C CD  . ARG A 146 ? 0.42711 0.50623 0.30638 -0.02776 -0.12106 -0.01441 146 ARG A CD  
1133 N NE  . ARG A 146 ? 0.44903 0.49146 0.31742 -0.02600 -0.13984 -0.00686 146 ARG A NE  
1134 C CZ  . ARG A 146 ? 0.55987 0.49060 0.34627 -0.04636 -0.17396 -0.01099 146 ARG A CZ  
1135 N NH1 . ARG A 146 ? 0.60987 0.47884 0.35087 -0.09645 -0.17895 -0.02458 146 ARG A NH1 
1136 N NH2 . ARG A 146 ? 0.58767 0.47821 0.37428 -0.02772 -0.15309 0.01659  146 ARG A NH2 
1137 N N   . PHE A 147 ? 0.40362 0.36403 0.19219 0.02086  -0.03655 -0.00874 147 PHE A N   
1138 C CA  . PHE A 147 ? 0.38492 0.36148 0.20936 0.04866  -0.04168 -0.00372 147 PHE A CA  
1139 C C   . PHE A 147 ? 0.38791 0.38443 0.26253 0.00668  -0.02131 0.00482  147 PHE A C   
1140 O O   . PHE A 147 ? 0.38078 0.39106 0.29800 0.02841  -0.04132 0.02368  147 PHE A O   
1141 C CB  . PHE A 147 ? 0.31631 0.39152 0.21131 0.05415  -0.06527 -0.01150 147 PHE A CB  
1142 C CG  . PHE A 147 ? 0.34207 0.38212 0.20681 0.08244  -0.04594 0.01142  147 PHE A CG  
1143 C CD1 . PHE A 147 ? 0.38773 0.39239 0.22877 0.07587  -0.08192 -0.01759 147 PHE A CD1 
1144 C CD2 . PHE A 147 ? 0.37140 0.36961 0.25048 0.14516  -0.07904 -0.00370 147 PHE A CD2 
1145 C CE1 . PHE A 147 ? 0.42652 0.36356 0.23741 0.08364  -0.07487 -0.01277 147 PHE A CE1 
1146 C CE2 . PHE A 147 ? 0.43778 0.33519 0.26016 0.11975  -0.06729 0.00759  147 PHE A CE2 
1147 C CZ  . PHE A 147 ? 0.46333 0.32873 0.24888 0.09528  -0.05688 0.02395  147 PHE A CZ  
1148 N N   . ARG A 148 ? 0.44004 0.37602 0.24009 0.02147  -0.02505 -0.00150 148 ARG A N   
1149 C CA  A ARG A 148 ? 0.45435 0.40863 0.28022 0.01756  -0.02701 -0.00424 148 ARG A CA  
1150 C CA  B ARG A 148 ? 0.44877 0.37657 0.22472 0.00205  -0.03957 -0.01392 148 ARG A CA  
1151 C C   . ARG A 148 ? 0.42779 0.39662 0.22629 0.05576  -0.04087 0.02230  148 ARG A C   
1152 O O   . ARG A 148 ? 0.40179 0.43082 0.26533 0.10964  0.03339  0.01225  148 ARG A O   
1153 C CB  A ARG A 148 ? 0.50113 0.46532 0.37957 0.02139  -0.03222 -0.02334 148 ARG A CB  
1154 C CB  B ARG A 148 ? 0.47862 0.37679 0.21952 -0.02573 -0.07103 -0.05146 148 ARG A CB  
1155 C CG  A ARG A 148 ? 0.56039 0.52266 0.47095 0.06498  -0.04355 -0.02568 148 ARG A CG  
1156 C CG  B ARG A 148 ? 0.51235 0.39960 0.26287 -0.03075 -0.09402 -0.06019 148 ARG A CG  
1157 C CD  A ARG A 148 ? 0.60268 0.54317 0.50078 0.10145  -0.02366 -0.00932 148 ARG A CD  
1158 C CD  B ARG A 148 ? 0.52850 0.42682 0.29848 -0.02782 -0.11610 -0.07449 148 ARG A CD  
1159 N NE  A ARG A 148 ? 0.62794 0.54935 0.55646 0.10117  -0.00333 0.01850  148 ARG A NE  
1160 N NE  B ARG A 148 ? 0.54550 0.46328 0.34937 0.00078  -0.12650 -0.07130 148 ARG A NE  
1161 C CZ  A ARG A 148 ? 0.61730 0.55701 0.53363 0.10749  0.04374  0.04489  148 ARG A CZ  
1162 C CZ  B ARG A 148 ? 0.55322 0.49823 0.39473 0.00601  -0.12103 -0.01217 148 ARG A CZ  
1163 N NH1 A ARG A 148 ? 0.60126 0.56251 0.53507 0.13266  0.07197  0.02971  148 ARG A NH1 
1164 N NH1 B ARG A 148 ? 0.57592 0.50515 0.40527 -0.00820 -0.12141 -0.00302 148 ARG A NH1 
1165 N NH2 A ARG A 148 ? 0.64580 0.55412 0.56219 0.11712  0.03791  0.05480  148 ARG A NH2 
1166 N NH2 B ARG A 148 ? 0.56903 0.52507 0.41947 0.03601  -0.11047 0.01579  148 ARG A NH2 
1167 N N   . GLY A 149 ? 0.44131 0.45980 0.22964 0.00339  -0.01491 -0.00358 149 GLY A N   
1168 C CA  . GLY A 149 ? 0.38144 0.46273 0.22053 0.00270  -0.00809 -0.02216 149 GLY A CA  
1169 C C   . GLY A 149 ? 0.34482 0.47706 0.22900 -0.04082 -0.02379 -0.00769 149 GLY A C   
1170 O O   . GLY A 149 ? 0.34345 0.53996 0.27443 -0.10040 -0.00735 -0.01971 149 GLY A O   
1171 N N   . ASP A 150 ? 0.30629 0.41023 0.21747 -0.02862 -0.00492 -0.03271 150 ASP A N   
1172 C CA  . ASP A 150 ? 0.31621 0.41657 0.24707 0.00340  0.01784  -0.06120 150 ASP A CA  
1173 C C   . ASP A 150 ? 0.28635 0.40512 0.27757 0.02146  0.02498  -0.03831 150 ASP A C   
1174 O O   . ASP A 150 ? 0.30494 0.47180 0.30359 -0.00791 0.03496  -0.03163 150 ASP A O   
1175 C CB  . ASP A 150 ? 0.29994 0.39018 0.27940 -0.04026 0.01270  -0.01654 150 ASP A CB  
1176 C CG  . ASP A 150 ? 0.33015 0.41252 0.30765 -0.01278 0.01484  -0.01572 150 ASP A CG  
1177 O OD1 . ASP A 150 ? 0.49799 0.42348 0.33382 -0.03078 0.01015  0.01080  150 ASP A OD1 
1178 O OD2 . ASP A 150 ? 0.37388 0.39037 0.32535 0.02150  0.03647  -0.02745 150 ASP A OD2 
1179 N N   . GLY A 151 ? 0.29005 0.34905 0.28206 -0.00856 -0.00871 -0.02534 151 GLY A N   
1180 C CA  . GLY A 151 ? 0.30506 0.38201 0.27871 0.00189  -0.01986 -0.01682 151 GLY A CA  
1181 C C   . GLY A 151 ? 0.27264 0.35842 0.24818 -0.01379 -0.02812 -0.00001 151 GLY A C   
1182 O O   . GLY A 151 ? 0.30693 0.37674 0.22729 0.01595  -0.02059 0.00132  151 GLY A O   
1183 N N   . LEU A 152 ? 0.29081 0.33928 0.24385 -0.02402 -0.00613 0.01196  152 LEU A N   
1184 C CA  . LEU A 152 ? 0.21370 0.36749 0.22873 -0.03373 -0.00131 -0.00800 152 LEU A CA  
1185 C C   . LEU A 152 ? 0.22444 0.38622 0.24577 -0.00228 0.00523  -0.01484 152 LEU A C   
1186 O O   . LEU A 152 ? 0.22074 0.38160 0.27880 0.00400  0.01412  -0.03156 152 LEU A O   
1187 C CB  . LEU A 152 ? 0.27845 0.41727 0.21144 0.02208  0.00286  -0.00077 152 LEU A CB  
1188 C CG  . LEU A 152 ? 0.32349 0.43752 0.22347 0.08391  0.02324  0.00825  152 LEU A CG  
1189 C CD1 . LEU A 152 ? 0.37858 0.44583 0.24129 0.08295  0.00363  0.05005  152 LEU A CD1 
1190 C CD2 . LEU A 152 ? 0.31141 0.45982 0.27046 0.07478  0.01405  0.00524  152 LEU A CD2 
1191 N N   . CYS A 153 ? 0.25655 0.33903 0.22043 0.01347  0.01424  -0.02309 153 CYS A N   
1192 C CA  . CYS A 153 ? 0.24375 0.33153 0.20836 0.03553  -0.04173 0.00709  153 CYS A CA  
1193 C C   . CYS A 153 ? 0.26031 0.33071 0.25540 0.04759  -0.01899 0.01664  153 CYS A C   
1194 O O   . CYS A 153 ? 0.23245 0.36320 0.26684 0.06269  -0.00836 -0.00393 153 CYS A O   
1195 C CB  . CYS A 153 ? 0.21761 0.36084 0.21193 0.04394  -0.03768 -0.02923 153 CYS A CB  
1196 S SG  . CYS A 153 ? 0.26632 0.42632 0.24380 0.00034  0.00381  -0.01645 153 CYS A SG  
1197 N N   . MET A 154 ? 0.21669 0.36603 0.25632 0.01320  -0.00030 0.01175  154 MET A N   
1198 C CA  . MET A 154 ? 0.25439 0.34417 0.23093 0.01071  0.00321  -0.00498 154 MET A CA  
1199 C C   . MET A 154 ? 0.26909 0.34506 0.22835 0.00759  0.00520  -0.01816 154 MET A C   
1200 O O   . MET A 154 ? 0.24144 0.33740 0.24920 0.03590  0.01993  -0.00076 154 MET A O   
1201 C CB  . MET A 154 ? 0.28693 0.32302 0.26212 0.07991  -0.01435 0.02414  154 MET A CB  
1202 C CG  . MET A 154 ? 0.25899 0.37238 0.27444 0.02483  0.02038  -0.00630 154 MET A CG  
1203 S SD  . MET A 154 ? 0.27872 0.36143 0.25681 0.04785  0.00462  0.01233  154 MET A SD  
1204 C CE  . MET A 154 ? 0.41473 0.29018 0.25539 0.02127  0.00453  -0.00679 154 MET A CE  
1205 N N   . SER A 155 ? 0.30235 0.32468 0.21148 0.02358  -0.00512 -0.01265 155 SER A N   
1206 C CA  . SER A 155 ? 0.32792 0.30168 0.20405 0.01788  0.00193  -0.01237 155 SER A CA  
1207 C C   . SER A 155 ? 0.35277 0.32776 0.21123 -0.01688 0.00546  -0.01747 155 SER A C   
1208 O O   . SER A 155 ? 0.35698 0.35595 0.23608 0.01394  0.02587  0.00232  155 SER A O   
1209 C CB  . SER A 155 ? 0.34380 0.31675 0.17707 0.06510  -0.02759 -0.01997 155 SER A CB  
1210 O OG  . SER A 155 ? 0.30718 0.32539 0.27307 0.03726  0.00167  -0.02007 155 SER A OG  
1211 N N   . THR A 156 ? 0.31742 0.29944 0.22813 0.02289  0.00422  -0.03290 156 THR A N   
1212 C CA  . THR A 156 ? 0.29502 0.29087 0.26323 0.01213  0.01015  -0.00891 156 THR A CA  
1213 C C   . THR A 156 ? 0.28259 0.31310 0.27271 0.01334  0.01335  0.00080  156 THR A C   
1214 O O   . THR A 156 ? 0.28965 0.43445 0.24763 0.03664  0.01230  0.00901  156 THR A O   
1215 C CB  . THR A 156 ? 0.26484 0.35770 0.25627 0.02792  0.01948  -0.00955 156 THR A CB  
1216 O OG1 . THR A 156 ? 0.32679 0.35953 0.23415 0.00229  -0.00105 -0.00098 156 THR A OG1 
1217 C CG2 . THR A 156 ? 0.25202 0.38698 0.32361 0.01736  0.03848  -0.02721 156 THR A CG2 
1218 N N   . PRO A 157 ? 0.32718 0.32921 0.26725 -0.01217 -0.00660 -0.02120 157 PRO A N   
1219 C CA  . PRO A 157 ? 0.34721 0.33411 0.24769 -0.01339 0.00833  -0.00767 157 PRO A CA  
1220 C C   . PRO A 157 ? 0.35451 0.36752 0.25763 -0.00485 0.01363  -0.04989 157 PRO A C   
1221 O O   . PRO A 157 ? 0.34122 0.40639 0.24705 -0.01479 0.01724  -0.05130 157 PRO A O   
1222 C CB  . PRO A 157 ? 0.32590 0.34731 0.26887 -0.01220 -0.04194 -0.01285 157 PRO A CB  
1223 C CG  . PRO A 157 ? 0.32065 0.34087 0.29603 0.01186  -0.07364 -0.02665 157 PRO A CG  
1224 C CD  . PRO A 157 ? 0.32877 0.30766 0.28644 0.02567  -0.02843 -0.02484 157 PRO A CD  
1225 N N   . SER A 158 ? 0.35221 0.36942 0.25353 0.02438  -0.00153 -0.03651 158 SER A N   
1226 C CA  . SER A 158 ? 0.36213 0.33240 0.23543 0.03755  0.00002  -0.01357 158 SER A CA  
1227 C C   . SER A 158 ? 0.29160 0.35828 0.22005 -0.01165 0.00303  -0.02843 158 SER A C   
1228 O O   . SER A 158 ? 0.33618 0.33099 0.25911 0.03433  0.01450  -0.01190 158 SER A O   
1229 C CB  . SER A 158 ? 0.38203 0.37878 0.22079 0.04285  -0.02175 -0.01750 158 SER A CB  
1230 O OG  . SER A 158 ? 0.35569 0.42587 0.24628 0.07860  -0.01191 -0.01184 158 SER A OG  
1231 N N   . GLY A 159 ? 0.30821 0.35215 0.23658 -0.00073 0.01910  -0.08933 159 GLY A N   
1232 C CA  . GLY A 159 ? 0.25924 0.38404 0.23373 0.01756  0.02164  -0.05489 159 GLY A CA  
1233 C C   . GLY A 159 ? 0.30658 0.38358 0.22549 -0.01651 -0.00457 -0.02654 159 GLY A C   
1234 O O   . GLY A 159 ? 0.28974 0.39867 0.24629 -0.04148 -0.01782 -0.01146 159 GLY A O   
1235 N N   . THR A 160 ? 0.27920 0.34182 0.22679 0.01733  -0.01190 -0.01658 160 THR A N   
1236 C CA  . THR A 160 ? 0.24413 0.30802 0.24680 0.02712  0.01786  -0.00614 160 THR A CA  
1237 C C   . THR A 160 ? 0.23750 0.31375 0.25388 -0.01777 -0.01432 -0.00720 160 THR A C   
1238 O O   . THR A 160 ? 0.28414 0.26991 0.25720 -0.01087 -0.00109 -0.03246 160 THR A O   
1239 C CB  . THR A 160 ? 0.23942 0.28785 0.26542 -0.05356 -0.02214 0.01918  160 THR A CB  
1240 O OG1 . THR A 160 ? 0.29101 0.24013 0.28613 -0.01737 -0.01091 -0.00991 160 THR A OG1 
1241 C CG2 . THR A 160 ? 0.29128 0.28730 0.26415 -0.03188 -0.04848 0.04608  160 THR A CG2 
1242 N N   . THR A 161 ? 0.24007 0.35371 0.25918 -0.02985 0.00303  0.01746  161 THR A N   
1243 C CA  . THR A 161 ? 0.26762 0.33530 0.23854 -0.04697 -0.00912 0.00783  161 THR A CA  
1244 C C   . THR A 161 ? 0.22727 0.37542 0.26161 -0.03790 0.01410  0.00303  161 THR A C   
1245 O O   . THR A 161 ? 0.25227 0.38622 0.26777 -0.05074 0.00162  0.00258  161 THR A O   
1246 C CB  . THR A 161 ? 0.24165 0.30353 0.26736 0.01125  0.00740  -0.04447 161 THR A CB  
1247 O OG1 . THR A 161 ? 0.33768 0.31983 0.24245 0.00635  -0.01219 -0.01537 161 THR A OG1 
1248 C CG2 . THR A 161 ? 0.30941 0.34412 0.31334 -0.04462 0.00364  -0.01670 161 THR A CG2 
1249 N N   . ALA A 162 ? 0.22144 0.36125 0.27479 -0.00990 -0.00755 -0.02949 162 ALA A N   
1250 C CA  . ALA A 162 ? 0.23942 0.37222 0.28794 0.03529  0.03261  -0.05574 162 ALA A CA  
1251 C C   . ALA A 162 ? 0.27452 0.34412 0.26363 0.00693  0.01358  -0.04093 162 ALA A C   
1252 O O   . ALA A 162 ? 0.25397 0.40889 0.24721 0.02771  -0.00148 -0.01143 162 ALA A O   
1253 C CB  . ALA A 162 ? 0.28374 0.40713 0.27299 0.05455  0.02729  -0.08200 162 ALA A CB  
1254 N N   . TYR A 163 ? 0.29557 0.32726 0.25795 -0.02944 0.02352  -0.05541 163 TYR A N   
1255 C CA  . TYR A 163 ? 0.21070 0.30470 0.25814 -0.01676 0.02510  -0.04787 163 TYR A CA  
1256 C C   . TYR A 163 ? 0.25717 0.34814 0.25286 -0.01888 -0.01182 -0.02460 163 TYR A C   
1257 O O   . TYR A 163 ? 0.22921 0.39331 0.25722 -0.00394 -0.00986 0.00077  163 TYR A O   
1258 C CB  . TYR A 163 ? 0.17864 0.32286 0.27539 0.00167  -0.00602 -0.02534 163 TYR A CB  
1259 C CG  . TYR A 163 ? 0.21130 0.34891 0.25182 -0.02288 -0.04029 -0.02699 163 TYR A CG  
1260 C CD1 . TYR A 163 ? 0.25403 0.36796 0.27094 -0.03130 -0.00400 -0.05455 163 TYR A CD1 
1261 C CD2 . TYR A 163 ? 0.25173 0.39212 0.32509 -0.04276 -0.06253 -0.03678 163 TYR A CD2 
1262 C CE1 . TYR A 163 ? 0.24301 0.32963 0.32155 -0.09303 -0.01836 -0.01935 163 TYR A CE1 
1263 C CE2 . TYR A 163 ? 0.35477 0.37761 0.34964 -0.06851 -0.05592 -0.01562 163 TYR A CE2 
1264 C CZ  . TYR A 163 ? 0.26695 0.31759 0.34503 -0.10926 -0.03652 -0.01866 163 TYR A CZ  
1265 O OH  . TYR A 163 ? 0.33540 0.34180 0.37542 -0.08580 -0.09399 -0.02666 163 TYR A OH  
1266 N N   . ASN A 164 ? 0.23664 0.35680 0.24280 -0.04387 0.02319  0.00588  164 ASN A N   
1267 C CA  . ASN A 164 ? 0.23409 0.33129 0.24011 -0.02832 0.03400  0.02237  164 ASN A CA  
1268 C C   . ASN A 164 ? 0.22721 0.33955 0.24206 0.00275  0.03460  0.01929  164 ASN A C   
1269 O O   . ASN A 164 ? 0.23173 0.31922 0.25409 0.00845  0.00551  0.01248  164 ASN A O   
1270 C CB  . ASN A 164 ? 0.26331 0.27256 0.23919 0.00124  0.03239  -0.00293 164 ASN A CB  
1271 C CG  . ASN A 164 ? 0.27829 0.32098 0.22467 -0.01765 0.00570  0.01195  164 ASN A CG  
1272 O OD1 . ASN A 164 ? 0.30351 0.39476 0.21024 -0.02821 0.01671  -0.01253 164 ASN A OD1 
1273 N ND2 . ASN A 164 ? 0.23098 0.31513 0.23943 0.02209  -0.01746 0.01625  164 ASN A ND2 
