data_8QG8
# 
_entry.id   8QG8 
# 
_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   8QG8         pdb_00008qg8 10.2210/pdb8qg8/pdb 
WWPDB D_1292133110 ?            ?                   
# 
_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                        8QG8 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8A9V 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gilles.labesse@cbs.cnrs.fr 
_pdbx_contact_author.name_first         Gilles 
_pdbx_contact_author.name_last          Labesse 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6861-3300 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gelin, M.'   1 ? 
'Labesse, G.' 2 ? 
'Lionne, C.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a di-adenosine derivative' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gelin, M.'      1 ? 
primary 'Labesse, G.'    2 ? 
primary 'Clement, D.'    3 ? 
primary 'Pochet, S.'     4 ? 
primary 'Lionne, C.'     5 ? 
primary 'Leseigneur, C.' 6 ? 
primary 'Huteau, V.'     7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'NAD kinase 1' 31045.279 1  2.7.1.23 ? ? ? 
2 non-polymer syn 'CITRIC ACID' 192.124   1  ?        ? ? ? 
3 non-polymer syn 
;1-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[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]amino]propyl]guanidine
;
668.664   1  ?        ? ? ? 
4 non-polymer syn GLYCEROL 92.094    1  ?        ? ? ? 
5 water       nat water 18.015    74 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ATP-dependent NAD kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 
;1-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[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]amino]propyl]guanidine
;
UQF 
4 GLYCEROL GOL 
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   TYR n 
1 4   MET n 
1 5   ILE n 
1 6   THR n 
1 7   SER n 
1 8   LYS n 
1 9   GLY n 
1 10  ASP n 
1 11  GLU n 
1 12  LYS n 
1 13  SER n 
1 14  ASP n 
1 15  LEU n 
1 16  LEU n 
1 17  ARG n 
1 18  LEU n 
1 19  ASN n 
1 20  MET n 
1 21  ILE n 
1 22  ALA n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  GLU n 
1 27  TYR n 
1 28  ASP n 
1 29  MET n 
1 30  GLU n 
1 31  TYR n 
1 32  ASP n 
1 33  ASP n 
1 34  VAL n 
1 35  GLU n 
1 36  PRO n 
1 37  GLU n 
1 38  ILE n 
1 39  VAL n 
1 40  ILE n 
1 41  SER n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  ASP n 
1 46  GLY n 
1 47  THR n 
1 48  PHE n 
1 49  LEU n 
1 50  SER n 
1 51  ALA n 
1 52  PHE n 
1 53  HIS n 
1 54  GLN n 
1 55  TYR n 
1 56  GLU n 
1 57  GLU n 
1 58  ARG n 
1 59  LEU n 
1 60  ASP n 
1 61  GLU n 
1 62  ILE n 
1 63  ALA n 
1 64  PHE n 
1 65  ILE n 
1 66  GLY n 
1 67  ILE n 
1 68  HIS n 
1 69  THR n 
1 70  GLY n 
1 71  HIS n 
1 72  LEU n 
1 73  GLY n 
1 74  PHE n 
1 75  TYR n 
1 76  ALA n 
1 77  ASP n 
1 78  TRP n 
1 79  ARG n 
1 80  PRO n 
1 81  ALA n 
1 82  GLU n 
1 83  ALA n 
1 84  ASP n 
1 85  LYS n 
1 86  LEU n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  LYS n 
1 93  GLY n 
1 94  GLU n 
1 95  TYR n 
1 96  GLN n 
1 97  LYS n 
1 98  VAL n 
1 99  SER n 
1 100 TYR n 
1 101 PRO n 
1 102 LEU n 
1 103 LEU n 
1 104 LYS n 
1 105 THR n 
1 106 THR n 
1 107 VAL n 
1 108 LYS n 
1 109 TYR n 
1 110 GLY n 
1 111 ILE n 
1 112 GLY n 
1 113 LYS n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 THR n 
1 118 TYR n 
1 119 LEU n 
1 120 ALA n 
1 121 LEU n 
1 122 ASN n 
1 123 GLU n 
1 124 SER n 
1 125 THR n 
1 126 VAL n 
1 127 LYS n 
1 128 SER n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 PRO n 
1 133 PHE n 
1 134 VAL n 
1 135 VAL n 
1 136 ASP n 
1 137 VAL n 
1 138 VAL n 
1 139 ILE n 
1 140 ASN n 
1 141 ASP n 
1 142 ILE n 
1 143 HIS n 
1 144 PHE n 
1 145 GLU n 
1 146 ARG n 
1 147 PHE n 
1 148 ARG n 
1 149 GLY n 
1 150 ASP n 
1 151 GLY n 
1 152 LEU n 
1 153 CYS n 
1 154 MET n 
1 155 SER n 
1 156 THR n 
1 157 PRO n 
1 158 SER n 
1 159 GLY n 
1 160 THR n 
1 161 THR n 
1 162 ALA n 
1 163 TYR n 
1 164 ASN n 
1 165 LYS n 
1 166 SER n 
1 167 LEU n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 LEU n 
1 172 MET n 
1 173 HIS n 
1 174 PRO n 
1 175 SER n 
1 176 ILE n 
1 177 GLU n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 LEU n 
1 182 THR n 
1 183 GLU n 
1 184 MET n 
1 185 ALA n 
1 186 SER n 
1 187 ILE n 
1 188 ASN n 
1 189 ASN n 
1 190 ARG n 
1 191 VAL n 
1 192 TYR n 
1 193 ARG n 
1 194 THR n 
1 195 ILE n 
1 196 GLY n 
1 197 SER n 
1 198 PRO n 
1 199 LEU n 
1 200 VAL n 
1 201 PHE n 
1 202 PRO n 
1 203 LYS n 
1 204 HIS n 
1 205 HIS n 
1 206 VAL n 
1 207 VAL n 
1 208 SER n 
1 209 LEU n 
1 210 GLN n 
1 211 PRO n 
1 212 VAL n 
1 213 ASN n 
1 214 ASP n 
1 215 LYS n 
1 216 ASP n 
1 217 PHE n 
1 218 GLN n 
1 219 ILE n 
1 220 SER n 
1 221 VAL n 
1 222 ASP n 
1 223 HIS n 
1 224 LEU n 
1 225 SER n 
1 226 ILE n 
1 227 LEU n 
1 228 HIS n 
1 229 ARG n 
1 230 ASP n 
1 231 VAL n 
1 232 GLN n 
1 233 GLU n 
1 234 ILE n 
1 235 ARG n 
1 236 TYR n 
1 237 GLU n 
1 238 VAL n 
1 239 SER n 
1 240 ALA n 
1 241 LYS n 
1 242 LYS n 
1 243 ILE n 
1 244 HIS n 
1 245 PHE n 
1 246 ALA n 
1 247 ARG n 
1 248 PHE n 
1 249 ARG n 
1 250 SER n 
1 251 PHE n 
1 252 PRO n 
1 253 PHE n 
1 254 TRP n 
1 255 ARG n 
1 256 ARG n 
1 257 VAL n 
1 258 HIS n 
1 259 ASP n 
1 260 SER n 
1 261 PHE n 
1 262 ILE n 
1 263 GLU n 
1 264 ASP n 
1 265 LEU n 
1 266 GLU n 
1 267 HIS n 
1 268 HIS n 
1 269 HIS n 
1 270 HIS n 
1 271 HIS n 
1 272 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   272 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nadK1, lmo0968' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Listeria monocytogenes EGD-e' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     169963 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CIT non-polymer         . 'CITRIC ACID' ?                               'C6 H8 O7'       192.124 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'    181.189 
UQF non-polymer         . 
;1-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[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]amino]propyl]guanidine
;
?                               'C27 H36 N14 O7' 668.664 
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        UQF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UQF 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CIT 1  301 1  CIT CIT A . 
C 3 UQF 1  302 1  UQF XXX A . 
D 4 GOL 1  303 3  GOL GOL A . 
E 5 HOH 1  401 72 HOH HOH A . 
E 5 HOH 2  402 5  HOH HOH A . 
E 5 HOH 3  403 31 HOH HOH A . 
E 5 HOH 4  404 15 HOH HOH A . 
E 5 HOH 5  405 4  HOH HOH A . 
E 5 HOH 6  406 18 HOH HOH A . 
E 5 HOH 7  407 54 HOH HOH A . 
E 5 HOH 8  408 77 HOH HOH A . 
E 5 HOH 9  409 9  HOH HOH A . 
E 5 HOH 10 410 20 HOH HOH A . 
E 5 HOH 11 411 76 HOH HOH A . 
E 5 HOH 12 412 16 HOH HOH A . 
E 5 HOH 13 413 41 HOH HOH A . 
E 5 HOH 14 414 25 HOH HOH A . 
E 5 HOH 15 415 24 HOH HOH A . 
E 5 HOH 16 416 30 HOH HOH A . 
E 5 HOH 17 417 23 HOH HOH A . 
E 5 HOH 18 418 75 HOH HOH A . 
E 5 HOH 19 419 2  HOH HOH A . 
E 5 HOH 20 420 19 HOH HOH A . 
E 5 HOH 21 421 12 HOH HOH A . 
E 5 HOH 22 422 7  HOH HOH A . 
E 5 HOH 23 423 1  HOH HOH A . 
E 5 HOH 24 424 26 HOH HOH A . 
E 5 HOH 25 425 61 HOH HOH A . 
E 5 HOH 26 426 35 HOH HOH A . 
E 5 HOH 27 427 6  HOH HOH A . 
E 5 HOH 28 428 40 HOH HOH A . 
E 5 HOH 29 429 11 HOH HOH A . 
E 5 HOH 30 430 39 HOH HOH A . 
E 5 HOH 31 431 3  HOH HOH A . 
E 5 HOH 32 432 34 HOH HOH A . 
E 5 HOH 33 433 8  HOH HOH A . 
E 5 HOH 34 434 64 HOH HOH A . 
E 5 HOH 35 435 17 HOH HOH A . 
E 5 HOH 36 436 65 HOH HOH A . 
E 5 HOH 37 437 14 HOH HOH A . 
E 5 HOH 38 438 22 HOH HOH A . 
E 5 HOH 39 439 21 HOH HOH A . 
E 5 HOH 40 440 38 HOH HOH A . 
E 5 HOH 41 441 56 HOH HOH A . 
E 5 HOH 42 442 60 HOH HOH A . 
E 5 HOH 43 443 13 HOH HOH A . 
E 5 HOH 44 444 79 HOH HOH A . 
E 5 HOH 45 445 57 HOH HOH A . 
E 5 HOH 46 446 42 HOH HOH A . 
E 5 HOH 47 447 51 HOH HOH A . 
E 5 HOH 48 448 47 HOH HOH A . 
E 5 HOH 49 449 63 HOH HOH A . 
E 5 HOH 50 450 66 HOH HOH A . 
E 5 HOH 51 451 43 HOH HOH A . 
E 5 HOH 52 452 62 HOH HOH A . 
E 5 HOH 53 453 46 HOH HOH A . 
E 5 HOH 54 454 67 HOH HOH A . 
E 5 HOH 55 455 50 HOH HOH A . 
E 5 HOH 56 456 29 HOH HOH A . 
E 5 HOH 57 457 32 HOH HOH A . 
E 5 HOH 58 458 68 HOH HOH A . 
E 5 HOH 59 459 28 HOH HOH A . 
E 5 HOH 60 460 74 HOH HOH A . 
E 5 HOH 61 461 33 HOH HOH A . 
E 5 HOH 62 462 69 HOH HOH A . 
E 5 HOH 63 463 81 HOH HOH A . 
E 5 HOH 64 464 44 HOH HOH A . 
E 5 HOH 65 465 71 HOH HOH A . 
E 5 HOH 66 466 52 HOH HOH A . 
E 5 HOH 67 467 37 HOH HOH A . 
E 5 HOH 68 468 83 HOH HOH A . 
E 5 HOH 69 469 49 HOH HOH A . 
E 5 HOH 70 470 48 HOH HOH A . 
E 5 HOH 71 471 78 HOH HOH A . 
E 5 HOH 72 472 84 HOH HOH A . 
E 5 HOH 73 473 73 HOH HOH A . 
E 5 HOH 74 474 53 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
6  1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
7  1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
8  1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
9  1 Y 1 A LYS 108 ? CG  ? A LYS 108 CG  
10 1 Y 1 A LYS 108 ? CD  ? A LYS 108 CD  
11 1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
12 1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
13 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
14 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
15 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
16 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19.1_4122 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QG8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.937 
_cell.length_a_esd                 ? 
_cell.length_b                     74.559 
_cell.length_b_esd                 ? 
_cell.length_c                     118.508 
_cell.length_c_esd                 ? 
_cell.volume                       556101.138 
_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                         8QG8 
_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                   8QG8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.07 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-09-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979257 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979257 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          34.22 
_reflns.entry_id                                       8QG8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.29 
_reflns.d_resolution_low                               34.91 
_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                                     12817 
_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                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          40.07 
_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                                0.025 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.023 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.29 2.43  ? ? ? ? ? ? 2027 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.087                ? ? 1 1 0.996              ? ? ? ? 0.077 ? ? ? ? ? 
? ? ? ? 
2.43 2.6   ? ? ? ? ? ? 1903 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.065                ? ? 2 1 0.998              ? ? ? ? 
0.057999999999999996 ? ? ? ? ? ? ? ? ? 
2.60 2.81  ? ? ? ? ? ? 1789 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.049                ? ? 3 1 0.9990000000000001 ? ? ? ? 
0.044000000000000004 ? ? ? ? ? ? ? ? ? 
2.81 3.07  ? ? ? ? ? ? 1663 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.039                ? ? 4 1 0.9990000000000001 ? ? ? ? 0.035 ? ? ? ? ? 
? ? ? ? 
3.07 3.43  ? ? ? ? ? ? 1500 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 5 1 0.9990000000000001 ? ? ? ? 0.025 ? ? ? ? ? 
? ? ? ? 
3.43 3.96  ? ? ? ? ? ? 1342 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.022000000000000002 ? ? 6 1 1.0                ? ? ? ? 0.019 ? ? ? ? ? 
? ? ? ? 
3.96 4.84  ? ? ? ? ? ? 1153 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.017                ? ? 7 1 1.0                ? ? ? ? 0.015 ? ? ? ? ? 
? ? ? ? 
4.84 6.82  ? ? ? ? ? ? 900  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.017                ? ? 8 1 1.0                ? ? ? ? 0.015 ? ? ? ? ? 
? ? ? ? 
6.82 34.91 ? ? ? ? ? ? 540  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.015                ? ? 9 1 1.0                ? ? ? ? 
0.013999999999999999 ? ? ? ? ? ? ? ? ? 
# 
_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                               42.58 
_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                                 8QG8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.29 
_refine.ls_d_res_low                             34.91 
_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                     12806 
_refine.ls_number_reflns_R_free                  639 
_refine.ls_number_reflns_R_work                  12167 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.27 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1850 
_refine.ls_R_factor_R_free                       0.2268 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1828 
_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                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8A9V 
_refine.pdbx_stereochemistry_target_values       '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                 24.0601 
_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                            0.2441 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.29 
_refine_hist.d_res_low                        34.91 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               2215 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_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' ? 0.0104  ? 2221 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1588  ? 3011 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0688  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0071  ? 412  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7029 ? 838  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.29 2.47  . . 125 2381 98.43 . . . . 0.1858 . . . . . . . . . . . 0.2684 
'X-RAY DIFFRACTION' 2.47 2.72  . . 125 2395 99.21 . . . . 0.1901 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 2.72 3.11  . . 127 2405 99.45 . . . . 0.2141 . . . . . . . . . . . 0.2723 
'X-RAY DIFFRACTION' 3.11 3.92  . . 129 2447 99.84 . . . . 0.1798 . . . . . . . . . . . 0.2222 
'X-RAY DIFFRACTION' 3.92 34.91 . . 133 2539 99.40 . . . . 0.1705 . . . . . . . . . . . 0.1962 
# 
_struct.entry_id                     8QG8 
_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        8QG8 
_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              8QG8 
_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 8QG8 LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QG8 GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QG8 HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QG8 HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QG8 HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QG8 HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QG8 HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QG8 HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12470 ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  39620 ? 
# 
_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 62.9370000000 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 62.9370000000 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 TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA2 4 5 O GLN A 210 ? O GLN A 210 N ASP A 136 ? N ASP A 136 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA2 6 7 N SER A 155 ? N SER A 155 O GLN A 180 ? O GLN A 180 
AA2 7 8 N MET A 179 ? N MET A 179 O PHE A 201 ? O PHE A 201 
AA3 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA3 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA3 3 4 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA3 4 5 O GLN A 210 ? O GLN A 210 N ASP A 136 ? N ASP A 136 
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 VAL A 221 ? N VAL A 221 O LEU A 224 ? O LEU A 224 
# 
_pdbx_entry_details.entry_id                   8QG8 
_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 TYR A 109 ? ? -110.83 -168.55 
2  1 ASN A 122 ? ? -98.19  -69.44  
3  1 SER A 129 ? ? -95.19  43.01   
4  1 ALA A 162 ? ? -99.86  -129.38 
5  1 ASN A 189 ? ? -142.64 -150.86 
6  1 HIS A 204 ? ? 71.86   -2.58   
7  1 ASN A 213 ? ? -132.42 -86.62  
8  1 ASP A 222 ? ? 50.13   -124.66 
9  1 GLU A 233 ? ? -173.80 146.43  
10 1 GLU A 263 ? ? 173.89  160.03  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     408 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 13.2548722656 21.9306103756 15.393458706    0.290915009452 ? 0.0466168318066 ? 0.0101166140097 ? 
0.27245075317  ? -0.0319140895075 ? 0.325506043556 ? 1.9138647593  ? -0.880704172168 ? -2.04310873609 ? 1.30228867075 ? 
1.54886543191   ? 6.4141374695  ? 0.0122483079954 ? -0.297580212838 ? 0.247923474849  ? 0.182575309701   ? 0.025304889276   ? 
0.076140805316 ? -0.457956817657   ? -0.131190034354 ? -0.037518172283 ? 
2 'X-RAY DIFFRACTION' ? refined 20.783234769  13.3159393713 -0.576875927287 0.148485133952 ? 0.0285618686924 ? 0.0117805653513 ? 
0.184550023672 ? 0.0139655499894  ? 0.273584756857 ? 2.12211337089 ? -0.234527503339 ? 0.497200462815 ? 2.24586020102 ? 
-0.104323212962 ? 3.56381448896 ? 0.0353402870926 ? 0.0282109071694 ? 0.0282793984173 ? -0.0866409475674 ? -0.0299384093411 ? 
0.286022379458 ? -0.00831150526701 ? -0.290986981153 ? 0.0232811595323 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 1   ? A 138 A 141 ? ? 
;chain 'A' and (resid    1  through  141 )
;
2 'X-RAY DIFFRACTION' 2 A 139 A 142 ? A 261 A 264 ? ? 
;chain 'A' and (resid  142  through  264 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
GOL C1   C N N 158 
GOL O1   O N N 159 
GOL C2   C N N 160 
GOL O2   O N N 161 
GOL C3   C N N 162 
GOL O3   O N N 163 
GOL H11  H N N 164 
GOL H12  H N N 165 
GOL HO1  H N N 166 
GOL H2   H N N 167 
GOL HO2  H N N 168 
GOL H31  H N N 169 
GOL H32  H N N 170 
GOL HO3  H N N 171 
HIS N    N N N 172 
HIS CA   C N S 173 
HIS C    C N N 174 
HIS O    O N N 175 
HIS CB   C N N 176 
HIS CG   C Y N 177 
HIS ND1  N Y N 178 
HIS CD2  C Y N 179 
HIS CE1  C Y N 180 
HIS NE2  N Y N 181 
HIS OXT  O N N 182 
HIS H    H N N 183 
HIS H2   H N N 184 
HIS HA   H N N 185 
HIS HB2  H N N 186 
HIS HB3  H N N 187 
HIS HD1  H N N 188 
HIS HD2  H N N 189 
HIS HE1  H N N 190 
HIS HE2  H N N 191 
HIS HXT  H N N 192 
HOH O    O N N 193 
HOH H1   H N N 194 
HOH H2   H N N 195 
ILE N    N N N 196 
ILE CA   C N S 197 
ILE C    C N N 198 
ILE O    O N N 199 
ILE CB   C N S 200 
ILE CG1  C N N 201 
ILE CG2  C N N 202 
ILE CD1  C N N 203 
ILE OXT  O N N 204 
ILE H    H N N 205 
ILE H2   H N N 206 
ILE HA   H N N 207 
ILE HB   H N N 208 
ILE HG12 H N N 209 
ILE HG13 H N N 210 
ILE HG21 H N N 211 
ILE HG22 H N N 212 
ILE HG23 H N N 213 
ILE HD11 H N N 214 
ILE HD12 H N N 215 
ILE HD13 H N N 216 
ILE HXT  H N N 217 
LEU N    N N N 218 
LEU CA   C N S 219 
LEU C    C N N 220 
LEU O    O N N 221 
LEU CB   C N N 222 
LEU CG   C N N 223 
LEU CD1  C N N 224 
LEU CD2  C N N 225 
LEU OXT  O N N 226 
LEU H    H N N 227 
LEU H2   H N N 228 
LEU HA   H N N 229 
LEU HB2  H N N 230 
LEU HB3  H N N 231 
LEU HG   H N N 232 
LEU HD11 H N N 233 
LEU HD12 H N N 234 
LEU HD13 H N N 235 
LEU HD21 H N N 236 
LEU HD22 H N N 237 
LEU HD23 H N N 238 
LEU HXT  H N N 239 
LYS N    N N N 240 
LYS CA   C N S 241 
LYS C    C N N 242 
LYS O    O N N 243 
LYS CB   C N N 244 
LYS CG   C N N 245 
LYS CD   C N N 246 
LYS CE   C N N 247 
LYS NZ   N N N 248 
LYS OXT  O N N 249 
LYS H    H N N 250 
LYS H2   H N N 251 
LYS HA   H N N 252 
LYS HB2  H N N 253 
LYS HB3  H N N 254 
LYS HG2  H N N 255 
LYS HG3  H N N 256 
LYS HD2  H N N 257 
LYS HD3  H N N 258 
LYS HE2  H N N 259 
LYS HE3  H N N 260 
LYS HZ1  H N N 261 
LYS HZ2  H N N 262 
LYS HZ3  H N N 263 
LYS HXT  H N N 264 
MET N    N N N 265 
MET CA   C N S 266 
MET C    C N N 267 
MET O    O N N 268 
MET CB   C N N 269 
MET CG   C N N 270 
MET SD   S N N 271 
MET CE   C N N 272 
MET OXT  O N N 273 
MET H    H N N 274 
MET H2   H N N 275 
MET HA   H N N 276 
MET HB2  H N N 277 
MET HB3  H N N 278 
MET HG2  H N N 279 
MET HG3  H N N 280 
MET HE1  H N N 281 
MET HE2  H N N 282 
MET HE3  H N N 283 
MET HXT  H N N 284 
PHE N    N N N 285 
PHE CA   C N S 286 
PHE C    C N N 287 
PHE O    O N N 288 
PHE CB   C N N 289 
PHE CG   C Y N 290 
PHE CD1  C Y N 291 
PHE CD2  C Y N 292 
PHE CE1  C Y N 293 
PHE CE2  C Y N 294 
PHE CZ   C Y N 295 
PHE OXT  O N N 296 
PHE H    H N N 297 
PHE H2   H N N 298 
PHE HA   H N N 299 
PHE HB2  H N N 300 
PHE HB3  H N N 301 
PHE HD1  H N N 302 
PHE HD2  H N N 303 
PHE HE1  H N N 304 
PHE HE2  H N N 305 
PHE HZ   H N N 306 
PHE HXT  H N N 307 
PRO N    N N N 308 
PRO CA   C N S 309 
PRO C    C N N 310 
PRO O    O N N 311 
PRO CB   C N N 312 
PRO CG   C N N 313 
PRO CD   C N N 314 
PRO OXT  O N N 315 
PRO H    H N N 316 
PRO HA   H N N 317 
PRO HB2  H N N 318 
PRO HB3  H N N 319 
PRO HG2  H N N 320 
PRO HG3  H N N 321 
PRO HD2  H N N 322 
PRO HD3  H N N 323 
PRO HXT  H N N 324 
SER N    N N N 325 
SER CA   C N S 326 
SER C    C N N 327 
SER O    O N N 328 
SER CB   C N N 329 
SER OG   O N N 330 
SER OXT  O N N 331 
SER H    H N N 332 
SER H2   H N N 333 
SER HA   H N N 334 
SER HB2  H N N 335 
SER HB3  H N N 336 
SER HG   H N N 337 
SER HXT  H N N 338 
THR N    N N N 339 
THR CA   C N S 340 
THR C    C N N 341 
THR O    O N N 342 
THR CB   C N R 343 
THR OG1  O N N 344 
THR CG2  C N N 345 
THR OXT  O N N 346 
THR H    H N N 347 
THR H2   H N N 348 
THR HA   H N N 349 
THR HB   H N N 350 
THR HG1  H N N 351 
THR HG21 H N N 352 
THR HG22 H N N 353 
THR HG23 H N N 354 
THR HXT  H N N 355 
TRP N    N N N 356 
TRP CA   C N S 357 
TRP C    C N N 358 
TRP O    O N N 359 
TRP CB   C N N 360 
TRP CG   C Y N 361 
TRP CD1  C Y N 362 
TRP CD2  C Y N 363 
TRP NE1  N Y N 364 
TRP CE2  C Y N 365 
TRP CE3  C Y N 366 
TRP CZ2  C Y N 367 
TRP CZ3  C Y N 368 
TRP CH2  C Y N 369 
TRP OXT  O N N 370 
TRP H    H N N 371 
TRP H2   H N N 372 
TRP HA   H N N 373 
TRP HB2  H N N 374 
TRP HB3  H N N 375 
TRP HD1  H N N 376 
TRP HE1  H N N 377 
TRP HE3  H N N 378 
TRP HZ2  H N N 379 
TRP HZ3  H N N 380 
TRP HH2  H N N 381 
TRP HXT  H N N 382 
TYR N    N N N 383 
TYR CA   C N S 384 
TYR C    C N N 385 
TYR O    O N N 386 
TYR CB   C N N 387 
TYR CG   C Y N 388 
TYR CD1  C Y N 389 
TYR CD2  C Y N 390 
TYR CE1  C Y N 391 
TYR CE2  C Y N 392 
TYR CZ   C Y N 393 
TYR OH   O N N 394 
TYR OXT  O N N 395 
TYR H    H N N 396 
TYR H2   H N N 397 
TYR HA   H N N 398 
TYR HB2  H N N 399 
TYR HB3  H N N 400 
TYR HD1  H N N 401 
TYR HD2  H N N 402 
TYR HE1  H N N 403 
TYR HE2  H N N 404 
TYR HH   H N N 405 
TYR HXT  H N N 406 
UQF N1   N N N 407 
UQF C7   C Y N 408 
UQF C8   C Y N 409 
UQF N2   N N N 410 
UQF C9   C Y N 411 
UQF O1   O N N 412 
UQF C1   C N N 413 
UQF O5   O N N 414 
UQF C5   C N N 415 
UQF C6   C N N 416 
UQF N3   N N N 417 
UQF C4   C N N 418 
UQF O4   O N N 419 
UQF C3   C N N 420 
UQF O3   O N N 421 
UQF C2   C N N 422 
UQF N4   N Y N 423 
UQF N    N N N 424 
UQF C    C N N 425 
UQF O    O N N 426 
UQF C10  C Y N 427 
UQF C11  C Y N 428 
UQF C12  C N R 429 
UQF C13  C N R 430 
UQF C14  C N N 431 
UQF C15  C N S 432 
UQF C16  C N R 433 
UQF C17  C N N 434 
UQF C18  C N R 435 
UQF C19  C N R 436 
UQF C20  C N R 437 
UQF C21  C N S 438 
UQF C22  C Y N 439 
UQF C23  C Y N 440 
UQF C24  C Y N 441 
UQF C25  C Y N 442 
UQF C26  C Y N 443 
UQF N10  N Y N 444 
UQF N11  N Y N 445 
UQF N12  N Y N 446 
UQF N13  N N N 447 
UQF N5   N Y N 448 
UQF N6   N Y N 449 
UQF N7   N N N 450 
UQF N8   N Y N 451 
UQF N9   N Y N 452 
UQF O2   O N N 453 
UQF O6   O N N 454 
UQF H6   H N N 455 
UQF H7   H N N 456 
UQF H21  H N N 457 
UQF H9   H N N 458 
UQF H8   H N N 459 
UQF H29  H N N 460 
UQF H15  H N N 461 
UQF H14  H N N 462 
UQF H13  H N N 463 
UQF H12  H N N 464 
UQF H25  H N N 465 
UQF H11  H N N 466 
UQF H10  H N N 467 
UQF H4   H N N 468 
UQF H5   H N N 469 
UQF H16  H N N 470 
UQF H    H N N 471 
UQF H1   H N N 472 
UQF H20  H N N 473 
UQF H19  H N N 474 
UQF H22  H N N 475 
UQF H24  H N N 476 
UQF H27  H N N 477 
UQF H26  H N N 478 
UQF H2   H N N 479 
UQF H3   H N N 480 
UQF H28  H N N 481 
UQF H30  H N N 482 
UQF H32  H N N 483 
UQF H33  H N N 484 
UQF H35  H N N 485 
UQF H34  H N N 486 
UQF H18  H N N 487 
UQF H17  H N N 488 
UQF H23  H N N 489 
UQF H31  H N N 490 
VAL N    N N N 491 
VAL CA   C N S 492 
VAL C    C N N 493 
VAL O    O N N 494 
VAL CB   C N N 495 
VAL CG1  C N N 496 
VAL CG2  C N N 497 
VAL OXT  O N N 498 
VAL H    H N N 499 
VAL H2   H N N 500 
VAL HA   H N N 501 
VAL HB   H N N 502 
VAL HG11 H N N 503 
VAL HG12 H N N 504 
VAL HG13 H N N 505 
VAL HG21 H N N 506 
VAL HG22 H N N 507 
VAL HG23 H N N 508 
VAL HXT  H N N 509 
# 
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 
UQF N   C    sing N N 391 
UQF N1  C    doub N N 392 
UQF C   N2   sing N N 393 
UQF N2  C1   sing N N 394 
UQF C1  C2   sing N N 395 
UQF C2  C3   sing N N 396 
UQF C3  N3   sing N N 397 
UQF C4  N3   sing N N 398 
UQF C5  C4   sing N N 399 
UQF C6  C5   trip N N 400 
UQF C7  C6   sing N N 401 
UQF C7  N4   doub Y N 402 
UQF N4  C8   sing Y N 403 
UQF C8  C9   doub Y N 404 
UQF N5  C9   sing Y N 405 
UQF C10 N5   doub Y N 406 
UQF N6  C10  sing Y N 407 
UQF C11 N6   doub Y N 408 
UQF C8  C11  sing Y N 409 
UQF N7  C11  sing N N 410 
UQF C9  N8   sing Y N 411 
UQF N8  C7   sing Y N 412 
UQF C12 N8   sing N N 413 
UQF C12 O    sing N N 414 
UQF O   C13  sing N N 415 
UQF C14 C13  sing N N 416 
UQF O1  C14  sing N N 417 
UQF C13 C15  sing N N 418 
UQF O2  C15  sing N N 419 
UQF C15 C16  sing N N 420 
UQF C16 C12  sing N N 421 
UQF O3  C16  sing N N 422 
UQF N3  C17  sing N N 423 
UQF C17 C18  sing N N 424 
UQF C18 O4   sing N N 425 
UQF O4  C19  sing N N 426 
UQF C19 C20  sing N N 427 
UQF O5  C20  sing N N 428 
UQF C20 C21  sing N N 429 
UQF C18 C21  sing N N 430 
UQF C21 O6   sing N N 431 
UQF N9  C19  sing N N 432 
UQF N9  C22  sing Y N 433 
UQF C22 N10  doub Y N 434 
UQF N10 C23  sing Y N 435 
UQF C23 C24  doub Y N 436 
UQF C24 N9   sing Y N 437 
UQF N11 C24  sing Y N 438 
UQF C25 N11  doub Y N 439 
UQF N12 C25  sing Y N 440 
UQF C26 N12  doub Y N 441 
UQF C23 C26  sing Y N 442 
UQF N13 C26  sing N N 443 
UQF N1  H6   sing N N 444 
UQF N2  H7   sing N N 445 
UQF O1  H21  sing N N 446 
UQF C1  H9   sing N N 447 
UQF C1  H8   sing N N 448 
UQF O5  H29  sing N N 449 
UQF C4  H15  sing N N 450 
UQF C4  H14  sing N N 451 
UQF C3  H13  sing N N 452 
UQF C3  H12  sing N N 453 
UQF O3  H25  sing N N 454 
UQF C2  H11  sing N N 455 
UQF C2  H10  sing N N 456 
UQF N   H4   sing N N 457 
UQF N   H5   sing N N 458 
UQF C10 H16  sing N N 459 
UQF C12 H    sing N N 460 
UQF C13 H1   sing N N 461 
UQF C14 H20  sing N N 462 
UQF C14 H19  sing N N 463 
UQF C15 H22  sing N N 464 
UQF C16 H24  sing N N 465 
UQF C17 H27  sing N N 466 
UQF C17 H26  sing N N 467 
UQF C18 H2   sing N N 468 
UQF C19 H3   sing N N 469 
UQF C20 H28  sing N N 470 
UQF C21 H30  sing N N 471 
UQF C22 H32  sing N N 472 
UQF C25 H33  sing N N 473 
UQF N13 H35  sing N N 474 
UQF N13 H34  sing N N 475 
UQF N7  H18  sing N N 476 
UQF N7  H17  sing N N 477 
UQF O2  H23  sing N N 478 
UQF O6  H31  sing N N 479 
VAL N   CA   sing N N 480 
VAL N   H    sing N N 481 
VAL N   H2   sing N N 482 
VAL CA  C    sing N N 483 
VAL CA  CB   sing N N 484 
VAL CA  HA   sing N N 485 
VAL C   O    doub N N 486 
VAL C   OXT  sing N N 487 
VAL CB  CG1  sing N N 488 
VAL CB  CG2  sing N N 489 
VAL CB  HB   sing N N 490 
VAL CG1 HG11 sing N N 491 
VAL CG1 HG12 sing N N 492 
VAL CG1 HG13 sing N N 493 
VAL CG2 HG21 sing N N 494 
VAL CG2 HG22 sing N N 495 
VAL CG2 HG23 sing N N 496 
VAL OXT HXT  sing N N 497 
# 
_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                    8QG8 
_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]   0.015889 
_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]   0.013412 
_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]   0.008438 
_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   ? 11.66912 36.23763 25.15776  1.000 69.71444  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.71542 36.43626 24.07447  1.000 64.96340  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.60251  35.39485 24.12131  1.000 61.14591  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.44939  34.67266 25.09649  1.000 57.37949  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.41982 36.35689 22.71701  1.000 65.81286  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.55736 37.33083 22.50099  0.700 64.89162  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 13.72864 36.54697 21.39123  0.600 68.33375  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 14.37691 35.29340 22.47629  0.600 64.42579  ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 8.82945  35.31974 23.04419  1.000 60.71209  ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 7.93256  34.19054 22.85207  1.000 58.19617  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.74240  32.91550 22.60655  1.000 49.64203  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.75511  32.93633 21.90012  1.000 47.05284  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 6.98442  34.47975 21.68897  1.000 56.99187  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.11577  35.70690 21.91864  1.000 61.39205  ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.06979  35.86183 20.83467  1.000 64.59434  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 3.98737  36.85732 21.21672  1.000 66.09858  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 4.49708  38.25386 21.37277  1.000 72.34116  ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.31254  31.81217 23.23230  1.000 48.42583  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 8.97676  30.51462 23.12302  1.000 44.70729  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.91349  29.42577 23.15272  1.000 44.10127  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.76292  29.67035 23.51285  1.000 46.58804  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 9.99544  30.27940 24.25149  1.000 42.04613  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.33701  29.91133 25.58510  1.000 46.27737  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.83470  30.89999 26.42698  1.000 48.16262  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.21606  28.58371 25.99166  1.000 41.27708  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.22479  30.58166 27.63976  1.000 48.89452  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.60323  28.25417 27.19918  1.000 43.21642  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.11073  29.26153 28.02059  1.000 45.08953  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.49993  28.94947 29.20998  1.000 42.87406  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.30957  28.20973 22.77569  1.000 41.11083  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.46436  27.03664 22.96765  1.000 40.91949  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.37611  25.83267 23.10010  1.000 35.95955  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.56462  25.90040 22.79656  1.000 34.81171  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.45353  26.83883 21.82668  1.000 40.69232  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.06977  26.33661 20.52934  1.000 40.15706  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.34025  24.53973 20.49345  1.000 41.00859  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.72721  24.01226 21.11778  1.000 42.21477  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.80065  24.71495 23.54113  1.000 36.04119  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.56156  23.51340 23.87507  1.000 37.30033  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.78273  22.30396 23.37174  1.000 38.19907  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.65495  22.07620 23.81980  1.000 39.96414  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.81266  23.38154 25.39453  1.000 35.45561  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.54074  24.61293 25.94492  1.000 36.22003  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.60005  22.10580 25.69711  1.000 32.68388  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.90551  24.53508 27.42842  1.000 39.04906  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.37806  21.51559 22.46555  1.000 34.68467  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.78059  20.24189 22.08964  1.000 36.61869  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.41807  19.13468 22.91471  1.000 36.40183  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.57075  19.22918 23.34171  1.000 37.13770  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 7.90757  19.91908 20.57264  1.000 40.42849  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 9.27978  19.84576 20.14980  1.000 40.21849  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.22998  20.95688 19.72369  1.000 38.83059  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.64010  18.09578 23.17200  1.000 39.30618  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 8.10538  16.93653 23.91268  1.000 37.42893  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.89647  15.67105 23.09450  1.000 39.64985  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.92675  15.55292 22.33943  1.000 40.40244  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.35652  16.80813 25.24670  1.000 38.12789  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.70761  15.61868 25.91420  1.000 37.92659  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.81201  14.71439 23.25749  1.000 39.04948  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.59598  13.38196 22.69620  1.000 41.88808  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.33965  12.72876 23.27673  1.000 42.96432  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.75233  11.84086 22.65397  1.000 44.86328  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.84520  12.52520 22.93819  1.000 43.61309  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.70364  11.02864 22.73249  1.000 44.62218  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.85715 10.31133 23.41338  1.000 45.16779  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.91850 8.86825  22.99920  1.000 51.03393  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 10.88708 8.77669  21.51805  1.000 58.39736  ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.90148  13.14363 24.45292  1.000 42.65424  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.63536  12.64438 24.95048  1.000 44.11232  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.71774  11.41988 25.83124  1.000 48.32584  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.67440  10.85783 26.17425  1.000 54.18591  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.91313  10.97422 26.18654  1.000 45.18128  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.06349  10.04612 27.29196  1.000 50.16650  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.15205  10.83923 28.59436  1.000 50.92379  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.27034  12.06864 28.58699  1.000 48.52841  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.30200  9.16358  27.09075  1.000 50.59767  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.58852  9.96876  26.99828  1.000 52.18011  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.52198  11.20905 26.92426  1.000 50.70746  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.67868 9.36121  27.01071  1.000 65.16233  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.10710  10.12515 29.72814  1.000 52.66559  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.04072  10.80604 31.02343  1.000 50.67959  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.27340  11.67423 31.27900  1.000 48.01465  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.15506  12.81003 31.75141  1.000 44.66022  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 6.85902  9.78840  32.15570  1.000 57.64764  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.54098  9.01567  32.10905  0.700 58.21445  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.29329  8.18217  33.35347  0.600 61.10504  ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 5.55052  8.67539  34.46993  0.600 63.37893  ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 4.83921  7.02700  33.21666  0.600 63.80511  ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.46630  11.15947 30.98223  1.000 50.29517  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.68035 11.94578 31.18845  1.000 47.96757  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.58663 13.29705 30.48497  1.000 44.01717  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.80880 14.35092 31.09871  1.000 43.30109  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.89427 11.15652 30.69883  1.000 51.39828  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.22624 11.69549 31.15194  0.800 51.46487  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.34665 10.85085 30.59398  0.700 54.05220  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.66248 11.14084 31.29947  0.600 57.41295  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 16.14982 12.52647 31.02823  0.600 57.32705  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.20086 13.29084 29.20794  1.000 48.23211  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.25442 14.50941 28.40093  1.000 42.26789  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.14669  15.48203 28.77632  1.000 42.19214  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.37667  16.69642 28.83710  1.000 39.98763  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.17364 14.15294 26.91921  1.000 44.45037  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.09281 13.11811 26.58947  1.000 43.60004  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.93816  14.97149 29.03270  1.000 41.91245  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.85282  15.83294 29.49559  1.000 43.88133  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.21482  16.55561 30.78376  1.000 41.71933  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.93122  17.75283 30.93771  1.000 37.38143  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.57898  15.01644 29.71253  1.000 43.39835  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.91170  14.67569 28.42142  1.000 46.28045  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.47166  15.06054 27.37450  1.000 40.75952  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.83894  14.04290 28.45052  1.000 51.00876  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.81003  15.83772 31.73363  1.000 41.49711  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.06337  16.45756 33.02775  1.000 43.04806  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.21588  17.44343 32.92987  1.000 40.34608  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.19870  18.48970 33.59446  1.000 40.86126  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.32401  15.39733 34.09810  1.000 42.19115  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.05036  15.17311 34.92508  0.700 52.57752  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 5.94496  14.55702 34.04748  0.700 51.39988  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 7.28620  14.36201 36.21171  0.700 51.21906  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.19758 17.16006 32.07661  1.000 38.02811  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.23872 18.15381 31.87210  1.000 38.45846  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.65965 19.39733 31.19111  1.000 37.99072  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 11.00907 20.52737 31.54002  1.000 37.29808  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.39241 17.53129 31.07557  1.000 39.33415  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.62554 18.39714 30.83642  1.000 38.89154  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.23228 18.86341 32.15552  1.000 38.31616  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.67237 17.66251 29.94395  1.000 40.12661  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.71952  19.21736 30.26476  1.000 36.94158  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.05693  20.38115 29.67856  1.000 37.71100  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.30458  21.18207 30.74933  1.000 36.30857  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.45946  22.40673 30.85564  1.000 36.73182  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.12885  19.93368 28.54887  1.000 34.04581  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.19984  21.00573 28.01777  1.000 34.76978  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.45309  20.45616 26.79801  1.000 36.28410  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.50291  21.40528 26.24813  1.000 33.92055  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.32117  21.65870 26.78896  1.000 35.01322  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.94210  21.07455 27.91007  1.000 36.14815  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.49879  22.52041 26.18762  1.000 35.62306  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.50268  20.51147 31.57322  1.000 37.27483  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.79674  21.23307 32.64262  1.000 38.85579  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.76486  21.98862 33.55578  1.000 39.56253  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.49561  23.13335 33.94468  1.000 40.32475  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.92376  20.27885 33.46232  1.000 40.18802  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.64841  19.75744 32.78068  1.000 40.80096  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.63988  19.23315 33.81763  1.000 42.35843  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 4.00627  20.83629 31.90690  1.000 40.22200  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.91596  21.40097 33.87779  1.000 39.67245  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.83721  22.13291 34.74686  1.000 40.82281  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.46094 23.33670 34.04818  1.000 40.24081  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.67648 24.37374 34.68988  1.000 41.50281  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.92805 21.22116 35.28452  1.000 41.57961  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.49371 20.49929 36.51512  1.000 43.31680  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.51640  20.88720 37.15729  1.000 44.13430  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.21270 19.45976 36.87053  1.000 44.16634  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.79233 23.21826 32.75367  1.000 38.61258  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.36886 24.36311 32.06094  1.000 38.36002  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.33904 25.46888 31.90111  1.000 38.76775  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.65187 26.65136 32.07887  1.000 44.46156  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.94086 23.94105 30.69651  1.000 38.93034  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.22942 23.19601 30.79906  1.000 38.81385  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.92915 22.78691 29.19203  1.000 37.68332  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.67478 24.33392 28.70382  1.000 40.61797  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.09897  25.11106 31.58885  1.000 38.22939  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.03985  26.11316 31.54554  1.000 39.05709  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 7.95511  26.85661 32.87540  1.000 41.00526  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.85914  28.09046 32.91885  1.000 42.15315  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.70537  25.45349 31.16582  1.000 38.69065  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.76317  24.98364 29.70667  1.000 39.33222  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.59884  26.45261 31.30309  1.000 43.29572  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.53012  24.24367 29.28009  1.000 38.83867  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.00262  26.11753 33.98147  1.000 41.65372  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 7.95142  26.76041 35.29370  1.000 43.61742  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.13238  27.70843 35.47907  1.000 44.53802  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 8.96638  28.84637 35.92890  1.000 46.12820  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.91721  25.70325 36.39555  1.000 44.28343  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.33347 27.26860 35.09163  1.000 43.82017  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.49506 28.13491 35.21927  1.000 45.04311  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.40641 29.37157 34.34205  1.000 47.10460  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.86898 30.45248 34.72312  1.000 47.77866  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.82399 29.22552 33.14674  1.000 43.89071  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.61738 30.37738 32.27746  1.000 47.45541  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.64260  31.38000 32.88036  1.000 50.51812  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.78774  32.59158 32.66586  1.000 52.77075  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.11540 29.91836 30.91118  1.000 45.17259  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.19871 29.45115 29.99640  1.000 46.11144  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.30759 30.25163 29.75394  1.000 49.36825  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.10809 28.21681 29.35904  1.000 42.94117  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.30625 29.82709 28.88007  1.000 52.77127  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.09278 27.78612 28.50003  1.000 43.89490  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.19663 28.58302 28.25536  1.000 47.46956  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.64313  30.90570 33.62688  1.000 49.66858  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.69840  31.82259 34.22362  1.000 47.92992  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.34035  32.80928 35.17904  1.000 56.29855  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.73387  33.83143 35.50189  1.000 52.29360  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.56171  32.53449 35.63396  1.000 56.07444  ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.27153 33.46588 36.50077  1.000 57.48466  ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.04400 34.50969 35.71454  1.000 61.80665  ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.86072 35.22028 36.30602  1.000 72.93251  ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.22901 32.71452 37.43193  1.000 55.26766  ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.61489 31.50398 38.12122  1.000 52.53245  ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.55074  31.88093 39.12878  1.000 57.66833  ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 9.42049  33.08735 39.44757  1.000 59.69234  ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.83833  30.96673 39.61053  1.000 62.57979  ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 10.80628 34.61582 34.40248  1.000 57.50269  ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.45282 35.61637 33.56246  1.000 61.39596  ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.41960 36.25597 32.63907  1.000 62.99052  ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.25458  35.85677 32.59700  1.000 62.38775  ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.59799 35.00913 32.73064  1.000 59.67028  ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.75687 34.42693 33.53215  1.000 58.96521  ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 14.80942 35.23218 33.95505  1.000 61.78817  ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 13.81256 33.07071 33.84414  1.000 54.88438  ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 15.87688 34.71248 34.67855  1.000 57.50519  ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 14.88040 32.53775 34.56510  1.000 51.99419  ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 15.91061 33.36611 34.97181  1.000 56.07643  ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 16.97532 32.85802 35.68589  1.000 58.96668  ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 10.86145 37.26051 31.88255  1.000 66.92443  ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.01419 37.86681 30.86172  1.000 72.50535  ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 9.93732  36.93596 29.66495  1.000 73.92023  ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.39750 37.27436 28.56962  1.000 73.52224  ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.54100 39.23814 30.42766  1.000 80.33065  ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.49143  40.06120 29.68668  1.000 88.81587  ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 8.38659  39.53303 29.42137  1.000 86.06910  ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 9.76574  41.24268 29.38106  1.000 98.82691  ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.37895  35.74956 29.87917  1.000 70.26606  ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.20818  34.75097 28.83977  1.000 63.53503  ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.73723  34.39454 28.76985  1.000 62.10206  ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.11064  34.11871 29.79995  1.000 63.68194  ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.04835 33.51040 29.12134  1.000 59.04932  ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.54544 33.79512 29.15618  1.000 63.33672  ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.30452 34.32953 27.60105  1.000 69.16488  ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 12.39122 32.79252 26.67001  1.000 62.59881  ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.19163  34.41874 27.56314  1.000 59.09982  ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.79378  34.10973 27.31588  1.000 58.29209  ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.70898  32.86472 26.43851  1.000 53.59363  ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.31267  32.82292 25.36342  1.000 53.23670  ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.11146  35.29908 26.64792  1.000 60.27290  ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.77915  34.98208 26.04614  1.000 63.22044  ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.31829  36.05931 25.09049  1.000 71.73718  ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 4.04118  37.07204 24.92088  1.000 72.38630  ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.23296  35.88067 24.50338  1.000 80.16655  ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 4.99070  31.84390 26.91158  1.000 50.57774  ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.76001  30.63991 26.12021  1.000 49.09710  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.78534  30.95770 24.98895  1.000 48.85773  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.62821  31.28989 25.25451  1.000 47.95959  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.19724  29.51941 26.99783  1.000 44.34861  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.14803  28.17228 26.30008  1.000 46.90184  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.14693  27.84928 25.36228  1.000 45.59022  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.11470  27.22172 26.55925  1.000 44.77104  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.13503  26.60575 24.71542  1.000 39.97431  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.11035  25.99514 25.91753  1.000 42.28468  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.12199  25.68543 25.00473  1.000 40.17249  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.16458  24.43221 24.41052  1.000 38.99678  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.24362  30.86889 23.73292  1.000 46.89321  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.37094  31.06131 22.56829  1.000 47.65941  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.79583  30.04821 21.52296  1.000 46.79304  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 4.91220  30.12478 21.00209  1.000 46.53049  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.45285  32.49151 22.01903  1.000 54.20893  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.64365  32.70921 20.69676  1.000 56.75775  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.34389  31.75367 19.93181  1.000 54.19672  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.32121  33.88027 20.40026  1.000 60.36139  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 2.91480  29.10813 21.20361  1.000 46.34832  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.23518  28.14237 20.16956  1.000 47.76406  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.66609  28.51656 18.80609  1.000 47.89591  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.63796  27.66687 17.91826  1.000 49.63269  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.77989  26.73876 20.58424  1.000 45.25977  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.28471  26.60632 20.67353  1.000 47.99114  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.56012  27.49799 20.18171  1.000 48.45930  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.82713  25.59097 21.23689  1.000 44.40043  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.19717  29.74585 18.61733  1.000 49.30213  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.78540  30.21009 17.29401  1.000 51.44432  ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 2.89508  30.99695 16.61231  1.000 52.54577  ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.22058  30.75409 15.45369  1.000 53.71047  ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.48661  31.03988 17.37511  1.000 51.21987  ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.19027  31.63290 16.01597  1.000 51.18985  ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.65652 30.16504 17.80318  1.000 50.40841  ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.48992  31.95256 17.31603  1.000 53.28456  ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.60470  32.73411 16.78371  1.000 54.38242  ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.76406  32.77270 17.77801  1.000 52.01149  ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.18523  33.84553 18.21516  1.000 55.76077  ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.13086  34.14346 16.43337  1.000 57.54014  ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.16791  34.18437 15.25765  0.700 