data_8QGJ
# 
_entry.id   8QGJ 
# 
_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   8QGJ         pdb_00008qgj 10.2210/pdb8qgj/pdb 
WWPDB D_1292133172 ?            ?                   
# 
_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                        8QGJ 
_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 
;~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-4-carbamimidamido-butanamide
;
696.674   1  ?        ? ? ? 
4 water       nat water 18.015    43 ?        ? ? ? 
# 
_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 
;~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-4-carbamimidamido-butanamide
;
UX6 
4 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   TYR n 
1 4   MET n 
1 5   ILE n 
1 6   THR n 
1 7   SER n 
1 8   LYS n 
1 9   GLY n 
1 10  ASP n 
1 11  GLU n 
1 12  LYS n 
1 13  SER n 
1 14  ASP n 
1 15  LEU n 
1 16  LEU n 
1 17  ARG n 
1 18  LEU n 
1 19  ASN n 
1 20  MET n 
1 21  ILE n 
1 22  ALA n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  GLU n 
1 27  TYR n 
1 28  ASP n 
1 29  MET n 
1 30  GLU n 
1 31  TYR n 
1 32  ASP n 
1 33  ASP n 
1 34  VAL n 
1 35  GLU n 
1 36  PRO n 
1 37  GLU n 
1 38  ILE n 
1 39  VAL n 
1 40  ILE n 
1 41  SER n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  ASP n 
1 46  GLY n 
1 47  THR n 
1 48  PHE n 
1 49  LEU n 
1 50  SER n 
1 51  ALA n 
1 52  PHE n 
1 53  HIS n 
1 54  GLN n 
1 55  TYR n 
1 56  GLU n 
1 57  GLU n 
1 58  ARG n 
1 59  LEU n 
1 60  ASP n 
1 61  GLU n 
1 62  ILE n 
1 63  ALA n 
1 64  PHE n 
1 65  ILE n 
1 66  GLY n 
1 67  ILE n 
1 68  HIS n 
1 69  THR n 
1 70  GLY n 
1 71  HIS n 
1 72  LEU n 
1 73  GLY n 
1 74  PHE n 
1 75  TYR n 
1 76  ALA n 
1 77  ASP n 
1 78  TRP n 
1 79  ARG n 
1 80  PRO n 
1 81  ALA n 
1 82  GLU n 
1 83  ALA n 
1 84  ASP n 
1 85  LYS n 
1 86  LEU n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  LYS n 
1 93  GLY n 
1 94  GLU n 
1 95  TYR n 
1 96  GLN n 
1 97  LYS n 
1 98  VAL n 
1 99  SER n 
1 100 TYR n 
1 101 PRO n 
1 102 LEU n 
1 103 LEU n 
1 104 LYS n 
1 105 THR n 
1 106 THR n 
1 107 VAL n 
1 108 LYS n 
1 109 TYR n 
1 110 GLY n 
1 111 ILE n 
1 112 GLY n 
1 113 LYS n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 THR n 
1 118 TYR n 
1 119 LEU n 
1 120 ALA n 
1 121 LEU n 
1 122 ASN n 
1 123 GLU n 
1 124 SER n 
1 125 THR n 
1 126 VAL n 
1 127 LYS n 
1 128 SER n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 PRO n 
1 133 PHE n 
1 134 VAL n 
1 135 VAL n 
1 136 ASP n 
1 137 VAL n 
1 138 VAL n 
1 139 ILE n 
1 140 ASN n 
1 141 ASP n 
1 142 ILE n 
1 143 HIS n 
1 144 PHE n 
1 145 GLU n 
1 146 ARG n 
1 147 PHE n 
1 148 ARG n 
1 149 GLY n 
1 150 ASP n 
1 151 GLY n 
1 152 LEU n 
1 153 CYS n 
1 154 MET n 
1 155 SER n 
1 156 THR n 
1 157 PRO n 
1 158 SER n 
1 159 GLY n 
1 160 THR n 
1 161 THR n 
1 162 ALA n 
1 163 TYR n 
1 164 ASN n 
1 165 LYS n 
1 166 SER n 
1 167 LEU n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 LEU n 
1 172 MET n 
1 173 HIS n 
1 174 PRO n 
1 175 SER n 
1 176 ILE n 
1 177 GLU n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 LEU n 
1 182 THR n 
1 183 GLU n 
1 184 MET n 
1 185 ALA n 
1 186 SER n 
1 187 ILE n 
1 188 ASN n 
1 189 ASN n 
1 190 ARG n 
1 191 VAL n 
1 192 TYR n 
1 193 ARG n 
1 194 THR n 
1 195 ILE n 
1 196 GLY n 
1 197 SER n 
1 198 PRO n 
1 199 LEU n 
1 200 VAL n 
1 201 PHE n 
1 202 PRO n 
1 203 LYS n 
1 204 HIS n 
1 205 HIS n 
1 206 VAL n 
1 207 VAL n 
1 208 SER n 
1 209 LEU n 
1 210 GLN n 
1 211 PRO n 
1 212 VAL n 
1 213 ASN n 
1 214 ASP n 
1 215 LYS n 
1 216 ASP n 
1 217 PHE n 
1 218 GLN n 
1 219 ILE n 
1 220 SER n 
1 221 VAL n 
1 222 ASP n 
1 223 HIS n 
1 224 LEU n 
1 225 SER n 
1 226 ILE n 
1 227 LEU n 
1 228 HIS n 
1 229 ARG n 
1 230 ASP n 
1 231 VAL n 
1 232 GLN n 
1 233 GLU n 
1 234 ILE n 
1 235 ARG n 
1 236 TYR n 
1 237 GLU n 
1 238 VAL n 
1 239 SER n 
1 240 ALA n 
1 241 LYS n 
1 242 LYS n 
1 243 ILE n 
1 244 HIS n 
1 245 PHE n 
1 246 ALA n 
1 247 ARG n 
1 248 PHE n 
1 249 ARG n 
1 250 SER n 
1 251 PHE n 
1 252 PRO n 
1 253 PHE n 
1 254 TRP n 
1 255 ARG n 
1 256 ARG n 
1 257 VAL n 
1 258 HIS n 
1 259 ASP n 
1 260 SER n 
1 261 PHE n 
1 262 ILE n 
1 263 GLU n 
1 264 ASP n 
1 265 LEU n 
1 266 GLU n 
1 267 HIS n 
1 268 HIS n 
1 269 HIS n 
1 270 HIS n 
1 271 HIS n 
1 272 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   272 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nadK1, lmo0968' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Listeria monocytogenes EGD-e' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     169963 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CIT non-polymer         . 'CITRIC ACID' ? 'C6 H8 O7'       192.124 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
UX6 non-polymer         . 
;~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-4-carbamimidamido-butanamide
;
? 'C28 H36 N14 O8' 696.674 
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        UX6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UX6 
_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 UX6 1  302 1  UX6 XXX A . 
D 4 HOH 1  401 25 HOH HOH A . 
D 4 HOH 2  402 8  HOH HOH A . 
D 4 HOH 3  403 50 HOH HOH A . 
D 4 HOH 4  404 9  HOH HOH A . 
D 4 HOH 5  405 5  HOH HOH A . 
D 4 HOH 6  406 22 HOH HOH A . 
D 4 HOH 7  407 7  HOH HOH A . 
D 4 HOH 8  408 44 HOH HOH A . 
D 4 HOH 9  409 30 HOH HOH A . 
D 4 HOH 10 410 31 HOH HOH A . 
D 4 HOH 11 411 29 HOH HOH A . 
D 4 HOH 12 412 6  HOH HOH A . 
D 4 HOH 13 413 1  HOH HOH A . 
D 4 HOH 14 414 2  HOH HOH A . 
D 4 HOH 15 415 26 HOH HOH A . 
D 4 HOH 16 416 4  HOH HOH A . 
D 4 HOH 17 417 37 HOH HOH A . 
D 4 HOH 18 418 3  HOH HOH A . 
D 4 HOH 19 419 12 HOH HOH A . 
D 4 HOH 20 420 23 HOH HOH A . 
D 4 HOH 21 421 14 HOH HOH A . 
D 4 HOH 22 422 32 HOH HOH A . 
D 4 HOH 23 423 17 HOH HOH A . 
D 4 HOH 24 424 28 HOH HOH A . 
D 4 HOH 25 425 19 HOH HOH A . 
D 4 HOH 26 426 24 HOH HOH A . 
D 4 HOH 27 427 16 HOH HOH A . 
D 4 HOH 28 428 15 HOH HOH A . 
D 4 HOH 29 429 27 HOH HOH A . 
D 4 HOH 30 430 10 HOH HOH A . 
D 4 HOH 31 431 11 HOH HOH A . 
D 4 HOH 32 432 41 HOH HOH A . 
D 4 HOH 33 433 42 HOH HOH A . 
D 4 HOH 34 434 39 HOH HOH A . 
D 4 HOH 35 435 18 HOH HOH A . 
D 4 HOH 36 436 43 HOH HOH A . 
D 4 HOH 37 437 40 HOH HOH A . 
D 4 HOH 38 438 34 HOH HOH A . 
D 4 HOH 39 439 47 HOH HOH A . 
D 4 HOH 40 440 49 HOH HOH A . 
D 4 HOH 41 441 45 HOH HOH A . 
D 4 HOH 42 442 46 HOH HOH A . 
D 4 HOH 43 443 48 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'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QGJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.020 
_cell.length_a_esd                 ? 
_cell.length_b                     74.914 
_cell.length_b_esd                 ? 
_cell.length_c                     118.490 
_cell.length_c_esd                 ? 
_cell.volume                       559400.807 
_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                         8QGJ 
_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                   8QGJ 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.39 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-06-11 
_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   0.87313 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.87313 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          38.14 
_reflns.entry_id                                       8QGJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.29 
_reflns.d_resolution_low                               63.32 
_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                                     22928 
_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                           97.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_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                                0.331 
_reflns.pdbx_Rpim_I_all                                0.142 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.981 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.29 
_reflns_shell.d_res_low                                     2.37 
_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                             1161 
_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                               4.7 
_reflns_shell.pdbx_chi_squared                              0.81 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.815 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.683 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.712 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.94 
_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                                 8QGJ 
_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                             63.32 
_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                     22928 
_refine.ls_number_reflns_R_free                  1157 
_refine.ls_number_reflns_R_work                  21771 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.69 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2276 
_refine.ls_R_factor_R_free                       0.2658 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2257 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.8857 
_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                            0.3862 
_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                        63.32 
_refine_hist.number_atoms_solvent             43 
_refine_hist.number_atoms_total               2180 
_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         63 
_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' ? 0.0033  ? 2195 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6016  ? 2974 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0477  ? 321  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0032  ? 408  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.8063 ? 826  ? 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 2.39  . . 146 2606 89.23 . . . . 0.3581 . . . . . . . . . . . 0.3705 
'X-RAY DIFFRACTION' 2.39 2.52  . . 157 2687 93.52 . . . . 0.3249 . . . . . . . . . . . 0.3894 
'X-RAY DIFFRACTION' 2.52 2.68  . . 165 2690 93.42 . . . . 0.3042 . . . . . . . . . . . 0.3527 
'X-RAY DIFFRACTION' 2.68 2.88  . . 164 2759 95.43 . . . . 0.3064 . . . . . . . . . . . 0.3427 
'X-RAY DIFFRACTION' 2.88 3.17  . . 144 2750 95.10 . . . . 0.2734 . . . . . . . . . . . 0.3475 
'X-RAY DIFFRACTION' 3.17 3.63  . . 137 2765 95.12 . . . . 0.2174 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 3.63 4.58  . . 124 2735 93.49 . . . . 0.1695 . . . . . . . . . . . 0.1958 
'X-RAY DIFFRACTION' 4.58 63.32 . . 120 2779 94.28 . . . . 0.1744 . . . . . . . . . . . 0.1853 
# 
_struct.entry_id                     8QGJ 
_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        8QGJ 
_struct_keywords.text            'tetrameric NAD-kinase, Transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NADK1_LISMO 
_struct_ref.pdbx_db_accession          Q8Y8D7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIED
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QGJ 
_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 8QGJ LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGJ GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGJ HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGJ HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGJ HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGJ HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGJ HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGJ HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D 
1 2 A,B,C,D 
1 3 A,B,C,D 
1 4 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 63.0200000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 63.0200000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLU A 26  ? ASP A 10  GLU A 26  1 ? 17 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 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 ? 6 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 2 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA2 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? GLY A 149 ? ILE A 142 GLY A 149 
AA3 1 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 2 ALA A 178 ? MET A 184 ? ALA A 178 MET A 184 
AA3 3 GLY A 151 ? SER A 155 ? GLY A 151 SER A 155 
AA3 4 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 5 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 6 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 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 ILE A 139 ? N ILE A 139 O ILE A 142 ? O ILE A 142 
AA3 1 2 O PHE A 201 ? O PHE A 201 N MET A 179 ? N MET A 179 
AA3 2 3 O GLN A 180 ? O GLN A 180 N SER A 155 ? N SER A 155 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 5 6 N VAL A 221 ? N VAL A 221 O LEU A 224 ? O LEU A 224 
# 
_pdbx_entry_details.entry_id                   8QGJ 
_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 ARG A 58  ? ? -142.02 37.31   
2  1 TYR A 109 ? ? -125.56 -156.76 
3  1 ASN A 122 ? ? -95.68  -73.83  
4  1 ALA A 162 ? ? -103.75 -127.32 
5  1 ASN A 189 ? ? -149.84 -159.16 
6  1 HIS A 204 ? ? 69.01   -0.39   
7  1 ASN A 213 ? ? -127.14 -90.25  
8  1 ASP A 222 ? ? 64.04   -126.14 
9  1 GLU A 233 ? ? -171.37 137.44  
10 1 ILE A 262 ? ? -95.27  -60.26  
11 1 GLU A 263 ? ? -176.45 134.38  
# 
_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     415 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 13.0021132916 23.9127869917 19.1395696236  0.430650716428 ? 0.047567807094  ? 0.0382079702863 ? 
0.430557405714 ? -0.0431906793274 ? 0.393436640431 ? 2.25802531042 ? -0.492928351265 ? -1.53842325675   ? 0.915285065214 ? 
0.504447702699 ? 3.28715747577 ? 0.0536371681733 ? -0.34572443331  ? 0.150328129439 ? 0.200048394374   ? 0.001754381687   ? 
0.133774182504 ? -0.184723678941  ? 0.139161607688  ? -0.0156250397201  ? 
2 'X-RAY DIFFRACTION' ? refined 20.2784861619 13.023625088  -1.25897686215 0.24348842504  ? 0.0394746798946 ? 0.0151266993604 ? 
0.339356967622 ? 0.00660806687766 ? 0.310381137328 ? 1.27632084993 ? -0.302606029344 ? -0.0103858574262 ? 1.8310294407   ? 
0.111809918643 ? 2.53735700973 ? 0.0849844634584 ? 0.0296742833887 ? 0.053075880673 ? -0.0862866238652 ? -0.0584552472754 ? 
0.123268742226 ? -0.0784786910757 ? -0.280489205932 ? -0.00543616332642 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 1   ? A 117 A 120 ? ? 
;chain 'A' and (resid    1  through  120 )
;
2 'X-RAY DIFFRACTION' 2 A 118 A 121 ? A 261 A 264 ? ? 
;chain 'A' and (resid  121  through  264 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
UX6 N1   N N N 393 
UX6 C7   C N R 394 
UX6 C8   C N R 395 
UX6 N2   N N N 396 
UX6 C9   C N S 397 
UX6 O1   O N N 398 
UX6 C1   C N N 399 
UX6 O5   O N N 400 
UX6 C5   C N N 401 
UX6 C6   C N R 402 
UX6 N3   N N N 403 
UX6 C4   C N N 404 
UX6 O4   O N N 405 
UX6 C3   C N N 406 
UX6 O3   O N N 407 
UX6 C2   C N N 408 
UX6 N4   N Y N 409 
UX6 N    N N N 410 
UX6 C    C N N 411 
UX6 O    O N N 412 
UX6 C10  C Y N 413 
UX6 C11  C Y N 414 
UX6 C12  C Y N 415 
UX6 C13  C Y N 416 
UX6 C14  C Y N 417 
UX6 C15  C N N 418 
UX6 C16  C N N 419 
UX6 C17  C N N 420 
UX6 C18  C N N 421 
UX6 C19  C N R 422 
UX6 C20  C N R 423 
UX6 C21  C N R 424 
UX6 C22  C N S 425 
UX6 C23  C Y N 426 
UX6 C24  C Y N 427 
UX6 C25  C Y N 428 
UX6 C26  C Y N 429 
UX6 C27  C Y N 430 
UX6 N10  N Y N 431 
UX6 N11  N N N 432 
UX6 N12  N Y N 433 
UX6 N13  N Y N 434 
UX6 N5   N Y N 435 
UX6 N6   N N N 436 
UX6 N7   N Y N 437 
UX6 N8   N Y N 438 
UX6 N9   N Y N 439 
UX6 O2   O N N 440 
UX6 O6   O N N 441 
UX6 O7   O N N 442 
UX6 H6   H N N 443 
UX6 H1   H N N 444 
UX6 H17  H N N 445 
UX6 H7   H N N 446 
UX6 H19  H N N 447 
UX6 H9   H N N 448 
UX6 H8   H N N 449 
UX6 H15  H N N 450 
UX6 H16  H N N 451 
UX6 H    H N N 452 
UX6 H14  H N N 453 
UX6 H13  H N N 454 
UX6 H12  H N N 455 
UX6 H20  H N N 456 
UX6 H10  H N N 457 
UX6 H11  H N N 458 
UX6 H4   H N N 459 
UX6 H5   H N N 460 
UX6 H23  H N N 461 
UX6 H24  H N N 462 
UX6 H25  H N N 463 
UX6 H27  H N N 464 
UX6 H26  H N N 465 
UX6 H2   H N N 466 
UX6 H3   H N N 467 
UX6 H28  H N N 468 
UX6 H30  H N N 469 
UX6 H32  H N N 470 
UX6 H35  H N N 471 
UX6 H33  H N N 472 
UX6 H34  H N N 473 
UX6 H21  H N N 474 
UX6 H22  H N N 475 
UX6 H18  H N N 476 
UX6 H29  H N N 477 
UX6 H31  H N N 478 
VAL N    N N N 479 
VAL CA   C N S 480 
VAL C    C N N 481 
VAL O    O N N 482 
VAL CB   C N N 483 
VAL CG1  C N N 484 
VAL CG2  C N N 485 
VAL OXT  O N N 486 
VAL H    H N N 487 
VAL H2   H N N 488 
VAL HA   H N N 489 
VAL HB   H N N 490 
VAL HG11 H N N 491 
VAL HG12 H N N 492 
VAL HG13 H N N 493 
VAL HG21 H N N 494 
VAL HG22 H N N 495 
VAL HG23 H N N 496 
VAL HXT  H N N 497 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
UX6 N   C    sing N N 378 
UX6 N1  C    doub N N 379 
UX6 C   N2   sing N N 380 
UX6 N2  C1   sing N N 381 
UX6 C1  C2   sing N N 382 
UX6 C2  C3   sing N N 383 
UX6 C3  C4   sing N N 384 
UX6 C4  O    doub N N 385 
UX6 N3  C4   sing N N 386 
UX6 C5  N3   sing N N 387 
UX6 C6  C5   sing N N 388 
UX6 C6  O1   sing N N 389 
UX6 O1  C7   sing N N 390 
UX6 C7  C8   sing N N 391 
UX6 O2  C8   sing N N 392 
UX6 C8  C9   sing N N 393 
UX6 C9  C6   sing N N 394 
UX6 O3  C9   sing N N 395 
UX6 N4  C7   sing N N 396 
UX6 N4  C10  sing Y N 397 
UX6 C10 N5   doub Y N 398 
UX6 N5  C11  sing Y N 399 
UX6 C11 C12  doub Y N 400 
UX6 N6  C12  sing N N 401 
UX6 C12 N7   sing Y N 402 
UX6 N7  C13  doub Y N 403 
UX6 C13 N8   sing Y N 404 
UX6 N8  C14  doub Y N 405 
UX6 C14 N4   sing Y N 406 
UX6 C11 C14  sing Y N 407 
UX6 C15 C10  sing N N 408 
UX6 C16 C15  trip N N 409 
UX6 C17 C16  sing N N 410 
UX6 O4  C17  sing N N 411 
UX6 C18 O4   sing N N 412 
UX6 C19 C18  sing N N 413 
UX6 C19 O5   sing N N 414 
UX6 O5  C20  sing N N 415 
UX6 C20 C21  sing N N 416 
UX6 O6  C21  sing N N 417 
UX6 C21 C22  sing N N 418 
UX6 C22 C19  sing N N 419 
UX6 O7  C22  sing N N 420 
UX6 N9  C20  sing N N 421 
UX6 N9  C23  sing Y N 422 
UX6 C23 N10  doub Y N 423 
UX6 N10 C24  sing Y N 424 
UX6 C24 C25  doub Y N 425 
UX6 N11 C25  sing N N 426 
UX6 C25 N12  sing Y N 427 
UX6 N12 C26  doub Y N 428 
UX6 C26 N13  sing Y N 429 
UX6 N13 C27  doub Y N 430 
UX6 C27 N9   sing Y N 431 
UX6 C24 C27  sing Y N 432 
UX6 N1  H6   sing N N 433 
UX6 C7  H1   sing N N 434 
UX6 C8  H17  sing N N 435 
UX6 N2  H7   sing N N 436 
UX6 C9  H19  sing N N 437 
UX6 C1  H9   sing N N 438 
UX6 C1  H8   sing N N 439 
UX6 C5  H15  sing N N 440 
UX6 C5  H16  sing N N 441 
UX6 C6  H    sing N N 442 
UX6 N3  H14  sing N N 443 
UX6 C3  H13  sing N N 444 
UX6 C3  H12  sing N N 445 
UX6 O3  H20  sing N N 446 
UX6 C2  H10  sing N N 447 
UX6 C2  H11  sing N N 448 
UX6 N   H4   sing N N 449 
UX6 N   H5   sing N N 450 
UX6 C13 H23  sing N N 451 
UX6 C17 H24  sing N N 452 
UX6 C17 H25  sing N N 453 
UX6 C18 H27  sing N N 454 
UX6 C18 H26  sing N N 455 
UX6 C19 H2   sing N N 456 
UX6 C20 H3   sing N N 457 
UX6 C21 H28  sing N N 458 
UX6 C22 H30  sing N N 459 
UX6 C23 H32  sing N N 460 
UX6 C26 H35  sing N N 461 
UX6 N11 H33  sing N N 462 
UX6 N11 H34  sing N N 463 
UX6 N6  H21  sing N N 464 
UX6 N6  H22  sing N N 465 
UX6 O2  H18  sing N N 466 
UX6 O6  H29  sing N N 467 
UX6 O7  H31  sing N N 468 
VAL N   CA   sing N N 469 
VAL N   H    sing N N 470 
VAL N   H2   sing N N 471 
VAL CA  C    sing N N 472 
VAL CA  CB   sing N N 473 
VAL CA  HA   sing N N 474 
VAL C   O    doub N N 475 
VAL C   OXT  sing N N 476 
VAL CB  CG1  sing N N 477 
VAL CB  CG2  sing N N 478 
VAL CB  HB   sing N N 479 
VAL CG1 HG11 sing N N 480 
VAL CG1 HG12 sing N N 481 
VAL CG1 HG13 sing N N 482 
VAL CG2 HG21 sing N N 483 
VAL CG2 HG22 sing N N 484 
VAL CG2 HG23 sing N N 485 
VAL OXT HXT  sing N N 486 
# 
_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                    8QGJ 
_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]   0.015868 
_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]   0.013349 
_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]   0.008440 