1274 N N   . LYS A 165 ? 0.27313 0.34338 0.21431 0.00099  -0.00071 0.02207  165 LYS A N   
1275 C CA  . LYS A 165 ? 0.24989 0.25639 0.19925 0.03733  -0.00817 0.00092  165 LYS A CA  
1276 C C   . LYS A 165 ? 0.26771 0.27944 0.22099 -0.00967 -0.00277 0.01486  165 LYS A C   
1277 O O   . LYS A 165 ? 0.26351 0.32529 0.25489 0.00365  0.00398  -0.02175 165 LYS A O   
1278 C CB  . LYS A 165 ? 0.26301 0.33727 0.21913 0.04393  -0.03269 -0.01616 165 LYS A CB  
1279 C CG  . LYS A 165 ? 0.29156 0.36344 0.22917 0.04052  -0.08050 -0.01435 165 LYS A CG  
1280 C CD  . LYS A 165 ? 0.29931 0.40686 0.22748 0.02094  -0.07655 -0.01459 165 LYS A CD  
1281 C CE  . LYS A 165 ? 0.44556 0.40938 0.28278 0.06108  -0.09188 -0.00029 165 LYS A CE  
1282 N NZ  . LYS A 165 ? 0.57132 0.41785 0.32656 0.06772  -0.14121 -0.03042 165 LYS A NZ  
1283 N N   . SER A 166 ? 0.28386 0.30401 0.22385 -0.03911 -0.00930 0.01044  166 SER A N   
1284 C CA  . SER A 166 ? 0.27812 0.29052 0.22111 -0.05636 0.04348  0.04734  166 SER A CA  
1285 C C   . SER A 166 ? 0.28346 0.30838 0.24436 -0.00395 0.04883  0.00224  166 SER A C   
1286 O O   . SER A 166 ? 0.34750 0.28596 0.24708 0.01301  0.02805  -0.01242 166 SER A O   
1287 C CB  . SER A 166 ? 0.27704 0.36914 0.22111 0.02083  0.07900  0.00936  166 SER A CB  
1288 O OG  . SER A 166 ? 0.33604 0.41133 0.23107 -0.00352 0.06434  0.01128  166 SER A OG  
1289 N N   . LEU A 167 ? 0.28407 0.36627 0.23934 -0.03677 0.01440  -0.00336 167 LEU A N   
1290 C CA  . LEU A 167 ? 0.24170 0.38857 0.23048 0.03379  0.02143  -0.02768 167 LEU A CA  
1291 C C   . LEU A 167 ? 0.25295 0.38233 0.25362 0.00448  -0.00567 -0.02860 167 LEU A C   
1292 O O   . LEU A 167 ? 0.26287 0.48522 0.25153 -0.01736 0.00687  -0.03191 167 LEU A O   
1293 C CB  . LEU A 167 ? 0.21707 0.37655 0.25000 0.02072  0.01296  -0.02405 167 LEU A CB  
1294 C CG  . LEU A 167 ? 0.23227 0.37754 0.26092 -0.01469 -0.03262 0.01515  167 LEU A CG  
1295 C CD1 . LEU A 167 ? 0.27605 0.38988 0.24931 0.01995  -0.01737 0.02706  167 LEU A CD1 
1296 C CD2 . LEU A 167 ? 0.26889 0.36112 0.25566 -0.05504 -0.03090 -0.00424 167 LEU A CD2 
1297 N N   . GLY A 168 ? 0.27138 0.36917 0.25771 -0.01692 -0.00038 -0.00742 168 GLY A N   
1298 C CA  . GLY A 168 ? 0.21526 0.37950 0.27008 -0.05200 0.01469  -0.01984 168 GLY A CA  
1299 C C   . GLY A 168 ? 0.22185 0.38127 0.24736 -0.07481 0.03990  -0.01141 168 GLY A C   
1300 O O   . GLY A 168 ? 0.28040 0.35357 0.24540 -0.01079 0.03876  -0.00910 168 GLY A O   
1301 N N   . GLY A 169 ? 0.23908 0.37230 0.23655 -0.04098 0.00453  -0.00452 169 GLY A N   
1302 C CA  . GLY A 169 ? 0.24994 0.34493 0.23237 -0.07554 -0.03398 0.00209  169 GLY A CA  
1303 C C   . GLY A 169 ? 0.25586 0.33618 0.21386 -0.04506 0.00360  -0.01730 169 GLY A C   
1304 O O   . GLY A 169 ? 0.28038 0.35224 0.21582 -0.02282 0.00940  -0.00038 169 GLY A O   
1305 N N   . ALA A 170 ? 0.25177 0.29464 0.23032 -0.02637 0.01120  -0.01557 170 ALA A N   
1306 C CA  . ALA A 170 ? 0.25396 0.30079 0.22862 0.00446  0.02566  -0.02899 170 ALA A CA  
1307 C C   . ALA A 170 ? 0.27745 0.35453 0.24314 0.01317  0.01638  -0.02816 170 ALA A C   
1308 O O   . ALA A 170 ? 0.26574 0.37029 0.24378 0.03669  -0.00362 0.01872  170 ALA A O   
1309 C CB  . ALA A 170 ? 0.30076 0.28549 0.25849 0.02437  0.05305  0.02465  170 ALA A CB  
1310 N N   . LEU A 171 ? 0.27911 0.31186 0.21337 -0.01896 0.00701  -0.02899 171 LEU A N   
1311 C CA  . LEU A 171 ? 0.29315 0.31654 0.22792 -0.01473 -0.00942 -0.03017 171 LEU A CA  
1312 C C   . LEU A 171 ? 0.28888 0.31875 0.28533 -0.00635 -0.01083 -0.01418 171 LEU A C   
1313 O O   . LEU A 171 ? 0.28310 0.38161 0.32601 0.03649  0.01519  -0.00294 171 LEU A O   
1314 C CB  . LEU A 171 ? 0.32148 0.32391 0.19858 0.00693  -0.00227 -0.02385 171 LEU A CB  
1315 C CG  . LEU A 171 ? 0.25032 0.36305 0.23695 -0.00635 -0.04726 0.02094  171 LEU A CG  
1316 C CD1 . LEU A 171 ? 0.24380 0.41815 0.25196 -0.03397 -0.04092 0.01318  171 LEU A CD1 
1317 C CD2 . LEU A 171 ? 0.24230 0.38918 0.28530 -0.00002 -0.05324 0.00635  171 LEU A CD2 
1318 N N   . MET A 172 ? 0.31883 0.24862 0.29206 -0.00706 0.00731  -0.02504 172 MET A N   
1319 C CA  A MET A 172 ? 0.36472 0.26612 0.30561 -0.04862 0.03066  -0.01596 172 MET A CA  
1320 C CA  B MET A 172 ? 0.37141 0.29253 0.32068 -0.05334 -0.00419 0.00365  172 MET A CA  
1321 C C   . MET A 172 ? 0.37184 0.28862 0.33639 -0.05224 0.03738  -0.01996 172 MET A C   
1322 O O   . MET A 172 ? 0.34613 0.25093 0.39976 -0.03895 0.06962  -0.04436 172 MET A O   
1323 C CB  A MET A 172 ? 0.43842 0.27184 0.30584 -0.03502 0.03512  0.00356  172 MET A CB  
1324 C CB  B MET A 172 ? 0.45150 0.35016 0.36896 -0.04183 -0.06181 0.06267  172 MET A CB  
1325 C CG  A MET A 172 ? 0.49997 0.32147 0.27987 -0.04933 0.03493  0.00481  172 MET A CG  
1326 C CG  B MET A 172 ? 0.51888 0.41923 0.39605 -0.02494 -0.05303 0.11297  172 MET A CG  
1327 S SD  A MET A 172 ? 0.54888 0.30857 0.24427 -0.06110 -0.01357 -0.03882 172 MET A SD  
1328 S SD  B MET A 172 ? 0.61044 0.50957 0.45341 -0.02682 -0.04059 0.12437  172 MET A SD  
1329 C CE  A MET A 172 ? 0.55313 0.30081 0.25632 0.00197  0.02675  -0.06509 172 MET A CE  
1330 C CE  B MET A 172 ? 0.62891 0.53495 0.47207 -0.07378 -0.00820 0.12292  172 MET A CE  
1331 N N   . HIS A 173 ? 0.38811 0.24951 0.31334 -0.05572 0.01074  -0.07627 173 HIS A N   
1332 C CA  . HIS A 173 ? 0.30867 0.32630 0.32385 -0.00293 -0.02390 -0.08693 173 HIS A CA  
1333 C C   . HIS A 173 ? 0.35571 0.33939 0.34053 0.03268  0.00685  -0.05113 173 HIS A C   
1334 O O   . HIS A 173 ? 0.35336 0.31679 0.38362 -0.02551 0.01699  -0.06002 173 HIS A O   
1335 C CB  . HIS A 173 ? 0.36739 0.32573 0.33054 -0.01925 -0.02872 -0.05591 173 HIS A CB  
1336 C CG  . HIS A 173 ? 0.40358 0.35044 0.33714 -0.01848 -0.02976 -0.04759 173 HIS A CG  
1337 N ND1 . HIS A 173 ? 0.48566 0.35595 0.34843 0.00069  -0.04914 -0.04433 173 HIS A ND1 
1338 C CD2 . HIS A 173 ? 0.38563 0.36250 0.32921 -0.03302 0.00040  -0.01223 173 HIS A CD2 
1339 C CE1 . HIS A 173 ? 0.48259 0.37137 0.33481 -0.01655 -0.04722 -0.01562 173 HIS A CE1 
1340 N NE2 . HIS A 173 ? 0.41678 0.37684 0.33509 -0.00900 -0.02520 -0.01194 173 HIS A NE2 
1341 N N   . PRO A 174 ? 0.35065 0.34905 0.32770 0.05181  0.00831  -0.10032 174 PRO A N   
1342 C CA  . PRO A 174 ? 0.35739 0.40338 0.35442 0.07008  0.00743  -0.08024 174 PRO A CA  
1343 C C   . PRO A 174 ? 0.39952 0.46094 0.38995 0.04618  -0.00780 -0.09396 174 PRO A C   
1344 O O   . PRO A 174 ? 0.46585 0.47233 0.43157 0.05639  -0.03560 -0.09083 174 PRO A O   
1345 C CB  . PRO A 174 ? 0.39582 0.48084 0.36374 0.09033  0.04001  -0.06535 174 PRO A CB  
1346 C CG  . PRO A 174 ? 0.40607 0.47097 0.33623 0.09445  0.00217  -0.05537 174 PRO A CG  
1347 C CD  . PRO A 174 ? 0.33301 0.37173 0.29272 0.04739  0.01745  -0.08354 174 PRO A CD  
1348 N N   . SER A 175 ? 0.41150 0.43797 0.39023 -0.00469 -0.06284 -0.08733 175 SER A N   
1349 C CA  . SER A 175 ? 0.47688 0.40532 0.38612 0.02367  -0.06890 -0.04108 175 SER A CA  
1350 C C   . SER A 175 ? 0.49717 0.39723 0.40401 0.00916  -0.02874 -0.02139 175 SER A C   
1351 O O   . SER A 175 ? 0.54205 0.36324 0.43075 0.04381  -0.07705 0.00593  175 SER A O   
1352 C CB  . SER A 175 ? 0.49768 0.42309 0.41434 0.05580  -0.07810 -0.01471 175 SER A CB  
1353 O OG  . SER A 175 ? 0.54740 0.46190 0.43082 0.02853  -0.08136 -0.03643 175 SER A OG  
1354 N N   . ILE A 176 ? 0.41294 0.40433 0.40244 -0.03041 -0.01970 -0.00785 176 ILE A N   
1355 C CA  . ILE A 176 ? 0.34471 0.39300 0.37002 -0.01805 -0.00094 -0.01126 176 ILE A CA  
1356 C C   . ILE A 176 ? 0.37952 0.36691 0.35520 0.00816  -0.01311 -0.00003 176 ILE A C   
1357 O O   . ILE A 176 ? 0.41150 0.37994 0.36672 0.03267  -0.01751 0.04156  176 ILE A O   
1358 C CB  . ILE A 176 ? 0.32081 0.38151 0.38763 -0.00059 0.01193  -0.03153 176 ILE A CB  
1359 C CG1 . ILE A 176 ? 0.30813 0.38508 0.39262 0.03871  -0.01343 -0.07518 176 ILE A CG1 
1360 C CG2 . ILE A 176 ? 0.27581 0.37568 0.39353 -0.01969 0.00527  -0.00649 176 ILE A CG2 
1361 C CD1 . ILE A 176 ? 0.33186 0.40321 0.39412 0.07676  0.01874  -0.09664 176 ILE A CD1 
1362 N N   . GLU A 177 ? 0.40671 0.29888 0.30975 0.01356  0.01340  -0.03314 177 GLU A N   
1363 C CA  . GLU A 177 ? 0.42140 0.23522 0.33870 0.00119  -0.00094 -0.02148 177 GLU A CA  
1364 C C   . GLU A 177 ? 0.42371 0.32748 0.31502 0.02625  0.01622  0.00002  177 GLU A C   
1365 O O   . GLU A 177 ? 0.40565 0.40752 0.31579 0.01712  0.04006  -0.00679 177 GLU A O   
1366 C CB  . GLU A 177 ? 0.53773 0.23758 0.41488 0.01993  0.01845  -0.02209 177 GLU A CB  
1367 C CG  . GLU A 177 ? 0.60579 0.32438 0.48153 0.03027  0.05411  -0.05022 177 GLU A CG  
1368 C CD  . GLU A 177 ? 0.64776 0.44407 0.54185 0.01610  0.10897  -0.03387 177 GLU A CD  
1369 O OE1 . GLU A 177 ? 0.66432 0.45577 0.56649 -0.02939 0.08718  -0.05256 177 GLU A OE1 
1370 O OE2 . GLU A 177 ? 0.66798 0.51218 0.56628 0.04616  0.14078  -0.02208 177 GLU A OE2 
1371 N N   . ALA A 178 ? 0.40507 0.29981 0.30627 0.05196  0.02339  -0.00419 178 ALA A N   
1372 C CA  . ALA A 178 ? 0.30314 0.30669 0.27486 0.08427  0.00700  -0.00090 178 ALA A CA  
1373 C C   . ALA A 178 ? 0.37985 0.32631 0.26902 0.01492  0.01299  0.03359  178 ALA A C   
1374 O O   . ALA A 178 ? 0.37614 0.38101 0.26302 0.03928  0.02153  0.02543  178 ALA A O   
1375 C CB  . ALA A 178 ? 0.35505 0.31579 0.28973 0.04394  0.00945  0.00311  178 ALA A CB  
1376 N N   . MET A 179 ? 0.31863 0.29714 0.27759 0.00599  -0.01984 0.04882  179 MET A N   
1377 C CA  . MET A 179 ? 0.31139 0.28461 0.26727 0.01647  -0.02992 0.01340  179 MET A CA  
1378 C C   . MET A 179 ? 0.28815 0.28979 0.24603 0.04942  -0.01743 0.03414  179 MET A C   
1379 O O   . MET A 179 ? 0.33176 0.32019 0.24697 0.01121  0.04905  0.03052  179 MET A O   
1380 C CB  . MET A 179 ? 0.31974 0.26340 0.21947 0.05206  -0.05148 0.01013  179 MET A CB  
1381 C CG  . MET A 179 ? 0.30715 0.28630 0.22496 0.04339  -0.04101 0.02793  179 MET A CG  
1382 S SD  . MET A 179 ? 0.34460 0.33725 0.26551 0.09552  -0.00869 0.01012  179 MET A SD  
1383 C CE  . MET A 179 ? 0.35055 0.35079 0.21956 0.08379  -0.00383 0.00862  179 MET A CE  
1384 N N   . GLN A 180 ? 0.26412 0.31919 0.25274 0.03547  -0.02175 0.00568  180 GLN A N   
1385 C CA  . GLN A 180 ? 0.25748 0.32597 0.24283 0.03272  -0.00812 0.00937  180 GLN A CA  
1386 C C   . GLN A 180 ? 0.30706 0.32503 0.23268 0.02500  0.00176  -0.01294 180 GLN A C   
1387 O O   . GLN A 180 ? 0.27432 0.32734 0.24767 0.03942  -0.00626 -0.01116 180 GLN A O   
1388 C CB  . GLN A 180 ? 0.29108 0.32017 0.22452 0.08006  -0.00328 0.03210  180 GLN A CB  
1389 C CG  . GLN A 180 ? 0.27481 0.29482 0.21061 0.06441  -0.00509 0.02938  180 GLN A CG  
1390 C CD  . GLN A 180 ? 0.27852 0.31386 0.23309 0.04790  -0.00623 -0.00088 180 GLN A CD  
1391 O OE1 . GLN A 180 ? 0.32912 0.31726 0.22579 0.05689  -0.01578 -0.00659 180 GLN A OE1 
1392 N NE2 . GLN A 180 ? 0.27764 0.29339 0.25708 0.00734  -0.01905 -0.02499 180 GLN A NE2 
1393 N N   . LEU A 181 ? 0.28994 0.34530 0.21838 -0.01822 -0.01122 -0.00362 181 LEU A N   
1394 C CA  . LEU A 181 ? 0.31941 0.36539 0.20672 0.00424  -0.02428 0.02000  181 LEU A CA  
1395 C C   . LEU A 181 ? 0.28591 0.33349 0.21494 -0.01376 0.01858  0.01302  181 LEU A C   
1396 O O   . LEU A 181 ? 0.27443 0.34015 0.23744 -0.01819 0.00408  0.00540  181 LEU A O   
1397 C CB  . LEU A 181 ? 0.31137 0.37624 0.20737 -0.00940 -0.03125 0.02378  181 LEU A CB  
1398 C CG  . LEU A 181 ? 0.28965 0.40572 0.21179 -0.02596 0.00455  0.00576  181 LEU A CG  
1399 C CD1 . LEU A 181 ? 0.23955 0.36092 0.26422 0.01601  0.01000  0.02846  181 LEU A CD1 
1400 C CD2 . LEU A 181 ? 0.30048 0.44185 0.20492 0.01348  0.02679  0.02208  181 LEU A CD2 
1401 N N   . THR A 182 ? 0.24939 0.32913 0.21905 0.00895  -0.01675 0.02567  182 THR A N   
1402 C CA  . THR A 182 ? 0.24860 0.33692 0.20340 0.02996  -0.01892 0.02203  182 THR A CA  
1403 C C   . THR A 182 ? 0.20815 0.35418 0.22937 0.05838  -0.03278 0.01199  182 THR A C   
1404 O O   . THR A 182 ? 0.21348 0.35975 0.23011 0.01186  -0.01320 0.00602  182 THR A O   
1405 C CB  . THR A 182 ? 0.18261 0.43237 0.20277 -0.01390 0.02021  -0.00798 182 THR A CB  
1406 O OG1 . THR A 182 ? 0.23891 0.43772 0.22475 0.01426  0.02320  0.03611  182 THR A OG1 
1407 C CG2 . THR A 182 ? 0.23133 0.47207 0.18904 0.00069  -0.01424 -0.02837 182 THR A CG2 
1408 N N   . GLU A 183 ? 0.27457 0.36199 0.24265 -0.00076 0.02045  -0.01874 183 GLU A N   
1409 C CA  . GLU A 183 ? 0.28922 0.35442 0.25678 -0.03744 0.00849  0.00086  183 GLU A CA  
1410 C C   . GLU A 183 ? 0.27082 0.31961 0.23753 0.00106  -0.03346 0.02119  183 GLU A C   
1411 O O   . GLU A 183 ? 0.26716 0.37292 0.26938 -0.02591 -0.03936 0.03356  183 GLU A O   
1412 C CB  . GLU A 183 ? 0.28186 0.37524 0.26290 0.00514  0.01835  -0.01340 183 GLU A CB  
1413 C CG  . GLU A 183 ? 0.34461 0.38780 0.25347 -0.00363 0.05392  0.00638  183 GLU A CG  
1414 C CD  . GLU A 183 ? 0.39915 0.43713 0.30857 -0.00555 0.01954  -0.01909 183 GLU A CD  
1415 O OE1 . GLU A 183 ? 0.47676 0.43658 0.37118 -0.01318 0.08233  -0.04736 183 GLU A OE1 