60.55239  ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.70845  35.58151 14.93796  0.600 63.67041  ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 2.58797  36.40301 15.87425  0.600 60.94049  ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 2.47718  35.85446 13.74344  0.600 68.12670  ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.32011  31.62108 18.14459  1.000 49.73288  ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.51823  31.63063 18.98816  1.000 50.70788  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.73080  32.19181 18.26286  1.000 47.18808  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.80610  32.22509 17.04104  1.000 51.39070  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.72691  30.15138 19.32638  1.000 46.93814  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.01871  29.41796 18.26552  1.000 46.20802  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 5.84916  30.24488 17.90185  1.000 47.25313  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.68506  32.67029 19.04335  1.000 47.39479  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.00850 32.98221 18.52163  1.000 45.85455  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.03815 31.95768 18.95315  1.000 42.89452  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.11266 31.88398 18.35603  1.000 41.92933  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.45788 34.37649 18.98876  1.000 50.34466  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.44434 35.47529 18.71680  0.700 53.57594  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 10.94068 36.85359 19.13164  0.600 59.36590  ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 11.94872 37.32226 18.56360  0.600 61.92916  ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.32638 37.46494 20.02894  0.600 55.52023  ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.72348 31.17219 19.98172  1.000 44.41177  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.57240 30.09980 20.46269  1.000 38.45298  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.73941 28.83163 20.50389  1.000 37.03424  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.64506 28.81543 21.07640  1.000 40.03564  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.16546 30.42736 21.84349  1.000 39.42522  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 13.97339 31.71824 21.75612  1.000 46.18191  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 14.07560 29.32369 22.31147  1.000 40.33016  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.17953 31.62161 20.82293  1.000 49.10135  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.24323 27.78416 19.87302  1.000 35.75118  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.60431 26.47984 19.83994  1.000 34.68923  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.58003 25.49554 20.47783  1.000 34.42191  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.70662 25.33221 19.99961  1.000 33.39778  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.23841 26.06787 18.40166  1.000 33.69371  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.87241 24.61700 18.35385  1.000 34.56204  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.07832 26.92699 17.87284  1.000 37.07659  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.17532 24.90577 21.59708  1.000 33.01214  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.95369 23.90591 22.31497  1.000 34.62828  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.29022 22.56752 22.07206  1.000 32.98833  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.07918 22.42425 22.26778  1.000 34.22791  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 13.00892 24.19389 23.82730  1.000 38.07664  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.58522 25.57618 24.08731  1.000 37.11082  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.77171 23.07110 24.58792  1.000 32.42708  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.54230 25.92725 25.53185  1.000 38.45640  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.08207 21.58940 21.70702  1.000 31.18105  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.60177 20.27361 21.37127  1.000 30.69699  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.19309 19.30002 22.37529  1.000 33.60799  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.41302 19.29069 22.58620  1.000 33.06716  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.03922 19.94079 19.93884  1.000 32.26273  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.89750 18.57785 19.68110  1.000 33.78011  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.35310 18.49374 23.01358  1.000 33.51803  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.83175 17.60951 24.07622  1.000 34.14377  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.51208 16.17463 23.68588  1.000 36.42601  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.34113 15.80814 23.51845  1.000 36.98511  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.23196 17.96532 25.44407  1.000 34.06243  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.56993 19.40901 25.83795  1.000 32.05195  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.72151 16.96393 26.54272  1.000 37.94691  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 12.01923 19.78759 27.24360  1.000 31.67752  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.54500 15.36628 23.53957  1.000 35.43398  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.35332 14.06340 22.94429  1.000 38.45417  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.59524 13.67076 22.18238  1.000 39.14923  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.69882 13.74655 22.71394  1.000 44.03625  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.44615 13.25097 20.94159  1.000 38.25751  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.60855 12.85268 20.18930  1.000 35.47590  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.60548 13.61259 18.88814  1.000 33.09756  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.91460 14.62421 18.78341  1.000 31.74068  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.34046 13.10867 17.89205  1.000 32.82676  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.38856 13.75276 16.58794  1.000 32.31027  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 15.04647 13.69940 15.87680  1.000 29.25767  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.70413 14.61918 15.11623  1.000 31.04088  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.47490 13.09681 15.73199  1.000 33.74475  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.86055 13.40243 16.24530  1.000 33.46126  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 19.03822 14.50564 16.79760  1.000 36.14311  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.75975 12.55628 16.11014  1.000 32.66666  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.30270 12.60596 16.04507  1.000 30.37457  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.95769 12.55115 15.48550  1.000 28.95531  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 12.04588 13.63258 16.04102  1.000 32.30681  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.29892 14.26902 15.29166  1.000 29.89952  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 12.12583 13.88732 17.36609  1.000 31.71054  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.36766 14.98924 17.95867  1.000 30.76117  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.84217 16.31909 17.38589  1.000 28.52874  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 11.03062 17.18544 17.05361  1.000 30.09688  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.49758 14.98339 19.50528  1.000 33.76410  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.16983 13.68788 20.02157  1.000 36.73566  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.60581 16.02860 20.14450  1.000 31.16028  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.15228 16.49954 17.25369  1.000 27.34124  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.65920 17.74431 16.66800  1.000 28.10565  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.20788 17.92142 15.21108  1.000 31.08255  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.76757 19.00929 14.81871  1.000 31.05332  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.18429 17.80114 16.76384  1.000 30.18533  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.75121 19.16529 16.42772  1.000 33.27844  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 16.00846 19.52073 15.10242  1.000 31.13179  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.99109 20.10312 17.42837  1.000 30.95717  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.50145 20.78777 14.78233  1.000 31.14497  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.49392 21.37388 17.11077  1.000 35.29449  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.74903 21.71503 15.77637  1.000 32.64195  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.26851 16.85914 14.39790  1.000 30.24318  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.77476 16.95998 13.01721  1.000 29.62888  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.30030 17.34897 12.96713  1.000 30.29305  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.87489 18.09047 12.07019  1.000 27.32943  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.98684 15.64058 12.28364  1.000 27.44501  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.42333 15.40432 11.83636  1.000 29.27292  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.55067 14.01964 11.24878  1.000 32.62865  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.73173 16.40526 10.78171  1.000 30.98167  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.49568 16.84212 13.90673  1.000 30.27479  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 9.08577  17.23939 13.93478  1.000 32.44379  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.94284  18.72295 14.20675  1.000 31.77282  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.09987  19.39261 13.60097  1.000 32.74666  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.30783  16.45215 14.99750  1.000 33.28667  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.01957  15.16499 14.49782  1.000 41.01284  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.76382  19.25100 15.12284  1.000 33.86298  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.65904  20.65274 15.50378  1.000 32.74274  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.06205 21.55839 14.35554  1.000 30.79134  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.45807  22.61467 14.15017  1.000 32.23121  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.53825 20.92830 16.72632  1.000 30.34201  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.10662 21.18182 13.62774  1.000 30.16935  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.46780 21.91621 12.41514  1.000 34.23875  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.29070 22.01001 11.45790  1.000 32.06405  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 9.95509  23.09437 10.97719  1.000 32.71105  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.65401 21.23703 11.73090  1.000 33.12027  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 12.97035 21.79457 10.37929  1.000 30.92772  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.60113 23.02109 10.24894  1.000 33.41773  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.66693 21.08202 9.24918   1.000 30.32419  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.91979 23.52592 8.98733   1.000 31.98024  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 12.96525 21.57464 8.00601   1.000 32.10126  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.59716 22.79208 7.87610   1.000 32.40076  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.61108  20.88843 11.21815  1.000 33.24289  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.53567  20.88841 10.22634  1.000 35.46151  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.28258  21.57669 10.74350  1.000 39.29842  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.57172  22.20662 9.95675   1.000 39.83564  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.24497  19.46336 9.76252   1.000 31.34825  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.30400  18.93889 8.84466   1.000 35.41944  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.44633  19.39006 7.55042   1.000 36.90116  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.32805 18.08192 9.05820   1.000 33.04540  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.48717 18.79735 6.99367   1.000 34.25669  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.04225 18.00428 7.88778   1.000 34.34141  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.00409  21.49323 12.05392  1.000 37.22137  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 5.89789  22.26733 12.61338  1.000 38.76644  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.05138  23.75218 12.31932  1.000 38.98158  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.05379  24.44833 12.12698  1.000 42.92773  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.78487  22.07116 14.14019  1.000 38.94976  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 5.12787  20.80458 14.60709  0.800 38.68812  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 5.20537  20.61458 16.11210  0.700 44.92376  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.69978  19.58516 16.59657  0.700 47.34686  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 4.73412  21.60902 16.86482  0.700 41.36482  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.28233  24.26374 12.29477  1.000 40.35434  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.49525  25.70411 12.18576  1.000 41.31508  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.29778  26.09396 10.94925  1.000 40.28411  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 8.91831  27.15840 10.93126  1.000 40.80628  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.16815  26.24643 13.44143  1.000 40.24153  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.28467  26.12552 14.65544  1.000 43.50057  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.31424  27.08516 14.94505  1.000 43.22633  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.40332  25.04359 15.49305  1.000 39.28991  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.49590  26.95252 16.06548  1.000 46.20358  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.59981  24.90073 16.59751  1.000 43.26446  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.65263  25.84567 16.88573  1.000 45.51506  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.87741  25.65410 18.01177  1.000 47.92141  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.24476  25.27532 9.89207   1.000 41.59006  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.05732  25.53441 8.69488   1.000 46.37510  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.67100  26.82488 7.97249   1.000 45.61701  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.47075  27.34977 7.19158   1.000 46.39602  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 8.97763  24.34798 7.71929   1.000 42.90069  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.56575  24.00951 7.28396   1.000 49.82008  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.46556  22.73319 6.45639   1.000 62.23285  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.38851  21.87909 6.50413   1.000 46.24930  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 6.43694  22.58992 5.75992   1.000 78.29623  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.48370  27.35964 8.20969   1.000 46.80352  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.11853  28.61612 7.57480   1.000 49.67931  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.59166  29.84539 8.34399   1.000 45.79145  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.37127  30.96319 7.88027   1.000 44.40454  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.60413  28.68134 7.35791   1.000 52.25501  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.16184  27.92463 6.10728   0.800 55.60805  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 4.17542  26.82624 6.41866   0.700 61.08335  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 3.03675  27.14671 6.82699   0.700 64.09692  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 4.54031  25.64252 6.25851   0.700 62.20062  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.26709  29.68160 9.47691   1.000 47.09821  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.80711  30.81155 10.24262  1.000 48.60048  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.25492 30.54122 10.63359  1.000 48.01722  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.72088 30.92832 11.71066  1.000 48.05480  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 7.93930  31.13039 11.46575  1.000 45.90058  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.78888  32.09644 11.10658  1.000 51.70766  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.90642  32.57376 12.28280  1.000 50.83137  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.57530  33.49976 13.19025  1.000 53.83594  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.15012  33.12916 14.33185  1.000 54.16073  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.19303  31.85698 14.70378  1.000 49.28112  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.68872  34.05656 15.12498  1.000 54.29766  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 10.98759 29.88951 9.72758   1.000 46.22302  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.38308 29.53971 9.97258   1.000 44.92161  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.23961 30.75229 10.28392  1.000 46.36299  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.14916 30.67646 11.11631  1.000 49.32691  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 12.95341 28.83129 8.76048   1.000 42.35345  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.36940 27.44716 8.63701   1.000 44.44632  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.00827 26.75694 7.44210   1.000 37.70514  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.59089 26.69702 9.97335   1.000 38.61358  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.00551 31.86097 9.60198   1.000 45.97075  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 13.89693 32.99369 9.77917   1.000 52.05355  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.64117 33.75457 11.07582  1.000 51.50470  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.53125 34.48013 11.52935  1.000 55.08651  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.79259 33.94137 8.58051   1.000 55.52028  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 15.15785 34.35101 8.04879   1.000 59.47548  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 15.95915 33.44738 7.71725   1.000 57.74183  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.43318 35.56828 7.95980   1.000 70.41087  ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.46459 33.60266 11.68981  1.000 50.94344  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.12534 34.28786 12.93690  1.000 49.60796  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.39846 33.43653 14.17758  1.000 46.86416  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.14640 33.89364 15.29272  1.000 49.51252  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 10.64428 34.71135 12.93009  1.000 50.60662  ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.27324 35.91448 12.05141  0.800 53.31514  ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 10.08126 35.55101 10.58480  0.700 56.70723  ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 9.31134  34.60896 10.29418  0.700 56.28680  ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 10.70719 36.20211 9.71674   0.700 58.59728  ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 12.91932 32.22301 14.01424  1.000 47.40726  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 12.99024 31.22362 15.07690  1.000 44.68741  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.42720 30.73485 15.23410  1.000 43.96874  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.11487 30.48019 14.23405  1.000 39.57844  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.05827 30.03263 14.74866  1.000 42.95008  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.58735 30.43135 14.89162  1.000 43.78395  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.41215 28.79175 15.56452  1.000 39.06408  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.65352  29.27865 14.64793  1.000 45.16190  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 14.88083 30.59736 16.48721  1.000 40.13549  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.07114 29.80645 16.81909  1.000 37.68503  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.66087 28.52337 17.53853  1.000 36.72583  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 14.84130 28.56727 18.46366  1.000 40.52066  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.04744 30.60248 17.69238  1.000 38.20981  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.25910 27.39979 17.14604  1.000 36.34387  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 15.94551 26.06668 17.64806  1.000 35.21334  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 16.99950 25.58033 18.64572  1.000 37.19634  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.18107 25.91647 18.54381  1.000 37.82410  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.86145 25.04150 16.50283  1.000 33.03873  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.67395 25.21240 15.58502  1.000 34.18505  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 14.74366 26.04510 14.47145  1.000 34.54884  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.51390 24.47812 15.78718  1.000 35.30560  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.66134 26.17964 13.60870  1.000 35.62948  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.41624 24.62181 14.92640  1.000 34.77387  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.49911 25.47408 13.83171  1.000 34.37959  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.55776 24.75381 19.60084  1.000 35.10004  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.42507 24.10928 20.59859  1.000 34.36452  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.87681 22.71296 20.84917  1.000 34.28063  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.66508 22.53518 21.00654  1.000 36.13580  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.49615 24.88093 21.94434  1.000 38.55561  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 18.09212 26.26821 21.75760  1.000 44.49551  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.31150 24.09219 23.01463  1.000 36.94302  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.04818 27.34678 21.78648  1.000 47.34254  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.74389 21.72492 20.90408  1.000 35.97856  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.33527 20.36233 21.16924  1.000 35.23802  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 17.91865 19.87059 22.47935  1.000 40.71322  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.09423 20.08956 22.77454  1.000 40.36336  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.08249 19.19700 23.25090  1.000 39.07961  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.49304 18.54090 24.47584  1.000 37.08447  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.28974 17.05457 24.25442  1.000 39.02539  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.19363 16.64139 23.86715  1.000 39.52817  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.67026 19.05861 25.66930  1.000 36.45235  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 16.95048 20.55924 25.82930  1.000 35.63906  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 16.95759 18.21156 26.91274  1.000 37.37839  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.13902 21.27138 26.85139  1.000 34.27701  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.32521 16.25184 24.47211  1.000 39.42385  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.18772 14.80955 24.28266  1.000 46.64597  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.88032 14.15400 25.61664  1.000 46.26894  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.71891 14.15825 26.51763  1.000 48.60761  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.41857 14.16582 23.62333  1.000 51.93674  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.69121 14.26918 24.40016  1.000 47.99049  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.08896 13.31501 25.31274  1.000 55.17769  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.68125 15.19281 24.36882  1.000 50.29521  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.25748 13.65838 25.82970  1.000 52.02137  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.64109 14.79367 25.27174  1.000 52.85259  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.68467 13.57368 25.73461  1.000 45.98767  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.37420 12.83314 26.95099  1.000 55.41898  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.80714 11.37224 26.88356  1.000 60.87647  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 17.00659 10.74973 27.93610  1.000 66.30776  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.88253 12.93548 27.32444  1.000 48.90306  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.03934 12.83181 26.16983  1.000 46.54738  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.63407 14.25779 28.02720  1.000 49.61524  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 16.99725 10.83091 25.68926  1.000 68.60005  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.70370 9.57633  25.46107  1.000 65.20881  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 19.16492 9.80284  25.13139  1.000 64.35446  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.83147 10.66212 25.71586  1.000 60.58333  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.67282 9.03000  24.17708  1.000 69.67447  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 21.06695 9.18666  23.78334  1.000 72.02286  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.28394 10.56766 23.16134  1.000 67.48573  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.33512 11.29758 22.87348  1.000 59.81279  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.46031 8.08939  22.80119  1.000 70.57385  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 20.61579 8.08405  21.56705  1.000 71.62026  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 21.00078 8.71898  20.40363  1.000 73.62090  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 19.38526 7.57084  21.32794  1.000 70.87587  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 20.06085 8.56695  19.48977  1.000 69.11993  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 19.06915 7.87508  20.02408  1.000 83.32569  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.55396 10.92902 22.97161  1.000 61.79324  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 22.88384 12.18175 22.30095  1.000 61.10017  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.30664 12.20213 20.88182  1.000 55.94962  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.29385 11.18504 20.17901  1.000 55.57139  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.41206 12.37921 22.27871  1.000 60.10696  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 25.06938 13.51331 21.46409  1.000 57.67117  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 24.50022 14.90124 21.79941  1.000 54.39131  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.58404 13.49700 21.66726  1.000 50.61366  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 21.76867 13.36040 20.48802  1.000 50.58966  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.28294 13.57165 19.14532  1.000 43.85115  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.25777 14.45307 18.38286  1.000 45.50252  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 23.10478 15.13713 18.95877  1.000 48.95540  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.15650 14.43623 17.06414  1.000 36.82407  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.92402 15.42590 16.34050  1.000 39.24629  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.29698 16.78806 16.42180  1.000 40.36743  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 22.99777 17.80873 16.34940  1.000 42.15082  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.09333 15.03879 14.85521  1.000 32.66260  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.34632 14.42868 14.64691  1.000 28.73145  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.51919 13.15031 15.04810  1.000 30.50787  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.41773 15.17895 14.28010  1.000 29.71035  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.73371 12.56956 14.95069  1.000 35.04033  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.65022 14.61892 14.16332  1.000 30.57318  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 26.82114 13.30537 14.50377  1.000 34.38662  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 20.98610 16.82338 16.50093  1.000 35.03188  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.32955 18.08996 16.67608  1.000 35.74312  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 20.06970 18.38814 18.13378  1.000 40.90927  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.19668 19.53488 18.56144  1.000 41.00624  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.04016 18.07876 15.89145  1.000 34.28378  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.30787 17.88985 14.40096  1.000 35.59677  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.13639 18.77669 13.70917  1.000 33.88697  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.75223 16.82823 13.69422  1.000 32.32537  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.39955 18.62549 12.34439  1.000 30.55911  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 18.99832 16.66937 12.31528  1.000 30.44459  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.83300 17.56578 11.65251  1.000 29.58727  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.07534 17.42429 10.30252  1.000 27.63653  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.74251 17.35501 18.90597  1.000 42.48257  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.30572 17.51765 20.28685  1.000 42.56292  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 20.52180 17.29510 21.15106  1.000 41.91550  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 20.73333 16.21868 21.70833  1.000 45.19095  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.19193 16.54058 20.62607  1.000 42.48341  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.33651 18.34468 21.26271  1.000 42.12222  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.68538 18.18996 21.77900  1.000 49.64004  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 22.92666 18.89552 23.12966  1.000 45.67013  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.06465 19.22137 23.44682  1.000 47.72295  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.68601 18.63558 20.71027  1.000 45.84988  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.44398 20.07430 20.21974  1.000 50.93105  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.44762 20.71478 20.62535  1.000 49.41686  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.26962 20.56757 19.41724  1.000 53.26420  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 21.87922 19.11611 23.93506  1.000 45.82996  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.98059 19.49882 25.35022  1.000 47.00994  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.47004 18.36690 26.24476  1.000 44.47940  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.50634 17.67721 25.90396  1.000 44.31377  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 21.16211 20.77176 25.68266  1.000 51.09764  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.77984 22.07387 25.25660  0.700 52.78763  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.76924 22.61634 24.00057  0.700 53.86177  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.50444 22.99426 26.08333  0.700 56.48091  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.44538 23.81568 23.99648  0.700 55.53875  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.90906 24.06774 25.26181  0.700 58.29507  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.85658 23.01303 27.43628  0.700 58.18531  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.64561 25.14814 25.75385  0.700 61.36609  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.58491 24.08458 27.91849  0.700 60.40325  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.97032 25.13568 27.08203  0.700 59.96722  ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 22.06188 18.21387 27.39417  1.000 48.55931  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.63340 17.17636 28.32853  1.000 51.69880  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.50843 17.66848 29.22700  1.000 51.91904  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.35778 18.86905 29.45827  1.000 53.17503  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.80948 16.72235 29.19228  1.000 53.37351  ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 24.06148 16.33757 28.38817  0.700 50.81728  ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 25.19213 15.86896 29.30107  0.700 51.32937  ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.70973 14.97742 30.35122  0.600 51.49506  ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 24.86518 15.18759 31.65522  0.600 57.86816  ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 25.53983 16.23078 32.11532  0.600 56.74955  ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 24.33881 14.32313 32.52175  0.600 56.94511  ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.70549 16.75325 29.76932  1.000 50.18204  ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.63044 17.17509 30.68344  1.000 50.77721  ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 19.10857 17.88991 31.94337  1.000 57.24307  ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.36372 18.72636 32.47817  1.000 54.68922  ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.92438 15.85238 31.01897  1.000 49.32637  ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 18.19319 14.98672 29.82888  1.000 52.12638  ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.59535 15.33393 29.39646  1.000 49.43635  ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.31676 17.60006 32.44753  1.000 55.65058  ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.72650 18.22866 33.70202  1.000 58.55547  ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 21.10442 19.68967 33.51169  1.000 57.29027  ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.12113 20.44850 34.49063  1.000 56.99821  ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.90188 17.46719 34.32964  1.000 58.20280  ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.42675 20.08044 32.27747  1.000 53.39852  ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.73332 21.44827 31.88137  1.000 56.16580  ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.49073 22.30025 31.65944  1.000 55.59559  ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.62472 23.45745 31.23250  1.000 53.04734  ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.54405 21.45830 30.57168  1.000 62.30276  ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 23.84193 20.65576 30.57829  1.000 68.32411  ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 25.08329 21.53442 30.62661  1.000 75.01028  ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 25.34367 22.15529 31.68528  1.000 74.71884  ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 25.80390 21.59308 29.60579  1.000 72.77350  ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.29176 21.76056 31.89436  1.000 52.77979  ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 18.09543 22.46717 31.45407  1.000 51.97642  ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 17.90733 23.77718 32.20408  1.000 52.11302  ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.52603 24.78449 31.59979  1.000 51.80057  ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.86552 21.57666 31.59948  1.000 50.80733  ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.17620 23.79053 33.51591  1.000 51.37426  ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 17.99793 25.01698 34.28807  1.000 53.44809  ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.00991 26.07881 33.87698  1.000 57.32264  ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.68512 27.27462 33.84071  1.000 55.40383  ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.10597 24.72092 35.78536  1.000 55.75514  ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.02386 23.76451 36.26501  1.000 59.30904  ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 15.94851 23.71850 35.62384  1.000 61.84249  ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.23750 23.05679 37.26757  1.000 60.15064  ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.24531 25.66330 33.56680  1.000 56.86312  ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.21366 26.61792 33.04490  1.000 56.39594  ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.79271 27.10579 31.66762  1.000 56.94911  ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.05813 28.25579 31.30001  1.000 59.62739  ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.60508 25.98423 33.01015  1.000 60.59165  ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.09772 26.25396 30.91380  1.000 56.64003  ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.55424 26.65155 29.62282  1.000 54.20767  ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.47189 27.71954 29.77176  1.000 57.06926  ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.46830 28.71721 29.03878  1.000 57.46304  ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 18.99184 25.42373 28.91420  1.000 52.14962  ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.94823 25.57394 27.41924  1.000 46.87037  ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.36900 25.81717 27.00716  1.000 53.44413  ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.45472 24.27465 26.86267  1.000 49.59682  ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.51517 27.49805 30.68628  1.000 55.32957  ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.46275 28.48410 30.94908  1.000 54.03680  ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.07867 29.85521 31.18939  1.000 57.90633  ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.68086 30.86046 30.58821  1.000 56.30741  ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.60446 28.04625 32.15491  1.000 54.12650  ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.70194 29.20016 32.63391  1.000 49.57158  ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.78635 26.81283 31.82535  1.000 50.69892  ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.07526 29.90178 32.07257  1.000 59.56144  ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.65961 31.16597 32.49668  1.000 63.40739  ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.33623 31.87969 31.32934  1.000 68.85822  ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 18.97053 33.00820 30.97050  1.000 69.14782  ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.64399 30.90269 33.63594  1.000 63.98719  ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 20.30437 32.12453 34.20139  1.000 67.40820  ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 21.49461 31.73084 35.07169  1.000 76.50874  ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 21.12812 31.61210 36.55612  1.000 90.77161  ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 20.19721 30.48410 36.87055  1.000 91.18580  ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.30894 31.21150 30.69612  1.000 70.71387  ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 21.12445 31.85049 29.66213  1.000 71.71000  ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 20.29931 32.37038 28.51106  1.000 68.90966  ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.76101 33.22521 27.74857  1.000 74.13485  ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.15942 30.86784 29.13110  1.000 73.72906  ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.34596 30.64637 30.05432  1.000 76.75741  ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 24.42161 29.85005 29.32539  1.000 76.24283  ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 23.85834 31.99312 30.52847  1.000 71.15862  ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 19.07033 31.90889 28.41791  1.000 69.77150  ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.22551 32.09859 27.25366  1.000 67.16894  ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.13785 33.11855 27.48236  1.000 74.59735  ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 16.61336 33.67590 26.51348  1.000 73.32641  ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.59601 30.76215 26.90279  1.000 63.61124  ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 16.58995 30.48368 25.82270  1.000 63.41238  ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 17.17458 30.72047 24.41508  1.000 60.11390  ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 16.21336 29.03352 26.03845  1.000 54.84935  ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 16.75356 33.30712 28.75273  1.000 74.47020  ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 15.88147 34.41323 29.12162  1.000 75.60456  ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 16.59785 35.74007 28.90737  1.000 80.13845  ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.01550 36.71400 28.40776  1.000 81.21717  ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 15.43412 34.26168 30.58187  1.000 71.93010  ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 17.88635 35.77964 29.25232  1.000 78.59729  ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 18.68313 36.96978 28.99074  1.000 80.26935  ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 18.85758 37.19372 27.49821  1.000 82.74639  ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 18.85413 38.33867 27.02815  1.000 89.34493  ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.05609 36.86862 29.66899  1.000 83.95133  ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 20.22298 35.81763 30.79545  1.000 81.80861  ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 19.26421 35.96619 31.99375  1.000 78.02161  ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 18.84471 37.40217 32.27652  1.000 81.44384  ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 19.79000 38.17389 33.13550  1.000 90.23933  ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 18.98945 36.11550 26.73671  1.000 81.56395  ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.39621 36.24147 25.35951  1.000 81.35733  ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 20.90324 36.33211 25.27060  1.000 83.09223  ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 21.61814 35.60834 25.97534  1.000 80.33028  ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 21.39400 37.23095 24.41969  1.000 90.03957  ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 22.82511 37.39660 24.19672  1.000 92.44840  ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 23.47320 36.05346 23.86770  1.000 97.93383  ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 24.49581 35.66200 24.43692  1.000 99.04854  ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 23.49701 38.05647 25.40304  1.000 90.44529  ? 94  GLU A CB  1 
ATOM   741  N N   . TYR A 1 95  ? 22.84088 35.32282 22.95827  1.000 85.08598  ? 95  TYR A N   1 
ATOM   742  C CA  . TYR A 1 95  ? 23.37564 34.06373 22.47773  1.000 79.90872  ? 95  TYR A CA  1 
ATOM   743  C C   . TYR A 1 95  ? 23.68648 34.19564 21.00162  1.000 79.20010  ? 95  TYR A C   1 
ATOM   744  O O   . TYR A 1 95  ? 23.11064 35.03079 20.29763  1.000 81.63745  ? 95  TYR A O   1 
ATOM   745  C CB  . TYR A 1 95  ? 22.40466 32.90010 22.69043  1.000 77.00599  ? 95  TYR A CB  1 
ATOM   746  C CG  . TYR A 1 95  ? 20.98433 33.21972 22.30218  1.000 75.58064  ? 95  TYR A CG  1 
ATOM   747  C CD1 . TYR A 1 95  ? 20.53936 33.06521 20.99830  1.000 69.24132  ? 95  TYR A CD1 1 
ATOM   748  C CD2 . TYR A 1 95  ? 20.08411 33.67750 23.24964  1.000 77.27781  ? 95  TYR A CD2 1 
ATOM   749  C CE1 . TYR A 1 95  ? 19.23390 33.35716 20.65289  1.000 64.92600  ? 95  TYR A CE1 1 
ATOM   750  C CE2 . TYR A 1 95  ? 18.78161 33.96843 22.91439  1.000 76.61139  ? 95  TYR A CE2 1 
ATOM   751  C CZ  . TYR A 1 95  ? 18.36220 33.80817 21.61115  1.000 69.54827  ? 95  TYR A CZ  1 
ATOM   752  O OH  . TYR A 1 95  ? 17.06021 34.10426 21.29325  1.000 68.83368  ? 95  TYR A OH  1 
ATOM   753  N N   . GLN A 1 96  ? 24.60342 33.35946 20.54432  1.000 75.16348  ? 96  GLN A N   1 
ATOM   754  C CA  . GLN A 1 96  ? 24.96029 33.34678 19.14566  1.000 68.54207  ? 96  GLN A CA  1 
ATOM   755  C C   . GLN A 1 96  ? 23.97138 32.47864 18.38712  1.000 65.26684  ? 96  GLN A C   1 
ATOM   756  O O   . GLN A 1 96  ? 23.45054 31.48874 18.91442  1.000 61.18509  ? 96  GLN A O   1 
ATOM   757  C CB  . GLN A 1 96  ? 26.38092 32.81430 18.97624  1.000 72.60288  ? 96  GLN A CB  1 
ATOM   758  C CG  . GLN A 1 96  ? 27.06319 33.23908 17.70035  1.000 79.74874  ? 96  GLN A CG  1 
ATOM   759  C CD  . GLN A 1 96  ? 27.84448 34.50999 17.88806  1.000 88.09726  ? 96  GLN A CD  1 
ATOM   760  O OE1 . GLN A 1 96  ? 28.09769 34.93377 19.02662  1.000 86.37254  ? 96  GLN A OE1 1 
ATOM   761  N NE2 . GLN A 1 96  ? 28.23237 35.13714 16.77801  1.000 85.94180  ? 96  GLN A NE2 1 
ATOM   762  N N   . LYS A 1 97  ? 23.70691 32.85723 17.14359  1.000 60.11504  ? 97  LYS A N   1 
ATOM   763  C CA  . LYS A 1 97  ? 22.94024 32.01819 16.24515  1.000 54.33976  ? 97  LYS A CA  1 
ATOM   764  C C   . LYS A 1 97  ? 23.87788 31.36878 15.24186  1.000 53.24226  ? 97  LYS A C   1 
ATOM   765  O O   . LYS A 1 97  ? 24.80889 32.00397 14.73261  1.000 54.79362  ? 97  LYS A O   1 
ATOM   766  C CB  . LYS A 1 97  ? 21.83962 32.80054 15.52519  1.000 54.50390  ? 97  LYS A CB  1 
ATOM   767  C CG  . LYS A 1 97  ? 20.62240 33.07746 16.39777  1.000 53.91523  ? 97  LYS A CG  1 
ATOM   768  C CD  . LYS A 1 97  ? 19.59082 33.93622 15.68324  1.000 53.72739  ? 97  LYS A CD  1 
ATOM   769  C CE  . LYS A 1 97  ? 19.62009 35.36842 16.18771  1.000 57.56474  ? 97  LYS A CE  1 
ATOM   770  N NZ  . LYS A 1 97  ? 18.43883 36.14709 15.71882  1.000 66.13071  ? 97  LYS A NZ  1 
ATOM   771  N N   . VAL A 1 98  ? 23.62627 30.08761 15.00648  1.000 47.71630  ? 98  VAL A N   1 
ATOM   772  C CA  . VAL A 1 98  ? 24.31791 29.24973 14.04261  1.000 46.91536  ? 98  VAL A CA  1 
ATOM   773  C C   . VAL A 1 98  ? 23.27164 28.76608 13.04794  1.000 42.81303  ? 98  VAL A C   1 
ATOM   774  O O   . VAL A 1 98  ? 22.17014 28.37172 13.44747  1.000 39.82016  ? 98  VAL A O   1 
ATOM   775  C CB  . VAL A 1 98  ? 25.01582 28.07023 14.75780  1.000 47.67663  ? 98  VAL A CB  1 
ATOM   776  C CG1 . VAL A 1 98  ? 25.61594 27.09652 13.76965  1.000 47.17348  ? 98  VAL A CG1 1 
ATOM   777  C CG2 . VAL A 1 98  ? 26.08984 28.60885 15.65521  1.000 51.50518  ? 98  VAL A CG2 1 
ATOM   778  N N   . SER A 1 99  ? 23.62485 28.80163 11.76307  1.000 38.99620  ? 99  SER A N   1 
ATOM   779  C CA  . SER A 1 99  ? 22.74559 28.50602 10.63668  1.000 37.16365  ? 99  SER A CA  1 
ATOM   780  C C   . SER A 1 99  ? 23.32861 27.35441 9.82283   1.000 36.34443  ? 99  SER A C   1 
ATOM   781  O O   . SER A 1 99  ? 24.51502 27.37781 9.48766   1.000 37.28022  ? 99  SER A O   1 
ATOM   782  C CB  . SER A 1 99  ? 22.59781 29.73084 9.71942   1.000 39.09554  ? 99  SER A CB  1 
ATOM   783  O OG  . SER A 1 99  ? 21.93388 30.79746 10.36073  1.000 46.03894  ? 99  SER A OG  1 
ATOM   784  N N   . TYR A 1 100 ? 22.48620 26.36171 9.48273   1.000 34.31452  ? 100 TYR A N   1 
ATOM   785  C CA  . TYR A 1 100 ? 22.75622 25.18084 8.66399   1.000 34.63095  ? 100 TYR A CA  1 
ATOM   786  C C   . TYR A 1 100 ? 21.93421 25.23496 7.37866   1.000 35.85383  ? 100 TYR A C   1 
ATOM   787  O O   . TYR A 1 100 ? 20.79437 25.72253 7.40527   1.000 35.58544  ? 100 TYR A O   1 
ATOM   788  C CB  . TYR A 1 100 ? 22.42551 23.85832 9.39156   1.000 31.14758  ? 100 TYR A CB  1 
ATOM   789  C CG  . TYR A 1 100 ? 23.43425 23.42492 10.46783  1.000 33.51330  ? 100 TYR A CG  1 
ATOM   790  C CD1 . TYR A 1 100 ? 24.57266 24.17235 10.72221  1.000 34.18112  ? 100 TYR A CD1 1 
ATOM   791  C CD2 . TYR A 1 100 ? 23.25194 22.24622 11.20376  1.000 31.44159  ? 100 TYR A CD2 1 
ATOM   792  C CE1 . TYR A 1 100 ? 25.49756 23.78563 11.70616  1.000 37.59446  ? 100 TYR A CE1 1 
ATOM   793  C CE2 . TYR A 1 100 ? 24.16750 21.85431 12.18320  1.000 32.59053  ? 100 TYR A CE2 1 
ATOM   794  C CZ  . TYR A 1 100 ? 25.28147 22.62090 12.43413  1.000 36.70795  ? 100 TYR A CZ  1 
ATOM   795  O OH  . TYR A 1 100 ? 26.20604 22.22658 13.38452  1.000 36.21587  ? 100 TYR A OH  1 
ATOM   796  N N   . PRO A 1 101 ? 22.49188 24.74179 6.26309   1.000 33.58689  ? 101 PRO A N   1 
ATOM   797  C CA  . PRO A 1 101 ? 21.74638 24.67969 5.00238   1.000 32.40340  ? 101 PRO A CA  1 
ATOM   798  C C   . PRO A 1 101 ? 20.63637 23.65014 5.03795   1.000 30.62182  ? 101 PRO A C   1 
ATOM   799  O O   . PRO A 1 101 ? 20.70120 22.63535 5.73649   1.000 29.25629  ? 101 PRO A O   1 
ATOM   800  C CB  . PRO A 1 101 ? 22.82014 24.27008 3.96566   1.000 30.77133  ? 101 PRO A CB  1 
ATOM   801  C CG  . PRO A 1 101 ? 24.16973 24.58026 4.65213   1.000 30.39847  ? 101 PRO A CG  1 
ATOM   802  C CD  . PRO A 1 101 ? 23.88416 24.27263 6.09355   1.000 31.54636  ? 101 PRO A CD  1 
ATOM   803  N N   . LEU A 1 102 ? 19.64763 23.89054 4.18011   1.000 31.29700  ? 102 LEU A N   1 
ATOM   804  C CA  . LEU A 1 102 ? 18.49608 23.03204 3.96052   1.000 28.88558  ? 102 LEU A CA  1 
ATOM   805  C C   . LEU A 1 102 ? 18.43715 22.66770 2.47384   1.000 30.14118  ? 102 LEU A C   1 
ATOM   806  O O   . LEU A 1 102 ? 19.09571 23.28342 1.63061   1.000 29.44252  ? 102 LEU A O   1 
ATOM   807  C CB  . LEU A 1 102 ? 17.19655 23.72808 4.40947   1.000 28.20667  ? 102 LEU A CB  1 
ATOM   808  C CG  . LEU A 1 102 ? 17.21615 24.28948 5.84927   1.000 32.44188  ? 102 LEU A CG  1 
ATOM   809  C CD1 . LEU A 1 102 ? 16.01204 25.16720 6.14282   1.000 30.15026  ? 102 LEU A CD1 1 
ATOM   810  C CD2 . LEU A 1 102 ? 17.33063 23.18569 6.88824   1.000 28.01676  ? 102 LEU A CD2 1 
ATOM   811  N N   . LEU A 1 103 ? 17.64738 21.64815 2.17521   1.000 28.02733  ? 103 LEU A N   1 
ATOM   812  C CA  . LEU A 1 103 ? 17.44720 21.12022 0.83448   1.000 29.52472  ? 103 LEU A CA  1 
ATOM   813  C C   . LEU A 1 103 ? 16.04190 21.46568 0.37040   1.000 32.37118  ? 103 LEU A C   1 
ATOM   814  O O   . LEU A 1 103 ? 15.06509 21.13236 1.05582   1.000 30.72904  ? 103 LEU A O   1 
ATOM   815  C CB  . LEU A 1 103 ? 17.62686 19.59667 0.82910   1.000 27.28535  ? 103 LEU A CB  1 
ATOM   816  C CG  . LEU A 1 103 ? 17.28799 18.92045 -0.51049  1.000 28.21252  ? 103 LEU A CG  1 
ATOM   817  C CD1 . LEU A 1 103 ? 18.29705 19.30584 -1.59597  1.000 26.76513  ? 103 LEU A CD1 1 
ATOM   818  C CD2 . LEU A 1 103 ? 17.17198 17.42679 -0.37136  1.000 25.59292  ? 103 LEU A CD2 1 
ATOM   819  N N   . LYS A 1 104 ? 15.92563 22.11363 -0.79067  1.000 31.89101  ? 104 LYS A N   1 
ATOM   820  C CA  . LYS A 1 104 ? 14.61155 22.31055 -1.39633  1.000 30.82497  ? 104 LYS A CA  1 
ATOM   821  C C   . LYS A 1 104 ? 14.31307 21.18737 -2.38698  1.000 32.43693  ? 104 LYS A C   1 
ATOM   822  O O   . LYS A 1 104 ? 15.14839 20.84454 -3.24139  1.000 31.50288  ? 104 LYS A O   1 
ATOM   823  C CB  . LYS A 1 104 ? 14.49216 23.67313 -2.07078  1.000 33.50691  ? 104 LYS A CB  1 
ATOM   824  C CG  . LYS A 1 104 ? 13.11857 23.83326 -2.74528  1.000 38.41502  ? 104 LYS A CG  1 
ATOM   825  C CD  . LYS A 1 104 ? 12.76539 25.26053 -3.18195  1.000 39.95971  ? 104 LYS A CD  1 
ATOM   826  C CE  . LYS A 1 104 ? 13.67468 25.76785 -4.23097  1.000 42.62644  ? 104 LYS A CE  1 
ATOM   827  N NZ  . LYS A 1 104 ? 13.00559 26.91983 -4.92753  1.000 56.41554  ? 104 LYS A NZ  1 
ATOM   828  N N   . THR A 1 105 ? 13.13772 20.58325 -2.22876  1.000 32.72215  ? 105 THR A N   1 
ATOM   829  C CA  . THR A 1 105 ? 12.59253 19.59332 -3.14655  1.000 34.31530  ? 105 THR A CA  1 
ATOM   830  C C   . THR A 1 105 ? 11.37172 20.16351 -3.84711  1.000 36.59852  ? 105 THR A C   1 
ATOM   831  O O   . THR A 1 105 ? 10.44606 20.64175 -3.18410  1.000 39.01804  ? 105 THR A O   1 
ATOM   832  C CB  . THR A 1 105 ? 12.18239 18.31559 -2.41953  1.000 31.83428  ? 105 THR A CB  1 
ATOM   833  O OG1 . THR A 1 105 ? 13.30759 17.80128 -1.72752  1.000 30.81704  ? 105 THR A OG1 1 
ATOM   834  C CG2 . THR A 1 105 ? 11.72733 17.26988 -3.42155  1.000 34.84546  ? 105 THR A CG2 1 
ATOM   835  N N   . THR A 1 106 ? 11.36003 20.08910 -5.17384  1.000 37.32397  ? 106 THR A N   1 
ATOM   836  C CA  . THR A 1 106 ? 10.19728 20.46365 -5.95644  1.000 38.72511  ? 106 THR A CA  1 
ATOM   837  C C   . THR A 1 106 ? 9.68615  19.26502 -6.73891  1.000 38.60253  ? 106 THR A C   1 
ATOM   838  O O   . THR A 1 106 ? 10.45609 18.59752 -7.43075  1.000 39.03763  ? 106 THR A O   1 
ATOM   839  C CB  . THR A 1 106 ? 10.51798 21.60339 -6.90057  1.000 40.13262  ? 106 THR A CB  1 
ATOM   840  O OG1 . THR A 1 106 ? 11.00937 22.70578 -6.12481  1.000 39.57906  ? 106 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 106 ? 9.24221  22.00818 -7.63450  1.000 42.15338  ? 106 THR A CG2 1 
ATOM   842  N N   . VAL A 1 107 ? 8.38844  19.00225 -6.62481  1.000 42.17539  ? 107 VAL A N   1 
ATOM   843  C CA  . VAL A 1 107 ? 7.73715  17.88440 -7.29074  1.000 45.40139  ? 107 VAL A CA  1 
ATOM   844  C C   . VAL A 1 107 ? 6.70865  18.46217 -8.25806  1.000 47.61263  ? 107 VAL A C   1 
ATOM   845  O O   . VAL A 1 107 ? 5.79128  19.18913 -7.85202  1.000 47.80116  ? 107 VAL A O   1 
ATOM   846  C CB  . VAL A 1 107 ? 7.07656  16.91748 -6.29078  1.000 46.58513  ? 107 VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 107 ? 6.43242  15.74289 -7.03568  1.000 48.63754  ? 107 VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 107 ? 8.09512  16.41230 -5.23875  1.000 45.03574  ? 107 VAL A CG2 1 
ATOM   849  N N   . LYS A 1 108 ? 6.85612  18.12343 -9.52655  1.000 47.86707  ? 108 LYS A N   1 
ATOM   850  C CA  . LYS A 1 108 ? 6.01435  18.63103 -10.58958 1.000 51.34987  ? 108 LYS A CA  1 
ATOM   851  C C   . LYS A 1 108 ? 5.14789  17.50119 -11.13586 1.000 59.23448  ? 108 LYS A C   1 