_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   ? 12.01181 36.28948 25.20915  1.000 86.50676  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.92295 36.59775 24.28885  1.000 82.85405  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.92396  35.44434 24.22086  1.000 75.13010  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.83990  34.63594 25.14341  1.000 68.31406  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.47794 36.91818 22.89629  1.000 86.30600  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.46954 35.89383 22.36489  1.000 85.00852  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 13.96806 36.63340 21.67630  1.000 108.97591 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.18237 36.16804 22.91101  1.000 80.07914  ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.16100  35.37920 23.13144  1.000 74.65364  ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.20214  34.29529 22.95750  1.000 65.97406  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.92874  32.98238 22.68464  1.000 56.41425  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.96768  32.95292 22.01859  1.000 53.31269  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.22962  34.61767 21.82253  1.000 60.95876  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.20461  35.68748 22.17598  0.800 66.74629  ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.32312  36.04117 20.98608  0.700 67.40805  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.33511  37.14657 21.33827  0.700 67.50008  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.57419  37.62659 20.14979  0.700 62.35884  ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.37766  31.89317 23.21539  1.000 56.26830  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.01782  30.58905 23.14552  1.000 49.85211  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.95627  29.50876 23.26537  1.000 50.91032  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.86417  29.73706 23.79351  1.000 51.41444  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.05958 30.40124 24.25773  1.000 45.85418  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.44040  30.03521 25.59502  1.000 50.51985  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.89528  31.00952 26.41864  1.000 54.82964  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.39312  28.71591 26.02746  1.000 45.35403  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.32536  30.68406 27.63173  1.000 52.66654  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.82229  28.38250 27.24034  1.000 48.88003  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.29215  29.37038 28.04045  1.000 50.57462  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.72165  29.04182 29.25246  1.000 48.81275  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.30463  28.31635 22.78986  1.000 42.41741  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.48110  27.13710 23.00254  1.000 42.39553  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.40931  25.94212 23.14173  1.000 40.19627  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.59929  26.01913 22.82827  1.000 39.97265  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.47074  26.94335 21.86728  1.000 47.20216  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.08208  26.51491 20.54599  1.000 42.01445  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.26838  24.73103 20.43013  1.000 42.80459  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.57659  24.20694 20.71321  1.000 46.41770  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.85410  24.83027 23.62485  1.000 40.34549  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.61995  23.61305 23.87694  1.000 40.41305  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.78828  22.41815 23.43486  1.000 43.56742  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.65546  22.24623 23.89734  1.000 44.15820  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 9.00594  23.45799 25.35849  1.000 41.24873  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.66028  24.73431 25.89747  1.000 42.28636  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.92911  22.26282 25.53151  1.000 40.38948  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.96368  24.68845 27.37779  1.000 38.75206  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.34691  21.58904 22.55390  1.000 42.13700  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.72663  20.33203 22.15793  1.000 43.32274  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.33001  19.18375 22.95720  1.000 41.78547  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.46919  19.25466 23.42522  1.000 46.15272  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 7.89698  20.06244 20.65645  1.000 46.33258  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 9.27938  20.16441 20.29450  1.000 48.95897  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.08967  21.04732 19.83734  1.000 49.95002  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.55517  18.11754 23.10707  1.000 41.73171  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 7.96666  16.97945 23.91188  1.000 46.99769  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.75847  15.69231 23.13054  1.000 51.77269  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.79333  15.56604 22.37105  1.000 54.35489  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.18519  16.92929 25.23521  1.000 47.89092  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.52500  15.78483 25.99684  1.000 44.65809  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.67837  14.74032 23.31362  1.000 47.56535  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.49889  13.41304 22.73857  1.000 46.10052  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.22428  12.75113 23.24791  1.000 50.70451  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.67301  11.87789 22.57018  1.000 55.37348  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.73354  12.55026 23.03774  1.000 51.14216  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.57175  11.05664 22.76870  1.000 55.80134  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.74374 10.47887 21.99070  1.000 58.27756  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.60778 8.96528  21.83866  1.000 68.06322  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 9.31247  8.55724  21.20982  1.000 62.61088  ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.72421  13.16815 24.40564  1.000 52.62151  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.47166  12.65597 24.90889  1.000 50.38235  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.59197  11.51207 25.88360  1.000 50.46888  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.56455  10.94760 26.27644  1.000 59.69050  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.80542  11.14017 26.27709  1.000 46.89559  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 6.97950  10.15486 27.32656  1.000 53.13681  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 6.99279  10.86460 28.67999  1.000 60.08371  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 6.92853  12.09426 28.76409  1.000 55.76597  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.24896  9.33388  27.09239  1.000 50.93669  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.52062  10.16241 27.19214  1.000 57.09764  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.43412  11.40409 27.27108  1.000 58.55737  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.61673 9.56283  27.19325  1.000 62.41263  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.08270  10.08261 29.75919  1.000 61.22838  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.07667  10.67499 31.09466  1.000 60.80726  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.28382  11.58065 31.31063  1.000 57.71815  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.15811  12.66613 31.89004  1.000 58.18083  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.03593  9.58015  32.16037  1.000 66.19064  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.63903  9.18703  32.60220  0.800 65.45648  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.65420  8.32233  33.84346  0.700 69.71411  ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.75148  8.10762  34.39985  0.700 71.26148  ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 4.57333  7.85896  34.26383  0.700 74.30786  ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.46131  11.15347 30.84977  1.000 60.59949  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.67674 11.92630 31.08758  1.000 58.30455  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.59135 13.30359 30.44149  1.000 57.09022  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.84304 14.32560 31.09082  1.000 56.61421  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.89449 11.16293 30.56499  1.000 60.57622  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.22638 11.77264 30.97642  0.800 65.60327  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.39033 10.84036 30.67716  0.700 66.83971  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.40024 10.86340 31.81250  0.700 66.87518  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 15.77226 12.25405 32.18542  0.600 68.22963  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.22664 13.35239 29.16071  1.000 57.43564  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.26233 14.62024 28.44099  1.000 52.01341  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.14432  15.55271 28.88992  1.000 51.25435  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.37075  16.75531 29.06618  1.000 50.48393  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.18874 14.36236 26.93903  1.000 47.36313  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.15672 13.39828 26.56398  1.000 49.49474  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.93208  15.02315 29.07630  1.000 49.55600  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.82605  15.86227 29.52935  1.000 50.57264  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.16541  16.56146 30.83459  1.000 49.78563  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.88648  17.75486 31.00344  1.000 46.33228  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.55990  15.02610 29.70293  1.000 51.45488  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.86035  14.75730 28.39575  1.000 55.16811  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.25548  15.36638 27.37997  1.000 55.61318  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.91709  13.93726 28.38441  1.000 57.05829  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.78084  15.83074 31.76602  1.000 52.83941  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.09373  16.39447 33.07439  1.000 52.57327  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.19397  17.44047 32.97291  1.000 48.60354  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.13234  18.47987 33.63794  1.000 45.82673  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.49409  15.27930 34.03984  1.000 51.54721  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.39007  14.58064 34.84247  1.000 62.70431  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 7.14387  15.30647 36.15808  1.000 55.62446  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 6.08909  14.45466 34.04802  1.000 59.02895  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.20810 17.18629 32.14331  1.000 50.14173  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.24697 18.18785 31.93799  1.000 47.43987  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.65953 19.46080 31.34394  1.000 46.14571  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 11.03427 20.57266 31.73740  1.000 43.98886  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.34688 17.62755 31.04110  1.000 49.44513  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.58254 18.51771 30.90575  1.000 56.44119  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.17399 18.80470 32.28370  1.000 58.07461  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.61394 17.87806 29.98417  1.000 46.36707  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.71110  19.31355 30.41577  1.000 47.72831  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.08378  20.47363 29.79222  1.000 46.54491  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.32180  21.30390 30.81975  1.000 42.50473  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.45925  22.53190 30.86764  1.000 42.22774  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.16236  20.01453 28.65988  1.000 44.77113  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.38986  21.12744 27.98275  1.000 42.82585  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.45546  20.56941 26.92125  1.000 43.57982  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.58959  21.59999 26.36457  1.000 39.76489  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.41609  21.94601 26.87440  1.000 43.85576  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.93155  21.35798 27.95670  1.000 44.12583  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.71070  22.90622 26.28344  1.000 45.35406  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.51736  20.64787 31.66044  1.000 46.90188  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.77507  21.37934 32.68563  1.000 46.54392  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.71488  22.09245 33.65023  1.000 44.55342  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.42351  23.20731 34.09799  1.000 45.09766  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.84034  20.43623 33.44450  1.000 50.10386  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.38357  20.35160 32.97272  1.000 45.70946  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 4.29987  19.85985 31.55114  1.000 46.46341  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.58148  19.44275 33.88372  1.000 50.82727  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.85603  21.47573 33.96939  1.000 44.97983  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.81353  22.12205 34.86187  1.000 46.14737  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.51594 23.29425 34.19266  1.000 48.35958  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.84989 24.27285 34.86949  1.000 50.37919  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.84183 21.11314 35.36597  1.000 47.03931  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.35306 20.34441 36.57664  1.000 48.62899  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.46451  20.79928 37.29499  1.000 49.34674  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 10.93248 19.17411 36.80883  1.000 49.34963  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.75066 23.22348 32.87746  1.000 44.00520  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.35993 24.35803 32.19004  1.000 43.54472  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.37030 25.50466 32.03506  1.000 45.58331  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.74119 26.67392 32.19082  1.000 49.47349  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.90377 23.92727 30.82963  1.000 44.98140  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.08551 22.97923 30.91858  1.000 47.28818  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.77805 22.56707 29.30788  1.000 44.80469  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.42291 24.16226 28.80085  1.000 46.73824  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.10810  25.18949 31.72890  1.000 46.07290  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.06877  26.21669 31.68736  1.000 48.57757  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 8.00139  26.95786 33.01539  1.000 44.87032  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.87211  28.18763 33.05229  1.000 47.01926  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.70916  25.59189 31.32240  1.000 47.12730  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.76736  24.95807 29.93456  1.000 45.88736  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.61710  26.64137 31.35961  1.000 47.34059  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.60292  24.04226 29.63914  1.000 43.61806  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.09531  26.22294 34.12697  1.000 47.90280  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 8.09592  26.86166 35.44017  1.000 52.32007  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.31132  27.76272 35.61351  1.000 48.72938  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.20842  28.85556 36.18313  1.000 53.04715  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 8.05059  25.80417 36.54129  1.000 48.52740  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.47134 27.32458 35.12279  1.000 48.17384  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.64915 28.17582 35.17278  1.000 53.93806  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.50091 29.42803 34.32954  1.000 53.51060  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.92420 30.51484 34.73333  1.000 55.22981  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.89393 29.29528 33.14695  1.000 52.21831  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.68286 30.46235 32.29671  1.000 57.39012  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.65573  31.41647 32.89439  1.000 56.80181  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.70862  32.62400 32.63223  1.000 60.91912  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.25509 30.03123 30.89170  1.000 53.45484  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.37384 29.47197 30.06012  1.000 51.11640  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.48017 30.24652 29.75812  1.000 53.49006  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.31367 28.17868 29.56788  1.000 48.64577  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.51149 29.73720 28.99114  1.000 58.13142  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.34205 27.66360 28.80097  1.000 46.30062  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.44065 28.44431 28.51150  1.000 53.81147  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.72073  30.90351 33.69580  1.000 57.96864  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.77897  31.77774 34.36819  1.000 57.64475  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.43905  32.79804 35.26772  1.000 59.83967  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.85333  33.85054 35.53788  1.000 63.35093  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.65903  32.51751 35.72495  1.000 62.70805  ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.39322 33.41198 36.61142  1.000 63.69948  ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.09531 34.54686 35.87808  1.000 70.03195  ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.68235 35.41140 36.53966  1.000 65.92265  ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.41967 32.61440 37.41692  1.000 57.50102  ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.80866 31.50077 38.23455  1.000 54.58153  ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.77762  32.01317 39.21749  1.000 70.13483  ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 9.99562  33.09948 39.80325  1.000 74.50733  ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.74577  31.33147 39.39849  1.000 68.16022  ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.05261 34.56389 34.54647  1.000 70.63391  ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.67099 35.59825 33.72451  1.000 72.41227  ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.61757 36.25281 32.83413  1.000 80.99706  ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.44404  35.87019 32.82677  1.000 77.37199  ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.80026 35.02335 32.86372  1.000 68.69169  ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.92423 34.36558 33.63144  1.000 66.43507  ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.86642 33.01859 33.96671  1.000 60.67463  ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 15.05570 35.08487 33.99942  1.000 66.92503  ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.89542 32.40985 34.65857  1.000 58.86438  ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 16.09293 34.48343 34.69295  1.000 59.92878  ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 16.00575 33.14583 35.01938  1.000 56.28102  ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 17.03114 32.54096 35.70819  1.000 55.61013  ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 11.06155 37.24633 32.06251  1.000 105.08864 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.21493 37.91467 31.07494  1.000 107.42474 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 10.10001 37.05121 29.81582  1.000 96.48785  ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.49585 37.43265 28.71435  1.000 97.58811  ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.76940 39.29727 30.75235  1.000 121.47423 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.77722  40.16585 29.99832  1.000 121.01032 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 8.56369  39.87193 30.05935  1.000 116.11362 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 10.21282 41.13791 29.34205  1.000 118.00797 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.55274  35.85322 30.00718  1.000 87.17305  ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.34560  34.89233 28.93236  1.000 80.08350  ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.86368  34.56424 28.84486  1.000 74.93719  ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.24620  34.18987 29.84731  1.000 77.50766  ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.15890 33.61219 29.15846  1.000 72.54837  ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.65934 33.83286 29.29486  1.000 73.26452  ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.45579 34.37883 27.77429  1.000 80.29313  ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 13.05944 32.82308 27.12203  1.000 67.51661  ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.30018  34.71266 27.65168  1.000 68.33537  ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.90402  34.40230 27.38335  1.000 67.94089  ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.82754  33.16329 26.50002  1.000 65.89674  ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.48189  33.10273 25.45337  1.000 60.07395  ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.20653  35.58575 26.70660  1.000 74.28279  ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.95874  35.20556 25.92173  1.000 80.11244  ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.36077  36.37408 25.15768  1.000 83.55305  ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 4.08460  37.36242 24.90234  1.000 79.81436  ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.16104  36.30017 24.81493  1.000 87.93255  ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.03509  32.17865 26.92352  1.000 64.12368  ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.84612  30.96207 26.14225  1.000 55.63947  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.89869  31.25262 24.98482  1.000 60.09454  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.75015  31.65545 25.20011  1.000 59.53468  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.30079  29.82868 27.01219  1.000 47.86192  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.21697  28.49219 26.29642  1.000 49.71902  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.11761  28.16608 25.50841  1.000 49.72461  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.24204  27.56101 26.40240  1.000 51.28398  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.04252  26.95476 24.84638  1.000 45.96425  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.17565  26.34233 25.74134  1.000 47.85887  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.07284  26.04625 24.96656  1.000 46.85460  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.00208  24.83789 24.31187  1.000 48.37257  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.37686  31.04779 23.75972  1.000 50.16253  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.55447  31.24781 22.57044  1.000 53.04400  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 4.00587  30.23130 21.53454  1.000 53.46116  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 5.13026  30.31804 21.03348  1.000 54.36813  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.68896  32.67309 22.03958  1.000 60.45798  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.62495  33.02187 21.01278  1.000 61.59853  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 1.88547  32.11372 20.57888  1.000 63.07775  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.52156  34.21239 20.64688  1.000 65.64158  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 3.15238  29.26019 21.22799  1.000 50.63546  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.47953  28.30251 20.18598  1.000 55.21498  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.93389  28.71886 18.82342  1.000 57.75734  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.98647  27.92647 17.87624  1.000 57.83197  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.98882  26.90073 20.56869  1.000 52.19219  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.47680  26.78678 20.61648  1.000 57.21222  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.77080  27.79258 20.38114  1.000 60.19846  