1416 O OE2 . GLU A 183 ? 0.36982 0.48612 0.27846 -0.02178 -0.01851 -0.02529 183 GLU A OE2 
1417 N N   . MET A 184 ? 0.25566 0.29778 0.27411 0.01217  -0.01467 -0.00137 184 MET A N   
1418 C CA  . MET A 184 ? 0.25975 0.33832 0.25723 0.02935  -0.03246 -0.01608 184 MET A CA  
1419 C C   . MET A 184 ? 0.31457 0.36233 0.26639 0.04809  -0.05087 -0.03050 184 MET A C   
1420 O O   . MET A 184 ? 0.29923 0.41455 0.30712 0.03166  -0.02054 0.00959  184 MET A O   
1421 C CB  . MET A 184 ? 0.23517 0.36923 0.26766 0.01299  -0.01773 -0.02534 184 MET A CB  
1422 C CG  . MET A 184 ? 0.30033 0.42246 0.26446 0.05574  0.04825  -0.06332 184 MET A CG  
1423 S SD  . MET A 184 ? 0.40827 0.53313 0.39248 0.01762  0.09727  -0.03439 184 MET A SD  
1424 C CE  . MET A 184 ? 0.34293 0.49917 0.42061 0.05193  0.03116  -0.02270 184 MET A CE  
1425 N N   . ALA A 185 ? 0.32039 0.34247 0.25645 0.03885  -0.02910 -0.02714 185 ALA A N   
1426 C CA  . ALA A 185 ? 0.40074 0.30869 0.23355 -0.04146 -0.00076 -0.00772 185 ALA A CA  
1427 C C   . ALA A 185 ? 0.43798 0.38929 0.23246 -0.00824 -0.03530 0.01938  185 ALA A C   
1428 O O   . ALA A 185 ? 0.49906 0.47285 0.26775 -0.05860 -0.08586 0.05960  185 ALA A O   
1429 C CB  . ALA A 185 ? 0.40728 0.24862 0.26998 -0.01782 0.00609  -0.00466 185 ALA A CB  
1430 N N   . SER A 186 ? 0.43719 0.43582 0.20353 0.04849  0.03777  0.02030  186 SER A N   
1431 C CA  . SER A 186 ? 0.47327 0.43736 0.21405 0.01483  0.08118  -0.02615 186 SER A CA  
1432 C C   . SER A 186 ? 0.46779 0.44307 0.26849 0.05707  0.06666  -0.01456 186 SER A C   
1433 O O   . SER A 186 ? 0.50919 0.44498 0.28946 0.06825  0.03346  -0.02370 186 SER A O   
1434 C CB  . SER A 186 ? 0.46084 0.47512 0.29682 0.04198  0.04784  0.00241  186 SER A CB  
1435 O OG  . SER A 186 ? 0.54800 0.51106 0.36250 0.08716  0.07186  -0.00983 186 SER A OG  
1436 N N   . ILE A 187 ? 0.46043 0.42226 0.26903 0.04796  0.07938  -0.01567 187 ILE A N   
1437 C CA  . ILE A 187 ? 0.45206 0.40247 0.29263 0.01840  0.05745  -0.03113 187 ILE A CA  
1438 C C   . ILE A 187 ? 0.49488 0.40712 0.29640 -0.01390 0.09325  -0.04274 187 ILE A C   
1439 O O   . ILE A 187 ? 0.59738 0.38133 0.28863 -0.00179 0.12263  -0.02124 187 ILE A O   
1440 C CB  . ILE A 187 ? 0.49939 0.40527 0.36796 0.03665  0.08975  -0.05882 187 ILE A CB  
1441 C CG1 . ILE A 187 ? 0.57136 0.43734 0.40179 0.01115  0.07229  0.00338  187 ILE A CG1 
1442 C CG2 . ILE A 187 ? 0.50048 0.43835 0.41841 0.01461  0.09354  -0.05643 187 ILE A CG2 
1443 C CD1 . ILE A 187 ? 0.62932 0.47434 0.43116 0.00135  0.08793  0.01319  187 ILE A CD1 
1444 N N   . ASN A 188 ? 0.44040 0.44395 0.30211 -0.01332 0.02548  -0.06686 188 ASN A N   
1445 C CA  . ASN A 188 ? 0.49630 0.45772 0.36662 0.01430  0.00410  -0.08436 188 ASN A CA  
1446 C C   . ASN A 188 ? 0.49499 0.49584 0.35612 0.01547  0.08236  -0.05005 188 ASN A C   
1447 O O   . ASN A 188 ? 0.47165 0.49037 0.35929 -0.00693 0.10606  -0.02798 188 ASN A O   
1448 C CB  . ASN A 188 ? 0.49127 0.47030 0.42997 0.04795  -0.02885 -0.05716 188 ASN A CB  
1449 C CG  . ASN A 188 ? 0.50027 0.46156 0.42079 0.05398  -0.02664 -0.06958 188 ASN A CG  
1450 O OD1 . ASN A 188 ? 0.48729 0.43742 0.41805 0.01388  -0.03213 -0.06545 188 ASN A OD1 
1451 N ND2 . ASN A 188 ? 0.44952 0.46150 0.41031 0.06368  -0.04546 -0.06070 188 ASN A ND2 
1452 N N   . ASN A 189 ? 0.54694 0.48947 0.35620 -0.00012 0.09095  -0.07808 189 ASN A N   
1453 C CA  . ASN A 189 ? 0.63177 0.47316 0.36625 0.02807  0.07428  -0.06181 189 ASN A CA  
1454 C C   . ASN A 189 ? 0.73309 0.50891 0.40766 0.01839  0.17833  -0.04505 189 ASN A C   
1455 O O   . ASN A 189 ? 0.78769 0.55855 0.42873 0.00704  0.22144  -0.02250 189 ASN A O   
1456 C CB  . ASN A 189 ? 0.67001 0.49416 0.36201 0.04584  0.01275  -0.01689 189 ASN A CB  
1457 C CG  . ASN A 189 ? 0.72634 0.53128 0.37779 0.03298  -0.03401 -0.01769 189 ASN A CG  
1458 O OD1 . ASN A 189 ? 0.79292 0.54743 0.40015 0.04795  -0.09770 -0.00412 189 ASN A OD1 
1459 N ND2 . ASN A 189 ? 0.72556 0.57518 0.38470 0.02316  -0.03080 -0.04256 189 ASN A ND2 
1460 N N   . ARG A 190 ? 0.83271 0.53759 0.43754 0.07178  0.14812  -0.02657 190 ARG A N   
1461 C CA  . ARG A 190 ? 0.88182 0.59615 0.45981 0.08933  0.13891  -0.05296 190 ARG A CA  
1462 C C   . ARG A 190 ? 0.90078 0.61654 0.44790 0.07552  0.11072  -0.04142 190 ARG A C   
1463 O O   . ARG A 190 ? 0.95967 0.63369 0.47009 0.06121  0.10896  0.01794  190 ARG A O   
1464 C CB  . ARG A 190 ? 0.88507 0.63398 0.52290 0.08451  0.12777  -0.06288 190 ARG A CB  
1465 C CG  . ARG A 190 ? 0.89585 0.67370 0.57940 0.03688  0.07710  -0.05482 190 ARG A CG  
1466 C CD  . ARG A 190 ? 0.89927 0.69952 0.62804 0.01806  0.04057  -0.03884 190 ARG A CD  
1467 N NE  . ARG A 190 ? 0.89664 0.71528 0.65717 0.01547  0.01180  -0.02327 190 ARG A NE  
1468 C CZ  . ARG A 190 ? 0.89514 0.72328 0.67830 0.01815  -0.02979 -0.02652 190 ARG A CZ  
1469 N NH1 . ARG A 190 ? 0.89286 0.71931 0.69427 0.03132  -0.03130 -0.01765 190 ARG A NH1 
1470 N NH2 . ARG A 190 ? 0.89181 0.73912 0.68402 0.03559  -0.06525 -0.03809 190 ARG A NH2 
1471 N N   . VAL A 191 ? 0.86518 0.63244 0.43973 0.03353  0.03921  -0.04080 191 VAL A N   
1472 C CA  . VAL A 191 ? 0.85413 0.63712 0.43970 0.03053  -0.02950 -0.04054 191 VAL A CA  
1473 C C   . VAL A 191 ? 0.83446 0.59795 0.37576 0.02581  -0.04902 -0.03663 191 VAL A C   
1474 O O   . VAL A 191 ? 0.90693 0.63162 0.32644 0.07664  -0.09185 -0.04475 191 VAL A O   
1475 C CB  . VAL A 191 ? 0.86221 0.68007 0.51333 0.06511  -0.02801 -0.05117 191 VAL A CB  
1476 C CG1 . VAL A 191 ? 0.85292 0.70542 0.54359 0.10603  -0.03588 -0.05426 191 VAL A CG1 
1477 C CG2 . VAL A 191 ? 0.88537 0.69894 0.56725 0.06190  -0.02595 -0.03098 191 VAL A CG2 
1478 N N   . TYR A 192 ? 0.70611 0.54381 0.37989 -0.02583 -0.07644 -0.03656 192 TYR A N   
1479 C CA  . TYR A 192 ? 0.60896 0.52705 0.39215 -0.06416 -0.06050 -0.07185 192 TYR A CA  
1480 C C   . TYR A 192 ? 0.53214 0.54014 0.38890 -0.02627 -0.07138 -0.08742 192 TYR A C   
1481 O O   . TYR A 192 ? 0.52580 0.55608 0.46905 0.01975  -0.06929 -0.06896 192 TYR A O   
1482 C CB  . TYR A 192 ? 0.63445 0.54757 0.45788 -0.09120 -0.11793 -0.03079 192 TYR A CB  
1483 C CG  . TYR A 192 ? 0.62902 0.57497 0.50382 -0.10979 -0.16908 -0.01818 192 TYR A CG  
1484 C CD1 . TYR A 192 ? 0.63831 0.57854 0.54083 -0.10586 -0.18616 -0.00928 192 TYR A CD1 
1485 C CD2 . TYR A 192 ? 0.62393 0.58804 0.51688 -0.08337 -0.17020 -0.00405 192 TYR A CD2 
1486 C CE1 . TYR A 192 ? 0.62975 0.59306 0.55968 -0.08561 -0.20759 -0.00144 192 TYR A CE1 
1487 C CE2 . TYR A 192 ? 0.62857 0.60967 0.53218 -0.05484 -0.18465 0.00646  192 TYR A CE2 
1488 C CZ  . TYR A 192 ? 0.62747 0.61778 0.56083 -0.05178 -0.20048 0.00892  192 TYR A CZ  
1489 O OH  . TYR A 192 ? 0.64107 0.63990 0.57562 0.00521  -0.20658 0.03326  192 TYR A OH  
1490 N N   . ARG A 193 ? 0.50618 0.51665 0.32097 -0.04734 -0.06601 -0.12842 193 ARG A N   
1491 C CA  . ARG A 193 ? 0.47068 0.49998 0.33256 -0.06367 -0.02573 -0.12744 193 ARG A CA  
1492 C C   . ARG A 193 ? 0.45982 0.48616 0.29956 0.00375  -0.10636 -0.08800 193 ARG A C   
1493 O O   . ARG A 193 ? 0.54529 0.55390 0.31800 0.07630  -0.13851 -0.06811 193 ARG A O   
1494 C CB  . ARG A 193 ? 0.51239 0.54319 0.40817 -0.12088 -0.00323 -0.08133 193 ARG A CB  
1495 C CG  . ARG A 193 ? 0.60071 0.58216 0.47246 -0.12128 0.01445  -0.08329 193 ARG A CG  
1496 C CD  . ARG A 193 ? 0.65668 0.61223 0.55297 -0.10392 0.00729  -0.08422 193 ARG A CD  
1497 N NE  . ARG A 193 ? 0.72013 0.65442 0.62257 -0.09354 0.00832  -0.08253 193 ARG A NE  
1498 C CZ  . ARG A 193 ? 0.77145 0.67635 0.67447 -0.10006 -0.00927 -0.07795 193 ARG A CZ  
1499 N NH1 . ARG A 193 ? 0.78505 0.67963 0.69107 -0.10477 -0.03353 -0.08150 193 ARG A NH1 
1500 N NH2 . ARG A 193 ? 0.77252 0.67463 0.69297 -0.12191 -0.00628 -0.07223 193 ARG A NH2 
1501 N N   . THR A 194 ? 0.39139 0.36549 0.25592 -0.01202 -0.04485 -0.05797 194 THR A N   
1502 C CA  . THR A 194 ? 0.29315 0.38081 0.25342 0.03505  -0.02763 -0.02784 194 THR A CA  
1503 C C   . THR A 194 ? 0.29215 0.31496 0.23197 0.05600  -0.02409 -0.01877 194 THR A C   
1504 O O   . THR A 194 ? 0.35833 0.31540 0.26217 0.05548  0.00006  -0.01115 194 THR A O   
1505 C CB  . THR A 194 ? 0.27753 0.45634 0.28272 0.01481  -0.01987 -0.00730 194 THR A CB  
1506 O OG1 . THR A 194 ? 0.32182 0.47192 0.28016 -0.02444 -0.01048 -0.02192 194 THR A OG1 
1507 C CG2 . THR A 194 ? 0.34633 0.54027 0.33467 -0.02468 -0.00495 -0.03877 194 THR A CG2 
1508 N N   . ILE A 195 ? 0.31389 0.30328 0.21861 -0.00853 -0.01020 -0.02280 195 ILE A N   
1509 C CA  . ILE A 195 ? 0.32392 0.33724 0.21907 0.00370  -0.05087 -0.01129 195 ILE A CA  
1510 C C   . ILE A 195 ? 0.37058 0.36283 0.22251 0.00525  0.00430  0.01738  195 ILE A C   
1511 O O   . ILE A 195 ? 0.39411 0.42674 0.23648 -0.00038 0.01973  0.02310  195 ILE A O   
1512 C CB  . ILE A 195 ? 0.30665 0.35700 0.24438 0.00327  0.00987  -0.00784 195 ILE A CB  
1513 C CG1 . ILE A 195 ? 0.26997 0.39068 0.25918 0.00946  0.06070  -0.00709 195 ILE A CG1 
1514 C CG2 . ILE A 195 ? 0.33632 0.34425 0.21219 -0.02090 0.03564  -0.00748 195 ILE A CG2 
1515 C CD1 . ILE A 195 ? 0.30130 0.42917 0.27320 0.03147  0.01101  -0.01492 195 ILE A CD1 
1516 N N   . GLY A 196 ? 0.40361 0.33169 0.22703 -0.02162 -0.00828 0.02505  196 GLY A N   
1517 C CA  . GLY A 196 ? 0.40285 0.36208 0.23897 -0.03310 -0.02946 0.06440  196 GLY A CA  
1518 C C   . GLY A 196 ? 0.32453 0.37613 0.24317 -0.03906 0.01315  0.01122  196 GLY A C   
1519 O O   . GLY A 196 ? 0.32499 0.43175 0.28701 -0.04553 0.00603  0.01954  196 GLY A O   
1520 N N   . SER A 197 ? 0.22703 0.31485 0.24454 -0.03313 -0.00684 -0.00659 197 SER A N   
1521 C CA  . SER A 197 ? 0.24399 0.36204 0.21518 0.03135  0.00024  -0.02663 197 SER A CA  
1522 C C   . SER A 197 ? 0.25176 0.34273 0.19947 0.01172  0.01264  0.00094  197 SER A C   
1523 O O   . SER A 197 ? 0.31190 0.37060 0.21662 0.02713  -0.00619 -0.01946 197 SER A O   
1524 C CB  . SER A 197 ? 0.25884 0.39800 0.25569 0.01077  0.03737  -0.00633 197 SER A CB  
1525 O OG  . SER A 197 ? 0.31052 0.39879 0.24004 0.02825  0.01675  -0.02792 197 SER A OG  
1526 N N   . PRO A 198 ? 0.25695 0.30983 0.19870 0.01170  0.01284  0.00364  198 PRO A N   
1527 C CA  . PRO A 198 ? 0.27585 0.28864 0.20003 -0.00139 0.01285  -0.00280 198 PRO A CA  
1528 C C   . PRO A 198 ? 0.27134 0.34112 0.22254 0.01499  -0.02158 0.01585  198 PRO A C   
1529 O O   . PRO A 198 ? 0.27390 0.35876 0.23143 0.03262  -0.02529 -0.00133 198 PRO A O   
1530 C CB  . PRO A 198 ? 0.34294 0.32966 0.22069 0.04256  -0.01095 0.01679  198 PRO A CB  
1531 C CG  . PRO A 198 ? 0.34932 0.31499 0.22440 0.06630  0.03108  0.02685  198 PRO A CG  
1532 C CD  . PRO A 198 ? 0.31242 0.37773 0.17249 0.02050  -0.00111 0.00904  198 PRO A CD  
1533 N N   . LEU A 199 ? 0.30857 0.31444 0.21693 0.02509  -0.02411 0.01704  199 LEU A N   
1534 C CA  . LEU A 199 ? 0.29417 0.29340 0.20158 0.02512  -0.02708 0.00065  199 LEU A CA  
1535 C C   . LEU A 199 ? 0.26752 0.28415 0.25237 -0.01316 -0.00956 -0.00720 199 LEU A C   
1536 O O   . LEU A 199 ? 0.25457 0.28872 0.26971 0.00260  0.02634  -0.02129 199 LEU A O   
1537 C CB  . LEU A 199 ? 0.31488 0.33234 0.17808 -0.00815 -0.03234 -0.01857 199 LEU A CB  
1538 C CG  . LEU A 199 ? 0.24171 0.37969 0.20357 0.03966  -0.00592 -0.03002 199 LEU A CG  
1539 C CD1 . LEU A 199 ? 0.30677 0.39191 0.26233 0.04856  -0.05316 -0.00665 199 LEU A CD1 
1540 C CD2 . LEU A 199 ? 0.22949 0.37969 0.22274 0.01191  0.03333  -0.01561 199 LEU A CD2 
1541 N N   . VAL A 200 ? 0.27681 0.28074 0.25056 0.01994  -0.00787 -0.01336 200 VAL A N   
1542 C CA  . VAL A 200 ? 0.29813 0.28957 0.24929 0.01434  0.03217  -0.03921 200 VAL A CA  
1543 C C   . VAL A 200 ? 0.27872 0.30402 0.27413 0.04428  0.00068  0.00252  200 VAL A C   
1544 O O   . VAL A 200 ? 0.27867 0.33080 0.28568 0.02913  0.01497  0.02934  200 VAL A O   
1545 C CB  . VAL A 200 ? 0.27806 0.31138 0.25914 0.01617  -0.02041 -0.01288 200 VAL A CB  
1546 C CG1 . VAL A 200 ? 0.30504 0.33390 0.27652 -0.04662 -0.04479 -0.02864 200 VAL A CG1 
1547 C CG2 . VAL A 200 ? 0.30271 0.32324 0.26863 -0.00542 0.01495  0.02809  200 VAL A CG2 
1548 N N   . PHE A 201 ? 0.28707 0.29334 0.26961 0.05926  0.00636  0.03481  201 PHE A N   
1549 C CA  . PHE A 201 ? 0.31670 0.30998 0.27110 0.07819  0.00078  0.01691  201 PHE A CA  
1550 C C   . PHE A 201 ? 0.32571 0.36648 0.26262 0.04822  0.01133  0.01220  201 PHE A C   
1551 O O   . PHE A 201 ? 0.37059 0.40109 0.25737 0.02365  0.01183  0.00040  201 PHE A O   
1552 C CB  . PHE A 201 ? 0.33041 0.30064 0.25508 0.05657  0.00566  -0.03271 201 PHE A CB  
1553 C CG  . PHE A 201 ? 0.29036 0.34659 0.26068 0.06699  0.02050  -0.01790 201 PHE A CG  
1554 C CD1 . PHE A 201 ? 0.29488 0.39923 0.21992 0.05532  -0.01182 0.02334  201 PHE A CD1 
1555 C CD2 . PHE A 201 ? 0.30055 0.37715 0.28604 0.06928  0.03233  0.00958  201 PHE A CD2 
1556 C CE1 . PHE A 201 ? 0.31777 0.36981 0.23951 0.01886  0.00094  0.04212  201 PHE A CE1 
1557 C CE2 . PHE A 201 ? 0.28241 0.36137 0.26754 0.04019  0.00839  0.00594  201 PHE A CE2 