ATOM   852  O O   . LYS A 1 108 ? 5.64778  16.40085 -11.40099 1.000 56.96409  ? 108 LYS A O   1 
ATOM   853  C CB  . LYS A 1 108 ? 6.88489  19.23711 -11.69649 1.000 48.01827  ? 108 LYS A CB  1 
ATOM   854  N N   . TYR A 1 109 ? 3.84866  17.79107 -11.32829 1.000 61.96592  ? 109 TYR A N   1 
ATOM   855  C CA  . TYR A 1 109 ? 2.84321  16.89631 -11.90581 1.000 67.15107  ? 109 TYR A CA  1 
ATOM   856  C C   . TYR A 1 109 ? 2.37779  17.36929 -13.29459 1.000 72.96261  ? 109 TYR A C   1 
ATOM   857  O O   . TYR A 1 109 ? 2.96508  18.27128 -13.90400 1.000 73.78976  ? 109 TYR A O   1 
ATOM   858  C CB  . TYR A 1 109 ? 1.64303  16.78573 -10.97550 1.000 63.23080  ? 109 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 109 ? 1.99813  16.58648 -9.50846  1.000 68.21291  ? 109 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 109 ? 2.10910  15.31576 -8.97259  1.000 66.74852  ? 109 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 109 ? 2.17963  17.67365 -8.65587  1.000 63.79013  ? 109 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 109 ? 2.40583  15.13160 -7.64854  1.000 75.75324  ? 109 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 109 ? 2.48470  17.49777 -7.34185  1.000 62.06907  ? 109 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 109 ? 2.59545  16.22197 -6.83645  1.000 68.88478  ? 109 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 109 ? 2.89217  16.03190 -5.50589  1.000 68.81296  ? 109 TYR A OH  1 
ATOM   866  N N   . GLY A 1 110 ? 1.29750  16.75188 -13.78935 1.000 73.99912  ? 110 GLY A N   1 
ATOM   867  C CA  . GLY A 1 110 ? 0.61891  17.18549 -15.00029 1.000 71.18513  ? 110 GLY A CA  1 
ATOM   868  C C   . GLY A 1 110 ? -0.90289 17.23024 -14.89919 1.000 76.57788  ? 110 GLY A C   1 
ATOM   869  O O   . GLY A 1 110 ? -1.60045 17.69522 -15.82358 1.000 70.01552  ? 110 GLY A O   1 
ATOM   870  N N   . LYS A 1 114 ? 1.46081  20.81279 -12.13492 1.000 69.10447  ? 114 LYS A N   1 
ATOM   871  C CA  . LYS A 1 114 ? 1.25401  21.38516 -10.80462 1.000 68.26544  ? 114 LYS A CA  1 
ATOM   872  C C   . LYS A 1 114 ? 2.54295  21.18578 -9.99777  1.000 64.03434  ? 114 LYS A C   1 
ATOM   873  O O   . LYS A 1 114 ? 3.29772  20.26411 -10.28243 1.000 65.76899  ? 114 LYS A O   1 
ATOM   874  C CB  . LYS A 1 114 ? 0.04410  20.73308 -10.12159 1.000 64.78994  ? 114 LYS A CB  1 
ATOM   875  C CG  . LYS A 1 114 ? -0.38549 21.38968 -8.82738  1.000 71.33347  ? 114 LYS A CG  1 
ATOM   876  C CD  . LYS A 1 114 ? -0.54929 22.88522 -8.99253  1.000 73.94044  ? 114 LYS A CD  1 
ATOM   877  C CE  . LYS A 1 114 ? -0.73079 23.56921 -7.65714  1.000 70.50965  ? 114 LYS A CE  1 
ATOM   878  N NZ  . LYS A 1 114 ? 0.47718  23.40976 -6.81396  1.000 77.01978  ? 114 LYS A NZ  1 
ATOM   879  N N   . GLU A 1 115 ? 2.82165  22.04203 -9.01249  1.000 61.48805  ? 115 GLU A N   1 
ATOM   880  C CA  . GLU A 1 115 ? 4.06021  21.93856 -8.25003  1.000 59.17076  ? 115 GLU A CA  1 
ATOM   881  C C   . GLU A 1 115 ? 3.81447  21.92080 -6.74699  1.000 56.96123  ? 115 GLU A C   1 
ATOM   882  O O   . GLU A 1 115 ? 2.91585  22.58567 -6.22835  1.000 59.55261  ? 115 GLU A O   1 
ATOM   883  C CB  . GLU A 1 115 ? 5.02332  23.06821 -8.57285  1.000 55.78387  ? 115 GLU A CB  1 
ATOM   884  C CG  . GLU A 1 115 ? 5.93249  22.72963 -9.72385  1.000 61.74925  ? 115 GLU A CG  1 
ATOM   885  C CD  . GLU A 1 115 ? 6.99977  23.76755 -9.92308  1.000 65.72142  ? 115 GLU A CD  1 
ATOM   886  O OE1 . GLU A 1 115 ? 7.18036  24.57943 -8.99356  1.000 68.78262  ? 115 GLU A OE1 1 
ATOM   887  O OE2 . GLU A 1 115 ? 7.64690  23.77374 -10.99517 1.000 58.62370  ? 115 GLU A OE2 1 
ATOM   888  N N   . ALA A 1 116 ? 4.63521  21.13805 -6.05258  1.000 53.80423  ? 116 ALA A N   1 
ATOM   889  C CA  . ALA A 1 116 ? 4.72580  21.15923 -4.60027  1.000 48.69900  ? 116 ALA A CA  1 
ATOM   890  C C   . ALA A 1 116 ? 6.18148  21.29211 -4.19194  1.000 46.84176  ? 116 ALA A C   1 
ATOM   891  O O   . ALA A 1 116 ? 7.05508  20.59516 -4.71961  1.000 45.30483  ? 116 ALA A O   1 
ATOM   892  C CB  . ALA A 1 116 ? 4.15482  19.89469 -3.96044  1.000 48.46448  ? 116 ALA A CB  1 
ATOM   893  N N   . THR A 1 117 ? 6.41996  22.14277 -3.20733  1.000 45.36691  ? 117 THR A N   1 
ATOM   894  C CA  . THR A 1 117 ? 7.73766  22.36847 -2.64127  1.000 45.40804  ? 117 THR A CA  1 
ATOM   895  C C   . THR A 1 117 ? 7.81341  21.82223 -1.20848  1.000 43.30536  ? 117 THR A C   1 
ATOM   896  O O   . THR A 1 117 ? 6.82354  21.84557 -0.48084  1.000 43.32683  ? 117 THR A O   1 
ATOM   897  C CB  . THR A 1 117 ? 8.02980  23.86626 -2.71846  1.000 47.28428  ? 117 THR A CB  1 
ATOM   898  O OG1 . THR A 1 117 ? 8.15222  24.22900 -4.10739  1.000 47.71942  ? 117 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 117 ? 9.30483  24.19852 -2.01106  1.000 53.86721  ? 117 THR A CG2 1 
ATOM   900  N N   . TYR A 1 118 ? 8.97731  21.28352 -0.81794  1.000 41.91523  ? 118 TYR A N   1 
ATOM   901  C CA  . TYR A 1 118 ? 9.23696  20.83339 0.55137   1.000 36.42023  ? 118 TYR A CA  1 
ATOM   902  C C   . TYR A 1 118 ? 10.64616 21.23241 0.94596   1.000 37.53412  ? 118 TYR A C   1 
ATOM   903  O O   . TYR A 1 118 ? 11.54243 21.31110 0.09556   1.000 36.67196  ? 118 TYR A O   1 
ATOM   904  C CB  . TYR A 1 118 ? 9.12231  19.30623 0.72648   1.000 36.33748  ? 118 TYR A CB  1 
ATOM   905  C CG  . TYR A 1 118 ? 7.85234  18.71425 0.17799   1.000 40.51902  ? 118 TYR A CG  1 
ATOM   906  C CD1 . TYR A 1 118 ? 7.68434  18.53924 -1.18609  1.000 43.23378  ? 118 TYR A CD1 1 
ATOM   907  C CD2 . TYR A 1 118 ? 6.81342  18.34554 1.02031   1.000 40.53547  ? 118 TYR A CD2 1 
ATOM   908  C CE1 . TYR A 1 118 ? 6.50180  18.01267 -1.71269  1.000 46.33607  ? 118 TYR A CE1 1 
ATOM   909  C CE2 . TYR A 1 118 ? 5.62587  17.81542 0.51371   1.000 45.66352  ? 118 TYR A CE2 1 
ATOM   910  C CZ  . TYR A 1 118 ? 5.47147  17.65358 -0.85868  1.000 48.15153  ? 118 TYR A CZ  1 
ATOM   911  O OH  . TYR A 1 118 ? 4.30319  17.12420 -1.36957  1.000 48.87694  ? 118 TYR A OH  1 
ATOM   912  N N   . LEU A 1 119 ? 10.85322 21.44780 2.24799   1.000 33.16130  ? 119 LEU A N   1 
ATOM   913  C CA  . LEU A 1 119 ? 12.17658 21.70420 2.80381   1.000 30.81553  ? 119 LEU A CA  1 
ATOM   914  C C   . LEU A 1 119 ? 12.59561 20.52632 3.66152   1.000 31.79313  ? 119 LEU A C   1 
ATOM   915  O O   . LEU A 1 119 ? 11.79888 20.01302 4.45064   1.000 34.17155  ? 119 LEU A O   1 
ATOM   916  C CB  . LEU A 1 119 ? 12.18927 22.97665 3.64214   1.000 34.10006  ? 119 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 119 ? 13.02061 24.20773 3.30242   1.000 36.21435  ? 119 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 119 ? 13.00320 24.55615 1.84461   1.000 36.81499  ? 119 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 119 ? 12.38219 25.33561 4.06427   1.000 36.83996  ? 119 LEU A CD2 1 
ATOM   920  N N   . ALA A 1 120 ? 13.83859 20.08236 3.51714   1.000 29.39419  ? 120 ALA A N   1 
ATOM   921  C CA  . ALA A 1 120 ? 14.33945 18.98379 4.32209   1.000 28.12212  ? 120 ALA A CA  1 
ATOM   922  C C   . ALA A 1 120 ? 15.53314 19.47938 5.12414   1.000 28.87697  ? 120 ALA A C   1 
ATOM   923  O O   . ALA A 1 120 ? 16.33473 20.27424 4.61595   1.000 29.91648  ? 120 ALA A O   1 
ATOM   924  C CB  . ALA A 1 120 ? 14.73348 17.77524 3.45565   1.000 25.94526  ? 120 ALA A CB  1 
ATOM   925  N N   . LEU A 1 121 ? 15.59952 19.05937 6.39333   1.000 25.69628  ? 121 LEU A N   1 
ATOM   926  C CA  . LEU A 1 121 ? 16.75247 19.26188 7.25759   1.000 25.45058  ? 121 LEU A CA  1 
ATOM   927  C C   . LEU A 1 121 ? 17.68838 18.06453 7.22557   1.000 26.06558  ? 121 LEU A C   1 
ATOM   928  O O   . LEU A 1 121 ? 18.90253 18.23160 7.39313   1.000 25.34935  ? 121 LEU A O   1 
ATOM   929  C CB  . LEU A 1 121 ? 16.29810 19.51044 8.71018   1.000 27.41225  ? 121 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 121 ? 17.31598 19.53308 9.86141   1.000 27.54830  ? 121 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 121 ? 18.25264 20.67795 9.65242   1.000 26.13781  ? 121 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 121 ? 16.61481 19.65578 11.24655  1.000 26.90350  ? 121 LEU A CD2 1 
ATOM   933  N N   . ASN A 1 122 ? 17.15598 16.85613 7.03453   1.000 22.64340  ? 122 ASN A N   1 
ATOM   934  C CA  . ASN A 1 122 ? 18.01308 15.68551 6.87037   1.000 23.68750  ? 122 ASN A CA  1 
ATOM   935  C C   . ASN A 1 122 ? 18.18944 15.34230 5.38457   1.000 26.42772  ? 122 ASN A C   1 
ATOM   936  O O   . ASN A 1 122 ? 19.29584 15.48466 4.86512   1.000 24.31975  ? 122 ASN A O   1 
ATOM   937  C CB  . ASN A 1 122 ? 17.46394 14.47519 7.60311   1.000 23.37246  ? 122 ASN A CB  1 
ATOM   938  C CG  . ASN A 1 122 ? 18.06501 14.27531 9.00267   1.000 26.79073  ? 122 ASN A CG  1 
ATOM   939  O OD1 . ASN A 1 122 ? 18.95916 15.00519 9.47125   1.000 24.42988  ? 122 ASN A OD1 1 
ATOM   940  N ND2 . ASN A 1 122 ? 17.55927 13.26619 9.68113   1.000 26.92855  ? 122 ASN A ND2 1 
ATOM   941  N N   . GLU A 1 123 ? 17.14697 14.86474 4.70010   1.000 24.81547  ? 123 GLU A N   1 
ATOM   942  C CA  . GLU A 1 123 ? 17.31381 14.42810 3.31321   1.000 23.73292  ? 123 GLU A CA  1 
ATOM   943  C C   . GLU A 1 123 ? 15.95283 14.22769 2.66897   1.000 28.76443  ? 123 GLU A C   1 
ATOM   944  O O   . GLU A 1 123 ? 14.92047 14.13944 3.34286   1.000 26.64964  ? 123 GLU A O   1 
ATOM   945  C CB  . GLU A 1 123 ? 18.10064 13.12204 3.19927   1.000 24.21085  ? 123 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 123 ? 17.35010 11.85634 3.63282   1.000 25.75331  ? 123 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 123 ? 17.11084 11.79794 5.16115   1.000 27.48336  ? 123 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 123 ? 18.10935 11.66288 5.92209   1.000 23.89510  ? 123 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 123 ? 15.92780 11.89684 5.57534   1.000 25.55810  ? 123 GLU A OE2 1 
ATOM   950  N N   . SER A 1 124 ? 15.97227 14.10938 1.33871   1.000 27.83481  ? 124 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 14.81495 13.67038 0.58446   1.000 26.19208  ? 124 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 15.19845 12.46310 -0.25019  1.000 28.93885  ? 124 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 16.25431 12.44550 -0.90039  1.000 28.33225  ? 124 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 14.28954 14.79293 -0.30267  1.000 29.72643  ? 124 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 13.16368 14.36583 -1.05243  1.000 32.14399  ? 124 SER A OG  1 
ATOM   956  N N   . THR A 1 125 ? 14.31888 11.47130 -0.27853  1.000 31.83336  ? 125 THR A N   1 
ATOM   957  C CA  . THR A 1 125 ? 14.58743 10.25328 -1.02098  1.000 30.19304  ? 125 THR A CA  1 
ATOM   958  C C   . THR A 1 125 ? 13.41082 9.89888  -1.91488  1.000 31.66797  ? 125 THR A C   1 
ATOM   959  O O   . THR A 1 125 ? 12.25143 10.18570 -1.61101  1.000 30.81933  ? 125 THR A O   1 
ATOM   960  C CB  . THR A 1 125 ? 14.88732 9.04276  -0.09828  1.000 29.62928  ? 125 THR A CB  1 
ATOM   961  O OG1 . THR A 1 125 ? 13.66153 8.56877  0.45850   1.000 31.37714  ? 125 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 125 ? 15.86959 9.41943  1.04408   1.000 28.26694  ? 125 THR A CG2 1 
ATOM   963  N N   . VAL A 1 126 ? 13.74735 9.25488  -3.02700  1.000 31.98496  ? 126 VAL A N   1 
ATOM   964  C CA  . VAL A 1 126 ? 12.79676 8.76392  -4.00323  1.000 32.02407  ? 126 VAL A CA  1 
ATOM   965  C C   . VAL A 1 126 ? 13.01877 7.27095  -4.16686  1.000 31.58030  ? 126 VAL A C   1 
ATOM   966  O O   . VAL A 1 126 ? 14.15092 6.84088  -4.41469  1.000 30.43770  ? 126 VAL A O   1 
ATOM   967  C CB  . VAL A 1 126 ? 12.97553 9.48051  -5.34623  1.000 33.10866  ? 126 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 126 ? 11.80420 9.16078  -6.23844  1.000 35.63382  ? 126 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 126 ? 13.10027 10.96274 -5.12732  1.000 34.83365  ? 126 VAL A CG2 1 
ATOM   970  N N   . LYS A 1 127 ? 11.94602 6.49585  -4.02018  1.000 32.72955  ? 127 LYS A N   1 
ATOM   971  C CA  . LYS A 1 127 ? 11.88386 5.06358  -4.30444  1.000 38.64370  ? 127 LYS A CA  1 
ATOM   972  C C   . LYS A 1 127 ? 10.63818 4.77699  -5.13819  1.000 43.51986  ? 127 LYS A C   1 
ATOM   973  O O   . LYS A 1 127 ? 9.66058  5.53396  -5.09857  1.000 43.49381  ? 127 LYS A O   1 
ATOM   974  C CB  . LYS A 1 127 ? 11.83006 4.22477  -3.01985  1.000 38.08919  ? 127 LYS A CB  1 
ATOM   975  C CG  . LYS A 1 127 ? 12.93355 4.57092  -2.01230  1.000 40.09386  ? 127 LYS A CG  1 
ATOM   976  C CD  . LYS A 1 127 ? 12.78311 3.75704  -0.70618  1.000 43.31422  ? 127 LYS A CD  1 
ATOM   977  C CE  . LYS A 1 127 ? 13.89270 4.12253  0.30878   1.000 45.83006  ? 127 LYS A CE  1 
ATOM   978  N NZ  . LYS A 1 127 ? 13.76092 3.53227  1.68452   1.000 43.06064  ? 127 LYS A NZ  1 
ATOM   979  N N   . SER A 1 128 ? 10.66478 3.66840  -5.88692  1.000 45.22520  ? 128 SER A N   1 
ATOM   980  C CA  . SER A 1 128 ? 9.51512  3.32920  -6.72300  1.000 53.13935  ? 128 SER A CA  1 
ATOM   981  C C   . SER A 1 128 ? 8.32739  2.89485  -5.87535  1.000 58.54826  ? 128 SER A C   1 
ATOM   982  O O   . SER A 1 128 ? 8.47224  2.47244  -4.72896  1.000 55.53383  ? 128 SER A O   1 
ATOM   983  C CB  . SER A 1 128 ? 9.82712  2.20439  -7.70180  1.000 58.25534  ? 128 SER A CB  1 
ATOM   984  O OG  . SER A 1 128 ? 8.73100  2.03147  -8.58390  1.000 64.19575  ? 128 SER A OG  1 
ATOM   985  N N   . SER A 1 129 ? 7.14267  2.96861  -6.47653  1.000 61.52519  ? 129 SER A N   1 
ATOM   986  C CA  . SER A 1 129 ? 5.89367  2.62972  -5.79726  1.000 67.97847  ? 129 SER A CA  1 
ATOM   987  C C   . SER A 1 129 ? 5.45965  1.19080  -6.05330  1.000 80.08153  ? 129 SER A C   1 
ATOM   988  O O   . SER A 1 129 ? 4.27621  0.93582  -6.29264  1.000 80.69022  ? 129 SER A O   1 
ATOM   989  C CB  . SER A 1 129 ? 4.80805  3.59623  -6.24147  1.000 64.72058  ? 129 SER A CB  1 
ATOM   990  O OG  . SER A 1 129 ? 4.38253  3.25682  -7.55353  1.000 71.98684  ? 129 SER A OG  1 
ATOM   991  N N   . GLY A 1 130 ? 6.38686  0.23301  -6.00933  1.000 100.72139 ? 130 GLY A N   1 
ATOM   992  C CA  . GLY A 1 130 ? 6.04730  -1.15592 -6.26663  1.000 97.43972  ? 130 GLY A CA  1 
ATOM   993  C C   . GLY A 1 130 ? 6.83048  -1.79788 -7.39777  1.000 101.71227 ? 130 GLY A C   1 
ATOM   994  O O   . GLY A 1 130 ? 7.30067  -2.93383 -7.27285  1.000 101.55829 ? 130 GLY A O   1 
ATOM   995  N N   . GLY A 1 131 ? 6.97237  -1.08985 -8.51274  1.000 89.76426  ? 131 GLY A N   1 
ATOM   996  C CA  . GLY A 1 131 ? 7.67319  -1.62939 -9.65150  1.000 86.77490  ? 131 GLY A CA  1 
ATOM   997  C C   . GLY A 1 131 ? 9.16905  -1.40802 -9.55780  1.000 83.16828  ? 131 GLY A C   1 
ATOM   998  O O   . GLY A 1 131 ? 9.72899  -1.18874 -8.47313  1.000 83.00869  ? 131 GLY A O   1 
ATOM   999  N N   . PRO A 1 132 ? 9.84664  -1.47733 -10.71452 1.000 70.11623  ? 132 PRO A N   1 
ATOM   1000 C CA  . PRO A 1 132 ? 11.28157 -1.16442 -10.77244 1.000 62.41682  ? 132 PRO A CA  1 
ATOM   1001 C C   . PRO A 1 132 ? 11.54059 0.32611  -10.89964 1.000 59.27991  ? 132 PRO A C   1 
ATOM   1002 O O   . PRO A 1 132 ? 10.95295 0.99657  -11.75917 1.000 62.32343  ? 132 PRO A O   1 
ATOM   1003 C CB  . PRO A 1 132 ? 11.75434 -1.90601 -12.03218 1.000 59.38803  ? 132 PRO A CB  1 
ATOM   1004 C CG  . PRO A 1 132 ? 10.53852 -1.91433 -12.92146 1.000 65.32054  ? 132 PRO A CG  1 
ATOM   1005 C CD  . PRO A 1 132 ? 9.31076  -1.89595 -12.02127 1.000 69.27273  ? 132 PRO A CD  1 
ATOM   1006 N N   . PHE A 1 133 ? 12.44820 0.84065  -10.08074 1.000 49.82733  ? 133 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 133 ? 12.77570 2.25299  -10.09460 1.000 43.64368  ? 133 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 133 ? 13.79450 2.51919  -11.18950 1.000 39.09743  ? 133 PHE A C   1 
ATOM   1009 O O   . PHE A 1 133 ? 14.90305 1.98012  -11.14348 1.000 37.17794  ? 133 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 133 ? 13.31493 2.64899  -8.72850  1.000 41.38843  ? 133 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 133 ? 13.61302 4.09949  -8.57249  1.000 38.39803  ? 133 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 133 ? 12.59830 4.99540  -8.34493  1.000 38.96324  ? 133 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 133 ? 14.91950 4.55799  -8.58981  1.000 36.89330  ? 133 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 133 ? 12.87154 6.33201  -8.16012  1.000 39.87964  ? 133 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 133 ? 15.20425 5.90205  -8.40804  1.000 34.31746  ? 133 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 133 ? 14.16745 6.79388  -8.18803  1.000 36.06094  ? 133 PHE A CZ  1 
ATOM   1017 N N   . VAL A 1 134 ? 13.40848 3.33380  -12.17818 1.000 40.39131  ? 134 VAL A N   1 
ATOM   1018 C CA  . VAL A 1 134 ? 14.27483 3.80963  -13.26415 1.000 37.19761  ? 134 VAL A CA  1 
ATOM   1019 C C   . VAL A 1 134 ? 14.03602 5.30609  -13.40022 1.000 39.04883  ? 134 VAL A C   1 
ATOM   1020 O O   . VAL A 1 134 ? 12.89715 5.72502  -13.64158 1.000 41.50971  ? 134 VAL A O   1 
ATOM   1021 C CB  . VAL A 1 134 ? 13.96989 3.12291  -14.60469 1.000 38.31876  ? 134 VAL A CB  1 
ATOM   1022 C CG1 . VAL A 1 134 ? 15.04580 3.44179  -15.60472 1.000 35.85250  ? 134 VAL A CG1 1 
ATOM   1023 C CG2 . VAL A 1 134 ? 13.76791 1.61123  -14.44197 1.000 40.79479  ? 134 VAL A CG2 1 
ATOM   1024 N N   . VAL A 1 135 ? 15.08302 6.11840  -13.24215 1.000 33.58074  ? 135 VAL A N   1 
ATOM   1025 C CA  . VAL A 1 135 ? 14.93326 7.55873  -13.43848 1.000 33.82451  ? 135 VAL A CA  1 
ATOM   1026 C C   . VAL A 1 135 ? 16.11853 8.08855  -14.20899 1.000 33.69827  ? 135 VAL A C   1 
ATOM   1027 O O   . VAL A 1 135 ? 17.25700 7.64839  -14.00277 1.000 33.76524  ? 135 VAL A O   1 
ATOM   1028 C CB  . VAL A 1 135 ? 14.78416 8.36130  -12.12265 1.000 33.77317  ? 135 VAL A CB  1 
ATOM   1029 C CG1 . VAL A 1 135 ? 13.50684 8.00800  -11.41605 1.000 40.26674  ? 135 VAL A CG1 1 
ATOM   1030 C CG2 . VAL A 1 135 ? 16.01210 8.19473  -11.20511 1.000 30.84385  ? 135 VAL A CG2 1 
ATOM   1031 N N   . ASP A 1 136 ? 15.85892 9.06410  -15.07951 1.000 33.64324  ? 136 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 136 ? 16.94853 9.79044  -15.71412 1.000 31.45360  ? 136 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 136 ? 17.37318 10.90842 -14.77563 1.000 30.70826  ? 136 ASP A C   1 
ATOM   1034 O O   . ASP A 1 136 ? 16.53258 11.58133 -14.17079 1.000 33.61750  ? 136 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 136 ? 16.52937 10.33110 -17.08560 1.000 34.10494  ? 136 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 136 ? 16.49560 9.25124  -18.14347 1.000 36.40988  ? 136 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 136 ? 17.36057 8.33998  -18.08064 1.000 37.93583  ? 136 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 136 ? 15.61773 9.29571  -19.05278 1.000 41.23184  ? 136 ASP A OD2 1 
ATOM   1039 N N   . VAL A 1 137 ? 18.67621 11.03651 -14.57753 1.000 31.37446  ? 137 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 137 ? 19.25962 11.98603 -13.64268 1.000 29.36725  ? 137 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 137 ? 19.88036 13.09295 -14.48014 1.000 30.65422  ? 137 VAL A C   1 
ATOM   1042 O O   . VAL A 1 137 ? 20.79970 12.83496 -15.25734 1.000 29.72687  ? 137 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 137 ? 20.31936 11.31728 -12.74553 1.000 28.28889  ? 137 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 137 ? 21.01817 12.35161 -11.89400 1.000 25.21640  ? 137 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 137 ? 19.70448 10.21427 -11.87399 1.000 24.90474  ? 137 VAL A CG2 1 
ATOM   1046 N N   . VAL A 1 138 ? 19.38900 14.31989 -14.32932 1.000 30.07602  ? 138 VAL A N   1 
ATOM   1047 C CA  . VAL A 1 138 ? 19.80218 15.44291 -15.16545 1.000 30.76805  ? 138 VAL A CA  1 
ATOM   1048 C C   . VAL A 1 138 ? 20.38509 16.51172 -14.24782 1.000 32.25976  ? 138 VAL A C   1 
ATOM   1049 O O   . VAL A 1 138 ? 19.71193 16.95979 -13.30919 1.000 32.23051  ? 138 VAL A O   1 
ATOM   1050 C CB  . VAL A 1 138 ? 18.61535 15.98885 -15.97526 1.000 33.24705  ? 138 VAL A CB  1 
ATOM   1051 C CG1 . VAL A 1 138 ? 19.04133 17.09289 -16.90342 1.000 33.38740  ? 138 VAL A CG1 1 
ATOM   1052 C CG2 . VAL A 1 138 ? 17.95486 14.86035 -16.75532 1.000 34.31828  ? 138 VAL A CG2 1 
ATOM   1053 N N   . ILE A 1 139 ? 21.63583 16.90581 -14.49759 1.000 32.54030  ? 139 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 139 ? 22.32889 17.91719 -13.70073 1.000 29.73936  ? 139 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 139 ? 22.46007 19.19301 -14.52416 1.000 31.96579  ? 139 ILE A C   1 
ATOM   1056 O O   . ILE A 1 139 ? 23.15837 19.20418 -15.54269 1.000 31.76937  ? 139 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 139 ? 23.71235 17.42278 -13.24390 1.000 29.21295  ? 139 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 139 ? 23.58881 16.11203 -12.46546 1.000 25.43981  ? 139 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 139 ? 24.39747 18.52117 -12.41607 1.000 28.84328  ? 139 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 139 ? 24.89932 15.35009 -12.21257 1.000 23.13304  ? 139 ILE A CD1 1 
ATOM   1061 N N   . ASN A 1 140 ? 21.82442 20.27875 -14.06594 1.000 30.01891  ? 140 ASN A N   1 
ATOM   1062 C CA  . ASN A 1 140 ? 21.85113 21.56767 -14.76280 1.000 32.04062  ? 140 ASN A CA  1 
ATOM   1063 C C   . ASN A 1 140 ? 21.48895 21.38623 -16.24464 1.000 36.11522  ? 140 ASN A C   1 
ATOM   1064 O O   . ASN A 1 140 ? 22.13799 21.91260 -17.15005 1.000 33.76174  ? 140 ASN A O   1 
ATOM   1065 C CB  . ASN A 1 140 ? 23.20932 22.27537 -14.57309 1.000 28.32808  ? 140 ASN A CB  1 
ATOM   1066 C CG  . ASN A 1 140 ? 23.52849 22.52075 -13.06956 1.000 33.57960  ? 140 ASN A CG  1 
ATOM   1067 O OD1 . ASN A 1 140 ? 22.67851 22.98574 -12.33281 1.000 30.68289  ? 140 ASN A OD1 1 
ATOM   1068 N ND2 . ASN A 1 140 ? 24.74283 22.17762 -12.62652 1.000 31.06330  ? 140 ASN A ND2 1 
ATOM   1069 N N   . ASP A 1 141 ? 20.42594 20.61898 -16.48037 1.000 34.01080  ? 141 ASP A N   1 
ATOM   1070 C CA  . ASP A 1 141 ? 19.87053 20.32681 -17.80456 1.000 38.95696  ? 141 ASP A CA  1 
ATOM   1071 C C   . ASP A 1 141 ? 20.74218 19.38622 -18.64868 1.000 37.53428  ? 141 ASP A C   1 
ATOM   1072 O O   . ASP A 1 141 ? 20.39289 19.08749 -19.78066 1.000 43.60119  ? 141 ASP A O   1 
ATOM   1073 C CB  . ASP A 1 141 ? 19.56287 21.62271 -18.56601 1.000 42.76514  ? 141 ASP A CB  1 
ATOM   1074 C CG  . ASP A 1 141 ? 18.62737 22.54660 -17.76807 1.000 46.58451  ? 141 ASP A CG  1 
ATOM   1075 O OD1 . ASP A 1 141 ? 17.73488 22.01023 -17.07982 1.000 44.89350  ? 141 ASP A OD1 1 
ATOM   1076 O OD2 . ASP A 1 141 ? 18.77833 23.79085 -17.80819 1.000 51.19808  ? 141 ASP A OD2 1 
ATOM   1077 N N   . ILE A 1 142 ? 21.83166 18.86420 -18.10651 1.000 37.38744  ? 142 ILE A N   1 
ATOM   1078 C CA  . ILE A 1 142 ? 22.69698 17.89848 -18.78056 1.000 40.15208  ? 142 ILE A CA  1 
ATOM   1079 C C   . ILE A 1 142 ? 22.32335 16.49040 -18.31448 1.000 35.93061  ? 142 ILE A C   1 
ATOM   1080 O O   . ILE A 1 142 ? 22.36265 16.19759 -17.11432 1.000 34.52919  ? 142 ILE A O   1 
ATOM   1081 C CB  . ILE A 1 142 ? 24.17774 18.18515 -18.47541 1.000 45.62003  ? 142 ILE A CB  1 
ATOM   1082 C CG1 . ILE A 1 142 ? 24.60126 19.56178 -19.01071 1.000 54.65011  ? 142 ILE A CG1 1 
ATOM   1083 C CG2 . ILE A 1 142 ? 25.06384 17.05182 -18.98289 1.000 53.81435  ? 142 ILE A CG2 1 
ATOM   1084 C CD1 . ILE A 1 142 ? 23.89771 19.99452 -20.30018 1.000 52.54459  ? 142 ILE A CD1 1 
ATOM   1085 N N   . HIS A 1 143 ? 21.98754 15.60368 -19.24957 1.000 37.50428  ? 143 HIS A N   1 
ATOM   1086 C CA  A HIS A 1 143 ? 21.63301 14.23295 -18.87072 0.500 35.52832  ? 143 HIS A CA  1 
ATOM   1087 C CA  B HIS A 1 143 ? 21.63732 14.23383 -18.90294 0.500 37.77936  ? 143 HIS A CA  1 
ATOM   1088 C C   . HIS A 1 143 ? 22.87787 13.50676 -18.40992 1.000 34.92905  ? 143 HIS A C   1 
ATOM   1089 O O   . HIS A 1 143 ? 23.75300 13.17796 -19.21568 1.000 34.43664  ? 143 HIS A O   1 
ATOM   1090 C CB  A HIS A 1 143 ? 20.98647 13.42178 -19.99148 0.500 36.47160  ? 143 HIS A CB  1 
ATOM   1091 C CB  B HIS A 1 143 ? 21.02755 13.53525 -20.11649 0.500 36.17217  ? 143 HIS A CB  1 
ATOM   1092 C CG  A HIS A 1 143 ? 20.78861 11.97699 -19.61244 0.500 37.00790  ? 143 HIS A CG  1 
ATOM   1093 C CG  B HIS A 1 143 ? 19.60868 13.93078 -20.38174 0.500 37.22593  ? 143 HIS A CG  1 
ATOM   1094 N ND1 A HIS A 1 143 ? 21.77258 11.02061 -19.77526 0.500 36.27833  ? 143 HIS A ND1 1 
ATOM   1095 N ND1 B HIS A 1 143 ? 18.53363 13.17511 -19.96061 0.500 39.84650  ? 143 HIS A ND1 1 
ATOM   1096 C CD2 A HIS A 1 143 ? 19.75064 11.34310 -19.00791 0.500 35.19590  ? 143 HIS A CD2 1 
ATOM   1097 C CD2 B HIS A 1 143 ? 19.08553 15.01694 -20.99620 0.500 38.24684  ? 143 HIS A CD2 1 
ATOM   1098 C CE1 A HIS A 1 143 ? 21.33655 9.85631  -19.32227 0.500 35.07720  ? 143 HIS A CE1 1 
ATOM   1099 C CE1 B HIS A 1 143 ? 17.41128 13.77063 -20.32175 0.500 41.09511  ? 143 HIS A CE1 1 
ATOM   1100 N NE2 A HIS A 1 143 ? 20.10996 10.02241 -18.85936 0.500 34.43143  ? 143 HIS A NE2 1 
ATOM   1101 N NE2 B HIS A 1 143 ? 17.71873 14.88886 -20.95490 0.500 40.24532  ? 143 HIS A NE2 1 
ATOM   1102 N N   . PHE A 1 144 ? 22.92692 13.22592 -17.11508 1.000 28.94874  ? 144 PHE A N   1 
ATOM   1103 C CA  . PHE A 1 144 ? 24.07782 12.59563 -16.49522 1.000 29.55147  ? 144 PHE A CA  1 
ATOM   1104 C C   . PHE A 1 144 ? 24.01814 11.06722 -16.51351 1.000 28.82110  ? 144 PHE A C   1 
ATOM   1105 O O   . PHE A 1 144 ? 25.01683 10.42262 -16.83453 1.000 27.26546  ? 144 PHE A O   1 
ATOM   1106 C CB  . PHE A 1 144 ? 24.22118 13.09514 -15.04391 1.000 23.94332  ? 144 PHE A CB  1 
ATOM   1107 C CG  . PHE A 1 144 ? 25.39280 12.54238 -14.35158 1.000 23.63349  ? 144 PHE A CG  1 
ATOM   1108 C CD1 . PHE A 1 144 ? 26.67226 12.98313 -14.66738 1.000 23.66305  ? 144 PHE A CD1 1 
ATOM   1109 C CD2 . PHE A 1 144 ? 25.23675 11.59650 -13.34830 1.000 24.68370  ? 144 PHE A CD2 1 
ATOM   1110 C CE1 . PHE A 1 144 ? 27.77597 12.46593 -14.01422 1.000 24.92975  ? 144 PHE A CE1 1 
ATOM   1111 C CE2 . PHE A 1 144 ? 26.35049 11.07837 -12.66362 1.000 23.30559  ? 144 PHE A CE2 1 
ATOM   1112 C CZ  . PHE A 1 144 ? 27.61286 11.50488 -13.00147 1.000 24.77215  ? 144 PHE A CZ  1 
ATOM   1113 N N   . GLU A 1 145 ? 22.90182 10.46067 -16.11130 1.000 25.73098  ? 145 GLU A N   1 
ATOM   1114 C CA  . GLU A 1 145 ? 22.88939 9.00603  -16.05063 1.000 27.08495  ? 145 GLU A CA  1 
ATOM   1115 C C   . GLU A 1 145 ? 21.44607 8.53340  -16.01637 1.000 28.55299  ? 145 GLU A C   1 
ATOM   1116 O O   . GLU A 1 145 ? 20.53454 9.30410  -15.69893 1.000 28.45993  ? 145 GLU A O   1 
ATOM   1117 C CB  . GLU A 1 145 ? 23.67186 8.48329  -14.82377 1.000 24.72720  ? 145 GLU A CB  1 
ATOM   1118 C CG  . GLU A 1 145 ? 22.94045 8.78193  -13.48525 1.000 26.67232  ? 145 GLU A CG  1 
ATOM   1119 C CD  . GLU A 1 145 ? 23.69500 8.35323  -12.21960 1.000 24.92756  ? 145 GLU A CD  1 
ATOM   1120 O OE1 . GLU A 1 145 ? 24.82861 7.83258  -12.27564 1.000 25.83377  ? 145 GLU A OE1 1 
ATOM   1121 O OE2 . GLU A 1 145 ? 23.12848 8.54581  -11.13884 1.000 24.61565  ? 145 GLU A OE2 1 
ATOM   1122 N N   . ARG A 1 146 ? 21.24423 7.25615  -16.37252 1.000 27.81308  ? 146 ARG A N   1 
ATOM   1123 C CA  . ARG A 1 146 ? 19.96728 6.56589  -16.17537 1.000 33.15252  ? 146 ARG A CA  1 
ATOM   1124 C C   . ARG A 1 146 ? 20.13055 5.62454  -14.97711 1.000 27.72232  ? 146 ARG A C   1 
ATOM   1125 O O   . ARG A 1 146 ? 20.88132 4.65444  -15.04999 1.000 29.57568  ? 146 ARG A O   1 
ATOM   1126 C CB  . ARG A 1 146 ? 19.54925 5.80357  -17.43883 1.000 34.03899  ? 146 ARG A CB  1 
ATOM   1127 C CG  . ARG A 1 146 ? 18.19269 5.10129  -17.34715 1.000 36.15704  ? 146 ARG A CG  1 
ATOM   1128 C CD  . ARG A 1 146 ? 17.56297 4.75196  -18.71959 1.000 38.52846  ? 146 ARG A CD  1 
ATOM   1129 N NE  . ARG A 1 146 ? 16.88114 5.91287  -19.27153 1.000 35.89727  ? 146 ARG A NE  1 
ATOM   1130 C CZ  . ARG A 1 146 ? 16.18147 5.94841  -20.40589 1.000 43.82021  ? 146 ARG A CZ  1 
ATOM   1131 N NH1 . ARG A 1 146 ? 16.06398 4.88719  -21.19306 1.000 43.23308  ? 146 ARG A NH1 1 
ATOM   1132 N NH2 . ARG A 1 146 ? 15.58372 7.08473  -20.76272 1.000 41.55862  ? 146 ARG A NH2 1 
ATOM   1133 N N   . PHE A 1 147 ? 19.44757 5.91550  -13.87831 1.000 28.92162  ? 147 PHE A N   1 
ATOM   1134 C CA  . PHE A 1 147 ? 19.60999 5.15973  -12.63484 1.000 27.43983  ? 147 PHE A CA  1 
ATOM   1135 C C   . PHE A 1 147 ? 18.57064 4.04975  -12.53873 1.000 29.36531  ? 147 PHE A C   1 
ATOM   1136 O O   . PHE A 1 147 ? 17.36399 4.30608  -12.57645 1.000 30.00583  ? 147 PHE A O   1 
ATOM   1137 C CB  . PHE A 1 147 ? 19.49626 6.05253  -11.40151 1.000 28.83196  ? 147 PHE A CB  1 
ATOM   1138 C CG  . PHE A 1 147 ? 19.64625 5.28979  -10.09794 1.000 25.17366  ? 147 PHE A CG  1 
ATOM   1139 C CD1 . PHE A 1 147 ? 18.58625 4.59469  -9.56147  1.000 27.38438  ? 147 PHE A CD1 1 
ATOM   1140 C CD2 . PHE A 1 147 ? 20.86399 5.22351  -9.46227  1.000 26.30252  ? 147 PHE A CD2 1 
ATOM   1141 C CE1 . PHE A 1 147 ? 18.73380 3.86521  -8.39117  1.000 28.11166  ? 147 PHE A CE1 1 
ATOM   1142 C CE2 . PHE A 1 147 ? 21.00942 4.51387  -8.28441  1.000 25.53923  ? 147 PHE A CE2 1 
ATOM   1143 C CZ  . PHE A 1 147 ? 19.94985 3.83161  -7.75976  1.000 26.02162  ? 147 PHE A CZ  1 
ATOM   1144 N N   . ARG A 1 148 ? 19.04340 2.82141  -12.39192 1.000 27.94405  ? 148 ARG A N   1 
ATOM   1145 C CA  . ARG A 1 148 ? 18.19264 1.67068  -12.13728 1.000 31.60559  ? 148 ARG A CA  1 
ATOM   1146 C C   . ARG A 1 148 ? 18.59005 1.07503  -10.80196 1.000 28.64308  ? 148 ARG A C   1 
ATOM   1147 O O   . ARG A 1 148 ? 19.77936 0.83833  -10.56991 1.000 28.91477  ? 148 ARG A O   1 
ATOM   1148 C CB  . ARG A 1 148 ? 18.33208 0.61074  -13.22250 1.000 33.77992  ? 148 ARG A CB  1 
ATOM   1149 C CG  . ARG A 1 148 ? 17.83373 1.00365  -14.55916 1.000 40.40764  ? 148 ARG A CG  1 
ATOM   1150 C CD  . ARG A 1 148 ? 17.97889 -0.16507 -15.49930 1.000 47.41491  ? 148 ARG A CD  1 
ATOM   1151 N NE  . ARG A 1 148 ? 17.28652 0.09578  -16.75774 1.000 52.58917  ? 148 ARG A NE  1 
ATOM   1152 C CZ  . ARG A 1 148 ? 17.69831 0.96203  -17.66603 1.000 50.20337  ? 148 ARG A CZ  1 
ATOM   1153 N NH1 . ARG A 1 148 ? 18.83163 1.63629  -17.51603 1.000 45.45202  ? 148 ARG A NH1 1 
ATOM   1154 N NH2 . ARG A 1 148 ? 16.95015 1.16106  -18.74936 1.000 57.66874  ? 148 ARG A NH2 1 
ATOM   1155 N N   . GLY A 1 149 ? 17.60764 0.81056  -9.94460  1.000 28.99685  ? 149 GLY A N   1 
ATOM   1156 C CA  . GLY A 1 149 ? 17.90516 0.31695  -8.57404  1.000 30.63055  ? 149 GLY A CA  1 
ATOM   1157 C C   . GLY A 1 149 ? 16.75769 0.61276  -7.60999  1.000 31.13665  ? 149 GLY A C   1 
ATOM   1158 O O   . GLY A 1 149 ? 15.61419 0.79460  -8.02816  1.000 32.24794  ? 149 GLY A O   1 
ATOM   1159 N N   . ASP A 1 150 ? 17.09461 0.65614  -6.31096  1.000 31.59430  ? 150 ASP A N   1 
ATOM   1160 C CA  . ASP A 1 150 ? 16.08874 0.86857  -5.26563  1.000 30.89733  ? 150 ASP A CA  1 
ATOM   1161 C C   . ASP A 1 150 ? 15.70596 2.33862  -5.12920  1.000 28.94744  ? 150 ASP A C   1 
ATOM   1162 O O   . ASP A 1 150 ? 14.52927 2.65101  -4.94359  1.000 33.13128  ? 150 ASP A O   1 
ATOM   1163 C CB  . ASP A 1 150 ? 16.58179 0.33495  -3.91188  1.000 27.16727  ? 150 ASP A CB  1 
ATOM   1164 C CG  . ASP A 1 150 ? 16.59412 -1.17018 -3.84165  1.000 28.99872  ? 150 ASP A CG  1 
ATOM   1165 O OD1 . ASP A 1 150 ? 16.17522 -1.82782 -4.80272  1.000 33.83152  ? 150 ASP A OD1 1 
ATOM   1166 O OD2 . ASP A 1 150 ? 17.03014 -1.71149 -2.81823  1.000 30.66608  ? 150 ASP A OD2 1 
ATOM   1167 N N   . GLY A 1 151 ? 16.65819 3.25765  -5.21001  1.000 27.23638  ? 151 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 151 ? 16.30305 4.65677  -5.11518  1.000 27.60399  ? 151 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 151 ? 17.50702 5.55578  -4.92152  1.000 25.89447  ? 151 GLY A C   1 
ATOM   1170 O O   . GLY A 1 151 ? 18.65466 5.12097  -4.97565  1.000 27.73742  ? 151 GLY A O   1 
ATOM   1171 N N   . LEU A 1 152 ? 17.20548 6.83280  -4.70595  1.000 23.70105  ? 152 LEU A N   1 
ATOM   1172 C CA  . LEU A 1 152 ? 18.18079 7.89116  -4.56074  1.000 25.32661  ? 152 LEU A CA  1 
ATOM   1173 C C   . LEU A 1 152 ? 17.91122 8.69811  -3.28437  1.000 24.89491  ? 152 LEU A C   1 
ATOM   1174 O O   . LEU A 1 152 ? 16.77220 8.86894  -2.85680  1.000 22.79175  ? 152 LEU A O   1 
ATOM   1175 C CB  . LEU A 1 152 ? 18.13975 8.81107  -5.81378  1.000 22.72469  ? 152 LEU A CB  1 
ATOM   1176 C CG  . LEU A 1 152 ? 18.66231 8.17999  -7.10788  1.000 26.10406  ? 152 LEU A CG  1 
ATOM   1177 C CD1 . LEU A 1 152 ? 18.22977 8.95507  -8.36211  1.000 25.88882  ? 152 LEU A CD1 1 
ATOM   1178 C CD2 . LEU A 1 152 ? 20.15561 8.04675  -7.07838  1.000 22.88963  ? 152 LEU A CD2 1 
ATOM   1179 N N   . CYS A 1 153 ? 18.97412 9.22780  -2.70084  1.000 24.08411  ? 153 CYS A N   1 
ATOM   1180 C CA  . CYS A 1 153 ? 18.90652 9.98546  -1.45525  1.000 23.47596  ? 153 CYS A CA  1 
ATOM   1181 C C   . CYS A 1 153 ? 19.64534 11.30502 -1.62333  1.000 22.53910  ? 153 CYS A C   1 
ATOM   1182 O O   . CYS A 1 153 ? 20.82418 11.30372 -1.98084  1.000 21.69488  ? 153 CYS A O   1 
ATOM   1183 C CB  . CYS A 1 153 ? 19.52661 9.17549  -0.30575  1.000 24.47864  ? 153 CYS A CB  1 
ATOM   1184 S SG  . CYS A 1 153 ? 19.60382 10.13078 1.30872   1.000 23.94118  ? 153 CYS A SG  1 
ATOM   1185 N N   . MET A 1 154 ? 18.97283 12.43653 -1.37127  1.000 22.88599  ? 154 MET A N   1 
ATOM   1186 C CA  . MET A 1 154 ? 19.61681 13.74718 -1.46414  1.000 23.55141  ? 154 MET A CA  1 
ATOM   1187 C C   . MET A 1 154 ? 19.67876 14.37004 -0.08214  1.000 23.63075  ? 154 MET A C   1 
ATOM   1188 O O   . MET A 1 154 ? 18.64038 14.63014 0.51995   1.000 20.40592  ? 154 MET A O   1 
ATOM   1189 C CB  . MET A 1 154 ? 18.88130 14.69945 -2.40510  1.000 23.26099  ? 154 MET A CB  1 
ATOM   1190 C CG  . MET A 1 154 ? 19.71907 15.98251 -2.63282  1.000 25.55756  ? 154 MET A CG  1 
ATOM   1191 S SD  . MET A 1 154 ? 21.29963 15.71440 -3.56345  1.000 27.69523  ? 154 MET A SD  1 
ATOM   1192 C CE  . MET A 1 154 ? 20.79381 16.17399 -5.20599  1.000 23.03347  ? 154 MET A CE  1 
ATOM   1193 N N   . SER A 1 155 ? 20.88617 14.66436 0.39122   1.000 23.28473  ? 155 SER A N   1 
ATOM   1194 C CA  . SER A 1 155 ? 21.11724 14.94990 1.80363   1.000 21.88499  ? 155 SER A CA  1 
ATOM   1195 C C   . SER A 1 155 ? 21.61747 16.37650 2.00226   1.000 23.47641  ? 155 SER A C   1 
ATOM   1196 O O   . SER A 1 155 ? 22.42270 16.88466 1.21411   1.000 24.81557  ? 155 SER A O   1 
ATOM   1197 C CB  . SER A 1 155 ? 22.14302 13.95384 2.37474   1.000 20.30869  ? 155 SER A CB  1 
ATOM   1198 O OG  . SER A 1 155 ? 22.48634 14.26391 3.74433   1.000 24.41669  ? 155 SER A OG  1 
ATOM   1199 N N   . THR A 1 156 ? 21.17451 17.00952 3.07211   1.000 22.87546  ? 156 THR A N   1 
ATOM   1200 C CA  . THR A 1 156 ? 21.78648 18.25651 3.51362   1.000 21.44903  ? 156 THR A CA  1 
ATOM   1201 C C   . THR A 1 156 ? 23.14277 17.94483 4.12856   1.000 21.20306  ? 156 THR A C   1 
ATOM   1202 O O   . THR A 1 156 ? 23.47784 16.78227 4.33385   1.000 19.82120  ? 156 THR A O   1 
ATOM   1203 C CB  . THR A 1 156 ? 20.90098 18.93558 4.54502   1.000 22.20142  ? 156 THR A CB  1 
ATOM   1204 O OG1 . THR A 1 156 ? 20.97366 18.17822 5.75331   1.000 23.01710  ? 156 THR A OG1 1 
ATOM   1205 C CG2 . THR A 1 156 ? 19.43596 19.01956 4.07170   1.000 23.15920  ? 156 THR A CG2 1 
ATOM   1206 N N   . PRO A 1 157 ? 23.95147 18.95998 4.43394   1.000 21.00796  ? 157 PRO A N   1 
ATOM   1207 C CA  . PRO A 1 157 ? 25.18300 18.69058 5.21528   1.000 22.55126  ? 157 PRO A CA  1 
ATOM   1208 C C   . PRO A 1 157 ? 24.91461 18.04402 6.57303   1.000 22.45543  ? 157 PRO A C   1 
ATOM   1209 O O   . PRO A 1 157 ? 25.49920 16.98762 6.88142   1.000 19.01027  ? 157 PRO A O   1 
ATOM   1210 C CB  . PRO A 1 157 ? 25.82148 20.07542 5.34245   1.000 24.77787  ? 157 PRO A CB  1 
ATOM   1211 C CG  . PRO A 1 157 ? 25.29145 20.84505 4.09919   1.000 26.79274  ? 157 PRO A CG  1 
ATOM   1212 C CD  . PRO A 1 157 ? 23.86982 20.35987 3.95267   1.000 22.17145  ? 157 PRO A CD  1 
ATOM   1213 N N   . SER A 1 158 ? 23.99841 18.59923 7.38200   1.000 22.66824  ? 158 SER A N   1 
ATOM   1214 C CA  . SER A 1 158 ? 23.71712 17.95005 8.66852   1.000 23.10056  ? 158 SER A CA  1 
ATOM   1215 C C   . SER A 1 158 ? 22.95433 16.63637 8.50791   1.000 22.39772  ? 158 SER A C   1 
ATOM   1216 O O   . SER A 1 158 ? 22.94133 15.81904 9.42978   1.000 23.49795  ? 158 SER A O   1 
ATOM   1217 C CB  . SER A 1 158 ? 22.96868 18.88524 9.61232   1.000 24.28167  ? 158 SER A CB  1 
ATOM   1218 O OG  . SER A 1 158 ? 21.73906 19.35225 9.06554   1.000 25.79611  ? 158 SER A OG  1 
ATOM   1219 N N   . GLY A 1 159 ? 22.37293 16.37573 7.34930   1.000 22.83977  ? 159 GLY A N   1 
ATOM   1220 C CA  . GLY A 1 159 ? 21.83789 15.04763 7.15541   1.000 22.09838  ? 159 GLY A CA  1 
ATOM   1221 C C   . GLY A 1 159 ? 22.87108 14.00307 6.78484   1.000 23.25317  ? 159 GLY A C   1 
ATOM   1222 O O   . GLY A 1 159 ? 22.54080 12.81283 6.71536   1.000 24.56808  ? 159 GLY A O   1 
ATOM   1223 N N   . THR A 1 160 ? 24.11724 14.40976 6.52948   1.000 20.07435  ? 160 THR A N   1 
ATOM   1224 C CA  . THR A 1 160 ? 25.07330 13.44057 6.01221   1.000 22.85043  ? 160 THR A CA  1 
ATOM   1225 C C   . THR A 1 160 ? 25.39053 12.35472 7.01578   1.000 23.21556  ? 160 THR A C   1 
ATOM   1226 O O   . THR A 1 160 ? 25.85033 11.26786 6.60914   1.000 22.42844  ? 160 THR A O   1 
ATOM   1227 C CB  . THR A 1 160 ? 26.38173 14.10458 5.53222   1.000 22.76241  ? 160 THR A CB  1 
ATOM   1228 O OG1 . THR A 1 160 ? 26.91164 14.99908 6.53199   1.000 22.93503  ? 160 THR A OG1 1 
ATOM   1229 C CG2 . THR A 1 160 ? 26.11889 14.87046 4.23012   1.000 20.86525  ? 160 THR A CG2 1 
ATOM   1230 N N   . THR A 1 161 ? 25.14375 12.60584 8.30182   1.000 20.90323  ? 161 THR A N   1 
ATOM   1231 C CA  . THR A 1 161 ? 25.34905 11.58385 9.32327   1.000 23.75015  ? 161 THR A CA  1 
ATOM   1232 C C   . THR A 1 161 ? 24.13265 10.68852 9.53775   1.000 23.85707  ? 161 THR A C   1 
ATOM   1233 O O   . THR A 1 161 ? 24.18929 9.77198  10.37261  1.000 21.84741  ? 161 THR A O   1 
ATOM   1234 C CB  . THR A 1 161 ? 25.75502 12.22770 10.65379  1.000 25.00071  ? 161 THR A CB  1 
ATOM   1235 O OG1 . THR A 1 161 ? 24.82432 13.24932 11.02815  1.000 26.22140  ? 161 THR A OG1 1 
ATOM   1236 C CG2 . THR A 1 161 ? 27.15735 12.83700 10.55097  1.000 26.08616  ? 161 THR A CG2 1 
ATOM   1237 N N   . ALA A 1 162 ? 23.05281 10.91688 8.80367   1.000 22.78435  ? 162 ALA A N   1 
ATOM   1238 C CA  . ALA A 1 162 ? 21.82744 10.14003 8.93780   1.000 24.65201  ? 162 ALA A CA  1 
ATOM   1239 C C   . ALA A 1 162 ? 21.79309 9.09757  7.81488   1.000 25.46622  ? 162 ALA A C   1 
ATOM   1240 O O   . ALA A 1 162 ? 22.80341 8.41693  7.62493   1.000 22.63961  ? 162 ALA A O   1 
ATOM   1241 C CB  . ALA A 1 162 ? 20.62234 11.08721 8.96687   1.000 24.53732  ? 162 ALA A CB  1 
ATOM   1242 N N   . TYR A 1 163 ? 20.70344 8.97939  7.04603   1.000 25.95626  ? 163 TYR A N   1 
ATOM   1243 C CA  . TYR A 1 163 ? 20.56259 7.98924  5.97869   1.000 26.73990  ? 163 TYR A CA  1 
ATOM   1244 C C   . TYR A 1 163 ? 21.74715 8.00393  5.00402   1.000 22.33464  ? 163 TYR A C   1 
ATOM   1245 O O   . TYR A 1 163 ? 22.24820 6.95691  4.59176   1.000 23.14019  ? 163 TYR A O   1 
ATOM   1246 C CB  . TYR A 1 163 ? 19.25455 8.28923  5.24699   1.000 26.32884  ? 163 TYR A CB  1 
ATOM   1247 C CG  . TYR A 1 163 ? 18.58658 7.13806  4.54504   1.000 27.67401  ? 163 TYR A CG  1 
ATOM   1248 C CD1 . TYR A 1 163 ? 19.15342 5.87278  4.48734   1.000 28.82606  ? 163 TYR A CD1 1 
ATOM   1249 C CD2 . TYR A 1 163 ? 17.37446 7.33509  3.93404   1.000 32.26713  ? 163 TYR A CD2 1 
ATOM   1250 C CE1 . TYR A 1 163 ? 18.50581 4.83809  3.84617   1.000 30.31136  ? 163 TYR A CE1 1 
ATOM   1251 C CE2 . TYR A 1 163 ? 16.72243 6.33625  3.28950   1.000 38.55669  ? 163 TYR A CE2 1 
ATOM   1252 C CZ  . TYR A 1 163 ? 17.27575 5.08920  3.22812   1.000 35.06992  ? 163 TYR A CZ  1 
ATOM   1253 O OH  . TYR A 1 163 ? 16.55189 4.12451  2.54741   1.000 32.93123  ? 163 TYR A OH  1 
ATOM   1254 N N   . ASN A 1 164 ? 22.18236 9.19045  4.61489   1.000 20.92495  ? 164 ASN A N   1 
ATOM   1255 C CA  . ASN A 1 164 ? 23.33865 9.34157  3.73616   1.000 21.84549  ? 164 ASN A CA  1 
ATOM   1256 C C   . ASN A 1 164 ? 24.52324 8.51666  4.22200   1.000 24.51725  ? 164 ASN A C   1 
ATOM   1257 O O   . ASN A 1 164 ? 25.21399 7.86347  3.41849   1.000 21.39348  ? 164 ASN A O   1 
ATOM   1258 C CB  . ASN A 1 164 ? 23.69666 10.83518 3.63195   1.000 21.47917  ? 164 ASN A CB  1 
ATOM   1259 C CG  . ASN A 1 164 ? 25.02505 11.08638 2.93027   1.000 22.34608  ? 164 ASN A CG  1 
ATOM   1260 O OD1 . ASN A 1 164 ? 25.06782 11.30464 1.71328   1.000 20.85623  ? 164 ASN A OD1 1 
ATOM   1261 N ND2 . ASN A 1 164 ? 26.12423 11.07302 3.70397   1.000 19.90306  ? 164 ASN A ND2 1 
ATOM   1262 N N   . LYS A 1 165 ? 24.75136 8.49424  5.54765   1.000 23.31836  ? 165 LYS A N   1 
ATOM   1263 C CA  . LYS A 1 165 ? 25.89655 7.76575  6.07706   1.000 21.98044  ? 165 LYS A CA  1 
ATOM   1264 C C   . LYS A 1 165 ? 25.75558 6.27106  5.82871   1.000 21.35701  ? 165 LYS A C   1 
ATOM   1265 O O   . LYS A 1 165 ? 26.73164 5.60188  5.47115   1.000 17.02712  ? 165 LYS A O   1 
ATOM   1266 C CB  . LYS A 1 165 ? 26.05983 8.03955  7.57538   1.000 22.07851  ? 165 LYS A CB  1 
ATOM   1267 C CG  . LYS A 1 165 ? 27.28241 7.34234  8.20525   1.000 21.06171  ? 165 LYS A CG  1 
ATOM   1268 C CD  . LYS A 1 165 ? 27.52580 7.77758  9.66198   1.000 24.48036  ? 165 LYS A CD  1 
ATOM   1269 C CE  . LYS A 1 165 ? 28.83201 7.20681  10.15610  1.000 25.72329  ? 165 LYS A CE  1 
ATOM   1270 N NZ  . LYS A 1 165 ? 28.72468 5.71090  10.26119  1.000 32.73786  ? 165 LYS A NZ  1 
ATOM   1271 N N   . SER A 1 166 ? 24.55144 5.73165  6.05601   1.000 19.65387  ? 166 SER A N   1 
ATOM   1272 C CA  . SER A 1 166 ? 24.33085 4.30655  5.89746   1.000 23.27672  ? 166 SER A CA  1 
ATOM   1273 C C   . SER A 1 166 ? 24.40931 3.88926  4.43750   1.000 22.96163  ? 166 SER A C   1 
ATOM   1274 O O   . SER A 1 166 ? 24.57185 2.70521  4.15610   1.000 21.21616  ? 166 SER A O   1 
ATOM   1275 C CB  . SER A 1 166 ? 22.96188 3.90664  6.46274   1.000 22.79644  ? 166 SER A CB  1 
ATOM   1276 O OG  . SER A 1 166 ? 22.86181 4.24745  7.81851   1.000 28.45797  ? 166 SER A OG  1 
ATOM   1277 N N   . LEU A 1 167 ? 24.28563 4.83424  3.51333   1.000 24.37679  ? 167 LEU A N   1 
ATOM   1278 C CA  . LEU A 1 167 ? 24.38416 4.54523  2.09279   1.000 22.47319  ? 167 LEU A CA  1 
ATOM   1279 C C   . LEU A 1 167 ? 25.78328 4.72905  1.55402   1.000 24.37696  ? 167 LEU A C   1 
ATOM   1280 O O   . LEU A 1 167 ? 25.98066 4.60086  0.33614   1.000 23.97449  ? 167 LEU A O   1 
ATOM   1281 C CB  . LEU A 1 167 ? 23.41715 5.42535  1.31425   1.000 20.67812  ? 167 LEU A CB  1 
ATOM   1282 C CG  . LEU A 1 167 ? 21.96467 5.18605  1.68472   1.000 22.92180  ? 167 LEU A CG  1 
ATOM   1283 C CD1 . LEU A 1 167 ? 21.10460 6.33170  1.21477   1.000 23.50826  ? 167 LEU A CD1 1 
ATOM   1284 C CD2 . LEU A 1 167 ? 21.51410 3.84789  1.11769   1.000 24.22824  ? 167 LEU A CD2 1 
ATOM   1285 N N   . GLY A 1 168 ? 26.77019 5.01536  2.41318   1.000 21.70268  ? 168 GLY A N   1 
ATOM   1286 C CA  . GLY A 1 168 ? 28.12992 5.15448  1.90099   1.000 20.17629  ? 168 GLY A CA  1 
ATOM   1287 C C   . GLY A 1 168 ? 28.53587 6.58358  1.64278   1.000 20.80899  ? 168 GLY A C   1 
ATOM   1288 O O   . GLY A 1 168 ? 29.68360 6.81732  1.23387   1.000 21.16662  ? 168 GLY A O   1 
ATOM   1289 N N   . GLY A 1 169 ? 27.65038 7.55697  1.92455   1.000 16.41495  ? 169 GLY A N   1 
ATOM   1290 C CA  . GLY A 1 169 ? 27.96498 8.95316  1.65908   1.000 16.97091  ? 169 GLY A CA  1 
ATOM   1291 C C   . GLY A 1 169 ? 29.07061 9.48621  2.55770   1.000 22.38728  ? 169 GLY A C   1 
ATOM   1292 O O   . GLY A 1 169 ? 29.44592 8.89597  3.58166   1.000 20.46050  ? 169 GLY A O   1 
ATOM   1293 N N   . ALA A 1 170 ? 29.60610 10.62987 2.15351   1.000 19.94098  ? 170 ALA A N   1 
ATOM   1294 C CA  . ALA A 1 170 ? 30.58752 11.33589 2.94415   1.000 21.42923  ? 170 ALA A CA  1 
ATOM   1295 C C   . ALA A 1 170 ? 29.88550 12.19288 3.98933   1.000 23.06984  ? 170 ALA A C   1 
ATOM   1296 O O   . ALA A 1 170 ? 28.77595 12.67081 3.76022   1.000 23.51804  ? 170 ALA A O   1 
ATOM   1297 C CB  . ALA A 1 170 ? 31.45427 12.23287 2.05678   1.000 19.85230  ? 170 ALA A CB  1 
ATOM   1298 N N   . LEU A 1 171 ? 30.54244 12.38020 5.14337   1.000 21.86854  ? 171 LEU A N   1 
ATOM   1299 C CA  . LEU A 1 171 ? 30.09132 13.34348 6.14953   1.000 21.16541  ? 171 LEU A CA  1 
ATOM   1300 C C   . LEU A 1 171 ? 30.62108 14.71929 5.78298   1.000 22.05817  ? 171 LEU A C   1 
ATOM   1301 O O   . LEU A 1 171 ? 31.81373 14.87743 5.52979   1.000 23.89994  ? 171 LEU A O   1 
ATOM   1302 C CB  . LEU A 1 171 ? 30.58014 12.97191 7.54553   1.000 19.95487  ? 171 LEU A CB  1 
ATOM   1303 C CG  . LEU A 1 171 ? 30.36784 11.51337 7.91936   1.000 21.67110  ? 171 LEU A CG  1 
ATOM   1304 C CD1 . LEU A 1 171 ? 30.65652 11.20532 9.39437   1.000 18.70736  ? 171 LEU A CD1 1 
ATOM   1305 C CD2 . LEU A 1 171 ? 28.93007 11.03624 7.47185   1.000 20.50257  ? 171 LEU A CD2 1 
ATOM   1306 N N   . MET A 1 172 ? 29.74595 15.71807 5.77187   1.000 23.45125  ? 172 MET A N   1 
ATOM   1307 C CA  . MET A 1 172 ? 30.09005 17.05392 5.29553   1.000 23.54486  ? 172 MET A CA  1 
ATOM   1308 C C   . MET A 1 172 ? 29.87787 18.06960 6.40118   1.000 27.34449  ? 172 MET A C   1 
ATOM   1309 O O   . MET A 1 172 ? 28.79061 18.12036 6.99812   1.000 23.22886  ? 172 MET A O   1 
ATOM   1310 C CB  . MET A 1 172 ? 29.20760 17.47312 4.11133   1.000 25.12911  ? 172 MET A CB  1 
ATOM   1311 C CG  . MET A 1 172 ? 29.39343 16.71011 2.84223   1.000 29.74428  ? 172 MET A CG  1 
ATOM   1312 S SD  . MET A 1 172 ? 28.15123 17.35454 1.69424   1.000 41.45488  ? 172 MET A SD  1 
ATOM   1313 C CE  . MET A 1 172 ? 28.81876 18.95774 1.47795   1.000 28.14114  ? 172 MET A CE  1 
ATOM   1314 N N   . HIS A 1 173 ? 30.86300 18.93408 6.59797   1.000 24.58558  ? 173 HIS A N   1 
ATOM   1315 C CA  . HIS A 1 173 ? 30.72315 19.94996 7.62183   1.000 27.36669  ? 173 HIS A CA  1 
ATOM   1316 C C   . HIS A 1 173 ? 29.57981 20.89852 7.27499   1.000 28.58280  ? 173 HIS A C   1 
ATOM   1317 O O   . HIS A 1 173 ? 29.47499 21.34250 6.12600   1.000 30.32674  ? 173 HIS A O   1 
ATOM   1318 C CB  . HIS A 1 173 ? 31.98992 20.75977 7.82592   1.000 27.09025  ? 173 HIS A CB  1 
ATOM   1319 C CG  . HIS A 1 173 ? 31.90020 21.64686 9.02194   1.000 29.75969  ? 173 HIS A CG  1 
ATOM   1320 N ND1 . HIS A 1 173 ? 31.48183 22.95958 8.94126   1.000 31.91003  ? 173 HIS A ND1 1 
ATOM   1321 C CD2 . HIS A 1 173 ? 32.09685 21.39155 10.33747  1.000 28.65181  ? 173 HIS A CD2 1 
ATOM   1322 C CE1 . HIS A 1 173 ? 31.45764 23.48575 10.15449  1.000 31.67561  ? 173 HIS A CE1 1 
ATOM   1323 N NE2 . HIS A 1 173 ? 31.82788 22.55378 11.02031  1.000 31.26932  ? 173 HIS A NE2 1 
ATOM   1324 N N   . PRO A 1 174 ? 28.71962 21.24785 8.24015   1.000 28.54209  ? 174 PRO A N   1 
ATOM   1325 C CA  . PRO A 1 174 ? 27.49285 21.99369 7.90089   1.000 28.75923  ? 174 PRO A CA  1 
ATOM   1326 C C   . PRO A 1 174 ? 27.73320 23.42808 7.46523   1.000 31.53104  ? 174 PRO A C   1 
ATOM   1327 O O   . PRO A 1 174 ? 26.77960 24.07098 7.01955   1.000 33.27708  ? 174 PRO A O   1 
ATOM   1328 C CB  . PRO A 1 174 ? 26.65163 21.94907 9.18716   1.000 32.25905  ? 174 PRO A CB  1 
ATOM   1329 C CG  . PRO A 1 174 ? 27.42673 21.16748 10.21181  1.000 30.13474  ? 174 PRO A CG  1 
ATOM   1330 C CD  . PRO A 1 174 ? 28.76028 20.75571 9.62948   1.000 26.27259  ? 174 PRO A CD  1 
ATOM   1331 N N   . SER A 1 175 ? 28.95618 23.95935 7.56768   1.000 30.57554  ? 175 SER A N   1 
ATOM   1332 C CA  . SER A 1 175 ? 29.24048 25.28015 7.01455   1.000 31.58589  ? 175 SER A CA  1 
ATOM   1333 C C   . SER A 1 175 ? 29.32717 25.27803 5.49826   1.000 32.50507  ? 175 SER A C   1 
ATOM   1334 O O   . SER A 1 175 ? 29.38764 26.35589 4.89652   1.000 31.96388  ? 175 SER A O   1 
ATOM   1335 C CB  . SER A 1 175 ? 30.55439 25.82770 7.56811   1.000 31.44980  ? 175 SER A CB  1 
ATOM   1336 O OG  . SER A 1 175 ? 31.61292 24.92838 7.27403   1.000 31.97114  ? 175 SER A OG  1 
ATOM   1337 N N   . ILE A 1 176 ? 29.38224 24.10737 4.87924   1.000 32.38597  ? 176 ILE A N   1 
ATOM   1338 C CA  . ILE A 1 176 ? 29.47589 23.98357 3.43195   1.000 30.98345  ? 176 ILE A CA  1 
ATOM   1339 C C   . ILE A 1 176 ? 28.06116 23.98863 2.85742   1.000 30.28764  ? 176 ILE A C   1 
ATOM   1340 O O   . ILE A 1 176 ? 27.22250 23.16607 3.24587   1.000 28.37164  ? 176 ILE A O   1 
ATOM   1341 C CB  . ILE A 1 176 ? 30.21397 22.69332 3.05300   1.000 28.53010  ? 176 ILE A CB  1 
ATOM   1342 C CG1 . ILE A 1 176 ? 31.63153 22.70863 3.60342   1.000 30.93331  ? 176 ILE A CG1 1 
ATOM   1343 C CG2 . ILE A 1 176 ? 30.22800 22.50532 1.58407   1.000 27.95187  ? 176 ILE A CG2 1 
ATOM   1344 C CD1 . ILE A 1 176 ? 32.38735 21.38287 3.38695   1.000 28.84718  ? 176 ILE A CD1 1 
ATOM   1345 N N   . GLU A 1 177 ? 27.78963 24.90528 1.92734   1.000 27.66777  ? 177 GLU A N   1 
ATOM   1346 C CA  . GLU A 1 177 ? 26.44390 25.03662 1.37136   1.000 29.22850  ? 177 GLU A CA  1 
ATOM   1347 C C   . GLU A 1 177 ? 26.33901 24.08568 0.18626   1.000 28.97436  ? 177 GLU A C   1 
ATOM   1348 O O   . GLU A 1 177 ? 26.73369 24.40644 -0.94403  1.000 28.91198  ? 177 GLU A O   1 
ATOM   1349 C CB  . GLU A 1 177 ? 26.16264 26.48610 0.99717   1.000 33.36119  ? 177 GLU A CB  1 
ATOM   1350 C CG  . GLU A 1 177 ? 26.13142 27.43137 2.20716   1.000 34.04212  ? 177 GLU A CG  1 
ATOM   1351 C CD  . GLU A 1 177 ? 25.62477 28.80845 1.83509   0.800 42.70886  ? 177 GLU A CD  1 
ATOM   1352 O OE1 . GLU A 1 177 ? 24.39087 28.97827 1.70971   0.800 46.70877  ? 177 GLU A OE1 1 
ATOM   1353 O OE2 . GLU A 1 177 ? 26.45937 29.71339 1.63541   0.800 42.76198  ? 177 GLU A OE2 1 
ATOM   1354 N N   . ALA A 1 178 ? 25.81640 22.89148 0.45142   1.000 26.98271  ? 178 ALA A N   1 
ATOM   1355 C CA  . ALA A 1 178 ? 25.84933 21.84718 -0.56031  1.000 26.86497  ? 178 ALA A CA  1 
ATOM   1356 C C   . ALA A 1 178 ? 24.76828 20.82096 -0.26574  1.000 24.12881  ? 178 ALA A C   1 
ATOM   1357 O O   . ALA A 1 178 ? 24.06218 20.87423 0.75353   1.000 24.37690  ? 178 ALA A O   1 
ATOM   1358 C CB  . ALA A 1 178 ? 27.24023 21.19064 -0.65176  1.000 23.69359  ? 178 ALA A CB  1 
ATOM   1359 N N   . MET A 1 179 ? 24.62592 19.89796 -1.20233  1.000 22.07383  ? 179 MET A N   1 
ATOM   1360 C CA  . MET A 1 179 ? 23.74236 18.75962 -1.03216  1.000 22.49021  ? 179 MET A CA  1 
ATOM   1361 C C   . MET A 1 179 ? 24.46997 17.59232 -1.65752  1.000 23.10920  ? 179 MET A C   1 
ATOM   1362 O O   . MET A 1 179 ? 25.36282 17.78208 -2.49353  1.000 22.76384  ? 179 MET A O   1 
ATOM   1363 C CB  . MET A 1 179 ? 22.36235 18.99428 -1.67106  1.000 24.09489  ? 179 MET A CB  1 
ATOM   1364 C CG  . MET A 1 179 ? 22.48391 19.27744 -3.18247  1.000 23.41431  ? 179 MET A CG  1 
ATOM   1365 S SD  . MET A 1 179 ? 20.89049 19.53882 -3.97329  1.000 25.87720  ? 179 MET A SD  1 
ATOM   1366 C CE  . MET A 1 179 ? 21.44928 19.74737 -5.65460  1.000 26.52189  ? 179 MET A CE  1 
ATOM   1367 N N   . GLN A 1 180 ? 24.11927 16.38473 -1.22446  1.000 20.77949  ? 180 GLN A N   1 
ATOM   1368 C CA  . GLN A 1 180 ? 24.88634 15.20634 -1.58273  1.000 20.31258  ? 180 GLN A CA  1 
ATOM   1369 C C   . GLN A 1 180 ? 23.92342 14.09544 -1.96215  1.000 23.22250  ? 180 GLN A C   1 
ATOM   1370 O O   . GLN A 1 180 ? 23.03563 13.73546 -1.17877  1.000 22.62877  ? 180 GLN A O   1 
ATOM   1371 C CB  . GLN A 1 180 ? 25.79087 14.74258 -0.42416  1.000 21.02409  ? 180 GLN A CB  1 
ATOM   1372 C CG  . GLN A 1 180 ? 26.46760 13.40565 -0.68670  1.000 22.16644  ? 180 GLN A CG  1 
ATOM   1373 C CD  . GLN A 1 180 ? 27.52380 12.99835 0.36152   1.000 21.00984  ? 180 GLN A CD  1 
ATOM   1374 O OE1 . GLN A 1 180 ? 28.26809 12.02957 0.15498   1.000 20.33070  ? 180 GLN A OE1 1 
ATOM   1375 N NE2 . GLN A 1 180 ? 27.56890 13.71153 1.49073   1.000 18.97113  ? 180 GLN A NE2 1 
ATOM   1376 N N   . LEU A 1 181 ? 24.16470 13.49105 -3.11448  1.000 21.40778  ? 181 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 181 ? 23.29773 12.47101 -3.65416  1.000 21.95043  ? 181 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 181 ? 23.98279 11.12290 -3.54453  1.000 22.09228  ? 181 LEU A C   1 
ATOM   1379 O O   . LEU A 1 181 ? 25.10475 10.95217 -4.05660  1.000 24.30326  ? 181 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 181 ? 22.97587 12.79439 -5.11938  1.000 22.16943  ? 181 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 181 ? 22.11766 11.79346 -5.86280  1.000 22.71814  ? 181 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 181 ? 20.64546 12.02019 -5.42708  1.000 19.92945  ? 181 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 181 ? 22.41664 11.97852 -7.42060  1.000 21.00215  ? 181 LEU A CD2 1 
ATOM   1384 N N   . THR A 1 182 ? 23.29472 10.15720 -2.92496  1.000 20.11076  ? 182 THR A N   1 
ATOM   1385 C CA  . THR A 1 182 ? 23.78719 8.79124  -2.84203  1.000 20.05403  ? 182 THR A CA  1 
ATOM   1386 C C   . THR A 1 182 ? 22.81225 7.84428  -3.51779  1.000 22.00220  ? 182 THR A C   1 
ATOM   1387 O O   . THR A 1 182 ? 21.63653 8.15966  -3.69666  1.000 18.77310  ? 182 THR A O   1 
ATOM   1388 C CB  . THR A 1 182 ? 24.00229 8.37825  -1.38651  1.000 21.54254  ? 182 THR A CB  1 
ATOM   1389 O OG1 . THR A 1 182 ? 22.79445 8.62334  -0.66056  1.000 22.56729  ? 182 THR A OG1 1 
ATOM   1390 C CG2 . THR A 1 182 ? 25.06112 9.24071  -0.77800  1.000 19.74911  ? 182 THR A CG2 1 
ATOM   1391 N N   . GLU A 1 183 ? 23.33343 6.68032  -3.91399  1.000 21.68556  ? 183 GLU A N   1 
ATOM   1392 C CA  . GLU A 1 183 ? 22.58991 5.63468  -4.58890  1.000 23.42726  ? 183 GLU A CA  1 
ATOM   1393 C C   . GLU A 1 183 ? 22.05195 4.64492  -3.58415  1.000 24.76529  ? 183 GLU A C   1 
ATOM   1394 O O   . GLU A 1 183 ? 22.69254 4.36065  -2.57267  1.000 22.85405  ? 183 GLU A O   1 
ATOM   1395 C CB  . GLU A 1 183 ? 23.48347 4.87625  -5.58032  1.000 23.90834  ? 183 GLU A CB  1 
ATOM   1396 C CG  . GLU A 1 183 ? 24.07428 5.77756  -6.67213  1.000 22.57252  ? 183 GLU A CG  1 
ATOM   1397 C CD  . GLU A 1 183 ? 24.83287 5.03650  -7.77103  1.000 26.17013  ? 183 GLU A CD  1 
ATOM   1398 O OE1 . GLU A 1 183 ? 25.10445 3.81167  -7.64255  1.000 26.42967  ? 183 GLU A OE1 1 
ATOM   1399 O OE2 . GLU A 1 183 ? 25.16767 5.70852  -8.78377  1.000 27.73780  ? 183 GLU A OE2 1 
ATOM   1400 N N   . MET A 1 184 ? 20.89953 4.06128  -3.89753  1.000 25.82219  ? 184 MET A N   1 
ATOM   1401 C CA  . MET A 1 184 ? 20.42119 2.91542  -3.14154  1.000 25.89791  ? 184 MET A CA  1 
ATOM   1402 C C   . MET A 1 184 ? 20.42024 1.71751  -4.08011  1.000 23.75261  ? 184 MET A C   1 
ATOM   1403 O O   . MET A 1 184 ? 19.59996 1.66476  -5.00216  1.000 28.71971  ? 184 MET A O   1 
ATOM   1404 C CB  . MET A 1 184 ? 19.02616 3.16348  -2.55976  1.000 26.72737  ? 184 MET A CB  1 
ATOM   1405 C CG  . MET A 1 184 ? 18.83254 4.54811  -1.87794  1.000 24.04566  ? 184 MET A CG  1 
ATOM   1406 S SD  . MET A 1 184 ? 17.13871 4.53653  -1.25557  1.000 36.48893  ? 184 MET A SD  1 
ATOM   1407 C CE  . MET A 1 184 ? 17.13477 6.04018  -0.28993  1.000 32.16282  ? 184 MET A CE  1 
ATOM   1408 N N   . ALA A 1 185 ? 21.32104 0.76828  -3.84369  1.000 23.22499  ? 185 ALA A N   1 
ATOM   1409 C CA  . ALA A 1 185 ? 21.41825 -0.47971 -4.59708  1.000 28.82415  ? 185 ALA A CA  1 