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.99243  25.66878 20.89392  1.000 56.80754  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.41739  29.94153 18.70600  1.000 56.16327  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.94587  30.45898 17.42905  1.000 57.26162  ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.09156  31.18167 16.73804  1.000 58.20992  ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.47754  30.83062 15.61754  1.000 57.07167  ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.73451  31.38768 17.61052  1.000 55.17220  ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.22066  31.85037 16.25551  1.000 52.38760  ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.35531 30.67152 18.38708  1.000 59.00145  ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.65112  32.18861 17.40248  1.000 58.16231  ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.79451  32.93756 16.87891  1.000 56.83873  ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.93798  32.94890 17.88901  1.000 55.73443  ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.35106  34.01130 18.36282  1.000 56.49071  ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.38229  34.36370 16.51705  1.000 59.09042  ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.46596  34.48242 15.31358  0.700 60.48626  ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 3.02655  35.91449 15.06938  0.600 72.88769  ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 3.00783  36.70219 16.03956  0.600 72.71076  ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 2.70739  36.25600 13.91025  0.600 74.35462  ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.48703  31.78496 18.23551  1.000 53.65013  ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.65109  31.77257 19.12357  1.000 53.89049  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.88406  32.31039 18.41627  1.000 51.63767  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.96815  32.34922 17.18778  1.000 54.27418  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.81743  30.29083 19.47327  1.000 50.39996  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.26593  29.58006 18.29725  1.000 51.47556  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 6.11779  30.42052 17.81393  1.000 53.32042  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.84532  32.75580 19.22388  1.000 51.65992  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.17056 33.09007 18.73058  1.000 47.02549  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.21938 32.07520 19.14369  1.000 47.61678  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.31447 32.07384 18.57695  1.000 48.89604  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.60023 34.47631 19.22638  1.000 52.22297  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.51371 35.52955 19.13295  0.800 59.91863  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 11.06977 36.93756 19.12300  0.700 64.55945  ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 12.03601 37.19046 18.37169  0.700 66.95122  ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.54458 37.78967 19.86843  0.700 66.37168  ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.91227 31.22629 20.11705  1.000 47.36906  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.78038 30.13895 20.53328  1.000 39.84415  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.94361 28.87468 20.57677  1.000 38.50149  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.88908 28.84667 21.21775  1.000 40.14290  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.42011 30.41179 21.90337  1.000 43.30098  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 14.32191 31.63869 21.82177  1.000 48.68198  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 14.19339 29.19504 22.37939  1.000 44.55887  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.46370 31.47239 20.86429  1.000 53.75060  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.39683 27.83940 19.88296  1.000 39.49213  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.73331 26.54342 19.88977  1.000 38.31110  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.67562 25.54717 20.54187  1.000 38.00487  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.79109 25.32515 20.05681  1.000 37.13213  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.33672 26.09110 18.47829  1.000 36.51863  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.91274 24.64063 18.50875  1.000 35.82389  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.20420 26.95384 17.95295  1.000 41.97173  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.23987 24.97212 21.65079  1.000 38.66662  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.99642 23.95513 22.36446  1.000 37.11146  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.33847 22.61303 22.09729  1.000 37.01811  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.10660 22.50031 22.08580  1.000 38.61874  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 13.05892 24.25703 23.87455  1.000 41.56325  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.70657 25.62124 24.11201  1.000 43.14983  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.81850 23.15778 24.62400  1.000 36.49467  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.87414 25.95835 25.57006  1.000 45.19047  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.15684 21.59723 21.86388  1.000 37.36053  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.68251 20.25981 21.55823  1.000 39.42662  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.28632 19.29629 22.56497  1.000 36.18965  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.50878 19.26227 22.73678  1.000 36.91167  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.05626 19.86921 20.12264  1.000 38.76950  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.96797 18.47064 19.92396  1.000 41.90143  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.43253 18.52737 23.23393  1.000 36.63334  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.85331 17.58977 24.27023  1.000 41.54133  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.47918 16.18845 23.80928  1.000 39.31178  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.29205 15.84431 23.73983  1.000 40.96599  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.21892 17.90731 25.63077  1.000 42.89156  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.44986 19.36830 26.00670  1.000 40.53602  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.80699 17.01896 26.70390  1.000 48.11601  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 11.83837 19.74562 27.32886  1.000 39.82732  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.48819 15.37687 23.50912  1.000 40.68975  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.27413 14.03207 23.01326  1.000 43.77725  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.44996 13.51760 22.20768  1.000 46.69126  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.57435 13.44049 22.71392  1.000 52.44956  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.20244 13.15629 20.95234  1.000 43.87826  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.26247 12.69130 20.08006  1.000 38.92061  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.40689 13.55003 18.83891  1.000 37.92428  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.87354 14.66210 18.77900  1.000 35.75219  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.12928 13.04831 17.83609  1.000 40.80976  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.25909 13.79609 16.59165  1.000 33.27543  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 14.94663 13.82791 15.81757  1.000 32.60501  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.62916 14.83951 15.18302  1.000 36.00174  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.38611 13.20706 15.74400  1.000 34.50909  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.76295 13.52172 16.30621  1.000 37.67110  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 18.96058 14.65326 16.80409  1.000 39.79060  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.64571 12.64039 16.25186  1.000 37.30834  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.16805 12.74672 15.86130  1.000 33.31485  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.83727 12.79425 15.27598  1.000 33.21979  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 11.98008 13.88596 15.88843  1.000 37.45925  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.33757 14.66371 15.17719  1.000 37.69016  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 11.96996 13.96294 17.22512  1.000 40.80946  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.26181 15.03873 17.91174  1.000 34.07172  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.75535 16.40054 17.44358  1.000 32.50964  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.95583 17.31594 17.21862  1.000 36.55156  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.42721 14.88790 19.42842  1.000 43.32235  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 10.95949 13.59555 19.83217  1.000 48.53870  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.64211 15.96157 20.18498  1.000 34.51154  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.06865 16.54921 17.26847  1.000 34.06975  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.59582 17.80495 16.74487  1.000 36.71401  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.15576 18.03006 15.30006  1.000 38.51081  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.74218 19.13684 14.93453  1.000 41.24198  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.12046 17.83613 16.85416  1.000 33.26367  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.71420 19.15802 16.46834  1.000 39.98927  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.97268 19.45778 15.13795  1.000 41.71824  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.98434 20.11509 17.42706  1.000 39.12926  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.50191 20.67723 14.77511  1.000 35.89336  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.51508 21.33885 17.06837  1.000 43.21015  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.77234 21.61790 15.73655  1.000 38.51821  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.24981 16.99661 14.45909  1.000 34.42965  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.79586 17.13221 13.07774  1.000 39.97968  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.31941 17.50792 13.01550  1.000 39.88529  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.92131 18.35316 12.20487  1.000 37.83104  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 13.05460 15.83589 12.30603  1.000 39.85006  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.49838 15.52536 11.90636  1.000 34.16256  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.65736 14.04724 11.61934  1.000 36.56537  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.89876 16.33845 10.69589  1.000 34.64605  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.49105 16.89216 13.86512  1.000 40.24904  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 9.08271  17.27688 13.92526  1.000 40.08671  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.92872  18.74739 14.28781  1.000 40.08077  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.03528  19.43161 13.77434  1.000 42.86773  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.32960  16.40744 14.93471  1.000 41.62208  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 7.95586  15.15929 14.37890  1.000 48.25542  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.79169  19.25191 15.17236  1.000 39.24087  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.68534  20.64385 15.59376  1.000 40.80712  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.09489 21.59081 14.47601  1.000 40.72115  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.47652  22.64507 14.28934  1.000 40.56811  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.53891 20.87949 16.83901  1.000 41.16545  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.14250 21.23515 13.73179  1.000 38.27482  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.56260 22.05352 12.60073  1.000 40.95070  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.44576 22.18979 11.57548  1.000 39.25164  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 10.18827 23.28755 11.06912  1.000 40.85981  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.81515 21.44887 11.96601  1.000 40.00547  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 13.11409 21.96851 10.59556  1.000 40.48263  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.78151 23.17025 10.42676  1.000 41.45554  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.74343 21.24587 9.46884   1.000 41.48435  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 14.06283 23.64607 9.15883   1.000 40.23793  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 13.01850 21.71933 8.20392   1.000 38.07172  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.67829 22.91917 8.04875   1.000 36.08313  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.76324  21.08695 11.26304  1.000 41.31475  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.70059  21.13501 10.26603  1.000 42.06925  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.44997  21.81824 10.78863  1.000 47.02610  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.63789  22.29574 9.99068   1.000 48.47977  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.37023  19.72684 9.78772   1.000 37.28599  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.43666  19.12935 8.92898   1.000 42.04232  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.71120  19.59203 7.66167   1.000 42.04133  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.31320 18.12482 9.16110   1.000 46.46763  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.70268 18.88977 7.14433   1.000 42.11992  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.08689 17.99366 8.03379   1.000 43.54772  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.27885  21.87776 12.10705  1.000 46.97632  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 6.13355  22.58151 12.66391  1.000 43.76241  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.24626  24.08249 12.43260  1.000 42.40051  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.22775  24.77732 12.34922  1.000 48.25543  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 6.01554  22.25439 14.15384  1.000 44.96720  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.74709  22.72328 14.82917  1.000 47.96473  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.71052  22.34070 16.29727  1.000 58.45931  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.35384  21.37623 16.71414  1.000 59.00783  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.96329  23.10092 17.09162  1.000 58.49705  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.46809  24.59423 12.29578  1.000 44.04281  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.70247  26.02603 12.16447  1.000 44.06505  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.57061  26.34789 10.95440  1.000 48.55724  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.26225  27.36970 10.93744  1.000 50.26488  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.33765  26.58454 13.43623  1.000 48.45946  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.45633  26.46669 14.65432  1.000 48.70868  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.40284  27.34686 14.85660  1.000 49.47767  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.67353  25.47598 15.59911  1.000 47.78756  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.59008  27.24348 15.96369  1.000 54.03283  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.86339  25.36598 16.71487  1.000 52.25170  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.82334  26.25342 16.89114  1.000 53.90520  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 5.01233  26.15440 17.99890  1.000 52.80928  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.54064  25.49702 9.92538   1.000 56.21017  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.31478  25.77987 8.71962   1.000 60.21907  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.83507  27.02958 7.99655   1.000 52.35386  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.52839  27.50692 7.09180   1.000 54.35072  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.28071  24.58094 7.76892   1.000 50.56885  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.89259  24.05327 7.47686   1.000 53.24196  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.91966  22.73891 6.72243   1.000 59.64245  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 9.01880  22.30328 6.31988   1.000 51.21119  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 6.84038  22.13873 6.53498   1.000 71.70624  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.68190  27.57205 8.37281   1.000 52.90707  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.18375  28.80985 7.79504   1.000 58.96482  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.72749  30.04752 8.49428   1.000 55.52124  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.39023  31.16306 8.09173   1.000 60.23085  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.65203  28.82947 7.83499   1.000 59.46696  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 4.97951  28.86265 6.46723   1.000 67.07708  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 5.06428  27.53767 5.72337   0.700 68.67500  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 6.12102  27.24827 5.12166   0.700 65.86492  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 4.06736  26.78463 5.73896   0.700 70.42708  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.55239  29.88350 9.52586   1.000 51.64418  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 9.08283  31.00859 10.28966  1.000 54.11509  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.52824 30.74621 10.68137  1.000 52.88764  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.96913 31.10898 11.77680  1.000 55.48700  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.23569  31.28733 11.53617  1.000 55.31301  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.87626  31.92641 11.25751  1.000 59.31559  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 6.11317  32.29094 12.53921  1.000 62.24698  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.73447  33.37433 13.29846  1.000 60.35083  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.37323  33.21244 14.45094  1.000 59.12264  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.49181  32.02114 15.01438  1.000 54.01940  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.90057  34.27282 15.05662  1.000 57.89344  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.28864 30.11466 9.78693   1.000 52.30316  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.64846 29.71556 10.13143  1.000 50.84153  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.52975 30.92230 10.41493  1.000 54.49159  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.39975 30.87271 11.29258  1.000 53.84500  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.24257 28.86778 9.01258   1.000 44.72452  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.53802 27.52408 8.86083   1.000 47.76919  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.14675 26.73297 7.72966   1.000 42.11375  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.60629 26.74646 10.16311  1.000 43.43577  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.31481 32.01942 9.69141   1.000 54.60839  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 14.13181 33.20877 9.88689   1.000 57.40633  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.82633 33.92383 11.19696  1.000 55.59265  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.59749 34.80219 11.59549  1.000 59.12843  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.94443 34.16503 8.70538   1.000 61.27332  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 15.25787 34.74757 8.20975   1.000 67.21071  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 16.21766 33.97246 8.00197   1.000 69.24943  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.32727 35.97954 8.01580   1.000 71.28449  ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.73976 33.56674 11.88015  1.000 53.27289  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.33953 34.23500 13.11088  1.000 53.36985  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.49771 33.35177 14.34499  1.000 53.00656  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.01926 33.71907 15.42378  1.000 51.89719  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 10.89028 34.72161 12.99837  1.000 58.26162  ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.66171 35.80721 11.94927  1.000 62.35004  ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 10.03178 35.27525 10.67109  0.700 63.34679  ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 9.37282  34.21702 10.72765  0.700 62.49656  ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 10.19482 35.91500 9.60932   0.700 62.77008  ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.16479 32.20775 14.22255  1.000 52.39810  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.21689 31.21633 15.29046  1.000 47.26143  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.63596 30.68379 15.41805  1.000 47.08982  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.29916 30.40571 14.41358  1.000 43.52498  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.23147 30.05935 15.02272  1.000 45.76097  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.78972 30.55062 15.11352  1.000 48.46780  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.46689 28.91033 15.98477  1.000 40.83044  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.78624  29.51485 14.71104  1.000 47.95613  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 15.09903 30.54130 16.65688  1.000 43.00258  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.32606 29.82376 16.96930  1.000 39.96145  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.96196 28.53977 17.70010  1.000 40.49000  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.23219 28.57465 18.69666  1.000 44.41496  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.26604 30.67852 17.82015  1.000 48.56604  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.46720 27.41514 17.20694  1.000 38.98911  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 16.11083 