1558 C CZ  . PHE A 201 ? 0.29567 0.35678 0.26008 -0.00951 -0.00461 0.04353  201 PHE A CZ  
1559 N N   . PRO A 202 ? 0.37425 0.32830 0.27260 0.01446  0.00652  0.02070  202 PRO A N   
1560 C CA  . PRO A 202 ? 0.37552 0.35527 0.29613 0.02800  0.02312  0.02100  202 PRO A CA  
1561 C C   . PRO A 202 ? 0.43977 0.35623 0.30681 0.01251  0.00279  0.01893  202 PRO A C   
1562 O O   . PRO A 202 ? 0.42264 0.31417 0.29506 0.05497  0.00857  0.02973  202 PRO A O   
1563 C CB  . PRO A 202 ? 0.36820 0.36106 0.29658 -0.00461 0.04302  0.00043  202 PRO A CB  
1564 C CG  . PRO A 202 ? 0.41946 0.31858 0.29379 -0.00122 0.06211  0.00239  202 PRO A CG  
1565 C CD  . PRO A 202 ? 0.40271 0.28892 0.27295 0.00947  0.04925  0.01968  202 PRO A CD  
1566 N N   . LYS A 203 ? 0.49080 0.36814 0.35858 0.03076  -0.02143 -0.00524 203 LYS A N   
1567 C CA  . LYS A 203 ? 0.49700 0.38337 0.38633 0.05742  -0.04213 -0.03199 203 LYS A CA  
1568 C C   . LYS A 203 ? 0.43484 0.35030 0.38647 0.06035  -0.02146 0.02206  203 LYS A C   
1569 O O   . LYS A 203 ? 0.39746 0.34671 0.38509 -0.00469 0.00208  0.04547  203 LYS A O   
1570 C CB  . LYS A 203 ? 0.60372 0.45284 0.43971 0.04832  -0.03090 -0.04107 203 LYS A CB  
1571 C CG  . LYS A 203 ? 0.69274 0.48863 0.45644 0.00239  0.02378  -0.03732 203 LYS A CG  
1572 C CD  . LYS A 203 ? 0.72943 0.50356 0.46527 -0.03586 0.03615  -0.05807 203 LYS A CD  
1573 C CE  . LYS A 203 ? 0.77601 0.54045 0.48759 -0.03275 0.06566  -0.04011 203 LYS A CE  
1574 N NZ  . LYS A 203 ? 0.80300 0.54706 0.48307 -0.04243 0.09414  -0.04143 203 LYS A NZ  
1575 N N   . HIS A 204 ? 0.45278 0.31261 0.38982 0.11020  -0.03960 0.03514  204 HIS A N   
1576 C CA  . HIS A 204 ? 0.47835 0.36137 0.37618 0.09128  -0.05457 0.01390  204 HIS A CA  
1577 C C   . HIS A 204 ? 0.45328 0.36038 0.34006 0.11754  -0.07083 0.02645  204 HIS A C   
1578 O O   . HIS A 204 ? 0.55684 0.42374 0.34557 0.12666  -0.05544 0.06350  204 HIS A O   
1579 C CB  . HIS A 204 ? 0.51852 0.38530 0.41664 0.07029  -0.06914 0.01161  204 HIS A CB  
1580 C CG  . HIS A 204 ? 0.57156 0.40157 0.46347 0.07376  -0.03900 -0.01487 204 HIS A CG  
1581 N ND1 . HIS A 204 ? 0.62704 0.40565 0.49753 0.09862  -0.05445 -0.02488 204 HIS A ND1 
1582 C CD2 . HIS A 204 ? 0.62143 0.43832 0.48255 0.08754  -0.04293 -0.04239 204 HIS A CD2 
1583 C CE1 . HIS A 204 ? 0.64451 0.43029 0.48670 0.08873  -0.07030 -0.05703 204 HIS A CE1 
1584 N NE2 . HIS A 204 ? 0.66676 0.44082 0.48147 0.09902  -0.05190 -0.06461 204 HIS A NE2 
1585 N N   . HIS A 205 ? 0.40950 0.32916 0.30290 0.06077  -0.03540 0.00204  205 HIS A N   
1586 C CA  . HIS A 205 ? 0.33719 0.38159 0.30681 0.03725  -0.01093 0.00385  205 HIS A CA  
1587 C C   . HIS A 205 ? 0.32560 0.41963 0.29987 0.02851  0.00399  0.04675  205 HIS A C   
1588 O O   . HIS A 205 ? 0.34608 0.50110 0.30704 0.04962  0.02052  0.06490  205 HIS A O   
1589 C CB  . HIS A 205 ? 0.31859 0.41748 0.27119 0.03102  -0.01325 -0.00465 205 HIS A CB  
1590 C CG  . HIS A 205 ? 0.30927 0.40308 0.29199 0.02012  0.00088  0.00734  205 HIS A CG  
1591 N ND1 . HIS A 205 ? 0.32203 0.38738 0.31519 0.05184  -0.00916 0.03900  205 HIS A ND1 
1592 C CD2 . HIS A 205 ? 0.35665 0.40182 0.35470 0.02102  0.05127  0.02518  205 HIS A CD2 
1593 C CE1 . HIS A 205 ? 0.40399 0.40165 0.36282 0.07067  0.02809  0.01457  205 HIS A CE1 
1594 N NE2 . HIS A 205 ? 0.40852 0.42166 0.37612 0.06339  0.04787  0.05675  205 HIS A NE2 
1595 N N   . VAL A 206 ? 0.31353 0.37755 0.28850 0.03491  -0.02866 0.00776  206 VAL A N   
1596 C CA  . VAL A 206 ? 0.30723 0.40453 0.30784 0.02579  -0.01884 0.00096  206 VAL A CA  
1597 C C   . VAL A 206 ? 0.30169 0.37881 0.28893 0.03135  0.01460  0.01764  206 VAL A C   
1598 O O   . VAL A 206 ? 0.38999 0.44946 0.30118 0.04039  -0.00018 -0.01875 206 VAL A O   
1599 C CB  . VAL A 206 ? 0.39057 0.45437 0.35392 0.02543  -0.01307 0.02222  206 VAL A CB  
1600 C CG1 . VAL A 206 ? 0.34199 0.51642 0.39059 0.00568  -0.01077 0.05163  206 VAL A CG1 
1601 C CG2 . VAL A 206 ? 0.43868 0.45233 0.33685 0.04552  -0.03800 -0.05515 206 VAL A CG2 
1602 N N   . VAL A 207 ? 0.29792 0.34089 0.26979 0.00306  0.02773  0.01206  207 VAL A N   
1603 C CA  . VAL A 207 ? 0.28604 0.38737 0.25277 0.06131  -0.04692 0.01864  207 VAL A CA  
1604 C C   . VAL A 207 ? 0.29669 0.40537 0.25015 0.05693  -0.03822 -0.00066 207 VAL A C   
1605 O O   . VAL A 207 ? 0.37436 0.41420 0.25949 0.04422  0.01918  -0.01242 207 VAL A O   
1606 C CB  . VAL A 207 ? 0.30511 0.42431 0.25847 0.08754  -0.03892 0.01326  207 VAL A CB  
1607 C CG1 . VAL A 207 ? 0.38911 0.46359 0.26718 0.10594  0.02630  0.01291  207 VAL A CG1 
1608 C CG2 . VAL A 207 ? 0.27528 0.50574 0.28664 0.03665  -0.02317 -0.01861 207 VAL A CG2 
1609 N N   . SER A 208 ? 0.32954 0.35463 0.29777 0.06633  -0.04353 0.01484  208 SER A N   
1610 C CA  . SER A 208 ? 0.30536 0.36011 0.34327 0.05374  -0.05817 0.02785  208 SER A CA  
1611 C C   . SER A 208 ? 0.32493 0.36204 0.40507 0.03980  0.00710  0.02724  208 SER A C   
1612 O O   . SER A 208 ? 0.31017 0.36737 0.41994 0.00495  0.01575  0.00416  208 SER A O   
1613 C CB  . SER A 208 ? 0.30574 0.46484 0.40307 0.05948  -0.13311 0.03954  208 SER A CB  
1614 O OG  . SER A 208 ? 0.38854 0.54231 0.46617 0.03932  -0.10727 0.08341  208 SER A OG  
1615 N N   . LEU A 209 ? 0.31812 0.36597 0.42746 0.05012  0.04586  0.06134  209 LEU A N   
1616 C CA  . LEU A 209 ? 0.36243 0.42634 0.49789 0.03973  0.04462  0.04604  209 LEU A CA  
1617 C C   . LEU A 209 ? 0.31926 0.42460 0.59660 0.04081  0.02955  0.02051  209 LEU A C   
1618 O O   . LEU A 209 ? 0.32942 0.43368 0.66027 0.05694  0.04185  0.02119  209 LEU A O   
1619 C CB  . LEU A 209 ? 0.36200 0.46369 0.46990 0.05531  0.10466  0.08908  209 LEU A CB  
1620 C CG  . LEU A 209 ? 0.42017 0.45247 0.41420 0.08053  0.10966  0.08430  209 LEU A CG  
1621 C CD1 . LEU A 209 ? 0.47256 0.41114 0.43398 0.05970  0.17138  0.07144  209 LEU A CD1 
1622 C CD2 . LEU A 209 ? 0.43864 0.45413 0.37746 0.08887  0.06299  0.07742  209 LEU A CD2 
1623 N N   . GLN A 210 ? 0.32962 0.44736 0.59946 -0.00254 -0.04515 -0.02736 210 GLN A N   
1624 C CA  . GLN A 210 ? 0.33601 0.47823 0.62404 0.02715  -0.09445 -0.08996 210 GLN A CA  
1625 C C   . GLN A 210 ? 0.31588 0.48838 0.62687 0.06983  -0.07045 -0.10491 210 GLN A C   
1626 O O   . GLN A 210 ? 0.36281 0.45853 0.58989 0.04342  -0.11149 -0.15567 210 GLN A O   
1627 C CB  . GLN A 210 ? 0.45202 0.54975 0.62288 0.04565  -0.11066 -0.09102 210 GLN A CB  
1628 C CG  . GLN A 210 ? 0.51785 0.59554 0.60468 0.07899  -0.09312 -0.10382 210 GLN A CG  
1629 C CD  . GLN A 210 ? 0.55711 0.67385 0.59501 0.10179  -0.08948 -0.10013 210 GLN A CD  
1630 O OE1 . GLN A 210 ? 0.55086 0.70413 0.57436 0.12561  -0.07958 -0.13601 210 GLN A OE1 
1631 N NE2 . GLN A 210 ? 0.59886 0.72316 0.58896 0.11150  -0.09654 -0.04329 210 GLN A NE2 
1632 N N   . PRO A 211 ? 0.42251 0.53064 0.63015 0.05487  -0.03884 -0.09001 211 PRO A N   
1633 C CA  . PRO A 211 ? 0.50345 0.53013 0.60303 0.06011  -0.04750 -0.10946 211 PRO A CA  
1634 C C   . PRO A 211 ? 0.61721 0.57224 0.58234 0.06426  -0.09361 -0.07092 211 PRO A C   
1635 O O   . PRO A 211 ? 0.65118 0.56480 0.55546 0.09907  -0.08322 -0.05249 211 PRO A O   
1636 C CB  . PRO A 211 ? 0.49376 0.51521 0.63905 0.05791  -0.02681 -0.10710 211 PRO A CB  
1637 C CG  . PRO A 211 ? 0.50682 0.51387 0.66601 0.04146  0.00788  -0.10019 211 PRO A CG  
1638 C CD  . PRO A 211 ? 0.43871 0.53665 0.65507 0.06406  0.01769  -0.08525 211 PRO A CD  
1639 N N   . VAL A 212 ? 0.65033 0.60032 0.58208 0.03514  -0.14536 -0.04137 212 VAL A N   
1640 C CA  . VAL A 212 ? 0.66126 0.61129 0.61284 0.01000  -0.15143 -0.06812 212 VAL A CA  
1641 C C   . VAL A 212 ? 0.70838 0.67350 0.65556 -0.02987 -0.15134 -0.03509 212 VAL A C   
1642 O O   . VAL A 212 ? 0.73532 0.68266 0.67140 -0.05154 -0.14205 -0.02000 212 VAL A O   
1643 C CB  . VAL A 212 ? 0.62712 0.59313 0.58296 0.03872  -0.19482 -0.09195 212 VAL A CB  
1644 C CG1 . VAL A 212 ? 0.64757 0.63832 0.58544 0.02643  -0.17604 -0.09442 212 VAL A CG1 
1645 C CG2 . VAL A 212 ? 0.64838 0.55399 0.56225 0.08981  -0.17162 -0.08966 212 VAL A CG2 
1646 N N   . ASN A 213 ? 0.71696 0.70802 0.68667 -0.03751 -0.12931 -0.01036 213 ASN A N   
1647 C CA  . ASN A 213 ? 0.72431 0.74595 0.73214 -0.05052 -0.11375 -0.00104 213 ASN A CA  
1648 C C   . ASN A 213 ? 0.73530 0.76377 0.75073 -0.03656 -0.09352 -0.01222 213 ASN A C   
1649 O O   . ASN A 213 ? 0.78043 0.77439 0.76314 -0.04191 -0.08299 -0.01230 213 ASN A O   
1650 C CB  . ASN A 213 ? 0.74256 0.76535 0.76355 -0.06347 -0.11229 0.01935  213 ASN A CB  
1651 C CG  . ASN A 213 ? 0.80586 0.79126 0.79496 -0.07192 -0.12877 0.03581  213 ASN A CG  
1652 O OD1 . ASN A 213 ? 0.84278 0.81108 0.81943 -0.07602 -0.12249 0.04684  213 ASN A OD1 
1653 N ND2 . ASN A 213 ? 0.82219 0.80001 0.80479 -0.08606 -0.14095 0.05022  213 ASN A ND2 
1654 N N   . ASP A 214 ? 0.74829 0.78012 0.76574 -0.03391 -0.06599 -0.01214 214 ASP A N   
1655 C CA  . ASP A 214 ? 0.76088 0.79259 0.78592 -0.00489 -0.04213 -0.02244 214 ASP A CA  
1656 C C   . ASP A 214 ? 0.74788 0.78868 0.77360 -0.01930 -0.03975 -0.02741 214 ASP A C   
1657 O O   . ASP A 214 ? 0.73905 0.78775 0.79284 -0.04009 -0.03949 -0.02628 214 ASP A O   
1658 C CB  . ASP A 214 ? 0.77521 0.80410 0.80512 0.03350  -0.03427 -0.00347 214 ASP A CB  
1659 C CG  . ASP A 214 ? 0.79454 0.83185 0.83567 0.04586  -0.02159 0.01957  214 ASP A CG  
1660 O OD1 . ASP A 214 ? 0.80503 0.84105 0.85508 0.04334  -0.00925 0.03102  214 ASP A OD1 
1661 O OD2 . ASP A 214 ? 0.80695 0.84220 0.83556 0.07357  -0.01480 0.02016  214 ASP A OD2 
1662 N N   . LYS A 215 ? 0.72872 0.78168 0.72858 0.00796  -0.04616 -0.03337 215 LYS A N   
1663 C CA  . LYS A 215 ? 0.71399 0.78193 0.69298 0.03145  -0.06438 -0.03118 215 LYS A CA  
1664 C C   . LYS A 215 ? 0.65681 0.75833 0.63374 0.03267  -0.11815 -0.05155 215 LYS A C   
1665 O O   . LYS A 215 ? 0.65746 0.75725 0.62172 0.07340  -0.12210 -0.05070 215 LYS A O   
1666 C CB  . LYS A 215 ? 0.78612 0.81573 0.71083 0.02462  -0.01549 -0.03983 215 LYS A CB  
1667 C CG  . LYS A 215 ? 0.83446 0.84011 0.72839 0.00498  0.02741  -0.06045 215 LYS A CG  
1668 C CD  . LYS A 215 ? 0.85131 0.85022 0.74249 -0.01679 0.06589  -0.07164 215 LYS A CD  
1669 C CE  . LYS A 215 ? 0.86463 0.85741 0.75341 -0.04015 0.08364  -0.07096 215 LYS A CE  
1670 N NZ  . LYS A 215 ? 0.87612 0.86252 0.76452 -0.05599 0.08699  -0.07038 215 LYS A NZ  
1671 N N   . ASP A 216 ? 0.63772 0.76367 0.59954 -0.00206 -0.15537 -0.05215 216 ASP A N   
1672 C CA  . ASP A 216 ? 0.61509 0.77929 0.60167 -0.00414 -0.17567 -0.05006 216 ASP A CA  
1673 C C   . ASP A 216 ? 0.58109 0.77798 0.53628 0.00797  -0.15652 -0.07818 216 ASP A C   
1674 O O   . ASP A 216 ? 0.62106 0.79407 0.52624 0.01809  -0.14633 -0.07782 216 ASP A O   
1675 C CB  . ASP A 216 ? 0.60692 0.79631 0.65619 0.01065  -0.20067 -0.02043 216 ASP A CB  
1676 C CG  . ASP A 216 ? 0.61823 0.80921 0.71631 0.00823  -0.22855 0.00455  216 ASP A CG  
1677 O OD1 . ASP A 216 ? 0.57890 0.81958 0.72718 0.04866  -0.26346 0.03944  216 ASP A OD1 
1678 O OD2 . ASP A 216 ? 0.63412 0.82085 0.73988 -0.01332 -0.23056 0.00263  216 ASP A OD2 
1679 N N   . PHE A 217 ? 0.49577 0.77433 0.49536 0.00841  -0.11898 -0.09254 217 PHE A N   
1680 C CA  . PHE A 217 ? 0.44292 0.76171 0.43520 -0.02626 -0.08578 -0.07889 217 PHE A CA  
1681 C C   . PHE A 217 ? 0.33011 0.74486 0.43039 -0.01890 -0.05760 -0.04464 217 PHE A C   
1682 O O   . PHE A 217 ? 0.29334 0.84915 0.44243 -0.03160 -0.03883 -0.03272 217 PHE A O   
1683 C CB  . PHE A 217 ? 0.41808 0.74590 0.41442 -0.02981 0.00674  -0.05605 217 PHE A CB  
1684 C CG  . PHE A 217 ? 0.50290 0.73882 0.44339 -0.01903 -0.01551 -0.02389 217 PHE A CG  
1685 C CD1 . PHE A 217 ? 0.49209 0.71978 0.42997 -0.00101 -0.03710 -0.00104 217 PHE A CD1 
1686 C CD2 . PHE A 217 ? 0.49847 0.72780 0.45804 0.00343  -0.03258 -0.02265 217 PHE A CD2 
1687 C CE1 . PHE A 217 ? 0.53219 0.70736 0.43544 0.04537  -0.03864 -0.00471 217 PHE A CE1 
1688 C CE2 . PHE A 217 ? 0.50303 0.70815 0.44233 0.00121  -0.04597 -0.02095 217 PHE A CE2 
1689 C CZ  . PHE A 217 ? 0.50743 0.68958 0.42158 0.05622  -0.09659 0.00067  217 PHE A CZ  
1690 N N   . GLN A 218 ? 0.31654 0.59885 0.42313 -0.04325 -0.02936 -0.01354 218 GLN A N   
1691 C CA  . GLN A 218 ? 0.30929 0.57211 0.41470 -0.03322 -0.02067 -0.03197 218 GLN A CA  
1692 C C   . GLN A 218 ? 0.26779 0.52160 0.35672 -0.02422 -0.02062 -0.06160 218 GLN A C   
1693 O O   . GLN A 218 ? 0.31871 0.51599 0.34708 -0.04806 -0.02219 -0.07186 218 GLN A O   
1694 C CB  . GLN A 218 ? 0.43958 0.65304 0.48586 0.00555  0.00703  -0.03077 218 GLN A CB  
1695 C CG  . GLN A 218 ? 0.46826 0.69913 0.53157 -0.03793 0.00365  -0.08204 218 GLN A CG  
1696 C CD  . GLN A 218 ? 0.48397 0.69760 0.55140 -0.11212 0.00669  -0.11158 218 GLN A CD  
1697 O OE1 . GLN A 218 ? 0.54487 0.69676 0.56990 -0.09184 0.02463  -0.14159 218 GLN A OE1 
1698 N NE2 . GLN A 218 ? 0.45787 0.68145 0.54416 -0.16562 0.02148  -0.10309 218 GLN A NE2 
1699 N N   . ILE A 219 ? 0.24123 0.52751 0.35825 0.00291  -0.02071 -0.06890 219 ILE A N   
1700 C CA  . ILE A 219 ? 0.25517 0.58126 0.33963 0.00459  -0.02924 -0.08276 219 ILE A CA  