ATOM   1410 C C   . ALA A 1 185 ? 21.30575 -0.29592 -6.12859  1.000 27.68760  ? 185 ALA A C   1 
ATOM   1411 O O   . ALA A 1 185 ? 20.33921 -0.75301 -6.72931  1.000 26.88145  ? 185 ALA A O   1 
ATOM   1412 C CB  . ALA A 1 185 ? 20.34329 -1.46311 -4.12996  1.000 26.58467  ? 185 ALA A CB  1 
ATOM   1413 N N   . SER A 1 186 ? 22.25004 0.37018  -6.77234  1.000 26.27757  ? 186 SER A N   1 
ATOM   1414 C CA  . SER A 1 186 ? 22.14996 0.51323  -8.22606  1.000 27.78876  ? 186 SER A CA  1 
ATOM   1415 C C   . SER A 1 186 ? 22.50880 -0.77716 -8.93301  1.000 29.13985  ? 186 SER A C   1 
ATOM   1416 O O   . SER A 1 186 ? 23.37641 -1.53896 -8.48909  1.000 30.12924  ? 186 SER A O   1 
ATOM   1417 C CB  . SER A 1 186 ? 23.07471 1.61487  -8.73851  1.000 29.05432  ? 186 SER A CB  1 
ATOM   1418 O OG  . SER A 1 186 ? 24.33814 1.49572  -8.09715  1.000 29.81559  ? 186 SER A OG  1 
ATOM   1419 N N   . ILE A 1 187 ? 21.83439 -1.02034 -10.04006 1.000 31.82576  ? 187 ILE A N   1 
ATOM   1420 C CA  . ILE A 1 187 ? 22.22303 -2.08483 -10.95558 1.000 31.17893  ? 187 ILE A CA  1 
ATOM   1421 C C   . ILE A 1 187 ? 23.36644 -1.58323 -11.82832 1.000 32.96960  ? 187 ILE A C   1 
ATOM   1422 O O   . ILE A 1 187 ? 23.30904 -0.47541 -12.36892 1.000 35.91429  ? 187 ILE A O   1 
ATOM   1423 C CB  . ILE A 1 187 ? 21.02800 -2.51291 -11.81154 1.000 32.63836  ? 187 ILE A CB  1 
ATOM   1424 C CG1 . ILE A 1 187 ? 19.81787 -2.85228 -10.92560 1.000 32.99509  ? 187 ILE A CG1 1 
ATOM   1425 C CG2 . ILE A 1 187 ? 21.39753 -3.66666 -12.72255 1.000 35.04666  ? 187 ILE A CG2 1 
ATOM   1426 C CD1 . ILE A 1 187 ? 18.57250 -3.28334 -11.71569 1.000 35.13880  ? 187 ILE A CD1 1 
ATOM   1427 N N   . ASN A 1 188 ? 24.41121 -2.38321 -11.97135 1.000 34.32839  ? 188 ASN A N   1 
ATOM   1428 C CA  . ASN A 1 188 ? 25.52013 -2.01070 -12.84764 1.000 38.03983  ? 188 ASN A CA  1 
ATOM   1429 C C   . ASN A 1 188 ? 25.99758 -3.24636 -13.58458 1.000 41.39137  ? 188 ASN A C   1 
ATOM   1430 O O   . ASN A 1 188 ? 26.56347 -4.15490 -12.97407 1.000 40.16691  ? 188 ASN A O   1 
ATOM   1431 C CB  . ASN A 1 188 ? 26.66375 -1.37363 -12.07103 1.000 39.21245  ? 188 ASN A CB  1 
ATOM   1432 C CG  . ASN A 1 188 ? 26.48344 0.11206  -11.91032 1.000 35.30020  ? 188 ASN A CG  1 
ATOM   1433 O OD1 . ASN A 1 188 ? 26.86980 0.88708  -12.78876 1.000 35.07947  ? 188 ASN A OD1 1 
ATOM   1434 N ND2 . ASN A 1 188 ? 25.86845 0.52399  -10.80146 1.000 31.81011  ? 188 ASN A ND2 1 
ATOM   1435 N N   . ASN A 1 189 ? 25.75551 -3.29905 -14.88753 1.000 40.80526  ? 189 ASN A N   1 
ATOM   1436 C CA  . ASN A 1 189 ? 26.35451 -4.38055 -15.64958 1.000 46.15577  ? 189 ASN A CA  1 
ATOM   1437 C C   . ASN A 1 189 ? 26.77466 -3.85125 -17.01477 1.000 52.80285  ? 189 ASN A C   1 
ATOM   1438 O O   . ASN A 1 189 ? 27.08488 -2.66027 -17.14687 1.000 55.88782  ? 189 ASN A O   1 
ATOM   1439 C CB  . ASN A 1 189 ? 25.38312 -5.56319 -15.75859 1.000 47.10431  ? 189 ASN A CB  1 
ATOM   1440 C CG  . ASN A 1 189 ? 24.02986 -5.15118 -16.29977 1.000 50.00055  ? 189 ASN A CG  1 
ATOM   1441 O OD1 . ASN A 1 189 ? 23.94283 -4.26845 -17.15031 1.000 49.75133  ? 189 ASN A OD1 1 
ATOM   1442 N ND2 . ASN A 1 189 ? 22.96689 -5.77436 -15.79537 1.000 49.69911  ? 189 ASN A ND2 1 
ATOM   1443 N N   . ARG A 1 190 ? 26.77408 -4.72548 -18.02497 1.000 63.49583  ? 190 ARG A N   1 
ATOM   1444 C CA  . ARG A 1 190 ? 27.18837 -4.33965 -19.37267 1.000 70.04118  ? 190 ARG A CA  1 
ATOM   1445 C C   . ARG A 1 190 ? 26.29602 -3.23616 -19.93288 1.000 67.39803  ? 190 ARG A C   1 
ATOM   1446 O O   . ARG A 1 190 ? 26.78973 -2.23162 -20.45251 1.000 70.36070  ? 190 ARG A O   1 
ATOM   1447 C CB  . ARG A 1 190 ? 27.17081 -5.57237 -20.28610 1.000 63.09688  ? 190 ARG A CB  1 
ATOM   1448 C CG  . ARG A 1 190 ? 27.67966 -5.36264 -21.70027 1.000 70.52380  ? 190 ARG A CG  1 
ATOM   1449 C CD  . ARG A 1 190 ? 27.05526 -6.39514 -22.63310 1.000 72.81708  ? 190 ARG A CD  1 
ATOM   1450 N NE  . ARG A 1 190 ? 26.83077 -7.64387 -21.91618 1.000 73.94175  ? 190 ARG A NE  1 
ATOM   1451 C CZ  . ARG A 1 190 ? 25.82323 -8.47814 -22.14258 1.000 87.45233  ? 190 ARG A CZ  1 
ATOM   1452 N NH1 . ARG A 1 190 ? 24.91603 -8.23460 -23.07637 1.000 77.89384  ? 190 ARG A NH1 1 
ATOM   1453 N NH2 . ARG A 1 190 ? 25.71450 -9.57936 -21.40170 1.000 77.10190  ? 190 ARG A NH2 1 
ATOM   1454 N N   . VAL A 1 191 ? 24.97511 -3.40206 -19.81824 1.000 58.63766  ? 191 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 191 ? 24.02059 -2.43339 -20.35439 1.000 56.00275  ? 191 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 191 ? 23.60050 -1.30905 -19.39498 1.000 50.42565  ? 191 VAL A C   1 
ATOM   1457 O O   . VAL A 1 191 ? 22.97908 -0.33694 -19.84513 1.000 49.57396  ? 191 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 191 ? 22.75164 -3.16442 -20.83029 1.000 57.14411  ? 191 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 191 ? 23.02755 -4.02574 -22.08905 1.000 56.60051  ? 191 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 191 ? 22.21461 -4.02597 -19.70865 1.000 57.45020  ? 191 VAL A CG2 1 
ATOM   1461 N N   . TYR A 1 192 ? 23.88615 -1.41181 -18.09164 1.000 49.13185  ? 192 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 192 ? 23.39073 -0.43324 -17.11662 1.000 46.21490  ? 192 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 192 ? 24.55337 0.13636  -16.30466 1.000 44.55139  ? 192 TYR A C   1 
ATOM   1464 O O   . TYR A 1 192 ? 25.29758 -0.61987 -15.67567 1.000 43.49588  ? 192 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 192 ? 22.33695 -1.04349 -16.17878 1.000 45.01493  ? 192 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 192 ? 21.18642 -1.75824 -16.86992 1.000 49.88619  ? 192 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 192 ? 20.68361 -1.30031 -18.08959 1.000 50.34473  ? 192 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 192 ? 20.61400 -2.90052 -16.31254 1.000 46.06411  ? 192 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 192 ? 19.63801 -1.95987 -18.73867 1.000 53.87282  ? 192 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 192 ? 19.57428 -3.56553 -16.94146 1.000 50.76077  ? 192 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 192 ? 19.08738 -3.09375 -18.16414 1.000 54.10509  ? 192 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 192 ? 18.05671 -3.75050 -18.79884 1.000 52.34931  ? 192 TYR A OH  1 
ATOM   1473 N N   . ARG A 1 193 ? 24.68361 1.47013  -16.29985 1.000 38.28913  ? 193 ARG A N   1 
ATOM   1474 C CA  . ARG A 1 193 ? 25.83327 2.16762  -15.72936 1.000 38.32539  ? 193 ARG A CA  1 
ATOM   1475 C C   . ARG A 1 193 ? 25.34902 3.34134  -14.89671 1.000 34.36559  ? 193 ARG A C   1 
ATOM   1476 O O   . ARG A 1 193 ? 24.63455 4.20214  -15.41185 1.000 34.84795  ? 193 ARG A O   1 
ATOM   1477 C CB  . ARG A 1 193 ? 26.77821 2.69157  -16.81429 1.000 40.84900  ? 193 ARG A CB  1 
ATOM   1478 C CG  . ARG A 1 193 ? 27.07851 1.72266  -17.95087 1.000 55.23396  ? 193 ARG A CG  1 
ATOM   1479 C CD  . ARG A 1 193 ? 28.36918 0.94061  -17.71900 0.800 60.07341  ? 193 ARG A CD  1 
ATOM   1480 N NE  . ARG A 1 193 ? 29.35225 1.18760  -18.76942 0.700 63.62378  ? 193 ARG A NE  1 
ATOM   1481 C CZ  . ARG A 1 193 ? 30.40754 1.98120  -18.63420 0.700 61.36625  ? 193 ARG A CZ  1 
ATOM   1482 N NH1 . ARG A 1 193 ? 30.65248 2.61744  -17.49727 0.700 51.51988  ? 193 ARG A NH1 1 
ATOM   1483 N NH2 . ARG A 1 193 ? 31.23869 2.13579  -19.66418 0.700 60.70755  ? 193 ARG A NH2 1 
ATOM   1484 N N   . THR A 1 194 ? 25.76295 3.40555  -13.63530 1.000 31.17999  ? 194 THR A N   1 
ATOM   1485 C CA  . THR A 1 194 ? 25.62285 4.62848  -12.85891 1.000 29.57171  ? 194 THR A CA  1 
ATOM   1486 C C   . THR A 1 194 ? 26.99444 5.04740  -12.37218 1.000 28.61745  ? 194 THR A C   1 
ATOM   1487 O O   . THR A 1 194 ? 27.96276 4.29785  -12.48243 1.000 24.80221  ? 194 THR A O   1 
ATOM   1488 C CB  . THR A 1 194 ? 24.69390 4.45252  -11.65902 1.000 30.22110  ? 194 THR A CB  1 
ATOM   1489 O OG1 . THR A 1 194 ? 25.31675 3.57632  -10.69932 1.000 28.93941  ? 194 THR A OG1 1 
ATOM   1490 C CG2 . THR A 1 194 ? 23.35220 3.88647  -12.09733 1.000 28.50875  ? 194 THR A CG2 1 
ATOM   1491 N N   . ILE A 1 195 ? 27.07307 6.25206  -11.80277 1.000 25.78330  ? 195 ILE A N   1 
ATOM   1492 C CA  . ILE A 1 195 ? 28.37638 6.71401  -11.35084 1.000 26.80853  ? 195 ILE A CA  1 
ATOM   1493 C C   . ILE A 1 195 ? 28.86323 5.90167  -10.13726 1.000 27.05035  ? 195 ILE A C   1 
ATOM   1494 O O   . ILE A 1 195 ? 30.06820 5.65888  -10.00043 1.000 25.65304  ? 195 ILE A O   1 
ATOM   1495 C CB  . ILE A 1 195 ? 28.34999 8.22498  -11.04599 1.000 24.56011  ? 195 ILE A CB  1 
ATOM   1496 C CG1 . ILE A 1 195 ? 29.76753 8.70348  -10.71119 1.000 25.09075  ? 195 ILE A CG1 1 
ATOM   1497 C CG2 . ILE A 1 195 ? 27.40013 8.52256  -9.88434  1.000 21.62799  ? 195 ILE A CG2 1 
ATOM   1498 C CD1 . ILE A 1 195 ? 30.77478 8.43916  -11.85263 1.000 22.68832  ? 195 ILE A CD1 1 
ATOM   1499 N N   . GLY A 1 196 ? 27.95592 5.45976  -9.25342  1.000 25.72646  ? 196 GLY A N   1 
ATOM   1500 C CA  . GLY A 1 196 ? 28.34664 4.70571  -8.06033  1.000 24.82198  ? 196 GLY A CA  1 
ATOM   1501 C C   . GLY A 1 196 ? 28.67615 5.61519  -6.89347  1.000 23.93402  ? 196 GLY A C   1 
ATOM   1502 O O   . GLY A 1 196 ? 28.00991 5.58592  -5.83765  1.000 25.94286  ? 196 GLY A O   1 
ATOM   1503 N N   . SER A 1 197 ? 29.66314 6.47996  -7.11028  1.000 22.87421  ? 197 SER A N   1 
ATOM   1504 C CA  . SER A 1 197 ? 30.09081 7.40808  -6.08428  1.000 22.94544  ? 197 SER A CA  1 
ATOM   1505 C C   . SER A 1 197 ? 28.96700 8.35147  -5.67488  1.000 24.34050  ? 197 SER A C   1 
ATOM   1506 O O   . SER A 1 197 ? 28.15722 8.76922  -6.50551  1.000 19.98005  ? 197 SER A O   1 
ATOM   1507 C CB  . SER A 1 197 ? 31.27890 8.22625  -6.57587  1.000 21.47899  ? 197 SER A CB  1 
ATOM   1508 O OG  . SER A 1 197 ? 32.29335 7.33599  -7.00722  1.000 23.04952  ? 197 SER A OG  1 
ATOM   1509 N N   . PRO A 1 198 ? 28.92497 8.72112  -4.39271  1.000 22.61471  ? 198 PRO A N   1 
ATOM   1510 C CA  . PRO A 1 198 ? 28.15573 9.89169  -3.98818  1.000 24.14322  ? 198 PRO A CA  1 
ATOM   1511 C C   . PRO A 1 198 ? 28.59180 11.11292 -4.77337  1.000 22.23407  ? 198 PRO A C   1 
ATOM   1512 O O   . PRO A 1 198 ? 29.75434 11.24569 -5.16347  1.000 23.62788  ? 198 PRO A O   1 
ATOM   1513 C CB  . PRO A 1 198 ? 28.50000 10.05268 -2.49333  1.000 21.50479  ? 198 PRO A CB  1 
ATOM   1514 C CG  . PRO A 1 198 ? 29.11353 8.76343  -2.09670  1.000 20.21703  ? 198 PRO A CG  1 
ATOM   1515 C CD  . PRO A 1 198 ? 29.74955 8.19130  -3.29136  1.000 19.06436  ? 198 PRO A CD  1 
ATOM   1516 N N   . LEU A 1 199 ? 27.66876 12.05560 -4.90806  1.000 18.54295  ? 199 LEU A N   1 
ATOM   1517 C CA  . LEU A 1 199 ? 27.92683 13.29045 -5.62307  1.000 21.41184  ? 199 LEU A CA  1 
ATOM   1518 C C   . LEU A 1 199 ? 27.58630 14.43714 -4.69656  1.000 22.18862  ? 199 LEU A C   1 
ATOM   1519 O O   . LEU A 1 199 ? 26.51051 14.43686 -4.09909  1.000 23.26607  ? 199 LEU A O   1 
ATOM   1520 C CB  . LEU A 1 199 ? 27.06603 13.38574 -6.90158  1.000 21.93050  ? 199 LEU A CB  1 
ATOM   1521 C CG  . LEU A 1 199 ? 27.19474 12.26886 -7.93902  1.000 21.68136  ? 199 LEU A CG  1 
ATOM   1522 C CD1 . LEU A 1 199 ? 26.35348 12.61308 -9.20169  1.000 21.13013  ? 199 LEU A CD1 1 
ATOM   1523 C CD2 . LEU A 1 199 ? 28.66571 12.07166 -8.32875  1.000 20.66041  ? 199 LEU A CD2 1 
ATOM   1524 N N   . VAL A 1 200 ? 28.48140 15.42231 -4.60086  1.000 23.74498  ? 200 VAL A N   1 
ATOM   1525 C CA  . VAL A 1 200 ? 28.27626 16.62146 -3.78680  1.000 21.88701  ? 200 VAL A CA  1 
ATOM   1526 C C   . VAL A 1 200 ? 28.12828 17.80946 -4.72211  1.000 23.67587  ? 200 VAL A C   1 
ATOM   1527 O O   . VAL A 1 200 ? 29.02474 18.08947 -5.53503  1.000 24.81228  ? 200 VAL A O   1 
ATOM   1528 C CB  . VAL A 1 200 ? 29.43084 16.83660 -2.78736  1.000 24.45067  ? 200 VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 200 ? 29.31451 18.21220 -2.07542  1.000 21.45781  ? 200 VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 200 ? 29.44223 15.71786 -1.76929  1.000 21.85257  ? 200 VAL A CG2 1 
ATOM   1531 N N   . PHE A 1 201 ? 26.99353 18.52434 -4.59680  1.000 24.32693  ? 201 PHE A N   1 
ATOM   1532 C CA  . PHE A 1 201 ? 26.61256 19.63505 -5.44579  1.000 23.64257  ? 201 PHE A CA  1 
ATOM   1533 C C   . PHE A 1 201 ? 26.65178 20.93901 -4.67851  1.000 26.41406  ? 201 PHE A C   1 
ATOM   1534 O O   . PHE A 1 201 ? 26.19532 20.98260 -3.53134  1.000 26.33823  ? 201 PHE A O   1 
ATOM   1535 C CB  . PHE A 1 201 ? 25.19691 19.45199 -5.99670  1.000 22.30486  ? 201 PHE A CB  1 
ATOM   1536 C CG  . PHE A 1 201 ? 25.03894 18.22741 -6.80899  1.000 24.84660  ? 201 PHE A CG  1 
ATOM   1537 C CD1 . PHE A 1 201 ? 24.64639 17.04167 -6.20797  1.000 23.81812  ? 201 PHE A CD1 1 
ATOM   1538 C CD2 . PHE A 1 201 ? 25.29572 18.24824 -8.17817  1.000 24.03084  ? 201 PHE A CD2 1 
ATOM   1539 C CE1 . PHE A 1 201 ? 24.50398 15.89452 -6.94778  1.000 24.25530  ? 201 PHE A CE1 1 
ATOM   1540 C CE2 . PHE A 1 201 ? 25.16020 17.08796 -8.93928  1.000 25.08228  ? 201 PHE A CE2 1 
ATOM   1541 C CZ  . PHE A 1 201 ? 24.76312 15.91106 -8.33367  1.000 24.20354  ? 201 PHE A CZ  1 
ATOM   1542 N N   . PRO A 1 202 ? 27.11570 22.03477 -5.30614  1.000 27.99586  ? 202 PRO A N   1 
ATOM   1543 C CA  . PRO A 1 202 ? 27.10479 23.33019 -4.62117  1.000 27.65555  ? 202 PRO A CA  1 
ATOM   1544 C C   . PRO A 1 202 ? 25.75783 24.01433 -4.77098  1.000 27.77695  ? 202 PRO A C   1 
ATOM   1545 O O   . PRO A 1 202 ? 24.85518 23.52634 -5.45231  1.000 26.36844  ? 202 PRO A O   1 
ATOM   1546 C CB  . PRO A 1 202 ? 28.21563 24.11322 -5.34248  1.000 26.82419  ? 202 PRO A CB  1 
ATOM   1547 C CG  . PRO A 1 202 ? 28.11034 23.63892 -6.72083  1.000 27.53788  ? 202 PRO A CG  1 
ATOM   1548 C CD  . PRO A 1 202 ? 27.67106 22.15932 -6.66982  1.000 27.48769  ? 202 PRO A CD  1 
ATOM   1549 N N   . LYS A 1 203 ? 25.63755 25.16103 -4.11544  1.000 28.77904  ? 203 LYS A N   1 
ATOM   1550 C CA  . LYS A 1 203 ? 24.49628 26.03888 -4.30815  1.000 32.14525  ? 203 LYS A CA  1 
ATOM   1551 C C   . LYS A 1 203 ? 24.29598 26.32159 -5.78078  1.000 30.29668  ? 203 LYS A C   1 
ATOM   1552 O O   . LYS A 1 203 ? 25.26263 26.42390 -6.53819  1.000 30.72868  ? 203 LYS A O   1 
ATOM   1553 C CB  . LYS A 1 203 ? 24.72590 27.37674 -3.59445  1.000 32.30794  ? 203 LYS A CB  1 
ATOM   1554 C CG  . LYS A 1 203 ? 24.16617 27.47737 -2.21642  1.000 35.28804  ? 203 LYS A CG  1 
ATOM   1555 C CD  . LYS A 1 203 ? 24.01410 28.95404 -1.85880  0.800 37.92330  ? 203 LYS A CD  1 
ATOM   1556 C CE  . LYS A 1 203 ? 25.30765 29.70399 -2.13184  0.700 38.67247  ? 203 LYS A CE  1 
ATOM   1557 N NZ  . LYS A 1 203 ? 25.12789 31.18366 -2.00746  0.700 43.35897  ? 203 LYS A NZ  1 
ATOM   1558 N N   . HIS A 1 204 ? 23.03382 26.50443 -6.17140  1.000 29.51092  ? 204 HIS A N   1 
ATOM   1559 C CA  . HIS A 1 204 ? 22.60227 26.90289 -7.52161  1.000 33.71711  ? 204 HIS A CA  1 
ATOM   1560 C C   . HIS A 1 204 ? 22.75649 25.81036 -8.57746  1.000 31.10051  ? 204 HIS A C   1 
ATOM   1561 O O   . HIS A 1 204 ? 22.43838 26.05210 -9.72978  1.000 34.70896  ? 204 HIS A O   1 
ATOM   1562 C CB  . HIS A 1 204 ? 23.33300 28.14926 -8.05337  1.000 33.15269  ? 204 HIS A CB  1 
ATOM   1563 C CG  . HIS A 1 204 ? 23.30712 29.31510 -7.12021  1.000 37.02300  ? 204 HIS A CG  1 
ATOM   1564 N ND1 . HIS A 1 204 ? 22.13563 29.92217 -6.71432  1.000 40.59661  ? 204 HIS A ND1 1 
ATOM   1565 C CD2 . HIS A 1 204 ? 24.31196 29.99847 -6.52352  1.000 37.44821  ? 204 HIS A CD2 1 
ATOM   1566 C CE1 . HIS A 1 204 ? 22.42215 30.92163 -5.89887  1.000 36.99927  ? 204 HIS A CE1 1 
ATOM   1567 N NE2 . HIS A 1 204 ? 23.73580 30.99173 -5.77232  1.000 37.69728  ? 204 HIS A NE2 1 
ATOM   1568 N N   . HIS A 1 205 ? 23.29291 24.64850 -8.23830  1.000 32.21238  ? 205 HIS A N   1 
ATOM   1569 C CA  . HIS A 1 205 ? 23.16286 23.48450 -9.09513  1.000 30.20266  ? 205 HIS A CA  1 
ATOM   1570 C C   . HIS A 1 205 ? 21.80596 22.83058 -8.86597  1.000 30.81405  ? 205 HIS A C   1 
ATOM   1571 O O   . HIS A 1 205 ? 21.33361 22.72670 -7.72396  1.000 26.36173  ? 205 HIS A O   1 
ATOM   1572 C CB  . HIS A 1 205 ? 24.28079 22.48086 -8.80606  1.000 26.94328  ? 205 HIS A CB  1 
ATOM   1573 C CG  . HIS A 1 205 ? 25.57153 22.84176 -9.45245  1.000 28.53714  ? 205 HIS A CG  1 
ATOM   1574 N ND1 . HIS A 1 205 ? 26.56302 21.91753 -9.71072  1.000 26.83439  ? 205 HIS A ND1 1 
ATOM   1575 C CD2 . HIS A 1 205 ? 26.02428 24.03327 -9.92196  1.000 26.13697  ? 205 HIS A CD2 1 
ATOM   1576 C CE1 . HIS A 1 205 ? 27.58504 22.53350 -10.28515 1.000 30.17868  ? 205 HIS A CE1 1 
ATOM   1577 N NE2 . HIS A 1 205 ? 27.27391 23.81285 -10.44521 1.000 27.61450  ? 205 HIS A NE2 1 
ATOM   1578 N N   . VAL A 1 206 ? 21.18549 22.38824 -9.95770  1.000 27.81167  ? 206 VAL A N   1 
ATOM   1579 C CA  . VAL A 1 206 ? 19.86231 21.77987 -9.92277  1.000 27.36749  ? 206 VAL A CA  1 
ATOM   1580 C C   . VAL A 1 206 ? 19.98770 20.34409 -10.42456 1.000 31.57718  ? 206 VAL A C   1 
ATOM   1581 O O   . VAL A 1 206 ? 20.43557 20.09575 -11.55684 1.000 30.89902  ? 206 VAL A O   1 
ATOM   1582 C CB  . VAL A 1 206 ? 18.85674 22.57206 -10.77178 1.000 30.47169  ? 206 VAL A CB  1 
ATOM   1583 C CG1 . VAL A 1 206 ? 17.50521 21.87152 -10.80299 1.000 29.93626  ? 206 VAL A CG1 1 
ATOM   1584 C CG2 . VAL A 1 206 ? 18.73071 24.00453 -10.25184 1.000 32.62247  ? 206 VAL A CG2 1 
ATOM   1585 N N   . VAL A 1 207 ? 19.56853 19.40463 -9.59226  1.000 27.02197  ? 207 VAL A N   1 
ATOM   1586 C CA  . VAL A 1 207 ? 19.54111 17.99797 -9.93068  1.000 28.87257  ? 207 VAL A CA  1 
ATOM   1587 C C   . VAL A 1 207 ? 18.08619 17.59172 -10.08111 1.000 33.00239  ? 207 VAL A C   1 
ATOM   1588 O O   . VAL A 1 207 ? 17.27883 17.81305 -9.16789  1.000 31.91216  ? 207 VAL A O   1 
ATOM   1589 C CB  . VAL A 1 207 ? 20.25125 17.16596 -8.86177  1.000 27.49248  ? 207 VAL A CB  1 
ATOM   1590 C CG1 . VAL A 1 207 ? 20.14717 15.69892 -9.19336  1.000 27.37109  ? 207 VAL A CG1 1 
ATOM   1591 C CG2 . VAL A 1 207 ? 21.71255 17.61449 -8.76274  1.000 26.71115  ? 207 VAL A CG2 1 
ATOM   1592 N N   . SER A 1 208 ? 17.74739 17.03548 -11.24670 1.000 29.82893  ? 208 SER A N   1 
ATOM   1593 C CA  . SER A 1 208 ? 16.37581 16.73406 -11.62497 1.000 33.50181  ? 208 SER A CA  1 
ATOM   1594 C C   . SER A 1 208 ? 16.27005 15.23998 -11.90645 1.000 33.00817  ? 208 SER A C   1 
ATOM   1595 O O   . SER A 1 208 ? 17.15673 14.66403 -12.53006 1.000 34.45807  ? 208 SER A O   1 
ATOM   1596 C CB  . SER A 1 208 ? 15.97290 17.56988 -12.86062 1.000 34.81151  ? 208 SER A CB  1 
ATOM   1597 O OG  . SER A 1 208 ? 14.82153 17.06746 -13.50549 1.000 40.83159  ? 208 SER A OG  1 
ATOM   1598 N N   . LEU A 1 209 ? 15.21684 14.60146 -11.41307 1.000 34.76376  ? 209 LEU A N   1 
ATOM   1599 C CA  . LEU A 1 209 ? 14.96392 13.19199 -11.67963 1.000 35.69859  ? 209 LEU A CA  1 
ATOM   1600 C C   . LEU A 1 209 ? 13.71219 13.09111 -12.52591 1.000 38.48556  ? 209 LEU A C   1 
ATOM   1601 O O   . LEU A 1 209 ? 12.67298 13.63180 -12.15634 1.000 41.93783  ? 209 LEU A O   1 
ATOM   1602 C CB  . LEU A 1 209 ? 14.78042 12.37823 -10.39938 1.000 34.42760  ? 209 LEU A CB  1 
ATOM   1603 C CG  . LEU A 1 209 ? 15.80650 12.54064 -9.29529  1.000 30.14285  ? 209 LEU A CG  1 
ATOM   1604 C CD1 . LEU A 1 209 ? 15.45199 11.55737 -8.23800  1.000 32.42790  ? 209 LEU A CD1 1 
ATOM   1605 C CD2 . LEU A 1 209 ? 17.26830 12.34573 -9.76608  1.000 28.86775  ? 209 LEU A CD2 1 
ATOM   1606 N N   . GLN A 1 210 ? 13.81605 12.41021 -13.65673 1.000 34.98567  ? 210 GLN A N   1 
ATOM   1607 C CA  . GLN A 1 210 ? 12.72838 12.32575 -14.57858 1.000 41.56920  ? 210 GLN A CA  1 
ATOM   1608 C C   . GLN A 1 210 ? 12.36782 10.86169 -14.80837 1.000 44.40088  ? 210 GLN A C   1 
ATOM   1609 O O   . GLN A 1 210 ? 13.26532 10.02042 -14.97971 1.000 42.61011  ? 210 GLN A O   1 
ATOM   1610 C CB  . GLN A 1 210 ? 13.11080 13.03331 -15.91370 1.000 43.37885  ? 210 GLN A CB  1 
ATOM   1611 C CG  . GLN A 1 210 ? 13.63145 14.47093 -15.69939 1.000 41.53540  ? 210 GLN A CG  1 
ATOM   1612 C CD  . GLN A 1 210 ? 14.13494 15.16721 -16.96080 1.000 45.83436  ? 210 GLN A CD  1 
ATOM   1613 O OE1 . GLN A 1 210 ? 14.07810 14.61767 -18.06255 1.000 49.11501  ? 210 GLN A OE1 1 
ATOM   1614 N NE2 . GLN A 1 210 ? 14.65099 16.39284 -16.79641 1.000 47.05870  ? 210 GLN A NE2 1 
ATOM   1615 N N   . PRO A 1 211 ? 11.08285 10.51797 -14.81520 1.000 48.61755  ? 211 PRO A N   1 
ATOM   1616 C CA  . PRO A 1 211 ? 10.69090 9.11406  -14.96569 1.000 48.81318  ? 211 PRO A CA  1 
ATOM   1617 C C   . PRO A 1 211 ? 10.93491 8.61024  -16.37812 1.000 51.64737  ? 211 PRO A C   1 
ATOM   1618 O O   . PRO A 1 211 ? 10.90849 9.36157  -17.35811 1.000 51.01006  ? 211 PRO A O   1 
ATOM   1619 C CB  . PRO A 1 211 ? 9.19332  9.13008  -14.64405 1.000 54.22488  ? 211 PRO A CB  1 
ATOM   1620 C CG  . PRO A 1 211 ? 8.93548  10.50228 -14.02131 1.000 53.85768  ? 211 PRO A CG  1 
ATOM   1621 C CD  . PRO A 1 211 ? 9.91362  11.39923 -14.69355 1.000 48.92462  ? 211 PRO A CD  1 
ATOM   1622 N N   . VAL A 1 212 ? 11.15096 7.30535  -16.48089 1.000 55.23926  ? 212 VAL A N   1 
ATOM   1623 C CA  . VAL A 1 212 ? 11.40143 6.66305  -17.75665 1.000 53.58959  ? 212 VAL A CA  1 
ATOM   1624 C C   . VAL A 1 212 ? 10.21196 5.82502  -18.20413 1.000 61.25119  ? 212 VAL A C   1 
ATOM   1625 O O   . VAL A 1 212 ? 9.83565  5.85758  -19.37751 1.000 64.01003  ? 212 VAL A O   1 
ATOM   1626 C CB  . VAL A 1 212 ? 12.69246 5.82355  -17.69030 1.000 46.73117  ? 212 VAL A CB  1 
ATOM   1627 C CG1 . VAL A 1 212 ? 12.87900 5.01890  -18.96722 1.000 46.95531  ? 212 VAL A CG1 1 
ATOM   1628 C CG2 . VAL A 1 212 ? 13.88403 6.75495  -17.46406 1.000 42.70849  ? 212 VAL A CG2 1 
ATOM   1629 N N   . ASN A 1 213 ? 9.59549  5.08585  -17.28350 1.000 65.75772  ? 213 ASN A N   1 
ATOM   1630 C CA  . ASN A 1 213 ? 8.32328  4.43397  -17.56972 1.000 71.45284  ? 213 ASN A CA  1 
ATOM   1631 C C   . ASN A 1 213 ? 7.34753  4.69726  -16.43287 1.000 69.36434  ? 213 ASN A C   1 
ATOM   1632 O O   . ASN A 1 213 ? 6.57662  5.65598  -16.49667 1.000 69.87627  ? 213 ASN A O   1 
ATOM   1633 C CB  . ASN A 1 213 ? 8.50533  2.93331  -17.81035 1.000 76.17324  ? 213 ASN A CB  1 
ATOM   1634 C CG  . ASN A 1 213 ? 8.22155  2.54267  -19.24928 1.000 86.42906  ? 213 ASN A CG  1 
ATOM   1635 O OD1 . ASN A 1 213 ? 7.27545  3.04114  -19.86621 1.000 89.44071  ? 213 ASN A OD1 1 
ATOM   1636 N ND2 . ASN A 1 213 ? 9.04726  1.65692  -19.79991 1.000 94.64605  ? 213 ASN A ND2 1 
ATOM   1637 N N   . ASP A 1 214 ? 7.37371  3.87129  -15.39213 1.000 70.76363  ? 214 ASP A N   1 
ATOM   1638 C CA  . ASP A 1 214 ? 6.53441  4.12441  -14.22789 1.000 70.87666  ? 214 ASP A CA  1 
ATOM   1639 C C   . ASP A 1 214 ? 6.71716  5.56250  -13.75057 1.000 68.46086  ? 214 ASP A C   1 
ATOM   1640 O O   . ASP A 1 214 ? 7.84342  6.05779  -13.63495 1.000 67.49917  ? 214 ASP A O   1 
ATOM   1641 C CB  . ASP A 1 214 ? 6.87297  3.13487  -13.10803 1.000 71.16317  ? 214 ASP A CB  1 
ATOM   1642 C CG  . ASP A 1 214 ? 5.86512  3.16971  -11.95972 1.000 76.78844  ? 214 ASP A CG  1 
ATOM   1643 O OD1 . ASP A 1 214 ? 4.88610  3.94145  -12.03493 1.000 78.23502  ? 214 ASP A OD1 1 
ATOM   1644 O OD2 . ASP A 1 214 ? 6.05236  2.42117  -10.97203 1.000 80.67462  ? 214 ASP A OD2 1 
ATOM   1645 N N   . LYS A 1 215 ? 5.60181  6.24416  -13.49763 1.000 65.93424  ? 215 LYS A N   1 
ATOM   1646 C CA  . LYS A 1 215 ? 5.62595  7.62341  -13.02615 1.000 65.64884  ? 215 LYS A CA  1 
ATOM   1647 C C   . LYS A 1 215 ? 5.09759  7.77754  -11.60161 1.000 61.97349  ? 215 LYS A C   1 
ATOM   1648 O O   . LYS A 1 215 ? 4.83427  8.90681  -11.17616 1.000 59.34192  ? 215 LYS A O   1 
ATOM   1649 C CB  . LYS A 1 215 ? 4.83197  8.53015  -13.97178 1.000 67.04460  ? 215 LYS A CB  1 
ATOM   1650 C CG  . LYS A 1 215 ? 4.87047  8.12805  -15.43760 1.000 67.18083  ? 215 LYS A CG  1 
ATOM   1651 C CD  . LYS A 1 215 ? 3.74665  7.13683  -15.79050 1.000 70.56069  ? 215 LYS A CD  1 
ATOM   1652 C CE  . LYS A 1 215 ? 3.73704  6.81733  -17.28730 1.000 72.81811  ? 215 LYS A CE  1 
ATOM   1653 N NZ  . LYS A 1 215 ? 2.97383  5.58413  -17.65323 1.000 70.58372  ? 215 LYS A NZ  1 
ATOM   1654 N N   . ASP A 1 216 ? 4.93089  6.68059  -10.85810 1.000 63.18770  ? 216 ASP A N   1 
ATOM   1655 C CA  . ASP A 1 216 ? 4.54716  6.73200  -9.44851  1.000 60.72603  ? 216 ASP A CA  1 
ATOM   1656 C C   . ASP A 1 216 ? 5.76150  6.44925  -8.56969  1.000 59.39865  ? 216 ASP A C   1 
ATOM   1657 O O   . ASP A 1 216 ? 6.44496  5.43695  -8.75764  1.000 59.52917  ? 216 ASP A O   1 
ATOM   1658 C CB  . ASP A 1 216 ? 3.44418  5.72353  -9.12815  1.000 60.51551  ? 216 ASP A CB  1 
ATOM   1659 C CG  . ASP A 1 216 ? 2.22695  5.87635  -10.02171 1.000 66.11580  ? 216 ASP A CG  1 
ATOM   1660 O OD1 . ASP A 1 216 ? 2.18588  6.82487  -10.83481 1.000 66.42933  ? 216 ASP A OD1 1 
ATOM   1661 O OD2 . ASP A 1 216 ? 1.31124  5.03622  -9.91397  1.000 66.52362  ? 216 ASP A OD2 1 
ATOM   1662 N N   . PHE A 1 217 ? 6.00941  7.32787  -7.59494  1.000 56.32418  ? 217 PHE A N   1 
ATOM   1663 C CA  . PHE A 1 217 ? 7.16195  7.20600  -6.70828  1.000 53.67148  ? 217 PHE A CA  1 
ATOM   1664 C C   . PHE A 1 217 ? 6.75269  7.47028  -5.26678  1.000 50.84043  ? 217 PHE A C   1 
ATOM   1665 O O   . PHE A 1 217 ? 5.86294  8.27912  -4.99367  1.000 52.50774  ? 217 PHE A O   1 
ATOM   1666 C CB  . PHE A 1 217 ? 8.28049  8.19303  -7.07026  1.000 45.93077  ? 217 PHE A CB  1 
ATOM   1667 C CG  . PHE A 1 217 ? 8.64105  8.18897  -8.50873  1.000 53.10978  ? 217 PHE A CG  1 
ATOM   1668 C CD1 . PHE A 1 217 ? 7.86520  8.87458  -9.44043  1.000 53.47229  ? 217 PHE A CD1 1 
ATOM   1669 C CD2 . PHE A 1 217 ? 9.77011  7.51288  -8.94708  1.000 50.03497  ? 217 PHE A CD2 1 
ATOM   1670 C CE1 . PHE A 1 217 ? 8.20573  8.86664  -10.78037 1.000 55.30957  ? 217 PHE A CE1 1 
ATOM   1671 C CE2 . PHE A 1 217 ? 10.11502 7.51715  -10.29912 1.000 50.79330  ? 217 PHE A CE2 1 
ATOM   1672 C CZ  . PHE A 1 217 ? 9.33278  8.19199  -11.20865 1.000 52.73640  ? 217 PHE A CZ  1 
ATOM   1673 N N   . GLN A 1 218 ? 7.44025  6.80372  -4.34901  1.000 46.82014  ? 218 GLN A N   1 
ATOM   1674 C CA  . GLN A 1 218 ? 7.37967  7.13232  -2.93331  1.000 44.65909  ? 218 GLN A CA  1 
ATOM   1675 C C   . GLN A 1 218 ? 8.46252  8.17415  -2.64641  1.000 41.14176  ? 218 GLN A C   1 
ATOM   1676 O O   . GLN A 1 218 ? 9.65294  7.87926  -2.75361  1.000 37.59381  ? 218 GLN A O   1 
ATOM   1677 C CB  . GLN A 1 218 ? 7.57745  5.86298  -2.10859  1.000 47.49895  ? 218 GLN A CB  1 
ATOM   1678 C CG  . GLN A 1 218 ? 7.19123  5.95328  -0.64659  1.000 48.70538  ? 218 GLN A CG  1 
ATOM   1679 C CD  . GLN A 1 218 ? 5.69299  5.77778  -0.40742  1.000 57.05803  ? 218 GLN A CD  1 
ATOM   1680 O OE1 . GLN A 1 218 ? 4.96172  5.24138  -1.24664  1.000 60.16503  ? 218 GLN A OE1 1 
ATOM   1681 N NE2 . GLN A 1 218 ? 5.23114  6.23172  0.75072   1.000 59.34183  ? 218 GLN A NE2 1 
ATOM   1682 N N   . ILE A 1 219 ? 8.06514  9.40600  -2.33740  1.000 43.38723  ? 219 ILE A N   1 
ATOM   1683 C CA  . ILE A 1 219 ? 9.01165  10.46986 -2.00055  1.000 41.20985  ? 219 ILE A CA  1 
ATOM   1684 C C   . ILE A 1 219 ? 8.95132  10.73129 -0.50178  1.000 43.80479  ? 219 ILE A C   1 
ATOM   1685 O O   . ILE A 1 219 ? 7.87565  10.97593 0.04926   1.000 47.18492  ? 219 ILE A O   1 
ATOM   1686 C CB  . ILE A 1 219 ? 8.73776  11.76244 -2.78672  1.000 43.34359  ? 219 ILE A CB  1 
ATOM   1687 C CG1 . ILE A 1 219 ? 8.67336  11.46971 -4.30812  1.000 43.79610  ? 219 ILE A CG1 1 
ATOM   1688 C CG2 . ILE A 1 219 ? 9.81537  12.78927 -2.46253  1.000 36.78770  ? 219 ILE A CG2 1 
ATOM   1689 C CD1 . ILE A 1 219 ? 8.09086  12.59650 -5.15757  1.000 43.88260  ? 219 ILE A CD1 1 
ATOM   1690 N N   . SER A 1 220 ? 10.10655 10.65469 0.16009   1.000 36.50409  ? 220 SER A N   1 
ATOM   1691 C CA  . SER A 1 220 ? 10.23773 10.97356 1.57194   1.000 35.90320  ? 220 SER A CA  1 
ATOM   1692 C C   . SER A 1 220 ? 10.91066 12.32610 1.73505   1.000 34.50639  ? 220 SER A C   1 
ATOM   1693 O O   . SER A 1 220 ? 11.79400 12.68820 0.95195   1.000 36.63128  ? 220 SER A O   1 
ATOM   1694 C CB  . SER A 1 220 ? 11.06901 9.92999  2.29559   1.000 34.35879  ? 220 SER A CB  1 
ATOM   1695 O OG  . SER A 1 220 ? 12.44745 10.18805 1.99814   1.000 37.63534  ? 220 SER A OG  1 
ATOM   1696 N N   . VAL A 1 221 ? 10.51543 13.05812 2.77048   1.000 35.60456  ? 221 VAL A N   1 
ATOM   1697 C CA  . VAL A 1 221 ? 11.17638 14.28842 3.18343   1.000 34.80504  ? 221 VAL A CA  1 
ATOM   1698 C C   . VAL A 1 221 ? 11.39825 14.18530 4.69087   1.000 37.08851  ? 221 VAL A C   1 
ATOM   1699 O O   . VAL A 1 221 ? 10.43531 14.22711 5.46571   1.000 39.00689  ? 221 VAL A O   1 
ATOM   1700 C CB  . VAL A 1 221 ? 10.35230 15.53690 2.84283   1.000 37.30232  ? 221 VAL A CB  1 
ATOM   1701 C CG1 . VAL A 1 221 ? 10.94712 16.73360 3.56992   1.000 35.44827  ? 221 VAL A CG1 1 
ATOM   1702 C CG2 . VAL A 1 221 ? 10.30897 15.79009 1.28977   1.000 35.02168  ? 221 VAL A CG2 1 
ATOM   1703 N N   . ASP A 1 222 ? 12.64938 14.04423 5.11028   1.000 32.76265  ? 222 ASP A N   1 
ATOM   1704 C CA  . ASP A 1 222 ? 12.90869 13.73677 6.51408   1.000 35.36334  ? 222 ASP A CA  1 
ATOM   1705 C C   . ASP A 1 222 ? 12.02727 12.54278 6.91344   1.000 37.10196  ? 222 ASP A C   1 
ATOM   1706 O O   . ASP A 1 222 ? 12.03827 11.51409 6.23320   1.000 37.92372  ? 222 ASP A O   1 
ATOM   1707 C CB  . ASP A 1 222 ? 12.66801 14.98960 7.38342   1.000 32.67755  ? 222 ASP A CB  1 
ATOM   1708 C CG  . ASP A 1 222 ? 13.63175 16.13037 7.04414   1.000 28.26030  ? 222 ASP A CG  1 
ATOM   1709 O OD1 . ASP A 1 222 ? 14.75934 15.86132 6.63216   1.000 26.02481  ? 222 ASP A OD1 1 
ATOM   1710 O OD2 . ASP A 1 222 ? 13.26687 17.29690 7.21366   1.000 30.43065  ? 222 ASP A OD2 1 
ATOM   1711 N N   . HIS A 1 223 ? 11.21029 12.66876 7.95413   1.000 37.65464  ? 223 HIS A N   1 
ATOM   1712 C CA  A HIS A 1 223 ? 10.40749 11.54457 8.41254   0.500 41.64921  ? 223 HIS A CA  1 
ATOM   1713 C CA  B HIS A 1 223 ? 10.40377 11.54042 8.41619   0.500 41.63950  ? 223 HIS A CA  1 
ATOM   1714 C C   . HIS A 1 223 ? 9.09170  11.38279 7.64989   1.000 46.29348  ? 223 HIS A C   1 
ATOM   1715 O O   . HIS A 1 223 ? 8.37369  10.40473 7.87855   1.000 46.95701  ? 223 HIS A O   1 
ATOM   1716 C CB  A HIS A 1 223 ? 10.13230 11.69992 9.91415   0.500 42.87583  ? 223 HIS A CB  1 
ATOM   1717 C CB  B HIS A 1 223 ? 10.11650 11.69171 9.92459   0.500 42.86110  ? 223 HIS A CB  1 
ATOM   1718 C CG  A HIS A 1 223 ? 9.43842  12.97779 10.27886  0.500 42.59267  ? 223 HIS A CG  1 
ATOM   1719 C CG  B HIS A 1 223 ? 9.31286  10.57060 10.53238  0.500 42.07607  ? 223 HIS A CG  1 
ATOM   1720 N ND1 A HIS A 1 223 ? 10.01495 14.21849 10.10007  0.500 37.88719  ? 223 HIS A ND1 1 
ATOM   1721 N ND1 B HIS A 1 223 ? 9.04511  9.38456  9.87917   0.500 41.95122  ? 223 HIS A ND1 1 
ATOM   1722 C CD2 A HIS A 1 223 ? 8.21943  13.20305 10.82527  0.500 40.52223  ? 223 HIS A CD2 1 
ATOM   1723 C CD2 B HIS A 1 223 ? 8.71941  10.46666 11.74588  0.500 42.35535  ? 223 HIS A CD2 1 
ATOM   1724 C CE1 A HIS A 1 223 ? 9.17563  15.15172 10.51055  0.500 38.18502  ? 223 HIS A CE1 1 
ATOM   1725 C CE1 B HIS A 1 223 ? 8.32174  8.60365  10.66124  0.500 40.96474  ? 223 HIS A CE1 1 
ATOM   1726 N NE2 A HIS A 1 223 ? 8.07861  14.56299 10.95381  0.500 39.95336  ? 223 HIS A NE2 1 
ATOM   1727 N NE2 B HIS A 1 223 ? 8.11151  9.23594  11.80050  0.500 41.02064  ? 223 HIS A NE2 1 
ATOM   1728 N N   . LEU A 1 224 ? 8.75103  12.29777 6.74988   1.000 47.45903  ? 224 LEU A N   1 
ATOM   1729 C CA  . LEU A 1 224 ? 7.45426  12.25781 6.07315   1.000 50.44166  ? 224 LEU A CA  1 
ATOM   1730 C C   . LEU A 1 224 ? 7.60636  11.55518 4.72702   1.000 52.83350  ? 224 LEU A C   1 
ATOM   1731 O O   . LEU A 1 224 ? 8.54367  11.84358 3.98153   1.000 50.18049  ? 224 LEU A O   1 
ATOM   1732 C CB  . LEU A 1 224 ? 6.91890  13.67602 5.88508   1.000 46.84789  ? 224 LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 224 ? 7.09729  14.51526 7.15421   1.000 52.01444  ? 224 LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 224 ? 6.90287  16.00453 6.92269   1.000 54.15254  ? 224 LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 224 ? 6.13934  14.03044 8.24164   1.000 51.59051  ? 224 LEU A CD2 1 
ATOM   1736 N N   . SER A 1 225 ? 6.70065  10.62452 4.42500   1.000 54.51069  ? 225 SER A N   1 
ATOM   1737 C CA  . SER A 1 225 ? 6.81864  9.79111  3.22846   1.000 56.10761  ? 225 SER A CA  1 
ATOM   1738 C C   . SER A 1 225 ? 5.49447  9.76980  2.48025   1.000 56.85492  ? 225 SER A C   1 
ATOM   1739 O O   . SER A 1 225 ? 4.51251  9.20239  2.96821   1.000 57.48736  ? 225 SER A O   1 
ATOM   1740 C CB  . SER A 1 225 ? 7.25360  8.36619  3.58261   1.000 54.81886  ? 225 SER A CB  1 
ATOM   1741 O OG  . SER A 1 225 ? 7.59595  7.63449  2.41597   1.000 54.46700  ? 225 SER A OG  1 
ATOM   1742 N N   . ILE A 1 226 ? 5.48173  10.35205 1.28040   1.000 57.58697  ? 226 ILE A N   1 
ATOM   1743 C CA  . ILE A 1 226 ? 4.25830  10.57744 0.51609   1.000 68.01388  ? 226 ILE A CA  1 
ATOM   1744 C C   . ILE A 1 226 ? 4.34289  9.80410  -0.79906  1.000 60.77543  ? 226 ILE A C   1 
ATOM   1745 O O   . ILE A 1 226 ? 5.33939  9.91033  -1.52883  1.000 53.62904  ? 226 ILE A O   1 
ATOM   1746 C CB  . ILE A 1 226 ? 4.03007  12.08096 0.24598   1.000 64.90896  ? 226 ILE A CB  1 
ATOM   1747 C CG1 . ILE A 1 226 ? 4.41434  12.93293 1.46885   1.000 64.45814  ? 226 ILE A CG1 1 
ATOM   1748 C CG2 . ILE A 1 226 ? 2.59237  12.34072 -0.17721  1.000 66.06775  ? 226 ILE A CG2 1 
ATOM   1749 C CD1 . ILE A 1 226 ? 5.83417  13.55163 1.39524   1.000 56.85176  ? 226 ILE A CD1 1 
ATOM   1750 N N   . LEU A 1 227 ? 3.29706  9.03606  -1.10309  1.000 60.31341  ? 227 LEU A N   1 
ATOM   1751 C CA  . LEU A 1 227 ? 3.15828  8.43577  -2.42338  1.000 60.51124  ? 227 LEU A CA  1 
ATOM   1752 C C   . LEU A 1 227 ? 2.68084  9.49823  -3.40017  1.000 63.18109  ? 227 LEU A C   1 
ATOM   1753 O O   . LEU A 1 227 ? 1.58036  10.03613 -3.24405  1.000 70.11046  ? 227 LEU A O   1 
ATOM   1754 C CB  . LEU A 1 227 ? 2.18510  7.26034  -2.39137  1.000 62.98279  ? 227 LEU A CB  1 
ATOM   1755 C CG  . LEU A 1 227 ? 2.07248  6.38595  -3.64962  1.000 62.91883  ? 227 LEU A CG  1 
ATOM   1756 C CD1 . LEU A 1 227 ? 1.03803  6.90945  -4.61961  1.000 66.46787  ? 227 LEU A CD1 1 
ATOM   1757 C CD2 . LEU A 1 227 ? 3.41651  6.26307  -4.34379  1.000 59.26160  ? 227 LEU A CD2 1 
ATOM   1758 N N   . HIS A 1 228 ? 3.50127  9.80118  -4.40638  1.000 61.35668  ? 228 HIS A N   1 
ATOM   1759 C CA  . HIS A 1 228 ? 3.17291  10.79806 -5.42267  1.000 64.60055  ? 228 HIS A CA  1 
ATOM   1760 C C   . HIS A 1 228 ? 2.82652  10.10805 -6.73932  1.000 63.51352  ? 228 HIS A C   1 
ATOM   1761 O O   . HIS A 1 228 ? 3.57252  9.23668  -7.20267  1.000 58.25607  ? 228 HIS A O   1 
ATOM   1762 C CB  . HIS A 1 228 ? 4.33891  11.77142 -5.62044  1.000 62.26362  ? 228 HIS A CB  1 
ATOM   1763 C CG  . HIS A 1 228 ? 4.50272  12.74300 -4.49768  1.000 61.46064  ? 228 HIS A CG  1 
ATOM   1764 N ND1 . HIS A 1 228 ? 4.10798  14.05970 -4.59374  1.000 65.03744  ? 228 HIS A ND1 1 
ATOM   1765 C CD2 . HIS A 1 228 ? 4.99488  12.58635 -3.24500  1.000 60.29006  ? 228 HIS A CD2 1 
ATOM   1766 C CE1 . HIS A 1 228 ? 4.36053  14.67590 -3.45163  1.000 65.49471  ? 228 HIS A CE1 1 
ATOM   1767 N NE2 . HIS A 1 228 ? 4.89540  13.80462 -2.61528  1.000 60.91810  ? 228 HIS A NE2 1 
ATOM   1768 N N   . ARG A 1 229 ? 1.70008  10.49569 -7.33823  1.000 65.59189  ? 229 ARG A N   1 
ATOM   1769 C CA  . ARG A 1 229 ? 1.27319  9.94255  -8.61438  1.000 66.17793  ? 229 ARG A CA  1 
ATOM   1770 C C   . ARG A 1 229 ? 1.38658  10.98948 -9.71361  1.000 66.54963  ? 229 ARG A C   1 
ATOM   1771 O O   . ARG A 1 229 ? 1.39168  12.19280 -9.44721  1.000 65.29986  ? 229 ARG A O   1 
ATOM   1772 C CB  . ARG A 1 229 ? -0.16193 9.42141  -8.54018  1.000 69.35820  ? 229 ARG A CB  1 
ATOM   1773 C CG  . ARG A 1 229 ? -0.31652 8.22177  -7.64272  1.000 69.65009  ? 229 ARG A CG  1 
ATOM   1774 C CD  . ARG A 1 229 ? -1.75299 7.77922  -7.58187  1.000 71.54109  ? 229 ARG A CD  1 
ATOM   1775 N NE  . ARG A 1 229 ? -1.90874 6.63319  -6.69719  1.000 78.15987  ? 229 ARG A NE  1 
ATOM   1776 C CZ  . ARG A 1 229 ? -1.61951 5.38129  -7.03254  1.000 85.20857  ? 229 ARG A CZ  1 
ATOM   1777 N NH1 . ARG A 1 229 ? -1.11839 5.08033  -8.22075  1.000 87.93385  ? 229 ARG A NH1 1 
ATOM   1778 N NH2 . ARG A 1 229 ? -1.84498 4.40408  -6.15685  1.000 85.45988  ? 229 ARG A NH2 1 
ATOM   1779 N N   . ASP A 1 230 ? 1.48443  10.50766 -10.95288 1.000 73.55031  ? 230 ASP A N   1 
ATOM   1780 C CA  . ASP A 1 230 ? 1.58955  11.35238 -12.14296 1.000 70.06860  ? 230 ASP A CA  1 
ATOM   1781 C C   . ASP A 1 230 ? 2.69863  12.39740 -11.99575 1.000 68.28935  ? 230 ASP A C   1 
ATOM   1782 O O   . ASP A 1 230 ? 2.51388  13.58681 -12.27736 1.000 67.98597  ? 230 ASP A O   1 
ATOM   1783 C CB  . ASP A 1 230 ? 0.25182  12.00820 -12.46368 1.000 69.93321  ? 230 ASP A CB  1 
ATOM   1784 C CG  . ASP A 1 230 ? 0.23860  12.62486 -13.83772 1.000 76.90273  ? 230 ASP A CG  1 
ATOM   1785 O OD1 . ASP A 1 230 ? 0.75101  11.96774 -14.77305 1.000 75.93794  ? 230 ASP A OD1 1 
ATOM   1786 O OD2 . ASP A 1 230 ? -0.27059 13.76018 -13.98012 1.000 83.41235  ? 230 ASP A OD2 1 
ATOM   1787 N N   . VAL A 1 231 ? 3.87151  11.92580 -11.55501 1.000 63.80689  ? 231 VAL A N   1 
ATOM   1788 C CA  . VAL A 1 231 ? 5.03862  12.77109 -11.32643 1.000 58.76610  ? 231 VAL A CA  1 
ATOM   1789 C C   . VAL A 1 231 ? 5.82138  12.90059 -12.62247 1.000 58.35186  ? 231 VAL A C   1 
ATOM   1790 O O   . VAL A 1 231 ? 6.12256  11.90170 -13.28949 1.000 60.73193  ? 231 VAL A O   1 
ATOM   1791 C CB  . VAL A 1 231 ? 5.92099  12.19865 -10.20334 1.000 59.72074  ? 231 VAL A CB  1 
ATOM   1792 C CG1 . VAL A 1 231 ? 7.35971  12.60820 -10.38658 1.000 52.93959  ? 231 VAL A CG1 1 
ATOM   1793 C CG2 . VAL A 1 231 ? 5.40108  12.65354 -8.83299  1.000 59.62381  ? 231 VAL A CG2 1 
ATOM   1794 N N   . GLN A 1 232 ? 6.13509  14.13778 -12.98984 1.000 55.04225  ? 232 GLN A N   1 
ATOM   1795 C CA  . GLN A 1 232 ? 6.92435  14.41025 -14.18155 1.000 53.92693  ? 232 GLN A CA  1 
ATOM   1796 C C   . GLN A 1 232 ? 8.38129  14.71624 -13.86843 1.000 51.86603  ? 232 GLN A C   1 
ATOM   1797 O O   . GLN A 1 232 ? 9.23352  14.59024 -14.76302 1.000 50.08313  ? 232 GLN A O   1 
ATOM   1798 C CB  . GLN A 1 232 ? 6.32085  15.58717 -14.95177 1.000 54.98740  ? 232 GLN A CB  1 
ATOM   1799 N N   . GLU A 1 233 ? 8.67695  15.10114 -12.62753 1.000 44.97271  ? 233 GLU A N   1 
ATOM   1800 C CA  . GLU A 1 233 ? 9.98298  15.63907 -12.28661 1.000 41.66215  ? 233 GLU A CA  1 
ATOM   1801 C C   . GLU A 1 233 ? 10.07313 15.84282 -10.78626 1.000 41.40618  ? 233 GLU A C   1 
ATOM   1802 O O   . GLU A 1 233 ? 9.08374  16.17350 -10.12475 1.000 40.69954  ? 233 GLU A O   1 
ATOM   1803 C CB  . GLU A 1 233 ? 10.24638 16.97351 -12.99601 1.000 45.47642  ? 233 GLU A CB  1 
ATOM   1804 C CG  . GLU A 1 233 ? 11.72680 17.35861 -13.02882 1.000 45.50134  ? 233 GLU A CG  1 
ATOM   1805 C CD  . GLU A 1 233 ? 11.97947 18.77763 -13.52349 1.000 42.66967  ? 233 GLU A CD  1 
ATOM   1806 O OE1 . GLU A 1 233 ? 11.01901 19.56386 -13.56258 1.000 43.09094  ? 233 GLU A OE1 1 
ATOM   1807 O OE2 . GLU A 1 233 ? 13.13973 19.10529 -13.85219 1.000 43.48047  ? 233 GLU A OE2 1 
ATOM   1808 N N   . ILE A 1 234 ? 11.28170 15.64424 -10.27193 1.000 39.50907  ? 234 ILE A N   1 
ATOM   1809 C CA  . ILE A 1 234 ? 11.65998 15.92032 -8.89566  1.000 38.01845  ? 234 ILE A CA  1 
ATOM   1810 C C   . ILE A 1 234 ? 12.93904 16.74696 -8.98057  1.000 36.27673  ? 234 ILE A C   1 
ATOM   1811 O O   . ILE A 1 234 ? 13.92575 16.28939 -9.57037  1.000 36.98144  ? 234 ILE A O   1 
ATOM   1812 C CB  . ILE A 1 234 ? 11.88533 14.61891 -8.09452  1.000 37.71674  ? 234 ILE A CB  1 
ATOM   1813 C CG1 . ILE A 1 234 ? 10.70066 13.66846 -8.26187  1.000 37.26427  ? 234 ILE A CG1 1 
ATOM   1814 C CG2 . ILE A 1 234 ? 12.04082 14.90777 -6.63530  1.000 34.05029  ? 234 ILE A CG2 1 
ATOM   1815 C CD1 . ILE A 1 234 ? 10.97930 12.23457 -7.89845  1.000 36.14198  ? 234 ILE A CD1 1 
ATOM   1816 N N   . ARG A 1 235 ? 12.91337 17.97940 -8.46904  1.000 34.84823  ? 235 ARG A N   1 
ATOM   1817 C CA  A ARG A 1 235 ? 14.05146 18.88667 -8.56965  0.500 37.03701  ? 235 ARG A CA  1 
ATOM   1818 C CA  B ARG A 1 235 ? 14.05169 18.88677 -8.56663  0.500 34.11095  ? 235 ARG A CA  1 
ATOM   1819 C C   . ARG A 1 235 ? 14.60741 19.18746 -7.18236  1.000 32.02537  ? 235 ARG A C   1 
ATOM   1820 O O   . ARG A 1 235 ? 13.87601 19.62086 -6.29675  1.000 33.73148  ? 235 ARG A O   1 
ATOM   1821 C CB  A ARG A 1 235 ? 13.67755 20.19284 -9.28758  0.500 38.21683  ? 235 ARG A CB  1 
ATOM   1822 C CB  B ARG A 1 235 ? 13.68554 20.20287 -9.26109  0.500 35.24113  ? 235 ARG A CB  1 
ATOM   1823 C CG  A ARG A 1 235 ? 13.35994 20.02590 -10.77196 0.500 39.23334  ? 235 ARG A CG  1 
ATOM   1824 C CG  B ARG A 1 235 ? 13.30500 20.07197 -10.71325 0.500 39.69019  ? 235 ARG A CG  1 
ATOM   1825 C CD  A ARG A 1 235 ? 12.82914 21.31474 -11.45012 0.500 40.96765  ? 235 ARG A CD  1 
ATOM   1826 C CD  B ARG A 1 235 ? 13.24837 21.43722 -11.41989 0.500 40.95829  ? 235 ARG A CD  1 
ATOM   1827 N NE  A ARG A 1 235 ? 13.88791 22.23698 -11.85580 0.500 42.54895  ? 235 ARG A NE  1 
ATOM   1828 N NE  B ARG A 1 235 ? 12.26038 22.35349 -10.85876 0.500 40.48012  ? 235 ARG A NE  1 
ATOM   1829 C CZ  A ARG A 1 235 ? 14.39164 22.34814 -13.08368 0.500 41.16990  ? 235 ARG A CZ  1 
ATOM   1830 C CZ  B ARG A 1 235 ? 10.98856 22.40752 -11.22995 0.500 42.60186  ? 235 ARG A CZ  1 
ATOM   1831 N NH1 A ARG A 1 235 ? 13.95035 21.60817 -14.09287 0.500 37.83334  ? 235 ARG A NH1 1 
ATOM   1832 N NH1 B ARG A 1 235 ? 10.50347 21.59715 -12.15543 0.500 42.05317  ? 235 ARG A NH1 1 
ATOM   1833 N NH2 A ARG A 1 235 ? 15.37075 23.22248 -13.30370 0.500 39.66208  ? 235 ARG A NH2 1 
ATOM   1834 N NH2 B ARG A 1 235 ? 10.18020 23.29049 -10.64958 0.500 45.04463  ? 235 ARG A NH2 1 
ATOM   1835 N N   . TYR A 1 236 ? 15.90569 18.99303 -7.03100  1.000 29.17221  ? 236 TYR A N   1 
ATOM   1836 C CA  . TYR A 1 236 ? 16.65911 19.22026 -5.81091  1.000 30.32358  ? 236 TYR A CA  1 
ATOM   1837 C C   . TYR A 1 236 ? 17.60735 20.38574 -6.01069  1.000 32.36990  ? 236 TYR A C   1 
ATOM   1838 O O   . TYR A 1 236 ? 18.30688 20.46109 -7.03310  1.000 29.46505  ? 236 TYR A O   1 
ATOM   1839 C CB  . TYR A 1 236 ? 17.47810 17.98591 -5.44158  1.000 27.80340  ? 236 TYR A CB  1 
ATOM   1840 C CG  . TYR A 1 236 ? 16.66505 16.78086 -5.08681  1.000 27.77448  ? 236 TYR A CG  1 
ATOM   1841 C CD1 . TYR A 1 236 ? 15.80272 16.81932 -4.02326  1.000 30.00175  ? 236 TYR A CD1 1 
ATOM   1842 C CD2 . TYR A 1 236 ? 16.76696 15.59847 -5.81089  1.000 31.19757  ? 236 TYR A CD2 1 
ATOM   1843 C CE1 . TYR A 1 236 ? 15.05620 15.71483 -3.67728  1.000 32.26611  ? 236 TYR A CE1 1 
ATOM   1844 C CE2 . TYR A 1 236 ? 16.02303 14.48933 -5.46815  1.000 31.26887  ? 236 TYR A CE2 1 
ATOM   1845 C CZ  . TYR A 1 236 ? 15.17592 14.56456 -4.38974  1.000 31.72046  ? 236 TYR A CZ  1 
ATOM   1846 O OH  . TYR A 1 236 ? 14.41404 13.48383 -4.02578  1.000 38.08249  ? 236 TYR A OH  1 
ATOM   1847 N N   . GLU A 1 237 ? 17.64492 21.28033 -5.03117  1.000 31.18007  ? 237 GLU A N   1 
ATOM   1848 C CA  . GLU A 1 237 ? 18.69170 22.28080 -4.97069  1.000 30.93375  ? 237 GLU A CA  1 
ATOM   1849 C C   . GLU A 1 237 ? 18.87656 22.70055 -3.51983  1.000 29.29081  ? 237 GLU A C   1 
ATOM   1850 O O   . GLU A 1 237 ? 17.97596 22.54773 -2.68629  1.000 29.46983  ? 237 GLU A O   1 
ATOM   1851 C CB  . GLU A 1 237 ? 18.37165 23.48503 -5.84440  1.000 30.04828  ? 237 GLU A CB  1 
ATOM   1852 C CG  . GLU A 1 237 ? 17.07717 24.13416 -5.51279  1.000 34.11057  ? 237 GLU A CG  1 
ATOM   1853 C CD  . GLU A 1 237 ? 16.53062 24.93248 -6.69142  1.000 44.04668  ? 237 GLU A CD  1 
ATOM   1854 O OE1 . GLU A 1 237 ? 17.15498 25.94810 -7.08606  1.000 44.12303  ? 237 GLU A OE1 1 
ATOM   1855 O OE2 . GLU A 1 237 ? 15.47626 24.53076 -7.22910  1.000 44.96946  ? 237 GLU A OE2 1 
ATOM   1856 N N   . VAL A 1 238 ? 20.05586 23.24262 -3.22900  1.000 29.47161  ? 238 VAL A N   1 
ATOM   1857 C CA  . VAL A 1 238 ? 20.28233 23.81587 -1.91380  1.000 30.05169  ? 238 VAL A CA  1 
ATOM   1858 C C   . VAL A 1 238 ? 19.32489 24.97075 -1.72534  1.000 32.81265  ? 238 VAL A C   1 
ATOM   1859 O O   . VAL A 1 238 ? 19.20004 25.85545 -2.58746  1.000 34.87795  ? 238 VAL A O   1 
ATOM   1860 C CB  . VAL A 1 238 ? 21.74353 24.25122 -1.74826  1.000 30.23441  ? 238 VAL A CB  1 
ATOM   1861 C CG1 . VAL A 1 238 ? 21.98423 24.90526 -0.34936  1.000 28.41101  ? 238 VAL A CG1 1 
ATOM   1862 C CG2 . VAL A 1 238 ? 22.64658 23.04287 -1.95153  1.000 26.16391  ? 238 VAL A CG2 1 
ATOM   1863 N N   . SER A 1 239 ? 18.62285 24.95880 -0.60331  1.000 31.85597  ? 239 SER A N   1 
ATOM   1864 C CA  . SER A 1 239 ? 17.64843 26.00127 -0.33548  1.000 34.81746  ? 239 SER A CA  1 
ATOM   1865 C C   . SER A 1 239 ? 18.32296 27.34691 -0.07787  1.000 35.48705  ? 239 SER A C   1 
ATOM   1866 O O   . SER A 1 239 ? 19.45570 27.42384 0.41639   1.000 37.66441  ? 239 SER A O   1 
ATOM   1867 C CB  . SER A 1 239 ? 16.78473 25.61918 0.86444   1.000 31.10330  ? 239 SER A CB  1 
ATOM   1868 O OG  . SER A 1 239 ? 15.94849 26.71407 1.16293   1.000 33.51220  ? 239 SER A OG  1 
ATOM   1869 N N   . ALA A 1 240 ? 17.60555 28.41996 -0.41171  1.000 35.81229  ? 240 ALA A N   1 
ATOM   1870 C CA  . ALA A 1 240 ? 17.98012 29.74156 0.06589   1.000 36.81609  ? 240 ALA A CA  1 
ATOM   1871 C C   . ALA A 1 240 ? 17.61443 29.95249 1.52243   1.000 39.46856  ? 240 ALA A C   1 
ATOM   1872 O O   . ALA A 1 240 ? 18.10244 30.91298 2.12924   1.000 42.65262  ? 240 ALA A O   1 
ATOM   1873 C CB  . ALA A 1 240 ? 17.30510 30.83790 -0.76107  1.000 35.49742  ? 240 ALA A CB  1 
ATOM   1874 N N   . LYS A 1 241 ? 16.74557 29.11283 2.08690   1.000 37.83179  ? 241 LYS A N   1 
ATOM   1875 C CA  . LYS A 1 241 ? 16.40254 29.24037 3.49577   1.000 42.26519  ? 241 LYS A CA  1 
ATOM   1876 C C   . LYS A 1 241 ? 17.36507 28.41176 4.33262   1.000 37.87906  ? 241 LYS A C   1 
ATOM   1877 O O   . LYS A 1 241 ? 17.91460 27.41752 3.86718   1.000 34.36243  ? 241 LYS A O   1 
ATOM   1878 C CB  . LYS A 1 241 ? 14.96050 28.79939 3.76583   1.000 39.42067  ? 241 LYS A CB  1 
ATOM   1879 C CG  . LYS A 1 241 ? 13.89935 29.62148 3.04447   1.000 38.75641  ? 241 LYS A CG  1 
ATOM   1880 C CD  . LYS A 1 241 ? 12.59549 28.80997 2.98983   1.000 46.86315  ? 241 LYS A CD  1 
ATOM   1881 C CE  . LYS A 1 241 ? 11.41053 29.56210 2.35805   1.000 52.48077  ? 241 LYS A CE  1 
ATOM   1882 N NZ  . LYS A 1 241 ? 10.18472 28.68289 2.33723   1.000 52.38705  ? 241 LYS A NZ  1 
ATOM   1883 N N   . LYS A 1 242 ? 17.57083 28.84662 5.57252   1.000 39.30033  ? 242 LYS A N   1 
ATOM   1884 C CA  . LYS A 1 242 ? 18.43458 28.16280 6.52695   1.000 36.44266  ? 242 LYS A CA  1 
ATOM   1885 C C   . LYS A 1 242 ? 17.69426 27.98480 7.84408   1.000 35.56164  ? 242 LYS A C   1 
ATOM   1886 O O   . LYS A 1 242 ? 16.77819 28.75116 8.17406   1.000 38.50896  ? 242 LYS A O   1 
ATOM   1887 C CB  . LYS A 1 242 ? 19.72395 28.94288 6.76441   1.000 38.45879  ? 242 LYS A CB  1 
ATOM   1888 C CG  . LYS A 1 242 ? 20.45706 29.29337 5.47740   1.000 42.77254  ? 242 LYS A CG  1 
ATOM   1889 C CD  . LYS A 1 242 ? 21.85368 29.83080 5.73623   1.000 54.77654  ? 242 LYS A CD  1 
ATOM   1890 C CE  . LYS A 1 242 ? 22.92931 28.80271 5.33309   1.000 49.40740  ? 242 LYS A CE  1 
ATOM   1891 N NZ  . LYS A 1 242 ? 24.06987 28.72319 6.31623   1.000 52.16384  ? 242 LYS A NZ  1 
ATOM   1892 N N   . ILE A 1 243 ? 18.08990 26.96469 8.58015   1.000 36.41000  ? 243 ILE A N   1 
ATOM   1893 C CA  . ILE A 1 243 ? 17.62339 26.74359 9.94258   1.000 36.35436  ? 243 ILE A CA  1 
ATOM   1894 C C   . ILE A 1 243 ? 18.63173 27.36370 10.89624  1.000 36.15241  ? 243 ILE A C   1 
ATOM   1895 O O   . ILE A 1 243 ? 19.84381 27.21313 10.72837  1.000 32.99308  ? 243 ILE A O   1 
ATOM   1896 C CB  . ILE A 1 243 ? 17.42294 25.23757 10.22803  1.000 36.83655  ? 243 ILE A CB  1 
ATOM   1897 C CG1 . ILE A 1 243 ? 16.76499 25.01319 11.59817  1.000 37.69515  ? 243 ILE A CG1 1 
ATOM   1898 C CG2 . ILE A 1 243 ? 18.72550 24.47878 10.16974  1.000 32.58142  ? 243 ILE A CG2 1 
ATOM   1899 C CD1 . ILE A 1 243 ? 16.83278 23.56495 12.04653  1.000 35.12284  ? 243 ILE A CD1 1 
ATOM   1900 N N   . HIS A 1 244 ? 18.13167 28.06488 11.90349  1.000 36.62117  ? 244 HIS A N   1 
ATOM   1901 C CA  . HIS A 1 244 ? 18.96571 28.75422 12.87611  1.000 39.06218  ? 244 HIS A CA  1 
ATOM   1902 C C   . HIS A 1 244 ? 18.92686 28.03145 14.21932  1.000 36.92595  ? 244 HIS A C   1 
ATOM   1903 O O   . HIS A 1 244 ? 17.84760 27.79895 14.77003  1.000 37.43257  ? 244 HIS A O   1 
ATOM   1904 C CB  . HIS A 1 244 ? 18.48961 30.20067 13.04454  1.000 38.44573  ? 244 HIS A CB  1 
ATOM   1905 C CG  . HIS A 1 244 ? 18.35464 30.93799 11.74643  1.000 41.97958  ? 244 HIS A CG  1 
ATOM   1906 N ND1 . HIS A 1 244 ? 19.44187 31.25986 10.95775  1.000 42.31006  ? 244 HIS A ND1 1 
ATOM   1907 C CD2 . HIS A 1 244 ? 17.26572 31.40965 11.09282  1.000 44.66631  ? 244 HIS A CD2 1 
ATOM   1908 C CE1 . HIS A 1 244 ? 19.03006 31.90695 9.88484   1.000 40.71679  ? 244 HIS A CE1 1 
ATOM   1909 N NE2 . HIS A 1 244 ? 17.71506 32.01006 9.93978   1.000 44.81785  ? 244 HIS A NE2 1 
ATOM   1910 N N   . PHE A 1 245 ? 20.09725 27.70792 14.75749  1.000 38.02810  ? 245 PHE A N   1 
ATOM   1911 C CA  . PHE A 1 245 ? 20.20910 27.17268 16.10737  1.000 40.38661  ? 245 PHE A CA  1 
ATOM   1912 C C   . PHE A 1 245 ? 20.65623 28.27007 17.07041  1.000 44.59886  ? 245 PHE A C   1 
ATOM   1913 O O   . PHE A 1 245 ? 21.43106 29.15971 16.70851  1.000 47.25410  ? 245 PHE A O   1 
ATOM   1914 C CB  . PHE A 1 245 ? 21.20010 26.00686 16.17661  1.000 42.33494  ? 245 PHE A CB  1 
ATOM   1915 C CG  . PHE A 1 245 ? 20.84199 24.85071 15.30050  1.000 40.08592  ? 245 PHE A CG  1 
ATOM   1916 C CD1 . PHE A 1 245 ? 21.11939 24.88098 13.93275  1.000 38.81187  ? 245 PHE A CD1 1 
ATOM   1917 C CD2 . PHE A 1 245 ? 20.22264 23.74528 15.82697  1.000 36.70027  ? 245 PHE A CD2 1 
ATOM   1918 C CE1 . PHE A 1 245 ? 20.78397 23.80941 13.11315  1.000 36.23696  ? 245 PHE A CE1 1 
ATOM   1919 C CE2 . PHE A 1 245 ? 19.88662 22.67362 15.01492  1.000 36.95553  ? 245 PHE A CE2 1 
ATOM   1920 C CZ  . PHE A 1 245 ? 20.16298 22.70746 13.65623  1.000 36.23593  ? 245 PHE A CZ  1 
ATOM   1921 N N   . ALA A 1 246 ? 20.15783 28.21204 18.29778  1.000 44.70500  ? 246 ALA A N   1 
ATOM   1922 C CA  . ALA A 1 246 ? 20.70857 29.01597 19.38335  1.000 45.79933  ? 246 ALA A CA  1 
ATOM   1923 C C   . ALA A 1 246 ? 21.84357 28.23013 20.02666  1.000 47.25063  ? 246 ALA A C   1 
ATOM   1924 O O   . ALA A 1 246 ? 21.65044 27.08076 20.43127  1.000 52.72190  ? 246 ALA A O   1 
ATOM   1925 C CB  . ALA A 1 246 ? 19.62403 29.34331 20.39554  1.000 49.39419  ? 246 ALA A CB  1 
ATOM   1926 N N   . ARG A 1 247 ? 23.03566 28.81202 20.08775  1.000 52.91695  ? 247 ARG A N   1 
ATOM   1927 C CA  . ARG A 1 247 ? 24.15665 28.13392 20.72834  1.000 58.07540  ? 247 ARG A CA  1 
ATOM   1928 C C   . ARG A 1 247 ? 24.58883 28.88360 21.98166  1.000 61.17275  ? 247 ARG A C   1 
ATOM   1929 O O   . ARG A 1 247 ? 24.63841 30.11503 21.99731  1.000 64.87620  ? 247 ARG A O   1 
ATOM   1930 C CB  . ARG A 1 247 ? 25.33479 27.96999 19.76400  1.000 54.67754  ? 247 ARG A CB  1 
ATOM   1931 C CG  . ARG A 1 247 ? 25.01970 27.08622 18.52990  1.000 56.59468  ? 247 ARG A CG  1 
ATOM   1932 C CD  . ARG A 1 247 ? 24.66942 25.59556 18.80691  1.000 60.64652  ? 247 ARG A CD  1 
ATOM   1933 N NE  . ARG A 1 247 ? 24.60240 24.82752 17.55310  1.000 68.66318  ? 247 ARG A NE  1 
ATOM   1934 C CZ  . ARG A 1 247 ? 24.09475 23.60442 17.41964  1.000 56.60549  ? 247 ARG A CZ  1 
ATOM   1935 N NH1 . ARG A 1 247 ? 23.61632 22.93613 18.45641  1.000 78.26248  ? 247 ARG A NH1 1 
ATOM   1936 N NH2 . ARG A 1 247 ? 24.06247 23.04423 16.21547  1.000 49.62534  ? 247 ARG A NH2 1 
ATOM   1937 N N   . PHE A 1 248 ? 24.88474 28.14112 23.04094  1.000 64.81927  ? 248 PHE A N   1 
ATOM   1938 C CA  . PHE A 1 248 ? 25.37550 28.75304 24.26536  1.000 66.69271  ? 248 PHE A CA  1 
ATOM   1939 C C   . PHE A 1 248 ? 26.77335 28.30067 24.63937  1.000 65.68431  ? 248 PHE A C   1 
ATOM   1940 O O   . PHE A 1 248 ? 27.35478 28.85731 25.58178  1.000 65.08394  ? 248 PHE A O   1 
ATOM   1941 C CB  . PHE A 1 248 ? 24.41864 28.47063 25.42514  1.000 75.25860  ? 248 PHE A CB  1 
ATOM   1942 C CG  . PHE A 1 248 ? 23.11514 29.17768 25.29335  1.000 82.41682  ? 248 PHE A CG  1 
ATOM   1943 C CD1 . PHE A 1 248 ? 22.94708 30.44070 25.82980  1.000 78.97572  ? 248 PHE A CD1 1 
ATOM   1944 C CD2 . PHE A 1 248 ? 22.06808 28.59594 24.59944  1.000 73.63005  ? 248 PHE A CD2 1 
ATOM   1945 C CE1 . PHE A 1 248 ? 21.75673 31.10667 25.70418  1.000 79.05227  ? 248 PHE A CE1 1 
ATOM   1946 C CE2 . PHE A 1 248 ? 20.86804 29.26131 24.46877  1.000 74.77662  ? 248 PHE A CE2 1 
ATOM   1947 C CZ  . PHE A 1 248 ? 20.71390 30.52109 25.02590  1.000 80.39526  ? 248 PHE A CZ  1 
ATOM   1948 N N   . ARG A 1 249 ? 27.32136 27.32171 23.92549  1.000 58.44161  ? 249 ARG A N   1 
ATOM   1949 C CA  . ARG A 1 249 ? 28.61913 26.75372 24.21787  1.000 56.43301  ? 249 ARG A CA  1 
ATOM   1950 C C   . ARG A 1 249 ? 29.20111 26.24190 22.90956  1.000 53.57474  ? 249 ARG A C   1 
ATOM   1951 O O   . ARG A 1 249 ? 28.48958 26.06894 21.92261  1.000 50.06556  ? 249 ARG A O   1 
ATOM   1952 C CB  . ARG A 1 249 ? 28.50431 25.62493 25.24944  1.000 60.62670  ? 249 ARG A CB  1 
ATOM   1953 C CG  . ARG A 1 249 ? 29.76827 25.36629 26.06011  1.000 67.11286  ? 249 ARG A CG  1 
ATOM   1954 C CD  . ARG A 1 249 ? 29.60907 24.21156 27.05903  1.000 73.77797  ? 249 ARG A CD  1 
ATOM   1955 N NE  . ARG A 1 249 ? 28.21286 23.88181 27.32499  1.000 75.91563  ? 249 ARG A NE  1 
ATOM   1956 C CZ  . ARG A 1 249 ? 27.58463 22.82886 26.81739  1.000 75.63457  ? 249 ARG A CZ  1 
ATOM   1957 N NH1 . ARG A 1 249 ? 28.20892 21.96425 26.03161  1.000 79.52312  ? 249 ARG A NH1 1 
ATOM   1958 N NH2 . ARG A 1 249 ? 26.29787 22.64084 27.10211  1.000 69.72785  ? 249 ARG A NH2 1 
ATOM   1959 N N   . SER A 1 250 ? 30.50725 26.02139 22.90110  1.000 52.73320  ? 250 SER A N   1 
ATOM   1960 C CA  . SER A 1 250 ? 31.14880 25.39505 21.75722  1.000 44.09071  ? 250 SER A CA  1 
ATOM   1961 C C   . SER A 1 250 ? 30.87333 23.90573 21.81759  1.000 41.62673  ? 250 SER A C   1 
ATOM   1962 O O   . SER A 1 250 ? 31.21648 23.24183 22.79677  1.000 46.27679  ? 250 SER A O   1 
ATOM   1963 C CB  . SER A 1 250 ? 32.65406 25.64769 21.75825  1.000 46.20406  ? 250 SER A CB  1 
ATOM   1964 O OG  . SER A 1 250 ? 33.23794 25.07971 20.58814  1.000 48.63409  ? 250 SER A OG  1 
ATOM   1965 N N   . PHE A 1 251 ? 30.22602 23.38029 20.79274  1.000 39.91254  ? 251 PHE A N   1 
ATOM   1966 C CA  . PHE A 1 251 ? 30.08002 21.93858 20.64358  1.000 39.18329  ? 251 PHE A CA  1 
ATOM   1967 C C   . PHE A 1 251 ? 30.28649 21.67492 19.15741  1.000 37.18892  ? 251 PHE A C   1 
ATOM   1968 O O   . PHE A 1 251 ? 29.33151 21.64734 18.37214  1.000 36.21668  ? 251 PHE A O   1 
ATOM   1969 C CB  . PHE A 1 251 ? 28.72444 21.45638 21.16243  1.000 41.89472  ? 251 PHE A CB  1 
ATOM   1970 C CG  . PHE A 1 251 ? 28.61473 19.96536 21.28724  1.000 44.34812  ? 251 PHE A CG  1 
ATOM   1971 C CD1 . PHE A 1 251 ? 29.66811 19.13618 20.92057  1.000 41.78759  ? 251 PHE A CD1 1 
ATOM   1972 C CD2 . PHE A 1 251 ? 27.45155 19.38690 21.76093  1.000 48.57230  ? 251 PHE A CD2 1 