26.10875 17.73968  1.000 38.36987  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.11945 25.64186 18.78604  1.000 41.84875  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.30049 25.99734 18.74799  1.000 42.58319  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 16.02121 25.07321 16.61362  1.000 39.97682  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.86875 25.29093 15.67136  1.000 38.19845  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 14.98395 26.16916 14.60321  1.000 39.65937  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.67124 24.61430 15.85104  1.000 35.43465  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.92284 26.37254 13.73176  1.000 37.32901  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.60729 24.81190 14.98805  1.000 35.05790  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.73288 25.69241 13.92601  1.000 38.21245  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.62963 24.84582 19.73491  1.000 41.25681  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.45962 24.14904 20.71347  1.000 43.02314  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.88195 22.75553 20.90132  1.000 38.53658  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.66071 22.58353 20.95971  1.000 40.55926  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.52685 24.88724 22.07104  1.000 39.97102  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 18.19638 26.24723 21.92278  1.000 44.63931  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.28732 24.06896 23.09654  1.000 43.01313  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.24353 27.38731 22.07537  1.000 53.15004  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.75405 21.75993 20.99700  1.000 42.78744  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.28968 20.41613 21.26636  1.000 42.06726  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 17.89335 19.80957 22.51562  1.000 48.39559  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.10920 19.86279 22.71524  1.000 50.94110  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.05042 19.23121 23.36492  1.000 46.92619  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.47784 18.50306 24.55292  1.000 42.74545  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.22097 17.02688 24.30110  1.000 48.88325  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.13135 16.65423 23.85097  1.000 53.84019  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.72450 18.98871 25.80227  1.000 47.11661  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 16.95437 20.48256 26.00093  1.000 43.26551  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 17.13859 18.20013 27.04153  1.000 49.64150  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 15.98841 21.09617 26.94855  1.000 39.21535  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.21510 16.18622 24.57413  1.000 51.59062  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.08217 14.75033 24.35309  1.000 52.19510  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.82298 14.07000 25.69188  1.000 60.30748  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.68632 14.06050 26.57586  1.000 62.05420  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.31164 14.17545 23.64725  1.000 62.25848  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.54499 14.12448 24.49341  1.000 63.75317  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 20.82368 13.06969 25.33635  1.000 72.05840  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.57633 14.99216 24.62345  1.000 65.06756  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 21.97179 13.29093 25.95178  1.000 70.52313  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.44953 14.45069 25.53673  1.000 69.27512  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.61804 13.52597 25.84900  1.000 60.05488  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.29586 12.74476 27.03347  1.000 66.36252  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.70564 11.28613 26.90048  1.000 77.93002  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 16.75672 10.57400 27.91239  1.000 75.49241  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.79897 12.83466 27.34174  1.000 60.94560  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.04874 12.72445 26.12779  1.000 53.83495  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.48306 14.15585 28.01430  1.000 62.32013  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 16.99197 10.83214 25.68179  1.000 76.18913  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.58911 9.53097  25.46143  1.000 76.12395  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 19.06652 9.65632  25.15527  1.000 77.59089  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.78514 10.38701 25.84301  1.000 74.00296  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.53395 8.96064  24.12303  1.000 93.28210  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 20.92910 9.07285  23.73150  1.000 96.51065  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.20243 10.45315 23.13506  1.000 94.16188  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.28899 11.23504 22.85227  1.000 89.64686  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.29659 7.97858  22.72815  1.000 91.66919  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 20.60218 8.10950  21.40622  1.000 95.05890  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 20.91473 9.09424  20.49265  1.000 92.08049  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 19.61226 7.37667  20.84316  1.000 94.57664  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 20.14633 8.96413  19.42617  1.000 84.53589  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 19.34761 7.92882  19.61279  1.000 91.46551  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.48645 10.74644 22.94013  1.000 80.56503  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 22.87382 11.98400 22.27684  1.000 74.37383  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.36295 11.99510 20.84040  1.000 73.96801  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.58793 11.05004 20.07825  1.000 76.56801  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.39507 12.14693 22.30187  1.000 67.10390  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 24.99744 13.24873 21.42115  1.000 66.51724  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 24.50217 14.62938 21.83301  1.000 59.55592  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.51925 13.19215 21.44750  1.000 59.52284  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 21.65277 13.06052 20.48133  1.000 64.72360  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.23755 13.26859 19.10988  1.000 55.84366  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.08805 14.33600 18.45748  1.000 50.71241  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 22.72714 15.12973 19.15424  1.000 54.29032  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.11602 14.37267 17.12641  1.000 44.61387  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.92623 15.38123 16.45552  1.000 44.01826  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.31845 16.76609 16.60252  1.000 43.17319  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.04099 17.74707 16.80756  1.000 47.91326  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.10966 15.02345 14.98038  1.000 38.52493  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.44780 14.45315 14.68590  1.000 36.21175  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.71077 13.12383 14.95146  1.000 37.12949  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.46453 15.25458 14.19940  1.000 37.83080  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.95591 12.58832 14.70573  1.000 41.69177  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.71718 14.72804 13.95293  1.000 39.47735  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 26.96338 13.39045 14.20674  1.000 40.56508  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 20.99676 16.86785 16.50574  1.000 42.13923  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.34239 18.15990 16.63357  1.000 44.05422  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 19.99728 18.47737 18.07834  1.000 43.73593  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.07485 19.63820 18.49577  1.000 48.57588  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.08435 18.19349 15.76787  1.000 45.03130  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.35535 17.98323 14.29241  1.000 41.62671  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.13702 18.88179 13.57555  1.000 36.87287  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.81807 16.89609 13.61878  1.000 36.74880  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.38339 18.70032 12.22955  1.000 34.25655  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 19.05595 16.70478 12.27100  1.000 38.26214  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.83916 17.60988 11.57980  1.000 37.67015  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.07550 17.41798 10.23729  1.000 37.53865  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.61619 17.46175 18.84736  1.000 46.09119  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.34868 17.61321 20.27618  1.000 52.78422  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 20.62524 17.25191 21.02097  1.000 50.19560  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 20.82028 16.11183 21.44425  1.000 53.49927  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.17625 16.73698 20.69998  1.000 51.17594  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.51102 18.23465 21.18445  1.000 47.03948  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.85406 17.98060 21.68892  1.000 55.94386  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 23.10887 18.61771 23.05730  1.000 60.08385  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.25469 18.91848 23.39740  1.000 63.09409  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.89619 18.44672 20.67020  1.000 54.73090  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.73574 19.90872 20.29014  1.000 61.10853  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.81735 20.56865 20.82543  1.000 62.10001  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.52988 20.39619 19.45340  1.000 57.20235  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 22.06034 18.81393 23.85944  1.000 53.72426  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 22.19515 19.30629 25.22474  1.000 61.60113  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.42361 18.38480 26.16218  1.000 59.02041  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.35602 17.87628 25.80937  1.000 57.27711  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 21.70881 20.76471 25.34737  1.000 59.62396  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 22.15872 21.63060 24.18987  0.700 64.71282  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.36160 22.20165 23.24081  0.700 68.57017  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 23.50929 21.99143 23.84463  0.700 71.74284  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.12404 22.90313 22.33561  0.700 67.02636  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 23.44420 22.79182 22.68358  0.700 67.34353  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 24.76274 21.72438 24.40878  0.700 70.00251  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 24.58239 23.32332 22.07430  0.700 65.70375  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 25.89409 22.25354 23.79905  0.700 67.00599  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 25.79334 23.04478 22.64540  0.700 64.35137  ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 21.98054 18.16115 27.36588  1.000 57.62520  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.54186 17.10055 28.26372  1.000 61.88607  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.43418 17.57558 29.20263  1.000 62.53806  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.33213 18.76961 29.50372  1.000 61.24702  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.72227 16.58913 29.08386  1.000 67.02009  ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 23.67763 15.69173 28.31289  1.000 67.38135  ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 25.04528 15.70373 28.96303  0.800 69.49676  ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.94935 15.61594 30.41546  0.700 67.62692  ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 25.85050 16.10887 31.25446  0.600 73.20160  ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 26.92168 16.75114 30.81774  0.600 76.77030  ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 25.66868 15.96118 32.56432  0.600 60.50968  ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.59411 16.65253 29.68642  1.000 58.93379  ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.47150 17.07156 30.54690  1.000 60.37477  ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 18.90801 17.70571 31.85512  1.000 65.69748  ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.23008 18.61521 32.35197  1.000 63.36257  ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.70312 15.76201 30.78690  1.000 60.64648  ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 18.14273 14.84282 29.69412  1.000 63.26127  ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.56461 15.20730 29.40562  1.000 59.15113  ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.01476 17.24645 32.44141  1.000 62.68434  ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.46907 17.82142 33.70093  1.000 59.52743  ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 20.98531 19.24238 33.53378  1.000 58.35172  ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.12947 19.95807 34.52740  1.000 66.35029  ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.54960 16.94187 34.32220  1.000 67.72260  ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.26321 19.66834 32.30913  1.000 59.93479  ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.68898 21.03107 32.03768  1.000 57.52751  ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.52471 21.94033 31.66837  1.000 57.97963  ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.75255 23.05372 31.18480  1.000 60.27145  ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.73259 21.03601 30.92094  1.000 63.62146  ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 23.89174 20.07835 31.15697  0.800 65.30877  ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.83088 19.99834 29.97103  0.700 66.88414  ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 24.40656 19.51672 28.89914  0.700 63.29255  ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 25.99235 20.43505 30.10303  0.700 71.36697  ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.28481 21.49366 31.89570  1.000 58.16391  ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 18.12019 22.26127 31.46434  1.000 52.37685  ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 18.00186 23.58635 32.20309  1.000 58.60284  ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.51700 24.57175 31.63278  1.000 54.21202  ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.84661 21.44077 31.65976  1.000 53.67449  ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.42658 23.63160 33.46829  1.000 57.27226  ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.31257 24.86420 34.24059  1.000 53.68889  ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.24921 25.93725 33.70542  1.000 57.30416  ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.82602 27.07020 33.44899  1.000 60.27187  ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.59349 24.58858 35.71735  1.000 59.97591  ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.42511 23.92428 36.41510  1.000 59.32736  ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 16.26980 24.30657 36.12719  1.000 57.35998  ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.66189 23.01825 37.24293  1.000 64.90545  ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.53031 25.60051 33.53280  1.000 55.73103  ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.46656 26.56535 32.96938  1.000 56.27902  ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 21.03316 26.99707 31.57614  1.000 58.42247  ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.31657 28.12390 31.15668  1.000 61.51365  ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.87850 25.97871 32.94335  1.000 55.07927  ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.33079 26.12336 30.85549  1.000 58.40773  ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.76274 26.50456 29.56955  1.000 51.31202  ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.68595 27.57085 29.74156  1.000 58.21272  ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.68622 28.58592 29.03648  1.000 59.99198  ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.19790 25.26772 28.87741  1.000 52.20004  ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.92934 25.38603 27.38376  1.000 51.24395  ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.23025 25.66879 26.64848  1.000 53.55790  ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.28214 24.11005 26.88161  1.000 51.42950  ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.76105 27.35293 30.68296  1.000 56.72603  ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.68176 28.30795 30.93189  1.000 56.56293  ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.25277 29.68229 31.26751  1.000 61.26474  ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.78668 30.70802 30.75742  1.000 57.87253  ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.76441 27.79661 32.05809  1.000 60.14334  ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.85375 28.91153 32.55896  1.000 58.48291  ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.94737 26.61453 31.57711  1.000 55.55735  ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.26878 29.71732 32.13946  1.000 65.36772  ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.89318 30.97321 32.54415  1.000 60.52295  ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.40635 31.74295 31.33826  1.000 64.67116  ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 18.94306 32.85323 31.04795  1.000 65.03323  ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 20.04682 30.71100 33.52100  1.000 58.93895  ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 19.63506 30.30202 34.91418  1.000 72.16313  ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 20.82498 30.38869 35.86846  1.000 73.02099  ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 21.37888 31.81377 35.93517  1.000 74.98226  ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 22.51215 31.95218 36.89985  1.000 77.24744  ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.37671 31.16024 30.62704  1.000 66.66078  ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 21.04060 31.86940 29.53906  1.000 65.57557  ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 20.05445 32.24911 28.44122  1.000 64.39892  ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.15431 33.33351 27.85468  1.000 73.37272  ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.17715 31.01555 28.98113  1.000 65.12984  ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.15734 30.42691 30.00406  1.000 64.75989  ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 24.05427 29.38274 29.34948  1.000 61.88187  ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 23.98755 31.51171 30.68871  1.000 54.31122  ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 19.08259 31.37691 28.16306  1.000 61.55460  ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.06765 31.69390 27.16475  1.000 65.40801  ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.23413 32.89536 27.57775  1.000 69.38119  ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 16.80342 33.67749 26.72225  1.000 74.59222  ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.16455 30.48432 26.93340  1.000 60.68392  ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 17.29784 29.80543 25.57476  1.000 63.35926  ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 16.42876 28.56713 25.53335  1.000 59.71634  ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 16.92824 30.77308 24.45590  1.000 68.02827  ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 16.99560 33.05576 28.87988  1.000 69.16551  ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 16.20212 34.18189 29.35511  1.000 73.79827  ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 16.97902 35.48720 29.24984  1.000 80.38918  ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.42845 36.51003 28.82528  1.000 82.62505  ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 15.75535 33.93146 30.79369  1.000 72.38198  ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 18.25710 35.47383 29.63867  1.000 78.03618  ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 19.09854 36.65042 29.44702  1.000 85.51518  ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 19.22177 37.00143 27.97068  1.000 90.64999  ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 19.21691 38.18200 27.59999  1.000 97.90437  ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.48260 36.41480 30.05424  1.000 91.18582  ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 21.55314 37.36441 29.52732  1.000 94.71373  ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 22.86926 37.20963 30.26850  1.000 92.02271  ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 23.86925 38.26483 29.82201  1.000 98.11105  ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 25.04819 38.34453 30.72923  1.000 99.57710  ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 19.31757 35.98960 27.11324  1.000 88.51458  ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.53688 36.21520 25.70030  1.000 92.95231  ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 21.00468 36.41117 25.38984  1.000 99.04078  ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 21.86401 35.74955 25.98294  1.000 93.46993  ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 21.30064 37.32212 24.46028  1.000 111.05568 ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 22.67383 37.64150 24.06333  1.000 115.01048 ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 23.43719 36.40072 23.60140  1.000 114.14433 ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 24.66308 36.32936 23.72778  1.000 110.62812 ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 23.42811 38.34796 25.19373  1.000 106.82854 ? 94  GLU A CB  1 
ATOM   741  N N   . TYR A 1 95  ? 22.71860 35.41491 23.06742  1.000 104.08310 ? 95  TYR A N   1 