1701 C C   . ILE A 219 ? 0.30032 0.64655 0.35123 -0.01916 0.00227  -0.11106 219 ILE A C   
1702 O O   . ILE A 219 ? 0.24687 0.70033 0.39445 -0.03834 0.00850  -0.14239 219 ILE A O   
1703 C CB  . ILE A 219 ? 0.29440 0.56974 0.35382 0.00002  -0.05375 -0.09486 219 ILE A CB  
1704 C CG1 . ILE A 219 ? 0.33439 0.58286 0.31481 0.04423  -0.09219 -0.04506 219 ILE A CG1 
1705 C CG2 . ILE A 219 ? 0.35343 0.58075 0.39164 -0.01697 -0.06064 -0.07332 219 ILE A CG2 
1706 C CD1 . ILE A 219 ? 0.35560 0.56855 0.32138 0.05180  -0.06357 -0.01773 219 ILE A CD1 
1707 N N   . SER A 220 ? 0.30843 0.65634 0.30258 0.01241  -0.00637 -0.06983 220 SER A N   
1708 C CA  . SER A 220 ? 0.28134 0.70551 0.32941 -0.01015 -0.02232 -0.06236 220 SER A CA  
1709 C C   . SER A 220 ? 0.27919 0.65586 0.32972 0.01602  0.01285  -0.08654 220 SER A C   
1710 O O   . SER A 220 ? 0.31207 0.67435 0.34510 0.02019  0.04106  -0.04272 220 SER A O   
1711 C CB  . SER A 220 ? 0.26991 0.79728 0.37396 -0.00061 -0.01000 -0.02007 220 SER A CB  
1712 O OG  . SER A 220 ? 0.29291 0.84429 0.35910 -0.02929 0.02573  -0.03868 220 SER A OG  
1713 N N   . VAL A 221 ? 0.27186 0.59364 0.30024 0.02324  0.02106  -0.11560 221 VAL A N   
1714 C CA  . VAL A 221 ? 0.31450 0.56925 0.30540 0.00435  0.00654  -0.08638 221 VAL A CA  
1715 C C   . VAL A 221 ? 0.27522 0.57897 0.31154 -0.00476 0.05924  -0.09101 221 VAL A C   
1716 O O   . VAL A 221 ? 0.29880 0.60620 0.32629 -0.00944 0.07353  -0.10948 221 VAL A O   
1717 C CB  . VAL A 221 ? 0.38257 0.58381 0.34585 0.00389  -0.01987 -0.07967 221 VAL A CB  
1718 C CG1 . VAL A 221 ? 0.35726 0.58421 0.39449 -0.04143 -0.00577 -0.06149 221 VAL A CG1 
1719 C CG2 . VAL A 221 ? 0.41407 0.57911 0.32979 0.04950  0.01317  -0.07471 221 VAL A CG2 
1720 N N   . ASP A 222 ? 0.27458 0.52448 0.30584 0.02091  0.02091  -0.09589 222 ASP A N   
1721 C CA  . ASP A 222 ? 0.31932 0.52718 0.34238 0.00528  0.06964  -0.08479 222 ASP A CA  
1722 C C   . ASP A 222 ? 0.34757 0.53774 0.38158 0.02733  0.13972  -0.06834 222 ASP A C   
1723 O O   . ASP A 222 ? 0.46581 0.46752 0.43116 0.02750  0.04299  -0.09212 222 ASP A O   
1724 C CB  . ASP A 222 ? 0.32925 0.52475 0.35109 0.04406  0.07351  -0.08330 222 ASP A CB  
1725 C CG  . ASP A 222 ? 0.29138 0.50454 0.29354 0.06649  0.07607  -0.03424 222 ASP A CG  
1726 O OD1 . ASP A 222 ? 0.29390 0.50458 0.26256 0.11161  -0.00588 -0.03992 222 ASP A OD1 
1727 O OD2 . ASP A 222 ? 0.31229 0.53036 0.28653 0.04733  0.02214  -0.03381 222 ASP A OD2 
1728 N N   . HIS A 223 ? 0.32323 0.55243 0.48884 -0.07653 0.10199  -0.01669 223 HIS A N   
1729 C CA  . HIS A 223 ? 0.48342 0.61523 0.56994 -0.12953 0.06221  -0.00059 223 HIS A CA  
1730 C C   . HIS A 223 ? 0.48562 0.63266 0.60416 -0.10428 0.04342  -0.02678 223 HIS A C   
1731 O O   . HIS A 223 ? 0.50204 0.65923 0.67325 -0.09744 0.01521  -0.03293 223 HIS A O   
1732 C CB  . HIS A 223 ? 0.58999 0.62672 0.61688 -0.12752 0.03272  0.01290  223 HIS A CB  
1733 C CG  . HIS A 223 ? 0.67821 0.63872 0.64896 -0.12800 0.02146  -0.02994 223 HIS A CG  
1734 N ND1 . HIS A 223 ? 0.71554 0.63577 0.64974 -0.12715 0.00919  -0.07250 223 HIS A ND1 
1735 C CD2 . HIS A 223 ? 0.73737 0.64625 0.65750 -0.11149 0.01396  -0.05485 223 HIS A CD2 
1736 C CE1 . HIS A 223 ? 0.72401 0.62044 0.65311 -0.15312 -0.00082 -0.08595 223 HIS A CE1 
1737 N NE2 . HIS A 223 ? 0.74323 0.62667 0.65776 -0.14270 -0.00571 -0.07813 223 HIS A NE2 
1738 N N   . LEU A 224 ? 0.48432 0.65464 0.51582 -0.09606 0.06450  -0.06217 224 LEU A N   
1739 C CA  . LEU A 224 ? 0.49899 0.66092 0.46222 -0.08489 0.06199  -0.11388 224 LEU A CA  
1740 C C   . LEU A 224 ? 0.56303 0.69754 0.44160 -0.13720 0.06582  -0.14148 224 LEU A C   
1741 O O   . LEU A 224 ? 0.64784 0.71017 0.47913 -0.16016 0.09392  -0.16559 224 LEU A O   
1742 C CB  . LEU A 224 ? 0.54433 0.63340 0.49062 -0.03351 0.03259  -0.09448 224 LEU A CB  
1743 C CG  . LEU A 224 ? 0.60468 0.63188 0.55837 -0.04575 0.01073  -0.06240 224 LEU A CG  
1744 C CD1 . LEU A 224 ? 0.61445 0.61352 0.59323 -0.03952 -0.00297 -0.01491 224 LEU A CD1 
1745 C CD2 . LEU A 224 ? 0.59455 0.63801 0.58211 -0.07619 0.01877  -0.07276 224 LEU A CD2 
1746 N N   . SER A 225 ? 0.49738 0.73868 0.43937 -0.12278 0.10686  -0.12786 225 SER A N   
1747 C CA  . SER A 225 ? 0.54837 0.78634 0.49390 -0.05228 0.04030  -0.14251 225 SER A CA  
1748 C C   . SER A 225 ? 0.51181 0.83443 0.52373 -0.05594 0.02228  -0.13315 225 SER A C   
1749 O O   . SER A 225 ? 0.52175 0.86040 0.51808 -0.07894 0.03487  -0.13949 225 SER A O   
1750 C CB  . SER A 225 ? 0.63473 0.77806 0.52424 -0.02364 0.02518  -0.14459 225 SER A CB  
1751 O OG  . SER A 225 ? 0.64271 0.79380 0.56780 0.02670  0.03696  -0.12834 225 SER A OG  
1752 N N   . ILE A 226 ? 0.49838 0.83499 0.57758 -0.02351 -0.02123 -0.13528 226 ILE A N   
1753 C CA  . ILE A 226 ? 0.56710 0.81390 0.60226 -0.03545 -0.04346 -0.15356 226 ILE A CA  
1754 C C   . ILE A 226 ? 0.52594 0.82638 0.62608 -0.07426 -0.06865 -0.15752 226 ILE A C   
1755 O O   . ILE A 226 ? 0.44118 0.82717 0.62105 -0.07111 -0.06109 -0.16144 226 ILE A O   
1756 C CB  . ILE A 226 ? 0.65254 0.79755 0.62943 -0.00412 0.00763  -0.13929 226 ILE A CB  
1757 C CG1 . ILE A 226 ? 0.68624 0.77031 0.65135 -0.00662 0.05484  -0.14965 226 ILE A CG1 
1758 C CG2 . ILE A 226 ? 0.66118 0.80200 0.62823 0.03900  0.02446  -0.12162 226 ILE A CG2 
1759 C CD1 . ILE A 226 ? 0.70537 0.73896 0.64152 0.01016  0.06854  -0.16362 226 ILE A CD1 
1760 N N   . LEU A 227 ? 0.52035 0.81793 0.63158 -0.10338 -0.09816 -0.15910 227 LEU A N   
1761 C CA  . LEU A 227 ? 0.56631 0.79068 0.64679 -0.08373 -0.08030 -0.12863 227 LEU A CA  
1762 C C   . LEU A 227 ? 0.58958 0.80863 0.65915 -0.01876 -0.07196 -0.08721 227 LEU A C   
1763 O O   . LEU A 227 ? 0.57980 0.84137 0.64239 0.02089  -0.06505 -0.07174 227 LEU A O   
1764 C CB  . LEU A 227 ? 0.58650 0.76479 0.66914 -0.11702 -0.06111 -0.13430 227 LEU A CB  
1765 C CG  . LEU A 227 ? 0.60243 0.73936 0.68746 -0.14323 -0.03042 -0.13494 227 LEU A CG  
1766 C CD1 . LEU A 227 ? 0.57873 0.73773 0.70261 -0.13177 -0.00843 -0.11092 227 LEU A CD1 
1767 C CD2 . LEU A 227 ? 0.60401 0.71263 0.70325 -0.18739 -0.03798 -0.15131 227 LEU A CD2 
1768 N N   . HIS A 228 ? 0.55658 0.78724 0.68726 -0.03291 -0.06625 -0.06237 228 HIS A N   
1769 C CA  . HIS A 228 ? 0.56775 0.77888 0.72521 -0.04808 -0.06187 -0.04694 228 HIS A CA  
1770 C C   . HIS A 228 ? 0.51367 0.77021 0.73235 -0.03234 -0.10180 -0.02508 228 HIS A C   
1771 O O   . HIS A 228 ? 0.44718 0.74146 0.72789 -0.01618 -0.09353 -0.03376 228 HIS A O   
1772 C CB  . HIS A 228 ? 0.59201 0.77458 0.75646 -0.05132 -0.06453 -0.04005 228 HIS A CB  
1773 C CG  . HIS A 228 ? 0.59335 0.78005 0.77693 -0.01233 -0.07075 -0.03485 228 HIS A CG  
1774 N ND1 . HIS A 228 ? 0.61152 0.79701 0.80863 0.02450  -0.07467 -0.01387 228 HIS A ND1 
1775 C CD2 . HIS A 228 ? 0.58076 0.77577 0.79051 0.02721  -0.06088 -0.03217 228 HIS A CD2 
1776 C CE1 . HIS A 228 ? 0.60769 0.80316 0.81376 0.05168  -0.05998 -0.01090 228 HIS A CE1 
1777 N NE2 . HIS A 228 ? 0.59535 0.79518 0.81537 0.06489  -0.04542 -0.00720 228 HIS A NE2 
1778 N N   . ARG A 229 ? 0.52047 0.77791 0.74763 -0.01198 -0.08421 -0.00618 229 ARG A N   
1779 C CA  . ARG A 229 ? 0.50008 0.76845 0.73891 -0.06093 -0.09927 0.02416  229 ARG A CA  
1780 C C   . ARG A 229 ? 0.43598 0.76174 0.74364 -0.07073 -0.10167 0.06772  229 ARG A C   
1781 O O   . ARG A 229 ? 0.34754 0.76336 0.73712 -0.07147 -0.08705 0.11367  229 ARG A O   
1782 C CB  . ARG A 229 ? 0.57607 0.78098 0.74297 -0.06896 -0.09408 -0.00002 229 ARG A CB  
1783 C CG  . ARG A 229 ? 0.62867 0.77797 0.75173 -0.06772 -0.07293 -0.01487 229 ARG A CG  
1784 C CD  . ARG A 229 ? 0.70157 0.79403 0.76533 -0.05373 -0.03867 -0.01800 229 ARG A CD  
1785 N NE  . ARG A 229 ? 0.76887 0.82555 0.78369 -0.02041 -0.00281 -0.02064 229 ARG A NE  
1786 C CZ  . ARG A 229 ? 0.81557 0.84326 0.79535 -0.00722 0.01746  -0.02412 229 ARG A CZ  
1787 N NH1 . ARG A 229 ? 0.84044 0.85323 0.80516 -0.01719 0.00618  -0.02584 229 ARG A NH1 
1788 N NH2 . ARG A 229 ? 0.82636 0.84832 0.79928 0.00479  0.03459  -0.02485 229 ARG A NH2 
1789 N N   . ASP A 230 ? 0.45528 0.75847 0.75063 -0.03724 -0.15251 0.09344  230 ASP A N   
1790 C CA  . ASP A 230 ? 0.52117 0.73435 0.76148 -0.03134 -0.15788 0.10737  230 ASP A CA  
1791 C C   . ASP A 230 ? 0.48557 0.69060 0.77181 -0.00211 -0.21309 0.09730  230 ASP A C   
1792 O O   . ASP A 230 ? 0.45983 0.67529 0.77227 0.01636  -0.20247 0.10823  230 ASP A O   
1793 C CB  . ASP A 230 ? 0.58818 0.75859 0.75810 -0.02267 -0.13805 0.11074  230 ASP A CB  
1794 C CG  . ASP A 230 ? 0.72708 0.79283 0.76032 -0.03398 -0.07508 0.09940  230 ASP A CG  
1795 O OD1 . ASP A 230 ? 0.78988 0.80545 0.76121 -0.04941 -0.06150 0.09887  230 ASP A OD1 
1796 O OD2 . ASP A 230 ? 0.77395 0.81414 0.76992 -0.03949 -0.04990 0.07703  230 ASP A OD2 
1797 N N   . VAL A 231 ? 0.45468 0.65015 0.77590 -0.01605 -0.23665 0.07307  231 VAL A N   
1798 C CA  . VAL A 231 ? 0.47537 0.59445 0.78121 -0.00924 -0.18696 0.06190  231 VAL A CA  
1799 C C   . VAL A 231 ? 0.47264 0.56709 0.77277 -0.00199 -0.12810 -0.00907 231 VAL A C   
1800 O O   . VAL A 231 ? 0.55060 0.60287 0.78605 -0.03407 -0.13418 -0.01918 231 VAL A O   
1801 C CB  . VAL A 231 ? 0.43567 0.60411 0.80003 0.00969  -0.20199 0.07358  231 VAL A CB  
1802 C CG1 . VAL A 231 ? 0.44937 0.60414 0.81314 0.02851  -0.19267 0.09448  231 VAL A CG1 
1803 C CG2 . VAL A 231 ? 0.40018 0.62059 0.78765 0.02610  -0.21019 0.08827  231 VAL A CG2 
1804 N N   . GLN A 232 ? 0.41523 0.53681 0.73999 -0.02718 -0.08754 -0.04721 232 GLN A N   
1805 C CA  . GLN A 232 ? 0.41302 0.52281 0.69241 -0.01894 -0.04820 -0.09260 232 GLN A CA  
1806 C C   . GLN A 232 ? 0.41328 0.53668 0.67124 -0.02468 -0.00519 -0.09008 232 GLN A C   
1807 O O   . GLN A 232 ? 0.45675 0.54149 0.67085 -0.02918 0.04160  -0.12266 232 GLN A O   
1808 C CB  . GLN A 232 ? 0.43217 0.53540 0.68346 -0.00699 -0.05382 -0.10079 232 GLN A CB  
1809 N N   . GLU A 233 ? 0.32642 0.50530 0.63262 0.02071  0.01164  -0.06192 233 GLU A N   
1810 C CA  . GLU A 233 ? 0.34720 0.52218 0.60758 0.04779  -0.00079 -0.01036 233 GLU A CA  
1811 C C   . GLU A 233 ? 0.30871 0.53438 0.58109 0.06970  0.00537  0.03570  233 GLU A C   
1812 O O   . GLU A 233 ? 0.29906 0.56191 0.56320 0.10665  0.03643  0.06522  233 GLU A O   
1813 C CB  . GLU A 233 ? 0.37419 0.52471 0.61560 0.01190  0.04996  0.00522  233 GLU A CB  
1814 C CG  . GLU A 233 ? 0.42198 0.55533 0.63984 0.06113  0.02603  0.04341  233 GLU A CG  
1815 C CD  . GLU A 233 ? 0.45613 0.56634 0.65209 0.06743  0.01575  0.09843  233 GLU A CD  
1816 O OE1 . GLU A 233 ? 0.45414 0.54619 0.66773 0.06114  0.03030  0.09046  233 GLU A OE1 
1817 O OE2 . GLU A 233 ? 0.52875 0.60786 0.66606 0.04961  0.01060  0.12063  233 GLU A OE2 
1818 N N   . ILE A 234 ? 0.29435 0.52745 0.57543 0.03487  0.02280  0.02973  234 ILE A N   
1819 C CA  . ILE A 234 ? 0.31332 0.49002 0.52807 0.06585  0.02216  0.09076  234 ILE A CA  
1820 C C   . ILE A 234 ? 0.33763 0.47100 0.47841 0.08740  0.02979  0.08609  234 ILE A C   
1821 O O   . ILE A 234 ? 0.41174 0.49916 0.52698 0.12348  0.07026  0.06914  234 ILE A O   
1822 C CB  . ILE A 234 ? 0.33712 0.47183 0.55676 0.06196  0.02254  0.11011  234 ILE A CB  
1823 C CG1 . ILE A 234 ? 0.36487 0.40762 0.54240 0.03374  0.02230  0.15493  234 ILE A CG1 
1824 C CG2 . ILE A 234 ? 0.39959 0.51233 0.58054 0.03694  -0.00938 0.08703  234 ILE A CG2 
1825 C CD1 . ILE A 234 ? 0.33259 0.41589 0.53760 0.05294  -0.00626 0.11920  234 ILE A CD1 
1826 N N   . ARG A 235 ? 0.30601 0.42811 0.37020 0.06753  -0.01044 0.04420  235 ARG A N   
1827 C CA  A ARG A 235 ? 0.31801 0.43360 0.35393 0.05333  -0.02127 0.03144  235 ARG A CA  
1828 C CA  B ARG A 235 ? 0.31872 0.43452 0.35565 0.05549  -0.02353 0.02881  235 ARG A CA  
1829 C C   . ARG A 235 ? 0.29522 0.46051 0.33062 0.03465  -0.01629 0.02884  235 ARG A C   
1830 O O   . ARG A 235 ? 0.31584 0.54318 0.32300 0.09234  0.02464  -0.03156 235 ARG A O   
1831 C CB  A ARG A 235 ? 0.37359 0.43620 0.36525 0.05024  -0.01503 0.04900  235 ARG A CB  
1832 C CB  B ARG A 235 ? 0.37509 0.44074 0.37320 0.05743  -0.02221 0.04231  235 ARG A CB  
1833 C CG  A ARG A 235 ? 0.45262 0.47762 0.41713 0.05344  -0.00085 0.05317  235 ARG A CG  
1834 C CG  B ARG A 235 ? 0.44417 0.49076 0.43449 0.06690  -0.01508 0.04448  235 ARG A CG  
1835 C CD  A ARG A 235 ? 0.51622 0.49203 0.45652 0.05915  -0.01358 0.06415  235 ARG A CD  
1836 C CD  B ARG A 235 ? 0.48675 0.52055 0.48053 0.06642  -0.03444 0.05860  235 ARG A CD  
1837 N NE  A ARG A 235 ? 0.52686 0.51583 0.47587 0.07810  -0.02084 0.05201  235 ARG A NE  
1838 N NE  B ARG A 235 ? 0.54599 0.55522 0.53061 0.06314  -0.05413 0.04614  235 ARG A NE  
1839 C CZ  A ARG A 235 ? 0.55787 0.54672 0.50177 0.07580  -0.06617 0.05360  235 ARG A CZ  
1840 C CZ  B ARG A 235 ? 0.57758 0.55595 0.55990 0.06276  -0.07965 0.04768  235 ARG A CZ  
1841 N NH1 A ARG A 235 ? 0.58567 0.58432 0.49597 0.06821  -0.08265 0.07091  235 ARG A NH1 
1842 N NH1 B ARG A 235 ? 0.58567 0.53083 0.55885 0.06015  -0.08597 0.01413  235 ARG A NH1 