ATOM   1973 C CE1 . PHE A 1 251 ? 29.56884 17.76303 21.02685  1.000 41.37961  ? 251 PHE A CE1 1 
ATOM   1974 C CE2 . PHE A 1 251 ? 27.33766 18.01119 21.87349  1.000 49.05162  ? 251 PHE A CE2 1 
ATOM   1975 C CZ  . PHE A 1 251 ? 28.40078 17.19586 21.50375  1.000 47.17545  ? 251 PHE A CZ  1 
ATOM   1976 N N   . PRO A 1 252 ? 31.54162 21.51551 18.73522  1.000 37.40398  ? 252 PRO A N   1 
ATOM   1977 C CA  . PRO A 1 252 ? 31.85207 21.44439 17.30514  1.000 34.31989  ? 252 PRO A CA  1 
ATOM   1978 C C   . PRO A 1 252 ? 31.24412 20.21942 16.63710  1.000 36.43414  ? 252 PRO A C   1 
ATOM   1979 O O   . PRO A 1 252 ? 31.12088 19.15022 17.23832  1.000 36.09571  ? 252 PRO A O   1 
ATOM   1980 C CB  . PRO A 1 252 ? 33.38576 21.38476 17.27856  1.000 34.08813  ? 252 PRO A CB  1 
ATOM   1981 C CG  . PRO A 1 252 ? 33.83625 21.95964 18.61668  1.000 35.54618  ? 252 PRO A CG  1 
ATOM   1982 C CD  . PRO A 1 252 ? 32.74672 21.62656 19.58235  1.000 38.03687  ? 252 PRO A CD  1 
ATOM   1983 N N   . PHE A 1 253 ? 30.90684 20.38422 15.35291  1.000 35.23519  ? 253 PHE A N   1 
ATOM   1984 C CA  . PHE A 1 253 ? 30.29975 19.30511 14.56828  1.000 32.24252  ? 253 PHE A CA  1 
ATOM   1985 C C   . PHE A 1 253 ? 31.12856 18.02390 14.60368  1.000 30.18398  ? 253 PHE A C   1 
ATOM   1986 O O   . PHE A 1 253 ? 30.59736 16.93085 14.83097  1.000 30.31221  ? 253 PHE A O   1 
ATOM   1987 C CB  . PHE A 1 253 ? 30.12175 19.76778 13.12389  1.000 29.82780  ? 253 PHE A CB  1 
ATOM   1988 C CG  . PHE A 1 253 ? 29.52261 18.73408 12.23595  1.000 28.82092  ? 253 PHE A CG  1 
ATOM   1989 C CD1 . PHE A 1 253 ? 28.14903 18.48886 12.26212  1.000 29.94041  ? 253 PHE A CD1 1 
ATOM   1990 C CD2 . PHE A 1 253 ? 30.30995 18.03054 11.35408  1.000 26.71078  ? 253 PHE A CD2 1 
ATOM   1991 C CE1 . PHE A 1 253 ? 27.58233 17.55592 11.43369  1.000 28.50302  ? 253 PHE A CE1 1 
ATOM   1992 C CE2 . PHE A 1 253 ? 29.75558 17.08349 10.50955  1.000 28.26094  ? 253 PHE A CE2 1 
ATOM   1993 C CZ  . PHE A 1 253 ? 28.38516 16.84285 10.54112  1.000 28.56334  ? 253 PHE A CZ  1 
ATOM   1994 N N   . TRP A 1 254 ? 32.43436 18.13092 14.35124  1.000 29.07185  ? 254 TRP A N   1 
ATOM   1995 C CA  . TRP A 1 254 ? 33.26409 16.92989 14.34677  1.000 29.25216  ? 254 TRP A CA  1 
ATOM   1996 C C   . TRP A 1 254 ? 33.34460 16.31573 15.72967  1.000 29.02872  ? 254 TRP A C   1 
ATOM   1997 O O   . TRP A 1 254 ? 33.48116 15.08982 15.85268  1.000 28.27938  ? 254 TRP A O   1 
ATOM   1998 C CB  . TRP A 1 254 ? 34.68629 17.23090 13.81832  1.000 28.73900  ? 254 TRP A CB  1 
ATOM   1999 C CG  . TRP A 1 254 ? 34.71777 17.75508 12.43671  1.000 27.73799  ? 254 TRP A CG  1 
ATOM   2000 C CD1 . TRP A 1 254 ? 35.25201 18.93889 12.02260  1.000 26.60823  ? 254 TRP A CD1 1 
ATOM   2001 C CD2 . TRP A 1 254 ? 34.17949 17.12675 11.27133  1.000 28.42144  ? 254 TRP A CD2 1 
ATOM   2002 N NE1 . TRP A 1 254 ? 35.08357 19.08718 10.67964  1.000 26.02609  ? 254 TRP A NE1 1 
ATOM   2003 C CE2 . TRP A 1 254 ? 34.43644 17.97986 10.18509  1.000 27.30945  ? 254 TRP A CE2 1 
ATOM   2004 C CE3 . TRP A 1 254 ? 33.53302 15.90536 11.03710  1.000 27.00521  ? 254 TRP A CE3 1 
ATOM   2005 C CZ2 . TRP A 1 254 ? 34.07471 17.65116 8.88545   1.000 25.57462  ? 254 TRP A CZ2 1 
ATOM   2006 C CZ3 . TRP A 1 254 ? 33.15941 15.58826 9.77193   1.000 26.21270  ? 254 TRP A CZ3 1 
ATOM   2007 C CH2 . TRP A 1 254 ? 33.41651 16.46364 8.69820   1.000 25.54393  ? 254 TRP A CH2 1 
ATOM   2008 N N   . ARG A 1 255 ? 33.24944 17.12462 16.78903  1.000 29.79621  ? 255 ARG A N   1 
ATOM   2009 C CA  . ARG A 1 255 ? 33.15529 16.50950 18.11058  1.000 30.62186  ? 255 ARG A CA  1 
ATOM   2010 C C   . ARG A 1 255 ? 31.82061 15.79720 18.27520  1.000 30.00536  ? 255 ARG A C   1 
ATOM   2011 O O   . ARG A 1 255 ? 31.76012 14.68649 18.81126  1.000 29.95343  ? 255 ARG A O   1 
ATOM   2012 C CB  . ARG A 1 255 ? 33.33078 17.53725 19.23545  1.000 34.10820  ? 255 ARG A CB  1 
ATOM   2013 C CG  . ARG A 1 255 ? 33.11317 16.88451 20.58869  1.000 38.96914  ? 255 ARG A CG  1 
ATOM   2014 C CD  . ARG A 1 255 ? 33.46645 17.78362 21.75808  0.800 42.64465  ? 255 ARG A CD  1 
ATOM   2015 N NE  . ARG A 1 255 ? 34.85483 18.20742 21.70298  0.700 48.42905  ? 255 ARG A NE  1 
ATOM   2016 C CZ  . ARG A 1 255 ? 35.87946 17.46038 22.08804  0.700 51.41207  ? 255 ARG A CZ  1 
ATOM   2017 N NH1 . ARG A 1 255 ? 35.70926 16.21331 22.49733  0.700 51.88523  ? 255 ARG A NH1 1 
ATOM   2018 N NH2 . ARG A 1 255 ? 37.10513 17.97771 22.06509  0.700 56.69732  ? 255 ARG A NH2 1 
ATOM   2019 N N   . ARG A 1 256 ? 30.74045 16.43355 17.83646  1.000 28.91448  ? 256 ARG A N   1 
ATOM   2020 C CA  . ARG A 1 256 ? 29.43836 15.77469 17.83113  1.000 30.96667  ? 256 ARG A CA  1 
ATOM   2021 C C   . ARG A 1 256 ? 29.50948 14.45966 17.05597  1.000 31.57804  ? 256 ARG A C   1 
ATOM   2022 O O   . ARG A 1 256 ? 28.97650 13.43911 17.50633  1.000 28.18730  ? 256 ARG A O   1 
ATOM   2023 C CB  . ARG A 1 256 ? 28.40275 16.72593 17.23333  1.000 34.54145  ? 256 ARG A CB  1 
ATOM   2024 C CG  . ARG A 1 256 ? 26.99483 16.58445 17.76914  1.000 42.48824  ? 256 ARG A CG  1 
ATOM   2025 C CD  . ARG A 1 256 ? 26.27358 17.94264 17.84758  1.000 43.90082  ? 256 ARG A CD  1 
ATOM   2026 N NE  . ARG A 1 256 ? 25.96439 18.47751 16.53002  1.000 40.72698  ? 256 ARG A NE  1 
ATOM   2027 C CZ  . ARG A 1 256 ? 26.51391 19.56805 16.01426  1.000 42.58698  ? 256 ARG A CZ  1 
ATOM   2028 N NH1 . ARG A 1 256 ? 27.41633 20.27570 16.67925  1.000 42.46207  ? 256 ARG A NH1 1 
ATOM   2029 N NH2 . ARG A 1 256 ? 26.14750 19.96273 14.80017  1.000 45.18056  ? 256 ARG A NH2 1 
ATOM   2030 N N   . VAL A 1 257 ? 30.25694 14.44994 15.93026  1.000 29.49335  ? 257 VAL A N   1 
ATOM   2031 C CA  . VAL A 1 257 ? 30.42042 13.22773 15.15141  1.000 28.85498  ? 257 VAL A CA  1 
ATOM   2032 C C   . VAL A 1 257 ? 31.23848 12.21407 15.93933  1.000 26.57567  ? 257 VAL A C   1 
ATOM   2033 O O   . VAL A 1 257 ? 30.90029 11.02471 15.98372  1.000 25.59220  ? 257 VAL A O   1 
ATOM   2034 C CB  . VAL A 1 257 ? 31.05110 13.51775 13.76209  1.000 27.53183  ? 257 VAL A CB  1 
ATOM   2035 C CG1 . VAL A 1 257 ? 31.48197 12.21977 13.08654  1.000 19.50497  ? 257 VAL A CG1 1 
ATOM   2036 C CG2 . VAL A 1 257 ? 30.10110 14.32963 12.82059  1.000 24.85660  ? 257 VAL A CG2 1 
ATOM   2037 N N   . HIS A 1 258 ? 32.36253 12.64764 16.52582  1.000 25.76679  ? 258 HIS A N   1 
ATOM   2038 C CA  . HIS A 1 258 ? 33.15155 11.71841 17.33389  1.000 29.21128  ? 258 HIS A CA  1 
ATOM   2039 C C   . HIS A 1 258 ? 32.29571 11.13435 18.45163  1.000 32.46964  ? 258 HIS A C   1 
ATOM   2040 O O   . HIS A 1 258 ? 32.28783 9.91771  18.66716  1.000 34.07463  ? 258 HIS A O   1 
ATOM   2041 C CB  . HIS A 1 258 ? 34.40049 12.42000 17.88329  1.000 28.86591  ? 258 HIS A CB  1 
ATOM   2042 C CG  . HIS A 1 258 ? 35.07553 11.72005 19.03117  1.000 29.53762  ? 258 HIS A CG  1 
ATOM   2043 N ND1 . HIS A 1 258 ? 34.60940 11.79617 20.33556  1.000 34.93152  ? 258 HIS A ND1 1 
ATOM   2044 C CD2 . HIS A 1 258 ? 36.21764 10.98628 19.08417  1.000 28.33723  ? 258 HIS A CD2 1 
ATOM   2045 C CE1 . HIS A 1 258 ? 35.40962 11.10381 21.13673  1.000 34.47808  ? 258 HIS A CE1 1 
ATOM   2046 N NE2 . HIS A 1 258 ? 36.39337 10.60193 20.39983  1.000 38.13773  ? 258 HIS A NE2 1 
ATOM   2047 N N   . ASP A 1 259 ? 31.50370 11.97831 19.11438  1.000 30.34305  ? 259 ASP A N   1 
ATOM   2048 C CA  . ASP A 1 259 ? 30.73607 11.51366 20.25760  1.000 38.22290  ? 259 ASP A CA  1 
ATOM   2049 C C   . ASP A 1 259 ? 29.66305 10.50564 19.84756  1.000 39.72587  ? 259 ASP A C   1 
ATOM   2050 O O   . ASP A 1 259 ? 29.43717 9.52232  20.55329  1.000 38.91054  ? 259 ASP A O   1 
ATOM   2051 C CB  . ASP A 1 259 ? 30.15357 12.72303 20.98365  1.000 38.29221  ? 259 ASP A CB  1 
ATOM   2052 C CG  . ASP A 1 259 ? 31.22526 13.50491 21.76239  1.000 39.58615  ? 259 ASP A CG  1 
ATOM   2053 O OD1 . ASP A 1 259 ? 32.36716 13.01933 21.88360  1.000 37.84081  ? 259 ASP A OD1 1 
ATOM   2054 O OD2 . ASP A 1 259 ? 30.92947 14.60437 22.24551  1.000 42.41509  ? 259 ASP A OD2 1 
ATOM   2055 N N   . SER A 1 260 ? 29.03844 10.69183 18.67496  1.000 35.60946  ? 260 SER A N   1 
ATOM   2056 C CA  . SER A 1 260 ? 27.96293 9.78319  18.26711  1.000 40.04423  ? 260 SER A CA  1 
ATOM   2057 C C   . SER A 1 260 ? 28.48501 8.47429  17.67751  1.000 36.69513  ? 260 SER A C   1 
ATOM   2058 O O   . SER A 1 260 ? 27.84260 7.43235  17.83809  1.000 40.80393  ? 260 SER A O   1 
ATOM   2059 C CB  . SER A 1 260 ? 27.02844 10.46531 17.25824  1.000 35.80268  ? 260 SER A CB  1 
ATOM   2060 O OG  . SER A 1 260 ? 26.37899 11.59672 17.82110  1.000 40.82914  ? 260 SER A OG  1 
ATOM   2061 N N   . PHE A 1 261 ? 29.63574 8.48781  17.00925  1.000 34.50818  ? 261 PHE A N   1 
ATOM   2062 C CA  . PHE A 1 261 ? 30.05929 7.30947  16.25629  1.000 35.13897  ? 261 PHE A CA  1 
ATOM   2063 C C   . PHE A 1 261 ? 31.34641 6.65329  16.75729  1.000 34.03543  ? 261 PHE A C   1 
ATOM   2064 O O   . PHE A 1 261 ? 31.51061 5.44640  16.57445  1.000 33.66418  ? 261 PHE A O   1 
ATOM   2065 C CB  . PHE A 1 261 ? 30.21320 7.66281  14.77247  1.000 30.59577  ? 261 PHE A CB  1 
ATOM   2066 C CG  . PHE A 1 261 ? 28.91862 8.09831  14.09806  1.000 31.57498  ? 261 PHE A CG  1 
ATOM   2067 C CD1 . PHE A 1 261 ? 27.92833 7.16584  13.77873  1.000 32.77304  ? 261 PHE A CD1 1 
ATOM   2068 C CD2 . PHE A 1 261 ? 28.70803 9.42531  13.76464  1.000 27.87733  ? 261 PHE A CD2 1 
ATOM   2069 C CE1 . PHE A 1 261 ? 26.74338 7.55749  13.17212  1.000 32.25607  ? 261 PHE A CE1 1 
ATOM   2070 C CE2 . PHE A 1 261 ? 27.51669 9.83298  13.13129  1.000 30.41317  ? 261 PHE A CE2 1 
ATOM   2071 C CZ  . PHE A 1 261 ? 26.53258 8.90015  12.83479  1.000 29.21655  ? 261 PHE A CZ  1 
ATOM   2072 N N   . ILE A 1 262 ? 32.26241 7.39398  17.37899  1.000 35.23611  ? 262 ILE A N   1 
ATOM   2073 C CA  . ILE A 1 262 ? 33.54679 6.80741  17.76345  1.000 37.03335  ? 262 ILE A CA  1 
ATOM   2074 C C   . ILE A 1 262 ? 33.46235 6.33289  19.21876  1.000 40.45507  ? 262 ILE A C   1 
ATOM   2075 O O   . ILE A 1 262 ? 33.73983 5.16759  19.50345  1.000 42.85113  ? 262 ILE A O   1 
ATOM   2076 C CB  . ILE A 1 262 ? 34.71430 7.79169  17.53167  1.000 31.82197  ? 262 ILE A CB  1 
ATOM   2077 C CG1 . ILE A 1 262 ? 34.70758 8.32141  16.10310  1.000 34.74525  ? 262 ILE A CG1 1 
ATOM   2078 C CG2 . ILE A 1 262 ? 36.06487 7.14963  17.87675  1.000 35.74924  ? 262 ILE A CG2 1 
ATOM   2079 C CD1 . ILE A 1 262 ? 35.10682 7.32373  14.98967  1.000 29.04713  ? 262 ILE A CD1 1 
ATOM   2080 N N   . GLU A 1 263 ? 33.09234 7.22040  20.14468  1.000 38.87980  ? 263 GLU A N   1 
ATOM   2081 C CA  . GLU A 1 263 ? 32.62920 6.82244  21.48309  1.000 51.93527  ? 263 GLU A CA  1 
ATOM   2082 C C   . GLU A 1 263 ? 32.42435 8.05026  22.35826  1.000 57.51278  ? 263 GLU A C   1 
ATOM   2083 O O   . GLU A 1 263 ? 32.98141 9.11467  22.07434  1.000 54.14467  ? 263 GLU A O   1 
ATOM   2084 C CB  . GLU A 1 263 ? 33.59686 5.85777  22.18796  1.000 61.25916  ? 263 GLU A CB  1 
ATOM   2085 C CG  . GLU A 1 263 ? 33.00813 5.06566  23.39991  0.800 72.58087  ? 263 GLU A CG  1 
ATOM   2086 C CD  . GLU A 1 263 ? 31.72554 4.27916  23.07905  0.800 70.50630  ? 263 GLU A CD  1 
ATOM   2087 O OE1 . GLU A 1 263 ? 31.52029 3.91844  21.89795  0.800 69.83198  ? 263 GLU A OE1 1 
ATOM   2088 O OE2 . GLU A 1 263 ? 30.92130 4.02062  24.00923  0.800 67.98145  ? 263 GLU A OE2 1 
ATOM   2089 N N   . ASP A 1 264 ? 31.63878 7.90927  23.42648  1.000 74.62284  ? 264 ASP A N   1 
ATOM   2090 C CA  . ASP A 1 264 ? 31.32546 9.01654  24.32938  1.000 67.30538  ? 264 ASP A CA  1 
ATOM   2091 C C   . ASP A 1 264 ? 31.20370 8.54322  25.78114  1.000 79.91229  ? 264 ASP A C   1 
ATOM   2092 O O   . ASP A 1 264 ? 32.17304 8.07521  26.38767  1.000 91.87072  ? 264 ASP A O   1 
ATOM   2093 C CB  . ASP A 1 264 ? 30.02238 9.70835  23.91082  1.000 65.01762  ? 264 ASP A CB  1 
ATOM   2094 C CG  . ASP A 1 264 ? 29.84248 11.06373 24.57966  1.000 72.93250  ? 264 ASP A CG  1 
ATOM   2095 O OD1 . ASP A 1 264 ? 30.84266 11.57211 25.13016  1.000 77.27526  ? 264 ASP A OD1 1 
ATOM   2096 O OD2 . ASP A 1 264 ? 28.71541 11.62048 24.56656  1.000 69.23211  ? 264 ASP A OD2 1 
HETATM 2097 C C1  . CIT B 2 .   ? 31.78698 23.92008 14.31324  1.000 40.05607  ? 301 CIT A C1  1 
HETATM 2098 O O1  . CIT B 2 .   ? 31.62008 22.70563 14.04716  1.000 35.58550  ? 301 CIT A O1  1 
HETATM 2099 O O2  . CIT B 2 .   ? 32.96885 24.25850 14.49313  1.000 42.85613  ? 301 CIT A O2  1 
HETATM 2100 C C2  . CIT B 2 .   ? 30.67708 24.96443 14.43749  1.000 42.71333  ? 301 CIT A C2  1 
HETATM 2101 C C3  . CIT B 2 .   ? 29.45359 24.55050 15.28546  1.000 44.08118  ? 301 CIT A C3  1 
HETATM 2102 O O7  . CIT B 2 .   ? 29.88472 23.96981 16.53907  1.000 47.26562  ? 301 CIT A O7  1 
HETATM 2103 C C4  . CIT B 2 .   ? 28.52654 25.71561 15.60150  1.000 48.72839  ? 301 CIT A C4  1 
HETATM 2104 C C5  . CIT B 2 .   ? 29.06054 26.50503 16.77853  1.000 57.93567  ? 301 CIT A C5  1 
HETATM 2105 O O3  . CIT B 2 .   ? 29.50259 27.65864 16.57352  1.000 56.50404  ? 301 CIT A O3  1 
HETATM 2106 O O4  . CIT B 2 .   ? 29.06802 26.02426 17.94750  1.000 56.70417  ? 301 CIT A O4  1 
HETATM 2107 C C6  . CIT B 2 .   ? 28.62624 23.48092 14.58810  1.000 44.11802  ? 301 CIT A C6  1 
HETATM 2108 O O5  . CIT B 2 .   ? 28.32294 23.60298 13.38899  1.000 40.58830  ? 301 CIT A O5  1 
HETATM 2109 O O6  . CIT B 2 .   ? 28.25396 22.44643 15.19562  1.000 45.82241  ? 301 CIT A O6  1 
HETATM 2110 N N1  . UQF C 3 .   ? 13.11262 3.51518  9.31850   1.000 51.05111  ? 302 UQF A N1  1 
HETATM 2111 C C7  . UQF C 3 .   ? 18.40933 11.30485 12.77343  1.000 28.10940  ? 302 UQF A C7  1 
HETATM 2112 C C8  . UQF C 3 .   ? 20.26841 12.25419 12.34299  1.000 28.67106  ? 302 UQF A C8  1 
HETATM 2113 N N2  . UQF C 3 .   ? 12.93949 5.64647  10.46904  1.000 51.29598  ? 302 UQF A N2  1 
HETATM 2114 C C9  . UQF C 3 .   ? 20.59781 11.08197 13.00440  1.000 27.13247  ? 302 UQF A C9  1 
HETATM 2115 O O1  . UQF C 3 .   ? 16.05347 7.20431  12.94411  1.000 39.83155  ? 302 UQF A O1  1 
HETATM 2116 C C1  . UQF C 3 .   ? 13.24174 6.45445  11.64997  1.000 40.36877  ? 302 UQF A C1  1 
HETATM 2117 O O5  . UQF C 3 .   ? 17.82720 10.17323 7.85921   1.000 29.67467  ? 302 UQF A O5  1 
HETATM 2118 C C5  . UQF C 3 .   ? 15.84965 10.84875 12.85543  1.000 31.91915  ? 302 UQF A C5  1 
HETATM 2119 C C6  . UQF C 3 .   ? 17.03251 11.00785 12.84598  1.000 31.11944  ? 302 UQF A C6  1 
HETATM 2120 N N3  . UQF C 3 .   ? 13.99656 9.52219  11.93394  1.000 36.24281  ? 302 UQF A N3  1 
HETATM 2121 C C4  . UQF C 3 .   ? 14.39609 10.64180 12.78442  1.000 30.59812  ? 302 UQF A C4  1 
HETATM 2122 O O4  . UQF C 3 .   ? 15.70198 8.38042  9.80305   1.000 32.24654  ? 302 UQF A O4  1 
HETATM 2123 C C3  . UQF C 3 .   ? 12.80280 8.88680  12.51231  1.000 36.52973  ? 302 UQF A C3  1 
HETATM 2124 O O3  . UQF C 3 .   ? 19.07487 9.42181  16.12570  1.000 38.38271  ? 302 UQF A O3  1 
HETATM 2125 C C2  . UQF C 3 .   ? 12.31093 7.65359  11.76749  1.000 42.04353  ? 302 UQF A C2  1 
HETATM 2126 N N4  . UQF C 3 .   ? 18.89046 12.38965 12.21821  1.000 28.06914  ? 302 UQF A N4  1 
HETATM 2127 N N   . UQF C 3 .   ? 14.89267 4.31280  10.79619  1.000 43.15436  ? 302 UQF A N   1 
HETATM 2128 C C   . UQF C 3 .   ? 13.63242 4.42556  10.15268  1.000 46.44923  ? 302 UQF A C   1 
HETATM 2129 O O   . UQF C 3 .   ? 18.76284 8.19641  12.82356  1.000 33.92889  ? 302 UQF A O   1 
HETATM 2130 C C10 . UQF C 3 .   ? 22.75271 11.43518 12.73612  1.000 25.97907  ? 302 UQF A C10 1 
HETATM 2131 C C11 . UQF C 3 .   ? 21.33105 13.03147 11.85492  1.000 26.55293  ? 302 UQF A C11 1 
HETATM 2132 C C12 . UQF C 3 .   ? 19.27067 9.10348  13.79040  1.000 32.97334  ? 302 UQF A C12 1 
HETATM 2133 C C13 . UQF C 3 .   ? 18.40267 6.99734  13.55187  1.000 36.60017  ? 302 UQF A C13 1 
HETATM 2134 C C14 . UQF C 3 .   ? 17.17947 6.34506  12.94601  1.000 36.77995  ? 302 UQF A C14 1 
HETATM 2135 C C15 . UQF C 3 .   ? 18.29380 7.40258  15.03428  1.000 34.04033  ? 302 UQF A C15 1 
HETATM 2136 C C16 . UQF C 3 .   ? 18.36655 8.92946  14.99499  1.000 33.95927  ? 302 UQF A C16 1 
HETATM 2137 C C17 . UQF C 3 .   ? 13.90035 9.83133  10.49114  1.000 31.56280  ? 302 UQF A C17 1 
HETATM 2138 C C18 . UQF C 3 .   ? 15.26456 9.75121  9.81600   1.000 31.99026  ? 302 UQF A C18 1 
HETATM 2139 C C19 . UQF C 3 .   ? 16.78916 8.28499  8.90538   1.000 31.52997  ? 302 UQF A C19 1 
HETATM 2140 C C20 . UQF C 3 .   ? 16.63163 9.40182  7.87222   1.000 27.67851  ? 302 UQF A C20 1 
HETATM 2141 C C21 . UQF C 3 .   ? 15.39058 10.17916 8.35219   1.000 28.94889  ? 302 UQF A C21 1 
HETATM 2142 C C22 . UQF C 3 .   ? 15.75698 6.29966  7.70935   1.000 31.35166  ? 302 UQF A C22 1 
HETATM 2143 C C23 . UQF C 3 .   ? 17.40623 4.96681  7.59178   1.000 31.16107  ? 302 UQF A C23 1 
HETATM 2144 C C24 . UQF C 3 .   ? 17.86279 6.09077  8.25965   1.000 29.14362  ? 302 UQF A C24 1 
HETATM 2145 C C25 . UQF C 3 .   ? 19.90467 5.29186  8.38476   1.000 27.08164  ? 302 UQF A C25 1 
HETATM 2146 C C26 . UQF C 3 .   ? 18.34700 3.95420  7.33048   1.000 28.87337  ? 302 UQF A C26 1 
HETATM 2147 N N10 . UQF C 3 .   ? 16.06689 5.10850  7.25629   1.000 32.73381  ? 302 UQF A N10 1 
HETATM 2148 N N11 . UQF C 3 .   ? 19.10515 6.31150  8.69459   1.000 27.57677  ? 302 UQF A N11 1 
HETATM 2149 N N12 . UQF C 3 .   ? 19.60883 4.15790  7.75128   1.000 25.57765  ? 302 UQF A N12 1 
HETATM 2150 N N13 . UQF C 3 .   ? 18.07685 2.82532  6.64509   1.000 27.59645  ? 302 UQF A N13 1 
HETATM 2151 N N5  . UQF C 3 .   ? 21.82771 10.62099 13.24805  1.000 25.00992  ? 302 UQF A N5  1 
HETATM 2152 N N6  . UQF C 3 .   ? 22.58750 12.57893 12.06364  1.000 24.47028  ? 302 UQF A N6  1 
HETATM 2153 N N7  . UQF C 3 .   ? 21.16366 14.17847 11.19434  1.000 25.03091  ? 302 UQF A N7  1 
HETATM 2154 N N8  . UQF C 3 .   ? 19.39932 10.45279 13.26793  1.000 29.19972  ? 302 UQF A N8  1 
HETATM 2155 N N9  . UQF C 3 .   ? 16.79475 6.95084  8.32332   1.000 31.52743  ? 302 UQF A N9  1 
HETATM 2156 O O2  . UQF C 3 .   ? 19.48698 6.99058  15.66673  1.000 37.72714  ? 302 UQF A O2  1 
HETATM 2157 O O6  . UQF C 3 .   ? 15.58881 11.58024 8.17715   1.000 24.28579  ? 302 UQF A O6  1 
HETATM 2158 C C1  . GOL D 4 .   ? 14.15970 9.03630  19.65884  0.700 40.91470  ? 303 GOL A C1  1 
HETATM 2159 O O1  . GOL D 4 .   ? 15.48618 8.56061  19.57552  0.700 41.72838  ? 303 GOL A O1  1 
HETATM 2160 C C2  . GOL D 4 .   ? 13.71929 9.67243  18.28140  0.700 39.35868  ? 303 GOL A C2  1 
HETATM 2161 O O2  . GOL D 4 .   ? 14.75743 9.71853  17.30714  0.700 36.25726  ? 303 GOL A O2  1 
HETATM 2162 C C3  . GOL D 4 .   ? 13.24514 11.10585 18.67336  0.700 34.33127  ? 303 GOL A C3  1 
HETATM 2163 O O3  . GOL D 4 .   ? 11.88963 11.10612 18.71063  0.700 38.58415  ? 303 GOL A O3  1 
HETATM 2164 O O   . HOH E 5 .   ? 16.53060 11.69770 23.47600  1.000 52.45337  ? 401 HOH A O   1 
HETATM 2165 O O   . HOH E 5 .   ? 7.980    31.607   41.855    1.000 31.49201  ? 402 HOH A O   1 
HETATM 2166 O O   . HOH E 5 .   ? 15.89381 31.02321 7.14854   1.000 46.14404  ? 403 HOH A O   1 
HETATM 2167 O O   . HOH E 5 .   ? 33.42053 20.99472 13.82668  1.000 31.20828  ? 404 HOH A O   1 
HETATM 2168 O O   . HOH E 5 .   ? 24.26446 8.10582  -8.95671  1.000 20.73081  ? 405 HOH A O   1 
HETATM 2169 O O   . HOH E 5 .   ? 20.54462 22.00928 19.63778  1.000 39.15071  ? 406 HOH A O   1 
HETATM 2170 O O   . HOH E 5 .   ? 34.11464 7.60345  27.90638  1.000 58.84358  ? 407 HOH A O   1 
HETATM 2171 O O   . HOH E 5 .   ? 31.46850 5.50155  0.00000   0.50  54.34524  ? 408 HOH A O   1 
HETATM 2172 O O   . HOH E 5 .   ? 13.68060 10.75621 4.44353   1.000 25.69111  ? 409 HOH A O   1 
HETATM 2173 O O   . HOH E 5 .   ? 27.98701 25.96233 -2.52483  1.000 32.73464  ? 410 HOH A O   1 
HETATM 2174 O O   . HOH E 5 .   ? 25.21185 3.52291  -1.84080  1.000 30.15334  ? 411 HOH A O   1 
HETATM 2175 O O   . HOH E 5 .   ? 24.57675 1.55823  -5.55319  1.000 28.12881  ? 412 HOH A O   1 
HETATM 2176 O O   . HOH E 5 .   ? 20.26109 1.90993  -19.61714 1.000 56.28018  ? 413 HOH A O   1 
HETATM 2177 O O   . HOH E 5 .   ? 20.20135 26.51713 2.69904   1.000 35.86650  ? 414 HOH A O   1 
HETATM 2178 O O   . HOH E 5 .   ? 12.17913 1.58064  -5.69099  1.000 45.11506  ? 415 HOH A O   1 
HETATM 2179 O O   . HOH E 5 .   ? 6.31979  30.78346 30.61673  1.000 48.68644  ? 416 HOH A O   1 
HETATM 2180 O O   . HOH E 5 .   ? 20.44320 7.65858  10.47085  1.000 28.87524  ? 417 HOH A O   1 
HETATM 2181 O O   . HOH E 5 .   ? 22.38103 27.42000 2.30815   1.000 41.32090  ? 418 HOH A O   1 
HETATM 2182 O O   . HOH E 5 .   ? 22.77716 11.27807 0.42990   1.000 19.53746  ? 419 HOH A O   1 
HETATM 2183 O O   . HOH E 5 .   ? 13.77253 22.25034 -6.18066  1.000 35.70773  ? 420 HOH A O   1 
HETATM 2184 O O   . HOH E 5 .   ? 22.23916 23.29309 -5.15217  1.000 28.57398  ? 421 HOH A O   1 
HETATM 2185 O O   . HOH E 5 .   ? 25.54416 9.22190  -6.52175  1.000 19.11464  ? 422 HOH A O   1 
HETATM 2186 O O   . HOH E 5 .   ? 29.24998 6.53019  4.77498   1.000 19.10974  ? 423 HOH A O   1 
HETATM 2187 O O   . HOH E 5 .   ? 11.11543 7.67818  -0.54271  1.000 31.98408  ? 424 HOH A O   1 
HETATM 2188 O O   . HOH E 5 .   ? 28.77086 2.24249  -10.99854 1.000 45.15998  ? 425 HOH A O   1 
HETATM 2189 O O   . HOH E 5 .   ? 32.23085 15.91984 24.16244  1.000 42.42936  ? 426 HOH A O   1 
HETATM 2190 O O   . HOH E 5 .   ? 15.49662 28.52880 12.05927  1.000 34.90114  ? 427 HOH A O   1 
HETATM 2191 O O   . HOH E 5 .   ? 14.28975 4.18069  5.47313   1.000 36.59578  ? 428 HOH A O   1 
HETATM 2192 O O   . HOH E 5 .   ? 26.01615 6.73354  -3.66457  1.000 23.31120  ? 429 HOH A O   1 
HETATM 2193 O O   . HOH E 5 .   ? 13.25401 18.95876 0.70587   1.000 35.83451  ? 430 HOH A O   1 
HETATM 2194 O O   . HOH E 5 .   ? 22.56178 20.93982 7.04298   1.000 26.10048  ? 431 HOH A O   1 
HETATM 2195 O O   . HOH E 5 .   ? 15.26875 28.25203 -1.75858  1.000 40.86524  ? 432 HOH A O   1 
HETATM 2196 O O   . HOH E 5 .   ? 20.59672 11.54033 4.85622   1.000 22.60481  ? 433 HOH A O   1 
HETATM 2197 O O   . HOH E 5 .   ? 4.95197  18.44673 23.03900  1.000 44.69816  ? 434 HOH A O   1 
HETATM 2198 O O   . HOH E 5 .   ? 23.50735 7.22057  11.07032  1.000 26.25396  ? 435 HOH A O   1 
HETATM 2199 O O   . HOH E 5 .   ? 7.02859  10.86894 20.11583  1.000 49.11879  ? 436 HOH A O   1 
HETATM 2200 O O   . HOH E 5 .   ? 24.19240 5.18627  10.01914  1.000 28.10865  ? 437 HOH A O   1 
HETATM 2201 O O   . HOH E 5 .   ? 21.30820 1.52055  -13.21774 1.000 34.37380  ? 438 HOH A O   1 
HETATM 2202 O O   . HOH E 5 .   ? 20.71133 26.84868 -4.67040  1.000 30.98643  ? 439 HOH A O   1 
HETATM 2203 O O   . HOH E 5 .   ? 31.88828 5.26580  -12.04081 1.000 31.47095  ? 440 HOH A O   1 
HETATM 2204 O O   . HOH E 5 .   ? 13.71053 26.92834 -0.44856  1.000 41.93348  ? 441 HOH A O   1 
HETATM 2205 O O   . HOH E 5 .   ? 8.46843  18.08019 18.16702  1.000 37.88083  ? 442 HOH A O   1 
HETATM 2206 O O   . HOH E 5 .   ? 15.11522 17.08391 20.47776  1.000 35.85154  ? 443 HOH A O   1 
HETATM 2207 O O   . HOH E 5 .   ? 26.17337 -1.56912 -8.43855  1.000 36.20141  ? 444 HOH A O   1 
HETATM 2208 O O   . HOH E 5 .   ? 4.84886  18.72931 29.23814  1.000 38.05266  ? 445 HOH A O   1 
HETATM 2209 O O   . HOH E 5 .   ? 17.74819 10.61789 18.37463  1.000 37.75650  ? 446 HOH A O   1 
HETATM 2210 O O   . HOH E 5 .   ? 2.60668  6.65464  1.87947   1.000 59.87034  ? 447 HOH A O   1 
HETATM 2211 O O   . HOH E 5 .   ? 22.843   -7.722   -13.643   1.000 36.38721  ? 448 HOH A O   1 
HETATM 2212 O O   . HOH E 5 .   ? 18.61417 19.78931 -14.35148 1.000 34.96068  ? 449 HOH A O   1 
HETATM 2213 O O   . HOH E 5 .   ? 21.16209 21.15632 1.29417   1.000 28.73081  ? 450 HOH A O   1 
HETATM 2214 O O   . HOH E 5 .   ? 3.51411  32.42712 29.43977  1.000 52.56088  ? 451 HOH A O   1 
HETATM 2215 O O   . HOH E 5 .   ? 6.889    29.365   38.009    1.000 47.54308  ? 452 HOH A O   1 
HETATM 2216 O O   . HOH E 5 .   ? 21.720   2.427    -17.339   1.000 44.41083  ? 453 HOH A O   1 
HETATM 2217 O O   . HOH E 5 .   ? 12.47259 -1.36064 -7.25280  1.000 52.22435  ? 454 HOH A O   1 
HETATM 2218 O O   . HOH E 5 .   ? 10.48342 4.00658  -12.40926 1.000 50.89814  ? 455 HOH A O   1 
HETATM 2219 O O   . HOH E 5 .   ? 30.01958 4.21588  7.96238   1.000 31.72758  ? 456 HOH A O   1 
HETATM 2220 O O   . HOH E 5 .   ? 27.54314 27.16813 9.68526   1.000 40.07240  ? 457 HOH A O   1 
HETATM 2221 O O   . HOH E 5 .   ? 29.96573 26.79919 0.96044   1.000 36.75434  ? 458 HOH A O   1 
HETATM 2222 O O   . HOH E 5 .   ? 28.82945 26.15537 11.58083  1.000 43.04872  ? 459 HOH A O   1 
HETATM 2223 O O   . HOH E 5 .   ? 16.40693 34.23462 14.20335  1.000 47.26814  ? 460 HOH A O   1 
HETATM 2224 O O   . HOH E 5 .   ? 23.55182 0.41589  -1.61003  1.000 35.65602  ? 461 HOH A O   1 
HETATM 2225 O O   . HOH E 5 .   ? 27.01872 21.34399 -14.71575 1.000 31.71019  ? 462 HOH A O   1 
HETATM 2226 O O   . HOH E 5 .   ? 10.11453 26.00470 0.38816   1.000 45.21077  ? 463 HOH A O   1 
HETATM 2227 O O   . HOH E 5 .   ? 16.01781 27.95352 -3.90580  1.000 46.30574  ? 464 HOH A O   1 
HETATM 2228 O O   . HOH E 5 .   ? 21.06834 40.47729 25.20161  1.000 70.63626  ? 465 HOH A O   1 
HETATM 2229 O O   . HOH E 5 .   ? 31.04194 29.44321 23.63865  1.000 55.29950  ? 466 HOH A O   1 
HETATM 2230 O O   . HOH E 5 .   ? 36.01558 10.29449 24.03460  1.000 40.89293  ? 467 HOH A O   1 
HETATM 2231 O O   . HOH E 5 .   ? 3.19920  21.81439 -1.05263  1.000 48.20065  ? 468 HOH A O   1 
HETATM 2232 O O   . HOH E 5 .   ? 12.13083 7.78630  7.58950   1.000 40.51744  ? 469 HOH A O   1 
HETATM 2233 O O   . HOH E 5 .   ? 13.76711 8.33678  5.42354   1.000 35.46026  ? 470 HOH A O   1 
HETATM 2234 O O   . HOH E 5 .   ? 30.96218 4.55626  4.14380   1.000 31.17997  ? 471 HOH A O   1 
HETATM 2235 O O   . HOH E 5 .   ? 15.25919 -2.73938 -14.63890 1.000 42.49897  ? 472 HOH A O   1 
HETATM 2236 O O   . HOH E 5 .   ? 0.44856  14.21104 -2.58350  1.000 49.55845  ? 473 HOH A O   1 
HETATM 2237 O O   . HOH E 5 .   ? 28.57232 29.34989 8.83300   1.000 42.94425  ? 474 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 1.14678 0.68136 0.82069 0.06993  0.12593  -0.21109 1   MET A N   
2    C CA  . MET A 1   ? 1.10078 0.60381 0.76372 0.10552  0.13089  -0.18965 1   MET A CA  
3    C C   . MET A 1   ? 1.01564 0.59096 0.71666 0.13697  0.11580  -0.17125 1   MET A C   
4    O O   . MET A 1   ? 0.94023 0.57377 0.66615 0.13405  0.10586  -0.17473 1   MET A O   
5    C CB  . MET A 1   ? 1.11723 0.59886 0.78450 0.09000  0.13226  -0.17962 1   MET A CB  
6    C CG  . MET A 1   ? 1.12891 0.56233 0.77435 0.05150  0.14429  -0.19139 1   MET A CG  
7    S SD  . MET A 1   ? 1.15712 0.61020 0.82905 0.02041  0.13887  -0.18833 1   MET A SD  
8    C CE  . MET A 1   ? 1.05763 0.61096 0.77929 -0.00113 0.11723  -0.20043 1   MET A CE  
9    N N   . LYS A 2   ? 1.01059 0.58250 0.71369 0.16614  0.11559  -0.15270 2   LYS A N   
10   C CA  . LYS A 2   ? 0.93890 0.58768 0.68461 0.18570  0.10162  -0.13744 2   LYS A CA  
11   C C   . LYS A 2   ? 0.79746 0.50098 0.58773 0.15562  0.08700  -0.13145 2   LYS A C   
12   O O   . LYS A 2   ? 0.77167 0.45380 0.56233 0.13258  0.08652  -0.13084 2   LYS A O   
13   C CB  . LYS A 2   ? 0.93105 0.56789 0.66650 0.22349  0.10472  -0.12250 2   LYS A CB  
14   C CG  . LYS A 2   ? 1.00912 0.61275 0.71075 0.24990  0.11398  -0.12093 2   LYS A CG  
15   C CD  . LYS A 2   ? 1.04273 0.66594 0.74562 0.28371  0.11038  -0.10254 2   LYS A CD  
16   C CE  . LYS A 2   ? 1.07504 0.68714 0.74926 0.31519  0.11620  -0.10016 2   LYS A CE  
17   N NZ  . LYS A 2   ? 1.20165 0.72420 0.82278 0.30945  0.13159  -0.10341 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.74845 0.51939 0.57212 0.15595  0.07719  -0.12763 3   TYR A N   
19   C CA  . TYR A 3   ? 0.67338 0.49269 0.53260 0.13311  0.06533  -0.12084 3   TYR A CA  
20   C C   . TYR A 3   ? 0.63654 0.51436 0.52475 0.14686  0.06088  -0.10989 3   TYR A C   
21   O O   . TYR A 3   ? 0.66486 0.55627 0.54900 0.16996  0.06595  -0.11123 3   TYR A O   
22   C CB  . TYR A 3   ? 0.63589 0.46748 0.49420 0.10837  0.06169  -0.13347 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.67816 0.54292 0.53725 0.11803  0.06199  -0.13766 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.71979 0.55883 0.55134 0.13052  0.07082  -0.15055 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.59007 0.50585 0.47242 0.11510  0.05579  -0.12849 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.71894 0.58883 0.55000 0.13968  0.07200  -0.15441 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.60740 0.54874 0.48589 0.12346  0.05889  -0.13143 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.64566 0.56715 0.50039 0.13560  0.06625  -0.14454 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.61041 0.55812 0.46049 0.14410  0.07005  -0.14753 3   TYR A OH  
30   N N   . MET A 4   ? 0.57787 0.49051 0.49364 0.13142  0.05308  -0.10049 4   MET A N   
31   C CA  . MET A 4   ? 0.55035 0.51435 0.49006 0.13471  0.05237  -0.09305 4   MET A CA  
32   C C   . MET A 4   ? 0.47715 0.45899 0.43016 0.11298  0.04664  -0.08700 4   MET A C   
33   O O   . MET A 4   ? 0.46940 0.43385 0.41944 0.09904  0.04101  -0.08763 4   MET A O   
34   C CB  . MET A 4   ? 0.53442 0.52082 0.49089 0.14972  0.05273  -0.08550 4   MET A CB  
35   C CG  . MET A 4   ? 0.52379 0.50738 0.49462 0.13856  0.04624  -0.07599 4   MET A CG  
36   S SD  . MET A 4   ? 0.51289 0.53518 0.51007 0.11564  0.04336  -0.06761 4   MET A SD  
37   C CE  . MET A 4   ? 0.50769 0.57936 0.51692 0.12452  0.05272  -0.07161 4   MET A CE  
38   N N   . ILE A 5   ? 0.46280 0.47895 0.42765 0.11084  0.04995  -0.08154 5   ILE A N   
39   C CA  . ILE A 5   ? 0.47465 0.50109 0.44150 0.09636  0.04796  -0.07460 5   ILE A CA  
40   C C   . ILE A 5   ? 0.47216 0.52337 0.45586 0.09164  0.05412  -0.06525 5   ILE A C   
41   O O   . ILE A 5   ? 0.48596 0.55945 0.47305 0.09555  0.06376  -0.06764 5   ILE A O   
42   C CB  . ILE A 5   ? 0.45644 0.48675 0.40396 0.09716  0.05082  -0.07969 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.47875 0.48834 0.40911 0.09808  0.04604  -0.09372 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.42083 0.45832 0.36269 0.08942  0.04978  -0.07025 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.51826 0.53687 0.42855 0.09947  0.04673  -0.10117 5   ILE A CD1 
46   N N   . THR A 6   ? 0.42534 0.47398 0.41854 0.08128  0.05023  -0.05653 6   THR A N   
47   C CA  . THR A 6   ? 0.44083 0.50635 0.44416 0.07174  0.05870  -0.04958 6   THR A CA  
48   C C   . THR A 6   ? 0.44838 0.50280 0.43193 0.06527  0.06441  -0.04207 6   THR A C   
49   O O   . THR A 6   ? 0.46710 0.50792 0.43604 0.06874  0.05668  -0.04046 6   THR A O   
50   C CB  . THR A 6   ? 0.48228 0.54990 0.50392 0.06553  0.05366  -0.04469 6   THR A CB  
51   O OG1 . THR A 6   ? 0.48857 0.53443 0.50512 0.06183  0.04407  -0.03907 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.45407 0.53226 0.48905 0.07741  0.04906  -0.05030 6   THR A CG2 
53   N N   . SER A 7   ? 0.48408 0.54548 0.46389 0.05661  0.07965  -0.03866 7   SER A N   
54   C CA  . SER A 7   ? 0.47645 0.51745 0.42823 0.05329  0.08998  -0.02913 7   SER A CA  
55   C C   . SER A 7   ? 0.50780 0.53860 0.46011 0.03778  0.10150  -0.02210 7   SER A C   
56   O O   . SER A 7   ? 0.50292 0.55452 0.47767 0.02510  0.10765  -0.02830 7   SER A O   
57   C CB  . SER A 7   ? 0.49031 0.53513 0.42324 0.05528  0.10474  -0.03168 7   SER A CB  
58   O OG  . SER A 7   ? 0.50833 0.52600 0.40670 0.05398  0.11857  -0.02051 7   SER A OG  
59   N N   . LYS A 8   ? 0.51961 0.51972 0.44436 0.04018  0.10507  -0.01040 8   LYS A N   
60   C CA  . LYS A 8   ? 0.56719 0.54433 0.48003 0.02524  0.12175  -0.00351 8   LYS A CA  
61   C C   . LYS A 8   ? 0.58521 0.56059 0.48665 0.00809  0.14778  -0.00733 8   LYS A C   
62   O O   . LYS A 8   ? 0.61175 0.57914 0.51371 -0.01359 0.16441  -0.00920 8   LYS A O   
63   C CB  . LYS A 8   ? 0.61409 0.55338 0.48963 0.03869  0.12226  0.01086  8   LYS A CB  
64   C CG  . LYS A 8   ? 0.65208 0.54812 0.49524 0.02802  0.14575  0.02044  8   LYS A CG  
65   C CD  . LYS A 8   ? 0.68814 0.54615 0.48188 0.05275  0.14811  0.03580  8   LYS A CD  
66   C CE  . LYS A 8   ? 0.79308 0.59686 0.54912 0.04645  0.17061  0.04670  8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.87222 0.68526 0.66135 0.02933  0.16411  0.04133  8   LYS A NZ  
68   N N   . GLY A 9   ? 0.58202 0.56602 0.47263 0.01467  0.15335  -0.01045 9   GLY A N   
69   C CA  . GLY A 9   ? 0.60014 0.59096 0.48496 -0.00443 0.17878  -0.01683 9   GLY A CA  
70   C C   . GLY A 9   ? 0.68806 0.62803 0.52008 -0.00922 0.20564  -0.00526 9   GLY A C   
71   O O   . GLY A 9   ? 0.76544 0.70471 0.58867 -0.03150 0.23202  -0.01110 9   GLY A O   
72   N N   . ASP A 10  ? 0.67494 0.57294 0.46880 0.01147  0.20152  0.01033  10  ASP A N   
73   C CA  . ASP A 10  ? 0.77482 0.62263 0.50864 0.01907  0.22511  0.02344  10  ASP A CA  
74   C C   . ASP A 10  ? 0.78183 0.64805 0.50499 0.04062  0.21720  0.02254  10  ASP A C   
75   O O   . ASP A 10  ? 0.72452 0.63539 0.48395 0.04999  0.19275  0.01219  10  ASP A O   
76   C CB  . ASP A 10  ? 0.81116 0.60834 0.50298 0.03841  0.22467  0.04089  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.81742 0.64139 0.52380 0.06794  0.19069  0.04273  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.76784 0.64132 0.51749 0.06864  0.16868  0.03011  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 1.00298 0.79826 0.67463 0.09077  0.18749  0.05580  10  ASP A OD2 
80   N N   . GLU A 11  ? 0.83562 0.66201 0.50342 0.04905  0.23984  0.03342  11  GLU A N   
81   C CA  . GLU A 11  ? 0.80867 0.65343 0.46350 0.06723  0.23583  0.03123  11  GLU A CA  
82   C C   . GLU A 11  ? 0.76452 0.63431 0.42551 0.09851  0.20286  0.03079  11  GLU A C   
83   O O   . GLU A 11  ? 0.70065 0.61052 0.38572 0.10462  0.18701  0.01841  11  GLU A O   
84   C CB  . GLU A 11  ? 0.93779 0.72871 0.52384 0.07349  0.26775  0.04542  11  GLU A CB  
85   C CG  . GLU A 11  ? 0.95435 0.72399 0.53354 0.03618  0.30406  0.04146  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.02127 0.74737 0.55307 0.03994  0.32189  0.05190  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.05284 0.78972 0.56555 0.06510  0.31445  0.05509  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.07755 0.75682 0.58993 0.01775  0.34386  0.05559  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.80823 0.65655 0.44621 0.11789  0.19348  0.04230  12  LYS A N   
90   C CA  . LYS A 12  ? 0.76502 0.64657 0.41096 0.14360  0.16325  0.03815  12  LYS A CA  
91   C C   . LYS A 12  ? 0.67799 0.60797 0.38649 0.12980  0.13936  0.01962  12  LYS A C   
92   O O   . LYS A 12  ? 0.65436 0.61656 0.37432 0.13830  0.12387  0.00752  12  LYS A O   
93   C CB  . LYS A 12  ? 0.82398 0.68435 0.44457 0.16332  0.15709  0.05104  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.81432 0.71168 0.42943 0.19322  0.13104  0.04706  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.86022 0.74214 0.45138 0.21426  0.12650  0.05936  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.89516 0.81872 0.46755 0.24980  0.10525  0.05587  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.85404 0.84213 0.48200 0.23714  0.07718  0.03267  12  LYS A NZ  
98   N N   . SER A 13  ? 0.71850 0.65038 0.46371 0.10841  0.13836  0.01661  13  SER A N   
99   C CA  . SER A 13  ? 0.61405 0.58201 0.40993 0.10012  0.11667  0.00228  13  SER A CA  
100  C C   . SER A 13  ? 0.59727 0.58965 0.41619 0.09180  0.11873  -0.01121 13  SER A C   
101  O O   . SER A 13  ? 0.55513 0.57029 0.39393 0.09671  0.10198  -0.02337 13  SER A O   
102  C CB  . SER A 13  ? 0.63453 0.59709 0.45729 0.08391  0.11558  0.00438  13  SER A CB  
103  O OG  . SER A 13  ? 0.64182 0.57659 0.43820 0.09266  0.11762  0.01773  13  SER A OG  
104  N N   . ASP A 14  ? 0.59701 0.58433 0.41114 0.07876  0.14096  -0.01053 14  ASP A N   
105  C CA  . ASP A 14  ? 0.60625 0.62215 0.43889 0.07504  0.14440  -0.02352 14  ASP A CA  
106  C C   . ASP A 14  ? 0.58361 0.60570 0.39584 0.09383  0.13751  -0.02822 14  ASP A C   
107  O O   . ASP A 14  ? 0.51443 0.55952 0.34637 0.09838  0.12704  -0.04162 14  ASP A O   
108  C CB  . ASP A 14  ? 0.60286 0.61724 0.42884 0.05647  0.17255  -0.02317 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.62393 0.65225 0.48227 0.03447  0.17750  -0.02770 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.54391 0.57815 0.42661 0.03709  0.15855  -0.02839 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.68086 0.71723 0.54001 0.01351  0.20078  -0.03214 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.60280 0.60271 0.37120 0.10671  0.14465  -0.01772 15  LEU A N   
113  C CA  . LEU A 15  ? 0.62614 0.63677 0.37271 0.12438  0.13959  -0.02367 15  LEU A CA  
114  C C   . LEU A 15  ? 0.58153 0.61110 0.34034 0.13527  0.11268  -0.03416 15  LEU A C   
115  O O   . LEU A 15  ? 0.58092 0.62884 0.34279 0.14106  0.10428  -0.04848 15  LEU A O   
116  C CB  . LEU A 15  ? 0.64319 0.62600 0.33389 0.13879  0.15614  -0.00904 15  LEU A CB  
117  C CG  . LEU A 15  ? 0.78140 0.75946 0.45684 0.13058  0.18165  -0.00932 15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.76159 0.73283 0.45854 0.10172  0.20205  -0.00830 15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.79503 0.74353 0.40753 0.14918  0.19875  0.00413  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.55096 0.57679 0.31715 0.13557  0.10051  -0.02938 16  LEU A N   
121  C CA  . LEU A 16  ? 0.54369 0.59156 0.32600 0.13887  0.07750  -0.04285 16  LEU A CA  
122  C C   . LEU A 16  ? 0.52260 0.57825 0.34262 0.12483  0.07127  -0.05721 16  LEU A C   
123  O O   . LEU A 16  ? 0.50863 0.57576 0.33276 0.12581  0.06069  -0.07343 16  LEU A O   
124  C CB  . LEU A 16  ? 0.55530 0.60158 0.33763 0.14213  0.06759  -0.03484 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.53541 0.60966 0.33264 0.14228  0.04591  -0.04976 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.52707 0.62815 0.30062 0.15656  0.03835  -0.06259 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.54957 0.62611 0.34895 0.14583  0.03819  -0.04077 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.50393 0.55245 0.34724 0.11295  0.07958  -0.05253 17  ARG A N   
129  C CA  . ARG A 17  ? 0.50211 0.55721 0.37353 0.10740  0.07542  -0.06444 17  ARG A CA  
130  C C   . ARG A 17  ? 0.48486 0.54792 0.34678 0.11528  0.08098  -0.07581 17  ARG A C   
131  O O   . ARG A 17  ? 0.48967 0.55131 0.35466 0.11859  0.07286  -0.08986 17  ARG A O   
132  C CB  . ARG A 17  ? 0.44692 0.50373 0.34294 0.09698  0.08331  -0.05820 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.44458 0.51279 0.36372 0.09879  0.08201  -0.06856 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.45152 0.53151 0.39560 0.08937  0.08703  -0.06360 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.40924 0.50695 0.37263 0.09735  0.08579  -0.07264 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.41378 0.53666 0.37991 0.10398  0.09590  -0.08006 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.43069 0.56081 0.38196 0.10007  0.10901  -0.07977 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.41003 0.55207 0.39141 0.11726  0.09363  -0.08777 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.50080 0.56828 0.34719 0.11769  0.09690  -0.07058 18  LEU A N   
140  C CA  . LEU A 18  ? 0.52101 0.59847 0.35686 0.12652  0.10286  -0.08143 18  LEU A CA  
141  C C   . LEU A 18  ? 0.53747 0.61334 0.35239 0.13619  0.09092  -0.09267 18  LEU A C   
142  O O   . LEU A 18  ? 0.54667 0.62398 0.36151 0.14120  0.08820  -0.10780 18  LEU A O   
143  C CB  . LEU A 18  ? 0.54268 0.62418 0.36011 0.12555  0.12402  -0.07343 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.53831 0.63369 0.37825 0.11187  0.14002  -0.07083 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.56099 0.66589 0.38255 0.10923  0.16327  -0.07034 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.51257 0.62867 0.38701 0.11437  0.13154  -0.08269 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.54558 0.62047 0.34132 0.13972  0.08375  -0.08747 19  ASN A N   
148  C CA  . ASN A 19  ? 0.56246 0.64799 0.34063 0.14700  0.07179  -0.10258 19  ASN A CA  
149  C C   . ASN A 19  ? 0.54944 0.63228 0.34724 0.13654  0.05805  -0.11942 19  ASN A C   
150  O O   . ASN A 19  ? 0.56784 0.65284 0.35624 0.13660  0.05393  -0.13862 19  ASN A O   
151  C CB  . ASN A 19  ? 0.57760 0.67336 0.32888 0.15799  0.06659  -0.09468 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.61215 0.70689 0.32680 0.17348  0.08013  -0.08563 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.62440 0.71782 0.33469 0.17427  0.09093  -0.09052 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.63328 0.72737 0.31747 0.18840  0.08083  -0.07218 19  ASN A ND2 
155  N N   . MET A 20  ? 0.52384 0.59840 0.34487 0.12617  0.05265  -0.11347 20  MET A N   
156  C CA  . MET A 20  ? 0.51953 0.58400 0.35397 0.11449  0.04350  -0.12863 20  MET A CA  
157  C C   . MET A 20  ? 0.53047 0.57318 0.36935 0.11599  0.05077  -0.13725 20  MET A C   
158  O O   . MET A 20  ? 0.61085 0.63765 0.44084 0.11122  0.04886  -0.15559 20  MET A O   
159  C CB  . MET A 20  ? 0.52118 0.58114 0.37686 0.10456  0.03738  -0.11884 20  MET A CB  
160  C CG  . MET A 20  ? 0.51442 0.59668 0.36365 0.10464  0.02768  -0.11636 20  MET A CG  
161  S SD  . MET A 20  ? 0.49343 0.57124 0.36712 0.09332  0.02092  -0.10677 20  MET A SD  
162  C CE  . MET A 20  ? 0.53030 0.59972 0.41328 0.07367  0.01449  -0.13034 20  MET A CE  
163  N N   . ILE A 21  ? 0.52019 0.56261 0.36974 0.12319  0.06059  -0.12585 21  ILE A N   
164  C CA  . ILE A 21  ? 0.53464 0.56450 0.38485 0.13238  0.06772  -0.13385 21  ILE A CA  
165  C C   . ILE A 21  ? 0.56846 0.59604 0.39350 0.13993  0.07095  -0.14968 21  ILE A C   
166  O O   . ILE A 21  ? 0.59519 0.59745 0.40899 0.14338  0.07244  -0.16444 21  ILE A O   
167  C CB  . ILE A 21  ? 0.51825 0.56654 0.38527 0.13913  0.07792  -0.12183 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.51838 0.56617 0.40989 0.13141  0.07406  -0.11068 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.57812 0.62429 0.44263 0.15510  0.08500  -0.13122 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.49698 0.57151 0.40720 0.13286  0.08403  -0.10252 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.57419 0.62340 0.38507 0.14358  0.07358  -0.14684 22  ALA A N   
172  C CA  . ALA A 22  ? 0.60693 0.65792 0.39241 0.15128  0.07618  -0.16234 22  ALA A CA  
173  C C   . ALA A 22  ? 0.62704 0.66531 0.39989 0.14085  0.06622  -0.18295 22  ALA A C   
174  O O   . ALA A 22  ? 0.65907 0.67757 0.41602 0.14255  0.06969  -0.20138 22  ALA A O   
175  C CB  . ALA A 22  ? 0.61309 0.68834 0.38114 0.15818  0.08089  -0.15356 22  ALA A CB  
176  N N   . GLY A 23  ? 0.61217 0.66170 0.39110 0.12865  0.05524  -0.18185 23  GLY A N   
177  C CA  . GLY A 23  ? 0.63152 0.67823 0.40169 0.11317  0.04711  -0.20501 23  GLY A CA  
178  C C   . GLY A 23  ? 0.67164 0.67360 0.44452 0.10167  0.05169  -0.21638 23  GLY A C   
179  O O   . GLY A 23  ? 0.69262 0.67543 0.44732 0.08977  0.05369  -0.24070 23  GLY A O   
180  N N   . PHE A 24  ? 0.63136 0.61345 0.42284 0.10504  0.05492  -0.19963 24  PHE A N   
181  C CA  . PHE A 24  ? 0.69458 0.62738 0.48113 0.10112  0.06160  -0.20656 24  PHE A CA  
182  C C   . PHE A 24  ? 0.75147 0.65399 0.51401 0.11720  0.07327  -0.21700 24  PHE A C   
183  O O   . PHE A 24  ? 0.80413 0.65668 0.54424 0.11208  0.08104  -0.23217 24  PHE A O   
184  C CB  . PHE A 24  ? 0.66005 0.58635 0.46995 0.10701  0.06164  -0.18534 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.66407 0.59716 0.49080 0.08851  0.05296  -0.18025 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.71594 0.62716 0.53268 0.06645  0.05216  -0.19776 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.60663 0.56722 0.45772 0.09126  0.04755  -0.15955 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.74959 0.67221 0.58327 0.04941  0.04489  -0.19387 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.61182 0.57880 0.47719 0.07673  0.03991  -0.15482 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.66471 0.61597 0.52295 0.05678  0.03788  -0.17150 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.73192 0.66016 0.49510 0.13672  0.07690  -0.20949 25  GLY A N   
192  C CA  . GLY A 25  ? 0.72513 0.63030 0.46569 0.15520  0.08795  -0.21956 25  GLY A CA  
193  C C   . GLY A 25  ? 0.85010 0.73062 0.55837 0.14496  0.09078  -0.24616 25  GLY A C   
194  O O   . GLY A 25  ? 0.82063 0.66371 0.50258 0.15812  0.10176  -0.25790 25  GLY A O   
195  N N   . GLU A 26  ? 0.83990 0.74285 0.54783 0.12261  0.08158  -0.25765 26  GLU A N   
196  C CA  . GLU A 26  ? 0.87258 0.75989 0.55168 0.10720  0.08394  -0.28772 26  GLU A CA  
197  C C   . GLU A 26  ? 0.94913 0.78388 0.61536 0.08256  0.08970  -0.30472 26  GLU A C   
198  O O   . GLU A 26  ? 1.10015 0.92573 0.74522 0.05976  0.09209  -0.33349 26  GLU A O   
199  C CB  . GLU A 26  ? 0.82351 0.77037 0.50604 0.09653  0.07125  -0.29598 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.77074 0.76398 0.46128 0.11905  0.06760  -0.27540 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.84505 0.83150 0.51458 0.13910  0.07786  -0.27987 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.89111 0.84017 0.53675 0.13656  0.08587  -0.30176 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 0.89602 0.91174 0.56999 0.15678  0.07994  -0.26204 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.90269 0.70320 0.57896 0.08516  0.09347  -0.28896 27  TYR A N   
205  C CA  . TYR A 27  ? 0.97827 0.71799 0.63650 0.06304  0.10311  -0.30200 27  TYR A CA  
206  C C   . TYR A 27  ? 1.02460 0.70176 0.66700 0.08833  0.11620  -0.28726 27  TYR A C   
207  O O   . TYR A 27  ? 1.00784 0.70203 0.66058 0.12107  0.11527  -0.26839 27  TYR A O   
208  C CB  . TYR A 27  ? 0.93798 0.70548 0.62374 0.03670  0.09271  -0.29813 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.90247 0.73666 0.60128 0.01459  0.07921  -0.31447 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.94627 0.77467 0.62672 -0.01914 0.08358  -0.34871 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.81866 0.72195 0.54475 0.02799  0.06349  -0.29683 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.86348 0.76515 0.55630 -0.03594 0.06980  -0.36600 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.75903 0.72501 0.49150 0.01534  0.05087  -0.31064 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.81396 0.78479 0.53190 -0.01528 0.05264  -0.34564 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.82359 0.86853 0.54835 -0.02482 0.03878  -0.36192 27  TYR A OH  
216  N N   . ASP A 28  ? 1.10752 0.71323 0.72208 0.07330  0.12977  -0.29691 28  ASP A N   
217  C CA  . ASP A 28  ? 1.19783 0.75369 0.80336 0.09875  0.13834  -0.27673 28  ASP A CA  
218  C C   . ASP A 28  ? 1.19970 0.77651 0.83242 0.10703  0.13067  -0.25432 28  ASP A C   
219  O O   . ASP A 28  ? 1.20892 0.74754 0.83705 0.09564  0.13537  -0.24845 28  ASP A O   
220  C CB  . ASP A 28  ? 1.32942 0.81545 0.90733 0.07900  0.15122  -0.28405 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.46124 0.89500 1.01835 0.11265  0.16186  -0.26363 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.41230 0.87420 0.98373 0.14955  0.15676  -0.24464 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 1.62078 0.98879 1.14540 0.10238  0.17582  -0.26634 28  ASP A OD2 
224  N N   . MET A 29  ? 1.11553 0.76639 0.78787 0.12241  0.11588  -0.23751 29  MET A N   
225  C CA  . MET A 29  ? 1.00517 0.69375 0.71512 0.12829  0.10518  -0.21358 29  MET A CA  
226  C C   . MET A 29  ? 0.97414 0.69014 0.69532 0.16609  0.10510  -0.19744 29  MET A C   
227  O O   . MET A 29  ? 0.98167 0.73203 0.70593 0.17787  0.10456  -0.20064 29  MET A O   
228  C CB  . MET A 29  ? 0.91422 0.66885 0.66053 0.10529  0.08939  -0.21055 29  MET A CB  
229  C CG  . MET A 29  ? 0.97337 0.71908 0.71406 0.06830  0.08773  -0.22885 29  MET A CG  
230  S SD  . MET A 29  ? 1.06610 0.76033 0.80151 0.04871  0.09426  -0.22631 29  MET A SD  
231  C CE  . MET A 29  ? 0.94640 0.70161 0.73045 0.05258  0.07730  -0.19948 29  MET A CE  
232  N N   . GLU A 30  ? 0.93810 0.64290 0.66452 0.18472  0.10630  -0.18181 30  GLU A N   
233  C CA  . GLU A 30  ? 0.91149 0.65209 0.65125 0.22020  0.10610  -0.16907 30  GLU A CA  
234  C C   . GLU A 30  ? 0.81866 0.61491 0.60274 0.21393  0.09449  -0.15178 30  GLU A C   
235  O O   . GLU A 30  ? 0.81925 0.59567 0.60784 0.20349  0.09144  -0.14443 30  GLU A O   
236  C CB  . GLU A 30  ? 0.96464 0.65318 0.67228 0.24967  0.11647  -0.16512 30  GLU A CB  
237  C CG  . GLU A 30  ? 0.97763 0.71678 0.70768 0.28104  0.11204  -0.14936 30  GLU A CG  
238  C CD  . GLU A 30  ? 1.10837 0.80474 0.81257 0.30302  0.11652  -0.13807 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.15390 0.77508 0.82137 0.29243  0.12548  -0.14141 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 1.19546 0.93624 0.91426 0.32969  0.11155  -0.12644 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.74839 0.61094 0.56239 0.21768  0.09001  -0.14644 31  TYR A N   
242  C CA  . TYR A 31  ? 0.69994 0.61317 0.55235 0.21119  0.08240  -0.13226 31  TYR A CA  
243  C C   . TYR A 31  ? 0.69328 0.61417 0.54891 0.24010  0.08408  -0.12516 31  TYR A C   
244  O O   . TYR A 31  ? 0.67553 0.61996 0.52676 0.26876  0.08962  -0.12861 31  TYR A O   
245  C CB  . TYR A 31  ? 0.61205 0.58547 0.48752 0.20506  0.08248  -0.13068 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.61885 0.63479 0.52842 0.18993  0.07762  -0.11833 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.58262 0.63579 0.51381 0.20252  0.07844  -0.11304 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.58802 0.60769 0.50539 0.16429  0.07280  -0.11330 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.49042 0.57827 0.45015 0.18445  0.07583  -0.10440 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.53906 0.58680 0.48076 0.15075  0.07078  -0.10226 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.49472 0.57407 0.45758 0.15831  0.07299  -0.09849 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.46491 0.56791 0.44888 0.14059  0.07287  -0.08995 31  TYR A OH  
253  N N   . ASP A 32  ? 0.67131 0.57702 0.53340 0.23519  0.07922  -0.11602 32  ASP A N   
254  C CA  . ASP A 32  ? 0.67482 0.59558 0.54045 0.26407  0.07895  -0.10863 32  ASP A CA  
255  C C   . ASP A 32  ? 0.64441 0.59195 0.54157 0.24399  0.06989  -0.09810 32  ASP A C   
256  O O   . ASP A 32  ? 0.65673 0.56378 0.54744 0.22467  0.06704  -0.09412 32  ASP A O   
257  C CB  . ASP A 32  ? 0.79725 0.64521 0.61723 0.28939  0.08657  -0.10855 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.82188 0.68895 0.64571 0.31251  0.08184  -0.09489 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.75923 0.68277 0.61723 0.31102  0.07397  -0.08959 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.89394 0.71749 0.68203 0.33243  0.08653  -0.08988 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.60470 0.62128 0.53505 0.24679  0.06672  -0.09544 33  ASP A N   
262  C CA  . ASP A 33  ? 0.60545 0.64619 0.56318 0.22870  0.05946  -0.08694 33  ASP A CA  
263  C C   . ASP A 33  ? 0.60392 0.65509 0.56081 0.25545  0.05652  -0.08218 33  ASP A C   
264  O O   . ASP A 33  ? 0.60569 0.69171 0.58842 0.24423  0.05078  -0.07752 33  ASP A O   
265  C CB  . ASP A 33  ? 0.54143 0.64502 0.53321 0.20698  0.06007  -0.08824 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.54868 0.71854 0.55623 0.22585  0.06499  -0.09612 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.55556 0.73354 0.55214 0.26090  0.06468  -0.09890 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.48107 0.69620 0.50974 0.20613  0.07061  -0.10012 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.64266 0.66374 0.56685 0.29277  0.06105  -0.08335 34  VAL A N   
270  C CA  . VAL A 34  ? 0.67326 0.69335 0.58804 0.31230  0.05609  -0.07369 34  VAL A CA  
271  C C   . VAL A 34  ? 0.72692 0.66231 0.60727 0.31013  0.05901  -0.06537 34  VAL A C   
272  O O   . VAL A 34  ? 0.74067 0.67418 0.62590 0.30797  0.05428  -0.05705 34  VAL A O   
273  C CB  . VAL A 34  ? 0.66923 0.71050 0.56639 0.34267  0.05612  -0.07360 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.67976 0.70988 0.55534 0.36484  0.05140  -0.06261 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.61555 0.74942 0.55031 0.34010  0.05305  -0.08261 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.77193 0.63656 0.61608 0.30732  0.06816  -0.06875 35  GLU A N   
277  C CA  . GLU A 35  ? 0.82528 0.60630 0.63470 0.29627  0.07482  -0.06407 35  GLU A CA  
278  C C   . GLU A 35  ? 0.81355 0.54928 0.61338 0.26709  0.08143  -0.07640 35  GLU A C   
279  O O   . GLU A 35  ? 0.89494 0.56645 0.65726 0.26098  0.09197  -0.08156 35  GLU A O   
280  C CB  . GLU A 35  ? 0.89776 0.62875 0.65976 0.32061  0.08266  -0.05692 35  GLU A CB  
281  C CG  . GLU A 35  ? 0.92368 0.69221 0.68483 0.34975  0.07578  -0.04475 35  GLU A CG  
282  C CD  . GLU A 35  ? 0.99945 0.71498 0.70476 0.37828  0.08474  -0.03656 35  GLU A CD  
283  O OE1 . GLU A 35  ? 0.98710 0.66409 0.66426 0.38368  0.09401  -0.04195 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.06371 0.77483 0.74997 0.39609  0.08325  -0.02474 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.75533 0.53807 0.59622 0.23260  0.07145  -0.07783 36  PRO A N   
286  C CA  . PRO A 36  ? 0.77720 0.53447 0.61500 0.19626  0.07274  -0.08725 36  PRO A CA  
287  C C   . PRO A 36  ? 0.75976 0.45692 0.57625 0.17539  0.07814  -0.08711 36  PRO A C   
288  O O   . PRO A 36  ? 0.81876 0.50172 0.63213 0.18232  0.07814  -0.07639 36  PRO A O   
289  C CB  . PRO A 36  ? 0.69160 0.51682 0.57502 0.17308  0.06067  -0.08472 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.65976 0.52767 0.56827 0.18587  0.05451  -0.07341 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.68150 0.54393 0.56997 0.22567  0.06002  -0.07256 36  PRO A CD  
292  N N   . GLU A 37  ? 0.77900 0.44264 0.57915 0.14851  0.08403  -0.10108 37  GLU A N   
293  C CA  . GLU A 37  ? 0.77602 0.40065 0.56560 0.11689  0.08885  -0.10558 37  GLU A CA  
294  C C   . GLU A 37  ? 0.70837 0.38657 0.53486 0.08309  0.07640  -0.11081 37  GLU A C   
295  O O   . GLU A 37  ? 0.69728 0.36766 0.52818 0.05779  0.07640  -0.11248 37  GLU A O   
296  C CB  . GLU A 37  ? 0.87605 0.42154 0.61528 0.10657  0.10785  -0.12210 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.95161 0.43818 0.64585 0.14426  0.12180  -0.11618 37  GLU A CG  
298  C CD  . GLU A 37  ? 1.06010 0.48217 0.71336 0.12530  0.13813  -0.12702 37  GLU A CD  
299  O OE1 . GLU A 37  ? 1.10980 0.49413 0.74910 0.09532  0.14727  -0.12960 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 1.02107 0.43230 0.65615 0.13932  0.14279  -0.13335 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.70191 0.43404 0.55149 0.08466  0.06702  -0.11322 38  ILE A N   
302  C CA  . ILE A 38  ? 0.59925 0.38375 0.47804 0.06231  0.05529  -0.11549 38  ILE A CA  
303  C C   . ILE A 38  ? 0.55338 0.39199 0.46176 0.07753  0.04605  -0.10126 38  ILE A C   
304  O O   . ILE A 38  ? 0.58758 0.43899 0.49460 0.09696  0.04838  -0.10026 38  ILE A O   
305  C CB  . ILE A 38  ? 0.61367 0.40338 0.48093 0.04652  0.05646  -0.13518 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.72861 0.46176 0.56434 0.02525  0.06921  -0.15322 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.59808 0.44421 0.49007 0.03039  0.04403  -0.13658 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.76321 0.49470 0.60772 -0.00169 0.06861  -0.15469 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.51902 0.38749 0.45187 0.06762  0.03768  -0.09146 39  VAL A N   