ATOM   742  C CA  . TYR A 1 95  ? 23.34036 34.20817 22.55103  1.000 96.24826  ? 95  TYR A CA  1 
ATOM   743  C C   . TYR A 1 95  ? 23.78991 34.41819 21.10742  1.000 96.30571  ? 95  TYR A C   1 
ATOM   744  O O   . TYR A 1 95  ? 23.46883 35.42007 20.46176  1.000 97.21939  ? 95  TYR A O   1 
ATOM   745  C CB  . TYR A 1 95  ? 22.37567 33.02340 22.64224  1.000 90.19018  ? 95  TYR A CB  1 
ATOM   746  C CG  . TYR A 1 95  ? 20.97340 33.32292 22.14471  1.000 90.24997  ? 95  TYR A CG  1 
ATOM   747  C CD1 . TYR A 1 95  ? 20.69132 33.37441 20.78416  1.000 89.67020  ? 95  TYR A CD1 1 
ATOM   748  C CD2 . TYR A 1 95  ? 19.93031 33.54320 23.03691  1.000 91.11053  ? 95  TYR A CD2 1 
ATOM   749  C CE1 . TYR A 1 95  ? 19.41684 33.64654 20.32750  1.000 84.79952  ? 95  TYR A CE1 1 
ATOM   750  C CE2 . TYR A 1 95  ? 18.65048 33.81450 22.58843  1.000 89.91615  ? 95  TYR A CE2 1 
ATOM   751  C CZ  . TYR A 1 95  ? 18.40164 33.86487 21.23205  1.000 89.68290  ? 95  TYR A CZ  1 
ATOM   752  O OH  . TYR A 1 95  ? 17.13511 34.13648 20.77151  1.000 100.86238 ? 95  TYR A OH  1 
ATOM   753  N N   . GLN A 1 96  ? 24.54717 33.45337 20.60244  1.000 89.73502  ? 96  GLN A N   1 
ATOM   754  C CA  . GLN A 1 96  ? 24.94024 33.42867 19.20381  1.000 83.73891  ? 96  GLN A CA  1 
ATOM   755  C C   . GLN A 1 96  ? 24.02078 32.49792 18.42233  1.000 75.23456  ? 96  GLN A C   1 
ATOM   756  O O   . GLN A 1 96  ? 23.41563 31.57508 18.97322  1.000 73.27429  ? 96  GLN A O   1 
ATOM   757  C CB  . GLN A 1 96  ? 26.39830 32.98789 19.05165  1.000 84.71787  ? 96  GLN A CB  1 
ATOM   758  C CG  . GLN A 1 96  ? 27.41906 34.04613 19.44282  1.000 86.13378  ? 96  GLN A CG  1 
ATOM   759  C CD  . GLN A 1 96  ? 28.83492 33.65156 19.06118  1.000 94.64045  ? 96  GLN A CD  1 
ATOM   760  O OE1 . GLN A 1 96  ? 29.23445 32.49851 19.22243  1.000 94.02281  ? 96  GLN A OE1 1 
ATOM   761  N NE2 . GLN A 1 96  ? 29.59736 34.60685 18.53973  1.000 98.80920  ? 96  GLN A NE2 1 
ATOM   762  N N   . LYS A 1 97  ? 23.91150 32.76126 17.12390  1.000 69.66225  ? 97  LYS A N   1 
ATOM   763  C CA  . LYS A 1 97  ? 23.06784 31.97542 16.23636  1.000 62.77465  ? 97  LYS A CA  1 
ATOM   764  C C   . LYS A 1 97  ? 23.92578 31.28441 15.18618  1.000 60.10611  ? 97  LYS A C   1 
ATOM   765  O O   . LYS A 1 97  ? 24.87170 31.87340 14.65290  1.000 56.82864  ? 97  LYS A O   1 
ATOM   766  C CB  . LYS A 1 97  ? 22.00045 32.84502 15.56615  1.000 62.10281  ? 97  LYS A CB  1 
ATOM   767  C CG  . LYS A 1 97  ? 20.91261 33.31661 16.51761  1.000 64.33216  ? 97  LYS A CG  1 
ATOM   768  C CD  . LYS A 1 97  ? 19.72637 33.89305 15.76440  1.000 63.33213  ? 97  LYS A CD  1 
ATOM   769  C CE  . LYS A 1 97  ? 19.54285 35.37283 16.05841  1.000 68.49191  ? 97  LYS A CE  1 
ATOM   770  N NZ  . LYS A 1 97  ? 18.34225 35.92690 15.36619  1.000 69.67159  ? 97  LYS A NZ  1 
ATOM   771  N N   . VAL A 1 98  ? 23.58278 30.03124 14.89810  1.000 55.91062  ? 98  VAL A N   1 
ATOM   772  C CA  . VAL A 1 98  ? 24.36162 29.15872 14.02979  1.000 50.96467  ? 98  VAL A CA  1 
ATOM   773  C C   . VAL A 1 98  ? 23.42960 28.61012 12.95969  1.000 50.17662  ? 98  VAL A C   1 
ATOM   774  O O   . VAL A 1 98  ? 22.44563 27.93022 13.27807  1.000 47.58099  ? 98  VAL A O   1 
ATOM   775  C CB  . VAL A 1 98  ? 25.02035 28.01222 14.81410  1.000 47.47297  ? 98  VAL A CB  1 
ATOM   776  C CG1 . VAL A 1 98  ? 25.66772 27.02730 13.86165  1.000 53.79218  ? 98  VAL A CG1 1 
ATOM   777  C CG2 . VAL A 1 98  ? 26.04062 28.55872 15.78634  1.000 52.27990  ? 98  VAL A CG2 1 
ATOM   778  N N   . SER A 1 99  ? 23.74142 28.89297 11.69752  1.000 51.01741  ? 99  SER A N   1 
ATOM   779  C CA  . SER A 1 99  ? 22.88965 28.51621 10.57730  1.000 44.66558  ? 99  SER A CA  1 
ATOM   780  C C   . SER A 1 99  ? 23.44827 27.29910 9.85170   1.000 41.53246  ? 99  SER A C   1 
ATOM   781  O O   . SER A 1 99  ? 24.65273 27.20749 9.60077   1.000 46.81878  ? 99  SER A O   1 
ATOM   782  C CB  . SER A 1 99  ? 22.73505 29.67858 9.59450   1.000 45.96947  ? 99  SER A CB  1 
ATOM   783  O OG  . SER A 1 99  ? 21.98235 30.73631 10.16473  1.000 49.57697  ? 99  SER A OG  1 
ATOM   784  N N   . TYR A 1 100 ? 22.55623 26.36553 9.51593   1.000 44.20632  ? 100 TYR A N   1 
ATOM   785  C CA  . TYR A 1 100 ? 22.81771 25.18372 8.71047   1.000 40.12687  ? 100 TYR A CA  1 
ATOM   786  C C   . TYR A 1 100 ? 22.04556 25.25849 7.39721   1.000 40.46246  ? 100 TYR A C   1 
ATOM   787  O O   . TYR A 1 100 ? 20.89496 25.70713 7.38611   1.000 40.92871  ? 100 TYR A O   1 
ATOM   788  C CB  . TYR A 1 100 ? 22.41277 23.90329 9.45389   1.000 37.00006  ? 100 TYR A CB  1 
ATOM   789  C CG  . TYR A 1 100 ? 23.37284 23.47130 10.53343  1.000 37.69567  ? 100 TYR A CG  1 
ATOM   790  C CD1 . TYR A 1 100 ? 24.48140 24.24156 10.85796  1.000 40.41594  ? 100 TYR A CD1 1 
ATOM   791  C CD2 . TYR A 1 100 ? 23.17903 22.27991 11.21739  1.000 37.21215  ? 100 TYR A CD2 1 
ATOM   792  C CE1 . TYR A 1 100 ? 25.36361 23.84088 11.84939  1.000 42.28177  ? 100 TYR A CE1 1 
ATOM   793  C CE2 . TYR A 1 100 ? 24.05284 21.87030 12.20338  1.000 42.96495  ? 100 TYR A CE2 1 
ATOM   794  C CZ  . TYR A 1 100 ? 25.14294 22.65150 12.51528  1.000 42.42705  ? 100 TYR A CZ  1 
ATOM   795  O OH  . TYR A 1 100 ? 26.01057 22.23485 13.49706  1.000 47.98382  ? 100 TYR A OH  1 
ATOM   796  N N   . PRO A 1 101 ? 22.63819 24.82886 6.28384   1.000 39.53153  ? 101 PRO A N   1 
ATOM   797  C CA  . PRO A 1 101 ? 21.91278 24.85493 5.01230   1.000 39.49939  ? 101 PRO A CA  1 
ATOM   798  C C   . PRO A 1 101 ? 20.76476 23.86594 5.02119   1.000 37.30408  ? 101 PRO A C   1 
ATOM   799  O O   . PRO A 1 101 ? 20.79822 22.84679 5.71335   1.000 37.66998  ? 101 PRO A O   1 
ATOM   800  C CB  . PRO A 1 101 ? 22.97697 24.45299 3.98071   1.000 36.02659  ? 101 PRO A CB  1 
ATOM   801  C CG  . PRO A 1 101 ? 24.29171 24.57908 4.68595   1.000 34.23110  ? 101 PRO A CG  1 
ATOM   802  C CD  . PRO A 1 101 ? 23.99541 24.29080 6.11941   1.000 38.93127  ? 101 PRO A CD  1 
ATOM   803  N N   . LEU A 1 102 ? 19.74214 24.17757 4.23281   1.000 37.95728  ? 102 LEU A N   1 
ATOM   804  C CA  . LEU A 1 102 ? 18.58470 23.31306 4.06069   1.000 36.86227  ? 102 LEU A CA  1 
ATOM   805  C C   . LEU A 1 102 ? 18.48967 22.89665 2.59849   1.000 39.25111  ? 102 LEU A C   1 
ATOM   806  O O   . LEU A 1 102 ? 19.19063 23.42724 1.73271   1.000 33.89893  ? 102 LEU A O   1 
ATOM   807  C CB  . LEU A 1 102 ? 17.29562 24.01241 4.51329   1.000 33.78397  ? 102 LEU A CB  1 
ATOM   808  C CG  . LEU A 1 102 ? 17.33302 24.66695 5.89836   1.000 38.38259  ? 102 LEU A CG  1 
ATOM   809  C CD1 . LEU A 1 102 ? 16.09128 25.49822 6.12743   1.000 37.77854  ? 102 LEU A CD1 1 
ATOM   810  C CD2 . LEU A 1 102 ? 17.48134 23.62456 6.98655   1.000 33.52835  ? 102 LEU A CD2 1 
ATOM   811  N N   . LEU A 1 103 ? 17.60963 21.93455 2.32935   1.000 34.59881  ? 103 LEU A N   1 
ATOM   812  C CA  . LEU A 1 103 ? 17.44519 21.36412 0.99920   1.000 39.67811  ? 103 LEU A CA  1 
ATOM   813  C C   . LEU A 1 103 ? 16.02373 21.59079 0.50699   1.000 38.35051  ? 103 LEU A C   1 
ATOM   814  O O   . LEU A 1 103 ? 15.06037 21.28361 1.21669   1.000 35.55208  ? 103 LEU A O   1 
ATOM   815  C CB  . LEU A 1 103 ? 17.76182 19.86944 1.00191   1.000 34.33745  ? 103 LEU A CB  1 
ATOM   816  C CG  . LEU A 1 103 ? 17.42612 19.13028 -0.28745  1.000 32.47779  ? 103 LEU A CG  1 
ATOM   817  C CD1 . LEU A 1 103 ? 18.37006 19.53307 -1.41092  1.000 33.89236  ? 103 LEU A CD1 1 
ATOM   818  C CD2 . LEU A 1 103 ? 17.47592 17.64133 -0.04152  1.000 31.42894  ? 103 LEU A CD2 1 
ATOM   819  N N   . LYS A 1 104 ? 15.89511 22.11430 -0.70873  1.000 36.74063  ? 104 LYS A N   1 
ATOM   820  C CA  . LYS A 1 104 ? 14.59413 22.33063 -1.32653  1.000 38.87122  ? 104 LYS A CA  1 
ATOM   821  C C   . LYS A 1 104 ? 14.32068 21.24676 -2.36033  1.000 36.64037  ? 104 LYS A C   1 
ATOM   822  O O   . LYS A 1 104 ? 15.17263 20.95356 -3.20543  1.000 36.95831  ? 104 LYS A O   1 
ATOM   823  C CB  . LYS A 1 104 ? 14.50549 23.70970 -1.97903  1.000 38.81536  ? 104 LYS A CB  1 
ATOM   824  C CG  . LYS A 1 104 ? 13.28904 23.85612 -2.88611  1.000 48.10072  ? 104 LYS A CG  1 
ATOM   825  C CD  . LYS A 1 104 ? 12.65995 25.23584 -2.80131  0.900 45.46512  ? 104 LYS A CD  1 
ATOM   826  C CE  . LYS A 1 104 ? 13.11992 26.12651 -3.93537  0.800 45.08943  ? 104 LYS A CE  1 
ATOM   827  N NZ  . LYS A 1 104 ? 11.96250 26.62657 -4.72123  0.700 50.05475  ? 104 LYS A NZ  1 
ATOM   828  N N   . THR A 1 105 ? 13.13419 20.65230 -2.27974  1.000 39.71185  ? 105 THR A N   1 
ATOM   829  C CA  . THR A 1 105 ? 12.65632 19.67346 -3.24503  1.000 42.10558  ? 105 THR A CA  1 
ATOM   830  C C   . THR A 1 105 ? 11.39996 20.21587 -3.90523  1.000 42.39714  ? 105 THR A C   1 
ATOM   831  O O   . THR A 1 105 ? 10.48769 20.67410 -3.21347  1.000 45.49212  ? 105 THR A O   1 
ATOM   832  C CB  . THR A 1 105 ? 12.34942 18.33691 -2.57343  1.000 39.84994  ? 105 THR A CB  1 
ATOM   833  O OG1 . THR A 1 105 ? 13.51151 17.87347 -1.87749  1.000 38.52414  ? 105 THR A OG1 1 
ATOM   834  C CG2 . THR A 1 105 ? 11.92435 17.30564 -3.61281  1.000 39.93447  ? 105 THR A CG2 1 
ATOM   835  N N   . THR A 1 106 ? 11.35215 20.16597 -5.23397  1.000 44.33452  ? 106 THR A N   1 
ATOM   836  C CA  . THR A 1 106 ? 10.19325 20.61829 -5.99312  1.000 49.06227  ? 106 THR A CA  1 
ATOM   837  C C   . THR A 1 106 ? 9.66341  19.46969 -6.83717  1.000 44.28537  ? 106 THR A C   1 
ATOM   838  O O   . THR A 1 106 ? 10.42427 18.83122 -7.56921  1.000 41.44051  ? 106 THR A O   1 
ATOM   839  C CB  . THR A 1 106 ? 10.53984 21.81171 -6.88302  1.000 46.24136  ? 106 THR A CB  1 
ATOM   840  O OG1 . THR A 1 106 ? 11.11617 22.84992 -6.08154  1.000 44.88771  ? 106 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 106 ? 9.28755  22.34244 -7.56174  1.000 46.72326  ? 106 THR A CG2 1 
ATOM   842  N N   . VAL A 1 107 ? 8.36562  19.20325 -6.72349  1.000 47.56518  ? 107 VAL A N   1 
ATOM   843  C CA  . VAL A 1 107 ? 7.71164  18.12232 -7.45091  1.000 50.12385  ? 107 VAL A CA  1 
ATOM   844  C C   . VAL A 1 107 ? 6.68919  18.74003 -8.39360  1.000 56.67891  ? 107 VAL A C   1 
ATOM   845  O O   . VAL A 1 107 ? 5.75420  19.41815 -7.94981  1.000 59.49060  ? 107 VAL A O   1 
ATOM   846  C CB  . VAL A 1 107 ? 7.03931  17.11866 -6.50331  1.000 51.21253  ? 107 VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 107 ? 6.68504  15.84242 -7.25919  1.000 46.77288  ? 107 VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 107 ? 7.93348  16.82361 -5.30743  1.000 49.16564  ? 107 VAL A CG2 1 
ATOM   849  N N   . LYS A 1 108 ? 6.86228  18.50551 -9.68762  1.000 53.35831  ? 108 LYS A N   1 
ATOM   850  C CA  . LYS A 1 108 ? 5.92191  18.96887 -10.69204 1.000 58.35233  ? 108 LYS A CA  1 
ATOM   851  C C   . LYS A 1 108 ? 5.00832  17.82049 -11.10546 1.000 63.63993  ? 108 LYS A C   1 
ATOM   852  O O   . LYS A 1 108 ? 5.39141  16.64866 -11.04440 1.000 61.61590  ? 108 LYS A O   1 
ATOM   853  C CB  . LYS A 1 108 ? 6.66213  19.53131 -11.90706 1.000 50.79597  ? 108 LYS A CB  1 
ATOM   854  N N   . TYR A 1 109 ? 3.79078  18.16527 -11.51344 1.000 69.64647  ? 109 TYR A N   1 
ATOM   855  C CA  . TYR A 1 109 ? 2.80431  17.17209 -11.92720 1.000 64.21297  ? 109 TYR A CA  1 
ATOM   856  C C   . TYR A 1 109 ? 2.29332  17.50090 -13.32751 1.000 75.42587  ? 109 TYR A C   1 
ATOM   857  O O   . TYR A 1 109 ? 2.94930  18.18870 -14.11956 1.000 75.21198  ? 109 TYR A O   1 
ATOM   858  C CB  . TYR A 1 109 ? 1.62768  17.10178 -10.95095 1.000 68.19446  ? 109 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 109 ? 1.98914  16.89245 -9.49958  1.000 72.29686  ? 109 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 109 ? 2.17156  17.97563 -8.65040  1.000 69.04966  ? 109 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 109 ? 2.11263  15.61557 -8.97079  1.000 64.50186  ? 109 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 109 ? 2.48328  17.79601 -7.32177  1.000 67.97437  ? 109 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 109 ? 2.42366  15.42389 -7.64093  1.000 70.96365  ? 109 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 109 ? 2.60911  16.51681 -6.81992  1.000 73.17227  ? 109 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 109 ? 2.92077  16.32258 -5.49242  1.000 72.06911  ? 109 TYR A OH  1 
ATOM   866  N N   . GLY A 1 110 ? 1.09653  17.00621 -13.63595 1.000 82.65626  ? 110 GLY A N   1 
ATOM   867  C CA  . GLY A 1 110 ? 0.42585  17.28898 -14.88992 1.000 75.25772  ? 110 GLY A CA  1 
ATOM   868  C C   . GLY A 1 110 ? -1.08157 17.13781 -14.78243 1.000 76.00349  ? 110 GLY A C   1 
ATOM   869  O O   . GLY A 1 110 ? -1.83680 18.05323 -15.11604 1.000 75.49235  ? 110 GLY A O   1 
ATOM   870  N N   . LYS A 1 114 ? 0.88018  21.33467 -11.96417 1.000 79.58450  ? 114 LYS A N   1 
ATOM   871  C CA  . LYS A 1 114 ? 0.89311  21.74170 -10.56333 1.000 79.23056  ? 114 LYS A CA  1 
ATOM   872  C C   . LYS A 1 114 ? 2.29114  21.52786 -9.97717  1.000 84.31540  ? 114 LYS A C   1 
ATOM   873  O O   . LYS A 1 114 ? 3.12407  20.85872 -10.59001 1.000 84.58091  ? 114 LYS A O   1 
ATOM   874  C CB  . LYS A 1 114 ? -0.16407 20.96589 -9.77186  1.000 75.65117  ? 114 LYS A CB  1 
ATOM   875  C CG  . LYS A 1 114 ? -0.60106 21.63791 -8.47518  1.000 85.53954  ? 114 LYS A CG  1 
ATOM   876  C CD  . LYS A 1 114 ? -0.90363 23.11261 -8.69514  1.000 85.21899  ? 114 LYS A CD  1 
ATOM   877  C CE  . LYS A 1 114 ? 0.02253  23.99313 -7.86641  1.000 83.59385  ? 114 LYS A CE  1 
ATOM   878  N NZ  . LYS A 1 114 ? 0.30951  25.29017 -8.54232  1.000 83.81951  ? 114 LYS A NZ  1 
ATOM   879  N N   . GLU A 1 115 ? 2.55687  22.09891 -8.80242  1.000 72.14900  ? 115 GLU A N   1 
ATOM   880  C CA  . GLU A 1 115 ? 3.88703  22.02877 -8.21425  1.000 66.97546  ? 115 GLU A CA  1 
ATOM   881  C C   . GLU A 1 115 ? 3.78972  22.04969 -6.69577  1.000 67.00377  ? 115 GLU A C   1 
ATOM   882  O O   . GLU A 1 115 ? 2.99640  22.80322 -6.12684  1.000 68.19346  ? 115 GLU A O   1 
ATOM   883  C CB  . GLU A 1 115 ? 4.76625  23.18932 -8.69191  1.000 63.58070  ? 115 GLU A CB  1 
ATOM   884  C CG  . GLU A 1 115 ? 6.10386  22.76444 -9.26342  1.000 66.84678  ? 115 GLU A CG  1 
ATOM   885  C CD  . GLU A 1 115 ? 6.96354  23.94655 -9.67731  1.000 70.79315  ? 115 GLU A CD  1 
ATOM   886  O OE1 . GLU A 1 115 ? 7.17565  24.84775 -8.83626  1.000 66.67710  ? 115 GLU A OE1 1 
ATOM   887  O OE2 . GLU A 1 115 ? 7.41938  23.97683 -10.84424 1.000 67.85392  ? 115 GLU A OE2 1 
ATOM   888  N N   . ALA A 1 116 ? 4.61238  21.22893 -6.04648  1.000 62.49577  ? 116 ALA A N   1 
ATOM   889  C CA  . ALA A 1 116 ? 4.71177  21.20499 -4.59456  1.000 56.59657  ? 116 ALA A CA  1 
ATOM   890  C C   . ALA A 1 116 ? 6.17747  21.21705 -4.18837  1.000 52.68073  ? 116 ALA A C   1 
ATOM   891  O O   . ALA A 1 116 ? 6.99799  20.50278 -4.77377  1.000 53.40519  ? 116 ALA A O   1 
ATOM   892  C CB  . ALA A 1 116 ? 4.01099  19.97688 -4.00356  1.000 60.10988  ? 116 ALA A CB  1 
ATOM   893  N N   . THR A 1 117 ? 6.50239  22.03160 -3.18831  1.000 52.27152  ? 117 THR A N   1 
ATOM   894  C CA  . THR A 1 117 ? 7.86306  22.15299 -2.68828  1.000 53.36931  ? 117 THR A CA  1 
ATOM   895  C C   . THR A 1 117 ? 7.92738  21.76076 -1.21534  1.000 52.58004  ? 117 THR A C   1 
ATOM   896  O O   . THR A 1 117 ? 6.94167  21.87415 -0.47772  1.000 47.59923  ? 117 THR A O   1 
ATOM   897  C CB  . THR A 1 117 ? 8.40602  23.57971 -2.87451  1.000 50.66738  ? 117 THR A CB  1 
ATOM   898  O OG1 . THR A 1 117 ? 7.68650  24.48506 -2.03195  1.000 57.69246  ? 117 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 117 ? 8.25122  24.01910 -4.32167  1.000 48.91644  ? 117 THR A CG2 1 
ATOM   900  N N   . TYR A 1 118 ? 9.10482  21.28985 -0.79879  1.000 51.57288  ? 118 TYR A N   1 
ATOM   901  C CA  . TYR A 1 118 ? 9.34456  20.83109 0.56213   1.000 42.16648  ? 118 TYR A CA  1 
ATOM   902  C C   . TYR A 1 118 ? 10.74871 21.23027 0.98961   1.000 40.88654  ? 118 TYR A C   1 
ATOM   903  O O   . TYR A 1 118 ? 11.66708 21.30113 0.17042   1.000 43.61668  ? 118 TYR A O   1 
ATOM   904  C CB  . TYR A 1 118 ? 9.19369  19.30663 0.69484   1.000 42.40605  ? 118 TYR A CB  1 
ATOM   905  C CG  . TYR A 1 118 ? 7.91281  18.75790 0.11828   1.000 47.30593  ? 118 TYR A CG  1 
ATOM   906  C CD1 . TYR A 1 118 ? 7.82672  18.40884 -1.22506  1.000 51.96001  ? 118 TYR A CD1 1 
ATOM   907  C CD2 . TYR A 1 118 ? 6.79036  18.58506 0.91330   1.000 48.94505  ? 118 TYR A CD2 1 
ATOM   908  C CE1 . TYR A 1 118 ? 6.65662  17.90693 -1.76032  1.000 52.93775  ? 118 TYR A CE1 1 
ATOM   909  C CE2 . TYR A 1 118 ? 5.61882  18.08450 0.38986   1.000 53.13502  ? 118 TYR A CE2 1 
ATOM   910  C CZ  . TYR A 1 118 ? 5.55479  17.74621 -0.94655  1.000 55.18278  ? 118 TYR A CZ  1 
ATOM   911  O OH  . TYR A 1 118 ? 4.38035  17.24789 -1.46236  1.000 52.06119  ? 118 TYR A OH  1 
ATOM   912  N N   . LEU A 1 119 ? 10.90833 21.47701 2.28584   1.000 39.49925  ? 119 LEU A N   1 
ATOM   913  C CA  . LEU A 1 119 ? 12.19050 21.83014 2.88077   1.000 37.15915  ? 119 LEU A CA  1 
ATOM   914  C C   . LEU A 1 119 ? 12.65511 20.67131 3.74988   1.000 36.35969  ? 119 LEU A C   1 
ATOM   915  O O   . LEU A 1 119 ? 11.87547 20.13655 4.54458   1.000 38.48783  ? 119 LEU A O   1 
ATOM   916  C CB  . LEU A 1 119 ? 12.06997 23.10870 3.71197   1.000 40.49751  ? 119 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 119 ? 13.13175 24.19340 3.54680   1.000 42.03813  ? 119 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 119 ? 13.27336 24.57505 2.08866   1.000 39.07978  ? 119 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 119 ? 12.76618 25.41317 4.38152   1.000 41.77108  ? 119 LEU A CD2 1 
ATOM   920  N N   . ALA A 1 120 ? 13.91097 20.27665 3.59399   1.000 33.36263  ? 120 ALA A N   1 
ATOM   921  C CA  . ALA A 1 120 ? 14.45478 19.14011 4.31707   1.000 34.68347  ? 120 ALA A CA  1 
ATOM   922  C C   . ALA A 1 120 ? 15.59591 19.59478 5.21415   1.000 36.80803  ? 120 ALA A C   1 
ATOM   923  O O   . ALA A 1 120 ? 16.41713 20.42949 4.81793   1.000 35.66337  ? 120 ALA A O   1 
ATOM   924  C CB  . ALA A 1 120 ? 14.94126 18.05258 3.35490   1.000 31.23093  ? 120 ALA A CB  1 
ATOM   925  N N   . LEU A 1 121 ? 15.62808 19.05641 6.43257   1.000 33.66982  ? 121 LEU A N   1 
ATOM   926  C CA  . LEU A 1 121 ? 16.75253 19.24714 7.33950   1.000 34.13973  ? 121 LEU A CA  1 
ATOM   927  C C   . LEU A 1 121 ? 17.74117 18.09514 7.26763   1.000 35.90859  ? 121 LEU A C   1 
ATOM   928  O O   . LEU A 1 121 ? 18.95441 18.31191 7.36011   1.000 33.63325  ? 121 LEU A O   1 
ATOM   929  C CB  . LEU A 1 121 ? 16.26011 19.41283 8.78041   1.000 30.86976  ? 121 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 121 ? 17.34594 19.55154 9.85044   1.000 34.01231  ? 121 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 121 ? 18.18224 20.77774 9.57480   1.000 33.84940  ? 121 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 121 ? 16.74908 19.61066 11.25652  1.000 36.06450  ? 121 LEU A CD2 1 
ATOM   933  N N   . ASN A 1 122 ? 17.24326 16.87356 7.09324   1.000 33.29644  ? 122 ASN A N   1 
ATOM   934  C CA  . ASN A 1 122 ? 18.11157 15.72610 6.90077   1.000 30.78828  ? 122 ASN A CA  1 
ATOM   935  C C   . ASN A 1 122 ? 18.28259 15.43926 5.41412   1.000 35.18949  ? 122 ASN A C   1 
ATOM   936  O O   . ASN A 1 122 ? 19.33875 15.72659 4.84094   1.000 33.36171  ? 122 ASN A O   1 
ATOM   937  C CB  . ASN A 1 122 ? 17.55490 14.50346 7.62686   1.000 32.81553  ? 122 ASN A CB  1 
ATOM   938  C CG  . ASN A 1 122 ? 18.18942 14.28970 8.99308   1.000 35.55660  ? 122 ASN A CG  1 
ATOM   939  O OD1 . ASN A 1 122 ? 18.89014 15.15813 9.52218   1.000 31.96971  ? 122 ASN A OD1 1 
ATOM   940  N ND2 . ASN A 1 122 ? 17.94331 13.12136 9.57081   1.000 34.74332  ? 122 ASN A ND2 1 
ATOM   941  N N   . GLU A 1 123 ? 17.25372 14.89068 4.77295   1.000 33.83574  ? 123 GLU A N   1 
ATOM   942  C CA  . GLU A 1 123 ? 17.39483 14.46019 3.38978   1.000 32.20415  ? 123 GLU A CA  1 
ATOM   943  C C   . GLU A 1 123 ? 16.02220 14.31721 2.75143   1.000 34.10865  ? 123 GLU A C   1 
ATOM   944  O O   . GLU A 1 123 ? 14.98962 14.31682 3.42612   1.000 34.72171  ? 123 GLU A O   1 
ATOM   945  C CB  . GLU A 1 123 ? 18.15846 13.13625 3.29203   1.000 30.07579  ? 123 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 123 ? 17.38748 11.93568 3.82520   1.000 33.20259  ? 123 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 123 ? 17.26459 11.93328 5.34416   1.000 37.75300  ? 123 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 123 ? 18.30623 11.83754 6.03167   1.000 32.92557  ? 123 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 123 ? 16.12666 12.03429 5.84943   1.000 35.99420  ? 123 GLU A OE2 1 
ATOM   950  N N   . SER A 1 124 ? 16.03539 14.19289 1.42640   1.000 36.55852  ? 124 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 14.87035 13.82607 0.63233   1.000 32.28099  ? 124 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 15.22761 12.59285 -0.18081  1.000 28.96833  ? 124 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 16.28087 12.56102 -0.82287  1.000 30.95122  ? 124 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 14.44358 14.96813 -0.28811  1.000 32.45832  ? 124 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 13.41220 14.55129 -1.16353  1.000 40.82494  ? 124 SER A OG  1 
ATOM   956  N N   . THR A 1 125 ? 14.37624 11.57145 -0.13664  1.000 31.22212  ? 125 THR A N   1 
ATOM   957  C CA  . THR A 1 125 ? 14.63483 10.34435 -0.87543  1.000 35.53933  ? 125 THR A CA  1 
ATOM   958  C C   . THR A 1 125 ? 13.49901 10.06256 -1.85463  1.000 33.03332  ? 125 THR A C   1 
ATOM   959  O O   . THR A 1 125 ? 12.38642 10.57786 -1.71881  1.000 32.03591  ? 125 THR A O   1 
ATOM   960  C CB  . THR A 1 125 ? 14.82557 9.13474  0.06083   1.000 31.07468  ? 125 THR A CB  1 
ATOM   961  O OG1 . THR A 1 125 ? 13.54893 8.60254  0.42227   1.000 35.24184  ? 125 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 125 ? 15.58114 9.53344  1.31751   1.000 33.45869  ? 125 THR A CG2 1 
ATOM   963  N N   . VAL A 1 126 ? 13.80447 9.24013  -2.85961  1.000 35.13240  ? 126 VAL A N   1 
ATOM   964  C CA  . VAL A 1 126 ? 12.85387 8.83365  -3.88949  1.000 35.47289  ? 126 VAL A CA  1 
ATOM   965  C C   . VAL A 1 126 ? 12.92814 7.32266  -4.04030  1.000 33.20336  ? 126 VAL A C   1 
ATOM   966  O O   . VAL A 1 126 ? 14.02176 6.76059  -4.13720  1.000 35.92350  ? 126 VAL A O   1 
ATOM   967  C CB  . VAL A 1 126 ? 13.13617 9.51118  -5.24537  1.000 34.56402  ? 126 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 126 ? 11.99045 9.24933  -6.22131  1.000 36.62857  ? 126 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 126 ? 13.34795 10.99978 -5.07989  1.000 33.30070  ? 126 VAL A CG2 1 
ATOM   970  N N   . LYS A 1 127 ? 11.77072 6.66806  -4.04469  1.000 36.03622  ? 127 LYS A N   1 
ATOM   971  C CA  . LYS A 1 127 ? 11.66322 5.24512  -4.33935  1.000 39.65695  ? 127 LYS A CA  1 
ATOM   972  C C   . LYS A 1 127 ? 10.44778 5.04478  -5.23005  1.000 45.07219  ? 127 LYS A C   1 