1843 N NH2 A ARG A 235 ? 0.56117 0.53613 0.50757 0.08591  -0.09333 0.04760  235 ARG A NH2 
1844 N NH2 B ARG A 235 ? 0.59381 0.55004 0.58286 0.07493  -0.10666 0.05614  235 ARG A NH2 
1845 N N   . TYR A 236 ? 0.23944 0.45687 0.30524 0.00979  -0.01028 0.04256  236 TYR A N   
1846 C CA  . TYR A 236 ? 0.32200 0.43456 0.29656 0.06532  -0.00605 0.03231  236 TYR A CA  
1847 C C   . TYR A 236 ? 0.36570 0.46650 0.29579 0.08928  0.00769  0.01545  236 TYR A C   
1848 O O   . TYR A 236 ? 0.33614 0.49370 0.29508 0.11462  0.01368  0.01410  236 TYR A O   
1849 C CB  . TYR A 236 ? 0.33068 0.46380 0.32274 0.12034  0.00048  0.03970  236 TYR A CB  
1850 C CG  . TYR A 236 ? 0.30923 0.49013 0.34409 0.12620  0.00231  0.04289  236 TYR A CG  
1851 C CD1 . TYR A 236 ? 0.29559 0.54242 0.35662 0.08540  0.00862  0.05798  236 TYR A CD1 
1852 C CD2 . TYR A 236 ? 0.34308 0.50372 0.37382 0.12521  -0.00201 0.03607  236 TYR A CD2 
1853 C CE1 . TYR A 236 ? 0.27628 0.54485 0.36987 0.06596  -0.03489 0.03368  236 TYR A CE1 
1854 C CE2 . TYR A 236 ? 0.37053 0.51855 0.37764 0.12315  0.00416  0.04178  236 TYR A CE2 
1855 C CZ  . TYR A 236 ? 0.35836 0.54993 0.40323 0.11345  -0.02891 0.01723  236 TYR A CZ  
1856 O OH  . TYR A 236 ? 0.53444 0.56295 0.42519 0.12069  -0.07539 -0.01771 236 TYR A OH  
1857 N N   . GLU A 237 ? 0.39879 0.44997 0.26948 0.11011  -0.01734 -0.00451 237 GLU A N   
1858 C CA  . GLU A 237 ? 0.41103 0.36460 0.28927 0.15990  -0.02323 0.01079  237 GLU A CA  
1859 C C   . GLU A 237 ? 0.40684 0.39172 0.30555 0.14095  -0.01786 -0.02825 237 GLU A C   
1860 O O   . GLU A 237 ? 0.37342 0.41009 0.32682 0.10196  0.01596  -0.03836 237 GLU A O   
1861 C CB  . GLU A 237 ? 0.47032 0.39534 0.35099 0.16087  -0.05623 0.02504  237 GLU A CB  
1862 C CG  . GLU A 237 ? 0.49757 0.38955 0.43391 0.13769  -0.03662 0.06208  237 GLU A CG  
1863 C CD  . GLU A 237 ? 0.52959 0.39901 0.49719 0.08324  -0.06083 0.10446  237 GLU A CD  
1864 O OE1 . GLU A 237 ? 0.52977 0.31028 0.51857 0.04332  -0.03098 0.13556  237 GLU A OE1 
1865 O OE2 . GLU A 237 ? 0.53386 0.45697 0.53407 0.07308  -0.09721 0.12060  237 GLU A OE2 
1866 N N   . VAL A 238 ? 0.39151 0.40395 0.28528 0.11444  -0.00710 -0.03790 238 VAL A N   
1867 C CA  . VAL A 238 ? 0.46336 0.35521 0.27630 0.09075  0.01697  -0.02958 238 VAL A CA  
1868 C C   . VAL A 238 ? 0.52219 0.37971 0.26436 0.12480  0.01940  0.00867  238 VAL A C   
1869 O O   . VAL A 238 ? 0.58480 0.41267 0.29279 0.13934  0.00661  0.00771  238 VAL A O   
1870 C CB  . VAL A 238 ? 0.42596 0.31211 0.28439 0.11277  0.03519  -0.03216 238 VAL A CB  
1871 C CG1 . VAL A 238 ? 0.46571 0.30730 0.29877 0.04526  0.00626  -0.05056 238 VAL A CG1 
1872 C CG2 . VAL A 238 ? 0.42354 0.31650 0.30025 0.17791  0.01510  -0.02215 238 VAL A CG2 
1873 N N   . SER A 239 ? 0.52341 0.37736 0.25295 0.20708  0.05364  0.02065  239 SER A N   
1874 C CA  . SER A 239 ? 0.53250 0.39730 0.26447 0.21117  0.01978  0.00725  239 SER A CA  
1875 C C   . SER A 239 ? 0.61544 0.44359 0.31689 0.20776  0.04785  0.04029  239 SER A C   
1876 O O   . SER A 239 ? 0.62835 0.40800 0.35951 0.15987  0.06724  0.01227  239 SER A O   
1877 C CB  . SER A 239 ? 0.49255 0.43745 0.34358 0.23031  0.07115  0.02379  239 SER A CB  
1878 O OG  . SER A 239 ? 0.54263 0.42345 0.37618 0.23142  0.04544  0.01146  239 SER A OG  
1879 N N   . ALA A 240 ? 0.65813 0.47314 0.31154 0.22245  0.04868  0.02702  240 ALA A N   
1880 C CA  . ALA A 240 ? 0.66135 0.49971 0.33858 0.16584  0.02513  0.00562  240 ALA A CA  
1881 C C   . ALA A 240 ? 0.65439 0.51924 0.34345 0.15848  0.01387  0.01302  240 ALA A C   
1882 O O   . ALA A 240 ? 0.68246 0.53244 0.37236 0.14038  0.03999  -0.00984 240 ALA A O   
1883 C CB  . ALA A 240 ? 0.68824 0.49724 0.33959 0.17685  -0.02352 0.01417  240 ALA A CB  
1884 N N   . LYS A 241 ? 0.62084 0.51983 0.34903 0.16321  0.03295  0.02865  241 LYS A N   
1885 C CA  . LYS A 241 ? 0.56724 0.50924 0.34195 0.18620  0.05795  0.03039  241 LYS A CA  
1886 C C   . LYS A 241 ? 0.55562 0.46417 0.34699 0.17242  0.08485  0.03456  241 LYS A C   
1887 O O   . LYS A 241 ? 0.55127 0.43493 0.34730 0.14405  0.10452  0.04385  241 LYS A O   
1888 C CB  . LYS A 241 ? 0.52130 0.51475 0.36538 0.21814  0.01535  0.00253  241 LYS A CB  
1889 C CG  . LYS A 241 ? 0.57595 0.57765 0.42324 0.15688  -0.04026 0.02998  241 LYS A CG  
1890 C CD  . LYS A 241 ? 0.63349 0.66064 0.48599 0.14480  -0.06694 0.04795  241 LYS A CD  
1891 C CE  . LYS A 241 ? 0.68632 0.72803 0.52817 0.08595  -0.07732 0.03560  241 LYS A CE  
1892 N NZ  . LYS A 241 ? 0.71391 0.76924 0.54883 0.08211  -0.06316 0.03013  241 LYS A NZ  
1893 N N   . LYS A 242 ? 0.59241 0.43686 0.36396 0.15267  0.04898  0.02128  242 LYS A N   
1894 C CA  . LYS A 242 ? 0.55449 0.47090 0.35079 0.12839  0.05424  0.01994  242 LYS A CA  
1895 C C   . LYS A 242 ? 0.53387 0.46579 0.34856 0.07953  0.02223  0.00756  242 LYS A C   
1896 O O   . LYS A 242 ? 0.56034 0.45861 0.35668 0.08526  0.01221  -0.00940 242 LYS A O   
1897 C CB  . LYS A 242 ? 0.54911 0.52300 0.38579 0.11941  0.08810  0.06036  242 LYS A CB  
1898 C CG  . LYS A 242 ? 0.53043 0.57464 0.40938 0.05854  0.13449  0.10177  242 LYS A CG  
1899 C CD  . LYS A 242 ? 0.55681 0.63587 0.48437 0.07763  0.11620  0.12232  242 LYS A CD  
1900 C CE  . LYS A 242 ? 0.58180 0.69593 0.54117 0.05420  0.13283  0.11381  242 LYS A CE  
1901 N NZ  . LYS A 242 ? 0.58854 0.73887 0.57417 0.08880  0.12865  0.10102  242 LYS A NZ  
1902 N N   . ILE A 243 ? 0.47797 0.42769 0.33793 0.05843  0.03960  0.00148  243 ILE A N   
1903 C CA  . ILE A 243 ? 0.46088 0.41897 0.29412 0.01601  0.06787  -0.04723 243 ILE A CA  
1904 C C   . ILE A 243 ? 0.46263 0.42538 0.31631 0.00584  0.06158  -0.06087 243 ILE A C   
1905 O O   . ILE A 243 ? 0.43350 0.40302 0.32048 -0.00098 0.03899  -0.07627 243 ILE A O   
1906 C CB  . ILE A 243 ? 0.44781 0.42176 0.29993 0.03760  0.09556  -0.02453 243 ILE A CB  
1907 C CG1 . ILE A 243 ? 0.53459 0.41931 0.30562 -0.00342 0.09140  -0.00635 243 ILE A CG1 
1908 C CG2 . ILE A 243 ? 0.38719 0.42958 0.31004 0.04471  0.04622  -0.03587 243 ILE A CG2 
1909 C CD1 . ILE A 243 ? 0.55267 0.42574 0.31523 -0.03360 0.09287  -0.02972 243 ILE A CD1 
1910 N N   . HIS A 244 ? 0.50304 0.42209 0.33308 0.02391  0.03511  -0.05288 244 HIS A N   
1911 C CA  . HIS A 244 ? 0.49395 0.41915 0.35084 -0.06713 0.02465  -0.04763 244 HIS A CA  
1912 C C   . HIS A 244 ? 0.50371 0.42442 0.34633 -0.04702 0.04350  -0.04503 244 HIS A C   
1913 O O   . HIS A 244 ? 0.51111 0.45032 0.36253 -0.05990 0.06833  -0.06103 244 HIS A O   
1914 C CB  . HIS A 244 ? 0.54397 0.44471 0.39596 -0.10433 0.06645  -0.00520 244 HIS A CB  
1915 C CG  . HIS A 244 ? 0.62673 0.48997 0.43938 -0.05621 0.02822  0.02605  244 HIS A CG  
1916 N ND1 . HIS A 244 ? 0.64981 0.52490 0.45123 -0.02005 0.06592  0.02722  244 HIS A ND1 
1917 C CD2 . HIS A 244 ? 0.66178 0.50696 0.46159 -0.03012 0.01090  0.03159  244 HIS A CD2 
1918 C CE1 . HIS A 244 ? 0.66345 0.52076 0.45680 0.02352  0.05307  0.01691  244 HIS A CE1 
1919 N NE2 . HIS A 244 ? 0.65997 0.50747 0.45826 0.00917  0.03459  0.02358  244 HIS A NE2 
1920 N N   . PHE A 245 ? 0.47537 0.42210 0.29111 0.00686  0.01281  -0.04972 245 PHE A N   
1921 C CA  . PHE A 245 ? 0.49428 0.43830 0.31015 0.01216  0.01919  -0.05247 245 PHE A CA  
1922 C C   . PHE A 245 ? 0.52925 0.49586 0.32434 -0.06038 0.04908  -0.04059 245 PHE A C   
1923 O O   . PHE A 245 ? 0.58997 0.51362 0.35187 -0.11924 0.06014  -0.00370 245 PHE A O   
1924 C CB  . PHE A 245 ? 0.52244 0.45494 0.31836 0.02885  0.04320  -0.06810 245 PHE A CB  
1925 C CG  . PHE A 245 ? 0.53037 0.47059 0.35683 0.02484  0.06597  -0.08462 245 PHE A CG  
1926 C CD1 . PHE A 245 ? 0.52394 0.50255 0.36872 0.05300  0.09596  -0.09474 245 PHE A CD1 
1927 C CD2 . PHE A 245 ? 0.52855 0.46384 0.40121 0.01814  0.05794  -0.10837 245 PHE A CD2 
1928 C CE1 . PHE A 245 ? 0.50219 0.50814 0.40966 0.05826  0.09564  -0.07719 245 PHE A CE1 
1929 C CE2 . PHE A 245 ? 0.49631 0.48120 0.41617 0.03847  0.07145  -0.12013 245 PHE A CE2 
1930 C CZ  . PHE A 245 ? 0.46837 0.48831 0.42011 0.05846  0.07925  -0.08600 245 PHE A CZ  
1931 N N   . ALA A 246 ? 0.56154 0.53598 0.33156 -0.08673 0.03547  -0.07939 246 ALA A N   
1932 C CA  . ALA A 246 ? 0.52822 0.57380 0.35469 -0.05001 0.05670  -0.10045 246 ALA A CA  
1933 C C   . ALA A 246 ? 0.58484 0.63350 0.42511 -0.07411 0.08594  -0.08432 246 ALA A C   
1934 O O   . ALA A 246 ? 0.60399 0.63514 0.46789 -0.04009 0.06320  -0.07262 246 ALA A O   
1935 C CB  . ALA A 246 ? 0.52017 0.58957 0.37056 0.01202  0.02363  -0.11230 246 ALA A CB  
1936 N N   . ARG A 247 ? 0.62125 0.68136 0.43121 -0.07164 0.11598  -0.08121 247 ARG A N   
1937 C CA  . ARG A 247 ? 0.68535 0.70769 0.49979 -0.04761 0.08832  -0.11088 247 ARG A CA  
1938 C C   . ARG A 247 ? 0.69755 0.69693 0.52823 -0.02413 0.03875  -0.14290 247 ARG A C   
1939 O O   . ARG A 247 ? 0.72430 0.71173 0.51418 -0.05964 0.00712  -0.19447 247 ARG A O   
1940 C CB  . ARG A 247 ? 0.73840 0.72718 0.54432 -0.01657 0.08581  -0.12720 247 ARG A CB  
1941 C CG  . ARG A 247 ? 0.78895 0.75815 0.57408 -0.01567 0.07676  -0.12667 247 ARG A CG  
1942 C CD  . ARG A 247 ? 0.82745 0.75600 0.60667 -0.00254 0.06455  -0.17201 247 ARG A CD  
1943 N NE  . ARG A 247 ? 0.82678 0.77297 0.63447 0.00456  0.07596  -0.16522 247 ARG A NE  
1944 C CZ  . ARG A 247 ? 0.80065 0.76215 0.66677 0.02492  0.05525  -0.16297 247 ARG A CZ  
1945 N NH1 . ARG A 247 ? 0.77490 0.77595 0.69567 0.02035  0.05991  -0.14539 247 ARG A NH1 
1946 N NH2 . ARG A 247 ? 0.77560 0.73288 0.65448 0.01968  0.00836  -0.17658 247 ARG A NH2 
1947 N N   . PHE A 248 ? 0.70607 0.69169 0.58634 0.03473  0.04408  -0.13109 248 PHE A N   
1948 C CA  . PHE A 248 ? 0.70346 0.69177 0.61725 0.08512  0.06677  -0.14140 248 PHE A CA  
1949 C C   . PHE A 248 ? 0.66789 0.64389 0.59466 0.09020  0.07595  -0.17700 248 PHE A C   
1950 O O   . PHE A 248 ? 0.68117 0.65835 0.59141 0.11740  0.10418  -0.19550 248 PHE A O   
1951 C CB  . PHE A 248 ? 0.73407 0.75226 0.68359 0.06967  0.04702  -0.08271 248 PHE A CB  
1952 C CG  . PHE A 248 ? 0.74110 0.79264 0.71726 0.07263  0.02068  -0.03251 248 PHE A CG  
1953 C CD1 . PHE A 248 ? 0.74426 0.78501 0.72354 0.08263  0.02465  -0.02965 248 PHE A CD1 
1954 C CD2 . PHE A 248 ? 0.75931 0.80812 0.72988 0.06868  0.01775  -0.01126 248 PHE A CD2 
1955 C CE1 . PHE A 248 ? 0.75250 0.78094 0.72582 0.08756  0.01798  -0.01671 248 PHE A CE1 
1956 C CE2 . PHE A 248 ? 0.78240 0.81098 0.73685 0.07725  0.01279  0.00297  248 PHE A CE2 
1957 C CZ  . PHE A 248 ? 0.78070 0.79402 0.72939 0.09233  0.02123  -0.00262 248 PHE A CZ  
1958 N N   . ARG A 249 ? 0.59307 0.54348 0.57387 0.12179  0.09512  -0.21879 249 ARG A N   
1959 C CA  . ARG A 249 ? 0.63975 0.56137 0.59243 0.02498  0.09526  -0.20051 249 ARG A CA  
1960 C C   . ARG A 249 ? 0.61899 0.54191 0.58489 0.04526  0.05594  -0.21265 249 ARG A C   
1961 O O   . ARG A 249 ? 0.60303 0.55117 0.61163 0.08256  0.03672  -0.19999 249 ARG A O   
1962 C CB  . ARG A 249 ? 0.67409 0.58976 0.58607 -0.01992 0.13061  -0.19446 249 ARG A CB  
1963 C CG  . ARG A 249 ? 0.73143 0.64604 0.60389 -0.00967 0.15612  -0.18056 249 ARG A CG  
1964 C CD  . ARG A 249 ? 0.76177 0.68539 0.61383 -0.00053 0.16714  -0.16671 249 ARG A CD  
1965 N NE  . ARG A 249 ? 0.81230 0.72535 0.63434 0.00615  0.15469  -0.13809 249 ARG A NE  
1966 C CZ  . ARG A 249 ? 0.84231 0.76650 0.64883 0.02326  0.12904  -0.13183 249 ARG A CZ  
1967 N NH1 . ARG A 249 ? 0.86338 0.78891 0.66275 0.01201  0.11840  -0.12092 249 ARG A NH1 
1968 N NH2 . ARG A 249 ? 0.82059 0.77679 0.65043 0.03976  0.12787  -0.13569 249 ARG A NH2 
1969 N N   . SER A 250 ? 0.59588 0.52550 0.56632 0.00496  0.04960  -0.21022 250 SER A N   
1970 C CA  . SER A 250 ? 0.59845 0.51640 0.52973 -0.01730 0.05307  -0.21973 250 SER A CA  
1971 C C   . SER A 250 ? 0.57946 0.52844 0.48097 -0.03113 0.01171  -0.20708 250 SER A C   
1972 O O   . SER A 250 ? 0.64632 0.55945 0.48508 0.01304  -0.01478 -0.21859 250 SER A O   
1973 C CB  . SER A 250 ? 0.64255 0.54588 0.55564 -0.01435 0.08828  -0.18585 250 SER A CB  
1974 O OG  . SER A 250 ? 0.66825 0.58253 0.55791 0.00029  0.10016  -0.16818 250 SER A OG  
1975 N N   . PHE A 251 ? 0.50482 0.51664 0.44964 -0.02369 0.05119  -0.18758 251 PHE A N   
1976 C CA  . PHE A 251 ? 0.45087 0.46921 0.42759 -0.03077 0.06488  -0.15020 251 PHE A CA  
1977 C C   . PHE A 251 ? 0.42508 0.46542 0.39706 -0.04588 0.03700  -0.12907 251 PHE A C   
1978 O O   . PHE A 251 ? 0.40009 0.50111 0.41961 -0.01836 0.00804  -0.11529 251 PHE A O   
1979 C CB  . PHE A 251 ? 0.46352 0.47678 0.46660 -0.01756 0.10317  -0.09252 251 PHE A CB  
1980 C CG  . PHE A 251 ? 0.46515 0.48489 0.48815 -0.03125 0.10354  -0.06932 251 PHE A CG  
1981 C CD1 . PHE A 251 ? 0.47718 0.50456 0.50386 -0.07942 0.11653  -0.05397 251 PHE A CD1 
1982 C CD2 . PHE A 251 ? 0.46632 0.47990 0.50609 -0.01530 0.09565  -0.06533 251 PHE A CD2 
1983 C CE1 . PHE A 251 ? 0.45716 0.50361 0.50550 -0.08231 0.13967  -0.04931 251 PHE A CE1 
1984 C CE2 . PHE A 251 ? 0.49709 0.49884 0.51572 -0.03553 0.10094  -0.06127 251 PHE A CE2 