310  C CA  . VAL A 39  ? 0.48269 0.39544 0.43990 0.07516  0.03206  -0.07941 39  VAL A CA  
311  C C   . VAL A 39  ? 0.46665 0.40841 0.43281 0.06007  0.02540  -0.08005 39  VAL A C   
312  O O   . VAL A 39  ? 0.45192 0.39462 0.42243 0.04576  0.02065  -0.08075 39  VAL A O   
313  C CB  . VAL A 39  ? 0.46362 0.38070 0.43589 0.08101  0.02992  -0.06656 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.45305 0.41179 0.44836 0.07906  0.02611  -0.05750 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.51583 0.41597 0.47695 0.10525  0.03573  -0.06510 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.44146 0.40652 0.40633 0.06542  0.02609  -0.08054 40  ILE A N   
317  C CA  . ILE A 40  ? 0.45325 0.44416 0.41831 0.05965  0.02130  -0.07888 40  ILE A CA  
318  C C   . ILE A 40  ? 0.42326 0.43117 0.39898 0.06479  0.02400  -0.06387 40  ILE A C   
319  O O   . ILE A 40  ? 0.43626 0.44962 0.41462 0.07231  0.03128  -0.06137 40  ILE A O   
320  C CB  . ILE A 40  ? 0.50007 0.49920 0.44747 0.06300  0.02270  -0.09015 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.49920 0.47766 0.43318 0.05386  0.02298  -0.10888 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.42115 0.44853 0.36240 0.06444  0.01807  -0.08607 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.51935 0.50634 0.43547 0.05727  0.02460  -0.12202 40  ILE A CD1 
324  N N   . SER A 41  ? 0.39613 0.41312 0.37548 0.06006  0.01987  -0.05577 41  SER A N   
325  C CA  . SER A 41  ? 0.38652 0.40946 0.37037 0.06120  0.02513  -0.04251 41  SER A CA  
326  C C   . SER A 41  ? 0.42796 0.45756 0.39144 0.06667  0.02679  -0.03767 41  SER A C   
327  O O   . SER A 41  ? 0.42069 0.45909 0.37662 0.06856  0.01837  -0.04049 41  SER A O   
328  C CB  . SER A 41  ? 0.40264 0.42167 0.40152 0.05469  0.02060  -0.03576 41  SER A CB  
329  O OG  . SER A 41  ? 0.42202 0.44224 0.41924 0.05359  0.02606  -0.02468 41  SER A OG  
330  N N   . ILE A 42  ? 0.43154 0.45879 0.38320 0.07027  0.03869  -0.03125 42  ILE A N   
331  C CA  . ILE A 42  ? 0.44992 0.47526 0.37212 0.08035  0.04325  -0.02494 42  ILE A CA  
332  C C   . ILE A 42  ? 0.48888 0.49557 0.39957 0.07816  0.05639  -0.01053 42  ILE A C   
333  O O   . ILE A 42  ? 0.49618 0.49689 0.41219 0.06819  0.07006  -0.00902 42  ILE A O   
334  C CB  . ILE A 42  ? 0.45295 0.48264 0.35863 0.08713  0.04976  -0.03071 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.42108 0.46305 0.33369 0.08760  0.03866  -0.04728 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.51677 0.54076 0.38429 0.10188  0.05613  -0.02168 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.42082 0.46783 0.31495 0.09568  0.04467  -0.05434 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.48483 0.48349 0.37801 0.08704  0.05364  -0.00170 43  GLY A N   
339  C CA  . GLY A 43  ? 0.53646 0.50820 0.41642 0.08367  0.06680  0.01108  43  GLY A CA  
340  C C   . GLY A 43  ? 0.54574 0.51764 0.42411 0.09173  0.05636  0.01643  43  GLY A C   
341  O O   . GLY A 43  ? 0.60754 0.59462 0.47101 0.10920  0.04617  0.01599  43  GLY A O   
342  N N   . GLY A 44  ? 0.53287 0.49407 0.42666 0.08004  0.05845  0.01992  44  GLY A N   
343  C CA  . GLY A 44  ? 0.49795 0.46014 0.38983 0.08845  0.04951  0.02494  44  GLY A CA  
344  C C   . GLY A 44  ? 0.44916 0.42761 0.38079 0.07303  0.03842  0.01789  44  GLY A C   
345  O O   . GLY A 44  ? 0.41973 0.41092 0.37535 0.06224  0.03490  0.00872  44  GLY A O   
346  N N   . ASP A 45  ? 0.44599 0.42095 0.38034 0.07454  0.03439  0.02294  45  ASP A N   
347  C CA  . ASP A 45  ? 0.42447 0.41141 0.39176 0.06142  0.02528  0.01796  45  ASP A CA  
348  C C   . ASP A 45  ? 0.38327 0.36138 0.36700 0.04532  0.03383  0.01653  45  ASP A C   
349  O O   . ASP A 45  ? 0.39260 0.38435 0.40246 0.03750  0.02666  0.01020  45  ASP A O   
350  C CB  . ASP A 45  ? 0.44429 0.43037 0.40749 0.06814  0.02065  0.02403  45  ASP A CB  
351  C CG  . ASP A 45  ? 0.43350 0.44763 0.39025 0.08285  0.00874  0.02042  45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.45563 0.49328 0.42437 0.07846  0.00073  0.00907  45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.42922 0.44423 0.36774 0.09899  0.00807  0.02719  45  ASP A OD2 
354  N N   . GLY A 46  ? 0.41070 0.36657 0.37682 0.04035  0.05040  0.02147  46  GLY A N   
355  C CA  . GLY A 46  ? 0.38529 0.34593 0.36896 0.02262  0.05934  0.01546  46  GLY A CA  
356  C C   . GLY A 46  ? 0.41400 0.39867 0.41484 0.02091  0.05696  0.00612  46  GLY A C   
357  O O   . GLY A 46  ? 0.36776 0.37409 0.39419 0.01502  0.05287  -0.00118 46  GLY A O   
358  N N   . THR A 47  ? 0.41281 0.39508 0.39697 0.02980  0.05903  0.00616  47  THR A N   
359  C CA  . THR A 47  ? 0.38967 0.39232 0.38679 0.03136  0.05637  -0.00305 47  THR A CA  
360  C C   . THR A 47  ? 0.35088 0.36565 0.36743 0.03672  0.03984  -0.00844 47  THR A C   
361  O O   . THR A 47  ? 0.36073 0.38913 0.39368 0.03719  0.03786  -0.01533 47  THR A O   
362  C CB  . THR A 47  ? 0.43829 0.43437 0.41023 0.04074  0.06147  -0.00216 47  THR A CB  
363  O OG1 . THR A 47  ? 0.49275 0.46591 0.43713 0.03682  0.08020  0.00524  47  THR A OG1 
364  C CG2 . THR A 47  ? 0.39550 0.41032 0.37813 0.04238  0.06131  -0.01223 47  THR A CG2 
365  N N   . PHE A 48  ? 0.33917 0.34872 0.35095 0.04146  0.02960  -0.00605 48  PHE A N   
366  C CA  . PHE A 48  ? 0.34288 0.35659 0.36842 0.04140  0.01822  -0.01218 48  PHE A CA  
367  C C   . PHE A 48  ? 0.37419 0.38860 0.41820 0.03696  0.01643  -0.01080 48  PHE A C   
368  O O   . PHE A 48  ? 0.37145 0.38540 0.42303 0.04009  0.01379  -0.01577 48  PHE A O   
369  C CB  . PHE A 48  ? 0.37056 0.38703 0.38931 0.04289  0.00952  -0.01272 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.40707 0.42348 0.43387 0.03734  0.00238  -0.02243 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.37818 0.38760 0.41709 0.03120  -0.00053 -0.02080 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.37975 0.39843 0.39805 0.03685  0.00102  -0.03398 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.38181 0.38060 0.42096 0.02389  -0.00237 -0.02943 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.43742 0.44638 0.45723 0.02738  -0.00101 -0.04477 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.40522 0.40112 0.43391 0.02048  -0.00153 -0.04189 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.36291 0.37613 0.41006 0.03192  0.01897  -0.00418 49  LEU A N   
377  C CA  . LEU A 49  ? 0.34748 0.36693 0.41135 0.02857  0.01705  -0.00408 49  LEU A CA  
378  C C   . LEU A 49  ? 0.34618 0.38410 0.42072 0.03060  0.02156  -0.01060 49  LEU A C   
379  O O   . LEU A 49  ? 0.30229 0.34897 0.38714 0.03698  0.01687  -0.01290 49  LEU A O   
380  C CB  . LEU A 49  ? 0.32176 0.33672 0.38431 0.02117  0.02121  0.00179  49  LEU A CB  
381  C CG  . LEU A 49  ? 0.35017 0.35494 0.40712 0.02341  0.01432  0.00777  49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.39893 0.39282 0.44799 0.01890  0.02105  0.01360  49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.36588 0.37460 0.43668 0.02369  0.00550  0.00614  49  LEU A CD2 
384  N N   . SER A 50  ? 0.34460 0.39108 0.41462 0.02707  0.03159  -0.01387 50  SER A N   
385  C CA  . SER A 50  ? 0.35846 0.43361 0.44065 0.02983  0.03606  -0.02266 50  SER A CA  
386  C C   . SER A 50  ? 0.35071 0.42495 0.43156 0.04687  0.02937  -0.02636 50  SER A C   
387  O O   . SER A 50  ? 0.35330 0.44755 0.44337 0.05843  0.02725  -0.03113 50  SER A O   
388  C CB  . SER A 50  ? 0.36845 0.45232 0.44397 0.02019  0.05070  -0.02652 50  SER A CB  
389  O OG  . SER A 50  ? 0.46536 0.55124 0.54170 0.00222  0.06144  -0.02692 50  SER A OG  
390  N N   . ALA A 51  ? 0.38993 0.44086 0.45584 0.05006  0.02687  -0.02524 51  ALA A N   
391  C CA  . ALA A 51  ? 0.38191 0.42223 0.43994 0.06338  0.02399  -0.03058 51  ALA A CA  
392  C C   . ALA A 51  ? 0.36360 0.38588 0.42045 0.07034  0.01782  -0.02865 51  ALA A C   
393  O O   . ALA A 51  ? 0.38639 0.40200 0.43625 0.08649  0.01858  -0.03188 51  ALA A O   
394  C CB  . ALA A 51  ? 0.36293 0.38530 0.40464 0.06062  0.02338  -0.03292 51  ALA A CB  
395  N N   . PHE A 52  ? 0.35886 0.36959 0.41784 0.06033  0.01321  -0.02299 52  PHE A N   
396  C CA  . PHE A 52  ? 0.41738 0.40993 0.47361 0.06500  0.00973  -0.01997 52  PHE A CA  
397  C C   . PHE A 52  ? 0.38070 0.39301 0.44458 0.07991  0.00975  -0.01899 52  PHE A C   
398  O O   . PHE A 52  ? 0.39874 0.39460 0.44953 0.09746  0.01040  -0.01889 52  PHE A O   
399  C CB  . PHE A 52  ? 0.40298 0.39106 0.46438 0.05124  0.00550  -0.01431 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.38134 0.35344 0.44033 0.05435  0.00352  -0.01004 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.43041 0.36761 0.47170 0.05419  0.00625  -0.01224 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.36415 0.35299 0.43504 0.05559  0.00094  -0.00476 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.42198 0.33785 0.45527 0.05678  0.00739  -0.00698 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.39326 0.36738 0.45906 0.06025  -0.00051 0.00001  52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.41638 0.35239 0.46231 0.06154  0.00314  -0.00001 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.37777 0.42600 0.45930 0.07413  0.01054  -0.01968 53  HIS A N   
407  C CA  . HIS A 53  ? 0.39144 0.47231 0.48362 0.08648  0.00926  -0.02222 53  HIS A CA  
408  C C   . HIS A 53  ? 0.43230 0.53777 0.52308 0.10623  0.01228  -0.02996 53  HIS A C   
409  O O   . HIS A 53  ? 0.43426 0.55660 0.52272 0.12904  0.00959  -0.03129 53  HIS A O   
410  C CB  . HIS A 53  ? 0.32261 0.43521 0.43327 0.06875  0.01116  -0.02444 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.38081 0.47366 0.49131 0.05828  0.00703  -0.01679 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.40033 0.49160 0.51015 0.06874  0.00101  -0.01310 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.35867 0.43106 0.46585 0.04209  0.00832  -0.01154 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.37293 0.44621 0.48246 0.05622  -0.00103 -0.00685 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.37802 0.44075 0.48605 0.04124  0.00298  -0.00597 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.40525 0.51440 0.49460 0.10141  0.01795  -0.03492 54  GLN A N   
417  C CA  . GLN A 54  ? 0.41910 0.54933 0.50453 0.12270  0.02120  -0.04250 54  GLN A CA  
418  C C   . GLN A 54  ? 0.44306 0.53507 0.50300 0.14977  0.01916  -0.03916 54  GLN A C   
419  O O   . GLN A 54  ? 0.48835 0.60068 0.54202 0.17815  0.01988  -0.04313 54  GLN A O   
420  C CB  . GLN A 54  ? 0.42284 0.55207 0.50500 0.11336  0.02823  -0.04711 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.40049 0.56957 0.49991 0.09357  0.03632  -0.05284 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.48680 0.64434 0.57577 0.08541  0.04420  -0.05442 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.52262 0.66815 0.60819 0.06514  0.04990  -0.05053 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.44501 0.60262 0.52405 0.10393  0.04540  -0.05958 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.48513 0.52134 0.52681 0.14202  0.01847  -0.03298 55  TYR A N   
426  C CA  . TYR A 55  ? 0.52515 0.51034 0.53430 0.16204  0.02201  -0.03134 55  TYR A CA  
427  C C   . TYR A 55  ? 0.52927 0.47689 0.52445 0.16229  0.02090  -0.02274 55  TYR A C   
428  O O   . TYR A 55  ? 0.56576 0.45480 0.52990 0.16552  0.02744  -0.02135 55  TYR A O   
429  C CB  . TYR A 55  ? 0.52977 0.47705 0.52217 0.15056  0.02704  -0.03660 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.55940 0.53618 0.55725 0.15686  0.03002  -0.04457 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.56334 0.53640 0.54267 0.18665  0.03516  -0.04908 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.48961 0.49612 0.50711 0.13566  0.02919  -0.04694 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.58846 0.59308 0.57398 0.19198  0.03857  -0.05711 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.53034 0.56268 0.55084 0.13989  0.03389  -0.05378 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.56256 0.59709 0.56971 0.16645  0.03816  -0.05947 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.58175 0.64585 0.59320 0.16907  0.04353  -0.06689 55  TYR A OH  
437  N N   . GLU A 56  ? 0.52894 0.50764 0.54365 0.15838  0.01474  -0.01807 56  GLU A N   
438  C CA  . GLU A 56  ? 0.60455 0.55044 0.60706 0.15678  0.01399  -0.00941 56  GLU A CA  
439  C C   . GLU A 56  ? 0.62021 0.52729 0.58574 0.19003  0.01969  -0.00410 56  GLU A C   
440  O O   . GLU A 56  ? 0.65357 0.51271 0.59656 0.18782  0.02420  0.00317  56  GLU A O   
441  C CB  . GLU A 56  ? 0.53658 0.52690 0.56655 0.14762  0.00636  -0.00676 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.59928 0.64965 0.64401 0.16801  0.00261  -0.01184 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.73199 0.82807 0.80451 0.15207  -0.00301 -0.01368 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.52996 0.61418 0.61312 0.12420  -0.00340 -0.01104 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.91548 1.06205 0.99737 0.16905  -0.00659 -0.01923 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.63315 0.55739 0.58778 0.22244  0.02126  -0.00729 57  GLU A N   
447  C CA  . GLU A 57  ? 0.69944 0.57889 0.60926 0.26082  0.02853  -0.00070 57  GLU A CA  
448  C C   . GLU A 57  ? 0.68979 0.49188 0.55820 0.25908  0.04205  -0.00163 57  GLU A C   
449  O O   . GLU A 57  ? 0.69991 0.46033 0.52693 0.27531  0.04981  0.00484  57  GLU A O   
450  C CB  . GLU A 57  ? 0.70960 0.65175 0.62410 0.28711  0.02258  -0.00371 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.72573 0.72606 0.66107 0.29039  0.01241  -0.00205 57  GLU A CG  
452  C CD  . GLU A 57  ? 0.74967 0.84181 0.72941 0.28437  0.00426  -0.01498 57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.77676 0.90575 0.75288 0.30105  0.00378  -0.02189 57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.74017 0.86687 0.75630 0.26109  -0.00027 -0.01897 57  GLU A OE2 
455  N N   . ARG A 58  ? 0.70775 0.49568 0.58609 0.23028  0.04463  -0.00996 58  ARG A N   
456  C CA  . ARG A 58  ? 0.76451 0.47861 0.60348 0.22490  0.05880  -0.01510 58  ARG A CA  
457  C C   . ARG A 58  ? 0.75990 0.45446 0.61008 0.17802  0.06012  -0.02085 58  ARG A C   
458  O O   . ARG A 58  ? 0.77086 0.44262 0.61238 0.15985  0.06593  -0.03195 58  ARG A O   
459  C CB  . ARG A 58  ? 0.72711 0.45476 0.56214 0.24130  0.06085  -0.02430 58  ARG A CB  
460  C CG  . ARG A 58  ? 0.81178 0.53640 0.61648 0.27727  0.06397  -0.01813 58  ARG A CG  
461  C CD  . ARG A 58  ? 0.79972 0.53551 0.59613 0.29333  0.06680  -0.02624 58  ARG A CD  
462  N NE  . ARG A 58  ? 0.87249 0.53755 0.63548 0.27923  0.08007  -0.03343 58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.87288 0.53538 0.64960 0.25638  0.08150  -0.04673 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.77454 0.50049 0.59743 0.24157  0.07026  -0.05085 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.90562 0.50771 0.64973 0.24241  0.09374  -0.05578 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.72667 0.43431 0.59528 0.15967  0.05464  -0.01460 59  LEU A N   
467  C CA  . LEU A 59  ? 0.70714 0.41007 0.58960 0.11852  0.05440  -0.02047 59  LEU A CA  
468  C C   . LEU A 59  ? 0.76275 0.39320 0.60563 0.10113  0.07147  -0.02926 59  LEU A C   
469  O O   . LEU A 59  ? 0.79527 0.43120 0.64773 0.06962  0.07203  -0.04222 59  LEU A O   
470  C CB  . LEU A 59  ? 0.66285 0.38346 0.56292 0.10861  0.04840  -0.01132 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.65112 0.44426 0.59338 0.11260  0.03302  -0.00756 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.55657 0.36278 0.51327 0.10192  0.02798  0.00025  59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.55707 0.38574 0.52433 0.09344  0.02732  -0.01663 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.79649 0.35840 0.59179 0.12034  0.08691  -0.02350 60  ASP A N   
475  C CA  . ASP A 60  ? 0.91384 0.39749 0.66647 0.09707  0.10784  -0.03322 60  ASP A CA  
476  C C   . ASP A 60  ? 0.92066 0.38234 0.65394 0.09525  0.11536  -0.04697 60  ASP A C   
477  O O   . ASP A 60  ? 0.98421 0.41013 0.69869 0.06254  0.12827  -0.06048 60  ASP A O   
478  C CB  . ASP A 60  ? 0.98436 0.42625 0.69890 0.10992  0.11917  -0.01896 60  ASP A CB  
479  C CG  . ASP A 60  ? 1.05083 0.45715 0.75182 0.07052  0.13294  -0.02340 60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.00808 0.44459 0.74126 0.04755  0.12560  -0.02573 60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.22259 0.57284 0.87986 0.06214  0.15233  -0.02504 60  ASP A OD2 
482  N N   . GLU A 61  ? 0.90269 0.39116 0.64177 0.12771  0.10786  -0.04534 61  GLU A N   
483  C CA  . GLU A 61  ? 0.89760 0.36863 0.61865 0.12957  0.11427  -0.05775 61  GLU A CA  
484  C C   . GLU A 61  ? 0.83095 0.35873 0.59094 0.10838  0.10231  -0.07181 61  GLU A C   
485  O O   . GLU A 61  ? 0.87266 0.38941 0.61918 0.10956  0.10701  -0.08405 61  GLU A O   
486  C CB  . GLU A 61  ? 0.91094 0.39359 0.61830 0.17537  0.11194  -0.04719 61  GLU A CB  
487  C CG  . GLU A 61  ? 0.97783 0.41039 0.63751 0.19565  0.12420  -0.03385 61  GLU A CG  
488  C CD  . GLU A 61  ? 1.01318 0.46398 0.67746 0.21186  0.11821  -0.01705 61  GLU A CD  
489  O OE1 . GLU A 61  ? 0.97404 0.49133 0.67327 0.23306  0.10201  -0.01185 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 1.06426 0.46551 0.69665 0.20181  0.13067  -0.01027 61  GLU A OE2 
491  N N   . ILE A 62  ? 0.79995 0.39373 0.60758 0.08886  0.08622  -0.06879 62  ILE A N   
492  C CA  . ILE A 62  ? 0.72985 0.39152 0.57654 0.07664  0.07196  -0.07533 62  ILE A CA  
493  C C   . ILE A 62  ? 0.70657 0.39104 0.57300 0.03799  0.06738  -0.08444 62  ILE A C   
494  O O   . ILE A 62  ? 0.64859 0.33244 0.52276 0.02550  0.06659  -0.07851 62  ILE A O   
495  C CB  . ILE A 62  ? 0.67453 0.40009 0.55729 0.09725  0.05749  -0.06169 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.68911 0.41535 0.55913 0.13495  0.06023  -0.05808 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.59278 0.37952 0.51196 0.07961  0.04531  -0.06475 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.67122 0.46692 0.57780 0.14859  0.04851  -0.05008 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.64712 0.35685 0.52099 0.02144  0.06407  -0.09946 63  ALA A N   
500  C CA  . ALA A 63  ? 0.59101 0.34975 0.49110 -0.00542 0.05435  -0.10725 63  ALA A CA  
501  C C   . ALA A 63  ? 0.54858 0.36933 0.47751 0.00685  0.03972  -0.10031 63  ALA A C   
502  O O   . ALA A 63  ? 0.59643 0.42284 0.52033 0.02141  0.03989  -0.10233 63  ALA A O   
503  C CB  . ALA A 63  ? 0.60732 0.35391 0.49058 -0.03445 0.06214  -0.13228 63  ALA A CB  
504  N N   . PHE A 64  ? 0.52120 0.38395 0.47576 0.00077  0.02933  -0.09268 64  PHE A N   
505  C CA  . PHE A 64  ? 0.48429 0.39445 0.45921 0.01177  0.01912  -0.08351 64  PHE A CA  
506  C C   . PHE A 64  ? 0.49523 0.44403 0.47403 0.00028  0.01240  -0.09436 64  PHE A C   
507  O O   . PHE A 64  ? 0.50045 0.45775 0.47894 -0.01911 0.01170  -0.10681 64  PHE A O   
508  C CB  . PHE A 64  ? 0.44507 0.37085 0.43940 0.01686  0.01376  -0.06677 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.46568 0.37286 0.46033 0.03348  0.01733  -0.05563 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.48598 0.35735 0.46937 0.03390  0.02271  -0.05321 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.46887 0.39863 0.47395 0.04865  0.01607  -0.04819 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.50334 0.36551 0.48490 0.05455  0.02452  -0.04324 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.46209 0.38914 0.47002 0.06481  0.01813  -0.04125 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.47165 0.36701 0.46761 0.07030  0.02110  -0.03842 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.45901 0.43473 0.43990 0.01333  0.00830  -0.09001 65  ILE A N   
516  C CA  . ILE A 65  ? 0.43671 0.45269 0.41629 0.01216  0.00123  -0.09662 65  ILE A CA  
517  C C   . ILE A 65  ? 0.42900 0.46195 0.41156 0.02982  -0.00076 -0.07930 65  ILE A C   
518  O O   . ILE A 65  ? 0.45727 0.47719 0.43854 0.03989  0.00506  -0.07124 65  ILE A O   
519  C CB  . ILE A 65  ? 0.49389 0.51409 0.45696 0.00911  0.00299  -0.11523 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.58002 0.57648 0.53412 -0.01345 0.00892  -0.13574 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.45841 0.52800 0.41725 0.01504  -0.00563 -0.12048 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.63908 0.58360 0.57612 -0.00913 0.02027  -0.13814 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.44086 0.50192 0.42424 0.03385  -0.00696 -0.07452 66  GLY A N   
524  C CA  . GLY A 66  ? 0.43220 0.49803 0.40865 0.04994  -0.00498 -0.05815 66  GLY A CA  
525  C C   . GLY A 66  ? 0.49945 0.59192 0.45555 0.06316  -0.00820 -0.06163 66  GLY A C   
526  O O   . GLY A 66  ? 0.48486 0.60969 0.43907 0.06182  -0.01670 -0.07373 66  GLY A O   
527  N N   . ILE A 67  ? 0.48778 0.56972 0.42735 0.07612  -0.00047 -0.05186 67  ILE A N   
528  C CA  . ILE A 67  ? 0.46573 0.56538 0.37792 0.09457  -0.00090 -0.05017 67  ILE A CA  
529  C C   . ILE A 67  ? 0.50265 0.58295 0.39719 0.10849  0.00772  -0.02920 67  ILE A C   
530  O O   . ILE A 67  ? 0.51781 0.56875 0.41533 0.10222  0.01964  -0.01929 67  ILE A O   
531  C CB  . ILE A 67  ? 0.46346 0.55870 0.36286 0.09750  0.00489  -0.05682 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.44539 0.55162 0.35712 0.08254  -0.00166 -0.07930 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.48272 0.59014 0.34735 0.12042  0.00708  -0.05087 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.43414 0.53287 0.33535 0.08389  0.00387  -0.08844 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.50902 0.60579 0.38311 0.12733  0.00314  -0.02377 68  HIS A N   
536  C CA  . HIS A 68  ? 0.61953 0.68603 0.46678 0.14283  0.01459  -0.00328 68  HIS A CA  
537  C C   . HIS A 68  ? 0.63380 0.68646 0.43776 0.16428  0.02544  0.00512  68  HIS A C   
538  O O   . HIS A 68  ? 0.66077 0.74361 0.44249 0.18635  0.01738  0.00077  68  HIS A O   
539  C CB  . HIS A 68  ? 0.68291 0.76527 0.52517 0.15683  0.00663  0.00155  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.62113 0.75396 0.44833 0.17932  -0.00668 -0.00763 68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.72786 0.86036 0.50828 0.21466  -0.00270 0.00334  68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.62378 0.81258 0.47462 0.17175  -0.02297 -0.02820 68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.66773 0.86260 0.44625 0.23088  -0.01855 -0.01075 68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.65107 0.88305 0.47403 0.20219  -0.03064 -0.03154 68  HIS A NE2 
545  N N   . THR A 69  ? 0.64897 0.65896 0.43939 0.15764  0.04472  0.01614  69  THR A N   
546  C CA  . THR A 69  ? 0.79214 0.77907 0.53446 0.17722  0.05965  0.02660  69  THR A CA  
547  C C   . THR A 69  ? 0.89018 0.83812 0.58472 0.20013  0.07293  0.04647  69  THR A C   
548  O O   . THR A 69  ? 0.98118 0.91341 0.62480 0.22753  0.08208  0.05637  69  THR A O   
549  C CB  . THR A 69  ? 0.71703 0.67931 0.46175 0.15848  0.07750  0.02661  69  THR A CB  
550  O OG1 . THR A 69  ? 0.68266 0.62840 0.45753 0.13208  0.08514  0.02690  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.70722 0.70446 0.47347 0.15295  0.06658  0.00928  69  THR A CG2 
552  N N   . GLY A 70  ? 0.99064 0.92032 0.69553 0.19254  0.07468  0.05261  70  GLY A N   
553  C CA  . GLY A 70  ? 0.97337 0.87016 0.63411 0.21819  0.08324  0.06917  70  GLY A CA  
554  C C   . GLY A 70  ? 0.94286 0.88902 0.61330 0.23997  0.06026  0.06399  70  GLY A C   
555  O O   . GLY A 70  ? 0.87089 0.87488 0.55612 0.24841  0.04142  0.05005  70  GLY A O   
556  N N   . HIS A 71  ? 1.01946 0.94602 0.68183 0.24737  0.06268  0.07307  71  HIS A N   
557  C CA  . HIS A 71  ? 1.02818 1.00706 0.70130 0.26778  0.04208  0.06732  71  HIS A CA  
558  C C   . HIS A 71  ? 0.92928 0.96614 0.66873 0.23700  0.02123  0.04577  71  HIS A C   
559  O O   . HIS A 71  ? 0.82395 0.85140 0.59726 0.20398  0.02343  0.03854  71  HIS A O   
560  C CB  . HIS A 71  ? 1.02950 0.97082 0.68117 0.28015  0.05082  0.08130  71  HIS A CB  
561  C CG  . HIS A 71  ? 1.04254 0.95076 0.72794 0.24150  0.05897  0.08073  71  HIS A CG  
562  N ND1 . HIS A 71  ? 1.03901 0.98310 0.77514 0.22179  0.04332  0.07009  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 1.05593 0.90473 0.73230 0.21774  0.08122  0.08724  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 0.98775 0.89593 0.74256 0.19199  0.05412  0.07149  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.19673 1.05106 0.91822 0.18765  0.07670  0.08030  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.83204 0.92950 0.58632 0.24926  0.00246  0.03480  72  LEU A N   
567  C CA  . LEU A 72  ? 0.78894 0.93355 0.59904 0.21841  -0.01332 0.01436  72  LEU A CA  
568  C C   . LEU A 72  ? 0.72530 0.83517 0.56536 0.19005  -0.00792 0.01888  72  LEU A C   
569  O O   . LEU A 72  ? 0.73782 0.81257 0.56107 0.19919  0.00101  0.03355  72  LEU A O   
570  C CB  . LEU A 72  ? 0.74943 0.96757 0.56679 0.23525  -0.03092 0.00098  72  LEU A CB  
571  C CG  . LEU A 72  ? 0.68480 0.95337 0.55307 0.20413  -0.04435 -0.02084 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.63216 0.90564 0.52882 0.16957  -0.04635 -0.03900 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.56827 0.91843 0.43640 0.22478  -0.05910 -0.03533 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.64223 0.75797 0.52198 0.15727  -0.01190 0.00624  73  GLY A N   
575  C CA  . GLY A 73  ? 0.55451 0.64790 0.46374 0.13279  -0.00946 0.00802  73  GLY A CA  
576  C C   . GLY A 73  ? 0.55089 0.68592 0.49207 0.11876  -0.02274 -0.00642 73  GLY A C   
577  O O   . GLY A 73  ? 0.57707 0.75903 0.52399 0.11894  -0.03272 -0.02229 73  GLY A O   
578  N N   . PHE A 74  ? 0.43954 0.55912 0.40049 0.10459  -0.02160 -0.00254 74  PHE A N   
579  C CA  . PHE A 74  ? 0.45022 0.60102 0.43994 0.08594  -0.03041 -0.01667 74  PHE A CA  
580  C C   . PHE A 74  ? 0.46164 0.60296 0.46917 0.06162  -0.02955 -0.02862 74  PHE A C   
581  O O   . PHE A 74  ? 0.47100 0.63797 0.49257 0.04508  -0.03425 -0.04533 74  PHE A O   
582  C CB  . PHE A 74  ? 0.36685 0.50463 0.36955 0.07983  -0.02926 -0.00880 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.30719 0.48034 0.30413 0.09595  -0.03519 -0.00919 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.34309 0.50735 0.30872 0.12595  -0.03182 0.00379  74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.29717 0.51692 0.31477 0.08340  -0.04301 -0.02481 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.39111 0.59348 0.34679 0.14845  -0.03787 0.00323  74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.29381 0.56035 0.30748 0.10093  -0.04937 -0.02784 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.35453 0.61486 0.33714 0.13660  -0.04797 -0.01340 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.40736 0.51095 0.41274 0.05842  -0.02176 -0.02129 75  TYR A N   
590  C CA  . TYR A 75  ? 0.41698 0.50859 0.43251 0.04245  -0.01998 -0.03154 75  TYR A CA  
591  C C   . TYR A 75  ? 0.48453 0.58419 0.48564 0.04870  -0.01942 -0.03909 75  TYR A C   
592  O O   . TYR A 75  ? 0.48252 0.58831 0.48722 0.03665  -0.02084 -0.05466 75  TYR A O   
593  C CB  . TYR A 75  ? 0.40748 0.46432 0.43083 0.03783  -0.01291 -0.02199 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.42168 0.47228 0.45855 0.03148  -0.01407 -0.01606 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.39404 0.45192 0.44159 0.01840  -0.01767 -0.02462 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.38511 0.42149 0.42162 0.03638  -0.00975 -0.00344 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.35049 0.40243 0.40819 0.01333  -0.01798 -0.01881 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.35880 0.39119 0.40677 0.03112  -0.01121 0.00097  75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.34162 0.38249 0.40007 0.02127  -0.01592 -0.00574 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.31542 0.35179 0.38286 0.01697  -0.01654 -0.00084 75  TYR A OH  
601  N N   . ALA A 76  ? 0.51258 0.60848 0.49309 0.06715  -0.01557 -0.02859 76  ALA A N   
602  C CA  . ALA A 76  ? 0.51848 0.61693 0.48179 0.07527  -0.01293 -0.03282 76  ALA A CA  
603  C C   . ALA A 76  ? 0.50174 0.64148 0.44939 0.09029  -0.02138 -0.04034 76  ALA A C   
604  O O   . ALA A 76  ? 0.55146 0.69311 0.47249 0.11409  -0.01919 -0.02922 76  ALA A O   
605  C CB  . ALA A 76  ? 0.53362 0.60122 0.47934 0.08509  -0.00050 -0.01740 76  ALA A CB  
606  N N   . ASP A 77  ? 0.48858 0.66208 0.44979 0.07649  -0.02979 -0.06079 77  ASP A N   
607  C CA  . ASP A 77  ? 0.56705 0.79727 0.52177 0.08727  -0.04012 -0.07270 77  ASP A CA  
608  C C   . ASP A 77  ? 0.50896 0.77268 0.45362 0.08745  -0.04456 -0.09249 77  ASP A C   
609  O O   . ASP A 77  ? 0.51437 0.83586 0.46303 0.08512  -0.05391 -0.11209 77  ASP A O   
610  C CB  . ASP A 77  ? 0.50197 0.75891 0.48121 0.06872  -0.04568 -0.08386 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.56634 0.80348 0.56532 0.03401  -0.04143 -0.09952 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.56073 0.76179 0.55510 0.02738  -0.03501 -0.10043 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.58425 0.83971 0.59984 0.01438  -0.04286 -0.11092 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.52523 0.75900 0.45709 0.08990  -0.03776 -0.08945 78  TRP A N   
615  C CA  . TRP A 78  ? 0.53682 0.79821 0.45113 0.09769  -0.04087 -0.10385 78  TRP A CA  
616  C C   . TRP A 78  ? 0.52064 0.76855 0.40082 0.13019  -0.03564 -0.08436 78  TRP A C   
617  O O   . TRP A 78  ? 0.53718 0.73635 0.41020 0.13500  -0.02425 -0.06326 78  TRP A O   
618  C CB  . TRP A 78  ? 0.59525 0.82969 0.51654 0.07522  -0.03498 -0.11776 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.60653 0.85241 0.54675 0.04356  -0.03696 -0.14312 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.62318 0.84063 0.58269 0.02146  -0.03259 -0.14300 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.64125 0.92638 0.57839 0.02857  -0.04116 -0.17349 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.63846 0.86791 0.60385 -0.00735 -0.03143 -0.17031 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.66298 0.93557 0.61640 -0.00577 -0.03655 -0.19098 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.65379 0.98349 0.57349 0.04014  -0.04727 -0.18877 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.69285 0.99313 0.64565 -0.03319 -0.03586 -0.22492 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.66905 1.03429 0.59171 0.01470  -0.04946 -0.22327 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.66339 1.01252 0.60256 -0.02370 -0.04285 -0.24188 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.56613 0.85578 0.42313 0.15067  -0.04204 -0.09277 79  ARG A N   
629  C CA  . ARG A 79  ? 0.62545 0.89759 0.44128 0.18383  -0.03475 -0.07394 79  ARG A CA  
630  C C   . ARG A 79  ? 0.64075 0.88496 0.44698 0.17782  -0.02559 -0.07572 79  ARG A C   
631  O O   . ARG A 79  ? 0.64675 0.90199 0.47166 0.15553  -0.02899 -0.09663 79  ARG A O   
632  C CB  . ARG A 79  ? 0.63532 0.96889 0.42374 0.21671  -0.04614 -0.08063 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.58432 0.96268 0.38383 0.22528  -0.05717 -0.08373 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.57566 1.01747 0.35716 0.26046  -0.06614 -0.08948 79  ARG A CD  
635  N NE  . ARG A 79  ? 0.60335 1.01008 0.34315 0.29531  -0.05548 -0.06840 79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.67734 1.11316 0.40822 0.30916  -0.05778 -0.07699 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.63056 1.13429 0.39138 0.29157  -0.06984 -0.10710 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.69335 1.08688 0.38342 0.33971  -0.04596 -0.05538 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.64273 0.84782 0.41614 0.19725  -0.01173 -0.05464 80  PRO A N   
640  C CA  . PRO A 80  ? 0.66078 0.84462 0.42390 0.19295  -0.00191 -0.05666 80  PRO A CA  
641  C C   . PRO A 80  ? 0.73190 0.96122 0.48185 0.20137  -0.01154 -0.07741 80  PRO A C   
642  O O   . PRO A 80  ? 0.70067 0.92092 0.45634 0.18788  -0.00752 -0.08843 80  PRO A O   
643  C CB  . PRO A 80  ? 0.67119 0.80834 0.39465 0.21343  0.01686  -0.02991 80  PRO A CB  
644  C CG  . PRO A 80  ? 0.71266 0.82694 0.44096 0.21346  0.01997  -0.01458 80  PRO A CG  
645  C CD  . PRO A 80  ? 0.65501 0.82258 0.40077 0.21773  -0.00030 -0.02810 80  PRO A CD  
646  N N   . ALA A 81  ? 0.70030 0.98238 0.43178 0.22471  -0.02421 -0.08471 81  ALA A N   
647  C CA  . ALA A 81  ? 0.72567 1.05673 0.44245 0.23329  -0.03318 -0.10642 81  ALA A CA  
648  C C   . ALA A 81  ? 0.68597 1.05056 0.44024 0.19768  -0.04347 -0.13989 81  ALA A C   
649  O O   . ALA A 81  ? 0.67608 1.06678 0.42281 0.19381  -0.04699 -0.16122 81  ALA A O   
650  C CB  . ALA A 81  ? 0.71074 1.09036 0.41034 0.26752  -0.04317 -0.10252 81  ALA A CB  
651  N N   . GLU A 82  ? 0.62610 0.98674 0.41606 0.17147  -0.04645 -0.14523 82  GLU A N   
652  C CA  . GLU A 82  ? 0.64637 1.02013 0.46754 0.13333  -0.05052 -0.17429 82  GLU A CA  
653  C C   . GLU A 82  ? 0.65646 0.96775 0.48817 0.11088  -0.03796 -0.17361 82  GLU A C   
654  O O   . GLU A 82  ? 0.62054 0.92393 0.47109 0.08016  -0.03703 -0.19451 82  GLU A O   
655  C CB  . GLU A 82  ? 0.70996 1.09725 0.56001 0.11611  -0.05566 -0.17696 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.76557 1.22058 0.60985 0.13867  -0.06849 -0.17894 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.81881 1.34443 0.68681 0.11411  -0.07828 -0.21418 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.80457 1.36064 0.67377 0.10846  -0.07937 -0.23277 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.77607 1.31993 0.66906 0.09774  -0.08079 -0.21908 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.64049 0.90657 0.45833 0.12553  -0.02657 -0.15070 83  ALA A N   
661  C CA  . ALA A 83  ? 0.64330 0.85674 0.47483 0.10826  -0.01525 -0.14806 83  ALA A CA  
662  C C   . ALA A 83  ? 0.64656 0.85968 0.47382 0.09410  -0.01394 -0.17399 83  ALA A C   
663  O O   . ALA A 83  ? 0.64907 0.82895 0.49017 0.07323  -0.00852 -0.18328 83  ALA A O   
664  C CB  . ALA A 83  ? 0.64471 0.82200 0.46373 0.12477  -0.00236 -0.12187 83  ALA A CB  
665  N N   . ASP A 84  ? 0.63391 0.88049 0.43759 0.10700  -0.01782 -0.18609 84  ASP A N   
666  C CA  . ASP A 84  ? 0.66332 0.90808 0.45938 0.09324  -0.01557 -0.21267 84  ASP A CA  
667  C C   . ASP A 84  ? 0.70172 0.96429 0.51199 0.06181  -0.02085 -0.24347 84  ASP A C   
668  O O   . ASP A 84  ? 0.68910 0.91733 0.49866 0.04016  -0.01275 -0.26177 84  ASP A O   
669  C CB  . ASP A 84  ? 0.69029 0.97193 0.45623 0.11525  -0.01909 -0.21920 84  ASP A CB  
670  C CG  . ASP A 84  ? 0.75073 1.00585 0.49689 0.14210  -0.00868 -0.19031 84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.79450 1.00247 0.55275 0.13738  0.00291  -0.17382 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.76209 1.04453 0.47883 0.16772  -0.01079 -0.18479 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.67523 0.98997 0.49534 0.05877  -0.03238 -0.25053 85  LYS A N   
674  C CA  . LYS A 85  ? 0.65796 0.99080 0.49403 0.02325  -0.03436 -0.28040 85  LYS A CA  
675  C C   . LYS A 85  ? 0.67998 0.94979 0.53404 0.00222  -0.02396 -0.27058 85  LYS A C   
676  O O   . LYS A 85  ? 0.72106 0.96698 0.57753 -0.03026 -0.01616 -0.29356 85  LYS A O   
677  C CB  . LYS A 85  ? 0.68137 1.09496 0.52588 0.02765  -0.04914 -0.29012 85  LYS A CB  
678  N N   . LEU A 86  ? 0.68364 0.92239 0.54602 0.02053  -0.02185 -0.23715 86  LEU A N   
679  C CA  . LEU A 86  ? 0.66729 0.84830 0.54405 0.00702  -0.01262 -0.22536 86  LEU A CA  
680  C C   . LEU A 86  ? 0.72773 0.84868 0.59197 0.00149  0.00065  -0.23021 86  LEU A C   
681  O O   . LEU A 86  ? 0.74716 0.82485 0.61132 -0.01965 0.00983  -0.23984 86  LEU A O   
682  C CB  . LEU A 86  ? 0.64180 0.81115 0.52850 0.02893  -0.01355 -0.19120 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.57953 0.71593 0.48540 0.01550  -0.00974 -0.18123 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.64693 0.82031 0.56339 -0.00565 -0.01618 -0.19973 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.61285 0.74535 0.52626 0.03592  -0.01087 -0.15144 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.71265 0.82698 0.56264 0.02295  0.00350  -0.22212 87  VAL A N   
687  C CA  . VAL A 87  ? 0.71782 0.78193 0.55339 0.02347  0.01577  -0.22754 87  VAL A CA  
688  C C   . VAL A 87  ? 0.77767 0.82408 0.59843 -0.00388 0.02165  -0.26056 87  VAL A C   
689  O O   . VAL A 87  ? 0.78032 0.76739 0.59171 -0.01458 0.03416  -0.26545 87  VAL A O   
690  C CB  . VAL A 87  ? 0.71996 0.79606 0.54055 0.04774  0.01715  -0.22066 87  VAL A CB  
691  C CG1 . VAL A 87  ? 0.68270 0.71614 0.48465 0.04858  0.02907  -0.23315 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.67256 0.75034 0.50342 0.06907  0.01817  -0.18933 87  VAL A CG2 
693  N N   . LYS A 88  ? 0.78353 0.88114 0.59840 -0.01511 0.01396  -0.28473 88  LYS A N   
694  C CA  . LYS A 88  ? 0.84146 0.92830 0.63943 -0.04528 0.02124  -0.32155 88  LYS A CA  
695  C C   . LYS A 88  ? 0.91901 0.97404 0.72325 -0.07862 0.02973  -0.33275 88  LYS A C   
696  O O   . LYS A 88  ? 0.95313 0.93686 0.73732 -0.09415 0.04687  -0.34243 88  LYS A O   
697  C CB  . LYS A 88  ? 0.82351 0.98960 0.61811 -0.04935 0.00880  -0.34608 88  LYS A CB  
698  C CG  . LYS A 88  ? 0.87149 1.03331 0.65640 -0.08151 0.01547  -0.37638 88  LYS A CG  
699  C CD  . LYS A 88  ? 0.95209 1.20376 0.75114 -0.08398 0.00069  -0.38768 88  LYS A CD  
700  C CE  . LYS A 88  ? 1.13002 1.40768 0.91122 -0.06204 -0.00450 -0.39101 88  LYS A CE  
701  N NZ  . LYS A 88  ? 1.13727 1.41931 0.90807 -0.01964 -0.01031 -0.36479 88  LYS A NZ  
702  N N   . LEU A 89  ? 0.91846 1.02170 0.74664 -0.08758 0.01961  -0.33005 89  LEU A N   
703  C CA  . LEU A 89  ? 0.93536 1.01956 0.76973 -0.12334 0.02818  -0.34426 89  LEU A CA  
704  C C   . LEU A 89  ? 0.93215 0.92751 0.75858 -0.12196 0.04331  -0.32444 89  LEU A C   
705  O O   . LEU A 89  ? 1.01567 0.96827 0.83285 -0.15249 0.05760  -0.33785 89  LEU A O   
706  C CB  . LEU A 89  ? 0.92756 1.08274 0.79106 -0.12452 0.01356  -0.33888 89  LEU A CB  
707  C CG  . LEU A 89  ? 0.93217 1.17686 0.80740 -0.13073 0.00146  -0.35729 89  LEU A CG  
708  C CD1 . LEU A 89  ? 0.89558 1.20218 0.79912 -0.13230 -0.00897 -0.35149 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 0.86896 1.09797 0.73677 -0.16561 0.01497  -0.38243 89  LEU A CD2 
710  N N   . LEU A 90  ? 0.95230 0.92003 0.77867 -0.08707 0.04200  -0.29464 90  LEU A N   
711  C CA  . LEU A 90  ? 0.94140 0.84489 0.76583 -0.07538 0.05133  -0.27073 90  LEU A CA  
712  C C   . LEU A 90  ? 1.07007 0.90168 0.86262 -0.06375 0.06703  -0.27219 90  LEU A C   
713  O O   . LEU A 90  ? 1.07945 0.84776 0.85886 -0.05836 0.07901  -0.26075 90  LEU A O   
714  C CB  . LEU A 90  ? 0.87787 0.81176 0.72731 -0.04430 0.03880  -0.23776 90  LEU A CB  
715  C CG  . LEU A 90  ? 0.88481 0.78275 0.74182 -0.02374 0.04204  -0.20946 90  LEU A CG  
716  C CD1 . LEU A 90  ? 0.84942 0.72178 0.71286 -0.04068 0.04629  -0.20531 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 0.75262 0.69999 0.63142 -0.00120 0.02955  -0.18785 90  LEU A CD2 
718  N N   . ALA A 91  ? 1.06941 0.91257 0.84755 -0.05468 0.06662  -0.28434 91  ALA A N   
719  C CA  . ALA A 91  ? 1.11818 0.89399 0.86045 -0.04581 0.08301  -0.29227 91  ALA A CA  
720  C C   . ALA A 91  ? 1.20661 0.92192 0.91637 -0.08144 0.10191  -0.32070 91  ALA A C   
721  O O   . ALA A 91  ? 1.25664 0.89243 0.93682 -0.07396 0.11844  -0.31452 91  ALA A O   
722  C CB  . ALA A 91  ? 1.06328 0.87178 0.79795 -0.03067 0.07801  -0.30111 91  ALA A CB  
723  N N   . LYS A 92  ? 1.16758 0.92962 0.88914 -0.11592 0.09627  -0.34229 92  LYS A N   
724  C CA  . LYS A 92  ? 1.20635 0.92985 0.91367 -0.14978 0.10994  -0.35455 92  LYS A CA  
725  C C   . LYS A 92  ? 1.25345 0.92974 0.96079 -0.15829 0.12025  -0.33858 92  LYS A C   
726  O O   . LYS A 92  ? 1.36976 0.97530 1.04964 -0.16952 0.13937  -0.33717 92  LYS A O   
727  C CB  . LYS A 92  ? 1.22008 1.02126 0.94844 -0.18274 0.10090  -0.37822 92  LYS A CB  
728  C CG  . LYS A 92  ? 1.15524 1.04913 0.90398 -0.16797 0.07925  -0.38532 92  LYS A CG  
729  C CD  . LYS A 92  ? 1.11854 1.00116 0.84477 -0.14297 0.07869  -0.38875 92  LYS A CD  
730  C CE  . LYS A 92  ? 1.20064 1.00325 0.89060 -0.15152 0.09804  -0.39858 92  LYS A CE  
731  N NZ  . LYS A 92  ? 1.30555 1.13227 0.99086 -0.18368 0.10123  -0.42599 92  LYS A NZ  
732  N N   . GLY A 93  ? 1.21705 0.93000 0.95201 -0.15143 0.10890  -0.32553 93  GLY A N   
733  C CA  . GLY A 93  ? 1.22306 0.90595 0.96219 -0.16404 0.11653  -0.31285 93  GLY A CA  
734  C C   . GLY A 93  ? 1.22129 0.95522 0.98062 -0.20498 0.11563  -0.32992 93  GLY A C   
735  O O   . GLY A 93  ? 1.14834 0.96898 0.93486 -0.21271 0.09929  -0.34372 93  GLY A O   
736  N N   . GLU A 94  ? 1.33070 1.01516 1.07523 -0.22862 0.13443  -0.32835 94  GLU A N   
737  C CA  . GLU A 94  ? 1.33954 1.07071 1.10237 -0.26884 0.13882  -0.34430 94  GLU A CA  
738  C C   . GLU A 94  ? 1.36509 1.18455 1.17140 -0.26662 0.11751  -0.34127 94  GLU A C   
739  O O   . GLU A 94  ? 1.34149 1.24745 1.17445 -0.28305 0.10725  -0.35892 94  GLU A O   
740  C CB  . GLU A 94  ? 1.30433 1.06865 1.06352 -0.29522 0.14356  -0.37327 94  GLU A CB  
741  N N   . TYR A 95  ? 1.20687 1.00664 1.01937 -0.24246 0.11080  -0.31817 95  TYR A N   
742  C CA  . TYR A 95  ? 1.10511 0.97668 0.95437 -0.23823 0.09256  -0.31234 95  TYR A CA  
743  C C   . TYR A 95  ? 1.10767 0.94385 0.95772 -0.24881 0.10323  -0.29770 95  TYR A C   
744  O O   . TYR A 95  ? 1.17762 0.92701 0.99722 -0.24570 0.12144  -0.28476 95  TYR A O   
745  C CB  . TYR A 95  ? 1.05847 0.94907 0.91834 -0.19987 0.07448  -0.29704 95  TYR A CB  
746  C CG  . TYR A 95  ? 1.07463 0.88473 0.91236 -0.16877 0.08286  -0.27121 95  TYR A CG  
747  C CD1 . TYR A 95  ? 1.00742 0.77710 0.84633 -0.15446 0.08652  -0.24484 95  TYR A CD1 
748  C CD2 . TYR A 95  ? 1.11336 0.89425 0.92859 -0.15159 0.08669  -0.27454 95  TYR A CD2 
749  C CE1 . TYR A 95  ? 0.97985 0.68820 0.79884 -0.12244 0.09288  -0.22344 95  TYR A CE1 
750  C CE2 . TYR A 95  ? 1.13226 0.85050 0.92813 -0.11983 0.09376  -0.25279 95  TYR A CE2 
751  C CZ  . TYR A 95  ? 1.05313 0.73810 0.85129 -0.10473 0.09644  -0.22775 95  TYR A CZ  
752  O OH  . TYR A 95  ? 1.06740 0.70153 0.84643 -0.06986 0.10233  -0.20840 95  TYR A OH  
753  N N   . GLN A 96  ? 1.02224 0.92860 0.90503 -0.25725 0.09162  -0.29849 96  GLN A N   
754  C CA  . GLN A 96  ? 0.94491 0.82796 0.83142 -0.26610 0.09988  -0.28472 96  GLN A CA  
755  C C   . GLN A 96  ? 0.91105 0.76703 0.80176 -0.23509 0.09002  -0.26045 96  GLN A C   
756  O O   . GLN A 96  ? 0.83837 0.73791 0.74847 -0.20328 0.07018  -0.24692 96  GLN A O   
757  C CB  . GLN A 96  ? 0.95501 0.92878 0.87479 -0.28580 0.09245  -0.29633 96  GLN A CB  
758  C CG  . GLN A 96  ? 1.05452 1.00441 0.97116 -0.30710 0.10918  -0.29090 96  GLN A CG  
759  C CD  . GLN A 96  ? 1.17224 1.10587 1.06918 -0.34320 0.13396  -0.31093 96  GLN A CD  
760  O OE1 . GLN A 96  ? 1.14187 1.10307 1.03683 -0.35504 0.13546  -0.33192 96  GLN A OE1 
761  N NE2 . GLN A 96  ? 1.16573 1.05414 1.04553 -0.36154 0.15506  -0.30550 96  GLN A NE2 
762  N N   . LYS A 97  ? 0.87238 0.66398 0.74774 -0.23343 0.10338  -0.24224 97  LYS A N   
763  C CA  . LYS A 97  ? 0.79831 0.58062 0.68573 -0.19966 0.09300  -0.21090 97  LYS A CA  
764  C C   . LYS A 97  ? 0.76175 0.58625 0.67497 -0.21248 0.08804  -0.20631 97  LYS A C   
765  O O   . LYS A 97  ? 0.78698 0.60250 0.69244 -0.24559 0.10311  -0.21977 97  LYS A O   
766  C CB  . LYS A 97  ? 0.84537 0.53025 0.69528 -0.17976 0.10911  -0.19234 97  LYS A CB  
767  C CG  . LYS A 97  ? 0.85311 0.51000 0.68543 -0.15018 0.10780  -0.18747 97  LYS A CG  
768  C CD  . LYS A 97  ? 0.89565 0.45982 0.68593 -0.12637 0.12468  -0.17128 97  LYS A CD  
769  C CE  . LYS A 97  ? 0.97769 0.48320 0.72631 -0.13885 0.14506  -0.18357 97  LYS A CE  
770  N NZ  . LYS A 97  ? 1.12274 0.55715 0.83278 -0.10197 0.15596  -0.16270 97  LYS A NZ  
771  N N   . VAL A 98  ? 0.66506 0.53937 0.60856 -0.18288 0.06741  -0.18447 98  VAL A N   
772  C CA  . VAL A 98  ? 0.63287 0.54819 0.60151 -0.18397 0.05955  -0.17459 98  VAL A CA  
773  C C   . VAL A 98  ? 0.59345 0.47183 0.56143 -0.15174 0.05603  -0.14256 98  VAL A C   
774  O O   . VAL A 98  ? 0.55777 0.42922 0.52599 -0.12190 0.04788  -0.12801 98  VAL A O   
775  C CB  . VAL A 98  ? 0.60012 0.61079 0.60059 -0.17555 0.03867  -0.17987 98  VAL A CB  
776  C CG1 . VAL A 98  ? 0.57300 0.62283 0.59655 -0.16903 0.03001  -0.16684 98  VAL A CG1 
777  C CG2 . VAL A 98  ? 0.63255 0.69018 0.63423 -0.20758 0.04177  -0.21480 98  VAL A CG2 
778  N N   . SER A 99  ? 0.55164 0.41120 0.51884 -0.15928 0.06285  -0.13371 99  SER A N   
779  C CA  . SER A 99  ? 0.54174 0.36563 0.50467 -0.13296 0.06192  -0.10688 99  SER A CA  
780  C C   . SER A 99  ? 0.50480 0.37935 0.49677 -0.12885 0.04978  -0.09625 99  SER A C   
781  O O   . SER A 99  ? 0.50449 0.40680 0.50519 -0.15410 0.05354  -0.10840 99  SER A O   
782  C CB  . SER A 99  ? 0.60658 0.34778 0.53110 -0.14271 0.08474  -0.10464 99  SER A CB  
783  O OG  . SER A 99  ? 0.72593 0.40758 0.61576 -0.14000 0.09802  -0.11141 99  SER A OG  
784  N N   . TYR A 100 ? 0.47053 0.35724 0.47603 -0.09836 0.03689  -0.07524 100 TYR A N   
785  C CA  . TYR A 100 ? 0.45504 0.37805 0.48273 -0.08816 0.02610  -0.06201 100 TYR A CA  
786  C C   . TYR A 100 ? 0.48701 0.37005 0.50522 -0.07216 0.02971  -0.04321 100 TYR A C   
787  O O   . TYR A 100 ? 0.50150 0.34714 0.50345 -0.05509 0.03323  -0.03611 100 TYR A O   
788  C CB  . TYR A 100 ? 0.38920 0.35818 0.43609 -0.06728 0.01019  -0.05519 100 TYR A CB  
789  C CG  . TYR A 100 ? 0.39708 0.42159 0.45468 -0.07473 0.00286  -0.07014 100 TYR A CG  
790  C CD1 . TYR A 100 ? 0.39931 0.44326 0.45616 -0.10192 0.00867  -0.09170 100 TYR A CD1 
791  C CD2 . TYR A 100 ? 0.35679 0.41565 0.42219 -0.05391 -0.00851 -0.06350 100 TYR A CD2 
792  C CE1 . TYR A 100 ? 0.41812 0.52515 0.48515 -0.10560 0.00042  -0.10778 100 TYR A CE1 
793  C CE2 . TYR A 100 ? 0.35255 0.46366 0.42209 -0.05380 -0.01555 -0.07601 100 TYR A CE2 
794  C CZ  . TYR A 100 ? 0.39397 0.53459 0.46617 -0.07800 -0.01266 -0.09856 100 TYR A CZ  
795  O OH  . TYR A 100 ? 0.36471 0.56950 0.44183 -0.07499 -0.02122 -0.11316 100 TYR A OH  
796  N N   . PRO A 101 ? 0.45121 0.34645 0.47849 -0.07504 0.02850  -0.03597 101 PRO A N   
797  C CA  . PRO A 101 ? 0.44856 0.31499 0.46763 -0.05782 0.03002  -0.01877 101 PRO A CA  
798  C C   . PRO A 101 ? 0.41424 0.30162 0.44763 -0.03182 0.01726  -0.00685 101 PRO A C   
799  O O   . PRO A 101 ? 0.37783 0.30405 0.42973 -0.02841 0.00731  -0.00812 101 PRO A O   
800  C CB  . PRO A 101 ? 0.41833 0.30390 0.44694 -0.07071 0.03098  -0.01729 101 PRO A CB  
801  C CG  . PRO A 101 ? 0.40201 0.31584 0.43715 -0.10016 0.03552  -0.03733 101 PRO A CG  
802  C CD  . PRO A 101 ? 0.40458 0.34522 0.44882 -0.09362 0.02614  -0.04508 101 PRO A CD  
803  N N   . LEU A 102 ? 0.43523 0.29694 0.45697 -0.01344 0.01918  0.00438  102 LEU A N   
804  C CA  . LEU A 102 ? 0.39342 0.27663 0.42747 0.00799  0.00981  0.01295  102 LEU A CA  
805  C C   . LEU A 102 ? 0.40879 0.29313 0.44330 0.01559  0.00833  0.02294  102 LEU A C   
806  O O   . LEU A 102 ? 0.41354 0.27219 0.43295 0.00893  0.01614  0.02561  102 LEU A O   
807  C CB  . LEU A 102 ? 0.39570 0.26035 0.41568 0.02711  0.01235  0.01334  102 LEU A CB  
808  C CG  . LEU A 102 ? 0.45433 0.31016 0.46816 0.02054  0.01577  0.00284  102 LEU A CG  
809  C CD1 . LEU A 102 ? 0.44049 0.27085 0.43423 0.04200  0.02073  0.00344  102 LEU A CD1 
810  C CD2 . LEU A 102 ? 0.37635 0.27465 0.41351 0.01468  0.00693  -0.00160 102 LEU A CD2 
811  N N   . LEU A 103 ? 0.36679 0.28101 0.41711 0.02743  -0.00020 0.02700  103 LEU A N   
812  C CA  . LEU A 103 ? 0.38126 0.30581 0.43473 0.03530  -0.00344 0.03401  103 LEU A CA  
813  C C   . LEU A 103 ? 0.41910 0.34627 0.46458 0.05883  -0.00487 0.03675  103 LEU A C   
814  O O   . LEU A 103 ? 0.38709 0.33748 0.44299 0.06566  -0.00846 0.03193  103 LEU A O   
815  C CB  . LEU A 103 ? 0.33395 0.29335 0.40942 0.02866  -0.01048 0.03303  103 LEU A CB  
816  C CG  . LEU A 103 ? 0.33947 0.31335 0.41912 0.03538  -0.01397 0.03729  103 LEU A CG  
817  C CD1 . LEU A 103 ? 0.32983 0.28747 0.39965 0.03156  -0.01075 0.04293  103 LEU A CD1 
818  C CD2 . LEU A 103 ? 0.29281 0.29190 0.38770 0.02922  -0.01748 0.03431  103 LEU A CD2 
819  N N   . LYS A 104 ? 0.42620 0.33368 0.45184 0.07276  -0.00155 0.04389  104 LYS A N   
820  C CA  . LYS A 104 ? 0.40991 0.33322 0.42808 0.10066  -0.00511 0.04592  104 LYS A CA  
821  C C   . LYS A 104 ? 0.40978 0.37603 0.44665 0.10165  -0.01364 0.04503  104 LYS A C   
822  O O   . LYS A 104 ? 0.40022 0.36021 0.43654 0.09268  -0.01329 0.04954  104 LYS A O   
823  C CB  . LYS A 104 ? 0.47307 0.34924 0.45079 0.12309  0.00412  0.05472  104 LYS A CB  
824  C CG  . LYS A 104 ? 0.52916 0.43286 0.49758 0.15935  -0.00149 0.05645  104 LYS A CG  
825  C CD  . LYS A 104 ? 0.58255 0.43456 0.50118 0.19246  0.00901  0.06623  104 LYS A CD  
826  C CE  . LYS A 104 ? 0.64292 0.44575 0.53094 0.18945  0.01932  0.07711  104 LYS A CE  
827  N NZ  . LYS A 104 ? 0.84002 0.61937 0.68415 0.21602  0.02719  0.08159  104 LYS A NZ  
828  N N   . THR A 105 ? 0.39240 0.40458 0.44631 0.10965  -0.02008 0.03696  105 THR A N   
829  C CA  . THR A 105 ? 0.39208 0.44998 0.46177 0.11035  -0.02681 0.03145  105 THR A CA  
830  C C   . THR A 105 ? 0.41437 0.50252 0.47368 0.14199  -0.03097 0.02930  105 THR A C   
831  O O   . THR A 105 ? 0.43990 0.54433 0.49828 0.15712  -0.03112 0.02431  105 THR A O   
832  C CB  . THR A 105 ? 0.33983 0.43292 0.43681 0.08934  -0.02817 0.01949  105 THR A CB  
833  O OG1 . THR A 105 ? 0.33489 0.40035 0.43567 0.06748  -0.02449 0.02272  105 THR A OG1 
834  C CG2 . THR A 105 ? 0.35995 0.49405 0.46997 0.08391  -0.03212 0.01102  105 THR A CG2 
835  N N   . THR A 106 ? 0.42228 0.52281 0.47306 0.15434  -0.03464 0.03232  106 THR A N   
836  C CA  . THR A 106 ? 0.42896 0.57203 0.47039 0.18766  -0.04063 0.02847  106 THR A CA  
837  C C   . THR A 106 ? 0.39747 0.60535 0.46390 0.17737  -0.04849 0.01410  106 THR A C   
838  O O   . THR A 106 ? 0.40512 0.60308 0.47506 0.16048  -0.04863 0.01624  106 THR A O   
839  C CB  . THR A 106 ? 0.47653 0.57310 0.47522 0.21168  -0.03540 0.04303  106 THR A CB  
840  O OG1 . THR A 106 ? 0.49975 0.53126 0.47282 0.21601  -0.02491 0.05348  106 THR A OG1 
841  C CG2 . THR A 106 ? 0.49465 0.63049 0.47650 0.23676  -0.03845 0.03585  106 THR A CG2 
842  N N   . VAL A 107 ? 0.41871 0.68588 0.49788 0.18033  -0.05192 -0.00264 107 VAL A N   
843  C CA  . VAL A 107 ? 0.43201 0.76121 0.53183 0.16430  -0.05614 -0.02154 107 VAL A CA  
844  C C   . VAL A 107 ? 0.45694 0.81878 0.53335 0.19035  -0.05928 -0.02723 107 VAL A C   
845  O O   . VAL A 107 ? 0.45836 0.83533 0.52253 0.20933  -0.05853 -0.03061 107 VAL A O   
846  C CB  . VAL A 107 ? 0.42175 0.79376 0.55451 0.13599  -0.05325 -0.04089 107 VAL A CB  
847  C CG1 . VAL A 107 ? 0.42443 0.85129 0.57229 0.11349  -0.05359 -0.06285 107 VAL A CG1 
848  C CG2 . VAL A 107 ? 0.41531 0.73763 0.55822 0.10846  -0.04605 -0.03353 107 VAL A CG2 
849  N N   . LYS A 108 ? 0.45822 0.83363 0.52688 0.19281  -0.06256 -0.02909 108 LYS A N   
850  C CA  . LYS A 108 ? 0.50037 0.90745 0.54324 0.22016  -0.06519 -0.03415 108 LYS A CA  
851  C C   . LYS A 108 ? 0.56817 1.05035 0.63212 0.20224  -0.06871 -0.06069 108 LYS A C   
852  O O   . LYS A 108 ? 0.53001 1.01906 0.61531 0.17345  -0.06889 -0.06819 108 LYS A O   
853  C CB  . LYS A 108 ? 0.48436 0.84476 0.49535 0.23939  -0.06388 -0.01550 108 LYS A CB  
854  N N   . TYR A 109 ? 0.58733 1.12543 0.64166 0.21966  -0.07019 -0.07620 109 TYR A N   
855  C CA  . TYR A 109 ? 0.62255 1.23875 0.69014 0.20636  -0.07167 -0.10498 109 TYR A CA  
856  C C   . TYR A 109 ? 0.69546 1.34374 0.73305 0.23975  -0.07523 -0.10827 109 TYR A C   
857  O O   . TYR A 109 ? 0.73169 1.33429 0.73769 0.26970  -0.07549 -0.08675 109 TYR A O   
858  C CB  . TYR A 109 ? 0.55158 1.21843 0.63248 0.19862  -0.06937 -0.12454 109 TYR A CB  
859  C CG  . TYR A 109 ? 0.61852 1.25133 0.72193 0.17445  -0.06455 -0.11888 109 TYR A CG  
860  C CD1 . TYR A 109 ? 0.58680 1.22862 0.72071 0.12965  -0.05819 -0.13361 109 TYR A CD1 
861  C CD2 . TYR A 109 ? 0.58099 1.17159 0.67115 0.19686  -0.06423 -0.10012 109 TYR A CD2 
862  C CE1 . TYR A 109 ? 0.70492 1.31742 0.85594 0.10979  -0.05223 -0.12885 109 TYR A CE1 
863  C CE2 . TYR A 109 ? 0.56128 1.12575 0.67131 0.17685  -0.05951 -0.09632 109 TYR A CE2 
864  C CZ  . TYR A 109 ? 0.63292 1.21044 0.77394 0.13411  -0.05379 -0.11041 109 TYR A CZ  
865  O OH  . TYR A 109 ? 0.63484 1.18688 0.79286 0.11534  -0.04743 -0.10680 109 TYR A OH  
866  N N   . GLY A 110 ? 0.67940 1.40748 0.72475 0.23390  -0.07592 -0.13691 110 GLY A N   
867  C CA  . GLY A 110 ? 0.63706 1.41289 0.65476 0.26836  -0.07866 -0.14535 110 GLY A CA  
868  C C   . GLY A 110 ? 0.67698 1.53971 0.69292 0.27949  -0.07873 -0.17274 110 GLY A C   
869  O O   . GLY A 110 ? 0.58636 1.49790 0.57601 0.31445  -0.08069 -0.18147 110 GLY A O   
870  N N   . LYS A 114 ? 0.69496 1.28010 0.65059 0.33462  -0.07061 -0.07313 114 LYS A N   
871  C CA  . LYS A 114 ? 0.69159 1.25339 0.64879 0.33658  -0.06781 -0.06742 114 LYS A CA  
872  C C   . LYS A 114 ? 0.65497 1.14547 0.63257 0.30830  -0.06435 -0.05055 114 LYS A C   
873  O O   . LYS A 114 ? 0.67090 1.15511 0.67291 0.27960  -0.06572 -0.05145 114 LYS A O   
874  C CB  . LYS A 114 ? 0.61176 1.25289 0.59708 0.32062  -0.07054 -0.09436 114 LYS A CB  
875  C CG  . LYS A 114 ? 0.69937 1.32861 0.68236 0.32883  -0.06811 -0.09091 114 LYS A CG  
876  C CD  . LYS A 114 ? 0.76241 1.35383 0.69316 0.37802  -0.06537 -0.07374 114 LYS A CD  
877  C CE  . LYS A 114 ? 0.72977 1.29243 0.65684 0.38404  -0.06174 -0.06693 114 LYS A CE  
878  N NZ  . LYS A 114 ? 0.82865 1.32066 0.77708 0.35542  -0.05728 -0.05174 114 LYS A NZ  
879  N N   . GLU A 115 ? 0.64445 1.08198 0.60983 0.31727  -0.05933 -0.03609 115 GLU A N   
880  C CA  . GLU A 115 ? 0.63167 1.00413 0.61242 0.29378  -0.05530 -0.02137 115 GLU A CA  
881  C C   . GLU A 115 ? 0.59664 0.96898 0.59864 0.28080  -0.05323 -0.02547 115 GLU A C   
882  O O   . GLU A 115 ? 0.62869 1.01764 0.61640 0.30105  -0.05220 -0.02964 115 GLU A O   
883  C CB  . GLU A 115 ? 0.63057 0.91858 0.57039 0.31329  -0.04753 0.00273  115 GLU A CB  
884  C CG  . GLU A 115 ? 0.71494 0.98193 0.64932 0.30691  -0.04767 0.01075  115 GLU A CG  
885  C CD  . GLU A 115 ? 0.80731 0.98635 0.70345 0.31719  -0.03675 0.03306  115 GLU A CD  
886  O OE1 . GLU A 115 ? 0.86692 0.99821 0.74830 0.32089  -0.02914 0.04094  115 GLU A OE1 
887  O OE2 . GLU A 115 ? 0.73016 0.88754 0.60973 0.31976  -0.03436 0.04129  115 GLU A OE2 
888  N N   . ALA A 116 ? 0.55180 0.90633 0.58619 0.24826  -0.05219 -0.02442 116 ALA A N   
889  C CA  . ALA A 116 ? 0.48648 0.82579 0.53807 0.23570  -0.04832 -0.02446 116 ALA A CA  
890  C C   . ALA A 116 ? 0.48674 0.75554 0.53750 0.22460  -0.04405 -0.00749 116 ALA A C   