ATOM   973  O O   . LYS A 1 127 ? 9.62420  5.94582  -5.40098  1.000 47.52140  ? 127 LYS A O   1 
ATOM   974  C CB  . LYS A 1 127 ? 11.53531 4.39318  -3.06820  1.000 42.29355  ? 127 LYS A CB  1 
ATOM   975  C CG  . LYS A 1 127 ? 12.74001 4.43108  -2.14107  1.000 42.58136  ? 127 LYS A CG  1 
ATOM   976  C CD  . LYS A 1 127 ? 12.55296 3.46839  -0.97757  1.000 42.69083  ? 127 LYS A CD  1 
ATOM   977  C CE  . LYS A 1 127 ? 13.67970 3.59062  0.03905   1.000 51.96483  ? 127 LYS A CE  1 
ATOM   978  N NZ  . LYS A 1 127 ? 13.50292 2.65268  1.18624   1.000 44.06076  ? 127 LYS A NZ  1 
ATOM   979  N N   . SER A 1 128 ? 10.32636 3.85204  -5.79586  1.000 48.19829  ? 128 SER A N   1 
ATOM   980  C CA  . SER A 1 128 ? 9.19274  3.58272  -6.66854  1.000 53.93987  ? 128 SER A CA  1 
ATOM   981  C C   . SER A 1 128 ? 7.96825  3.16335  -5.85497  1.000 60.12642  ? 128 SER A C   1 
ATOM   982  O O   . SER A 1 128 ? 8.07479  2.69121  -4.72037  1.000 56.37955  ? 128 SER A O   1 
ATOM   983  C CB  . SER A 1 128 ? 9.52943  2.49994  -7.68892  1.000 55.16041  ? 128 SER A CB  1 
ATOM   984  O OG  . SER A 1 128 ? 9.27994  1.20656  -7.16090  1.000 60.42787  ? 128 SER A OG  1 
ATOM   985  N N   . SER A 1 129 ? 6.79106  3.33991  -6.46544  1.000 63.12508  ? 129 SER A N   1 
ATOM   986  C CA  . SER A 1 129 ? 5.53622  2.96654  -5.82419  1.000 60.60496  ? 129 SER A CA  1 
ATOM   987  C C   . SER A 1 129 ? 5.44667  1.46708  -5.57636  1.000 67.98150  ? 129 SER A C   1 
ATOM   988  O O   . SER A 1 129 ? 4.75160  1.03843  -4.64882  1.000 74.03358  ? 129 SER A O   1 
ATOM   989  C CB  . SER A 1 129 ? 4.35756  3.41672  -6.68280  1.000 66.66885  ? 129 SER A CB  1 
ATOM   990  O OG  . SER A 1 129 ? 4.30577  2.68634  -7.90005  1.000 66.53037  ? 129 SER A OG  1 
ATOM   991  N N   . GLY A 1 130 ? 6.12550  0.66127  -6.38993  1.000 72.44316  ? 130 GLY A N   1 
ATOM   992  C CA  . GLY A 1 130 ? 6.08081  -0.78249 -6.26437  1.000 77.51638  ? 130 GLY A CA  1 
ATOM   993  C C   . GLY A 1 130 ? 6.86527  -1.47864 -7.35485  1.000 81.91451  ? 130 GLY A C   1 
ATOM   994  O O   . GLY A 1 130 ? 7.55498  -2.47338 -7.10803  1.000 88.16142  ? 130 GLY A O   1 
ATOM   995  N N   . GLY A 1 131 ? 6.76610  -0.95584 -8.57371  1.000 70.89820  ? 131 GLY A N   1 
ATOM   996  C CA  . GLY A 1 131 ? 7.52665  -1.46876 -9.69108  1.000 72.28285  ? 131 GLY A CA  1 
ATOM   997  C C   . GLY A 1 131 ? 8.99228  -1.09109 -9.61078  1.000 65.33188  ? 131 GLY A C   1 
ATOM   998  O O   . GLY A 1 131 ? 9.45498  -0.50978 -8.62880  1.000 62.10601  ? 131 GLY A O   1 
ATOM   999  N N   . PRO A 1 132 ? 9.75128  -1.42943 -10.64532 1.000 62.38613  ? 132 PRO A N   1 
ATOM   1000 C CA  . PRO A 1 132 ? 11.15766 -1.02516 -10.68022 1.000 55.93148  ? 132 PRO A CA  1 
ATOM   1001 C C   . PRO A 1 132 ? 11.30199 0.49068  -10.68991 1.000 51.14782  ? 132 PRO A C   1 
ATOM   1002 O O   . PRO A 1 132 ? 10.42768 1.21832  -11.16604 1.000 54.57205  ? 132 PRO A O   1 
ATOM   1003 C CB  . PRO A 1 132 ? 11.67610 -1.64603 -11.98791 1.000 53.78954  ? 132 PRO A CB  1 
ATOM   1004 C CG  . PRO A 1 132 ? 10.46068 -1.90315 -12.81075 1.000 55.87008  ? 132 PRO A CG  1 
ATOM   1005 C CD  . PRO A 1 132 ? 9.37940  -2.23402 -11.82297 1.000 59.29985  ? 132 PRO A CD  1 
ATOM   1006 N N   . PHE A 1 133 ? 12.43270 0.96218  -10.17208 1.000 45.73339  ? 133 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 133 ? 12.71314 2.39184  -10.06135 1.000 44.19032  ? 133 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 133 ? 13.73856 2.75575  -11.12830 1.000 38.11282  ? 133 PHE A C   1 
ATOM   1009 O O   . PHE A 1 133 ? 14.92116 2.42701  -11.00464 1.000 33.93926  ? 133 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 133 ? 13.20959 2.73970  -8.65990  1.000 44.52128  ? 133 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 133 ? 13.52744 4.19663  -8.46607  1.000 39.16997  ? 133 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 133 ? 12.51308 5.13890  -8.38377  1.000 43.75454  ? 133 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 133 ? 14.83842 4.62127  -8.34775  1.000 36.56623  ? 133 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 133 ? 12.80717 6.47702  -8.19756  1.000 39.44946  ? 133 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 133 ? 15.13756 5.95527  -8.16226  1.000 35.09799  ? 133 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 133 ? 14.12235 6.88422  -8.08679  1.000 33.90171  ? 133 PHE A CZ  1 
ATOM   1017 N N   . VAL A 1 134 ? 13.27743 3.41424  -12.18908 1.000 41.02224  ? 134 VAL A N   1 
ATOM   1018 C CA  . VAL A 1 134 ? 14.14074 3.93375  -13.24389 1.000 39.23787  ? 134 VAL A CA  1 
ATOM   1019 C C   . VAL A 1 134 ? 13.86960 5.42057  -13.37343 1.000 40.08142  ? 134 VAL A C   1 
ATOM   1020 O O   . VAL A 1 134 ? 12.71121 5.83727  -13.48509 1.000 47.38671  ? 134 VAL A O   1 
ATOM   1021 C CB  . VAL A 1 134 ? 13.91387 3.22661  -14.59286 1.000 35.65799  ? 134 VAL A CB  1 
ATOM   1022 C CG1 . VAL A 1 134 ? 14.95204 3.69056  -15.59623 1.000 37.13974  ? 134 VAL A CG1 1 
ATOM   1023 C CG2 . VAL A 1 134 ? 13.97791 1.72337  -14.43037 1.000 42.37382  ? 134 VAL A CG2 1 
ATOM   1024 N N   . VAL A 1 135 ? 14.93180 6.21468  -13.36103 1.000 37.57413  ? 135 VAL A N   1 
ATOM   1025 C CA  . VAL A 1 135 ? 14.80231 7.66291  -13.43726 1.000 39.53441  ? 135 VAL A CA  1 
ATOM   1026 C C   . VAL A 1 135 ? 16.03403 8.20531  -14.14999 1.000 37.06978  ? 135 VAL A C   1 
ATOM   1027 O O   . VAL A 1 135 ? 17.13578 7.66994  -14.00106 1.000 36.71365  ? 135 VAL A O   1 
ATOM   1028 C CB  . VAL A 1 135 ? 14.61310 8.27268  -12.02581 1.000 33.19401  ? 135 VAL A CB  1 
ATOM   1029 C CG1 . VAL A 1 135 ? 15.92889 8.32168  -11.25972 1.000 32.06318  ? 135 VAL A CG1 1 
ATOM   1030 C CG2 . VAL A 1 135 ? 13.98447 9.64313  -12.10798 1.000 38.32801  ? 135 VAL A CG2 1 
ATOM   1031 N N   . ASP A 1 136 ? 15.84235 9.24397  -14.95968 1.000 36.49214  ? 136 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 136 ? 16.96012 9.93369  -15.58907 1.000 36.21944  ? 136 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 136 ? 17.43449 11.06221 -14.68550 1.000 36.86153  ? 136 ASP A C   1 
ATOM   1034 O O   . ASP A 1 136 ? 16.62674 11.86908 -14.21334 1.000 37.81296  ? 136 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 136 ? 16.56977 10.48269 -16.96034 1.000 36.52875  ? 136 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 136 ? 16.56391 9.41432  -18.02474 1.000 37.88098  ? 136 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 136 ? 17.41650 8.50905  -17.94136 1.000 37.77409  ? 136 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 136 ? 15.70413 9.46783  -18.93133 1.000 39.69778  ? 136 ASP A OD2 1 
ATOM   1039 N N   . VAL A 1 137 ? 18.74152 11.11981 -14.45106 1.000 32.41171  ? 137 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 137 ? 19.33712 12.12760 -13.58152 1.000 38.29147  ? 137 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 137 ? 19.96820 13.20545 -14.44885 1.000 34.18857  ? 137 VAL A C   1 
ATOM   1042 O O   . VAL A 1 137 ? 20.90139 12.93278 -15.21204 1.000 39.24696  ? 137 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 137 ? 20.36915 11.50908 -12.62822 1.000 36.51531  ? 137 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 137 ? 20.93878 12.57945 -11.71160 1.000 35.14868  ? 137 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 137 ? 19.72662 10.39710 -11.81963 1.000 31.63134  ? 137 VAL A CG2 1 
ATOM   1046 N N   . VAL A 1 138 ? 19.46561 14.42979 -14.32287 1.000 34.64463  ? 138 VAL A N   1 
ATOM   1047 C CA  . VAL A 1 138 ? 19.89641 15.56140 -15.13346 1.000 38.01785  ? 138 VAL A CA  1 
ATOM   1048 C C   . VAL A 1 138 ? 20.48949 16.61529 -14.20647 1.000 40.82944  ? 138 VAL A C   1 
ATOM   1049 O O   . VAL A 1 138 ? 19.85433 17.01240 -13.22133 1.000 40.99058  ? 138 VAL A O   1 
ATOM   1050 C CB  . VAL A 1 138 ? 18.72498 16.13632 -15.94990 1.000 38.73269  ? 138 VAL A CB  1 
ATOM   1051 C CG1 . VAL A 1 138 ? 19.22347 17.08140 -17.00983 1.000 36.93440  ? 138 VAL A CG1 1 
ATOM   1052 C CG2 . VAL A 1 138 ? 17.92084 15.00966 -16.56848 1.000 35.62619  ? 138 VAL A CG2 1 
ATOM   1053 N N   . ILE A 1 139 ? 21.70436 17.06129 -14.51501 1.000 39.45788  ? 139 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 139 ? 22.42522 18.02595 -13.68974 1.000 37.64918  ? 139 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 139 ? 22.59381 19.30049 -14.50684 1.000 37.13083  ? 139 ILE A C   1 
ATOM   1056 O O   . ILE A 1 139 ? 23.31253 19.31310 -15.51479 1.000 38.53698  ? 139 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 139 ? 23.78047 17.47866 -13.21797 1.000 33.12366  ? 139 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 139 ? 23.60663 16.11399 -12.55504 1.000 31.60184  ? 139 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 139 ? 24.42258 18.42802 -12.23148 1.000 35.20885  ? 139 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 139 ? 24.89526 15.51700 -12.03305 1.000 28.81256  ? 139 ILE A CD1 1 
ATOM   1061 N N   . ASN A 1 140 ? 21.93325 20.37306 -14.07107 1.000 36.53059  ? 140 ASN A N   1 
ATOM   1062 C CA  . ASN A 1 140 ? 21.98239 21.66269 -14.75527 1.000 39.35552  ? 140 ASN A CA  1 
ATOM   1063 C C   . ASN A 1 140 ? 21.67893 21.49359 -16.23860 1.000 39.97439  ? 140 ASN A C   1 
ATOM   1064 O O   . ASN A 1 140 ? 22.39312 21.99253 -17.10791 1.000 44.18346  ? 140 ASN A O   1 
ATOM   1065 C CB  . ASN A 1 140 ? 23.33189 22.34748 -14.54316 1.000 34.10666  ? 140 ASN A CB  1 
ATOM   1066 C CG  . ASN A 1 140 ? 23.59701 22.66384 -13.08534 1.000 36.76948  ? 140 ASN A CG  1 
ATOM   1067 O OD1 . ASN A 1 140 ? 22.72373 23.16662 -12.37811 1.000 36.76988  ? 140 ASN A OD1 1 
ATOM   1068 N ND2 . ASN A 1 140 ? 24.80437 22.36637 -12.62633 1.000 36.88162  ? 140 ASN A ND2 1 
ATOM   1069 N N   . ASP A 1 141 ? 20.61710 20.74101 -16.51552 1.000 40.26376  ? 141 ASP A N   1 
ATOM   1070 C CA  . ASP A 1 141 ? 20.09215 20.45131 -17.84770 1.000 45.83949  ? 141 ASP A CA  1 
ATOM   1071 C C   . ASP A 1 141 ? 20.98757 19.52508 -18.66340 1.000 42.41998  ? 141 ASP A C   1 
ATOM   1072 O O   . ASP A 1 141 ? 20.70190 19.28904 -19.83610 1.000 44.37909  ? 141 ASP A O   1 
ATOM   1073 C CB  . ASP A 1 141 ? 19.81223 21.73463 -18.63544 1.000 46.37026  ? 141 ASP A CB  1 
ATOM   1074 C CG  . ASP A 1 141 ? 18.82442 22.63099 -17.92568 1.000 53.55524  ? 141 ASP A CG  1 
ATOM   1075 O OD1 . ASP A 1 141 ? 17.81173 22.09786 -17.41994 1.000 51.71799  ? 141 ASP A OD1 1 
ATOM   1076 O OD2 . ASP A 1 141 ? 19.06813 23.85387 -17.85141 1.000 59.30393  ? 141 ASP A OD2 1 
ATOM   1077 N N   . ILE A 1 142 ? 22.04235 18.97407 -18.07025 1.000 43.45593  ? 142 ILE A N   1 
ATOM   1078 C CA  . ILE A 1 142 ? 22.89195 17.98256 -18.71631 1.000 40.24446  ? 142 ILE A CA  1 
ATOM   1079 C C   . ILE A 1 142 ? 22.47074 16.60458 -18.21779 1.000 40.71737  ? 142 ILE A C   1 
ATOM   1080 O O   . ILE A 1 142 ? 22.44596 16.35960 -17.00467 1.000 38.95156  ? 142 ILE A O   1 
ATOM   1081 C CB  . ILE A 1 142 ? 24.37620 18.23763 -18.40984 1.000 39.55437  ? 142 ILE A CB  1 
ATOM   1082 C CG1 . ILE A 1 142 ? 24.77557 19.66459 -18.80602 0.700 44.06566  ? 142 ILE A CG1 1 
ATOM   1083 C CG2 . ILE A 1 142 ? 25.24555 17.18470 -19.07219 0.700 43.45890  ? 142 ILE A CG2 1 
ATOM   1084 C CD1 . ILE A 1 142 ? 24.48313 19.98877 -20.24635 0.700 48.89624  ? 142 ILE A CD1 1 
ATOM   1085 N N   . HIS A 1 143 ? 22.14702 15.69413 -19.13995 1.000 40.43085  ? 143 HIS A N   1 
ATOM   1086 C CA  . HIS A 1 143 ? 21.77403 14.33829 -18.74471 1.000 41.51851  ? 143 HIS A CA  1 
ATOM   1087 C C   . HIS A 1 143 ? 23.01185 13.57501 -18.29546 1.000 41.13712  ? 143 HIS A C   1 
ATOM   1088 O O   . HIS A 1 143 ? 23.92101 13.32365 -19.08974 1.000 39.77663  ? 143 HIS A O   1 
ATOM   1089 C CB  . HIS A 1 143 ? 21.08696 13.58826 -19.87875 1.000 45.08331  ? 143 HIS A CB  1 
ATOM   1090 C CG  . HIS A 1 143 ? 20.74425 12.17402 -19.52414 1.000 60.26456  ? 143 HIS A CG  1 
ATOM   1091 N ND1 . HIS A 1 143 ? 21.56173 11.10588 -19.83271 1.000 61.67168  ? 143 HIS A ND1 1 
ATOM   1092 C CD2 . HIS A 1 143 ? 19.68371 11.65516 -18.85838 1.000 54.38248  ? 143 HIS A CD2 1 
ATOM   1093 C CE1 . HIS A 1 143 ? 21.01204 9.98843  -19.38724 1.000 48.87183  ? 143 HIS A CE1 1 
ATOM   1094 N NE2 . HIS A 1 143 ? 19.87162 10.29408 -18.79212 1.000 55.99078  ? 143 HIS A NE2 1 
ATOM   1095 N N   . PHE A 1 144 ? 23.02606 13.17722 -17.02745 1.000 39.97907  ? 144 PHE A N   1 
ATOM   1096 C CA  . PHE A 1 144 ? 24.18845 12.56010 -16.41165 1.000 34.67222  ? 144 PHE A CA  1 
ATOM   1097 C C   . PHE A 1 144 ? 24.15051 11.03680 -16.43848 1.000 33.78859  ? 144 PHE A C   1 
ATOM   1098 O O   . PHE A 1 144 ? 25.17033 10.39904 -16.70078 1.000 33.65828  ? 144 PHE A O   1 
ATOM   1099 C CB  . PHE A 1 144 ? 24.31954 13.04597 -14.96797 1.000 32.75306  ? 144 PHE A CB  1 
ATOM   1100 C CG  . PHE A 1 144 ? 25.50913 12.49778 -14.25120 1.000 31.94017  ? 144 PHE A CG  1 
ATOM   1101 C CD1 . PHE A 1 144 ? 26.77135 13.01865 -14.48104 1.000 32.08524  ? 144 PHE A CD1 1 
ATOM   1102 C CD2 . PHE A 1 144 ? 25.36866 11.46215 -13.34849 1.000 31.76767  ? 144 PHE A CD2 1 
ATOM   1103 C CE1 . PHE A 1 144 ? 27.87067 12.50946 -13.82566 1.000 34.67281  ? 144 PHE A CE1 1 
ATOM   1104 C CE2 . PHE A 1 144 ? 26.46055 10.94823 -12.69167 1.000 32.37620  ? 144 PHE A CE2 1 
ATOM   1105 C CZ  . PHE A 1 144 ? 27.71460 11.47072 -12.92920 1.000 34.27042  ? 144 PHE A CZ  1 
ATOM   1106 N N   . GLU A 1 145 ? 23.00429 10.43653 -16.14894 1.000 31.29514  ? 145 GLU A N   1 
ATOM   1107 C CA  . GLU A 1 145 ? 22.91325 8.98585  -16.08039 1.000 30.68407  ? 145 GLU A CA  1 
ATOM   1108 C C   . GLU A 1 145 ? 21.43950 8.61678  -16.06243 1.000 30.89450  ? 145 GLU A C   1 
ATOM   1109 O O   . GLU A 1 145 ? 20.56927 9.46908  -15.86780 1.000 32.64615  ? 145 GLU A O   1 
ATOM   1110 C CB  . GLU A 1 145 ? 23.63276 8.43125  -14.83926 1.000 36.43002  ? 145 GLU A CB  1 
ATOM   1111 C CG  . GLU A 1 145 ? 22.98601 8.83772  -13.51529 1.000 30.23402  ? 145 GLU A CG  1 
ATOM   1112 C CD  . GLU A 1 145 ? 23.77847 8.39195  -12.29011 1.000 33.87474  ? 145 GLU A CD  1 
ATOM   1113 O OE1 . GLU A 1 145 ? 24.80415 7.70243  -12.44111 1.000 38.53615  ? 145 GLU A OE1 1 
ATOM   1114 O OE2 . GLU A 1 145 ? 23.37735 8.73654  -11.16367 1.000 30.76778  ? 145 GLU A OE2 1 
ATOM   1115 N N   . ARG A 1 146 ? 21.17240 7.33206  -16.27054 1.000 33.48143  ? 146 ARG A N   1 
ATOM   1116 C CA  . ARG A 1 146 ? 19.85142 6.74364  -16.07004 1.000 37.03066  ? 146 ARG A CA  1 
ATOM   1117 C C   . ARG A 1 146 ? 19.95615 5.77306  -14.90101 1.000 34.30365  ? 146 ARG A C   1 
ATOM   1118 O O   . ARG A 1 146 ? 20.53592 4.69153  -15.04296 1.000 35.20437  ? 146 ARG A O   1 
ATOM   1119 C CB  . ARG A 1 146 ? 19.36421 6.03557  -17.33082 1.000 37.79356  ? 146 ARG A CB  1 
ATOM   1120 C CG  . ARG A 1 146 ? 18.11002 5.21367  -17.13338 1.000 40.94584  ? 146 ARG A CG  1 
ATOM   1121 C CD  . ARG A 1 146 ? 17.46978 4.84285  -18.46782 1.000 41.45262  ? 146 ARG A CD  1 
ATOM   1122 N NE  . ARG A 1 146 ? 16.97104 6.01716  -19.17028 1.000 40.06382  ? 146 ARG A NE  1 
ATOM   1123 C CZ  . ARG A 1 146 ? 16.21577 5.97773  -20.25925 1.000 44.70327  ? 146 ARG A CZ  1 
ATOM   1124 N NH1 . ARG A 1 146 ? 15.84729 4.82997  -20.80565 1.000 44.99191  ? 146 ARG A NH1 1 
ATOM   1125 N NH2 . ARG A 1 146 ? 15.81754 7.11940  -20.81267 1.000 39.16941  ? 146 ARG A NH2 1 
ATOM   1126 N N   . PHE A 1 147 ? 19.40040 6.15255  -13.74870 1.000 35.15984  ? 147 PHE A N   1 
ATOM   1127 C CA  . PHE A 1 147 ? 19.54972 5.35054  -12.53854 1.000 31.42669  ? 147 PHE A CA  1 
ATOM   1128 C C   . PHE A 1 147 ? 18.52636 4.22175  -12.49855 1.000 29.81651  ? 147 PHE A C   1 
ATOM   1129 O O   . PHE A 1 147 ? 17.31668 4.46645  -12.54340 1.000 30.87028  ? 147 PHE A O   1 
ATOM   1130 C CB  . PHE A 1 147 ? 19.41118 6.20644  -11.28345 1.000 33.31911  ? 147 PHE A CB  1 
ATOM   1131 C CG  . PHE A 1 147 ? 19.63377 5.42929  -10.01370 1.000 31.38888  ? 147 PHE A CG  1 
ATOM   1132 C CD1 . PHE A 1 147 ? 18.57613 4.79881  -9.37001  1.000 32.51874  ? 147 PHE A CD1 1 
ATOM   1133 C CD2 . PHE A 1 147 ? 20.90642 5.29166  -9.49041  1.000 26.60951  ? 147 PHE A CD2 1 
ATOM   1134 C CE1 . PHE A 1 147 ? 18.78782 4.06410  -8.22048  1.000 31.60623  ? 147 PHE A CE1 1 
ATOM   1135 C CE2 . PHE A 1 147 ? 21.11764 4.56082  -8.34221  1.000 30.65742  ? 147 PHE A CE2 1 
ATOM   1136 C CZ  . PHE A 1 147 ? 20.06055 3.94720  -7.70659  1.000 26.64066  ? 147 PHE A CZ  1 
ATOM   1137 N N   . ARG A 1 148 ? 19.01623 2.99003  -12.38296 1.000 30.02979  ? 148 ARG A N   1 
ATOM   1138 C CA  . ARG A 1 148 ? 18.19186 1.81891  -12.11487 1.000 34.20691  ? 148 ARG A CA  1 
ATOM   1139 C C   . ARG A 1 148 ? 18.63304 1.23645  -10.78142 1.000 32.01810  ? 148 ARG A C   1 
ATOM   1140 O O   . ARG A 1 148 ? 19.81025 0.90816  -10.60877 1.000 34.28024  ? 148 ARG A O   1 
ATOM   1141 C CB  . ARG A 1 148 ? 18.32735 0.77026  -13.21921 1.000 34.75085  ? 148 ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 148 ? 18.03033 1.26222  -14.60967 1.000 39.80552  ? 148 ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 148 ? 18.23536 0.15363  -15.62315 0.800 41.06406  ? 148 ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 148 ? 17.38259 0.34341  -16.78707 0.700 39.53504  ? 148 ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 148 ? 17.65744 1.16575  -17.78774 0.700 41.05469  ? 148 ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 148 ? 18.77439 1.87507  -17.81224 0.700 40.53216  ? 148 ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 148 ? 16.78819 1.28141  -18.78736 0.700 44.02196  ? 148 ARG A NH2 1 
ATOM   1148 N N   . GLY A 1 149 ? 17.69847 1.11275  -9.84539  1.000 31.87742  ? 149 GLY A N   1 
ATOM   1149 C CA  . GLY A 1 149 ? 18.04814 0.64144  -8.51392  1.000 30.81435  ? 149 GLY A CA  1 
ATOM   1150 C C   . GLY A 1 149 ? 16.86611 0.74097  -7.57531  1.000 35.72049  ? 149 GLY A C   1 
ATOM   1151 O O   . GLY A 1 149 ? 15.71054 0.72567  -8.00782  1.000 43.41578  ? 149 GLY A O   1 
ATOM   1152 N N   . ASP A 1 150 ? 17.16966 0.84202  -6.28059  1.000 31.32602  ? 150 ASP A N   1 
ATOM   1153 C CA  . ASP A 1 150 ? 16.11299 0.94070  -5.28154  1.000 31.52844  ? 150 ASP A CA  1 
ATOM   1154 C C   . ASP A 1 150 ? 15.66956 2.37763  -5.04727  1.000 31.17114  ? 150 ASP A C   1 
ATOM   1155 O O   . ASP A 1 150 ? 14.48041 2.62717  -4.83863  1.000 36.47878  ? 150 ASP A O   1 
ATOM   1156 C CB  . ASP A 1 150 ? 16.56592 0.31426  -3.96010  1.000 32.62966  ? 150 ASP A CB  1 
ATOM   1157 C CG  . ASP A 1 150 ? 16.61321 -1.20058 -4.01941  1.000 35.24193  ? 150 ASP A CG  1 
ATOM   1158 O OD1 . ASP A 1 150 ? 16.19424 -1.77045 -5.05002  1.000 37.99293  ? 150 ASP A OD1 1 
ATOM   1159 O OD2 . ASP A 1 150 ? 17.07074 -1.82399 -3.03899  1.000 31.43240  ? 150 ASP A OD2 1 
ATOM   1160 N N   . GLY A 1 151 ? 16.59025 3.33129  -5.07909  1.000 31.18242  ? 151 GLY A N   1 
ATOM   1161 C CA  . GLY A 1 151 ? 16.20748 4.71394  -4.89771  1.000 27.98569  ? 151 GLY A CA  1 
ATOM   1162 C C   . GLY A 1 151 ? 17.42301 5.60447  -4.74699  1.000 28.39118  ? 151 GLY A C   1 
ATOM   1163 O O   . GLY A 1 151 ? 18.56735 5.16187  -4.87582  1.000 26.33842  ? 151 GLY A O   1 
ATOM   1164 N N   . LEU A 1 152 ? 17.14209 6.87483  -4.46408  1.000 30.04545  ? 152 LEU A N   1 
ATOM   1165 C CA  . LEU A 1 152 ? 18.15943 7.91097  -4.35986  1.000 29.02625  ? 152 LEU A CA  1 
ATOM   1166 C C   . LEU A 1 152 ? 17.90968 8.75739  -3.11833  1.000 24.94468  ? 152 LEU A C   1 
ATOM   1167 O O   . LEU A 1 152 ? 16.77792 8.88138  -2.65068  1.000 25.51783  ? 152 LEU A O   1 
ATOM   1168 C CB  . LEU A 1 152 ? 18.17410 8.80705  -5.61163  1.000 26.96355  ? 152 LEU A CB  1 
ATOM   1169 C CG  . LEU A 1 152 ? 18.67570 8.17278  -6.91223  1.000 29.56320  ? 152 LEU A CG  1 
ATOM   1170 C CD1 . LEU A 1 152 ? 18.43421 9.10536  -8.08601  1.000 27.72095  ? 152 LEU A CD1 1 
ATOM   1171 C CD2 . LEU A 1 152 ? 20.15212 7.81487  -6.81691  1.000 25.06937  ? 152 LEU A CD2 1 
ATOM   1172 N N   . CYS A 1 153 ? 18.97954 9.35225  -2.59888  1.000 25.59852  ? 153 CYS A N   1 
ATOM   1173 C CA  . CYS A 1 153 ? 18.93164 10.13458 -1.36766  1.000 26.82092  ? 153 CYS A CA  1 
ATOM   1174 C C   . CYS A 1 153 ? 19.70504 11.42862 -1.57829  1.000 25.15353  ? 153 CYS A C   1 
ATOM   1175 O O   . CYS A 1 153 ? 20.89487 11.39408 -1.90688  1.000 26.56458  ? 153 CYS A O   1 
ATOM   1176 C CB  . CYS A 1 153 ? 19.51331 9.32584  -0.19900  1.000 27.48570  ? 153 CYS A CB  1 
ATOM   1177 S SG  . CYS A 1 153 ? 19.76483 10.20547 1.36966   1.000 33.54766  ? 153 CYS A SG  1 
ATOM   1178 N N   . MET A 1 154 ? 19.03096 12.56294 -1.40711  1.000 25.86396  ? 154 MET A N   1 
ATOM   1179 C CA  . MET A 1 154 ? 19.65561 13.87818 -1.49274  1.000 29.24949  ? 154 MET A CA  1 
ATOM   1180 C C   . MET A 1 154 ? 19.68746 14.48144 -0.09711  1.000 28.28323  ? 154 MET A C   1 
ATOM   1181 O O   . MET A 1 154 ? 18.63387 14.71903 0.50077   1.000 28.94459  ? 154 MET A O   1 
ATOM   1182 C CB  . MET A 1 154 ? 18.90246 14.79321 -2.45785  1.000 27.92586  ? 154 MET A CB  1 
ATOM   1183 C CG  . MET A 1 154 ? 19.64102 16.08760 -2.76708  1.000 27.48165  ? 154 MET A CG  1 
ATOM   1184 S SD  . MET A 1 154 ? 21.18760 15.78432 -3.65313  1.000 35.52503  ? 154 MET A SD  1 
ATOM   1185 C CE  . MET A 1 154 ? 20.71131 16.16758 -5.33419  1.000 27.59288  ? 154 MET A CE  1 
ATOM   1186 N N   . SER A 1 155 ? 20.88903 14.73998 0.41055   1.000 31.70971  ? 155 SER A N   1 
ATOM   1187 C CA  . SER A 1 155 ? 21.09873 15.03151 1.82298   1.000 30.97021  ? 155 SER A CA  1 
ATOM   1188 C C   . SER A 1 155 ? 21.65460 16.43602 2.02944   1.000 30.71142  ? 155 SER A C   1 
ATOM   1189 O O   . SER A 1 155 ? 22.46401 16.92132 1.23277   1.000 30.23264  ? 155 SER A O   1 
ATOM   1190 C CB  . SER A 1 155 ? 22.05154 13.99902 2.44379   1.000 28.42709  ? 155 SER A CB  1 
ATOM   1191 O OG  . SER A 1 155 ? 22.53088 14.42162 3.71016   1.000 32.25038  ? 155 SER A OG  1 
ATOM   1192 N N   . THR A 1 156 ? 21.19852 17.08515 3.10550   1.000 31.69268  ? 156 THR A N   1 
ATOM   1193 C CA  . THR A 1 156 ? 21.79771 18.31688 3.59597   1.000 29.26373  ? 156 THR A CA  1 
ATOM   1194 C C   . THR A 1 156 ? 23.16481 17.99243 4.18975   1.000 28.23212  ? 156 THR A C   1 
ATOM   1195 O O   . THR A 1 156 ? 23.48648 16.82650 4.42526   1.000 30.34646  ? 156 THR A O   1 
ATOM   1196 C CB  . THR A 1 156 ? 20.90353 18.97342 4.65322   1.000 33.40235  ? 156 THR A CB  1 
ATOM   1197 O OG1 . THR A 1 156 ? 20.71380 18.07568 5.75731   1.000 32.40058  ? 156 THR A OG1 1 
ATOM   1198 C CG2 . THR A 1 156 ? 19.55482 19.36361 4.08269   1.000 33.01456  ? 156 THR A CG2 1 
ATOM   1199 N N   . PRO A 1 157 ? 24.00092 19.01293 4.43697   1.000 29.46510  ? 157 PRO A N   1 
ATOM   1200 C CA  . PRO A 1 157 ? 25.24792 18.75582 5.18152   1.000 28.79459  ? 157 PRO A CA  1 
ATOM   1201 C C   . PRO A 1 157 ? 25.00131 18.10318 6.53074   1.000 32.08354  ? 157 PRO A C   1 
ATOM   1202 O O   . PRO A 1 157 ? 25.58573 17.05221 6.81404   1.000 31.44396  ? 157 PRO A O   1 
ATOM   1203 C CB  . PRO A 1 157 ? 25.86916 20.15018 5.32329   1.000 29.75519  ? 157 PRO A CB  1 