1985 C CZ  . PHE A 251 ? 0.49711 0.48947 0.53926 -0.06392 0.10606  -0.04592 251 PHE A CZ  
1986 N N   . PRO A 252 ? 0.41456 0.40876 0.37028 -0.03038 0.05268  -0.09055 252 PRO A N   
1987 C CA  . PRO A 252 ? 0.38953 0.40979 0.35253 -0.02942 0.07835  -0.07711 252 PRO A CA  
1988 C C   . PRO A 252 ? 0.41162 0.44381 0.29440 0.00308  0.04297  -0.05309 252 PRO A C   
1989 O O   . PRO A 252 ? 0.41770 0.50486 0.26282 -0.01634 -0.02203 -0.01646 252 PRO A O   
1990 C CB  . PRO A 252 ? 0.41853 0.40004 0.38350 -0.08691 0.08769  -0.07206 252 PRO A CB  
1991 C CG  . PRO A 252 ? 0.42170 0.37724 0.37626 -0.04872 0.05260  -0.06759 252 PRO A CG  
1992 C CD  . PRO A 252 ? 0.36158 0.37270 0.39051 -0.00836 0.06234  -0.08750 252 PRO A CD  
1993 N N   . PHE A 253 ? 0.40588 0.41363 0.31945 0.04058  0.00063  -0.08442 253 PHE A N   
1994 C CA  . PHE A 253 ? 0.38860 0.44109 0.28999 0.00058  0.01117  -0.09703 253 PHE A CA  
1995 C C   . PHE A 253 ? 0.34957 0.42206 0.27038 -0.01420 0.00707  -0.06667 253 PHE A C   
1996 O O   . PHE A 253 ? 0.38531 0.38850 0.27307 -0.04546 0.01530  -0.07239 253 PHE A O   
1997 C CB  . PHE A 253 ? 0.42414 0.41034 0.29211 -0.01318 0.01996  -0.08920 253 PHE A CB  
1998 C CG  . PHE A 253 ? 0.40253 0.38633 0.27785 -0.04365 0.00255  -0.05164 253 PHE A CG  
1999 C CD1 . PHE A 253 ? 0.44197 0.37169 0.28917 -0.05844 0.00692  -0.04389 253 PHE A CD1 
2000 C CD2 . PHE A 253 ? 0.45632 0.37310 0.30504 -0.06627 0.04082  0.00062  253 PHE A CD2 
2001 C CE1 . PHE A 253 ? 0.47050 0.40753 0.32241 -0.06419 0.04213  -0.02275 253 PHE A CE1 
2002 C CE2 . PHE A 253 ? 0.49192 0.36377 0.31205 -0.13260 0.05191  -0.00078 253 PHE A CE2 
2003 C CZ  . PHE A 253 ? 0.51893 0.39603 0.32123 -0.09318 0.04630  -0.00173 253 PHE A CZ  
2004 N N   . TRP A 254 ? 0.33714 0.43386 0.26276 0.05373  0.02833  -0.06516 254 TRP A N   
2005 C CA  . TRP A 254 ? 0.29534 0.40138 0.25378 0.02163  0.02325  -0.01276 254 TRP A CA  
2006 C C   . TRP A 254 ? 0.35938 0.38282 0.23233 -0.02125 0.00625  -0.04016 254 TRP A C   
2007 O O   . TRP A 254 ? 0.38541 0.34841 0.25982 -0.04013 -0.00478 -0.04964 254 TRP A O   
2008 C CB  . TRP A 254 ? 0.29903 0.40920 0.26170 0.03849  0.04796  0.02567  254 TRP A CB  
2009 C CG  . TRP A 254 ? 0.32695 0.36325 0.27740 0.01277  0.01850  0.00012  254 TRP A CG  
2010 C CD1 . TRP A 254 ? 0.39199 0.38619 0.30819 0.01249  0.01950  -0.00889 254 TRP A CD1 
2011 C CD2 . TRP A 254 ? 0.37779 0.36087 0.29526 0.02544  0.04241  -0.04624 254 TRP A CD2 
2012 N NE1 . TRP A 254 ? 0.39447 0.37558 0.29252 0.02300  0.04370  -0.02988 254 TRP A NE1 
2013 C CE2 . TRP A 254 ? 0.34325 0.36430 0.29371 0.03578  0.04708  -0.06084 254 TRP A CE2 
2014 C CE3 . TRP A 254 ? 0.40600 0.35965 0.28255 0.04314  0.04983  -0.09180 254 TRP A CE3 
2015 C CZ2 . TRP A 254 ? 0.29780 0.39826 0.30005 -0.00620 0.05077  -0.07024 254 TRP A CZ2 
2016 C CZ3 . TRP A 254 ? 0.37347 0.40926 0.28402 0.02540  0.07249  -0.04573 254 TRP A CZ3 
2017 C CH2 . TRP A 254 ? 0.38992 0.39216 0.30048 0.01645  0.06023  -0.05122 254 TRP A CH2 
2018 N N   . ARG A 255 ? 0.41536 0.40824 0.20642 -0.00801 0.01295  -0.04656 255 ARG A N   
2019 C CA  . ARG A 255 ? 0.47147 0.40521 0.21932 -0.07058 -0.00780 -0.05434 255 ARG A CA  
2020 C C   . ARG A 255 ? 0.45456 0.41640 0.26877 -0.04601 0.01484  -0.05303 255 ARG A C   
2021 O O   . ARG A 255 ? 0.42661 0.43611 0.26836 -0.07925 0.03054  -0.06183 255 ARG A O   
2022 C CB  . ARG A 255 ? 0.57672 0.44427 0.19245 -0.03532 0.00908  -0.05947 255 ARG A CB  
2023 C CG  . ARG A 255 ? 0.59165 0.52089 0.22976 -0.05822 -0.02036 -0.05075 255 ARG A CG  
2024 C CD  . ARG A 255 ? 0.62290 0.60960 0.28217 -0.02458 -0.04406 -0.07913 255 ARG A CD  
2025 N NE  . ARG A 255 ? 0.68146 0.71004 0.31161 -0.07542 -0.10574 -0.09549 255 ARG A NE  
2026 C CZ  . ARG A 255 ? 0.73915 0.76371 0.29790 -0.01330 -0.09475 -0.06532 255 ARG A CZ  
2027 N NH1 . ARG A 255 ? 0.73467 0.76333 0.32397 0.00791  -0.11438 -0.02069 255 ARG A NH1 
2028 N NH2 . ARG A 255 ? 0.76448 0.79576 0.25158 -0.01330 -0.03231 -0.07780 255 ARG A NH2 
2029 N N   . ARG A 256 ? 0.38897 0.40231 0.27986 -0.01310 0.02824  -0.04346 256 ARG A N   
2030 C CA  . ARG A 256 ? 0.42611 0.41433 0.28680 0.00309  0.04462  -0.03745 256 ARG A CA  
2031 C C   . ARG A 256 ? 0.38319 0.43306 0.23848 -0.06562 0.04281  -0.04435 256 ARG A C   
2032 O O   . ARG A 256 ? 0.36160 0.47241 0.25372 -0.06268 0.04487  -0.06495 256 ARG A O   
2033 C CB  . ARG A 256 ? 0.59501 0.45435 0.29912 0.05402  0.02679  -0.00610 256 ARG A CB  
2034 C CG  . ARG A 256 ? 0.69712 0.49203 0.37602 0.09005  0.00956  0.00517  256 ARG A CG  
2035 C CD  . ARG A 256 ? 0.65534 0.47038 0.36270 0.07334  -0.01993 -0.00144 256 ARG A CD  
2036 N NE  . ARG A 256 ? 0.46348 0.46010 0.32173 0.03042  0.02329  0.02440  256 ARG A NE  
2037 C CZ  . ARG A 256 ? 0.51657 0.51657 0.38399 0.03882  0.00512  -0.08038 256 ARG A CZ  
2038 N NH1 . ARG A 256 ? 0.51924 0.48933 0.41951 0.10431  0.03285  -0.16441 256 ARG A NH1 
2039 N NH2 . ARG A 256 ? 0.57908 0.56155 0.42760 0.01338  0.04710  -0.02748 256 ARG A NH2 
2040 N N   . VAL A 257 ? 0.39104 0.42449 0.20937 -0.00613 0.02831  -0.09889 257 VAL A N   
2041 C CA  . VAL A 257 ? 0.37383 0.41066 0.21505 0.00083  0.04126  -0.04341 257 VAL A CA  
2042 C C   . VAL A 257 ? 0.40309 0.41024 0.23034 -0.02053 0.01096  -0.02899 257 VAL A C   
2043 O O   . VAL A 257 ? 0.40388 0.38871 0.22147 -0.03438 0.01562  -0.02402 257 VAL A O   
2044 C CB  . VAL A 257 ? 0.33701 0.39281 0.22197 0.01772  0.05356  -0.03796 257 VAL A CB  
2045 C CG1 . VAL A 257 ? 0.35933 0.32975 0.25406 -0.03787 0.03895  -0.04264 257 VAL A CG1 
2046 C CG2 . VAL A 257 ? 0.32975 0.38274 0.22162 -0.00190 0.02767  -0.03469 257 VAL A CG2 
2047 N N   . HIS A 258 ? 0.39709 0.40905 0.22747 -0.01534 -0.02182 0.00279  258 HIS A N   
2048 C CA  . HIS A 258 ? 0.34803 0.41740 0.23957 -0.01812 -0.01896 -0.00571 258 HIS A CA  
2049 C C   . HIS A 258 ? 0.40010 0.41046 0.23357 -0.02080 0.02742  -0.02292 258 HIS A C   
2050 O O   . HIS A 258 ? 0.40086 0.44426 0.23634 -0.05940 0.03012  0.00714  258 HIS A O   
2051 C CB  . HIS A 258 ? 0.35054 0.44284 0.23574 -0.02495 -0.01035 -0.01989 258 HIS A CB  
2052 C CG  . HIS A 258 ? 0.36257 0.48148 0.24204 -0.03883 0.00506  -0.02602 258 HIS A CG  
2053 N ND1 . HIS A 258 ? 0.42302 0.55461 0.26453 0.04524  0.01810  -0.00314 258 HIS A ND1 
2054 C CD2 . HIS A 258 ? 0.37593 0.48859 0.24467 -0.08453 -0.01126 -0.04250 258 HIS A CD2 
2055 C CE1 . HIS A 258 ? 0.37783 0.55855 0.27034 0.01428  0.03246  -0.01643 258 HIS A CE1 
2056 N NE2 . HIS A 258 ? 0.41665 0.57117 0.31446 -0.02915 -0.03350 0.00654  258 HIS A NE2 
2057 N N   . ASP A 259 ? 0.40873 0.40452 0.25890 -0.05787 0.05048  -0.05986 259 ASP A N   
2058 C CA  . ASP A 259 ? 0.41232 0.43906 0.27434 -0.07953 0.07334  -0.08405 259 ASP A CA  
2059 C C   . ASP A 259 ? 0.45092 0.47564 0.28869 -0.08457 0.07081  -0.07051 259 ASP A C   
2060 O O   . ASP A 259 ? 0.51779 0.48127 0.32374 -0.12529 0.06447  -0.04887 259 ASP A O   
2061 C CB  . ASP A 259 ? 0.42134 0.46967 0.28481 -0.07923 0.05378  -0.11047 259 ASP A CB  
2062 C CG  . ASP A 259 ? 0.40558 0.48235 0.31452 -0.02992 0.06029  -0.11573 259 ASP A CG  
2063 O OD1 . ASP A 259 ? 0.41239 0.50675 0.31733 -0.05800 0.06120  -0.09241 259 ASP A OD1 
2064 O OD2 . ASP A 259 ? 0.45263 0.52718 0.33987 0.00234  0.01580  -0.08499 259 ASP A OD2 
2065 N N   . SER A 260 ? 0.42970 0.45925 0.27718 -0.06839 0.05672  -0.05061 260 SER A N   
2066 C CA  . SER A 260 ? 0.42379 0.46258 0.31001 -0.06710 0.03129  -0.05598 260 SER A CA  
2067 C C   . SER A 260 ? 0.42861 0.42881 0.32742 -0.07754 0.06158  -0.05911 260 SER A C   
2068 O O   . SER A 260 ? 0.43427 0.45079 0.38603 -0.12490 0.12479  -0.08755 260 SER A O   
2069 C CB  . SER A 260 ? 0.50913 0.50592 0.35485 -0.01597 0.01178  -0.04399 260 SER A CB  
2070 O OG  . SER A 260 ? 0.51383 0.50579 0.38698 -0.05535 0.03213  -0.02642 260 SER A OG  
2071 N N   . PHE A 261 ? 0.39622 0.39004 0.26547 -0.05592 0.02394  -0.02296 261 PHE A N   
2072 C CA  . PHE A 261 ? 0.40941 0.41279 0.24635 -0.04462 0.01362  -0.02953 261 PHE A CA  
2073 C C   . PHE A 261 ? 0.48006 0.42630 0.29048 -0.00187 -0.02857 -0.01801 261 PHE A C   
2074 O O   . PHE A 261 ? 0.53391 0.40506 0.34613 -0.00051 -0.05941 -0.04177 261 PHE A O   
2075 C CB  . PHE A 261 ? 0.38334 0.42531 0.23952 -0.00528 -0.02680 0.01756  261 PHE A CB  
2076 C CG  . PHE A 261 ? 0.36958 0.41234 0.23346 0.03363  -0.02941 -0.00781 261 PHE A CG  
2077 C CD1 . PHE A 261 ? 0.37412 0.43278 0.27695 0.02791  -0.01772 -0.00143 261 PHE A CD1 
2078 C CD2 . PHE A 261 ? 0.33276 0.36944 0.22519 0.01753  -0.02411 -0.00869 261 PHE A CD2 
2079 C CE1 . PHE A 261 ? 0.34196 0.42684 0.29153 0.01433  0.02274  -0.01519 261 PHE A CE1 
2080 C CE2 . PHE A 261 ? 0.39388 0.44091 0.24232 -0.02198 -0.02691 -0.02675 261 PHE A CE2 
2081 C CZ  . PHE A 261 ? 0.36288 0.45226 0.25931 -0.00627 0.03444  -0.01415 261 PHE A CZ  
2082 N N   . ILE A 262 ? 0.45214 0.48063 0.25241 0.01222  -0.03843 0.01933  262 ILE A N   
2083 C CA  . ILE A 262 ? 0.47033 0.49932 0.25990 0.04173  -0.03981 0.02711  262 ILE A CA  
2084 C C   . ILE A 262 ? 0.51992 0.51106 0.25683 0.07902  -0.03595 0.04260  262 ILE A C   
2085 O O   . ILE A 262 ? 0.63592 0.49517 0.29172 0.03015  -0.04474 0.01772  262 ILE A O   
2086 C CB  . ILE A 262 ? 0.45102 0.51718 0.26725 0.04932  -0.02862 0.04251  262 ILE A CB  
2087 C CG1 . ILE A 262 ? 0.45569 0.53608 0.27886 0.06965  0.02315  -0.01019 262 ILE A CG1 
2088 C CG2 . ILE A 262 ? 0.46584 0.52831 0.28146 0.00026  -0.05254 -0.01555 262 ILE A CG2 
2089 C CD1 . ILE A 262 ? 0.41268 0.54640 0.30766 0.04938  0.05311  -0.01942 262 ILE A CD1 
2090 N N   . GLU A 263 ? 0.48524 0.56131 0.21713 0.05021  0.01870  0.03410  263 GLU A N   
2091 C CA  . GLU A 263 ? 0.60707 0.66518 0.32729 0.07331  -0.03927 0.06186  263 GLU A CA  
2092 C C   . GLU A 263 ? 0.70207 0.72567 0.37283 0.04795  -0.00558 0.05783  263 GLU A C   
2093 O O   . GLU A 263 ? 0.71531 0.76123 0.38378 0.03868  -0.00025 0.03715  263 GLU A O   
2094 C CB  . GLU A 263 ? 0.70264 0.70521 0.41108 0.03256  -0.02913 0.04292  263 GLU A CB  
2095 C CG  . GLU A 263 ? 0.76776 0.73034 0.47527 -0.02943 -0.04323 0.02854  263 GLU A CG  
2096 C CD  . GLU A 263 ? 0.79738 0.74525 0.51624 -0.02911 -0.07113 0.02599  263 GLU A CD  
2097 O OE1 . GLU A 263 ? 0.86004 0.79015 0.56361 -0.03214 -0.08774 0.00762  263 GLU A OE1 
2098 O OE2 . GLU A 263 ? 0.76723 0.72158 0.50357 -0.03687 -0.06172 0.00328  263 GLU A OE2 
2099 N N   . ASP A 264 ? 0.81484 0.79058 0.46679 0.02908  0.03386  0.01023  264 ASP A N   
2100 C CA  . ASP A 264 ? 0.87377 0.82292 0.53732 0.05856  0.00292  -0.00112 264 ASP A CA  
2101 C C   . ASP A 264 ? 0.91682 0.84026 0.57191 0.06608  -0.01028 0.01055  264 ASP A C   
2102 O O   . ASP A 264 ? 0.95909 0.86558 0.61125 0.06187  -0.00933 0.00141  264 ASP A O   
2103 C CB  . ASP A 264 ? 0.86596 0.82404 0.55982 0.07209  -0.00914 0.00856  264 ASP A CB  
2104 C CG  . ASP A 264 ? 0.85522 0.86120 0.58400 0.02971  -0.02530 0.01698  264 ASP A CG  
2105 O OD1 . ASP A 264 ? 0.85114 0.87109 0.59515 -0.01247 -0.05016 0.01361  264 ASP A OD1 
2106 O OD2 . ASP A 264 ? 0.83115 0.86856 0.58155 0.04264  -0.02541 0.03298  264 ASP A OD2 
2107 C C1  . CIT B .   ? 0.62362 0.57326 0.51177 -0.05621 -0.07906 -0.04328 301 CIT A C1  
2108 O O1  . CIT B .   ? 0.59975 0.49908 0.42333 -0.06452 -0.05196 -0.04510 301 CIT A O1  
2109 O O2  . CIT B .   ? 0.69874 0.61625 0.56893 -0.03722 -0.03147 -0.01124 301 CIT A O2  
2110 C C2  . CIT B .   ? 0.65863 0.60188 0.55072 -0.03186 -0.10848 -0.05494 301 CIT A C2  
2111 C C3  . CIT B .   ? 0.70770 0.61665 0.57982 0.03899  -0.08216 -0.06942 301 CIT A C3  
2112 O O7  . CIT B .   ? 0.73199 0.58442 0.60785 0.01197  -0.07305 -0.09107 301 CIT A O7  
2113 C C4  . CIT B .   ? 0.74348 0.65749 0.62952 0.08247  -0.07971 -0.05998 301 CIT A C4  
2114 C C5  . CIT B .   ? 0.81064 0.69607 0.68951 0.07489  -0.03726 -0.07251 301 CIT A C5  
2115 O O3  . CIT B .   ? 0.84901 0.71369 0.73099 0.07311  -0.01647 -0.04929 301 CIT A O3  
2116 O O4  . CIT B .   ? 0.82195 0.71667 0.67828 0.04584  -0.02367 -0.10768 301 CIT A O4  
2117 C C6  . CIT B .   ? 0.69110 0.62111 0.55449 0.06486  -0.07134 -0.04852 301 CIT A C6  
2118 O O5  . CIT B .   ? 0.67123 0.57722 0.53431 0.03643  -0.10342 -0.04851 301 CIT A O5  
2119 O O6  . CIT B .   ? 0.72139 0.66839 0.54130 0.09081  -0.02520 -0.04514 301 CIT A O6  
2120 C C1  . GOL C .   ? 0.90926 0.73175 0.62329 0.04294  0.03748  -0.11834 302 GOL A C1  
2121 O O1  . GOL C .   ? 0.92010 0.71813 0.61989 0.07625  0.06251  -0.16335 302 GOL A O1  
2122 C C2  . GOL C .   ? 0.90828 0.73504 0.62070 0.03137  -0.00374 -0.07490 302 GOL A C2  
2123 O O2  . GOL C .   ? 0.92322 0.72183 0.60372 -0.00042 -0.05310 -0.02113 302 GOL A O2  
2124 C C3  . GOL C .   ? 0.88179 0.73623 0.61375 0.07897  0.00060  -0.10276 302 GOL A C3  
2125 O O3  . GOL C .   ? 0.90431 0.75911 0.60470 0.09108  0.03055  -0.09383 302 GOL A O3  
2126 N N1  . UJT D .   ? 0.30494 0.44078 0.27353 0.04086  0.02254  -0.00434 303 UJT A N1  