891  O O   . ALA A 116 ? 0.46678 0.72542 0.52918 0.20754  -0.04567 -0.00397 116 ALA A O   
892  C CB  . ALA A 116 ? 0.44987 0.84850 0.54305 0.20343  -0.04889 -0.04502 116 ALA A CB  
893  N N   . THR A 117 ? 0.48791 0.71126 0.52456 0.23320  -0.03824 0.00101  117 THR A N   
894  C CA  . THR A 117 ? 0.51199 0.66907 0.54424 0.22238  -0.03273 0.01419  117 THR A CA  
895  C C   . THR A 117 ? 0.47350 0.63836 0.53355 0.20037  -0.03074 0.00683  117 THR A C   
896  O O   . THR A 117 ? 0.45705 0.66101 0.52816 0.20730  -0.03104 -0.00376 117 THR A O   
897  C CB  . THR A 117 ? 0.57496 0.66220 0.55943 0.24482  -0.02388 0.02815  117 THR A CB  
898  O OG1 . THR A 117 ? 0.59385 0.66838 0.55088 0.25876  -0.02323 0.03568  117 THR A OG1 
899  C CG2 . THR A 117 ? 0.68403 0.70232 0.66036 0.22987  -0.01570 0.03781  117 THR A CG2 
900  N N   . TYR A 118 ? 0.46609 0.59258 0.53392 0.16692  -0.02712 0.01121  118 TYR A N   
901  C CA  . TYR A 118 ? 0.39436 0.51208 0.47736 0.14132  -0.02295 0.00656  118 TYR A CA  
902  C C   . TYR A 118 ? 0.43446 0.48877 0.50290 0.12652  -0.01787 0.01675  118 TYR A C   
903  O O   . TYR A 118 ? 0.43563 0.46362 0.49412 0.12257  -0.01749 0.02478  118 TYR A O   
904  C CB  . TYR A 118 ? 0.37098 0.52627 0.48341 0.11146  -0.02345 -0.00379 118 TYR A CB  
905  C CG  . TYR A 118 ? 0.39464 0.61970 0.52520 0.11545  -0.02679 -0.01861 118 TYR A CG  
906  C CD1 . TYR A 118 ? 0.42000 0.67208 0.55061 0.12501  -0.03276 -0.02040 118 TYR A CD1 
907  C CD2 . TYR A 118 ? 0.37457 0.64352 0.52207 0.10853  -0.02323 -0.03286 118 TYR A CD2 
908  C CE1 . TYR A 118 ? 0.42826 0.75534 0.57695 0.12732  -0.03627 -0.03818 118 TYR A CE1 
909  C CE2 . TYR A 118 ? 0.40833 0.75181 0.57487 0.10829  -0.02503 -0.05094 118 TYR A CE2 
910  C CZ  . TYR A 118 ? 0.42884 0.80402 0.59668 0.11757  -0.03213 -0.05460 118 TYR A CZ  
911  O OH  . TYR A 118 ? 0.41378 0.85235 0.59097 0.11033  -0.03274 -0.07387 118 TYR A OH  
912  N N   . LEU A 119 ? 0.38530 0.42107 0.45361 0.11675  -0.01365 0.01450  119 LEU A N   
913  C CA  . LEU A 119 ? 0.37344 0.36428 0.43313 0.09852  -0.00938 0.01892  119 LEU A CA  
914  C C   . LEU A 119 ? 0.37332 0.38104 0.45364 0.07451  -0.01042 0.01441  119 LEU A C   
915  O O   . LEU A 119 ? 0.39089 0.42472 0.48275 0.07250  -0.00980 0.00775  119 LEU A O   
916  C CB  . LEU A 119 ? 0.43557 0.38789 0.47219 0.10764  -0.00271 0.01864  119 LEU A CB  
917  C CG  . LEU A 119 ? 0.49311 0.38553 0.49734 0.10968  0.00601  0.02443  119 LEU A CG  
918  C CD1 . LEU A 119 ? 0.51159 0.38944 0.49777 0.12584  0.00736  0.03356  119 LEU A CD1 
919  C CD2 . LEU A 119 ? 0.51861 0.38288 0.49826 0.12772  0.01304  0.02171  119 LEU A CD2 
920  N N   . ALA A 120 ? 0.34728 0.34037 0.42920 0.05803  -0.01065 0.01801  120 ALA A N   
921  C CA  . ALA A 120 ? 0.32413 0.32737 0.41701 0.04184  -0.01071 0.01574  120 ALA A CA  
922  C C   . ALA A 120 ? 0.34358 0.32533 0.42828 0.03295  -0.00929 0.01538  120 ALA A C   
923  O O   . ALA A 120 ? 0.36681 0.32780 0.44208 0.03011  -0.00778 0.01714  120 ALA A O   
924  C CB  . ALA A 120 ? 0.28974 0.30493 0.39113 0.03360  -0.01253 0.01831  120 ALA A CB  
925  N N   . LEU A 121 ? 0.30055 0.28896 0.38684 0.02810  -0.00842 0.01156  121 LEU A N   
926  C CA  . LEU A 121 ? 0.30103 0.28393 0.38205 0.01975  -0.00867 0.00833  121 LEU A CA  
927  C C   . LEU A 121 ? 0.30304 0.29964 0.38769 0.01512  -0.01112 0.01134  121 LEU A C   
928  O O   . LEU A 121 ? 0.29279 0.29467 0.37570 0.00944  -0.01308 0.00854  121 LEU A O   
929  C CB  . LEU A 121 ? 0.32703 0.31141 0.40311 0.02194  -0.00667 0.00248  121 LEU A CB  
930  C CG  . LEU A 121 ? 0.32865 0.31896 0.39910 0.01579  -0.00792 -0.00341 121 LEU A CG  
931  C CD1 . LEU A 121 ? 0.31645 0.29503 0.38164 0.00556  -0.00705 -0.01043 121 LEU A CD1 
932  C CD2 . LEU A 121 ? 0.32183 0.31441 0.38597 0.02071  -0.00547 -0.00817 121 LEU A CD2 
933  N N   . ASN A 122 ? 0.25670 0.25981 0.34383 0.01755  -0.00959 0.01549  122 ASN A N   
934  C CA  . ASN A 122 ? 0.27010 0.27678 0.35313 0.01763  -0.00974 0.01984  122 ASN A CA  
935  C C   . ASN A 122 ? 0.30304 0.30929 0.39180 0.01586  -0.01106 0.02375  122 ASN A C   
936  O O   . ASN A 122 ? 0.27472 0.28501 0.36430 0.01475  -0.01422 0.02501  122 ASN A O   
937  C CB  . ASN A 122 ? 0.27138 0.27286 0.34381 0.02010  -0.00291 0.02201  122 ASN A CB  
938  C CG  . ASN A 122 ? 0.31926 0.32170 0.37697 0.02714  -0.00219 0.02195  122 ASN A CG  
939  O OD1 . ASN A 122 ? 0.28471 0.30011 0.34341 0.02895  -0.00834 0.01781  122 ASN A OD1 
940  N ND2 . ASN A 122 ? 0.33093 0.32003 0.37220 0.03029  0.00688  0.02529  122 ASN A ND2 
941  N N   . GLU A 123 ? 0.28112 0.28770 0.37406 0.01464  -0.00830 0.02387  123 GLU A N   
942  C CA  . GLU A 123 ? 0.26567 0.27394 0.36213 0.01335  -0.00959 0.02637  123 GLU A CA  
943  C C   . GLU A 123 ? 0.32327 0.34272 0.42692 0.01136  -0.00764 0.02176  123 GLU A C   
944  O O   . GLU A 123 ? 0.29300 0.32056 0.39900 0.00913  -0.00355 0.01628  123 GLU A O   
945  C CB  . GLU A 123 ? 0.27750 0.27849 0.36392 0.01350  -0.00641 0.03000  123 GLU A CB  
946  C CG  . GLU A 123 ? 0.30499 0.29369 0.37983 0.00939  0.00370  0.02842  123 GLU A CG  
947  C CD  . GLU A 123 ? 0.33282 0.31427 0.39715 0.01155  0.00873  0.02820  123 GLU A CD  
948  O OE1 . GLU A 123 ? 0.29320 0.26992 0.34479 0.02138  0.00738  0.03261  123 GLU A OE1 
949  O OE2 . GLU A 123 ? 0.30551 0.29129 0.37428 0.00461  0.01382  0.02268  123 GLU A OE2 
950  N N   . SER A 124 ? 0.30823 0.33382 0.41554 0.01187  -0.01031 0.02245  124 SER A N   
951  C CA  . SER A 124 ? 0.27830 0.32425 0.39263 0.00884  -0.00898 0.01511  124 SER A CA  
952  C C   . SER A 124 ? 0.31622 0.35715 0.42618 0.00092  -0.00566 0.01430  124 SER A C   
953  O O   . SER A 124 ? 0.31358 0.34385 0.41907 0.00478  -0.00884 0.02103  124 SER A O   
954  C CB  . SER A 124 ? 0.31627 0.37811 0.43508 0.02156  -0.01563 0.01507  124 SER A CB  
955  O OG  . SER A 124 ? 0.33316 0.42787 0.46029 0.02077  -0.01605 0.00527  124 SER A OG  
956  N N   . THR A 125 ? 0.35012 0.39921 0.46020 -0.01166 0.00228  0.00436  125 THR A N   
957  C CA  . THR A 125 ? 0.33647 0.37356 0.43716 -0.02144 0.00869  0.00127  125 THR A CA  
958  C C   . THR A 125 ? 0.34083 0.41067 0.45174 -0.03297 0.01057  -0.01423 125 THR A C   
959  O O   . THR A 125 ? 0.31542 0.41705 0.43853 -0.03783 0.01157  -0.02505 125 THR A O   
960  C CB  . THR A 125 ? 0.34895 0.34915 0.42768 -0.03017 0.02304  0.00249  125 THR A CB  
961  O OG1 . THR A 125 ? 0.36874 0.37584 0.44761 -0.04724 0.03478  -0.00975 125 THR A OG1 
962  C CG2 . THR A 125 ? 0.34145 0.32199 0.41057 -0.01648 0.02055  0.01482  125 THR A CG2 
963  N N   . VAL A 126 ? 0.34757 0.41432 0.45339 -0.03691 0.01106  -0.01683 126 VAL A N   
964  C CA  . VAL A 126 ? 0.33444 0.43452 0.44781 -0.04989 0.01306  -0.03422 126 VAL A CA  
965  C C   . VAL A 126 ? 0.34674 0.41300 0.44017 -0.06992 0.02876  -0.04147 126 VAL A C   
966  O O   . VAL A 126 ? 0.35041 0.37927 0.42681 -0.06233 0.03001  -0.03027 126 VAL A O   
967  C CB  . VAL A 126 ? 0.33663 0.46350 0.45784 -0.03375 -0.00084 -0.03149 126 VAL A CB  
968  C CG1 . VAL A 126 ? 0.34795 0.52582 0.48015 -0.04373 -0.00144 -0.05238 126 VAL A CG1 
969  C CG2 . VAL A 126 ? 0.35367 0.48865 0.48120 -0.01086 -0.01217 -0.01912 126 VAL A CG2 
970  N N   . LYS A 127 ? 0.35721 0.43601 0.45035 -0.09555 0.04240  -0.06120 127 LYS A N   
971  C CA  . LYS A 127 ? 0.45084 0.49643 0.52101 -0.12066 0.06177  -0.07379 127 LYS A CA  
972  C C   . LYS A 127 ? 0.48845 0.58996 0.57514 -0.14488 0.06477  -0.10202 127 LYS A C   
973  O O   . LYS A 127 ? 0.45806 0.62282 0.57168 -0.14373 0.05585  -0.11256 127 LYS A O   
974  C CB  . LYS A 127 ? 0.47062 0.46271 0.51388 -0.13559 0.08394  -0.07248 127 LYS A CB  
975  C CG  . LYS A 127 ? 0.51478 0.46533 0.54328 -0.10957 0.07983  -0.04726 127 LYS A CG  
976  C CD  . LYS A 127 ? 0.58344 0.48198 0.58032 -0.12062 0.10252  -0.04540 127 LYS A CD  
977  C CE  . LYS A 127 ? 0.63046 0.49827 0.61260 -0.09118 0.09632  -0.02200 127 LYS A CE  
978  N NZ  . LYS A 127 ? 0.62143 0.44323 0.57145 -0.09432 0.11566  -0.01710 127 LYS A NZ  
979  N N   . SER A 128 ? 0.52279 0.60386 0.59170 -0.16614 0.07797  -0.11610 128 SER A N   
980  C CA  . SER A 128 ? 0.59790 0.73869 0.68246 -0.19283 0.08146  -0.14743 128 SER A CA  
981  C C   . SER A 128 ? 0.65986 0.81778 0.74693 -0.22482 0.10017  -0.16858 128 SER A C   
982  O O   . SER A 128 ? 0.64791 0.74968 0.71244 -0.23191 0.11699  -0.15964 128 SER A O   
983  C CB  . SER A 128 ? 0.68060 0.79092 0.74192 -0.21162 0.09365  -0.16023 128 SER A CB  
984  O OG  . SER A 128 ? 0.72644 0.90728 0.80543 -0.23262 0.09295  -0.19101 128 SER A OG  
985  N N   . SER A 129 ? 0.66881 0.89778 0.77108 -0.23129 0.09603  -0.19151 129 SER A N   
986  C CA  . SER A 129 ? 0.74422 0.99601 0.84263 -0.25024 0.11074  -0.20983 129 SER A CA  
987  C C   . SER A 129 ? 0.91840 1.13943 0.98490 -0.28422 0.13823  -0.23138 129 SER A C   
988  O O   . SER A 129 ? 0.90682 1.18126 0.97779 -0.30138 0.14563  -0.25761 129 SER A O   
989  C CB  . SER A 129 ? 0.66012 1.00936 0.78961 -0.23456 0.09196  -0.22323 129 SER A CB  
990  O OG  . SER A 129 ? 0.73693 1.13057 0.86767 -0.23984 0.08943  -0.24329 129 SER A OG  
991  N N   . GLY A 130 ? 1.22032 1.35557 1.25107 -0.29304 0.15528  -0.22147 130 GLY A N   
992  C CA  . GLY A 130 ? 1.20345 1.30101 1.19780 -0.32311 0.18419  -0.24016 130 GLY A CA  
993  C C   . GLY A 130 ? 1.27408 1.33935 1.25117 -0.32426 0.18663  -0.23997 130 GLY A C   
994  O O   . GLY A 130 ? 1.31358 1.29922 1.24595 -0.33602 0.21128  -0.23715 130 GLY A O   
995  N N   . GLY A 131 ? 1.09242 1.21744 1.10078 -0.30968 0.16187  -0.24266 131 GLY A N   
996  C CA  . GLY A 131 ? 1.06687 1.16875 1.06143 -0.31046 0.16212  -0.24445 131 GLY A CA  
997  C C   . GLY A 131 ? 1.04742 1.08341 1.02918 -0.28671 0.15294  -0.21635 131 GLY A C   
998  O O   . GLY A 131 ? 1.06521 1.05224 1.03650 -0.27427 0.15525  -0.19493 131 GLY A O   
999  N N   . PRO A 132 ? 0.88289 0.91798 0.86323 -0.27931 0.14311  -0.21725 132 PRO A N   
1000 C CA  . PRO A 132 ? 0.80666 0.78889 0.77601 -0.25356 0.13241  -0.19294 132 PRO A CA  
1001 C C   . PRO A 132 ? 0.73347 0.77736 0.74154 -0.21430 0.09955  -0.17175 132 PRO A C   
1002 O O   . PRO A 132 ? 0.73544 0.85879 0.77377 -0.20974 0.08136  -0.18381 132 PRO A O   
1003 C CB  . PRO A 132 ? 0.78228 0.74411 0.73008 -0.25776 0.13652  -0.20328 132 PRO A CB  
1004 C CG  . PRO A 132 ? 0.81992 0.86867 0.79330 -0.27680 0.13237  -0.23171 132 PRO A CG  
1005 C CD  . PRO A 132 ? 0.85457 0.93739 0.84009 -0.29324 0.14311  -0.24149 132 PRO A CD  
1006 N N   . PHE A 133 ? 0.62819 0.63395 0.63107 -0.18485 0.09307  -0.14089 133 PHE A N   
1007 C CA  . PHE A 133 ? 0.52548 0.57484 0.55794 -0.15094 0.06670  -0.12055 133 PHE A CA  
1008 C C   . PHE A 133 ? 0.46946 0.51718 0.49889 -0.12607 0.05302  -0.10726 133 PHE A C   
1009 O O   . PHE A 133 ? 0.47288 0.46322 0.47650 -0.11525 0.05978  -0.09301 133 PHE A O   
1010 C CB  . PHE A 133 ? 0.51117 0.52292 0.53848 -0.13530 0.06774  -0.09751 133 PHE A CB  
1011 C CG  . PHE A 133 ? 0.45279 0.50011 0.50605 -0.10598 0.04525  -0.07891 133 PHE A CG  
1012 C CD1 . PHE A 133 ? 0.43190 0.53607 0.51246 -0.10572 0.03565  -0.08620 133 PHE A CD1 
1013 C CD2 . PHE A 133 ? 0.44429 0.46599 0.49150 -0.07926 0.03609  -0.05524 133 PHE A CD2 
1014 C CE1 . PHE A 133 ? 0.43153 0.55578 0.52793 -0.07865 0.01858  -0.06897 133 PHE A CE1 
1015 C CE2 . PHE A 133 ? 0.39699 0.44351 0.46341 -0.05738 0.01955  -0.04013 133 PHE A CE2 
1016 C CZ  . PHE A 133 ? 0.39647 0.48873 0.48495 -0.05684 0.01157  -0.04638 133 PHE A CZ  
1017 N N   . VAL A 134 ? 0.45662 0.56856 0.50951 -0.11506 0.03484  -0.11222 134 VAL A N   
1018 C CA  . VAL A 134 ? 0.41427 0.53285 0.46622 -0.09011 0.02096  -0.09881 134 VAL A CA  
1019 C C   . VAL A 134 ? 0.41370 0.58117 0.48881 -0.06498 0.00130  -0.08708 134 VAL A C   
1020 O O   . VAL A 134 ? 0.41943 0.64621 0.51154 -0.06735 -0.00559 -0.10249 134 VAL A O   
1021 C CB  . VAL A 134 ? 0.42300 0.56469 0.46824 -0.10256 0.02258  -0.12025 134 VAL A CB  
1022 C CG1 . VAL A 134 ? 0.39708 0.53062 0.43454 -0.07750 0.01254  -0.10386 134 VAL A CG1 
1023 C CG2 . VAL A 134 ? 0.47778 0.57466 0.49757 -0.13616 0.04665  -0.14081 134 VAL A CG2 
1024 N N   . VAL A 135 ? 0.35295 0.49681 0.42615 -0.04076 -0.00624 -0.06140 135 VAL A N   
1025 C CA  . VAL A 135 ? 0.34142 0.51684 0.42692 -0.01685 -0.02084 -0.04926 135 VAL A CA  
1026 C C   . VAL A 135 ? 0.34933 0.50624 0.42481 0.00281  -0.02613 -0.03042 135 VAL A C   
1027 O O   . VAL A 135 ? 0.36684 0.48381 0.43227 0.00193  -0.02010 -0.02011 135 VAL A O   
1028 C CB  . VAL A 135 ? 0.34057 0.50737 0.43529 -0.01151 -0.02179 -0.03863 135 VAL A CB  
1029 C CG1 . VAL A 135 ? 0.40973 0.60414 0.51608 -0.02920 -0.01689 -0.05752 135 VAL A CG1 
1030 C CG2 . VAL A 135 ? 0.32437 0.43756 0.41000 -0.01112 -0.01532 -0.02185 135 VAL A CG2 
1031 N N   . ASP A 136 ? 0.33859 0.52554 0.41417 0.02253  -0.03634 -0.02573 136 ASP A N   
1032 C CA  . ASP A 136 ? 0.32172 0.48783 0.38554 0.04018  -0.03871 -0.00618 136 ASP A CA  
1033 C C   . ASP A 136 ? 0.31976 0.46198 0.38503 0.04888  -0.03841 0.01108  136 ASP A C   
1034 O O   . ASP A 136 ? 0.35000 0.50593 0.42138 0.05461  -0.04160 0.00983  136 ASP A O   
1035 C CB  . ASP A 136 ? 0.34739 0.54668 0.40177 0.05905  -0.04662 -0.00725 136 ASP A CB  
1036 C CG  . ASP A 136 ? 0.37242 0.58909 0.42190 0.05014  -0.04609 -0.02263 136 ASP A CG  
1037 O OD1 . ASP A 136 ? 0.40393 0.58855 0.44890 0.03671  -0.03816 -0.02257 136 ASP A OD1 
1038 O OD2 . ASP A 136 ? 0.41833 0.68216 0.46614 0.05834  -0.05337 -0.03578 136 ASP A OD2 
1039 N N   . VAL A 137 ? 0.34091 0.45018 0.40100 0.04802  -0.03360 0.02453  137 VAL A N   
1040 C CA  . VAL A 137 ? 0.32278 0.40896 0.38408 0.05012  -0.03117 0.03738  137 VAL A CA  
1041 C C   . VAL A 137 ? 0.34793 0.42266 0.39412 0.06275  -0.02970 0.05090  137 VAL A C   
1042 O O   . VAL A 137 ? 0.34034 0.40950 0.37964 0.06201  -0.02651 0.05504  137 VAL A O   
1043 C CB  . VAL A 137 ? 0.31461 0.37981 0.38043 0.03870  -0.02555 0.03955  137 VAL A CB  
1044 C CG1 . VAL A 137 ? 0.28027 0.32999 0.34785 0.03885  -0.02328 0.04969  137 VAL A CG1 
1045 C CG2 . VAL A 137 ? 0.27030 0.33426 0.34171 0.02733  -0.02302 0.02818  137 VAL A CG2 
1046 N N   . VAL A 138 ? 0.34618 0.41341 0.38316 0.07480  -0.02988 0.05783  138 VAL A N   
1047 C CA  . VAL A 138 ? 0.37010 0.41621 0.38274 0.08820  -0.02466 0.07113  138 VAL A CA  
1048 C C   . VAL A 138 ? 0.40286 0.41352 0.40935 0.08198  -0.01591 0.07979  138 VAL A C   
1049 O O   . VAL A 138 ? 0.40258 0.40939 0.41264 0.08458  -0.01744 0.07786  138 VAL A O   
1050 C CB  . VAL A 138 ? 0.40163 0.46472 0.39689 0.11390  -0.03017 0.07151  138 VAL A CB  
1051 C CG1 . VAL A 138 ? 0.42556 0.45711 0.38589 0.13105  -0.02187 0.08729  138 VAL A CG1 
1052 C CG2 . VAL A 138 ? 0.39660 0.50502 0.40231 0.11499  -0.03933 0.05704  138 VAL A CG2 
1053 N N   . ILE A 139 ? 0.41701 0.40476 0.41461 0.07162  -0.00575 0.08704  139 ILE A N   
1054 C CA  . ILE A 139 ? 0.39440 0.35041 0.38515 0.05928  0.00530  0.09144  139 ILE A CA  
1055 C C   . ILE A 139 ? 0.44882 0.36402 0.40172 0.06841  0.01870  0.10350  139 ILE A C   
1056 O O   . ILE A 139 ? 0.45277 0.36198 0.39234 0.06663  0.02588  0.10880  139 ILE A O   
1057 C CB  . ILE A 139 ? 0.37812 0.34466 0.38718 0.03667  0.00939  0.08677  139 ILE A CB  
1058 C CG1 . ILE A 139 ? 0.31114 0.30823 0.34723 0.03333  -0.00147 0.07729  139 ILE A CG1 
1059 C CG2 . ILE A 139 ? 0.38400 0.32509 0.38682 0.01991  0.02149  0.08682  139 ILE A CG2 
1060 C CD1 . ILE A 139 ? 0.27085 0.28702 0.32108 0.02163  0.00019  0.07299  139 ILE A CD1 
1061 N N   . ASN A 140 ? 0.44251 0.32446 0.37362 0.07871  0.02434  0.10826  140 ASN A N   
1062 C CA  . ASN A 140 ? 0.50189 0.33000 0.38551 0.09115  0.04084  0.12127  140 ASN A CA  
1063 C C   . ASN A 140 ? 0.55825 0.39413 0.41983 0.11601  0.03815  0.12943  140 ASN A C   
1064 O O   . ASN A 140 ? 0.54998 0.35268 0.38013 0.11584  0.05300  0.13934  140 ASN A O   
1065 C CB  . ASN A 140 ? 0.47166 0.26142 0.34325 0.06091  0.06167  0.12220  140 ASN A CB  
1066 C CG  . ASN A 140 ? 0.53222 0.31965 0.42399 0.03735  0.06365  0.11158  140 ASN A CG  
1067 O OD1 . ASN A 140 ? 0.50297 0.27490 0.38795 0.04913  0.06104  0.11131  140 ASN A OD1 
1068 N ND2 . ASN A 140 ? 0.48478 0.29408 0.40141 0.00650  0.06742  0.10180  140 ASN A ND2 
1069 N N   . ASP A 141 ? 0.51051 0.39354 0.38821 0.13610  0.01986  0.12349  141 ASP A N   
1070 C CA  . ASP A 141 ? 0.57080 0.47708 0.43231 0.16214  0.01296  0.12664  141 ASP A CA  
1071 C C   . ASP A 141 ? 0.54072 0.46923 0.41618 0.14714  0.01172  0.12368  141 ASP A C   
1072 O O   . ASP A 141 ? 0.61501 0.56420 0.47744 0.16591  0.00638  0.12487  141 ASP A O   
1073 C CB  . ASP A 141 ? 0.65184 0.51283 0.46021 0.18850  0.02588  0.13931  141 ASP A CB  
1074 C CG  . ASP A 141 ? 0.70955 0.55427 0.50617 0.20194  0.02745  0.13618  141 ASP A CG  
1075 O OD1 . ASP A 141 ? 0.66372 0.55266 0.48937 0.20679  0.01214  0.12562  141 ASP A OD1 
1076 O OD2 . ASP A 141 ? 0.79976 0.58806 0.55747 0.20676  0.04514  0.14309  141 ASP A OD2 
1077 N N   . ILE A 142 ? 0.53835 0.49434 0.38786 0.07805  -0.05552 0.09090  142 ILE A N   
1078 C CA  . ILE A 142 ? 0.57854 0.54125 0.40581 0.07492  -0.04661 0.08388  142 ILE A CA  
1079 C C   . ILE A 142 ? 0.51524 0.49019 0.35976 0.07418  -0.05115 0.06411  142 ILE A C   
1080 O O   . ILE A 142 ? 0.48540 0.46518 0.36137 0.07002  -0.04647 0.05766  142 ILE A O   
1081 C CB  . ILE A 142 ? 0.64812 0.61043 0.47480 0.06687  -0.02530 0.09020  142 ILE A CB  
1082 C CG1 . ILE A 142 ? 0.77420 0.72138 0.58088 0.06392  -0.02032 0.11130  142 ILE A CG1 
1083 C CG2 . ILE A 142 ? 0.75331 0.72748 0.56391 0.06682  -0.01478 0.07981  142 ILE A CG2 
1084 C CD1 . ILE A 142 ? 0.76283 0.69952 0.53410 0.07171  -0.03320 0.12132  142 ILE A CD1 
1085 N N   . HIS A 143 ? 0.54206 0.51942 0.36352 0.07744  -0.06043 0.05451  143 HIS A N   
1086 C CA  A HIS A 143 ? 0.51092 0.49380 0.34519 0.07495  -0.06592 0.03591  143 HIS A CA  
1087 C CA  B HIS A 143 ? 0.53978 0.52255 0.37311 0.07507  -0.06600 0.03596  143 HIS A CA  
1088 C C   . HIS A 143 ? 0.50281 0.48544 0.33889 0.07250  -0.04816 0.02883  143 HIS A C   
1089 O O   . HIS A 143 ? 0.50678 0.48776 0.31389 0.07608  -0.03918 0.02688  143 HIS A O   
1090 C CB  A HIS A 143 ? 0.53250 0.51403 0.33922 0.07791  -0.08191 0.02530  143 HIS A CB  
1091 C CB  B HIS A 143 ? 0.53018 0.51119 0.33300 0.07862  -0.08167 0.02694  143 HIS A CB  
1092 C CG  A HIS A 143 ? 0.53650 0.51688 0.35274 0.07321  -0.08621 0.00623  143 HIS A CG  
1093 C CG  B HIS A 143 ? 0.53883 0.52628 0.34930 0.08064  -0.10350 0.02968  143 HIS A CG  
1094 N ND1 A HIS A 143 ? 0.53595 0.50788 0.33459 0.07471  -0.07507 -0.00471 143 HIS A ND1 
1095 N ND1 B HIS A 143 ? 0.56051 0.55785 0.39562 0.07578  -0.11853 0.01783  143 HIS A ND1 
1096 C CD2 A HIS A 143 ? 0.50294 0.48852 0.34583 0.06665  -0.09946 -0.00287 143 HIS A CD2 
1097 C CD2 B HIS A 143 ? 0.55578 0.54292 0.35451 0.08727  -0.11309 0.04378  143 HIS A CD2 
1098 C CE1 A HIS A 143 ? 0.51860 0.48493 0.32924 0.06960  -0.08271 -0.01971 143 HIS A CE1 
1099 C CE1 B HIS A 143 ? 0.57100 0.57874 0.41169 0.07990  -0.13645 0.02367  143 HIS A CE1 
1100 N NE2 A HIS A 143 ? 0.49850 0.47363 0.33610 0.06296  -0.09728 -0.01837 143 HIS A NE2 
1101 N NE2 B HIS A 143 ? 0.57041 0.57056 0.38817 0.08827  -0.13412 0.03931  143 HIS A NE2 
1102 N N   . PHE A 144 ? 0.41483 0.40073 0.28435 0.06774  -0.04345 0.02469  144 PHE A N   
1103 C CA  . PHE A 144 ? 0.41977 0.40694 0.29611 0.06664  -0.02816 0.01920  144 PHE A CA  
1104 C C   . PHE A 144 ? 0.41439 0.39538 0.28530 0.06794  -0.03231 0.00186  144 PHE A C   
1105 O O   . PHE A 144 ? 0.40076 0.37977 0.25543 0.07327  -0.02219 -0.00440 144 PHE A O   
1106 C CB  . PHE A 144 ? 0.33562 0.32707 0.24705 0.06127  -0.02158 0.02422  144 PHE A CB  
1107 C CG  . PHE A 144 ? 0.32754 0.32273 0.24770 0.06072  -0.00786 0.02014  144 PHE A CG  
1108 C CD1 . PHE A 144 ? 0.32862 0.33111 0.23935 0.06173  0.00659  0.02698  144 PHE A CD1 
1109 C CD2 . PHE A 144 ? 0.33519 0.32848 0.27420 0.05883  -0.00932 0.01067  144 PHE A CD2 
1110 C CE1 . PHE A 144 ? 0.33801 0.34912 0.26009 0.06261  0.01822  0.02316  144 PHE A CE1 
1111 C CE2 . PHE A 144 ? 0.31389 0.31077 0.26085 0.06036  0.00201  0.00764  144 PHE A CE2 
1112 C CZ  . PHE A 144 ? 0.33136 0.33877 0.27110 0.06309  0.01514  0.01326  144 PHE A CZ  
1113 N N   . GLU A 145 ? 0.37140 0.34917 0.25709 0.06302  -0.04629 -0.00596 145 GLU A N   
1114 C CA  . GLU A 145 ? 0.39456 0.36018 0.27437 0.06209  -0.05034 -0.02163 145 GLU A CA  
1115 C C   . GLU A 145 ? 0.41003 0.37433 0.30052 0.05375  -0.06933 -0.02795 145 GLU A C   
1116 O O   . GLU A 145 ? 0.39720 0.37509 0.30906 0.04977  -0.07631 -0.01999 145 GLU A O   
1117 C CB  . GLU A 145 ? 0.35876 0.32197 0.25879 0.06122  -0.03827 -0.02356 145 GLU A CB  
1118 C CG  . GLU A 145 ? 0.36890 0.33921 0.30531 0.05220  -0.04055 -0.01815 145 GLU A CG  
1119 C CD  . GLU A 145 ? 0.34171 0.30985 0.29558 0.05140  -0.02967 -0.01833 145 GLU A CD  
1120 O OE1 . GLU A 145 ? 0.35867 0.32160 0.30129 0.05853  -0.02046 -0.02215 145 GLU A OE1 
1121 O OE2 . GLU A 145 ? 0.32759 0.30104 0.30666 0.04456  -0.03053 -0.01448 145 GLU A OE2 
1122 N N   . ARG A 146 ? 0.41114 0.35915 0.28649 0.05130  -0.07801 -0.04280 146 ARG A N   
1123 C CA  . ARG A 146 ? 0.47472 0.42076 0.36417 0.03912  -0.09543 -0.05013 146 ARG A CA  
1124 C C   . ARG A 146 ? 0.40347 0.33756 0.31229 0.03184  -0.09002 -0.05449 146 ARG A C   
1125 O O   . ARG A 146 ? 0.44086 0.35205 0.33083 0.03597  -0.08580 -0.06418 146 ARG A O   
1126 C CB  . ARG A 146 ? 0.50181 0.43351 0.35801 0.03857  -0.11173 -0.06386 146 ARG A CB  
1127 C CG  . ARG A 146 ? 0.52346 0.45553 0.39481 0.02280  -0.13216 -0.07163 146 ARG A CG  
1128 C CD  . ARG A 146 ? 0.56594 0.49185 0.40612 0.02146  -0.15280 -0.08278 146 ARG A CD  
1129 N NE  . ARG A 146 ? 0.52210 0.47479 0.36704 0.02508  -0.16172 -0.07194 146 ARG A NE  
1130 C CZ  . ARG A 146 ? 0.62833 0.58515 0.45149 0.02491  -0.18157 -0.07699 146 ARG A CZ  
1131 N NH1 . ARG A 146 ? 0.63862 0.57353 0.43051 0.02034  -0.19527 -0.09458 146 ARG A NH1 
1132 N NH2 . ARG A 146 ? 0.58884 0.57041 0.41978 0.03032  -0.18898 -0.06441 146 ARG A NH2 
1133 N N   . PHE A 147 ? 0.40191 0.35074 0.34624 0.02258  -0.08970 -0.04703 147 PHE A N   
1134 C CA  . PHE A 147 ? 0.38051 0.31953 0.34255 0.01549  -0.08307 -0.04769 147 PHE A CA  
1135 C C   . PHE A 147 ? 0.40636 0.33484 0.37455 -0.00064 -0.09755 -0.05592 147 PHE A C   
1136 O O   . PHE A 147 ? 0.40109 0.34986 0.38913 -0.01112 -0.10877 -0.05379 147 PHE A O   
1137 C CB  . PHE A 147 ? 0.38038 0.34044 0.37467 0.01388  -0.07280 -0.03517 147 PHE A CB  
1138 C CG  . PHE A 147 ? 0.33232 0.28276 0.34141 0.00661  -0.06609 -0.03452 147 PHE A CG  
1139 C CD1 . PHE A 147 ? 0.35434 0.30559 0.38055 -0.00897 -0.07383 -0.03584 147 PHE A CD1 
1140 C CD2 . PHE A 147 ? 0.35132 0.29238 0.35567 0.01484  -0.05275 -0.03213 147 PHE A CD2 
1141 C CE1 . PHE A 147 ? 0.36446 0.30390 0.39975 -0.01622 -0.06742 -0.03353 147 PHE A CE1 
1142 C CE2 . PHE A 147 ? 0.34189 0.27242 0.35606 0.00934  -0.04794 -0.03050 147 PHE A CE2 
1143 C CZ  . PHE A 147 ? 0.34450 0.27214 0.37206 -0.00607 -0.05492 -0.03076 147 PHE A CZ  
1144 N N   . ARG A 148 ? 0.40412 0.30116 0.35647 -0.00275 -0.09748 -0.06488 148 ARG A N   
1145 C CA  . ARG A 148 ? 0.45468 0.33426 0.41193 -0.02080 -0.10973 -0.07155 148 ARG A CA  
1146 C C   . ARG A 148 ? 0.41801 0.28291 0.38739 -0.02507 -0.09912 -0.06625 148 ARG A C   
1147 O O   . ARG A 148 ? 0.43257 0.27942 0.38664 -0.01117 -0.08824 -0.06707 148 ARG A O   
1148 C CB  . ARG A 148 ? 0.50615 0.35066 0.42668 -0.02024 -0.12221 -0.08826 148 ARG A CB  
1149 C CG  . ARG A 148 ? 0.59220 0.44735 0.49575 -0.01830 -0.13586 -0.09491 148 ARG A CG  
1150 C CD  . ARG A 148 ? 0.70724 0.52265 0.57166 -0.01849 -0.14827 -0.11356 148 ARG A CD  
1151 N NE  . ARG A 148 ? 0.77515 0.60050 0.62251 -0.02052 -0.16561 -0.12099 148 ARG A NE  
1152 C CZ  . ARG A 148 ? 0.74660 0.58698 0.57392 -0.00447 -0.16245 -0.11917 148 ARG A CZ  
1153 N NH1 . ARG A 148 ? 0.68577 0.53314 0.50806 0.01349  -0.14217 -0.11094 148 ARG A NH1 
1154 N NH2 . ARG A 148 ? 0.84331 0.69274 0.65510 -0.00765 -0.18067 -0.12493 148 ARG A NH2 
1155 N N   . GLY A 149 ? 0.41044 0.28470 0.40661 -0.04386 -0.10235 -0.06045 149 GLY A N   
1156 C CA  . GLY A 149 ? 0.43149 0.29381 0.43852 -0.04896 -0.09169 -0.05263 149 GLY A CA  
1157 C C   . GLY A 149 ? 0.41577 0.30835 0.45894 -0.06671 -0.09027 -0.04206 149 GLY A C   
1158 O O   . GLY A 149 ? 0.41632 0.33243 0.47652 -0.07918 -0.10095 -0.04315 149 GLY A O   
1159 N N   . ASP A 150 ? 0.41739 0.31142 0.47164 -0.06669 -0.07684 -0.03195 150 ASP A N   
1160 C CA  . ASP A 150 ? 0.38863 0.31095 0.47438 -0.08236 -0.07213 -0.02161 150 ASP A CA  
1161 C C   . ASP A 150 ? 0.34081 0.30856 0.45051 -0.07346 -0.06583 -0.01606 150 ASP A C   
1162 O O   . ASP A 150 ? 0.37360 0.37441 0.51083 -0.08458 -0.06842 -0.01252 150 ASP A O   
1163 C CB  . ASP A 150 ? 0.34810 0.25262 0.43152 -0.08526 -0.06038 -0.01274 150 ASP A CB  
1164 C CG  . ASP A 150 ? 0.39227 0.25211 0.45744 -0.09907 -0.06760 -0.01515 150 ASP A CG  
1165 O OD1 . ASP A 150 ? 0.46269 0.30479 0.51796 -0.10827 -0.08190 -0.02489 150 ASP A OD1 
1166 O OD2 . ASP A 150 ? 0.42256 0.26179 0.48082 -0.10069 -0.05993 -0.00732 150 ASP A OD2 
1167 N N   . GLY A 151 ? 0.32120 0.29171 0.42195 -0.05370 -0.05778 -0.01513 151 GLY A N   
1168 C CA  . GLY A 151 ? 0.30774 0.31352 0.42756 -0.04493 -0.05311 -0.01032 151 GLY A CA  
1169 C C   . GLY A 151 ? 0.29110 0.29294 0.39983 -0.02702 -0.04246 -0.00773 151 GLY A C   
1170 O O   . GLY A 151 ? 0.32958 0.30683 0.41749 -0.02013 -0.03893 -0.01000 151 GLY A O   
1171 N N   . LEU A 152 ? 0.24972 0.27703 0.37378 -0.01952 -0.03797 -0.00316 152 LEU A N   
1172 C CA  . LEU A 152 ? 0.27310 0.29934 0.38985 -0.00532 -0.02944 -0.00021 152 LEU A CA  
1173 C C   . LEU A 152 ? 0.25591 0.29934 0.39064 -0.00362 -0.01923 0.00543  152 LEU A C   
1174 O O   . LEU A 152 ? 0.21478 0.28061 0.37060 -0.00859 -0.01937 0.00719  152 LEU A O   
1175 C CB  . LEU A 152 ? 0.24041 0.27278 0.35024 0.00420  -0.03617 -0.00101 152 LEU A CB  
1176 C CG  . LEU A 152 ? 0.29769 0.31178 0.38237 0.00609  -0.04390 -0.00713 152 LEU A CG  
1177 C CD1 . LEU A 152 ? 0.29407 0.31743 0.37216 0.01241  -0.05331 -0.00691 152 LEU A CD1 
1178 C CD2 . LEU A 152 ? 0.26941 0.26540 0.33489 0.01379  -0.03492 -0.00761 152 LEU A CD2 
1179 N N   . CYS A 153 ? 0.25135 0.28617 0.37756 0.00397  -0.01048 0.00756  153 CYS A N   
1180 C CA  . CYS A 153 ? 0.23668 0.28205 0.37325 0.00658  -0.00103 0.01101  153 CYS A CA  
1181 C C   . CYS A 153 ? 0.22779 0.27035 0.35824 0.01758  0.00176  0.01195  153 CYS A C   
1182 O O   . CYS A 153 ? 0.22661 0.25535 0.34234 0.02060  0.00263  0.01185  153 CYS A O   
1183 C CB  . CYS A 153 ? 0.25544 0.28930 0.38534 0.00160  0.00584  0.01284  153 CYS A CB  
1184 S SG  . CYS A 153 ? 0.24336 0.28759 0.37870 0.00575  0.01744  0.01562  153 CYS A SG  
1185 N N   . MET A 154 ? 0.22415 0.27945 0.36596 0.02364  0.00325  0.01294  154 MET A N   
1186 C CA  . MET A 154 ? 0.23776 0.28470 0.37239 0.03244  0.00520  0.01426  154 MET A CA  
1187 C C   . MET A 154 ? 0.23710 0.28533 0.37544 0.03489  0.01353  0.01333  154 MET A C   
1188 O O   . MET A 154 ? 0.18672 0.25009 0.33852 0.03773  0.01628  0.01211  154 MET A O   
1189 C CB  . MET A 154 ? 0.23102 0.28311 0.36968 0.04055  -0.00164 0.01584  154 MET A CB  
1190 C CG  . MET A 154 ? 0.27002 0.30496 0.39609 0.04708  -0.00029 0.01883  154 MET A CG  
1191 S SD  . MET A 154 ? 0.30962 0.32828 0.41439 0.04233  0.00001  0.02178  154 MET A SD  
1192 C CE  . MET A 154 ? 0.25424 0.27111 0.34982 0.04785  -0.00954 0.02622  154 MET A CE  
1193 N N   . SER A 155 ? 0.24126 0.27575 0.36770 0.03440  0.01729  0.01337  155 SER A N   
1194 C CA  . SER A 155 ? 0.22433 0.25791 0.34929 0.03448  0.02409  0.01125  155 SER A CA  
1195 C C   . SER A 155 ? 0.25082 0.27197 0.36920 0.03988  0.02456  0.00971  155 SER A C   
1196 O O   . SER A 155 ? 0.27402 0.28372 0.38514 0.03916  0.02116  0.01217  155 SER A O   
1197 C CB  . SER A 155 ? 0.20921 0.23720 0.32523 0.02808  0.02606  0.01209  155 SER A CB  
1198 O OG  . SER A 155 ? 0.26361 0.28989 0.37422 0.02817  0.03109  0.01019  155 SER A OG  
1199 N N   . THR A 156 ? 0.24266 0.26469 0.36182 0.04448  0.02916  0.00556  156 THR A N   
1200 C CA  . THR A 156 ? 0.23397 0.23819 0.34281 0.04759  0.02912  0.00223  156 THR A CA  
1201 C C   . THR A 156 ? 0.23655 0.23410 0.33497 0.03904  0.02939  0.00189  156 THR A C   
1202 O O   . THR A 156 ? 0.21589 0.22243 0.31480 0.03392  0.03045  0.00410  156 THR A O   
1203 C CB  . THR A 156 ? 0.24245 0.24886 0.35224 0.05675  0.03425  -0.00429 156 THR A CB  
1204 O OG1 . THR A 156 ? 0.25075 0.26692 0.35688 0.05250  0.04049  -0.00652 156 THR A OG1 
1205 C CG2 . THR A 156 ? 0.24345 0.26708 0.36942 0.06653  0.03471  -0.00390 156 THR A CG2 
1206 N N   . PRO A 157 ? 0.24265 0.22388 0.33167 0.03722  0.02732  -0.00076 157 PRO A N   
1207 C CA  . PRO A 157 ? 0.26503 0.24535 0.34647 0.02925  0.02639  -0.00211 157 PRO A CA  
1208 C C   . PRO A 157 ? 0.26278 0.25133 0.33908 0.03046  0.03045  -0.00593 157 PRO A C   
1209 O O   . PRO A 157 ? 0.21662 0.21395 0.29173 0.02623  0.03014  -0.00277 157 PRO A O   
1210 C CB  . PRO A 157 ? 0.30277 0.26283 0.37584 0.02606  0.02249  -0.00550 157 PRO A CB  
1211 C CG  . PRO A 157 ? 0.33105 0.27976 0.40719 0.03019  0.02069  -0.00118 157 PRO A CG  
1212 C CD  . PRO A 157 ? 0.26547 0.22682 0.35013 0.04098  0.02402  -0.00151 157 PRO A CD  
1213 N N   . SER A 158 ? 0.26770 0.25391 0.33968 0.03750  0.03485  -0.01209 158 SER A N   
1214 C CA  . SER A 158 ? 0.27262 0.26827 0.33682 0.03811  0.04036  -0.01436 158 SER A CA  
1215 C C   . SER A 158 ? 0.25435 0.26807 0.32859 0.03677  0.04523  -0.00762 158 SER A C   
1216 O O   . SER A 158 ? 0.26866 0.28883 0.33533 0.03396  0.04909  -0.00559 158 SER A O   
1217 C CB  . SER A 158 ? 0.29253 0.28281 0.34726 0.04701  0.04554  -0.02366 158 SER A CB  
1218 O OG  . SER A 158 ? 0.30579 0.30150 0.37285 0.05700  0.04949  -0.02479 158 SER A OG  
1219 N N   . GLY A 159 ? 0.25288 0.27293 0.34200 0.03732  0.04400  -0.00352 159 GLY A N   
1220 C CA  . GLY A 159 ? 0.23651 0.26951 0.33362 0.03245  0.04616  0.00253  159 GLY A CA  
1221 C C   . GLY A 159 ? 0.25469 0.28156 0.34727 0.02595  0.04118  0.00755  159 GLY A C   
1222 O O   . GLY A 159 ? 0.26928 0.29993 0.36426 0.02124  0.04197  0.01229  159 GLY A O   
1223 N N   . THR A 160 ? 0.21951 0.23708 0.30614 0.02561  0.03601  0.00661  160 THR A N   
1224 C CA  . THR A 160 ? 0.25581 0.27141 0.34099 0.02281  0.03183  0.01073  160 THR A CA  
1225 C C   . THR A 160 ? 0.26381 0.27857 0.33971 0.02107  0.03256  0.01394  160 THR A C   
1226 O O   . THR A 160 ? 0.25546 0.26659 0.33013 0.02081  0.02969  0.01774  160 THR A O   
1227 C CB  . THR A 160 ? 0.25599 0.26870 0.34018 0.02231  0.02733  0.00984  160 THR A CB  
1228 O OG1 . THR A 160 ? 0.26153 0.27119 0.33871 0.02096  0.02632  0.00582  160 THR A OG1 
1229 C CG2 . THR A 160 ? 0.23054 0.24093 0.32131 0.02317  0.02624  0.01014  160 THR A CG2 
1230 N N   . THR A 161 ? 0.23720 0.25309 0.30394 0.02102  0.03618  0.01255  161 THR A N   
1231 C CA  . THR A 161 ? 0.27828 0.29174 0.33238 0.01938  0.03697  0.01750  161 THR A CA  
1232 C C   . THR A 161 ? 0.27842 0.29411 0.33392 0.01497  0.04343  0.02290  161 THR A C   
1233 O O   . THR A 161 ? 0.25893 0.26937 0.30181 0.01220  0.04481  0.02924  161 THR A O   
1234 C CB  . THR A 161 ? 0.29923 0.31268 0.33801 0.02078  0.03726  0.01389  161 THR A CB  
1235 O OG1 . THR A 161 ? 0.31342 0.33061 0.35226 0.02272  0.04376  0.00756  161 THR A OG1 
1236 C CG2 . THR A 161 ? 0.31376 0.32596 0.35143 0.02163  0.02855  0.01017  161 THR A CG2 
1237 N N   . ALA A 162 ? 0.25709 0.28094 0.32768 0.01347  0.04668  0.02149  162 ALA A N   
1238 C CA  . ALA A 162 ? 0.27603 0.30755 0.35309 0.00662  0.05254  0.02651  162 ALA A CA  
1239 C C   . ALA A 162 ? 0.28694 0.30991 0.37075 0.00146  0.04637  0.02984  162 ALA A C   
1240 O O   . ALA A 162 ? 0.25981 0.26688 0.33350 0.00298  0.04051  0.03179  162 ALA A O   
1241 C CB  . ALA A 162 ? 0.26351 0.31434 0.35445 0.00934  0.05940  0.02200  162 ALA A CB  
1242 N N   . TYR A 163 ? 0.28426 0.31763 0.38433 -0.00335 0.04655  0.02950  163 TYR A N   
1243 C CA  . TYR A 163 ? 0.29617 0.31968 0.40014 -0.00938 0.03953  0.03087  163 TYR A CA  
1244 C C   . TYR A 163 ? 0.24774 0.25639 0.34448 -0.00179 0.03165  0.02704  163 TYR A C   
1245 O O   . TYR A 163 ? 0.26686 0.25765 0.35472 -0.00303 0.02662  0.02827  163 TYR A O   
1246 C CB  . TYR A 163 ? 0.27744 0.32076 0.40217 -0.01345 0.03908  0.02876  163 TYR A CB  
1247 C CG  . TYR A 163 ? 0.29396 0.33281 0.42472 -0.02562 0.03338  0.03092  163 TYR A CG  
1248 C CD1 . TYR A 163 ? 0.32264 0.33441 0.43821 -0.03156 0.02887  0.03398  163 TYR A CD1 
1249 C CD2 . TYR A 163 ? 0.33781 0.39882 0.48937 -0.03073 0.03127  0.02933  163 TYR A CD2 
1250 C CE1 . TYR A 163 ? 0.34322 0.34620 0.46227 -0.04413 0.02246  0.03468  163 TYR A CE1 
1251 C CE2 . TYR A 163 ? 0.41631 0.47446 0.57421 -0.04399 0.02437  0.03026  163 TYR A CE2 
1252 C CZ  . TYR A 163 ? 0.38817 0.41537 0.52896 -0.05165 0.01982  0.03248  163 TYR A CZ  
1253 O OH  . TYR A 163 ? 0.36124 0.38251 0.50748 -0.06652 0.01151  0.03205  163 TYR A OH  
1254 N N   . ASN A 164 ? 0.22657 0.24200 0.32649 0.00621  0.03105  0.02249  164 ASN A N   
1255 C CA  . ASN A 164 ? 0.24289 0.24994 0.33719 0.01250  0.02596  0.01994  164 ASN A CA  
1256 C C   . ASN A 164 ? 0.28514 0.27974 0.36667 0.01525  0.02443  0.02217  164 ASN A C   
1257 O O   . ASN A 164 ? 0.25036 0.23561 0.32689 0.01918  0.02026  0.02099  164 ASN A O   
1258 C CB  . ASN A 164 ? 0.23463 0.24922 0.33226 0.01789  0.02709  0.01696  164 ASN A CB  
1259 C CG  . ASN A 164 ? 0.24865 0.25909 0.34131 0.02212  0.02405  0.01608  164 ASN A CG  
1260 O OD1 . ASN A 164 ? 0.22929 0.23975 0.32340 0.02384  0.02154  0.01523  164 ASN A OD1 
1261 N ND2 . ASN A 164 ? 0.21990 0.22960 0.30673 0.02365  0.02430  0.01670  164 ASN A ND2 
1262 N N   . LYS A 165 ? 0.27223 0.26684 0.34692 0.01473  0.02750  0.02522  165 LYS A N   
1263 C CA  . LYS A 165 ? 0.26262 0.24725 0.32529 0.01935  0.02438  0.02811  165 LYS A CA  
1264 C C   . LYS A 165 ? 0.26378 0.22908 0.31861 0.01788  0.02130  0.03184  165 LYS A C   
1265 O O   . LYS A 165 ? 0.21472 0.16944 0.26280 0.02585  0.01665  0.03149  165 LYS A O   
1266 C CB  . LYS A 165 ? 0.26585 0.25368 0.31936 0.01880  0.02702  0.03100  165 LYS A CB  
1267 C CG  . LYS A 165 ? 0.25981 0.23976 0.30067 0.02517  0.02173  0.03477  165 LYS A CG  
1268 C CD  . LYS A 165 ? 0.30540 0.29027 0.33447 0.02504  0.02251  0.03659  165 LYS A CD  
1269 C CE  . LYS A 165 ? 0.32557 0.30702 0.34478 0.03307  0.01468  0.03993  165 LYS A CE  
1270 N NZ  . LYS A 165 ? 0.42549 0.38562 0.43278 0.03518  0.01265  0.04826  165 LYS A NZ  
1271 N N   . SER A 166 ? 0.24353 0.20398 0.29925 0.00770  0.02389  0.03543  166 SER A N   
1272 C CA  . SER A 166 ? 0.30048 0.23704 0.34689 0.00304  0.02023  0.03948  166 SER A CA  
1273 C C   . SER A 166 ? 0.29917 0.22572 0.34755 0.00561  0.01416  0.03290  166 SER A C   
1274 O O   . SER A 166 ? 0.28961 0.19020 0.32630 0.00580  0.00914  0.03358  166 SER A O   
1275 C CB  . SER A 166 ? 0.29286 0.23062 0.34268 -0.01229 0.02501  0.04556  166 SER A CB  
1276 O OG  . SER A 166 ? 0.36336 0.31037 0.40754 -0.01395 0.03203  0.05150  166 SER A OG  
1277 N N   . LEU A 167 ? 0.30752 0.25127 0.36742 0.00805  0.01419  0.02656  167 LEU A N   
1278 C CA  . LEU A 167 ? 0.28641 0.22276 0.34471 0.01140  0.00877  0.01995  167 LEU A CA  
1279 C C   . LEU A 167 ? 0.31232 0.24929 0.36460 0.02562  0.00809  0.01619  167 LEU A C   
1280 O O   . LEU A 167 ? 0.30962 0.24319 0.35811 0.03038  0.00526  0.01025  167 LEU A O   
1281 C CB  . LEU A 167 ? 0.25300 0.20771 0.32496 0.00635  0.00848  0.01664  167 LEU A CB  
1282 C CG  . LEU A 167 ? 0.27575 0.23672 0.35845 -0.00755 0.00886  0.01964  167 LEU A CG  
1283 C CD1 . LEU A 167 ? 0.26923 0.25537 0.36860 -0.00824 0.00943  0.01749  167 LEU A CD1 
1284 C CD2 . LEU A 167 ? 0.30218 0.24082 0.37757 -0.01631 0.00155  0.01803  167 LEU A CD2 
1285 N N   . GLY A 168 ? 0.27657 0.22026 0.32777 0.03239  0.01053  0.01934  168 GLY A N   
1286 C CA  . GLY A 168 ? 0.25539 0.20608 0.30514 0.04511  0.01026  0.01628  168 GLY A CA  
1287 C C   . GLY A 168 ? 0.25140 0.22679 0.31245 0.04492  0.01389  0.01531  168 GLY A C   
1288 O O   . GLY A 168 ? 0.25134 0.23848 0.31442 0.05293  0.01491  0.01390  168 GLY A O   
1289 N N   . GLY A 169 ? 0.19039 0.17414 0.25916 0.03612  0.01607  0.01643  169 GLY A N   
1290 C CA  . GLY A 169 ? 0.18940 0.18924 0.26617 0.03520  0.01852  0.01584  169 GLY A CA  
1291 C C   . GLY A 169 ? 0.25361 0.26417 0.33283 0.03685  0.01911  0.01736  169 GLY A C   
1292 O O   . GLY A 169 ? 0.23166 0.23936 0.30639 0.03899  0.01742  0.01934  169 GLY A O   
1293 N N   . ALA A 170 ? 0.21662 0.23897 0.30208 0.03491  0.02055  0.01698  170 ALA A N   
1294 C CA  . ALA A 170 ? 0.23022 0.26407 0.31993 0.03288  0.01968  0.01761  170 ALA A CA  
1295 C C   . ALA A 170 ? 0.25327 0.28204 0.34124 0.02682  0.01961  0.01649  170 ALA A C   
1296 O O   . ALA A 170 ? 0.26125 0.28303 0.34931 0.02460  0.02164  0.01551  170 ALA A O   
1297 C CB  . ALA A 170 ? 0.20341 0.25053 0.30036 0.03023  0.02146  0.01841  170 ALA A CB  
1298 N N   . LEU A 171 ? 0.23722 0.27073 0.32295 0.02554  0.01678  0.01598  171 LEU A N   
1299 C CA  . LEU A 171 ? 0.23157 0.26017 0.31244 0.02068  0.01660  0.01284  171 LEU A CA  
1300 C C   . LEU A 171 ? 0.24045 0.27104 0.32662 0.01428  0.01522  0.01066  171 LEU A C   
1301 O O   . LEU A 171 ? 0.25733 0.30038 0.35037 0.01120  0.01238  0.01194  171 LEU A O   
1302 C CB  . LEU A 171 ? 0.21851 0.24939 0.29030 0.02156  0.01275  0.01264  171 LEU A CB  
1303 C CG  . LEU A 171 ? 0.24422 0.27057 0.30861 0.02734  0.01285  0.01737  171 LEU A CG  
1304 C CD1 . LEU A 171 ? 0.21167 0.23716 0.26196 0.02846  0.00913  0.01875  171 LEU A CD1 
1305 C CD2 . LEU A 171 ? 0.23317 0.24883 0.29700 0.02656  0.01891  0.01883  171 LEU A CD2 
1306 N N   . MET A 172 ? 0.26303 0.28153 0.34648 0.01224  0.01716  0.00774  172 MET A N   
1307 C CA  . MET A 172 ? 0.26564 0.27767 0.35129 0.00579  0.01565  0.00682  172 MET A CA  
1308 C C   . MET A 172 ? 0.32140 0.32003 0.39753 0.00299  0.01317  -0.00004 172 MET A C   
1309 O O   . MET A 172 ? 0.27435 0.26483 0.34341 0.00909  0.01631  -0.00397 172 MET A O   
1310 C CB  . MET A 172 ? 0.28798 0.29108 0.37573 0.00836  0.01874  0.00945  172 MET A CB  
1311 C CG  . MET A 172 ? 0.34158 0.35405 0.43452 0.01059  0.02064  0.01481  172 MET A CG  
1312 S SD  . MET A 172 ? 0.49456 0.49463 0.58590 0.01434  0.02161  0.01710  172 MET A SD  
1313 C CE  . MET A 172 ? 0.33151 0.31815 0.41957 0.00603  0.01982  0.01941  172 MET A CE  
1314 N N   . HIS A 173 ? 0.28726 0.28357 0.36330 -0.00653 0.00790  -0.00191 173 HIS A N   
1315 C CA  . HIS A 173 ? 0.33253 0.31123 0.39605 -0.00967 0.00406  -0.01041 173 HIS A CA  
1316 C C   . HIS A 173 ? 0.35779 0.31288 0.41535 -0.00433 0.00734  -0.01327 173 HIS A C   
1317 O O   . HIS A 173 ? 0.38015 0.32859 0.44354 -0.00580 0.00842  -0.00764 173 HIS A O   
1318 C CB  . HIS A 173 ? 0.32868 0.30692 0.39371 -0.02387 -0.00397 -0.01225 173 HIS A CB  
1319 C CG  . HIS A 173 ? 0.37478 0.33303 0.42291 -0.02692 -0.00974 -0.02327 173 HIS A CG  
1320 N ND1 . HIS A 173 ? 0.41568 0.34289 0.45386 -0.02972 -0.01126 -0.02875 173 HIS A ND1 
1321 C CD2 . HIS A 173 ? 0.36375 0.32548 0.39941 -0.02575 -0.01444 -0.03049 173 HIS A CD2 
1322 C CE1 . HIS A 173 ? 0.42371 0.33573 0.44410 -0.03030 -0.01655 -0.04042 173 HIS A CE1 
1323 N NE2 . HIS A 173 ? 0.41202 0.34598 0.43009 -0.02834 -0.01850 -0.04156 173 HIS A NE2 
1324 N N   . PRO A 174 ? 0.36565 0.30829 0.41053 0.00323  0.00904  -0.02175 174 PRO A N   
1325 C CA  . PRO A 174 ? 0.37518 0.30037 0.41718 0.01326  0.01299  -0.02444 174 PRO A CA  
1326 C C   . PRO A 174 ? 0.42212 0.31795 0.45796 0.00861  0.00786  -0.02643 174 PRO A C   
1327 O O   . PRO A 174 ? 0.45017 0.33000 0.48421 0.01870  0.00985  -0.02708 174 PRO A O   
1328 C CB  . PRO A 174 ? 0.42404 0.34807 0.45358 0.02319  0.01742  -0.03391 174 PRO A CB  
1329 C CG  . PRO A 174 ? 0.39491 0.33273 0.41734 0.01742  0.01519  -0.03522 174 PRO A CG  
1330 C CD  . PRO A 174 ? 0.33861 0.28789 0.37174 0.00549  0.00869  -0.02788 174 PRO A CD  
1331 N N   . SER A 175 ? 0.41359 0.30152 0.44662 -0.00653 0.00071  -0.02681 175 SER A N   
1332 C CA  . SER A 175 ? 0.43860 0.29563 0.46589 -0.01456 -0.00433 -0.02597 175 SER A CA  
1333 C C   . SER A 175 ? 0.44544 0.30582 0.48378 -0.01781 -0.00209 -0.01237 175 SER A C   
1334 O O   . SER A 175 ? 0.45026 0.28215 0.48207 -0.02305 -0.00525 -0.00879 175 SER A O   
1335 C CB  . SER A 175 ? 0.44049 0.29090 0.46356 -0.03367 -0.01321 -0.02972 175 SER A CB  
1336 O OG  . SER A 175 ? 0.42972 0.31548 0.46955 -0.04399 -0.01349 -0.02179 175 SER A OG  
1337 N N   . ILE A 176 ? 0.42905 0.32055 0.48092 -0.01528 0.00280  -0.00474 176 ILE A N   
1338 C CA  . ILE A 176 ? 0.40688 0.30434 0.46601 -0.01724 0.00545  0.00727  176 ILE A CA  
1339 C C   . ILE A 176 ? 0.40136 0.29090 0.45853 -0.00093 0.00808  0.00861  176 ILE A C   
1340 O O   . ILE A 176 ? 0.37048 0.27536 0.43215 0.01041  0.01136  0.00451  176 ILE A O   
1341 C CB  . ILE A 176 ? 0.35962 0.29263 0.43176 -0.02031 0.00885  0.01260  176 ILE A CB  
1342 C CG1 . ILE A 176 ? 0.38357 0.33034 0.46142 -0.03493 0.00530  0.01172  176 ILE A CG1 
1343 C CG2 . ILE A 176 ? 0.34900 0.28842 0.42463 -0.02013 0.01246  0.02315  176 ILE A CG2 
1344 C CD1 . ILE A 176 ? 0.34072 0.32364 0.43171 -0.03379 0.00827  0.01545  176 ILE A CD1 
1345 N N   . GLU A 177 ? 0.37789 0.24461 0.42875 -0.00031 0.00612  0.01528  177 GLU A N   
1346 C CA  . GLU A 177 ? 0.40034 0.26020 0.45001 0.01640  0.00631  0.01672  177 GLU A CA  
1347 C C   . GLU A 177 ? 0.38660 0.27043 0.44386 0.01778  0.00869  0.02570  177 GLU A C   
1348 O O   . GLU A 177 ? 0.38964 0.26713 0.44175 0.01226  0.00789  0.03606  177 GLU A O   
1349 C CB  . GLU A 177 ? 0.47052 0.29047 0.50658 0.01901  0.00134  0.01962  177 GLU A CB  
1350 C CG  . GLU A 177 ? 0.49255 0.28333 0.51757 0.02038  -0.00177 0.00771  177 GLU A CG  
1351 C CD  . GLU A 177 ? 0.62228 0.36834 0.63212 0.02807  -0.00724 0.00959  177 GLU A CD  
1352 O OE1 . GLU A 177 ? 0.67401 0.41640 0.68431 0.04917  -0.00736 0.00732  177 GLU A OE1 
1353 O OE2 . GLU A 177 ? 0.63722 0.35217 0.63537 0.01290  -0.01180 0.01415  177 GLU A OE2 
1354 N N   . ALA A 178 ? 0.34933 0.25932 0.41657 0.02437  0.01167  0.02170  178 ALA A N   
1355 C CA  . ALA A 178 ? 0.33916 0.27014 0.41144 0.02423  0.01313  0.02759  178 ALA A CA  
1356 C C   . ALA A 178 ? 0.29517 0.24478 0.37684 0.03360  0.01420  0.02265  178 ALA A C   
1357 O O   . ALA A 178 ? 0.29656 0.24747 0.38218 0.03956  0.01561  0.01572  178 ALA A O   
1358 C CB  . ALA A 178 ? 0.29320 0.23937 0.36768 0.01243  0.01614  0.03009  178 ALA A CB  
1359 N N   . MET A 179 ? 0.26359 0.22741 0.34770 0.03417  0.01372  0.02629  179 MET A N   
1360 C CA  . MET A 179 ? 0.25996 0.24135 0.35322 0.03849  0.01395  0.02255  179 MET A CA  
1361 C C   . MET A 179 ? 0.26516 0.25670 0.35618 0.03337  0.01479  0.02428  179 MET A C   
1362 O O   . MET A 179 ? 0.26439 0.25291 0.34762 0.02980  0.01526  0.02900  179 MET A O   
1363 C CB  . MET A 179 ? 0.27746 0.26219 0.37585 0.04788  0.00920  0.02355  179 MET A CB  
1364 C CG  . MET A 179 ? 0.27423 0.25261 0.36279 0.04883  0.00402  0.03090  179 MET A CG  
1365 S SD  . MET A 179 ? 0.30111 0.28635 0.39576 0.06093  -0.00471 0.03254  179 MET A SD  
1366 C CE  . MET A 179 ? 0.31939 0.29417 0.39415 0.05927  -0.00974 0.04194  179 MET A CE  
1367 N N   . GLN A 180 ? 0.23006 0.23265 0.32681 0.03308  0.01564  0.02057  180 GLN A N   
1368 C CA  . GLN A 180 ? 0.22379 0.23131 0.31669 0.03021  0.01648  0.02038  180 GLN A CA  
1369 C C   . GLN A 180 ? 0.25806 0.27054 0.35375 0.03110  0.01305  0.01807  180 GLN A C   
1370 O O   . GLN A 180 ? 0.24595 0.26351 0.35033 0.03006  0.01337  0.01600  180 GLN A O   
1371 C CB  . GLN A 180 ? 0.23171 0.24158 0.32553 0.02716  0.02006  0.01842  180 GLN A CB  
1372 C CG  . GLN A 180 ? 0.24621 0.25955 0.33646 0.02778  0.02030  0.01765  180 GLN A CG  
1373 C CD  . GLN A 180 ? 0.23027 0.24716 0.32084 0.02704  0.02218  0.01709  180 GLN A CD  
1374 O OE1 . GLN A 180 ? 0.22185 0.24116 0.30946 0.03028  0.02221  0.01672  180 GLN A OE1 
1375 N NE2 . GLN A 180 ? 0.20383 0.22043 0.29655 0.02430  0.02288  0.01638  180 GLN A NE2 
1376 N N   . LEU A 181 ? 0.23828 0.24954 0.32558 0.03187  0.01023  0.01811  181 LEU A N   
1377 C CA  . LEU A 181 ? 0.24482 0.25722 0.33198 0.03103  0.00469  0.01490  181 LEU A CA  
1378 C C   . LEU A 181 ? 0.25104 0.25722 0.33115 0.02988  0.00577  0.01145  181 LEU A C   
1379 O O   . LEU A 181 ? 0.28334 0.28689 0.35318 0.03357  0.00844  0.01117  181 LEU A O   
1380 C CB  . LEU A 181 ? 0.25093 0.26263 0.32878 0.03416  -0.00131 0.01605  181 LEU A CB  
1381 C CG  . LEU A 181 ? 0.25867 0.27083 0.33368 0.03230  -0.00971 0.01145  181 LEU A CG  
1382 C CD1 . LEU A 181 ? 0.21295 0.23761 0.30666 0.02994  -0.01473 0.01158  181 LEU A CD1 
1383 C CD2 . LEU A 181 ? 0.24494 0.25284 0.30021 0.03679  -0.01407 0.01202  181 LEU A CD2 
1384 N N   . THR A 182 ? 0.22501 0.22882 0.31029 0.02515  0.00386  0.00927  182 THR A N   
1385 C CA  . THR A 182 ? 0.23158 0.22261 0.30776 0.02462  0.00305  0.00623  182 THR A CA  
1386 C C   . THR A 182 ? 0.25975 0.24322 0.33302 0.01913  -0.00497 0.00207  182 THR A C   
1387 O O   . THR A 182 ? 0.21178 0.20566 0.29585 0.01380  -0.00938 0.00248  182 THR A O   
1388 C CB  . THR A 182 ? 0.24987 0.23831 0.33034 0.02193  0.00741  0.00884  182 THR A CB  
1389 O OG1 . THR A 182 ? 0.25563 0.25297 0.34885 0.01484  0.00812  0.01101  182 THR A OG1 
1390 C CG2 . THR A 182 ? 0.22445 0.21988 0.30605 0.02655  0.01292  0.01136  182 THR A CG2 
1391 N N   . GLU A 183 ? 0.26669 0.23198 0.32528 0.02108  -0.00763 -0.00263 183 GLU A N   
1392 C CA  . GLU A 183 ? 0.29610 0.24698 0.34704 0.01497  -0.01672 -0.00846 183 GLU A CA  
1393 C C   . GLU A 183 ? 0.31539 0.25423 0.37135 0.00443  -0.01777 -0.00648 183 GLU A C   
1394 O O   . GLU A 183 ? 0.29389 0.22585 0.34862 0.00675  -0.01194 -0.00240 183 GLU A O   
1395 C CB  . GLU A 183 ? 0.31624 0.24817 0.34400 0.02436  -0.01895 -0.01612 183 GLU A CB  
1396 C CG  . GLU A 183 ? 0.29810 0.24232 0.31723 0.03393  -0.01641 -0.01701 183 GLU A CG  
1397 C CD  . GLU A 183 ? 0.35698 0.28612 0.35125 0.04417  -0.01754 -0.02581 183 GLU A CD  
1398 O OE1 . GLU A 183 ? 0.37187 0.27769 0.35464 0.04701  -0.02000 -0.03223 183 GLU A OE1 
1399 O OE2 . GLU A 183 ? 0.37678 0.31622 0.36091 0.05026  -0.01552 -0.02608 183 GLU A OE2 
1400 N N   . MET A 184 ? 0.32845 0.26403 0.38864 -0.00805 -0.02607 -0.00890 184 MET A N   
1401 C CA  . MET A 184 ? 0.33512 0.25313 0.39575 -0.02089 -0.02801 -0.00678 184 MET A CA  
1402 C C   . MET A 184 ? 0.32506 0.21170 0.36573 -0.02388 -0.03879 -0.01589 184 MET A C   
1403 O O   . MET A 184 ? 0.38606 0.27705 0.42811 -0.03132 -0.04865 -0.02167 184 MET A O   
1404 C CB  . MET A 184 ? 0.32958 0.27137 0.41457 -0.03663 -0.02799 -0.00127 184 MET A CB  
1405 C CG  . MET A 184 ? 0.27827 0.25316 0.38220 -0.03100 -0.01864 0.00461  184 MET A CG  
1406 S SD  . MET A 184 ? 0.41671 0.42056 0.54914 -0.04860 -0.01817 0.00966  184 MET A SD  
1407 C CE  . MET A 184 ? 0.34725 0.38050 0.49430 -0.03728 -0.00547 0.01455  184 MET A CE  
1408 N N   . ALA A 185 ? 0.33555 0.19005 0.35684 -0.01717 -0.03799 -0.01776 185 ALA A N   
1409 C CA  . ALA A 185 ? 0.42715 0.24304 0.42500 -0.01787 -0.04790 -0.02755 185 ALA A CA  
1410 C C   . ALA A 185 ? 0.41635 0.23380 0.40186 -0.01286 -0.05607 -0.03948 185 ALA A C   
1411 O O   . ALA A 185 ? 0.40929 0.21898 0.39311 -0.02687 -0.06784 -0.04531 185 ALA A O   
1412 C CB  . ALA A 185 ? 0.40404 0.20042 0.40564 -0.04064 -0.05524 -0.02481 185 ALA A CB  
1413 N N   . SER A 186 ? 0.39768 0.22657 0.37418 0.00545  -0.05043 -0.04273 186 SER A N   
1414 C CA  . SER A 186 ? 0.42226 0.25138 0.38220 0.01040  -0.05755 -0.05313 186 SER A CA  
1415 C C   . SER A 186 ? 0.46362 0.25107 0.39248 0.01594  -0.06520 -0.06680 186 SER A C   
1416 O O   . SER A 186 ? 0.48865 0.25067 0.40546 0.02650  -0.06092 -0.06847 186 SER A O   
1417 C CB  . SER A 186 ? 0.43096 0.28464 0.38833 0.02703  -0.04773 -0.05108 186 SER A CB  
1418 O OG  . SER A 186 ? 0.44229 0.29270 0.39786 0.04055  -0.03668 -0.04814 186 SER A OG  
1419 N N   . ILE A 187 ? 0.50515 0.28449 0.41960 0.01000  -0.07760 -0.07721 187 ILE A N   
1420 C CA  . ILE A 187 ? 0.52200 0.26181 0.40084 0.01841  -0.08522 -0.09343 187 ILE A CA  
1421 C C   . ILE A 187 ? 0.54755 0.29838 0.40676 0.04248  -0.07557 -0.09862 187 ILE A C   
1422 O O   . ILE A 187 ? 0.57178 0.35603 0.43678 0.04492  -0.07202 -0.09400 187 ILE A O   
1423 C CB  . ILE A 187 ? 0.54752 0.27562 0.41697 0.00118  -0.10384 -0.10352 187 ILE A CB  
1424 C CG1 . ILE A 187 ? 0.54278 0.27176 0.43912 -0.02589 -0.11171 -0.09578 187 ILE A CG1 
1425 C CG2 . ILE A 187 ? 0.60742 0.28830 0.43589 0.00940  -0.11298 -0.12251 187 ILE A CG2 
1426 C CD1 . ILE A 187 ? 0.57311 0.29603 0.46597 -0.04648 -0.13192 -0.10523 187 ILE A CD1 
1427 N N   . ASN A 188 ? 0.58163 0.30515 0.41754 0.06080  -0.07080 -0.10748 188 ASN A N   
1428 C CA  . ASN A 188 ? 0.63059 0.36729 0.44746 0.08392  -0.06015 -0.11320 188 ASN A CA  
1429 C C   . ASN A 188 ? 0.70020 0.39378 0.47870 0.09914  -0.06484 -0.13217 188 ASN A C   
1430 O O   . ASN A 188 ? 0.69626 0.36045 0.46945 0.10881  -0.06326 -0.13517 188 ASN A O   
1431 C CB  . ASN A 188 ? 0.62929 0.39449 0.46611 0.09714  -0.04291 -0.10138 188 ASN A CB  
1432 C CG  . ASN A 188 ? 0.55630 0.36641 0.41854 0.08919  -0.03607 -0.08699 188 ASN A CG  
1433 O OD1 . ASN A 188 ? 0.54880 0.38150 0.40256 0.09660  -0.02980 -0.08661 188 ASN A OD1 
1434 N ND2 . ASN A 188 ? 0.49875 0.31995 0.38994 0.07406  -0.03716 -0.07497 188 ASN A ND2 
1435 N N   . ASN A 189 ? 0.70470 0.39176 0.45395 0.10235  -0.07145 -0.14537 189 ASN A N   
1436 C CA  . ASN A 189 ? 0.79913 0.44665 0.50793 0.12138  -0.07353 -0.16529 189 ASN A CA  
1437 C C   . ASN A 189 ? 0.88587 0.55328 0.56712 0.13607  -0.06758 -0.17363 189 ASN A C   
1438 O O   . ASN A 189 ? 0.90438 0.61776 0.60134 0.13771  -0.05570 -0.16068 189 ASN A O   
1439 C CB  . ASN A 189 ? 0.83521 0.42949 0.52505 0.10565  -0.09437 -0.17857 189 ASN A CB  
1440 C CG  . ASN A 189 ? 0.86698 0.47227 0.56054 0.08056  -0.11050 -0.17877 189 ASN A CG  
1441 O OD1 . ASN A 189 ? 0.85503 0.49244 0.54286 0.08342  -0.10874 -0.17791 189 ASN A OD1 
1442 N ND2 . ASN A 189 ? 0.86774 0.44854 0.57206 0.05549  -0.12636 -0.17858 189 ASN A ND2 
1443 N N   . ARG A 190 ? 1.04413 0.68071 0.68771 0.14379  -0.07485 -0.19169 190 ARG A N   
1444 C CA  . ARG A 190 ? 1.13020 0.78586 0.74518 0.15727  -0.06822 -0.19855 190 ARG A CA  
1445 C C   . ARG A 190 ? 1.09043 0.76922 0.70117 0.14349  -0.07676 -0.19461 190 ARG A C   
1446 O O   . ARG A 190 ? 1.11551 0.83291 0.72497 0.15157  -0.06346 -0.18553 190 ARG A O   
1447 C CB  . ARG A 190 ? 1.06425 0.68533 0.64781 0.16188  -0.07605 -0.21495 190 ARG A CB  
1448 C CG  . ARG A 190 ? 1.16393 0.80066 0.71499 0.17726  -0.06824 -0.22307 190 ARG A CG  
1449 C CD  . ARG A 190 ? 1.21642 0.81511 0.73518 0.17167  -0.08460 -0.24050 190 ARG A CD  
1450 N NE  . ARG A 190 ? 1.24274 0.79827 0.76843 0.16514  -0.09428 -0.24573 190 ARG A NE  
1451 C CZ  . ARG A 190 ? 1.43015 0.94863 0.94401 0.14681  -0.11441 -0.25578 190 ARG A CZ  
1452 N NH1 . ARG A 190 ? 1.31458 0.83484 0.81019 0.13331  -0.12875 -0.26296 190 ARG A NH1 
1453 N NH2 . ARG A 190 ? 1.30935 0.78954 0.83064 0.14087  -0.12067 -0.25756 190 ARG A NH2 
1454 N N   . VAL A 191 ? 0.98141 0.64620 0.60035 0.11878  -0.09773 -0.19521 191 VAL A N   
1455 C CA  . VAL A 191 ? 0.93598 0.63035 0.56152 0.10314  -0.10765 -0.18681 191 VAL A CA  
1456 C C   . VAL A 191 ? 0.83509 0.57004 0.51081 0.08871  -0.10278 -0.16285 191 VAL A C   
1457 O O   . VAL A 191 ? 0.81279 0.57619 0.49461 0.08111  -0.10792 -0.15373 191 VAL A O   
1458 C CB  . VAL A 191 ? 0.96577 0.63007 0.57537 0.08400  -0.13474 -0.20102 191 VAL A CB  
1459 C CG1 . VAL A 191 ? 0.98325 0.62049 0.54682 0.09536  -0.13856 -0.22004 191 VAL A CG1 
1460 C CG2 . VAL A 191 ? 0.97034 0.60702 0.60548 0.06630  -0.14362 -0.20073 191 VAL A CG2 
1461 N N   . TYR A 192 ? 0.80693 0.54351 0.51635 0.08559  -0.09408 -0.15279 192 TYR A N   
1462 C CA  . TYR A 192 ? 0.74377 0.51406 0.49813 0.07148  -0.09085 -0.13266 192 TYR A CA  
1463 C C   . TYR A 192 ? 0.70876 0.50059 0.48340 0.08389  -0.06938 -0.11998 192 TYR A C   
1464 O O   . TYR A 192 ? 0.70141 0.47484 0.47639 0.09295  -0.06249 -0.12354 192 TYR A O   
1465 C CB  . TYR A 192 ? 0.72516 0.48050 0.50470 0.04950  -0.10391 -0.13113 192 TYR A CB  
1466 C CG  . TYR A 192 ? 0.79965 0.53263 0.56317 0.03348  -0.12694 -0.14445 192 TYR A CG  
1467 C CD1 . TYR A 192 ? 0.80810 0.55343 0.55135 0.03334  -0.13807 -0.15000 192 TYR A CD1 
1468 C CD2 . TYR A 192 ? 0.76148 0.46006 0.52868 0.01743  -0.13853 -0.15105 192 TYR A CD2 
1469 C CE1 . TYR A 192 ? 0.86384 0.59066 0.59242 0.01777  -0.16143 -0.16322 192 TYR A CE1 
1470 C CE2 . TYR A 192 ? 0.83212 0.51054 0.58602 -0.00017 -0.16083 -0.16365 192 TYR A CE2 
1471 C CZ  . TYR A 192 ? 0.87556 0.56949 0.61069 0.00016  -0.17294 -0.17055 192 TYR A CZ  
1472 O OH  . TYR A 192 ? 0.86358 0.53967 0.58579 -0.01823 -0.19724 -0.18391 192 TYR A OH  
1473 N N   . ARG A 193 ? 0.61128 0.44069 0.40284 0.08373  -0.06037 -0.10497 193 ARG A N   
1474 C CA  . ARG A 193 ? 0.59815 0.45180 0.40624 0.09401  -0.04090 -0.09333 193 ARG A CA  
1475 C C   . ARG A 193 ? 0.52693 0.40792 0.37088 0.08136  -0.03899 -0.07582 193 ARG A C   
1476 O O   . ARG A 193 ? 0.52782 0.42350 0.37275 0.07474  -0.04497 -0.06971 193 ARG A O   
1477 C CB  . ARG A 193 ? 0.63286 0.50305 0.41617 0.10944  -0.02857 -0.09375 193 ARG A CB  
1478 C CG  . ARG A 193 ? 0.83752 0.68363 0.57749 0.12334  -0.03128 -0.11266 193 ARG A CG  
1479 C CD  . ARG A 193 ? 0.90359 0.74227 0.63666 0.14331  -0.01753 -0.12065 193 ARG A CD  
1480 N NE  . ARG A 193 ? 0.95161 0.80779 0.65801 0.16129  -0.00279 -0.12426 193 ARG A NE  
1481 C CZ  . ARG A 193 ? 0.90556 0.79875 0.62733 0.16842  0.01641  -0.11205 193 ARG A CZ  
1482 N NH1 . ARG A 193 ? 0.76050 0.67468 0.52234 0.15988  0.02196  -0.09671 193 ARG A NH1 
1483 N NH2 . ARG A 193 ? 0.90024 0.81055 0.59582 0.18360  0.03042  -0.11556 193 ARG A NH2 
1484 N N   . THR A 194 ? 0.47558 0.36265 0.34646 0.07981  -0.03099 -0.06803 194 THR A N   
1485 C CA  . THR A 194 ? 0.43657 0.34998 0.33704 0.07220  -0.02544 -0.05253 194 THR A CA  
1486 C C   . THR A 194 ? 0.41610 0.34583 0.32540 0.08190  -0.00916 -0.04599 194 THR A C   
1487 O O   . THR A 194 ? 0.37396 0.29683 0.27159 0.09468  -0.00266 -0.05299 194 THR A O   
1488 C CB  . THR A 194 ? 0.43709 0.34698 0.36420 0.05826  -0.03210 -0.04842 194 THR A CB  
1489 O OG1 . THR A 194 ? 0.42403 0.31933 0.35620 0.06162  -0.02743 -0.05038 194 THR A OG1 
1490 C CG2 . THR A 194 ? 0.42132 0.31822 0.34366 0.04660  -0.04876 -0.05546 194 THR A CG2 
1491 N N   . ILE A 195 ? 0.36565 0.31736 0.29663 0.07606  -0.00328 -0.03297 195 ILE A N   
1492 C CA  . ILE A 195 ? 0.36908 0.33912 0.31039 0.08229  0.01066  -0.02661 195 ILE A CA  
1493 C C   . ILE A 195 ? 0.36974 0.33303 0.32502 0.08538  0.01236  -0.02881 195 ILE A C   