ATOM   1204 C CG  . PRO A 1 157 ? 25.29858 20.94134 4.20237   1.000 36.23281  ? 157 PRO A CG  1 
ATOM   1205 C CD  . PRO A 1 157 ? 23.90890 20.41283 3.98017   1.000 32.18214  ? 157 PRO A CD  1 
ATOM   1206 N N   . SER A 1 158 ? 24.13089 18.69237 7.36408   1.000 33.17323  ? 158 SER A N   1 
ATOM   1207 C CA  A SER A 1 158 ? 23.88343 18.08088 8.65940   0.700 33.62253  ? 158 SER A CA  1 
ATOM   1208 C CA  B SER A 1 158 ? 23.79634 18.11859 8.66676   0.300 39.47781  ? 158 SER A CA  1 
ATOM   1209 C C   . SER A 1 158 ? 23.22609 16.71604 8.53293   1.000 33.13837  ? 158 SER A C   1 
ATOM   1210 O O   . SER A 1 158 ? 23.33725 15.90629 9.45922   1.000 34.60762  ? 158 SER A O   1 
ATOM   1211 C CB  A SER A 1 158 ? 23.02548 18.99336 9.53808   0.700 33.29285  ? 158 SER A CB  1 
ATOM   1212 C CB  B SER A 1 158 ? 22.78554 19.01345 9.38941   0.300 32.45318  ? 158 SER A CB  1 
ATOM   1213 O OG  A SER A 1 158 ? 21.72715 19.16665 9.00149   0.700 31.42641  ? 158 SER A OG  1 
ATOM   1214 O OG  B SER A 1 158 ? 23.12169 19.18099 10.75495  0.300 32.80652  ? 158 SER A OG  1 
ATOM   1215 N N   . GLY A 1 159 ? 22.57407 16.42931 7.40892   1.000 32.34524  ? 159 GLY A N   1 
ATOM   1216 C CA  . GLY A 1 159 ? 21.98435 15.12414 7.20466   1.000 30.72753  ? 159 GLY A CA  1 
ATOM   1217 C C   . GLY A 1 159 ? 22.95763 14.04735 6.80431   1.000 31.47182  ? 159 GLY A C   1 
ATOM   1218 O O   . GLY A 1 159 ? 22.57661 12.87341 6.79360   1.000 28.80874  ? 159 GLY A O   1 
ATOM   1219 N N   . THR A 1 160 ? 24.20600 14.41435 6.48472   1.000 32.97274  ? 160 THR A N   1 
ATOM   1220 C CA  . THR A 1 160 ? 25.16745 13.42723 5.99792   1.000 30.14554  ? 160 THR A CA  1 
ATOM   1221 C C   . THR A 1 160 ? 25.46453 12.36422 7.04205   1.000 31.91333  ? 160 THR A C   1 
ATOM   1222 O O   . THR A 1 160 ? 25.83442 11.23881 6.68576   1.000 32.26400  ? 160 THR A O   1 
ATOM   1223 C CB  . THR A 1 160 ? 26.47258 14.10034 5.55849   1.000 29.43391  ? 160 THR A CB  1 
ATOM   1224 O OG1 . THR A 1 160 ? 26.96595 14.96096 6.59071   1.000 27.52869  ? 160 THR A OG1 1 
ATOM   1225 C CG2 . THR A 1 160 ? 26.25903 14.90886 4.28339   1.000 32.18909  ? 160 THR A CG2 1 
ATOM   1226 N N   . THR A 1 161 ? 25.29759 12.68949 8.32427   1.000 27.96726  ? 161 THR A N   1 
ATOM   1227 C CA  . THR A 1 161 ? 25.48931 11.70263 9.37646   1.000 30.48701  ? 161 THR A CA  1 
ATOM   1228 C C   . THR A 1 161 ? 24.27308 10.80730 9.57258   1.000 32.69804  ? 161 THR A C   1 
ATOM   1229 O O   . THR A 1 161 ? 24.32044 9.90363  10.41542  1.000 31.31801  ? 161 THR A O   1 
ATOM   1230 C CB  . THR A 1 161 ? 25.84394 12.39844 10.69280  1.000 31.56918  ? 161 THR A CB  1 
ATOM   1231 O OG1 . THR A 1 161 ? 24.90841 13.45113 10.94741  1.000 34.20309  ? 161 THR A OG1 1 
ATOM   1232 C CG2 . THR A 1 161 ? 27.23418 12.98789 10.61006  1.000 32.20089  ? 161 THR A CG2 1 
ATOM   1233 N N   . ALA A 1 162 ? 23.21306 11.01221 8.80253   1.000 32.22202  ? 162 ALA A N   1 
ATOM   1234 C CA  . ALA A 1 162 ? 21.94589 10.31522 8.98606   1.000 31.35071  ? 162 ALA A CA  1 
ATOM   1235 C C   . ALA A 1 162 ? 21.81701 9.23173  7.91224   1.000 29.91840  ? 162 ALA A C   1 
ATOM   1236 O O   . ALA A 1 162 ? 22.73141 8.40872  7.80115   1.000 27.41975  ? 162 ALA A O   1 
ATOM   1237 C CB  . ALA A 1 162 ? 20.81042 11.34245 9.00784   1.000 30.56259  ? 162 ALA A CB  1 
ATOM   1238 N N   . TYR A 1 163 ? 20.72546 9.17377  7.14395   1.000 34.32350  ? 163 TYR A N   1 
ATOM   1239 C CA  . TYR A 1 163 ? 20.56385 8.17724  6.09065   1.000 29.38189  ? 163 TYR A CA  1 
ATOM   1240 C C   . TYR A 1 163 ? 21.74440 8.19084  5.12325   1.000 30.93790  ? 163 TYR A C   1 
ATOM   1241 O O   . TYR A 1 163 ? 22.22632 7.13142  4.69965   1.000 30.76619  ? 163 TYR A O   1 
ATOM   1242 C CB  . TYR A 1 163 ? 19.24975 8.45562  5.35479   1.000 32.17524  ? 163 TYR A CB  1 
ATOM   1243 C CG  . TYR A 1 163 ? 18.61376 7.27653  4.64466   1.000 31.80558  ? 163 TYR A CG  1 
ATOM   1244 C CD1 . TYR A 1 163 ? 19.26421 6.05539  4.53900   1.000 30.72170  ? 163 TYR A CD1 1 
ATOM   1245 C CD2 . TYR A 1 163 ? 17.35692 7.39839  4.07421   1.000 32.70462  ? 163 TYR A CD2 1 
ATOM   1246 C CE1 . TYR A 1 163 ? 18.67502 4.98782  3.88893   1.000 32.75936  ? 163 TYR A CE1 1 
ATOM   1247 C CE2 . TYR A 1 163 ? 16.75891 6.34020  3.42159   1.000 36.56829  ? 163 TYR A CE2 1 
ATOM   1248 C CZ  . TYR A 1 163 ? 17.41893 5.13687  3.32993   1.000 38.63850  ? 163 TYR A CZ  1 
ATOM   1249 O OH  . TYR A 1 163 ? 16.81060 4.08624  2.67464   1.000 35.39844  ? 163 TYR A OH  1 
ATOM   1250 N N   . ASN A 1 164 ? 22.22683 9.38793  4.77184   1.000 27.10331  ? 164 ASN A N   1 
ATOM   1251 C CA  . ASN A 1 164 ? 23.35953 9.51731  3.85976   1.000 25.83868  ? 164 ASN A CA  1 
ATOM   1252 C C   . ASN A 1 164 ? 24.54744 8.67927  4.30871   1.000 31.25959  ? 164 ASN A C   1 
ATOM   1253 O O   . ASN A 1 164 ? 25.26803 8.11241  3.47736   1.000 31.65213  ? 164 ASN A O   1 
ATOM   1254 C CB  . ASN A 1 164 ? 23.76248 10.98977 3.74906   1.000 28.89738  ? 164 ASN A CB  1 
ATOM   1255 C CG  . ASN A 1 164 ? 25.07495 11.18690 3.01527   1.000 30.36614  ? 164 ASN A CG  1 
ATOM   1256 O OD1 . ASN A 1 164 ? 25.10085 11.31707 1.79351   1.000 31.56360  ? 164 ASN A OD1 1 
ATOM   1257 N ND2 . ASN A 1 164 ? 26.17158 11.22709 3.76075   1.000 30.45258  ? 164 ASN A ND2 1 
ATOM   1258 N N   . LYS A 1 165 ? 24.76894 8.58990  5.62268   1.000 28.54110  ? 165 LYS A N   1 
ATOM   1259 C CA  . LYS A 1 165 ? 25.91924 7.85124  6.13408   1.000 26.53825  ? 165 LYS A CA  1 
ATOM   1260 C C   . LYS A 1 165 ? 25.78889 6.35607  5.86259   1.000 26.62130  ? 165 LYS A C   1 
ATOM   1261 O O   . LYS A 1 165 ? 26.77658 5.69047  5.52753   1.000 26.60097  ? 165 LYS A O   1 
ATOM   1262 C CB  . LYS A 1 165 ? 26.08400 8.11396  7.63095   1.000 31.30042  ? 165 LYS A CB  1 
ATOM   1263 C CG  . LYS A 1 165 ? 27.29489 7.44051  8.25395   1.000 24.06593  ? 165 LYS A CG  1 
ATOM   1264 C CD  . LYS A 1 165 ? 27.63991 8.07475  9.58519   1.000 27.89018  ? 165 LYS A CD  1 
ATOM   1265 C CE  . LYS A 1 165 ? 28.89035 7.46298  10.18633  1.000 26.00070  ? 165 LYS A CE  1 
ATOM   1266 N NZ  . LYS A 1 165 ? 28.81962 5.97833  10.23217  1.000 29.53495  ? 165 LYS A NZ  1 
ATOM   1267 N N   . SER A 1 166 ? 24.57944 5.80870  5.99821   1.000 27.19651  ? 166 SER A N   1 
ATOM   1268 C CA  . SER A 1 166 ? 24.38751 4.37821  5.78376   1.000 30.28526  ? 166 SER A CA  1 
ATOM   1269 C C   . SER A 1 166 ? 24.49118 3.98925  4.31122   1.000 31.13675  ? 166 SER A C   1 
ATOM   1270 O O   . SER A 1 166 ? 24.64542 2.80108  4.00487   1.000 27.15692  ? 166 SER A O   1 
ATOM   1271 C CB  . SER A 1 166 ? 23.03392 3.93577  6.34607   1.000 30.97138  ? 166 SER A CB  1 
ATOM   1272 O OG  . SER A 1 166 ? 22.98558 4.09398  7.75567   1.000 32.79402  ? 166 SER A OG  1 
ATOM   1273 N N   . LEU A 1 167 ? 24.41468 4.95552  3.39787   1.000 30.04179  ? 167 LEU A N   1 
ATOM   1274 C CA  . LEU A 1 167 ? 24.50189 4.68933  1.97043   1.000 30.30384  ? 167 LEU A CA  1 
ATOM   1275 C C   . LEU A 1 167 ? 25.90177 4.93139  1.42264   1.000 30.98914  ? 167 LEU A C   1 
ATOM   1276 O O   . LEU A 1 167 ? 26.07755 5.00910  0.20163   1.000 31.84475  ? 167 LEU A O   1 
ATOM   1277 C CB  . LEU A 1 167 ? 23.47445 5.53783  1.21297   1.000 26.51721  ? 167 LEU A CB  1 
ATOM   1278 C CG  . LEU A 1 167 ? 22.01357 5.34611  1.64942   1.000 26.86600  ? 167 LEU A CG  1 
ATOM   1279 C CD1 . LEU A 1 167 ? 21.13895 6.46545  1.12863   1.000 27.76453  ? 167 LEU A CD1 1 
ATOM   1280 C CD2 . LEU A 1 167 ? 21.46383 3.99760  1.20525   1.000 27.81485  ? 167 LEU A CD2 1 
ATOM   1281 N N   . GLY A 1 168 ? 26.89911 5.04853  2.29561   1.000 30.67096  ? 168 GLY A N   1 
ATOM   1282 C CA  . GLY A 1 168 ? 28.26530 5.26381  1.87236   1.000 27.13086  ? 168 GLY A CA  1 
ATOM   1283 C C   . GLY A 1 168 ? 28.64445 6.70105  1.58841   1.000 25.04067  ? 168 GLY A C   1 
ATOM   1284 O O   . GLY A 1 168 ? 29.77499 6.94640  1.14948   1.000 26.99626  ? 168 GLY A O   1 
ATOM   1285 N N   . GLY A 1 169 ? 27.75070 7.65812  1.83020   1.000 27.31745  ? 169 GLY A N   1 
ATOM   1286 C CA  . GLY A 1 169 ? 28.06787 9.04503  1.56117   1.000 26.57252  ? 169 GLY A CA  1 
ATOM   1287 C C   . GLY A 1 169 ? 29.13031 9.59981  2.49499   1.000 31.80672  ? 169 GLY A C   1 
ATOM   1288 O O   . GLY A 1 169 ? 29.44059 9.04413  3.55002   1.000 28.19621  ? 169 GLY A O   1 
ATOM   1289 N N   . ALA A 1 170 ? 29.71011 10.72253 2.08528   1.000 26.69485  ? 170 ALA A N   1 
ATOM   1290 C CA  . ALA A 1 170 ? 30.67887 11.41008 2.91701   1.000 26.67711  ? 170 ALA A CA  1 
ATOM   1291 C C   . ALA A 1 170 ? 29.96711 12.26324 3.95516   1.000 31.62851  ? 170 ALA A C   1 
ATOM   1292 O O   . ALA A 1 170 ? 28.84655 12.73360 3.73909   1.000 32.32263  ? 170 ALA A O   1 
ATOM   1293 C CB  . ALA A 1 170 ? 31.59665 12.29054 2.06719   1.000 28.91519  ? 170 ALA A CB  1 
ATOM   1294 N N   . LEU A 1 171 ? 30.62942 12.46399 5.09268   1.000 23.68123  ? 171 LEU A N   1 
ATOM   1295 C CA  . LEU A 1 171 ? 30.14076 13.38962 6.10629   1.000 27.08871  ? 171 LEU A CA  1 
ATOM   1296 C C   . LEU A 1 171 ? 30.79842 14.74111 5.86711   1.000 25.52968  ? 171 LEU A C   1 
ATOM   1297 O O   . LEU A 1 171 ? 32.02784 14.84799 5.90513   1.000 27.96119  ? 171 LEU A O   1 
ATOM   1298 C CB  . LEU A 1 171 ? 30.45571 12.88932 7.51598   1.000 26.27738  ? 171 LEU A CB  1 
ATOM   1299 C CG  . LEU A 1 171 ? 30.37931 11.39126 7.78643   1.000 24.25585  ? 171 LEU A CG  1 
ATOM   1300 C CD1 . LEU A 1 171 ? 30.76980 11.10930 9.23258   1.000 29.47036  ? 171 LEU A CD1 1 
ATOM   1301 C CD2 . LEU A 1 171 ? 28.99423 10.86389 7.48813   1.000 23.74737  ? 171 LEU A CD2 1 
ATOM   1302 N N   . MET A 1 172 ? 29.99593 15.76976 5.62545   1.000 27.46103  ? 172 MET A N   1 
ATOM   1303 C CA  . MET A 1 172 ? 30.54206 17.09470 5.39300   1.000 29.73974  ? 172 MET A CA  1 
ATOM   1304 C C   . MET A 1 172 ? 30.06270 18.06780 6.45915   1.000 30.95023  ? 172 MET A C   1 
ATOM   1305 O O   . MET A 1 172 ? 28.99001 17.90576 7.04365   1.000 32.08808  ? 172 MET A O   1 
ATOM   1306 C CB  . MET A 1 172 ? 30.19425 17.62198 3.99065   1.000 30.09328  ? 172 MET A CB  1 
ATOM   1307 C CG  . MET A 1 172 ? 28.75180 17.50137 3.58709   1.000 35.39949  ? 172 MET A CG  1 
ATOM   1308 S SD  . MET A 1 172 ? 28.55755 17.87630 1.82364   1.000 37.58102  ? 172 MET A SD  1 
ATOM   1309 C CE  . MET A 1 172 ? 26.83075 17.48260 1.60380   1.000 29.29365  ? 172 MET A CE  1 
ATOM   1310 N N   . HIS A 1 173 ? 30.88628 19.07584 6.70385   1.000 33.30299  ? 173 HIS A N   1 
ATOM   1311 C CA  . HIS A 1 173 ? 30.67272 20.07816 7.73507   1.000 37.86554  ? 173 HIS A CA  1 
ATOM   1312 C C   . HIS A 1 173 ? 29.59686 21.07206 7.29713   1.000 40.17749  ? 173 HIS A C   1 
ATOM   1313 O O   . HIS A 1 173 ? 29.59241 21.51423 6.14491   1.000 38.54064  ? 173 HIS A O   1 
ATOM   1314 C CB  . HIS A 1 173 ? 31.97305 20.81336 8.02855   1.000 33.82559  ? 173 HIS A CB  1 
ATOM   1315 C CG  . HIS A 1 173 ? 31.87464 21.77452 9.16642   1.000 35.87595  ? 173 HIS A CG  1 
ATOM   1316 N ND1 . HIS A 1 173 ? 31.37262 23.04915 9.01974   1.000 39.40933  ? 173 HIS A ND1 1 
ATOM   1317 C CD2 . HIS A 1 173 ? 32.21535 21.64997 10.47050  1.000 37.02371  ? 173 HIS A CD2 1 
ATOM   1318 C CE1 . HIS A 1 173 ? 31.40945 23.66969 10.18506  1.000 42.84873  ? 173 HIS A CE1 1 
ATOM   1319 N NE2 . HIS A 1 173 ? 31.91751 22.84304 11.08180  1.000 42.92243  ? 173 HIS A NE2 1 
ATOM   1320 N N   . PRO A 1 174 ? 28.68982 21.45733 8.20270   1.000 39.85487  ? 174 PRO A N   1 
ATOM   1321 C CA  . PRO A 1 174 ? 27.51013 22.23016 7.78556   1.000 35.88572  ? 174 PRO A CA  1 
ATOM   1322 C C   . PRO A 1 174 ? 27.81003 23.65288 7.34852   1.000 36.99002  ? 174 PRO A C   1 
ATOM   1323 O O   . PRO A 1 174 ? 26.89480 24.32697 6.86425   1.000 35.74426  ? 174 PRO A O   1 
ATOM   1324 C CB  . PRO A 1 174 ? 26.62127 22.22026 9.03792   1.000 39.02379  ? 174 PRO A CB  1 
ATOM   1325 C CG  . PRO A 1 174 ? 27.17372 21.15552 9.91468   1.000 36.71355  ? 174 PRO A CG  1 
ATOM   1326 C CD  . PRO A 1 174 ? 28.63390 21.11230 9.62947   1.000 38.90308  ? 174 PRO A CD  1 
ATOM   1327 N N   . SER A 1 175 ? 29.03510 24.14884 7.51440   1.000 37.16818  ? 175 SER A N   1 
ATOM   1328 C CA  . SER A 1 175 ? 29.34816 25.45214 6.94542   1.000 37.32968  ? 175 SER A CA  1 
ATOM   1329 C C   . SER A 1 175 ? 29.49484 25.39765 5.43039   1.000 38.34302  ? 175 SER A C   1 
ATOM   1330 O O   . SER A 1 175 ? 29.61235 26.45298 4.79491   1.000 37.90898  ? 175 SER A O   1 
ATOM   1331 C CB  . SER A 1 175 ? 30.61905 26.01463 7.58097   1.000 37.76265  ? 175 SER A CB  1 
ATOM   1332 O OG  . SER A 1 175 ? 31.68834 25.09846 7.46801   1.000 40.43645  ? 175 SER A OG  1 
ATOM   1333 N N   . ILE A 1 176 ? 29.48875 24.20168 4.84664   1.000 37.79778  ? 176 ILE A N   1 
ATOM   1334 C CA  . ILE A 1 176 ? 29.53007 24.02512 3.39791   1.000 41.56165  ? 176 ILE A CA  1 
ATOM   1335 C C   . ILE A 1 176 ? 28.10290 24.06405 2.86910   1.000 38.68451  ? 176 ILE A C   1 
ATOM   1336 O O   . ILE A 1 176 ? 27.29179 23.18516 3.18338   1.000 35.08342  ? 176 ILE A O   1 
ATOM   1337 C CB  . ILE A 1 176 ? 30.21365 22.70322 3.01356   1.000 37.92083  ? 176 ILE A CB  1 
ATOM   1338 C CG1 . ILE A 1 176 ? 31.63188 22.63843 3.58227   1.000 36.85810  ? 176 ILE A CG1 1 
ATOM   1339 C CG2 . ILE A 1 176 ? 30.22296 22.52490 1.50102   1.000 34.43045  ? 176 ILE A CG2 1 
ATOM   1340 C CD1 . ILE A 1 176 ? 32.38109 21.38268 3.18693   1.000 36.63915  ? 176 ILE A CD1 1 
ATOM   1341 N N   . GLU A 1 177 ? 27.79581 25.07391 2.05971   1.000 37.49408  ? 177 GLU A N   1 
ATOM   1342 C CA  . GLU A 1 177 ? 26.46817 25.19382 1.46444   1.000 36.72990  ? 177 GLU A CA  1 
ATOM   1343 C C   . GLU A 1 177 ? 26.42095 24.27171 0.25290   1.000 36.77230  ? 177 GLU A C   1 
ATOM   1344 O O   . GLU A 1 177 ? 26.85399 24.63394 -0.84360  1.000 37.61349  ? 177 GLU A O   1 
ATOM   1345 C CB  . GLU A 1 177 ? 26.16681 26.64682 1.11422   1.000 38.82764  ? 177 GLU A CB  1 
ATOM   1346 C CG  . GLU A 1 177 ? 25.89157 27.50284 2.35057   0.800 37.84387  ? 177 GLU A CG  1 
ATOM   1347 C CD  . GLU A 1 177 ? 25.65994 28.96489 2.03105   0.700 42.56484  ? 177 GLU A CD  1 
ATOM   1348 O OE1 . GLU A 1 177 ? 26.16873 29.44457 0.99676   0.700 42.08927  ? 177 GLU A OE1 1 
ATOM   1349 O OE2 . GLU A 1 177 ? 24.96665 29.63792 2.82038   0.700 45.74595  ? 177 GLU A OE2 1 
ATOM   1350 N N   . ALA A 1 178 ? 25.90644 23.06295 0.45916   1.000 35.39395  ? 178 ALA A N   1 
ATOM   1351 C CA  . ALA A 1 178 ? 25.98562 22.01131 -0.54121  1.000 29.68226  ? 178 ALA A CA  1 
ATOM   1352 C C   . ALA A 1 178 ? 24.92658 20.95960 -0.23678  1.000 32.18228  ? 178 ALA A C   1 
ATOM   1353 O O   . ALA A 1 178 ? 24.22075 21.02718 0.77396   1.000 34.01686  ? 178 ALA A O   1 
ATOM   1354 C CB  . ALA A 1 178 ? 27.38667 21.39934 -0.58232  1.000 29.69803  ? 178 ALA A CB  1 
ATOM   1355 N N   . MET A 1 179 ? 24.82404 19.98217 -1.13568  1.000 33.36721  ? 179 MET A N   1 
ATOM   1356 C CA  . MET A 1 179 ? 23.90259 18.86275 -1.01127  1.000 29.91799  ? 179 MET A CA  1 
ATOM   1357 C C   . MET A 1 179 ? 24.56238 17.64931 -1.64935  1.000 30.71801  ? 179 MET A C   1 
ATOM   1358 O O   . MET A 1 179 ? 25.36535 17.78411 -2.57762  1.000 31.59576  ? 179 MET A O   1 
ATOM   1359 C CB  . MET A 1 179 ? 22.54734 19.16187 -1.67311  1.000 34.76990  ? 179 MET A CB  1 
ATOM   1360 C CG  . MET A 1 179 ? 22.63789 19.52732 -3.15657  1.000 30.20493  ? 179 MET A CG  1 
ATOM   1361 S SD  . MET A 1 179 ? 21.03911 19.70463 -3.97818  1.000 36.97924  ? 179 MET A SD  1 
ATOM   1362 C CE  . MET A 1 179 ? 21.55601 20.08574 -5.64681  1.000 28.79456  ? 179 MET A CE  1 
ATOM   1363 N N   . GLN A 1 180 ? 24.22166 16.46285 -1.14811  1.000 28.60056  ? 180 GLN A N   1 
ATOM   1364 C CA  . GLN A 1 180 ? 24.92111 15.24257 -1.52597  1.000 26.30497  ? 180 GLN A CA  1 
ATOM   1365 C C   . GLN A 1 180 ? 23.93790 14.16312 -1.93583  1.000 29.22476  ? 180 GLN A C   1 
ATOM   1366 O O   . GLN A 1 180 ? 23.03195 13.81878 -1.16862  1.000 28.90029  ? 180 GLN A O   1 
ATOM   1367 C CB  . GLN A 1 180 ? 25.79299 14.72974 -0.38651  1.000 27.60074  ? 180 GLN A CB  1 
ATOM   1368 C CG  . GLN A 1 180 ? 26.60692 13.50457 -0.73983  1.000 26.71122  ? 180 GLN A CG  1 
ATOM   1369 C CD  . GLN A 1 180 ? 27.59705 13.15925 0.34517   1.000 30.56920  ? 180 GLN A CD  1 
ATOM   1370 O OE1 . GLN A 1 180 ? 28.27503 12.13513 0.28364   1.000 30.55897  ? 180 GLN A OE1 1 
ATOM   1371 N NE2 . GLN A 1 180 ? 27.68544 14.01966 1.35457   1.000 29.26993  ? 180 GLN A NE2 1 
ATOM   1372 N N   . LEU A 1 181 ? 24.14340 13.61353 -3.13151  1.000 28.18669  ? 181 LEU A N   1 
ATOM   1373 C CA  . LEU A 1 181 ? 23.29499 12.56485 -3.67899  1.000 27.50701  ? 181 LEU A CA  1 
ATOM   1374 C C   . LEU A 1 181 ? 24.00047 11.22062 -3.55307  1.000 26.21758  ? 181 LEU A C   1 
ATOM   1375 O O   . LEU A 1 181 ? 25.16744 11.08906 -3.94010  1.000 23.91236  ? 181 LEU A O   1 
ATOM   1376 C CB  . LEU A 1 181 ? 22.96055 12.85471 -5.14368  1.000 31.28211  ? 181 LEU A CB  1 
ATOM   1377 C CG  . LEU A 1 181 ? 22.01262 11.90093 -5.87416  1.000 28.32559  ? 181 LEU A CG  1 
ATOM   1378 C CD1 . LEU A 1 181 ? 20.58280 12.04853 -5.36163  1.000 24.15801  ? 181 LEU A CD1 1 
ATOM   1379 C CD2 . LEU A 1 181 ? 22.08419 12.14063 -7.37507  1.000 24.43457  ? 181 LEU A CD2 1 
ATOM   1380 N N   . THR A 1 182 ? 23.29351 10.23224 -3.00554  1.000 24.47219  ? 182 THR A N   1 
ATOM   1381 C CA  . THR A 1 182 ? 23.81285 8.88267  -2.86179  1.000 24.92056  ? 182 THR A CA  1 
ATOM   1382 C C   . THR A 1 182 ? 22.81528 7.89234  -3.44313  1.000 23.89789  ? 182 THR A C   1 
ATOM   1383 O O   . THR A 1 182 ? 21.61816 8.16685  -3.52670  1.000 23.52689  ? 182 THR A O   1 
ATOM   1384 C CB  . THR A 1 182 ? 24.10855 8.51760  -1.39098  1.000 28.69616  ? 182 THR A CB  1 
ATOM   1385 O OG1 . THR A 1 182 ? 22.91543 8.63568  -0.60898  1.000 28.74341  ? 182 THR A OG1 1 
ATOM   1386 C CG2 . THR A 1 182 ? 25.18398 9.42151  -0.80869  1.000 25.03242  ? 182 THR A CG2 1 
ATOM   1387 N N   . GLU A 1 183 ? 23.33012 6.73076  -3.84057  1.000 28.47966  ? 183 GLU A N   1 
ATOM   1388 C CA  . GLU A 1 183 ? 22.56165 5.67438  -4.48455  1.000 24.18553  ? 183 GLU A CA  1 
ATOM   1389 C C   . GLU A 1 183 ? 22.08922 4.63780  -3.47417  1.000 28.10868  ? 183 GLU A C   1 
ATOM   1390 O O   . GLU A 1 183 ? 22.70023 4.43548  -2.42196  1.000 28.98380  ? 183 GLU A O   1 
ATOM   1391 C CB  . GLU A 1 183 ? 23.39965 4.97408  -5.55545  1.000 25.87376  ? 183 GLU A CB  1 
ATOM   1392 C CG  . GLU A 1 183 ? 23.89376 5.88915  -6.66918  1.000 31.28244  ? 183 GLU A CG  1 
ATOM   1393 C CD  . GLU A 1 183 ? 24.71279 5.15154  -7.71294  1.000 28.34392  ? 183 GLU A CD  1 
ATOM   1394 O OE1 . GLU A 1 183 ? 25.03556 3.96274  -7.49572  1.000 25.54888  ? 183 GLU A OE1 1 
ATOM   1395 O OE2 . GLU A 1 183 ? 25.03620 5.76433  -8.75150  1.000 33.71015  ? 183 GLU A OE2 1 
ATOM   1396 N N   . MET A 1 184 ? 20.99121 3.96816  -3.81591  1.000 31.89682  ? 184 MET A N   1 
ATOM   1397 C CA  . MET A 1 184 ? 20.53179 2.78323  -3.09651  1.000 28.64594  ? 184 MET A CA  1 
ATOM   1398 C C   . MET A 1 184 ? 20.53681 1.62081  -4.08127  1.000 28.98856  ? 184 MET A C   1 
ATOM   1399 O O   . MET A 1 184 ? 19.74739 1.61385  -5.03159  1.000 33.11221  ? 184 MET A O   1 
ATOM   1400 C CB  . MET A 1 184 ? 19.13370 2.97554  -2.50557  1.000 26.13406  ? 184 MET A CB  1 
ATOM   1401 C CG  . MET A 1 184 ? 18.92665 4.22912  -1.67565  1.000 25.47610  ? 184 MET A CG  1 
ATOM   1402 S SD  . MET A 1 184 ? 17.22237 4.30295  -1.06650  1.000 36.91567  ? 184 MET A SD  1 
ATOM   1403 C CE  . MET A 1 184 ? 17.20581 5.89614  -0.26230  1.000 28.73902  ? 184 MET A CE  1 
ATOM   1404 N N   . ALA A 1 185 ? 21.43196 0.66103  -3.86109  1.000 26.62488  ? 185 ALA A N   1 
ATOM   1405 C CA  . ALA A 1 185 ? 21.49201 -0.60052 -4.60106  1.000 32.22409  ? 185 ALA A CA  1 
ATOM   1406 C C   . ALA A 1 185 ? 21.24952 -0.40654 -6.10075  1.000 35.55788  ? 185 ALA A C   1 
ATOM   1407 O O   . ALA A 1 185 ? 20.27317 -0.88956 -6.67508  1.000 32.85782  ? 185 ALA A O   1 
ATOM   1408 C CB  . ALA A 1 185 ? 20.50789 -1.61076 -4.02364  1.000 28.60103  ? 185 ALA A CB  1 
ATOM   1409 N N   . SER A 1 186 ? 22.15785 0.32736  -6.73421  1.000 31.36429  ? 186 SER A N   1 
ATOM   1410 C CA  . SER A 1 186 ? 22.08518 0.48629  -8.17962  1.000 33.98072  ? 186 SER A CA  1 
ATOM   1411 C C   . SER A 1 186 ? 22.49939 -0.80541 -8.86576  1.000 35.39068  ? 186 SER A C   1 
ATOM   1412 O O   . SER A 1 186 ? 23.40542 -1.50705 -8.40795  1.000 40.67748  ? 186 SER A O   1 
ATOM   1413 C CB  . SER A 1 186 ? 22.98880 1.62193  -8.64068  1.000 33.97888  ? 186 SER A CB  1 
ATOM   1414 O OG  . SER A 1 186 ? 24.29915 1.43592  -8.13214  1.000 43.49525  ? 186 SER A OG  1 
ATOM   1415 N N   . ILE A 1 187 ? 21.83285 -1.12493 -9.96716  1.000 34.48007  ? 187 ILE A N   1 
ATOM   1416 C CA  . ILE A 1 187 ? 22.22267 -2.26632 -10.78253 1.000 35.60126  ? 187 ILE A CA  1 
ATOM   1417 C C   . ILE A 1 187 ? 23.20021 -1.77678 -11.84078 1.000 36.01955  ? 187 ILE A C   1 
ATOM   1418 O O   . ILE A 1 187 ? 22.89565 -0.85714 -12.60893 1.000 34.43745  ? 187 ILE A O   1 
ATOM   1419 C CB  . ILE A 1 187 ? 21.00449 -2.95831 -11.41040 1.000 37.09692  ? 187 ILE A CB  1 
ATOM   1420 C CG1 . ILE A 1 187 ? 21.42434 -3.77096 -12.63521 1.000 39.49661  ? 187 ILE A CG1 1 
ATOM   1421 C CG2 . ILE A 1 187 ? 19.93188 -1.95687 -11.75016 1.000 39.00176  ? 187 ILE A CG2 1 
ATOM   1422 C CD1 . ILE A 1 187 ? 20.94016 -5.19924 -12.60139 1.000 38.28940  ? 187 ILE A CD1 1 
ATOM   1423 N N   . ASN A 1 188 ? 24.38972 -2.37156 -11.85527 1.000 38.91014  ? 188 ASN A N   1 
ATOM   1424 C CA  . ASN A 1 188 ? 25.45065 -1.99636 -12.77862 1.000 39.79766  ? 188 ASN A CA  1 
ATOM   1425 C C   . ASN A 1 188 ? 25.92537 -3.23590 -13.51561 1.000 37.39919  ? 188 ASN A C   1 
ATOM   1426 O O   . ASN A 1 188 ? 26.39334 -4.19261 -12.89037 1.000 39.10950  ? 188 ASN A O   1 
ATOM   1427 C CB  . ASN A 1 188 ? 26.61263 -1.32944 -12.04013 1.000 37.69143  ? 188 ASN A CB  1 
ATOM   1428 C CG  . ASN A 1 188 ? 26.46498 0.17484  -11.97399 1.000 41.56037  ? 188 ASN A CG  1 
ATOM   1429 O OD1 . ASN A 1 188 ? 26.95661 0.89352  -12.84581 1.000 40.98861  ? 188 ASN A OD1 1 
ATOM   1430 N ND2 . ASN A 1 188 ? 25.77197 0.66183  -10.94689 1.000 35.74958  ? 188 ASN A ND2 1 
ATOM   1431 N N   . ASN A 1 189 ? 25.80211 -3.21938 -14.83543 1.000 43.15988  ? 189 ASN A N   1 
ATOM   1432 C CA  . ASN A 1 189 ? 26.31600 -4.30188 -15.66350 1.000 46.92144  ? 189 ASN A CA  1 
ATOM   1433 C C   . ASN A 1 189 ? 26.71223 -3.71436 -17.01422 1.000 52.69972  ? 189 ASN A C   1 
ATOM   1434 O O   . ASN A 1 189 ? 26.93333 -2.50470 -17.13655 1.000 52.79985  ? 189 ASN A O   1 
ATOM   1435 C CB  . ASN A 1 189 ? 25.28339 -5.44005 -15.76904 1.000 45.60923  ? 189 ASN A CB  1 
ATOM   1436 C CG  . ASN A 1 189 ? 23.92301 -4.96078 -16.23776 1.000 43.73880  ? 189 ASN A CG  1 
ATOM   1437 O OD1 . ASN A 1 189 ? 23.81715 -4.01987 -17.02264 1.000 46.84886  ? 189 ASN A OD1 1 
ATOM   1438 N ND2 . ASN A 1 189 ? 22.87061 -5.60865 -15.75098 1.000 40.53134  ? 189 ASN A ND2 1 