2127 C C7  . UJT D .   ? 0.32404 0.47191 0.31086 0.00001  0.11314  -0.00745 303 UJT A C7  
2128 C C8  . UJT D .   ? 0.49890 0.54833 0.45255 -0.09205 0.04242  -0.01215 303 UJT A C8  
2129 N N2  . UJT D .   ? 0.25045 0.42987 0.31038 0.02544  0.03828  0.01614  303 UJT A N2  
2130 C C9  . UJT D .   ? 0.58839 0.59272 0.46196 -0.08938 0.05827  -0.02665 303 UJT A C9  
2131 O O1  . UJT D .   ? 0.67460 0.66758 0.50678 -0.07816 0.10462  -0.01704 303 UJT A O1  
2132 C C1  . UJT D .   ? 0.27453 0.41393 0.31325 0.03007  0.01638  0.01005  303 UJT A C1  
2133 O O5  . UJT D .   ? 0.57943 0.51600 0.36284 -0.14415 0.01114  -0.04809 303 UJT A O5  
2134 C C5  . UJT D .   ? 0.28927 0.40516 0.29865 0.03315  0.02149  -0.03194 303 UJT A C5  
2135 C C6  . UJT D .   ? 0.33370 0.42521 0.29588 0.02971  0.05897  -0.01824 303 UJT A C6  
2136 N N3  . UJT D .   ? 0.26954 0.39735 0.28962 0.02010  0.01495  -0.06701 303 UJT A N3  
2137 C C4  . UJT D .   ? 0.26216 0.39502 0.29054 0.04174  0.01483  -0.04968 303 UJT A C4  
2138 O O4  . UJT D .   ? 0.63537 0.55885 0.41121 0.01872  0.06196  0.02611  303 UJT A O4  
2139 C C3  . UJT D .   ? 0.32574 0.37059 0.30862 0.00710  0.00410  -0.08195 303 UJT A C3  
2140 O O3  . UJT D .   ? 0.54819 0.61707 0.43832 -0.05576 0.12021  -0.07111 303 UJT A O3  
2141 C C2  . UJT D .   ? 0.23138 0.41704 0.30566 0.04021  0.00729  -0.01404 303 UJT A C2  
2142 N N4  . UJT D .   ? 0.28424 0.39384 0.32232 0.01279  0.04126  -0.05772 303 UJT A N4  
2143 N N   . UJT D .   ? 0.37992 0.44105 0.25927 -0.01239 0.03286  -0.04480 303 UJT A N   
2144 C C   . UJT D .   ? 0.28349 0.43662 0.27277 0.01664  0.02453  -0.02542 303 UJT A C   
2145 O O   . UJT D .   ? 0.32588 0.42671 0.31277 0.00241  0.01012  -0.02370 303 UJT A O   
2146 C C10 . UJT D .   ? 0.62727 0.63279 0.49023 -0.08571 0.08853  -0.01908 303 UJT A C10 
2147 C C11 . UJT D .   ? 0.40715 0.51123 0.37439 -0.07655 0.03076  -0.06276 303 UJT A C11 
2148 C C12 . UJT D .   ? 0.41157 0.49661 0.33781 -0.10042 0.02730  -0.02071 303 UJT A C12 
2149 C C13 . UJT D .   ? 0.38721 0.45682 0.28517 -0.10713 0.03646  -0.02403 303 UJT A C13 
2150 C C14 . UJT D .   ? 0.38753 0.39678 0.27468 -0.09702 0.04250  -0.00373 303 UJT A C14 
2151 C C15 . UJT D .   ? 0.33185 0.34127 0.24870 -0.00587 0.02290  -0.01156 303 UJT A C15 
2152 C C16 . UJT D .   ? 0.31920 0.31835 0.25157 -0.00528 0.01416  -0.03481 303 UJT A C16 
2153 C C17 . UJT D .   ? 0.38289 0.32895 0.27677 -0.06344 0.02860  -0.03228 303 UJT A C17 
2154 C C18 . UJT D .   ? 0.33686 0.35362 0.26270 -0.05535 0.06793  -0.02974 303 UJT A C18 
2155 C C19 . UJT D .   ? 0.45015 0.41857 0.34771 -0.12839 0.06683  -0.00164 303 UJT A C19 
2156 C C20 . UJT D .   ? 0.51756 0.52071 0.36519 -0.07245 0.05708  -0.04089 303 UJT A C20 
2157 C C21 . UJT D .   ? 0.54143 0.58081 0.43052 -0.03201 0.09488  -0.07290 303 UJT A C21 
2158 C C22 . UJT D .   ? 0.57129 0.52552 0.37249 -0.02871 0.06466  -0.03899 303 UJT A C22 
2159 C C23 . UJT D .   ? 0.52783 0.48274 0.34593 -0.11429 0.07793  -0.02711 303 UJT A C23 
2160 C C24 . UJT D .   ? 0.31059 0.40816 0.28087 0.02593  0.05461  -0.01139 303 UJT A C24 
2161 C C25 . UJT D .   ? 0.30182 0.41977 0.27858 -0.01306 0.05956  -0.01761 303 UJT A C25 
2162 N N10 . UJT D .   ? 0.43323 0.39178 0.29780 -0.06757 0.07807  -0.00260 303 UJT A N10 
2163 N N5  . UJT D .   ? 0.40666 0.51585 0.37776 -0.06807 0.07772  -0.02186 303 UJT A N5  
2164 N N6  . UJT D .   ? 0.36624 0.39633 0.23876 -0.02261 0.01620  0.00187  303 UJT A N6  
2165 N N7  . UJT D .   ? 0.33876 0.32969 0.28022 0.00917  -0.00663 0.02557  303 UJT A N7  
2166 N N8  . UJT D .   ? 0.41342 0.32191 0.26299 0.01433  0.04454  -0.02708 303 UJT A N8  
2167 N N9  . UJT D .   ? 0.40624 0.33676 0.26288 -0.01684 0.04441  -0.00903 303 UJT A N9  
2168 O O2  . UJT D .   ? 0.47008 0.46323 0.35132 -0.07560 0.05797  -0.02827 303 UJT A O2  
2169 O O6  . UJT D .   ? 0.32750 0.39226 0.29154 0.01655  0.03567  -0.03726 303 UJT A O6  
2170 O O7  . UJT D .   ? 0.32531 0.43713 0.27124 -0.05639 0.05413  -0.03346 303 UJT A O7  
2171 O O   . HOH E .   ? 0.36217 0.43880 0.37648 -0.02600 0.00898  0.02515  401 HOH A O   
2172 O O   . HOH E .   ? 0.91607 0.59179 0.53177 -0.12958 -0.08202 -0.05361 402 HOH A O   
2173 O O   . HOH E .   ? 0.31675 0.97867 0.59283 0.02883  -0.01136 0.15027  403 HOH A O   
2174 O O   . HOH E .   ? 0.61341 0.65554 0.57477 -0.24488 0.14222  -0.05901 404 HOH A O   
2175 O O   . HOH E .   ? 0.31187 0.60779 0.26857 -0.01890 0.01362  0.01750  405 HOH A O   
2176 O O   . HOH E .   ? 0.76431 0.60866 0.46822 0.23557  -0.05598 0.09589  406 HOH A O   
2177 O O   . HOH E .   ? 0.74071 0.77710 0.56623 0.16171  0.13159  0.04616  407 HOH A O   
2178 O O   . HOH E .   ? 0.47415 0.53747 0.31243 0.06175  0.03515  -0.01922 408 HOH A O   
2179 O O   . HOH E .   ? 1.04781 0.80941 0.40107 -0.22715 0.18116  -0.05733 409 HOH A O   
2180 O O   . HOH E .   ? 0.69175 0.63835 0.88874 0.12169  0.16429  -0.20672 410 HOH A O   
2181 O O   . HOH E .   ? 0.71718 0.77091 0.64194 0.16426  -0.06390 -0.23526 411 HOH A O   
2182 O O   . HOH E .   ? 0.68547 0.85835 0.60294 0.05987  0.05137  0.10643  412 HOH A O   
2183 O O   . HOH E .   ? 0.72698 0.96732 0.36945 0.14094  -0.08555 -0.09852 413 HOH A O   
2184 O O   . HOH E .   ? 0.52248 0.44945 0.40577 -0.01929 0.08275  -0.09429 414 HOH A O   
2185 O O   . HOH E .   ? 0.60125 0.69439 0.60342 -0.04063 0.01016  -0.05629 415 HOH A O   
2186 O O   . HOH E .   ? 0.52105 0.87667 0.48567 0.03598  0.03101  -0.08741 416 HOH A O   
2187 O O   . HOH E .   ? 0.48347 1.01568 0.43294 -0.01082 0.08588  -0.13164 417 HOH A O   
2188 O O   . HOH E .   ? 0.43823 0.69234 0.47395 0.10628  -0.01994 0.00083  418 HOH A O   
2189 O O   . HOH E .   ? 0.33072 0.45363 0.32718 -0.03707 0.01215  -0.05044 419 HOH A O   
2190 O O   . HOH E .   ? 0.88495 0.70893 0.75842 0.02799  0.14964  0.32469  420 HOH A O   
2191 O O   . HOH E .   ? 0.84867 0.62747 0.86317 -0.04557 -0.06333 -0.06333 421 HOH A O   
2192 O O   . HOH E .   ? 0.40716 0.86414 0.41516 0.10973  0.07625  -0.12723 422 HOH A O   
2193 O O   . HOH E .   ? 0.46298 0.70208 0.37808 0.22902  -0.16803 -0.12489 423 HOH A O   
2194 O O   . HOH E .   ? 0.92127 0.86651 0.49215 -0.02964 0.06521  0.02909  424 HOH A O   
2195 O O   . HOH E .   ? 0.49981 0.45444 0.43155 -0.01482 -0.02608 0.00949  425 HOH A O   
2196 O O   . HOH E .   ? 0.31478 0.44796 0.35778 -0.00504 0.01631  0.02018  426 HOH A O   
2197 O O   . HOH E .   ? 0.36779 0.59286 0.80977 -0.00408 0.01423  0.16641  427 HOH A O   
2198 O O   . HOH E .   ? 0.87801 0.78886 0.46682 0.11534  0.13756  -0.14702 428 HOH A O   
2199 O O   . HOH E .   ? 0.53347 0.56655 0.33785 0.01864  0.03440  -0.08023 430 HOH A O   
2200 O O   . HOH E .   ? 0.26431 0.33247 0.20826 -0.01259 0.02526  -0.04005 431 HOH A O   
2201 O O   . HOH E .   ? 0.80479 0.51423 0.55111 0.21041  0.11781  -0.01183 432 HOH A O   
2202 O O   . HOH E .   ? 0.46230 0.48155 0.30351 0.12919  0.01232  0.01296  433 HOH A O   
2203 O O   . HOH E .   ? 0.48383 0.41398 0.40515 -0.06167 -0.04703 0.05655  434 HOH A O   
2204 O O   . HOH E .   ? 0.62769 0.51472 0.52143 -0.05229 -0.02125 -0.07232 435 HOH A O   
2205 O O   . HOH E .   ? 0.39147 0.44315 0.33707 0.02181  0.00317  -0.03377 436 HOH A O   
2206 O O   . HOH E .   ? 0.38254 0.48244 0.33304 -0.04736 0.00586  -0.03316 437 HOH A O   
2207 O O   . HOH E .   ? 0.26469 0.33067 0.25822 -0.00483 0.02420  -0.01330 438 HOH A O   
2208 O O   . HOH E .   ? 0.64194 0.59695 0.60581 -0.01168 0.15547  0.14027  439 HOH A O   
2209 O O   . HOH E .   ? 0.37784 0.84347 0.28340 0.06969  0.02646  -0.00904 440 HOH A O   
2210 O O   . HOH E .   ? 0.57626 0.44523 0.49972 0.12961  0.06226  0.03655  441 HOH A O   
2211 O O   . HOH E .   ? 0.85397 0.69728 0.69557 0.05858  -0.00173 0.06644  442 HOH A O   
2212 O O   . HOH E .   ? 0.82249 0.76889 0.54519 0.03745  0.32745  0.05653  443 HOH A O   
2213 O O   . HOH E .   ? 0.73252 0.47351 0.36364 -0.08218 0.08349  -0.09752 444 HOH A O   
2214 O O   . HOH E .   ? 0.47267 0.61317 0.32387 0.10666  -0.00300 -0.02652 445 HOH A O   
2215 O O   . HOH E .   ? 0.42683 0.49812 0.52750 -0.05437 0.09553  -0.04297 446 HOH A O   
2216 O O   . HOH E .   ? 0.41172 0.37931 0.27214 -0.00082 0.01343  -0.03081 447 HOH A O   
2217 O O   . HOH E .   ? 0.37301 0.52958 0.41775 0.07965  -0.02404 0.01418  448 HOH A O   
2218 O O   . HOH E .   ? 0.56663 0.70752 0.65719 0.35983  -0.12575 -0.12583 449 HOH A O   
2219 O O   . HOH E .   ? 0.86668 0.73108 0.41071 0.34461  0.23198  0.12557  450 HOH A O   
2220 O O   . HOH E .   ? 0.75602 0.53839 0.74616 -0.19454 0.17010  -0.18869 451 HOH A O   
2221 O O   . HOH E .   ? 0.32433 0.49369 0.28353 -0.03759 0.01413  -0.02513 452 HOH A O   
2222 O O   . HOH E .   ? 0.73336 0.64929 0.90346 -0.04041 -0.04479 0.16061  453 HOH A O   
2223 O O   . HOH E .   ? 0.60287 0.77955 0.79319 -0.12596 -0.09308 -0.24503 454 HOH A O   
2224 O O   . HOH E .   ? 0.27088 0.35846 0.24174 0.01925  0.01700  -0.01236 455 HOH A O   
2225 O O   . HOH E .   ? 0.30678 0.75801 0.34408 -0.10230 -0.01015 -0.04801 456 HOH A O   
2226 O O   . HOH E .   ? 1.02139 0.57623 0.45761 0.07345  -0.06547 -0.03405 457 HOH A O   
2227 O O   . HOH E .   ? 0.30124 0.34049 0.26460 -0.00038 0.00454  -0.00347 458 HOH A O   
2228 O O   . HOH E .   ? 0.58887 0.72671 0.51844 -0.11545 0.12950  -0.03283 459 HOH A O   
2229 O O   . HOH E .   ? 0.63784 0.69463 0.35496 0.03120  0.14643  -0.07512 460 HOH A O   
2230 O O   . HOH E .   ? 0.69959 0.28678 0.53469 0.10789  0.20806  0.01043  461 HOH A O   
2231 O O   . HOH E .   ? 0.63146 1.15261 0.32296 0.22013  0.06598  0.02460  462 HOH A O   
2232 O O   . HOH E .   ? 0.74696 0.59469 0.42484 0.15009  0.23640  -0.00750 463 HOH A O   
2233 O O   . HOH E .   ? 0.69682 0.79013 0.45030 -0.04702 0.03757  0.10364  464 HOH A O   
2234 O O   . HOH E .   ? 0.77137 0.93900 0.62233 0.12918  -0.20384 0.12013  465 HOH A O   
2235 O O   . HOH E .   ? 0.40242 0.40285 0.41758 -0.01271 -0.12066 0.05851  466 HOH A O   
2236 O O   . HOH E .   ? 0.29969 0.50677 0.77821 -0.06145 0.15198  -0.15300 467 HOH A O   
2237 O O   . HOH E .   ? 0.49399 0.57769 0.42558 0.11971  -0.04577 0.01257  468 HOH A O   
2238 O O   . HOH E .   ? 0.70319 0.66692 0.48568 0.24189  -0.17860 0.11786  469 HOH A O   
2239 O O   . HOH E .   ? 0.69921 0.43019 0.52113 -0.23136 -0.06618 0.09438  470 HOH A O   
2240 O O   . HOH E .   ? 0.46845 0.42003 0.32846 0.13161  0.03759  0.04318  471 HOH A O   
2241 O O   . HOH E .   ? 0.73025 0.75577 0.59486 0.16876  -0.13225 -0.18191 472 HOH A O   
2242 O O   . HOH E .   ? 0.30879 0.29256 0.33324 -0.03337 -0.00817 -0.00038 473 HOH A O   
2243 O O   . HOH E .   ? 0.30288 0.88873 0.35015 0.02589  0.00301  0.03375  474 HOH A O   
2244 O O   . HOH E .   ? 0.81997 0.68131 0.79315 0.11287  0.13275  -0.12034 475 HOH A O   
2245 O O   . HOH E .   ? 0.60932 0.69323 0.52851 -0.05671 -0.28926 -0.08233 476 HOH A O   
2246 O O   . HOH E .   ? 0.56352 0.75183 0.79656 0.16520  -0.00729 0.00315  477 HOH A O   
2247 O O   . HOH E .   ? 0.72959 0.48282 0.43653 0.10417  0.12225  -0.00407 478 HOH A O   
2248 O O   . HOH E .   ? 0.49501 0.81838 0.38040 0.01823  0.03725  -0.10361 479 HOH A O   
2249 O O   . HOH E .   ? 0.79995 0.70768 0.92614 0.10288  -0.04714 -0.01257 480 HOH A O   
2250 O O   . HOH E .   ? 0.77658 0.70956 0.74345 -0.21343 0.02062  0.01706  481 HOH A O   
2251 O O   . HOH E .   ? 0.55323 0.64852 0.48270 0.11328  0.00582  -0.08519 482 HOH A O   
2252 O O   . HOH E .   ? 0.41701 0.60020 0.36591 0.08487  0.01109  0.01664  483 HOH A O   
2253 O O   . HOH E .   ? 0.76209 0.59930 0.74893 0.11617  0.07919  -0.15984 484 HOH A O   
2254 O O   . HOH E .   ? 0.48428 0.89143 0.50404 0.01817  0.04794  -0.08572 485 HOH A O   
2255 O O   . HOH E .   ? 0.77568 0.66767 0.94217 -0.13215 -0.09591 0.10201  486 HOH A O   
2256 O O   . HOH E .   ? 0.37507 0.75306 0.76131 -0.04974 0.01514  -0.06916 487 HOH A O   
2257 O O   . HOH E .   ? 0.61605 0.89271 0.72277 0.17346  -0.10716 -0.04701 488 HOH A O   
2258 O O   . HOH E .   ? 0.75132 0.95502 0.54880 -0.16939 0.19311  0.01987  489 HOH A O   
2259 O O   . HOH E .   ? 0.41437 0.61269 0.67731 -0.11628 -0.10133 0.06327  490 HOH A O   
2260 O O   . HOH E .   ? 0.89996 0.72156 0.58357 -0.14251 0.09148  -0.10084 491 HOH A O   
2261 O O   . HOH E .   ? 0.65740 0.59268 0.74855 0.01376  0.15819  0.12137  492 HOH A O   
2262 O O   . HOH E .   ? 0.79691 0.58639 0.74346 -0.00874 -0.10021 -0.03054 493 HOH A O   
2263 O O   . HOH E .   ? 0.56075 0.56930 0.48462 -0.02637 -0.07406 0.18972  494 HOH A O   
2264 O O   . HOH E .   ? 0.65477 0.72860 0.53081 0.04455  -0.17902 0.01337  495 HOH A O   
2265 O O   . HOH E .   ? 0.47816 0.61406 0.42716 0.07798  -0.05084 0.00550  496 HOH A O   
2266 O O   . HOH E .   ? 0.33102 0.56200 0.47825 -0.00751 -0.03667 0.16239  497 HOH A O   
2267 O O   . HOH E .   ? 0.58978 0.63463 0.44880 0.11331  -0.03656 0.01742  498 HOH A O   
2268 O O   . HOH E .   ? 0.87062 0.57277 0.74767 0.11866  0.15878  -0.23513 499 HOH A O   
# 