1494 O O   . ILE A 195 ? 0.34838 0.32165 0.30467 0.09630  0.02142  -0.02960 195 ILE A O   
1495 C CB  . ILE A 195 ? 0.32836 0.31819 0.28662 0.07378  0.01503  -0.01294 195 ILE A CB  
1496 C CG1 . ILE A 195 ? 0.32478 0.33552 0.29304 0.07768  0.02854  -0.00688 195 ILE A CG1 
1497 C CG2 . ILE A 195 ? 0.28486 0.27127 0.26564 0.06320  0.00839  -0.00882 195 ILE A CG2 
1498 C CD1 . ILE A 195 ? 0.29747 0.31886 0.24572 0.08908  0.03823  -0.01030 195 ILE A CD1 
1499 N N   . GLY A 196 ? 0.35440 0.30272 0.32037 0.07636  0.00388  -0.02907 196 GLY A N   
1500 C CA  . GLY A 196 ? 0.34276 0.28179 0.31857 0.07852  0.00470  -0.02900 196 GLY A CA  
1501 C C   . GLY A 196 ? 0.31702 0.27602 0.31635 0.07329  0.01029  -0.01844 196 GLY A C   
1502 O O   . GLY A 196 ? 0.34006 0.29395 0.35170 0.06424  0.00678  -0.01452 196 GLY A O   
1503 N N   . SER A 197 ? 0.29399 0.27651 0.29862 0.07756  0.01908  -0.01379 197 SER A N   
1504 C CA  . SER A 197 ? 0.28223 0.28271 0.30689 0.07190  0.02337  -0.00519 197 SER A CA  
1505 C C   . SER A 197 ? 0.29684 0.29683 0.33116 0.05909  0.01947  0.00014  197 SER A C   
1506 O O   . SER A 197 ? 0.24467 0.24186 0.27262 0.05554  0.01602  0.00016  197 SER A O   
1507 C CB  . SER A 197 ? 0.25392 0.27986 0.28233 0.07521  0.03275  -0.00091 197 SER A CB  
1508 O OG  . SER A 197 ? 0.27455 0.30574 0.29548 0.08970  0.03749  -0.00666 197 SER A OG  
1509 N N   . PRO A 198 ? 0.26894 0.27265 0.31767 0.05369  0.01977  0.00440  198 PRO A N   
1510 C CA  . PRO A 198 ? 0.28363 0.29156 0.34214 0.04479  0.01886  0.00927  198 PRO A CA  
1511 C C   . PRO A 198 ? 0.25632 0.27475 0.31372 0.04340  0.02264  0.01399  198 PRO A C   
1512 O O   . PRO A 198 ? 0.27068 0.30065 0.32642 0.04638  0.02839  0.01560  198 PRO A O   
1513 C CB  . PRO A 198 ? 0.24527 0.25702 0.31480 0.04207  0.02042  0.01170  198 PRO A CB  
1514 C CG  . PRO A 198 ? 0.23242 0.23823 0.29751 0.04875  0.01979  0.00893  198 PRO A CG  
1515 C CD  . PRO A 198 ? 0.22122 0.22714 0.27600 0.05762  0.02128  0.00496  198 PRO A CD  
1516 N N   . LEU A 199 ? 0.20982 0.22521 0.26952 0.03863  0.01972  0.01723  199 LEU A N   
1517 C CA  . LEU A 199 ? 0.24634 0.26491 0.30230 0.03633  0.02203  0.02359  199 LEU A CA  
1518 C C   . LEU A 199 ? 0.25381 0.26907 0.32019 0.03109  0.02137  0.02708  199 LEU A C   
1519 O O   . LEU A 199 ? 0.26696 0.27748 0.33957 0.03140  0.01734  0.02472  199 LEU A O   
1520 C CB  . LEU A 199 ? 0.25917 0.27190 0.30219 0.03879  0.01696  0.02426  199 LEU A CB  
1521 C CG  . LEU A 199 ? 0.26172 0.27315 0.28892 0.04453  0.01577  0.01851  199 LEU A CG  
1522 C CD1 . LEU A 199 ? 0.26138 0.26799 0.27347 0.04602  0.00913  0.02017  199 LEU A CD1 
1523 C CD2 . LEU A 199 ? 0.24742 0.26937 0.26821 0.04827  0.02531  0.01917  199 LEU A CD2 
1524 N N   . VAL A 200 ? 0.27214 0.29002 0.34005 0.02598  0.02544  0.03232  200 VAL A N   
1525 C CA  . VAL A 200 ? 0.24961 0.25872 0.32327 0.02092  0.02421  0.03450  200 VAL A CA  
1526 C C   . VAL A 200 ? 0.27897 0.27708 0.34352 0.01858  0.02344  0.04230  200 VAL A C   
1527 O O   . VAL A 200 ? 0.29401 0.29682 0.35192 0.01402  0.02783  0.04863  200 VAL A O   
1528 C CB  . VAL A 200 ? 0.27691 0.29344 0.35866 0.01443  0.02711  0.03388  200 VAL A CB  
1529 C CG1 . VAL A 200 ? 0.24339 0.24556 0.32635 0.00801  0.02499  0.03507  200 VAL A CG1 
1530 C CG2 . VAL A 200 ? 0.23976 0.26313 0.32741 0.01828  0.02636  0.02757  200 VAL A CG2 
1531 N N   . PHE A 201 ? 0.29213 0.27611 0.35607 0.02236  0.01825  0.04262  201 PHE A N   
1532 C CA  . PHE A 201 ? 0.29224 0.26053 0.34553 0.02330  0.01518  0.05055  201 PHE A CA  
1533 C C   . PHE A 201 ? 0.33349 0.28231 0.38781 0.01976  0.01408  0.05206  201 PHE A C   
1534 O O   . PHE A 201 ? 0.33028 0.27707 0.39338 0.02274  0.01300  0.04452  201 PHE A O   
1535 C CB  . PHE A 201 ? 0.27632 0.24325 0.32792 0.03368  0.00794  0.04948  201 PHE A CB  
1536 C CG  . PHE A 201 ? 0.30534 0.28603 0.35268 0.03628  0.00661  0.04670  201 PHE A CG  
1537 C CD1 . PHE A 201 ? 0.28498 0.27710 0.34289 0.03749  0.00598  0.03800  201 PHE A CD1 
1538 C CD2 . PHE A 201 ? 0.30123 0.28082 0.33101 0.03699  0.00592  0.05278  201 PHE A CD2 
1539 C CE1 . PHE A 201 ? 0.29029 0.28933 0.34197 0.03913  0.00352  0.03418  201 PHE A CE1 
1540 C CE2 . PHE A 201 ? 0.31388 0.30314 0.33600 0.04007  0.00395  0.04794  201 PHE A CE2 
1541 C CZ  . PHE A 201 ? 0.29638 0.29369 0.32956 0.04102  0.00213  0.03806  201 PHE A CZ  
1542 N N   . PRO A 202 ? 0.36313 0.29455 0.40603 0.01368  0.01411  0.06174  202 PRO A N   
1543 C CA  . PRO A 202 ? 0.36847 0.27339 0.40893 0.01023  0.01145  0.06246  202 PRO A CA  
1544 C C   . PRO A 202 ? 0.37837 0.26337 0.41366 0.02430  0.00443  0.06278  202 PRO A C   
1545 O O   . PRO A 202 ? 0.35725 0.25216 0.39247 0.03504  0.00089  0.06356  202 PRO A O   
1546 C CB  . PRO A 202 ? 0.36504 0.25931 0.39484 -0.00441 0.01461  0.07452  202 PRO A CB  
1547 C CG  . PRO A 202 ? 0.37395 0.27891 0.39345 -0.00066 0.01632  0.08260  202 PRO A CG  
1548 C CD  . PRO A 202 ? 0.36102 0.29347 0.38993 0.00912  0.01685  0.07284  202 PRO A CD  
1549 N N   . LYS A 203 ? 0.40190 0.25867 0.43291 0.02472  0.00155  0.06140  203 LYS A N   
1550 C CA  . LYS A 203 ? 0.45473 0.28771 0.47893 0.03985  -0.00533 0.06293  203 LYS A CA  
1551 C C   . LYS A 203 ? 0.43891 0.26350 0.44873 0.04270  -0.00937 0.07681  203 LYS A C   
1552 O O   . LYS A 203 ? 0.44906 0.27063 0.44786 0.02909  -0.00592 0.08723  203 LYS A O   
1553 C CB  . LYS A 203 ? 0.47299 0.26697 0.48759 0.03726  -0.00786 0.06123  203 LYS A CB  
1554 C CG  . LYS A 203 ? 0.50876 0.30078 0.53124 0.04670  -0.00766 0.04622  203 LYS A CG  
1555 C CD  . LYS A 203 ? 0.56317 0.30759 0.57015 0.05134  -0.01299 0.04492  203 LYS A CD  
1556 C CE  . LYS A 203 ? 0.58654 0.30304 0.57980 0.02895  -0.01389 0.05360  203 LYS A CE  
1557 N NZ  . LYS A 203 ? 0.67080 0.33197 0.64467 0.03250  -0.02083 0.05465  203 LYS A NZ  
1558 N N   . HIS A 204 ? 0.42994 0.25190 0.43944 0.06083  -0.01677 0.07744  204 HIS A N   
1559 C CA  . HIS A 204 ? 0.49243 0.30310 0.48556 0.06794  -0.02384 0.09061  204 HIS A CA  
1560 C C   . HIS A 204 ? 0.45067 0.29023 0.44078 0.06402  -0.02278 0.09452  204 HIS A C   
1561 O O   . HIS A 204 ? 0.50422 0.33683 0.47773 0.06936  -0.02890 0.10518  204 HIS A O   
1562 C CB  . HIS A 204 ? 0.50691 0.27643 0.47631 0.05879  -0.02470 0.10504  204 HIS A CB  
1563 C CG  . HIS A 204 ? 0.56962 0.30113 0.53596 0.06080  -0.02697 0.10133  204 HIS A CG  
1564 N ND1 . HIS A 204 ? 0.61955 0.33472 0.58822 0.08283  -0.03452 0.09569  204 HIS A ND1 
1565 C CD2 . HIS A 204 ? 0.58552 0.29149 0.54585 0.04381  -0.02329 0.10157  204 HIS A CD2 
1566 C CE1 . HIS A 204 ? 0.58902 0.26643 0.55035 0.08059  -0.03499 0.09161  204 HIS A CE1 
1567 N NE2 . HIS A 204 ? 0.60214 0.27224 0.55795 0.05567  -0.02904 0.09514  204 HIS A NE2 
1568 N N   . HIS A 205 ? 0.45120 0.31941 0.45331 0.05526  -0.01561 0.08641  205 HIS A N   
1569 C CA  . HIS A 205 ? 0.41758 0.31195 0.41803 0.05601  -0.01629 0.08548  205 HIS A CA  
1570 C C   . HIS A 205 ? 0.41338 0.32723 0.43018 0.06885  -0.02387 0.07627  205 HIS A C   
1571 O O   . HIS A 205 ? 0.34827 0.26916 0.38420 0.07238  -0.02246 0.06692  205 HIS A O   
1572 C CB  . HIS A 205 ? 0.36779 0.28194 0.37399 0.04351  -0.00616 0.08009  205 HIS A CB  
1573 C CG  . HIS A 205 ? 0.39505 0.30327 0.38597 0.03101  0.00141  0.09041  205 HIS A CG  
1574 N ND1 . HIS A 205 ? 0.36614 0.29616 0.35729 0.02358  0.00998  0.08833  205 HIS A ND1 
1575 C CD2 . HIS A 205 ? 0.37814 0.26183 0.35311 0.02453  0.00216  0.10372  205 HIS A CD2 
1576 C CE1 . HIS A 205 ? 0.41442 0.33905 0.39318 0.01266  0.01686  0.09974  205 HIS A CE1 
1577 N NE2 . HIS A 205 ? 0.39531 0.29071 0.36321 0.01151  0.01216  0.10998  205 HIS A NE2 
1578 N N   . VAL A 206 ? 0.37457 0.29884 0.38330 0.07482  -0.03191 0.07908  206 VAL A N   
1579 C CA  . VAL A 206 ? 0.35615 0.30233 0.38136 0.08478  -0.04109 0.07172  206 VAL A CA  
1580 C C   . VAL A 206 ? 0.40273 0.37018 0.42688 0.07786  -0.04130 0.06530  206 VAL A C   
1581 O O   . VAL A 206 ? 0.40254 0.36704 0.40444 0.07533  -0.04292 0.07007  206 VAL A O   
1582 C CB  . VAL A 206 ? 0.40042 0.33973 0.41763 0.09933  -0.05455 0.07974  206 VAL A CB  
1583 C CG1 . VAL A 206 ? 0.37656 0.34625 0.41464 0.10774  -0.06502 0.07208  206 VAL A CG1 
1584 C CG2 . VAL A 206 ? 0.43732 0.34898 0.45321 0.10838  -0.05482 0.08537  206 VAL A CG2 
1585 N N   . VAL A 207 ? 0.33141 0.31813 0.37717 0.07511  -0.03968 0.05452  207 VAL A N   
1586 C CA  . VAL A 207 ? 0.34965 0.35173 0.39565 0.06874  -0.04142 0.04700  207 VAL A CA  
1587 C C   . VAL A 207 ? 0.38976 0.41206 0.45211 0.07350  -0.05374 0.04253  207 VAL A C   
1588 O O   . VAL A 207 ? 0.36376 0.39852 0.45023 0.07727  -0.05361 0.03975  207 VAL A O   
1589 C CB  . VAL A 207 ? 0.32744 0.33321 0.38394 0.05979  -0.03056 0.03973  207 VAL A CB  
1590 C CG1 . VAL A 207 ? 0.32315 0.33854 0.37829 0.05424  -0.03359 0.03178  207 VAL A CG1 
1591 C CG2 . VAL A 207 ? 0.32661 0.31818 0.37011 0.05495  -0.01983 0.04444  207 VAL A CG2 
1592 N N   . SER A 208 ? 0.35230 0.37977 0.40129 0.07340  -0.06449 0.04169  208 SER A N   
1593 C CA  . SER A 208 ? 0.38706 0.43582 0.45003 0.07696  -0.07951 0.03848  208 SER A CA  
1594 C C   . SER A 208 ? 0.37830 0.43569 0.44017 0.06557  -0.08394 0.02834  208 SER A C   
1595 O O   . SER A 208 ? 0.40981 0.45275 0.44669 0.06125  -0.08104 0.02597  208 SER A O   
1596 C CB  . SER A 208 ? 0.41161 0.45546 0.45561 0.08806  -0.09257 0.04726  208 SER A CB  
1597 O OG  . SER A 208 ? 0.47790 0.54380 0.52971 0.08964  -0.10979 0.04323  208 SER A OG  
1598 N N   . LEU A 209 ? 0.38397 0.46413 0.47277 0.06037  -0.09011 0.02216  209 LEU A N   
1599 C CA  . LEU A 209 ? 0.39433 0.47934 0.48271 0.04761  -0.09686 0.01257  209 LEU A CA  
1600 C C   . LEU A 209 ? 0.41988 0.52654 0.51585 0.04826  -0.11678 0.01078  209 LEU A C   
1601 O O   . LEU A 209 ? 0.44544 0.57820 0.56980 0.05336  -0.12198 0.01372  209 LEU A O   
1602 C CB  . LEU A 209 ? 0.36719 0.46055 0.48035 0.03616  -0.08831 0.00761  209 LEU A CB  
1603 C CG  . LEU A 209 ? 0.31792 0.39677 0.43060 0.03617  -0.07020 0.00966  209 LEU A CG  
1604 C CD1 . LEU A 209 ? 0.33754 0.42469 0.46988 0.02389  -0.06545 0.00529  209 LEU A CD1 
1605 C CD2 . LEU A 209 ? 0.32092 0.37308 0.40284 0.03727  -0.06308 0.00936  209 LEU A CD2 
1606 N N   . GLN A 210 ? 0.38715 0.48457 0.45758 0.04414  -0.12821 0.00532  210 GLN A N   
1607 C CA  . GLN A 210 ? 0.46344 0.57999 0.53602 0.04452  -0.14955 0.00319  210 GLN A CA  
1608 C C   . GLN A 210 ? 0.49908 0.61652 0.57143 0.02706  -0.15973 -0.00958 210 GLN A C   
1609 O O   . GLN A 210 ? 0.49408 0.58402 0.54089 0.02100  -0.15373 -0.01664 210 GLN A O   
1610 C CB  . GLN A 210 ? 0.50397 0.60580 0.53844 0.05708  -0.15748 0.00910  210 GLN A CB  
1611 C CG  . GLN A 210 ? 0.48579 0.57712 0.51524 0.07192  -0.14639 0.02287  210 GLN A CG  
1612 C CD  . GLN A 210 ? 0.56010 0.63282 0.54858 0.08208  -0.15123 0.03148  210 GLN A CD  
1613 O OE1 . GLN A 210 ? 0.61184 0.68135 0.57295 0.08021  -0.16329 0.02681  210 GLN A OE1 
1614 N NE2 . GLN A 210 ? 0.58283 0.64088 0.56431 0.09212  -0.14159 0.04435  210 GLN A NE2 
1615 N N   . PRO A 211 ? 0.53290 0.68091 0.63343 0.01864  -0.17534 -0.01306 211 PRO A N   
1616 C CA  . PRO A 211 ? 0.53551 0.68173 0.63743 -0.00162 -0.18599 -0.02512 211 PRO A CA  
1617 C C   . PRO A 211 ? 0.59236 0.71757 0.65243 -0.00206 -0.20194 -0.03385 211 PRO A C   
1618 O O   . PRO A 211 ? 0.59076 0.71790 0.62949 0.01154  -0.21145 -0.02965 211 PRO A O   
1619 C CB  . PRO A 211 ? 0.57347 0.76600 0.72083 -0.00978 -0.19889 -0.02421 211 PRO A CB  
1620 C CG  . PRO A 211 ? 0.55273 0.76886 0.72475 0.00870  -0.18918 -0.01218 211 PRO A CG  
1621 C CD  . PRO A 211 ? 0.51279 0.69959 0.64653 0.02733  -0.18462 -0.00621 211 PRO A CD  
1622 N N   . VAL A 212 ? 0.65013 0.75283 0.69588 -0.01762 -0.20540 -0.04629 212 VAL A N   
1623 C CA  . VAL A 212 ? 0.65164 0.73018 0.65433 -0.01878 -0.22002 -0.05800 212 VAL A CA  
1624 C C   . VAL A 212 ? 0.73983 0.83334 0.75410 -0.03756 -0.24546 -0.06868 212 VAL A C   
1625 O O   . VAL A 212 ? 0.78167 0.87789 0.77252 -0.03500 -0.26578 -0.07429 212 VAL A O   
1626 C CB  . VAL A 212 ? 0.59063 0.62513 0.55981 -0.01868 -0.20553 -0.06626 212 VAL A CB  
1627 C CG1 . VAL A 212 ? 0.61760 0.62546 0.54102 -0.02002 -0.22073 -0.08153 212 VAL A CG1 
1628 C CG2 . VAL A 212 ? 0.54698 0.57244 0.50330 -0.00021 -0.18320 -0.05546 212 VAL A CG2 
1629 N N   . ASN A 213 ? 0.78137 0.88586 0.83126 -0.05771 -0.24527 -0.07094 213 ASN A N   
1630 C CA  . ASN A 213 ? 0.83797 0.96679 0.91012 -0.07876 -0.26930 -0.07835 213 ASN A CA  
1631 C C   . ASN A 213 ? 0.77606 0.95139 0.90808 -0.08902 -0.26426 -0.06849 213 ASN A C   
1632 O O   . ASN A 213 ? 0.75836 0.97808 0.91854 -0.07889 -0.27040 -0.06012 213 ASN A O   
1633 C CB  . ASN A 213 ? 0.91929 1.00789 0.96706 -0.09955 -0.27811 -0.09458 213 ASN A CB  
1634 C CG  . ASN A 213 ? 1.06511 1.14214 1.07666 -0.10205 -0.30481 -0.10879 213 ASN A CG  
1635 O OD1 . ASN A 213 ? 1.08596 1.20108 1.11129 -0.10144 -0.32193 -0.10654 213 ASN A OD1 
1636 N ND2 . ASN A 213 ? 1.20273 1.22762 1.16577 -0.10241 -0.30551 -0.12321 213 ASN A ND2 
1637 N N   . ASP A 214 ? 0.79080 0.95662 0.94128 -0.10751 -0.25261 -0.06886 214 ASP A N   
1638 C CA  . ASP A 214 ? 0.75929 0.96969 0.96401 -0.11654 -0.24344 -0.05864 214 ASP A CA  
1639 C C   . ASP A 214 ? 0.71564 0.95032 0.93525 -0.09018 -0.22740 -0.04583 214 ASP A C   
1640 O O   . ASP A 214 ? 0.72295 0.92687 0.91485 -0.07234 -0.21147 -0.04250 214 ASP A O   
1641 C CB  . ASP A 214 ? 0.76929 0.95475 0.97983 -0.13559 -0.22762 -0.05815 214 ASP A CB  
1642 C CG  . ASP A 214 ? 0.80629 1.03979 1.07153 -0.15080 -0.21964 -0.04859 214 ASP A CG  
1643 O OD1 . ASP A 214 ? 0.79404 1.08292 1.09561 -0.14561 -0.22646 -0.04365 214 ASP A OD1 
1644 O OD2 . ASP A 214 ? 0.85909 1.07581 1.13037 -0.16701 -0.20606 -0.04552 214 ASP A OD2 
1645 N N   . LYS A 215 ? 0.65038 0.94074 0.91408 -0.08745 -0.23242 -0.03914 215 LYS A N   
1646 C CA  . LYS A 215 ? 0.63393 0.94694 0.91348 -0.06183 -0.21914 -0.02811 215 LYS A CA  
1647 C C   . LYS A 215 ? 0.56084 0.90830 0.88557 -0.06660 -0.20099 -0.02089 215 LYS A C   
1648 O O   . LYS A 215 ? 0.51182 0.88617 0.85673 -0.04605 -0.19255 -0.01336 215 LYS A O   
1649 C CB  . LYS A 215 ? 0.63694 0.98490 0.92555 -0.04531 -0.23926 -0.02567 215 LYS A CB  
1650 C CG  . LYS A 215 ? 0.65674 0.98645 0.90938 -0.04823 -0.26414 -0.03425 215 LYS A CG  
1651 C CD  . LYS A 215 ? 0.68426 1.04157 0.95516 -0.07362 -0.28068 -0.04262 215 LYS A CD  
1652 C CE  . LYS A 215 ? 0.73263 1.07171 0.96242 -0.07429 -0.30329 -0.05170 215 LYS A CE  
1653 N NZ  . LYS A 215 ? 0.70075 1.04681 0.93430 -0.10243 -0.31602 -0.06394 215 LYS A NZ  
1654 N N   . ASP A 216 ? 0.57229 0.91765 0.91090 -0.09261 -0.19462 -0.02284 216 ASP A N   
1655 C CA  . ASP A 216 ? 0.51964 0.89324 0.89444 -0.09857 -0.17442 -0.01533 216 ASP A CA  
1656 C C   . ASP A 216 ? 0.52790 0.85375 0.87523 -0.09794 -0.15220 -0.01317 216 ASP A C   
1657 O O   . ASP A 216 ? 0.55441 0.83535 0.87207 -0.11188 -0.15419 -0.01842 216 ASP A O   
1658 C CB  . ASP A 216 ? 0.49710 0.90070 0.90151 -0.12762 -0.17745 -0.01790 216 ASP A CB  
1659 C CG  . ASP A 216 ? 0.54814 0.99329 0.97067 -0.12694 -0.19533 -0.02441 216 ASP A CG  
1660 O OD1 . ASP A 216 ? 0.55059 1.00703 0.96640 -0.10387 -0.20694 -0.02412 216 ASP A OD1 
1661 O OD2 . ASP A 216 ? 0.53980 1.00450 0.98330 -0.14936 -0.19826 -0.02956 216 ASP A OD2 
1662 N N   . PHE A 217 ? 0.48246 0.81810 0.83951 -0.08116 -0.13203 -0.00608 217 PHE A N   
1663 C CA  . PHE A 217 ? 0.47039 0.76587 0.80301 -0.07815 -0.11188 -0.00353 217 PHE A CA  
1664 C C   . PHE A 217 ? 0.41512 0.73994 0.77664 -0.07915 -0.09176 0.00365  217 PHE A C   
1665 O O   . PHE A 217 ? 0.40955 0.78163 0.80388 -0.06874 -0.08932 0.00664  217 PHE A O   
1666 C CB  . PHE A 217 ? 0.39354 0.65775 0.69387 -0.05231 -0.10711 -0.00334 217 PHE A CB  
1667 C CG  . PHE A 217 ? 0.50149 0.74359 0.77285 -0.04667 -0.12458 -0.00890 217 PHE A CG  
1668 C CD1 . PHE A 217 ? 0.49333 0.76342 0.77495 -0.03637 -0.14111 -0.00901 217 PHE A CD1 
1669 C CD2 . PHE A 217 ? 0.49170 0.68570 0.72370 -0.04972 -0.12445 -0.01393 217 PHE A CD2 
1670 C CE1 . PHE A 217 ? 0.53417 0.78303 0.78430 -0.03110 -0.15716 -0.01359 217 PHE A CE1 
1671 C CE2 . PHE A 217 ? 0.51777 0.69253 0.71962 -0.04343 -0.13905 -0.01953 217 PHE A CE2 
1672 C CZ  . PHE A 217 ? 0.53096 0.73237 0.74041 -0.03492 -0.15527 -0.01907 217 PHE A CZ  
1673 N N   . GLN A 218 ? 0.37887 0.67455 0.72553 -0.08947 -0.07723 0.00625  218 GLN A N   
1674 C CA  . GLN A 218 ? 0.34137 0.65339 0.70209 -0.08659 -0.05572 0.01293  218 GLN A CA  
1675 C C   . GLN A 218 ? 0.31374 0.59976 0.64970 -0.06107 -0.04506 0.01290  218 GLN A C   
1676 O O   . GLN A 218 ? 0.29524 0.53563 0.59752 -0.05929 -0.04360 0.01132  218 GLN A O   
1677 C CB  . GLN A 218 ? 0.38655 0.67787 0.74032 -0.11122 -0.04733 0.01702  218 GLN A CB  
1678 C CG  . GLN A 218 ? 0.38692 0.70443 0.75923 -0.11537 -0.02643 0.02518  218 GLN A CG  
1679 C CD  . GLN A 218 ? 0.45718 0.83543 0.87534 -0.13133 -0.02593 0.02918  218 GLN A CD  
1680 O OE1 . GLN A 218 ? 0.48931 0.87830 0.91838 -0.14510 -0.04154 0.02433  218 GLN A OE1 
1681 N NE2 . GLN A 218 ? 0.47311 0.87850 0.90311 -0.12440 -0.00569 0.03216  218 GLN A NE2 
1682 N N   . ILE A 219 ? 0.32718 0.64163 0.67970 -0.04088 -0.03873 0.01409  219 ILE A N   
1683 C CA  . ILE A 219 ? 0.31509 0.60488 0.64582 -0.01871 -0.02920 0.01389  219 ILE A CA  
1684 C C   . ILE A 219 ? 0.34112 0.64327 0.67999 -0.01613 -0.00894 0.01686  219 ILE A C   
1685 O O   . ILE A 219 ? 0.35876 0.70534 0.72871 -0.01489 -0.00243 0.01837  219 ILE A O   
1686 C CB  . ILE A 219 ? 0.33705 0.63784 0.67197 0.00465  -0.03799 0.01246  219 ILE A CB  
1687 C CG1 . ILE A 219 ? 0.34857 0.64142 0.67407 0.00152  -0.05910 0.01008  219 ILE A CG1 
1688 C CG2 . ILE A 219 ? 0.27371 0.54131 0.58275 0.02310  -0.02904 0.01252  219 ILE A CG2 
1689 C CD1 . ILE A 219 ? 0.34053 0.65209 0.67472 0.02221  -0.07117 0.01066  219 ILE A CD1 
1690 N N   . SER A 220 ? 0.27030 0.53563 0.58106 -0.01510 0.00097  0.01748  220 SER A N   
1691 C CA  . SER A 220 ? 0.26151 0.53153 0.57112 -0.01078 0.01914  0.01938  220 SER A CA  
1692 C C   . SER A 220 ? 0.25468 0.50763 0.54878 0.01248  0.02301  0.01580  220 SER A C   
1693 O O   . SER A 220 ? 0.29877 0.52087 0.57218 0.01927  0.01460  0.01408  220 SER A O   
1694 C CB  . SER A 220 ? 0.25918 0.49951 0.54679 -0.02620 0.02603  0.02298  220 SER A CB  
1695 O OG  . SER A 220 ? 0.32488 0.52335 0.58175 -0.01742 0.02276  0.02048  220 SER A OG  
1696 N N   . VAL A 221 ? 0.25957 0.53125 0.56199 0.02382  0.03626  0.01455  221 VAL A N   
1697 C CA  . VAL A 221 ? 0.26250 0.51288 0.54705 0.04346  0.04132  0.01021  221 VAL A CA  
1698 C C   . VAL A 221 ? 0.29468 0.54500 0.56951 0.04144  0.05814  0.00991  221 VAL A C   
1699 O O   . VAL A 221 ? 0.30092 0.58671 0.59446 0.04347  0.06950  0.00988  221 VAL A O   
1700 C CB  . VAL A 221 ? 0.28157 0.55256 0.58318 0.06573  0.03851  0.00649  221 VAL A CB  
1701 C CG1 . VAL A 221 ? 0.27282 0.51942 0.55464 0.08379  0.04623  0.00112  221 VAL A CG1 
1702 C CG2 . VAL A 221 ? 0.25471 0.51821 0.55774 0.07022  0.01996  0.00775  221 VAL A CG2 
1703 N N   . ASP A 222 ? 0.26172 0.47557 0.50753 0.03780  0.05985  0.00987  222 ASP A N   
1704 C CA  . ASP A 222 ? 0.29952 0.51186 0.53226 0.03318  0.07364  0.01083  222 ASP A CA  
1705 C C   . ASP A 222 ? 0.30624 0.54745 0.55602 0.01524  0.08036  0.01803  222 ASP A C   
1706 O O   . ASP A 222 ? 0.31704 0.55291 0.57098 -0.00084 0.07190  0.02298  222 ASP A O   
1707 C CB  . ASP A 222 ? 0.26451 0.48354 0.49356 0.05251  0.08369  0.00342  222 ASP A CB  
1708 C CG  . ASP A 222 ? 0.22713 0.41045 0.43618 0.06619  0.07621  -0.00287 222 ASP A CG  
1709 O OD1 . ASP A 222 ? 0.21444 0.36805 0.40633 0.05867  0.06837  -0.00085 222 ASP A OD1 
1710 O OD2 . ASP A 222 ? 0.25369 0.43844 0.46409 0.08437  0.07853  -0.00974 222 ASP A OD2 
1711 N N   . HIS A 223 ? 0.29949 0.57175 0.55947 0.01718  0.09544  0.01859  223 HIS A N   
1712 C CA  A HIS A 223 ? 0.33574 0.63573 0.61101 -0.00280 0.10359  0.02737  223 HIS A CA  
1713 C CA  B HIS A 223 ? 0.33555 0.63568 0.61088 -0.00288 0.10365  0.02741  223 HIS A CA  
1714 C C   . HIS A 223 ? 0.36656 0.71065 0.68173 -0.00799 0.09945  0.02887  223 HIS A C   
1715 O O   . HIS A 223 ? 0.36111 0.72995 0.69310 -0.02856 0.10427  0.03682  223 HIS A O   
1716 C CB  A HIS A 223 ? 0.34838 0.66559 0.61512 0.00011  0.12361  0.02858  223 HIS A CB  
1717 C CB  B HIS A 223 ? 0.34790 0.66571 0.61492 -0.00006 0.12382  0.02868  223 HIS A CB  
1718 C CG  A HIS A 223 ? 0.33099 0.67722 0.61011 0.02373  0.13295  0.01943  223 HIS A CG  
1719 C CG  B HIS A 223 ? 0.32404 0.67061 0.60405 -0.02231 0.13515  0.03999  223 HIS A CG  
1720 N ND1 A HIS A 223 ? 0.28439 0.60626 0.54890 0.04635  0.12759  0.00873  223 HIS A ND1 
1721 N ND1 B HIS A 223 ? 0.31822 0.66445 0.61128 -0.04623 0.12653  0.04855  223 HIS A ND1 
1722 C CD2 A HIS A 223 ? 0.28737 0.66912 0.58318 0.02669  0.14336  0.01559  223 HIS A CD2 
1723 C CD2 B HIS A 223 ? 0.32208 0.68964 0.59759 -0.02546 0.15263  0.04206  223 HIS A CD2 
1724 C CE1 A HIS A 223 ? 0.27742 0.62200 0.55144 0.06407  0.13528  -0.00008 223 HIS A CE1 
1725 C CE1 B HIS A 223 ? 0.29830 0.66295 0.59523 -0.06404 0.13813  0.05610  223 HIS A CE1 
1726 N NE2 A HIS A 223 ? 0.28201 0.66142 0.57461 0.05273  0.14451  0.00326  223 HIS A NE2 
1727 N NE2 B HIS A 223 ? 0.29861 0.67568 0.58431 -0.05160 0.15423  0.05235  223 HIS A NE2 
1728 N N   . LEU A 224 ? 0.37258 0.72730 0.70335 0.00900  0.08973  0.02227  224 LEU A N   
1729 C CA  . LEU A 224 ? 0.38428 0.78146 0.75081 0.00676  0.08361  0.02150  224 LEU A CA  
1730 C C   . LEU A 224 ? 0.41560 0.80267 0.78916 -0.00688 0.06435  0.02490  224 LEU A C   
1731 O O   . LEU A 224 ? 0.40311 0.75004 0.75349 0.00034  0.05273  0.02156  224 LEU A O   
1732 C CB  . LEU A 224 ? 0.33228 0.74073 0.70699 0.03464  0.08198  0.01144  224 LEU A CB  
1733 C CG  . LEU A 224 ? 0.40615 0.80706 0.76310 0.05104  0.09848  0.00549  224 LEU A CG  
1734 C CD1 . LEU A 224 ? 0.43601 0.82935 0.79220 0.07979  0.09474  -0.00414 224 LEU A CD1 
1735 C CD2 . LEU A 224 ? 0.38620 0.81887 0.75513 0.04094  0.11513  0.00720  224 LEU A CD2 
1736 N N   . SER A 225 ? 0.42047 0.83404 0.81665 -0.02777 0.05983  0.02827  225 SER A N   
1737 C CA  . SER A 225 ? 0.44367 0.84498 0.84318 -0.04439 0.04102  0.03049  225 SER A CA  
1738 C C   . SER A 225 ? 0.42928 0.87062 0.86032 -0.04799 0.03017  0.02653  225 SER A C   
1739 O O   . SER A 225 ? 0.42204 0.89019 0.87202 -0.06287 0.03692  0.02758  225 SER A O   
1740 C CB  . SER A 225 ? 0.44227 0.81551 0.82509 -0.07215 0.04270  0.03697  225 SER A CB  
1741 O OG  . SER A 225 ? 0.45099 0.79520 0.82330 -0.08381 0.02369  0.03473  225 SER A OG  
1742 N N   . ILE A 226 ? 0.43687 0.87882 0.87236 -0.03477 0.01283  0.02256  226 ILE A N   
1743 C CA  . ILE A 226 ? 0.54755 1.02553 1.01113 -0.03162 0.00063  0.01766  226 ILE A CA  
1744 C C   . ILE A 226 ? 0.45970 0.92803 0.92146 -0.04770 -0.02199 0.01764  226 ILE A C   
1745 O O   . ILE A 226 ? 0.38841 0.82203 0.82722 -0.04242 -0.03246 0.01854  226 ILE A O   
1746 C CB  . ILE A 226 ? 0.50412 0.99010 0.97203 0.00158  -0.00166 0.01274  226 ILE A CB  
1747 C CG1 . ILE A 226 ? 0.50617 0.98163 0.96131 0.01955  0.01862  0.01141  226 ILE A CG1 
1748 C CG2 . ILE A 226 ? 0.49331 1.02058 0.99638 0.00623  -0.00961 0.01012  226 ILE A CG2 
1749 C CD1 . ILE A 226 ? 0.43572 0.86732 0.85707 0.03377  0.01882  0.01198  226 ILE A CD1 
1750 N N   . LEU A 227 ? 0.43754 0.93196 0.92213 -0.06695 -0.02966 0.01579  227 LEU A N   
1751 C CA  . LEU A 227 ? 0.44211 0.93144 0.92561 -0.07973 -0.05355 0.01261  227 LEU A CA  
1752 C C   . LEU A 227 ? 0.46571 0.97531 0.95957 -0.05527 -0.06862 0.00807  227 LEU A C   
1753 O O   . LEU A 227 ? 0.53097 1.07793 1.05498 -0.04487 -0.06702 0.00625  227 LEU A O   
1754 C CB  . LEU A 227 ? 0.46058 0.96814 0.96433 -0.10914 -0.05705 0.01149  227 LEU A CB  
1755 C CG  . LEU A 227 ? 0.46641 0.96091 0.96331 -0.12809 -0.08151 0.00634  227 LEU A CG  
1756 C CD1 . LEU A 227 ? 0.49050 1.02288 1.01210 -0.11770 -0.09928 0.00007  227 LEU A CD1 
1757 C CD2 . LEU A 227 ? 0.44962 0.89390 0.90815 -0.12560 -0.09229 0.00648  227 LEU A CD2 
1758 N N   . HIS A 228 ? 0.46007 0.94206 0.92915 -0.04559 -0.08366 0.00808  228 HIS A N   
1759 C CA  . HIS A 228 ? 0.49695 0.99004 0.96753 -0.02190 -0.09954 0.00549  228 HIS A CA  
1760 C C   . HIS A 228 ? 0.48379 0.97885 0.95058 -0.03618 -0.12486 0.00116  228 HIS A C   
1761 O O   . HIS A 228 ? 0.43657 0.89715 0.87975 -0.05394 -0.13341 0.00101  228 HIS A O   
1762 C CB  . HIS A 228 ? 0.48883 0.94600 0.93090 0.00167  -0.09770 0.00996  228 HIS A CB  
1763 C CG  . HIS A 228 ? 0.47809 0.93523 0.92190 0.02178  -0.07646 0.01122  228 HIS A CG  
1764 N ND1 . HIS A 228 ? 0.52021 0.98216 0.96876 0.05010  -0.07702 0.01056  228 HIS A ND1 
1765 C CD2 . HIS A 228 ? 0.46805 0.91481 0.90788 0.01715  -0.05519 0.01312  228 HIS A CD2 
1766 C CE1 . HIS A 228 ? 0.52961 0.98341 0.97547 0.06160  -0.05702 0.01046  228 HIS A CE1 
1767 N NE2 . HIS A 228 ? 0.47567 0.92338 0.91556 0.04256  -0.04350 0.01114  228 HIS A NE2 
1768 N N   . ARG A 229 ? 0.49080 1.01978 0.98161 -0.02759 -0.13831 -0.00297 229 ARG A N   
1769 C CA  . ARG A 229 ? 0.49795 1.03244 0.98407 -0.03861 -0.16361 -0.00888 229 ARG A CA  
1770 C C   . ARG A 229 ? 0.51147 1.03834 0.97878 -0.01162 -0.17986 -0.00735 229 ARG A C   
1771 O O   . ARG A 229 ? 0.49519 1.01673 0.96918 0.01352  -0.17374 0.00319  229 ARG A O   
1772 C CB  . ARG A 229 ? 0.51012 1.08654 1.03864 -0.05344 -0.16952 -0.01299 229 ARG A CB  
1773 C CG  . ARG A 229 ? 0.50961 1.08771 1.04907 -0.08448 -0.15557 -0.01338 229 ARG A CG  
1774 C CD  . ARG A 229 ? 0.50427 1.12678 1.08718 -0.09867 -0.16073 -0.01584 229 ARG A CD  
1775 N NE  . ARG A 229 ? 0.58591 1.20651 1.17730 -0.12902 -0.14643 -0.01431 229 ARG A NE  
1776 C CZ  . ARG A 229 ? 0.69124 1.28316 1.26314 -0.15798 -0.15437 -0.01834 229 ARG A CZ  
1777 N NH1 . ARG A 229 ? 0.74565 1.30906 1.28638 -0.16097 -0.17559 -0.02540 229 ARG A NH1 
1778 N NH2 . ARG A 229 ? 0.69260 1.28087 1.27362 -0.18411 -0.14065 -0.01474 229 ARG A NH2 
1779 N N   . ASP A 230 ? 0.61087 1.13167 1.05204 -0.02072 -0.20061 -0.00993 230 ASP A N   
1780 C CA  . ASP A 230 ? 0.57788 1.09113 0.99328 -0.00163 -0.21716 0.00033  230 ASP A CA  
1781 C C   . ASP A 230 ? 0.57682 1.04961 0.96826 0.02366  -0.20773 0.00636  230 ASP A C   
1782 O O   . ASP A 230 ? 0.57393 1.04646 0.96277 0.04872  -0.20942 0.01527  230 ASP A O   
1783 C CB  . ASP A 230 ? 0.55491 1.09550 1.00674 0.00781  -0.23040 0.01202  230 ASP A CB  
1784 C CG  . ASP A 230 ? 0.65392 1.19158 1.07645 0.02341  -0.25054 0.01618  230 ASP A CG  
1785 O OD1 . ASP A 230 ? 0.65944 1.18029 1.04557 0.01279  -0.26390 0.00751  230 ASP A OD1 
1786 O OD2 . ASP A 230 ? 0.72882 1.27562 1.16485 0.04782  -0.25405 0.02461  230 ASP A OD2 
1787 N N   . VAL A 231 ? 0.53992 0.97157 0.91288 0.01584  -0.19789 0.00116  231 VAL A N   
1788 C CA  . VAL A 231 ? 0.50172 0.88874 0.84239 0.03478  -0.18260 0.00556  231 VAL A CA  
1789 C C   . VAL A 231 ? 0.52631 0.87235 0.81845 0.04100  -0.19515 0.00524  231 VAL A C   
1790 O O   . VAL A 231 ? 0.57038 0.89731 0.83984 0.02383  -0.20461 -0.00170 231 VAL A O   
1791 C CB  . VAL A 231 ? 0.52601 0.88465 0.85846 0.02169  -0.15891 0.00416  231 VAL A CB  
1792 C CG1 . VAL A 231 ? 0.47355 0.77727 0.76064 0.03152  -0.14895 0.00598  231 VAL A CG1 
1793 C CG2 . VAL A 231 ? 0.50179 0.89245 0.87119 0.02744  -0.14083 0.00758  231 VAL A CG2 
1794 N N   . GLN A 232 ? 0.49523 0.82649 0.76963 0.06576  -0.19514 0.01282  232 GLN A N   
1795 C CA  . GLN A 232 ? 0.51001 0.80284 0.73612 0.07307  -0.20394 0.01524  232 GLN A CA  
1796 C C   . GLN A 232 ? 0.51160 0.75556 0.70351 0.07603  -0.18352 0.01842  232 GLN A C   
1797 O O   . GLN A 232 ? 0.51385 0.72491 0.66416 0.07528  -0.18617 0.01864  232 GLN A O   
1798 C CB  . GLN A 232 ? 0.51969 0.82545 0.74413 0.09744  -0.21987 0.02391  232 GLN A CB  
1799 N N   . GLU A 233 ? 0.41963 0.66092 0.62820 0.07906  -0.16348 0.02048  233 GLU A N   
1800 C CA  . GLU A 233 ? 0.40061 0.60084 0.58152 0.08416  -0.14595 0.02472  233 GLU A CA  
1801 C C   . GLU A 233 ? 0.38757 0.59305 0.59262 0.08402  -0.12665 0.02407  233 GLU A C   
1802 O O   . GLU A 233 ? 0.35598 0.59477 0.59565 0.09077  -0.12619 0.02402  233 GLU A O   
1803 C CB  . GLU A 233 ? 0.46351 0.64365 0.62074 0.10463  -0.15063 0.03509  233 GLU A CB  
1804 C CG  . GLU A 233 ? 0.49045 0.62643 0.61196 0.10421  -0.13606 0.03977  233 GLU A CG  
1805 C CD  . GLU A 233 ? 0.46927 0.58218 0.56980 0.12217  -0.13819 0.05202  233 GLU A CD  
1806 O OE1 . GLU A 233 ? 0.46399 0.59245 0.58082 0.13846  -0.14829 0.05645  233 GLU A OE1 
1807 O OE2 . GLU A 233 ? 0.50134 0.58083 0.56989 0.11996  -0.12953 0.05768  233 GLU A OE2 
1808 N N   . ILE A 234 ? 0.38044 0.55467 0.56605 0.07720  -0.11086 0.02336  234 ILE A N   
1809 C CA  . ILE A 234 ? 0.35910 0.52888 0.55655 0.07764  -0.09234 0.02308  234 ILE A CA  
1810 C C   . ILE A 234 ? 0.36018 0.49100 0.52717 0.08450  -0.08356 0.02825  234 ILE A C   
1811 O O   . ILE A 234 ? 0.38567 0.49361 0.52585 0.07681  -0.08234 0.02822  234 ILE A O   
1812 C CB  . ILE A 234 ? 0.35139 0.52446 0.55722 0.05805  -0.08323 0.01682  234 ILE A CB  
1813 C CG1 . ILE A 234 ? 0.32565 0.53305 0.55717 0.04578  -0.09430 0.01252  234 ILE A CG1 
1814 C CG2 . ILE A 234 ? 0.29948 0.47493 0.51934 0.05940  -0.06604 0.01677  234 ILE A CG2 
1815 C CD1 . ILE A 234 ? 0.31458 0.51441 0.54424 0.02407  -0.09055 0.00726  234 ILE A CD1 
1816 N N   . ARG A 235 ? 0.34345 0.46681 0.51381 0.09912  -0.07819 0.03255  235 ARG A N   
1817 C CA  A ARG A 235 ? 0.39264 0.47879 0.53580 0.10376  -0.07148 0.03847  235 ARG A CA  
1818 C CA  B ARG A 235 ? 0.35557 0.44173 0.49876 0.10375  -0.07145 0.03846  235 ARG A CA  
1819 C C   . ARG A 235 ? 0.33050 0.40656 0.47976 0.10212  -0.05556 0.03535  235 ARG A C   
1820 O O   . ARG A 235 ? 0.34039 0.43084 0.51041 0.11100  -0.05182 0.03235  235 ARG A O   
1821 C CB  A ARG A 235 ? 0.41491 0.48906 0.54809 0.12187  -0.08123 0.04711  235 ARG A CB  
1822 C CB  B ARG A 235 ? 0.37724 0.45117 0.51059 0.12190  -0.08093 0.04706  235 ARG A CB  
1823 C CG  A ARG A 235 ? 0.43214 0.50931 0.54924 0.12407  -0.09769 0.05214  235 ARG A CG  
1824 C CG  B ARG A 235 ? 0.43704 0.51510 0.55591 0.12491  -0.09760 0.05207  235 ARG A CG  
1825 C CD  A ARG A 235 ? 0.46073 0.52719 0.56867 0.14432  -0.10946 0.06228  235 ARG A CD  
1826 C CD  B ARG A 235 ? 0.46739 0.52196 0.56688 0.14215  -0.10561 0.06371  235 ARG A CD  
1827 N NE  A ARG A 235 ? 0.50623 0.53000 0.58043 0.14588  -0.10472 0.07265  235 ARG A NE  
1828 N NE  B ARG A 235 ? 0.45055 0.51516 0.57235 0.16172  -0.10924 0.06429  235 ARG A NE  
1829 C CZ  A ARG A 235 ? 0.50571 0.51142 0.54714 0.14381  -0.11104 0.08172  235 ARG A CZ  
1830 C CZ  B ARG A 235 ? 0.46022 0.55610 0.60236 0.17509  -0.12390 0.06422  235 ARG A CZ  
1831 N NH1 A ARG A 235 ? 0.45989 0.48369 0.49391 0.14172  -0.12392 0.08055  235 ARG A NH1 
1832 N NH1 B ARG A 235 ? 0.44508 0.56480 0.58796 0.16899  -0.13794 0.06330  235 ARG A NH1 
1833 N NH2 A ARG A 235 ? 0.50814 0.47666 0.52218 0.14266  -0.10417 0.09220  235 ARG A NH2 
1834 N NH2 B ARG A 235 ? 0.48196 0.58566 0.64387 0.19259  -0.12308 0.06439  235 ARG A NH2 
1835 N N   . TYR A 236 ? 0.30844 0.36130 0.43867 0.09194  -0.04670 0.03586  236 TYR A N   
1836 C CA  . TYR A 236 ? 0.32698 0.36756 0.45761 0.08813  -0.03345 0.03298  236 TYR A CA  
1837 C C   . TYR A 236 ? 0.37088 0.37886 0.48017 0.09124  -0.03104 0.03929  236 TYR A C   
1838 O O   . TYR A 236 ? 0.34562 0.33935 0.43456 0.08726  -0.03393 0.04580  236 TYR A O   
1839 C CB  . TYR A 236 ? 0.29553 0.33776 0.42312 0.07280  -0.02637 0.02880  236 TYR A CB  
1840 C CG  . TYR A 236 ? 0.28042 0.34809 0.42679 0.06588  -0.02745 0.02329  236 TYR A CG  
1841 C CD1 . TYR A 236 ? 0.29467 0.38201 0.46325 0.06842  -0.02265 0.01998  236 TYR A CD1 
1842 C CD2 . TYR A 236 ? 0.32474 0.39547 0.46515 0.05613  -0.03282 0.02130  236 TYR A CD2 
1843 C CE1 . TYR A 236 ? 0.30941 0.42072 0.49583 0.05902  -0.02270 0.01673  236 TYR A CE1 
1844 C CE2 . TYR A 236 ? 0.31390 0.40352 0.47065 0.04695  -0.03455 0.01684  236 TYR A CE2 
1845 C CZ  . TYR A 236 ? 0.30468 0.41528 0.48528 0.04730  -0.02914 0.01555  236 TYR A CZ  
1846 O OH  . TYR A 236 ? 0.37283 0.50345 0.57069 0.03549  -0.02991 0.01296  236 TYR A OH  
1847 N N   . GLU A 237 ? 0.35885 0.35450 0.47135 0.09728  -0.02538 0.03720  237 GLU A N   
1848 C CA  . GLU A 237 ? 0.37328 0.33552 0.46654 0.09488  -0.02199 0.04176  237 GLU A CA  
1849 C C   . GLU A 237 ? 0.35310 0.30787 0.45195 0.09554  -0.01376 0.03408  237 GLU A C   
1850 O O   . GLU A 237 ? 0.34372 0.31663 0.45936 0.10357  -0.01117 0.02684  237 GLU A O   
1851 C CB  . GLU A 237 ? 0.37415 0.31358 0.45397 0.10665  -0.03068 0.05073  237 GLU A CB  
1852 C CG  . GLU A 237 ? 0.41901 0.36431 0.51272 0.12626  -0.03592 0.04772  237 GLU A CG  
1853 C CD  . GLU A 237 ? 0.55321 0.48500 0.63536 0.13986  -0.04850 0.05803  237 GLU A CD  
1854 O OE1 . GLU A 237 ? 0.57463 0.46815 0.63369 0.14024  -0.05021 0.06679  237 GLU A OE1 
1855 O OE2 . GLU A 237 ? 0.55110 0.51066 0.64688 0.14922  -0.05746 0.05808  237 GLU A OE2 
1856 N N   . VAL A 238 ? 0.36867 0.29826 0.45285 0.08640  -0.00963 0.03565  238 VAL A N   
1857 C CA  . VAL A 238 ? 0.38040 0.29699 0.46445 0.08717  -0.00417 0.02782  238 VAL A CA  
1858 C C   . VAL A 238 ? 0.42094 0.32123 0.50457 0.10574  -0.00809 0.02567  238 VAL A C   
1859 O O   . VAL A 238 ? 0.45869 0.33560 0.53091 0.11269  -0.01529 0.03360  238 VAL A O   
1860 C CB  . VAL A 238 ? 0.39555 0.28859 0.46463 0.07209  -0.00160 0.03032  238 VAL A CB  
1861 C CG1 . VAL A 238 ? 0.37912 0.25559 0.44478 0.07227  0.00181  0.02050  238 VAL A CG1 
1862 C CG2 . VAL A 238 ? 0.33597 0.25009 0.40805 0.05777  0.00245  0.03191  238 VAL A CG2 
1863 N N   . SER A 239 ? 0.40104 0.31352 0.49583 0.11529  -0.00309 0.01532  239 SER A N   
1864 C CA  . SER A 239 ? 0.44202 0.34275 0.53813 0.13683  -0.00554 0.01111  239 SER A CA  
1865 C C   . SER A 239 ? 0.47483 0.32560 0.54792 0.13820  -0.00785 0.01010  239 SER A C   
1866 O O   . SER A 239 ? 0.51251 0.34531 0.57326 0.12184  -0.00489 0.00811  239 SER A O   
1867 C CB  . SER A 239 ? 0.37977 0.30939 0.49261 0.14641  0.00299  -0.00039 239 SER A CB  
1868 O OG  . SER A 239 ? 0.41490 0.33119 0.52722 0.16966  0.00164  -0.00590 239 SER A OG  
1869 N N   . ALA A 240 ? 0.48852 0.31612 0.55606 0.15804  -0.01431 0.01144  240 ALA A N   
1870 C CA  . ALA A 240 ? 0.52548 0.30205 0.57131 0.16333  -0.01649 0.00712  240 ALA A CA  
1871 C C   . ALA A 240 ? 0.55706 0.33726 0.60531 0.17226  -0.00843 -0.00972 240 ALA A C   
1872 O O   . ALA A 240 ? 0.61647 0.35810 0.64603 0.16952  -0.00879 -0.01618 240 ALA A O   
1873 C CB  . ALA A 240 ? 0.51708 0.27368 0.55798 0.17628  -0.02425 0.01493  240 ALA A CB  
1874 N N   . LYS A 241 ? 0.51357 0.34021 0.58365 0.18111  -0.00092 -0.01661 241 LYS A N   
1875 C CA  . LYS A 241 ? 0.56706 0.40144 0.63739 0.18812  0.00874  -0.03178 241 LYS A CA  
1876 C C   . LYS A 241 ? 0.51137 0.35255 0.57531 0.16963  0.01517  -0.03664 241 LYS A C   
1877 O O   . LYS A 241 ? 0.45707 0.31944 0.52911 0.15075  0.01507  -0.02798 241 LYS A O   
1878 C CB  . LYS A 241 ? 0.50521 0.38977 0.60282 0.20267  0.01547  -0.03527 241 LYS A CB  
1879 C CG  . LYS A 241 ? 0.49316 0.37873 0.60068 0.21918  0.00930  -0.03074 241 LYS A CG  
1880 C CD  . LYS A 241 ? 0.56508 0.50981 0.70569 0.22688  0.01363  -0.03009 241 LYS A CD  
1881 C CE  . LYS A 241 ? 0.62895 0.58197 0.78311 0.24539  0.00744  -0.02650 241 LYS A CE  
1882 N NZ  . LYS A 241 ? 0.59582 0.60992 0.78473 0.24914  0.01122  -0.02590 241 LYS A NZ  
1883 N N   . LYS A 242 ? 0.54000 0.36457 0.58866 0.17285  0.02041  -0.05035 242 LYS A N   
1884 C CA  . LYS A 242 ? 0.50342 0.33667 0.54456 0.15418  0.02585  -0.05533 242 LYS A CA  
1885 C C   . LYS A 242 ? 0.48529 0.33977 0.52612 0.16771  0.03740  -0.06884 242 LYS A C   
1886 O O   . LYS A 242 ? 0.52463 0.37417 0.56437 0.18968  0.04054  -0.07750 242 LYS A O   
1887 C CB  . LYS A 242 ? 0.55303 0.33944 0.56879 0.13916  0.01860  -0.05849 242 LYS A CB  
1888 C CG  . LYS A 242 ? 0.61607 0.37922 0.62987 0.12585  0.00881  -0.04447 242 LYS A CG  
1889 C CD  . LYS A 242 ? 0.78612 0.51437 0.78077 0.10432  0.00272  -0.04573 242 LYS A CD  
1890 C CE  . LYS A 242 ? 0.70553 0.46101 0.71072 0.08004  0.00294  -0.03530 242 LYS A CE  
1891 N NZ  . LYS A 242 ? 0.74537 0.49626 0.74036 0.06227  0.00147  -0.04270 242 LYS A NZ  
1892 N N   . ILE A 243 ? 0.48716 0.36731 0.52895 0.15345  0.04402  -0.06935 243 ILE A N   
1893 C CA  . ILE A 243 ? 0.48294 0.38069 0.51767 0.16165  0.05575  -0.08101 243 ILE A CA  
1894 C C   . ILE A 243 ? 0.50345 0.36376 0.50641 0.15456  0.05224  -0.09256 243 ILE A C   
1895 O O   . ILE A 243 ? 0.47146 0.31580 0.46632 0.13383  0.04388  -0.08793 243 ILE A O   
1896 C CB  . ILE A 243 ? 0.46777 0.41292 0.51893 0.14978  0.06450  -0.07332 243 ILE A CB  
1897 C CG1 . ILE A 243 ? 0.47359 0.44108 0.51757 0.15942  0.07887  -0.08318 243 ILE A CG1 
1898 C CG2 . ILE A 243 ? 0.41803 0.35771 0.46221 0.12537  0.05867  -0.06604 243 ILE A CG2 
1899 C CD1 . ILE A 243 ? 0.42679 0.42954 0.47818 0.14332  0.08636  -0.07462 243 ILE A CD1 
1900 N N   . HIS A 244 ? 0.51943 0.36754 0.50446 0.17215  0.05835  -0.10839 244 HIS A N   
1901 C CA  . HIS A 244 ? 0.57441 0.38412 0.52566 0.16753  0.05385  -0.12251 244 HIS A CA  
1902 C C   . HIS A 244 ? 0.54297 0.37869 0.48135 0.16585  0.06461  -0.12970 244 HIS A C   
1903 O O   . HIS A 244 ? 0.53788 0.40315 0.48124 0.18314  0.07878  -0.13436 244 HIS A O   
1904 C CB  . HIS A 244 ? 0.58407 0.35618 0.52052 0.18506  0.05110  -0.13487 244 HIS A CB  
1905 C CG  . HIS A 244 ? 0.63174 0.38200 0.58130 0.18678  0.04151  -0.12472 244 HIS A CG  
1906 N ND1 . HIS A 244 ? 0.65060 0.36435 0.59264 0.16981  0.02824  -0.11747 244 HIS A ND1 
1907 C CD2 . HIS A 244 ? 0.65591 0.41666 0.62454 0.20270  0.04308  -0.11958 244 HIS A CD2 
1908 C CE1 . HIS A 244 ? 0.63073 0.33216 0.58416 0.17540  0.02290  -0.10771 244 HIS A CE1 
1909 N NE2 . HIS A 244 ? 0.66830 0.39706 0.63752 0.19610  0.03088  -0.10919 244 HIS A NE2 
1910 N N   . PHE A 245 ? 0.56580 0.39188 0.48721 0.14556  0.05790  -0.13020 245 PHE A N   
1911 C CA  . PHE A 245 ? 0.59746 0.43900 0.49805 0.14385  0.06526  -0.13765 245 PHE A CA  
1912 C C   . PHE A 245 ? 0.67809 0.47651 0.53995 0.14877  0.05919  -0.15816 245 PHE A C   
1913 O O   . PHE A 245 ? 0.72926 0.48528 0.58091 0.14057  0.04474  -0.16276 245 PHE A O   
1914 C CB  . PHE A 245 ? 0.61401 0.47546 0.51907 0.12016  0.06054  -0.12501 245 PHE A CB  
1915 C CG  . PHE A 245 ? 0.56210 0.46074 0.50024 0.11403  0.06544  -0.10652 245 PHE A CG  
1916 C CD1 . PHE A 245 ? 0.54002 0.43375 0.50090 0.10680  0.05724  -0.09559 245 PHE A CD1 
1917 C CD2 . PHE A 245 ? 0.50467 0.44088 0.44889 0.11470  0.07802  -0.10005 245 PHE A CD2 
1918 C CE1 . PHE A 245 ? 0.48785 0.41304 0.47595 0.10140  0.06064  -0.08049 245 PHE A CE1 
1919 C CE2 . PHE A 245 ? 0.48841 0.45428 0.46145 0.10747  0.08106  -0.08407 245 PHE A CE2 
1920 C CZ  . PHE A 245 ? 0.47414 0.43402 0.46864 0.10145  0.07189  -0.07535 245 PHE A CZ  
1921 N N   . ALA A 246 ? 0.68382 0.49223 0.52253 0.16132  0.07033  -0.17059 246 ALA A N   
1922 C CA  . ALA A 246 ? 0.72433 0.49524 0.52059 0.16281  0.06381  -0.19084 246 ALA A CA  
1923 C C   . ALA A 246 ? 0.74403 0.52462 0.52665 0.13968  0.05575  -0.18618 246 ALA A C   
1924 O O   . ALA A 246 ? 0.79807 0.61878 0.58634 0.13620  0.06555  -0.17566 246 ALA A O   
1925 C CB  . ALA A 246 ? 0.76821 0.55492 0.55362 0.18102  0.07914  -0.20115 246 ALA A CB  
1926 N N   . ARG A 247 ? 0.83302 0.57814 0.59944 0.12303  0.03717  -0.19252 247 ARG A N   
1927 C CA  . ARG A 247 ? 0.89884 0.65484 0.65292 0.10275  0.02721  -0.18909 247 ARG A CA  
1928 C C   . ARG A 247 ? 0.96420 0.68822 0.67186 0.10387  0.01881  -0.21159 247 ARG A C   
1929 O O   . ARG A 247 ? 1.03250 0.71066 0.72184 0.10837  0.01082  -0.22833 247 ARG A O   
1930 C CB  . ARG A 247 ? 0.84829 0.60214 0.62707 0.07850  0.01135  -0.17545 247 ARG A CB  
1931 C CG  . ARG A 247 ? 0.84755 0.63419 0.66860 0.07614  0.01861  -0.15333 247 ARG A CG  
1932 C CD  . ARG A 247 ? 0.87963 0.71279 0.71187 0.07697  0.03026  -0.13943 247 ARG A CD  
1933 N NE  . ARG A 247 ? 0.96096 0.81722 0.83071 0.07098  0.03250  -0.12042 247 ARG A NE  
1934 C CZ  . ARG A 247 ? 0.79115 0.68226 0.67733 0.07213  0.04283  -0.10687 247 ARG A CZ  
1935 N NH1 . ARG A 247 ? 1.06444 0.97438 0.93479 0.07764  0.05307  -0.10731 247 ARG A NH1 
1936 N NH2 . ARG A 247 ? 0.68771 0.59313 0.60469 0.06687  0.04279  -0.09249 247 ARG A NH2 
1937 N N   . PHE A 248 ? 1.01060 0.75591 0.69632 0.10014  0.01992  -0.21215 248 PHE A N   
1938 C CA  . PHE A 248 ? 1.05931 0.77692 0.69778 0.09958  0.00993  -0.23337 248 PHE A CA  
1939 C C   . PHE A 248 ? 1.04674 0.77049 0.67847 0.07548  -0.00982 -0.22885 248 PHE A C   
1940 O O   . PHE A 248 ? 1.06008 0.75921 0.65361 0.07086  -0.02312 -0.24672 248 PHE A O   
1941 C CB  . PHE A 248 ? 1.17150 0.90715 0.78084 0.11941  0.02860  -0.24128 248 PHE A CB  
1942 C CG  . PHE A 248 ? 1.25788 0.99333 0.88026 0.13965  0.04589  -0.24604 248 PHE A CG  
1943 C CD1 . PHE A 248 ? 1.23121 0.93434 0.83516 0.14589  0.04261  -0.26394 248 PHE A CD1 
1944 C CD2 . PHE A 248 ? 1.12482 0.89313 0.77965 0.15208  0.06410  -0.23248 248 PHE A CD2 
1945 C CE1 . PHE A 248 ? 1.22818 0.93139 0.84406 0.16606  0.05719  -0.26844 248 PHE A CE1 
1946 C CE2 . PHE A 248 ? 1.13306 0.90518 0.80293 0.17048  0.07787  -0.23649 248 PHE A CE2 
1947 C CZ  . PHE A 248 ? 1.22197 0.96109 0.87160 0.17846  0.07441  -0.25458 248 PHE A CZ  
1948 N N   . ARG A 249 ? 0.93238 0.68843 0.59971 0.06119  -0.01279 -0.20649 249 ARG A N   
1949 C CA  . ARG A 249 ? 0.90214 0.67271 0.56935 0.04132  -0.03046 -0.19966 249 ARG A CA  
1950 C C   . ARG A 249 ? 0.84341 0.63370 0.55849 0.02721  -0.03476 -0.17930 249 ARG A C   
1951 O O   . ARG A 249 ? 0.78681 0.58486 0.53059 0.03400  -0.02205 -0.16866 249 ARG A O   
1952 C CB  . ARG A 249 ? 0.95210 0.75333 0.59811 0.04682  -0.02396 -0.19287 249 ARG A CB  
1953 C CG  . ARG A 249 ? 1.03951 0.84550 0.66498 0.03227  -0.04519 -0.19503 249 ARG A CG  
1954 C CD  . ARG A 249 ? 1.12277 0.95627 0.72419 0.03915  -0.03858 -0.18556 249 ARG A CD  
1955 N NE  . ARG A 249 ? 1.15029 0.99259 0.74157 0.05782  -0.01247 -0.18316 249 ARG A NE  
1956 C CZ  . ARG A 249 ? 1.12838 0.99916 0.74624 0.06160  0.00374  -0.16246 249 ARG A CZ  
1957 N NH1 . ARG A 249 ? 1.15970 1.04960 0.81222 0.05053  -0.00299 -0.14312 249 ARG A NH1 
1958 N NH2 . ARG A 249 ? 1.05292 0.93382 0.66260 0.07673  0.02726  -0.16174 249 ARG A NH2 
1959 N N   . SER A 250 ? 0.82678 0.62679 0.55005 0.00811  -0.05315 -0.17463 250 SER A N   
1960 C CA  . SER A 250 ? 0.69458 0.51958 0.46108 -0.00383 -0.05619 -0.15522 250 SER A CA  
1961 C C   . SER A 250 ? 0.64737 0.50991 0.42434 0.00393  -0.04555 -0.13758 250 SER A C   
1962 O O   . SER A 250 ? 0.70846 0.58535 0.46450 0.00482  -0.05032 -0.13647 250 SER A O   
1963 C CB  . SER A 250 ? 0.71745 0.54618 0.49192 -0.02597 -0.07875 -0.15624 250 SER A CB  
1964 O OG  . SER A 250 ? 0.72533 0.58025 0.54229 -0.03534 -0.07911 -0.13802 250 SER A OG  
1965 N N   . PHE A 251 ? 0.61146 0.48710 0.41794 0.00957  -0.03188 -0.12380 251 PHE A N   
1966 C CA  . PHE A 251 ? 0.58697 0.49414 0.40767 0.01342  -0.02394 -0.10577 251 PHE A CA  
1967 C C   . PHE A 251 ? 0.54472 0.46230 0.40599 0.00776  -0.02258 -0.09272 251 PHE A C   
1968 O O   . PHE A 251 ? 0.52746 0.44427 0.40433 0.01514  -0.00965 -0.08814 251 PHE A O   
1969 C CB  . PHE A 251 ? 0.62444 0.53698 0.43039 0.02889  -0.00474 -0.10429 251 PHE A CB  
1970 C CG  . PHE A 251 ? 0.64501 0.58364 0.45638 0.03048  0.00162  -0.08658 251 PHE A CG  
1971 C CD1 . PHE A 251 ? 0.60207 0.55574 0.42993 0.02210  -0.00971 -0.07416 251 PHE A CD1 
1972 C CD2 . PHE A 251 ? 0.69911 0.64696 0.49946 0.04048  0.01923  -0.08198 251 PHE A CD2 
1973 C CE1 . PHE A 251 ? 0.59046 0.56119 0.42058 0.02471  -0.00487 -0.05804 251 PHE A CE1 
1974 C CE2 . PHE A 251 ? 0.69799 0.66434 0.50141 0.03977  0.02459  -0.06462 251 PHE A CE2 
1975 C CZ  . PHE A 251 ? 0.66704 0.64152 0.48389 0.03238  0.01188  -0.05284 251 PHE A CZ  
1976 N N   . PRO A 252 ? 0.53764 0.46704 0.41650 -0.00510 -0.03615 -0.08709 252 PRO A N   
1977 C CA  . PRO A 252 ? 0.48408 0.42186 0.39807 -0.01124 -0.03510 -0.07670 252 PRO A CA  
1978 C C   . PRO A 252 ? 0.49871 0.45541 0.43021 -0.00246 -0.02276 -0.06192 252 PRO A C   
1979 O O   . PRO A 252 ? 0.49273 0.46314 0.41561 0.00348  -0.02000 -0.05534 252 PRO A O   
1980 C CB  . PRO A 252 ? 0.47148 0.42601 0.39770 -0.02558 -0.05162 -0.07424 252 PRO A CB  
1981 C CG  . PRO A 252 ? 0.50360 0.44725 0.39975 -0.03030 -0.06467 -0.08830 252 PRO A CG  
1982 C CD  . PRO A 252 ? 0.54836 0.48298 0.41389 -0.01513 -0.05417 -0.09269 252 PRO A CD  
1983 N N   . PHE A 253 ? 0.47629 0.43142 0.43106 -0.00278 -0.01657 -0.05629 253 PHE A N   
1984 C CA  . PHE A 253 ? 0.42783 0.39769 0.39955 0.00401  -0.00629 -0.04391 253 PHE A CA  
1985 C C   . PHE A 253 ? 0.39190 0.38380 0.37115 0.00310  -0.01090 -0.03342 253 PHE A C   
1986 O O   . PHE A 253 ? 0.39246 0.39130 0.36796 0.01002  -0.00443 -0.02603 253 PHE A O   
1987 C CB  . PHE A 253 ? 0.39142 0.35673 0.38517 0.00169  -0.00318 -0.04001 253 PHE A CB  
1988 C CG  . PHE A 253 ? 0.36897 0.34735 0.37874 0.00749  0.00529  -0.02923 253 PHE A CG  
1989 C CD1 . PHE A 253 ? 0.38436 0.36106 0.39217 0.01660  0.01598  -0.02886 253 PHE A CD1 
1990 C CD2 . PHE A 253 ? 0.33149 0.32478 0.35863 0.00385  0.00253  -0.02032 253 PHE A CD2 
1991 C CE1 . PHE A 253 ? 0.35768 0.34521 0.38010 0.01955  0.02189  -0.01988 253 PHE A CE1 
1992 C CE2 . PHE A 253 ? 0.34472 0.34574 0.38333 0.00901  0.00911  -0.01224 253 PHE A CE2 
1993 C CZ  . PHE A 253 ? 0.35072 0.34770 0.38685 0.01568  0.01793  -0.01202 253 PHE A CZ  
1994 N N   . TRP A 254 ? 0.37011 0.37343 0.36106 -0.00530 -0.02207 -0.03212 254 TRP A N   
1995 C CA  . TRP A 254 ? 0.36215 0.38752 0.36178 -0.00270 -0.02697 -0.02267 254 TRP A CA  
1996 C C   . TRP A 254 ? 0.36677 0.39398 0.34222 0.00238  -0.03188 -0.02276 254 TRP A C   
1997 O O   . TRP A 254 ? 0.35438 0.39086 0.32925 0.00963  -0.03174 -0.01304 254 TRP A O   
1998 C CB  . TRP A 254 ? 0.34240 0.38666 0.36289 -0.01208 -0.03755 -0.02160 254 TRP A CB  
1999 C CG  . TRP A 254 ? 0.32260 0.36680 0.36452 -0.01781 -0.03216 -0.01906 254 TRP A CG  
2000 C CD1 . TRP A 254 ? 0.30669 0.34709 0.35721 -0.03138 -0.03660 -0.02313 254 TRP A CD1 
2001 C CD2 . TRP A 254 ? 0.32646 0.37233 0.38109 -0.01112 -0.02174 -0.01136 254 TRP A CD2 
2002 N NE1 . TRP A 254 ? 0.29398 0.33426 0.36063 -0.03285 -0.02873 -0.01712 254 TRP A NE1 
2003 C CE2 . TRP A 254 ? 0.30791 0.35258 0.37714 -0.01991 -0.01996 -0.01058 254 TRP A CE2 
2004 C CE3 . TRP A 254 ? 0.30857 0.35541 0.36210 0.00028  -0.01464 -0.00488 254 TRP A CE3 
2005 C CZ2 . TRP A 254 ? 0.28143 0.32784 0.36245 -0.01607 -0.01145 -0.00404 254 TRP A CZ2 
2006 C CZ3 . TRP A 254 ? 0.29421 0.34136 0.36040 0.00313  -0.00721 0.00005  254 TRP A CZ3 
2007 C CH2 . TRP A 254 ? 0.28129 0.32895 0.36031 -0.00418 -0.00559 0.00020  254 TRP A CH2 
2008 N N   . ARG A 255 ? 0.38818 0.40374 0.34020 -0.00055 -0.03650 -0.03348 255 ARG A N   
2009 C CA  . ARG A 255 ? 0.40810 0.42379 0.33160 0.00544  -0.03919 -0.03263 255 ARG A CA  
2010 C C   . ARG A 255 ? 0.40671 0.41456 0.31879 0.01422  -0.02315 -0.02648 255 ARG A C   
2011 O O   . ARG A 255 ? 0.40865 0.42080 0.30865 0.01962  -0.02212 -0.01650 255 ARG A O   
2012 C CB  . ARG A 255 ? 0.46524 0.46920 0.36152 0.00092  -0.04777 -0.04716 255 ARG A CB  
2013 C CG  . ARG A 255 ? 0.53843 0.54187 0.40035 0.00817  -0.04864 -0.04542 255 ARG A CG  
2014 C CD  . ARG A 255 ? 0.59863 0.59214 0.42953 0.00420  -0.06012 -0.06048 255 ARG A CD  
2015 N NE  . ARG A 255 ? 0.66363 0.66916 0.50729 -0.00674 -0.08032 -0.06473 255 ARG A NE  
2016 C CZ  . ARG A 255 ? 0.69339 0.72092 0.53911 -0.00627 -0.09468 -0.05716 255 ARG A CZ  
2017 N NH1 . ARG A 255 ? 0.70078 0.73555 0.53507 0.00509  -0.09144 -0.04380 255 ARG A NH1 
2018 N NH2 . ARG A 255 ? 0.75049 0.79324 0.61051 -0.01766 -0.11327 -0.06257 255 ARG A NH2 
2019 N N   . ARG A 256 ? 0.39533 0.39202 0.31127 0.01536  -0.01102 -0.03168 256 ARG A N   
2020 C CA  . ARG A 256 ? 0.42258 0.41842 0.33559 0.02172  0.00469  -0.02524 256 ARG A CA  
2021 C C   . ARG A 256 ? 0.42136 0.42605 0.35241 0.02256  0.00659  -0.01054 256 ARG A C   
2022 O O   . ARG A 256 ? 0.38183 0.38704 0.30212 0.02529  0.01298  -0.00113 256 ARG A O   
2023 C CB  . ARG A 256 ? 0.46740 0.45489 0.39013 0.02382  0.01487  -0.03306 256 ARG A CB  
2024 C CG  . ARG A 256 ? 0.57142 0.56014 0.48280 0.03082  0.03057  -0.03342 256 ARG A CG  
2025 C CD  . ARG A 256 ? 0.59481 0.57198 0.50124 0.03664  0.03600  -0.04803 256 ARG A CD  
2026 N NE  . ARG A 256 ? 0.54684 0.52040 0.48021 0.03697  0.03685  -0.04823 256 ARG A NE  
2027 C CZ  . ARG A 256 ? 0.57428 0.53161 0.51221 0.03404  0.02820  -0.05607 256 ARG A CZ  
2028 N NH1 . ARG A 256 ? 0.58329 0.52680 0.50328 0.02899  0.01721  -0.06571 256 ARG A NH1 
2029 N NH2 . ARG A 256 ? 0.60099 0.55488 0.56079 0.03507  0.02982  -0.05370 256 ARG A NH2 
2030 N N   . VAL A 257 ? 0.38475 0.39513 0.34074 0.01981  0.00046  -0.00836 257 VAL A N   
2031 C CA  . VAL A 257 ? 0.36992 0.38587 0.34057 0.02237  0.00123  0.00318  257 VAL A CA  
2032 C C   . VAL A 257 ? 0.34431 0.36410 0.30135 0.02638  -0.00740 0.01091  257 VAL A C   
2033 O O   . VAL A 257 ? 0.33538 0.34986 0.28715 0.03028  -0.00385 0.02130  257 VAL A O   
2034 C CB  . VAL A 257 ? 0.34187 0.36470 0.33952 0.01996  -0.00197 0.00266  257 VAL A CB  
2035 C CG1 . VAL A 257 ? 0.23492 0.26309 0.24310 0.02503  -0.00336 0.01236  257 VAL A CG1 
2036 C CG2 . VAL A 257 ? 0.30612 0.32227 0.31605 0.01775  0.00664  -0.00167 257 VAL A CG2 
2037 N N   . HIS A 258 ? 0.33297 0.36128 0.28477 0.02528  -0.02030 0.00648  258 HIS A N   
2038 C CA  . HIS A 258 ? 0.37960 0.41296 0.31734 0.03124  -0.03051 0.01417  258 HIS A CA  
2039 C C   . HIS A 258 ? 0.43589 0.45581 0.34200 0.03402  -0.02420 0.02002  258 HIS A C   
2040 O O   . HIS A 258 ? 0.46140 0.47512 0.35816 0.03967  -0.02447 0.03246  258 HIS A O   
2041 C CB  . HIS A 258 ? 0.37053 0.41868 0.30756 0.02810  -0.04664 0.00702  258 HIS A CB  
2042 C CG  . HIS A 258 ? 0.38481 0.43775 0.29973 0.03463  -0.05901 0.01287  258 HIS A CG  
2043 N ND1 . HIS A 258 ? 0.46890 0.51059 0.34774 0.03506  -0.05922 0.01160  258 HIS A ND1 
2044 C CD2 . HIS A 258 ? 0.36158 0.43078 0.28433 0.04216  -0.07240 0.01978  258 HIS A CD2 
2045 C CE1 . HIS A 258 ? 0.46610 0.51453 0.32938 0.04191  -0.07283 0.01868  258 HIS A CE1 
2046 N NE2 . HIS A 258 ? 0.49760 0.56306 0.38840 0.04701  -0.08155 0.02370  258 HIS A NE2 
2047 N N   . ASP A 259 ? 0.41678 0.43044 0.30567 0.03035  -0.01701 0.01160  259 ASP A N   
2048 C CA  . ASP A 259 ? 0.53013 0.53534 0.38682 0.03243  -0.00955 0.01695  259 ASP A CA  
2049 C C   . ASP A 259 ? 0.54987 0.54823 0.41130 0.03217  0.00479  0.02918  259 ASP A C   
2050 O O   . ASP A 259 ? 0.54923 0.54014 0.38905 0.03355  0.00714  0.04154  259 ASP A O   
2051 C CB  . ASP A 259 ? 0.53821 0.54027 0.37646 0.03051  -0.00402 0.00282  259 ASP A CB  
2052 C CG  . ASP A 259 ? 0.55942 0.56352 0.38115 0.02929  -0.02073 -0.00813 259 ASP A CG  
2053 O OD1 . ASP A 259 ? 0.53386 0.54633 0.35759 0.03028  -0.03622 -0.00284 259 ASP A OD1 
2054 O OD2 . ASP A 259 ? 0.60234 0.59983 0.40942 0.02775  -0.01922 -0.02262 259 ASP A OD2 
2055 N N   . SER A 260 ? 0.48797 0.48782 0.37720 0.02940  0.01303  0.02689  260 SER A N   
2056 C CA  . SER A 260 ? 0.54374 0.53861 0.43915 0.02663  0.02531  0.03716  260 SER A CA  
2057 C C   . SER A 260 ? 0.50190 0.48779 0.40455 0.02849  0.01888  0.04920  260 SER A C   
2058 O O   . SER A 260 ? 0.56048 0.53535 0.45454 0.02545  0.02508  0.06105  260 SER A O   
2059 C CB  . SER A 260 ? 0.47953 0.48039 0.40042 0.02367  0.03500  0.02988  260 SER A CB  
2060 O OG  . SER A 260 ? 0.54412 0.55022 0.45698 0.02462  0.04255  0.01906  260 SER A OG  
2061 N N   . PHE A 261 ? 0.46792 0.45769 0.38554 0.03341  0.00691  0.04648  261 PHE A N   
2062 C CA  . PHE A 261 ? 0.47589 0.45650 0.40273 0.03799  0.00227  0.05517  261 PHE A CA  
2063 C C   . PHE A 261 ? 0.46589 0.44544 0.38187 0.04800  -0.01195 0.06112  261 PHE A C   
2064 O O   . PHE A 261 ? 0.46803 0.43185 0.37921 0.05387  -0.01490 0.07120  261 PHE A O   
2065 C CB  . PHE A 261 ? 0.40590 0.39376 0.36285 0.03796  0.00267  0.04815  261 PHE A CB  
2066 C CG  . PHE A 261 ? 0.41418 0.40193 0.38359 0.03024  0.01465  0.04428  261 PHE A CG  
2067 C CD1 . PHE A 261 ? 0.43333 0.40902 0.40288 0.02573  0.02168  0.05162  261 PHE A CD1 
2068 C CD2 . PHE A 261 ? 0.35959 0.35865 0.34097 0.02742  0.01751  0.03364  261 PHE A CD2 
2069 C CE1 . PHE A 261 ? 0.42033 0.40122 0.40404 0.01896  0.03100  0.04815  261 PHE A CE1 
2070 C CE2 . PHE A 261 ? 0.38705 0.38774 0.38077 0.02300  0.02709  0.03053  261 PHE A CE2 
2071 C CZ  . PHE A 261 ? 0.37305 0.36769 0.36936 0.01901  0.03362  0.03761  261 PHE A CZ  
2072 N N   . ILE A 262 ? 0.47732 0.47228 0.38921 0.05054  -0.02200 0.05501  262 ILE A N   
2073 C CA  . ILE A 262 ? 0.49982 0.50041 0.40687 0.06146  -0.03739 0.06021  262 ILE A CA  
2074 C C   . ILE A 262 ? 0.55924 0.54849 0.42937 0.06390  -0.04160 0.06931  262 ILE A C   
2075 O O   . ILE A 262 ? 0.59929 0.57363 0.45523 0.07279  -0.04718 0.08212  262 ILE A O   
2076 C CB  . ILE A 262 ? 0.41784 0.44608 0.34516 0.06166  -0.04830 0.04943  262 ILE A CB  
2077 C CG1 . ILE A 262 ? 0.44082 0.47877 0.40057 0.05755  -0.04196 0.04213  262 ILE A CG1 
2078 C CG2 . ILE A 262 ? 0.46297 0.50446 0.39088 0.07443  -0.06493 0.05493  262 ILE A CG2 
2079 C CD1 . ILE A 262 ? 0.36304 0.40010 0.34051 0.06759  -0.04170 0.04736  262 ILE A CD1 
2080 N N   . GLU A 263 ? 0.54398 0.53778 0.39550 0.05710  -0.03921 0.06289  263 GLU A N   
2081 C CA  . GLU A 263 ? 0.72694 0.70773 0.53863 0.05700  -0.03729 0.07169  263 GLU A CA  
2082 C C   . GLU A 263 ? 0.80032 0.79043 0.59447 0.05135  -0.03615 0.05906  263 GLU A C   
2083 O O   . GLU A 263 ? 0.74721 0.75218 0.55786 0.04874  -0.04296 0.04469  263 GLU A O   
2084 C CB  . GLU A 263 ? 0.85367 0.82893 0.64498 0.06867  -0.05332 0.08420  263 GLU A CB  
2085 C CG  . GLU A 263 ? 1.01902 0.97267 0.76605 0.06886  -0.04941 0.09971  263 GLU A CG  
2086 C CD  . GLU A 263 ? 1.00132 0.93252 0.74508 0.06085  -0.03105 0.11105  263 GLU A CD  
2087 O OE1 . GLU A 263 ? 0.98477 0.91091 0.75762 0.05964  -0.02664 0.11052  263 GLU A OE1 
2088 O OE2 . GLU A 263 ? 0.98380 0.90374 0.69545 0.05483  -0.02105 0.12051  263 GLU A OE2 
2089 N N   . ASP A 264 ? 1.03206 1.01218 0.79108 0.04912  -0.02738 0.06424  264 ASP A N   
2090 C CA  . ASP A 264 ? 0.94525 0.93075 0.68129 0.04578  -0.02434 0.05120  264 ASP A CA  
2091 C C   . ASP A 264 ? 1.12395 1.10108 0.81128 0.04862  -0.02506 0.06069  264 ASP A C   
2092 O O   . ASP A 264 ? 1.28174 1.25819 0.95074 0.05515  -0.04239 0.06744  264 ASP A O   
2093 C CB  . ASP A 264 ? 0.91215 0.89838 0.65985 0.03945  -0.00395 0.04267  264 ASP A CB  
2094 C CG  . ASP A 264 ? 1.01666 1.00697 0.74748 0.03869  -0.00252 0.02418  264 ASP A CG  
2095 O OD1 . ASP A 264 ? 1.07527 1.06825 0.79259 0.04021  -0.01953 0.01579  264 ASP A OD1 
2096 O OD2 . ASP A 264 ? 0.96958 0.96050 0.70042 0.03712  0.01468  0.01739  264 ASP A OD2 
# 