ATOM   1439 N N   . ARG A 1 190 ? 26.79345 -4.57646 -18.03210 1.000 62.12322  ? 190 ARG A N   1 
ATOM   1440 C CA  . ARG A 1 190 ? 27.23270 -4.14697 -19.35616 1.000 69.98235  ? 190 ARG A CA  1 
ATOM   1441 C C   . ARG A 1 190 ? 26.28088 -3.12448 -19.96876 1.000 66.31631  ? 190 ARG A C   1 
ATOM   1442 O O   . ARG A 1 190 ? 26.71776 -2.24299 -20.71800 1.000 61.47616  ? 190 ARG A O   1 
ATOM   1443 C CB  . ARG A 1 190 ? 27.37510 -5.37391 -20.26289 1.000 67.45728  ? 190 ARG A CB  1 
ATOM   1444 C CG  . ARG A 1 190 ? 27.89607 -5.10426 -21.66492 1.000 73.55244  ? 190 ARG A CG  1 
ATOM   1445 C CD  . ARG A 1 190 ? 26.85126 -5.47379 -22.71001 1.000 78.83325  ? 190 ARG A CD  1 
ATOM   1446 N NE  . ARG A 1 190 ? 26.06291 -6.63203 -22.30319 1.000 84.74131  ? 190 ARG A NE  1 
ATOM   1447 C CZ  . ARG A 1 190 ? 26.35649 -7.88880 -22.60784 1.000 83.50272  ? 190 ARG A CZ  1 
ATOM   1448 N NH1 . ARG A 1 190 ? 27.41419 -8.19282 -23.34014 1.000 77.16608  ? 190 ARG A NH1 1 
ATOM   1449 N NH2 . ARG A 1 190 ? 25.56775 -8.86532 -22.16634 1.000 88.99120  ? 190 ARG A NH2 1 
ATOM   1450 N N   . VAL A 1 191 ? 24.98971 -3.20826 -19.64728 1.000 57.84113  ? 191 VAL A N   1 
ATOM   1451 C CA  . VAL A 1 191 ? 23.97785 -2.34533 -20.24833 1.000 53.62259  ? 191 VAL A CA  1 
ATOM   1452 C C   . VAL A 1 191 ? 23.64365 -1.17917 -19.32314 1.000 52.26851  ? 191 VAL A C   1 
ATOM   1453 O O   . VAL A 1 191 ? 23.36388 -0.06805 -19.78708 1.000 53.19976  ? 191 VAL A O   1 
ATOM   1454 C CB  . VAL A 1 191 ? 22.71252 -3.15276 -20.59720 1.000 59.26201  ? 191 VAL A CB  1 
ATOM   1455 C CG1 . VAL A 1 191 ? 21.66049 -2.26030 -21.24752 1.000 65.88160  ? 191 VAL A CG1 1 
ATOM   1456 C CG2 . VAL A 1 191 ? 23.06244 -4.31693 -21.51348 1.000 63.06146  ? 191 VAL A CG2 1 
ATOM   1457 N N   . TYR A 1 192 ? 23.67814 -1.41229 -18.01378 1.000 49.13012  ? 192 TYR A N   1 
ATOM   1458 C CA  . TYR A 1 192 ? 23.23117 -0.43300 -17.02868 1.000 49.93735  ? 192 TYR A CA  1 
ATOM   1459 C C   . TYR A 1 192 ? 24.42620 0.14005  -16.27692 1.000 43.89112  ? 192 TYR A C   1 
ATOM   1460 O O   . TYR A 1 192 ? 25.22572 -0.60910 -15.70670 1.000 40.93650  ? 192 TYR A O   1 
ATOM   1461 C CB  . TYR A 1 192 ? 22.23773 -1.06341 -16.05302 1.000 46.61889  ? 192 TYR A CB  1 
ATOM   1462 C CG  . TYR A 1 192 ? 21.03669 -1.68008 -16.72932 0.700 45.39972  ? 192 TYR A CG  1 
ATOM   1463 C CD1 . TYR A 1 192 ? 20.55010 -1.16727 -17.92482 0.700 47.25173  ? 192 TYR A CD1 1 
ATOM   1464 C CD2 . TYR A 1 192 ? 20.39503 -2.78019 -16.17679 0.700 43.90025  ? 192 TYR A CD2 1 
ATOM   1465 C CE1 . TYR A 1 192 ? 19.45298 -1.73079 -18.54917 0.700 49.59616  ? 192 TYR A CE1 1 
ATOM   1466 C CE2 . TYR A 1 192 ? 19.29938 -3.35017 -16.79297 0.700 46.01404  ? 192 TYR A CE2 1 
ATOM   1467 C CZ  . TYR A 1 192 ? 18.83231 -2.82176 -17.97848 0.700 45.55881  ? 192 TYR A CZ  1 
ATOM   1468 O OH  . TYR A 1 192 ? 17.74053 -3.38803 -18.59384 0.700 52.71750  ? 192 TYR A OH  1 
ATOM   1469 N N   . ARG A 1 193 ? 24.53034 1.46812  -16.25974 1.000 40.93408  ? 193 ARG A N   1 
ATOM   1470 C CA  . ARG A 1 193 ? 25.73005 2.14868  -15.78603 1.000 38.31751  ? 193 ARG A CA  1 
ATOM   1471 C C   . ARG A 1 193 ? 25.34018 3.39362  -15.00424 1.000 37.84772  ? 193 ARG A C   1 
ATOM   1472 O O   . ARG A 1 193 ? 24.75285 4.32256  -15.56636 1.000 35.19320  ? 193 ARG A O   1 
ATOM   1473 C CB  . ARG A 1 193 ? 26.63527 2.52157  -16.96613 1.000 49.47630  ? 193 ARG A CB  1 
ATOM   1474 C CG  . ARG A 1 193 ? 27.91302 3.24641  -16.57664 1.000 53.16439  ? 193 ARG A CG  1 
ATOM   1475 C CD  . ARG A 1 193 ? 29.14412 2.43265  -16.94927 1.000 51.21128  ? 193 ARG A CD  1 
ATOM   1476 N NE  . ARG A 1 193 ? 30.08131 2.33928  -15.83604 0.700 52.33073  ? 193 ARG A NE  1 
ATOM   1477 C CZ  . ARG A 1 193 ? 30.10270 1.34649  -14.95730 0.700 50.74695  ? 193 ARG A CZ  1 
ATOM   1478 N NH1 . ARG A 1 193 ? 29.25254 0.33418  -15.03696 0.700 47.42403  ? 193 ARG A NH1 1 
ATOM   1479 N NH2 . ARG A 1 193 ? 31.00129 1.36852  -13.97626 0.700 53.69654  ? 193 ARG A NH2 1 
ATOM   1480 N N   . THR A 1 194 ? 25.66756 3.41436  -13.71601 1.000 36.36592  ? 194 THR A N   1 
ATOM   1481 C CA  . THR A 1 194 ? 25.57183 4.61494  -12.90076 1.000 34.44956  ? 194 THR A CA  1 
ATOM   1482 C C   . THR A 1 194 ? 26.95493 4.96400  -12.36555 1.000 30.72113  ? 194 THR A C   1 
ATOM   1483 O O   . THR A 1 194 ? 27.90727 4.19352  -12.49431 1.000 34.44174  ? 194 THR A O   1 
ATOM   1484 C CB  . THR A 1 194 ? 24.56905 4.44452  -11.74549 1.000 37.58372  ? 194 THR A CB  1 
ATOM   1485 O OG1 . THR A 1 194 ? 25.10130 3.55270  -10.75340 1.000 30.36409  ? 194 THR A OG1 1 
ATOM   1486 C CG2 . THR A 1 194 ? 23.23559 3.90019  -12.26301 1.000 30.30473  ? 194 THR A CG2 1 
ATOM   1487 N N   . ILE A 1 195 ? 27.06263 6.15117  -11.76605 1.000 28.81963  ? 195 ILE A N   1 
ATOM   1488 C CA  . ILE A 1 195 ? 28.35880 6.60897  -11.26922 1.000 30.75139  ? 195 ILE A CA  1 
ATOM   1489 C C   . ILE A 1 195 ? 28.76863 5.84354  -10.01298 1.000 30.61678  ? 195 ILE A C   1 
ATOM   1490 O O   . ILE A 1 195 ? 29.95924 5.59190  -9.79126  1.000 26.87028  ? 195 ILE A O   1 
ATOM   1491 C CB  . ILE A 1 195 ? 28.32879 8.13351  -11.03024 1.000 29.38152  ? 195 ILE A CB  1 
ATOM   1492 C CG1 . ILE A 1 195 ? 29.72849 8.66822  -10.72836 1.000 26.77432  ? 195 ILE A CG1 1 
ATOM   1493 C CG2 . ILE A 1 195 ? 27.35158 8.50190  -9.91943  1.000 26.75874  ? 195 ILE A CG2 1 
ATOM   1494 C CD1 . ILE A 1 195 ? 30.66544 8.60247  -11.90368 1.000 27.54812  ? 195 ILE A CD1 1 
ATOM   1495 N N   . GLY A 1 196 ? 27.81260 5.43312  -9.19148  1.000 29.27921  ? 196 GLY A N   1 
ATOM   1496 C CA  . GLY A 1 196 ? 28.17350 4.74220  -7.95213  1.000 31.91554  ? 196 GLY A CA  1 
ATOM   1497 C C   . GLY A 1 196 ? 28.66375 5.65849  -6.85095  1.000 31.60930  ? 196 GLY A C   1 
ATOM   1498 O O   . GLY A 1 196 ? 28.12641 5.63538  -5.73935  1.000 32.62667  ? 196 GLY A O   1 
ATOM   1499 N N   . SER A 1 197 ? 29.66688 6.48073  -7.14062  1.000 25.78977  ? 197 SER A N   1 
ATOM   1500 C CA  . SER A 1 197 ? 30.17567 7.41403  -6.15378  1.000 27.24032  ? 197 SER A CA  1 
ATOM   1501 C C   . SER A 1 197 ? 29.08732 8.40321  -5.74086  1.000 29.15219  ? 197 SER A C   1 
ATOM   1502 O O   . SER A 1 197 ? 28.22057 8.75910  -6.54486  1.000 26.62556  ? 197 SER A O   1 
ATOM   1503 C CB  . SER A 1 197 ? 31.37961 8.17471  -6.70606  1.000 24.84074  ? 197 SER A CB  1 
ATOM   1504 O OG  . SER A 1 197 ? 32.47756 7.31325  -6.93060  1.000 26.13623  ? 197 SER A OG  1 
ATOM   1505 N N   . PRO A 1 198 ? 29.09555 8.84333  -4.48182  1.000 30.19905  ? 198 PRO A N   1 
ATOM   1506 C CA  . PRO A 1 198 ? 28.23671 9.96477  -4.09396  1.000 27.77982  ? 198 PRO A CA  1 
ATOM   1507 C C   . PRO A 1 198 ? 28.65964 11.22826 -4.82170  1.000 29.22849  ? 198 PRO A C   1 
ATOM   1508 O O   . PRO A 1 198 ? 29.82152 11.39435 -5.20344  1.000 27.22299  ? 198 PRO A O   1 
ATOM   1509 C CB  . PRO A 1 198 ? 28.46779 10.08941 -2.58267  1.000 25.21622  ? 198 PRO A CB  1 
ATOM   1510 C CG  . PRO A 1 198 ? 28.99260 8.75542  -2.16689  1.000 24.88146  ? 198 PRO A CG  1 
ATOM   1511 C CD  . PRO A 1 198 ? 29.80751 8.27243  -3.32463  1.000 27.73938  ? 198 PRO A CD  1 
ATOM   1512 N N   . LEU A 1 199 ? 27.70039 12.12782 -5.00613  1.000 26.29524  ? 199 LEU A N   1 
ATOM   1513 C CA  . LEU A 1 199 ? 27.93745 13.39978 -5.66886  1.000 27.62854  ? 199 LEU A CA  1 
ATOM   1514 C C   . LEU A 1 199 ? 27.57228 14.52161 -4.71382  1.000 25.93157  ? 199 LEU A C   1 
ATOM   1515 O O   . LEU A 1 199 ? 26.50134 14.49321 -4.10036  1.000 26.35791  ? 199 LEU A O   1 
ATOM   1516 C CB  . LEU A 1 199 ? 27.12092 13.51529 -6.96248  1.000 29.06403  ? 199 LEU A CB  1 
ATOM   1517 C CG  . LEU A 1 199 ? 27.23175 12.34506 -7.93935  1.000 26.43369  ? 199 LEU A CG  1 
ATOM   1518 C CD1 . LEU A 1 199 ? 26.37948 12.58477 -9.17425  1.000 27.38107  ? 199 LEU A CD1 1 
ATOM   1519 C CD2 . LEU A 1 199 ? 28.67513 12.11712 -8.32076  1.000 24.71540  ? 199 LEU A CD2 1 
ATOM   1520 N N   . VAL A 1 200 ? 28.46156 15.50191 -4.59377  1.000 28.36363  ? 200 VAL A N   1 
ATOM   1521 C CA  . VAL A 1 200 ? 28.26146 16.66842 -3.74241  1.000 28.69412  ? 200 VAL A CA  1 
ATOM   1522 C C   . VAL A 1 200 ? 28.10803 17.87817 -4.65251  1.000 30.50172  ? 200 VAL A C   1 
ATOM   1523 O O   . VAL A 1 200 ? 29.00571 18.18245 -5.45106  1.000 32.55915  ? 200 VAL A O   1 
ATOM   1524 C CB  . VAL A 1 200 ? 29.42155 16.85003 -2.74979  1.000 28.98457  ? 200 VAL A CB  1 
ATOM   1525 C CG1 . VAL A 1 200 ? 29.22418 18.10783 -1.91823  1.000 29.58594  ? 200 VAL A CG1 1 
ATOM   1526 C CG2 . VAL A 1 200 ? 29.53044 15.63189 -1.84886  1.000 26.50103  ? 200 VAL A CG2 1 
ATOM   1527 N N   . PHE A 1 201 ? 26.95834 18.56105 -4.54103  1.000 30.12404  ? 201 PHE A N   1 
ATOM   1528 C CA  . PHE A 1 201 ? 26.60941 19.66417 -5.41686  1.000 28.44328  ? 201 PHE A CA  1 
ATOM   1529 C C   . PHE A 1 201 ? 26.64782 20.98932 -4.67484  1.000 33.48060  ? 201 PHE A C   1 
ATOM   1530 O O   . PHE A 1 201 ? 26.19988 21.06796 -3.52678  1.000 34.81398  ? 201 PHE A O   1 
ATOM   1531 C CB  . PHE A 1 201 ? 25.21433 19.46423 -6.00939  1.000 28.86907  ? 201 PHE A CB  1 
ATOM   1532 C CG  . PHE A 1 201 ? 25.08847 18.22860 -6.83421  1.000 31.08914  ? 201 PHE A CG  1 
ATOM   1533 C CD1 . PHE A 1 201 ? 25.45197 18.23628 -8.16803  1.000 29.82079  ? 201 PHE A CD1 1 
ATOM   1534 C CD2 . PHE A 1 201 ? 24.61739 17.05460 -6.27541  1.000 28.63273  ? 201 PHE A CD2 1 
ATOM   1535 C CE1 . PHE A 1 201 ? 25.33906 17.10019 -8.93275  1.000 31.55378  ? 201 PHE A CE1 1 
ATOM   1536 C CE2 . PHE A 1 201 ? 24.50260 15.91081 -7.03618  1.000 32.00461  ? 201 PHE A CE2 1 
ATOM   1537 C CZ  . PHE A 1 201 ? 24.86460 15.93612 -8.37310  1.000 31.07602  ? 201 PHE A CZ  1 
ATOM   1538 N N   . PRO A 1 202 ? 27.16136 22.04020 -5.29686  1.000 36.13604  ? 202 PRO A N   1 
ATOM   1539 C CA  . PRO A 1 202 ? 27.21820 23.34670 -4.64005  1.000 35.13315  ? 202 PRO A CA  1 
ATOM   1540 C C   . PRO A 1 202 ? 25.86760 24.05196 -4.70614  1.000 39.40273  ? 202 PRO A C   1 
ATOM   1541 O O   . PRO A 1 202 ? 24.91738 23.57913 -5.33760  1.000 37.99834  ? 202 PRO A O   1 
ATOM   1542 C CB  . PRO A 1 202 ? 28.27395 24.09150 -5.45442  1.000 34.57954  ? 202 PRO A CB  1 
ATOM   1543 C CG  . PRO A 1 202 ? 28.10526 23.53307 -6.83790  1.000 35.88573  ? 202 PRO A CG  1 
ATOM   1544 C CD  . PRO A 1 202 ? 27.74403 22.07703 -6.65206  1.000 33.97623  ? 202 PRO A CD  1 
ATOM   1545 N N   . LYS A 1 203 ? 25.80131 25.20179 -4.03799  1.000 39.88878  ? 203 LYS A N   1 
ATOM   1546 C CA  . LYS A 1 203 ? 24.65665 26.08520 -4.17328  1.000 42.62573  ? 203 LYS A CA  1 
ATOM   1547 C C   . LYS A 1 203 ? 24.45131 26.43008 -5.63719  1.000 40.54892  ? 203 LYS A C   1 
ATOM   1548 O O   . LYS A 1 203 ? 25.38415 26.37384 -6.44035  1.000 43.93211  ? 203 LYS A O   1 
ATOM   1549 C CB  . LYS A 1 203 ? 24.88962 27.36974 -3.36622  1.000 45.90775  ? 203 LYS A CB  1 
ATOM   1550 C CG  . LYS A 1 203 ? 23.73770 27.82619 -2.49368  0.900 42.13812  ? 203 LYS A CG  1 
ATOM   1551 C CD  . LYS A 1 203 ? 24.16943 29.05676 -1.70782  0.800 48.30016  ? 203 LYS A CD  1 
ATOM   1552 C CE  . LYS A 1 203 ? 24.85508 30.07854 -2.62274  0.700 52.59108  ? 203 LYS A CE  1 
ATOM   1553 N NZ  . LYS A 1 203 ? 25.41436 31.26000 -1.90271  0.700 52.19467  ? 203 LYS A NZ  1 
ATOM   1554 N N   . HIS A 1 204 ? 23.21436 26.77207 -5.98549  1.000 44.79721  ? 204 HIS A N   1 
ATOM   1555 C CA  . HIS A 1 204 ? 22.78252 27.22096 -7.31301  1.000 48.32265  ? 204 HIS A CA  1 
ATOM   1556 C C   . HIS A 1 204 ? 22.82500 26.12179 -8.37495  1.000 41.84584  ? 204 HIS A C   1 
ATOM   1557 O O   . HIS A 1 204 ? 22.47253 26.38424 -9.52343  1.000 42.72116  ? 204 HIS A O   1 
ATOM   1558 C CB  . HIS A 1 204 ? 23.59980 28.42371 -7.82056  1.000 48.96754  ? 204 HIS A CB  1 
ATOM   1559 C CG  . HIS A 1 204 ? 23.49075 29.64271 -6.95704  1.000 51.25196  ? 204 HIS A CG  1 
ATOM   1560 N ND1 . HIS A 1 204 ? 22.29747 30.07066 -6.41528  1.000 52.07750  ? 204 HIS A ND1 1 
ATOM   1561 C CD2 . HIS A 1 204 ? 24.42900 30.52689 -6.54492  1.000 52.22756  ? 204 HIS A CD2 1 
ATOM   1562 C CE1 . HIS A 1 204 ? 22.50612 31.16589 -5.70678  1.000 50.28851  ? 204 HIS A CE1 1 
ATOM   1563 N NE2 . HIS A 1 204 ? 23.79141 31.46296 -5.76866  1.000 57.94628  ? 204 HIS A NE2 1 
ATOM   1564 N N   . HIS A 1 205 ? 23.23820 24.90443 -8.03065  1.000 41.14806  ? 205 HIS A N   1 
ATOM   1565 C CA  . HIS A 1 205 ? 23.13656 23.77557 -8.94127  1.000 38.53758  ? 205 HIS A CA  1 
ATOM   1566 C C   . HIS A 1 205 ? 21.77805 23.10148 -8.78798  1.000 40.49213  ? 205 HIS A C   1 
ATOM   1567 O O   . HIS A 1 205 ? 21.26936 22.94947 -7.67437  1.000 39.35671  ? 205 HIS A O   1 
ATOM   1568 C CB  . HIS A 1 205 ? 24.25268 22.76045 -8.68432  1.000 37.15593  ? 205 HIS A CB  1 
ATOM   1569 C CG  . HIS A 1 205 ? 25.54093 23.08313 -9.37810  1.000 37.50158  ? 205 HIS A CG  1 
ATOM   1570 N ND1 . HIS A 1 205 ? 26.37877 22.11394 -9.88787  1.000 33.29898  ? 205 HIS A ND1 1 
ATOM   1571 C CD2 . HIS A 1 205 ? 26.13207 24.27067 -9.64961  1.000 39.20428  ? 205 HIS A CD2 1 
ATOM   1572 C CE1 . HIS A 1 205 ? 27.43126 22.69148 -10.43940 1.000 34.81700  ? 205 HIS A CE1 1 
ATOM   1573 N NE2 . HIS A 1 205 ? 27.30596 24.00001 -10.30854 1.000 31.18807  ? 205 HIS A NE2 1 
ATOM   1574 N N   . VAL A 1 206 ? 21.18870 22.70501 -9.91473  1.000 40.96442  ? 206 VAL A N   1 
ATOM   1575 C CA  . VAL A 1 206 ? 19.88357 22.05161 -9.93469  1.000 35.90518  ? 206 VAL A CA  1 
ATOM   1576 C C   . VAL A 1 206 ? 20.07359 20.61591 -10.39333 1.000 36.85594  ? 206 VAL A C   1 
ATOM   1577 O O   . VAL A 1 206 ? 20.60713 20.37042 -11.48261 1.000 40.20474  ? 206 VAL A O   1 
ATOM   1578 C CB  . VAL A 1 206 ? 18.88383 22.77724 -10.84643 1.000 32.66689  ? 206 VAL A CB  1 
ATOM   1579 C CG1 . VAL A 1 206 ? 17.52763 22.08961 -10.78508 1.000 33.69301  ? 206 VAL A CG1 1 
ATOM   1580 C CG2 . VAL A 1 206 ? 18.76317 24.23963 -10.45899 1.000 36.70639  ? 206 VAL A CG2 1 
ATOM   1581 N N   . VAL A 1 207 ? 19.63966 19.66989 -9.56628  1.000 36.83083  ? 207 VAL A N   1 
ATOM   1582 C CA  . VAL A 1 207 ? 19.62137 18.25807 -9.92111  1.000 37.70066  ? 207 VAL A CA  1 
ATOM   1583 C C   . VAL A 1 207 ? 18.16592 17.86495 -10.11261 1.000 39.31241  ? 207 VAL A C   1 
ATOM   1584 O O   . VAL A 1 207 ? 17.33481 18.07469 -9.22099  1.000 37.54305  ? 207 VAL A O   1 
ATOM   1585 C CB  . VAL A 1 207 ? 20.31046 17.38828 -8.85656  1.000 32.79689  ? 207 VAL A CB  1 
ATOM   1586 C CG1 . VAL A 1 207 ? 20.08146 15.91838 -9.14130  1.000 31.15657  ? 207 VAL A CG1 1 
ATOM   1587 C CG2 . VAL A 1 207 ? 21.79153 17.68892 -8.82847  1.000 28.75252  ? 207 VAL A CG2 1 
ATOM   1588 N N   . SER A 1 208 ? 17.85183 17.31407 -11.28033 1.000 42.27551  ? 208 SER A N   1 
ATOM   1589 C CA  . SER A 1 208 ? 16.47722 17.03244 -11.66952 1.000 41.33264  ? 208 SER A CA  1 
ATOM   1590 C C   . SER A 1 208 ? 16.32692 15.55458 -11.98767 1.000 41.00909  ? 208 SER A C   1 
ATOM   1591 O O   . SER A 1 208 ? 17.08216 15.01030 -12.80050 1.000 44.15497  ? 208 SER A O   1 
ATOM   1592 C CB  . SER A 1 208 ? 16.07257 17.87343 -12.87865 1.000 42.27676  ? 208 SER A CB  1 
ATOM   1593 O OG  . SER A 1 208 ? 14.79316 17.49285 -13.34190 1.000 50.32699  ? 208 SER A OG  1 
ATOM   1594 N N   . LEU A 1 209 ? 15.35652 14.91038 -11.35208 1.000 40.25764  ? 209 LEU A N   1 
ATOM   1595 C CA  . LEU A 1 209 ? 15.03011 13.52228 -11.64407 1.000 41.36224  ? 209 LEU A CA  1 
ATOM   1596 C C   . LEU A 1 209 ? 13.81764 13.49324 -12.56525 1.000 41.44223  ? 209 LEU A C   1 
ATOM   1597 O O   . LEU A 1 209 ? 12.85005 14.22749 -12.34535 1.000 42.84804  ? 209 LEU A O   1 
ATOM   1598 C CB  . LEU A 1 209 ? 14.76147 12.73756 -10.35938 1.000 36.77705  ? 209 LEU A CB  1 
ATOM   1599 C CG  . LEU A 1 209 ? 15.86314 12.86399 -9.29950  1.000 37.48157  ? 209 LEU A CG  1 
ATOM   1600 C CD1 . LEU A 1 209 ? 15.54377 12.04474 -8.05254  1.000 33.02151  ? 209 LEU A CD1 1 
ATOM   1601 C CD2 . LEU A 1 209 ? 17.21319 12.46571 -9.87344  1.000 36.04044  ? 209 LEU A CD2 1 
ATOM   1602 N N   . GLN A 1 210 ? 13.87899 12.66407 -13.60525 1.000 41.25195  ? 210 GLN A N   1 
ATOM   1603 C CA  . GLN A 1 210 ? 12.83970 12.63088 -14.61841 1.000 44.32194  ? 210 GLN A CA  1 
ATOM   1604 C C   . GLN A 1 210 ? 12.43950 11.18661 -14.89752 1.000 43.94927  ? 210 GLN A C   1 
ATOM   1605 O O   . GLN A 1 210 ? 13.30905 10.34574 -15.19189 1.000 38.75361  ? 210 GLN A O   1 
ATOM   1606 C CB  . GLN A 1 210 ? 13.32271 13.32363 -15.89760 1.000 40.21310  ? 210 GLN A CB  1 
ATOM   1607 C CG  . GLN A 1 210 ? 13.50083 14.82105 -15.71391 1.000 42.35258  ? 210 GLN A CG  1 
ATOM   1608 C CD  . GLN A 1 210 ? 14.13362 15.51042 -16.90491 1.000 51.27904  ? 210 GLN A CD  1 
ATOM   1609 O OE1 . GLN A 1 210 ? 14.13271 14.99195 -18.02263 1.000 43.50908  ? 210 GLN A OE1 1 
ATOM   1610 N NE2 . GLN A 1 210 ? 14.68160 16.69619 -16.66721 1.000 53.08315  ? 210 GLN A NE2 1 
ATOM   1611 N N   . PRO A 1 211 ? 11.14870 10.86445 -14.84672 1.000 47.46618  ? 211 PRO A N   1 
ATOM   1612 C CA  . PRO A 1 211 ? 10.72564 9.46529  -14.96687 1.000 48.03452  ? 211 PRO A CA  1 
ATOM   1613 C C   . PRO A 1 211 ? 10.99288 8.91986  -16.35830 1.000 51.99256  ? 211 PRO A C   1 
ATOM   1614 O O   . PRO A 1 211 ? 11.09480 9.65863  -17.34181 1.000 54.48244  ? 211 PRO A O   1 
ATOM   1615 C CB  . PRO A 1 211 ? 9.21957  9.51551  -14.67454 1.000 50.36021  ? 211 PRO A CB  1 
ATOM   1616 C CG  . PRO A 1 211 ? 8.94795  10.92344 -14.17398 1.000 51.98513  ? 211 PRO A CG  1 
ATOM   1617 C CD  . PRO A 1 211 ? 10.00244 11.78459 -14.77092 1.000 46.62104  ? 211 PRO A CD  1 
ATOM   1618 N N   . VAL A 1 212 ? 11.11736 7.59333  -16.42101 1.000 54.72843  ? 212 VAL A N   1 
ATOM   1619 C CA  . VAL A 1 212 ? 11.35698 6.86995  -17.66471 1.000 57.92758  ? 212 VAL A CA  1 
ATOM   1620 C C   . VAL A 1 212 ? 10.12183 6.08282  -18.09977 1.000 60.62283  ? 212 VAL A C   1 
ATOM   1621 O O   . VAL A 1 212 ? 9.72887  6.11924  -19.26790 1.000 63.20388  ? 212 VAL A O   1 
ATOM   1622 C CB  . VAL A 1 212 ? 12.58498 5.94317  -17.53275 1.000 46.25215  ? 212 VAL A CB  1 
ATOM   1623 C CG1 . VAL A 1 212 ? 12.73964 5.06580  -18.77359 1.000 47.52188  ? 212 VAL A CG1 1 
ATOM   1624 C CG2 . VAL A 1 212 ? 13.84274 6.76141  -17.29292 1.000 39.66079  ? 212 VAL A CG2 1 
ATOM   1625 N N   . ASN A 1 213 ? 9.49514  5.36437  -17.16647 1.000 59.85214  ? 213 ASN A N   1 
ATOM   1626 C CA  . ASN A 1 213 ? 8.24389  4.66467  -17.44200 1.000 59.95159  ? 213 ASN A CA  1 
ATOM   1627 C C   . ASN A 1 213 ? 7.18791  5.04337  -16.41444 1.000 59.18610  ? 213 ASN A C   1 
ATOM   1628 O O   . ASN A 1 213 ? 6.44108  6.00911  -16.60278 1.000 60.96423  ? 213 ASN A O   1 
ATOM   1629 C CB  . ASN A 1 213 ? 8.44585  3.14796  -17.44193 1.000 61.18974  ? 213 ASN A CB  1 
ATOM   1630 C CG  . ASN A 1 213 ? 9.24319  2.66704  -18.62838 1.000 62.78263  ? 213 ASN A CG  1 
ATOM   1631 O OD1 . ASN A 1 213 ? 9.31468  3.33677  -19.65754 1.000 69.99794  ? 213 ASN A OD1 1 
ATOM   1632 N ND2 . ASN A 1 213 ? 9.84281  1.49321  -18.49664 1.000 67.10152  ? 213 ASN A ND2 1 
ATOM   1633 N N   . ASP A 1 214 ? 7.12937  4.28321  -15.32584 1.000 60.55588  ? 214 ASP A N   1 
ATOM   1634 C CA  . ASP A 1 214 ? 6.19327  4.57382  -14.25207 1.000 61.53543  ? 214 ASP A CA  1 
ATOM   1635 C C   . ASP A 1 214 ? 6.50140  5.93096  -13.63364 1.000 57.81087  ? 214 ASP A C   1 
ATOM   1636 O O   . ASP A 1 214 ? 7.66234  6.27741  -13.39935 1.000 56.41658  ? 214 ASP A O   1 
ATOM   1637 C CB  . ASP A 1 214 ? 6.25918  3.46776  -13.19893 1.000 63.04027  ? 214 ASP A CB  1 
ATOM   1638 C CG  . ASP A 1 214 ? 5.53773  3.83157  -11.92131 1.000 67.46400  ? 214 ASP A CG  1 
ATOM   1639 O OD1 . ASP A 1 214 ? 4.39591  4.33135  -11.99399 1.000 68.81368  ? 214 ASP A OD1 1 
ATOM   1640 O OD2 . ASP A 1 214 ? 6.10942  3.60468  -10.83543 1.000 71.72979  ? 214 ASP A OD2 1 
ATOM   1641 N N   . LYS A 1 215 ? 5.44829  6.70706  -13.38320 1.000 61.99838  ? 215 LYS A N   1 
ATOM   1642 C CA  . LYS A 1 215 ? 5.57544  8.05942  -12.85817 1.000 61.48082  ? 215 LYS A CA  1 
ATOM   1643 C C   . LYS A 1 215 ? 5.11895  8.17823  -11.40799 1.000 56.94523  ? 215 LYS A C   1 
ATOM   1644 O O   . LYS A 1 215 ? 4.94703  9.29607  -10.91284 1.000 52.10293  ? 215 LYS A O   1 
ATOM   1645 C CB  . LYS A 1 215 ? 4.78814  9.03463  -13.73943 1.000 58.08220  ? 215 LYS A CB  1 
ATOM   1646 C CG  . LYS A 1 215 ? 5.07060  8.88544  -15.22177 1.000 61.02603  ? 215 LYS A CG  1 
ATOM   1647 C CD  . LYS A 1 215 ? 4.37715  9.96853  -16.03798 1.000 67.84864  ? 215 LYS A CD  1 
ATOM   1648 C CE  . LYS A 1 215 ? 4.65581  9.79519  -17.52576 1.000 77.93106  ? 215 LYS A CE  1 
ATOM   1649 N NZ  . LYS A 1 215 ? 6.11868  9.67863  -17.80967 1.000 73.13811  ? 215 LYS A NZ  1 
ATOM   1650 N N   . ASP A 1 216 ? 4.91214  7.06180  -10.71876 1.000 56.62661  ? 216 ASP A N   1 
ATOM   1651 C CA  . ASP A 1 216 ? 4.57180  7.06721  -9.30149  1.000 56.37847  ? 216 ASP A CA  1 
ATOM   1652 C C   . ASP A 1 216 ? 5.83259  6.84168  -8.47518  1.000 56.25475  ? 216 ASP A C   1 
ATOM   1653 O O   . ASP A 1 216 ? 6.60892  5.92212  -8.75655  1.000 56.84998  ? 216 ASP A O   1 
ATOM   1654 C CB  . ASP A 1 216 ? 3.53380  5.99098  -8.98547  1.000 61.17703  ? 216 ASP A CB  1 
ATOM   1655 C CG  . ASP A 1 216 ? 2.24820  6.17682  -9.75974  1.000 61.26601  ? 216 ASP A CG  1 
ATOM   1656 O OD1 . ASP A 1 216 ? 2.20078  7.08936  -10.61198 1.000 63.90636  ? 216 ASP A OD1 1 
ATOM   1657 O OD2 . ASP A 1 216 ? 1.28873  5.41205  -9.51203  1.000 61.49597  ? 216 ASP A OD2 1 
ATOM   1658 N N   . PHE A 1 217 ? 6.02972  7.67477  -7.45649  1.000 53.90104  ? 217 PHE A N   1 
ATOM   1659 C CA  . PHE A 1 217 ? 7.24166  7.63470  -6.65438  1.000 52.11691  ? 217 PHE A CA  1 
ATOM   1660 C C   . PHE A 1 217 ? 6.92083  7.89542  -5.19206  1.000 53.26182  ? 217 PHE A C   1 
ATOM   1661 O O   . PHE A 1 217 ? 6.15865  8.81008  -4.86425  1.000 54.55973  ? 217 PHE A O   1 
ATOM   1662 C CB  . PHE A 1 217 ? 8.26332  8.66856  -7.13439  1.000 49.82851  ? 217 PHE A CB  1 
ATOM   1663 C CG  . PHE A 1 217 ? 8.69183  8.47629  -8.55442  1.000 51.44665  ? 217 PHE A CG  1 
ATOM   1664 C CD1 . PHE A 1 217 ? 9.59744  7.48423  -8.88905  1.000 51.66621  ? 217 PHE A CD1 1 
ATOM   1665 C CD2 . PHE A 1 217 ? 8.19229  9.29005  -9.55644  1.000 52.67605  ? 217 PHE A CD2 1 
ATOM   1666 C CE1 . PHE A 1 217 ? 9.99685  7.30593  -10.19945 1.000 51.88503  ? 217 PHE A CE1 1 
ATOM   1667 C CE2 . PHE A 1 217 ? 8.58630  9.11796  -10.86839 1.000 53.86885  ? 217 PHE A CE2 1 
ATOM   1668 C CZ  . PHE A 1 217 ? 9.48927  8.12527  -11.19136 1.000 53.51057  ? 217 PHE A CZ  1 
ATOM   1669 N N   . GLN A 1 218 ? 7.51332  7.08928  -4.31718  1.000 52.35790  ? 218 GLN A N   1 
ATOM   1670 C CA  . GLN A 1 218 ? 7.43539  7.32131  -2.88075  1.000 46.73452  ? 218 GLN A CA  1 
ATOM   1671 C C   . GLN A 1 218 ? 8.52448  8.31858  -2.50700  1.000 42.94092  ? 218 GLN A C   1 
ATOM   1672 O O   . GLN A 1 218 ? 9.71040  7.97560  -2.49065  1.000 40.22891  ? 218 GLN A O   1 
ATOM   1673 C CB  . GLN A 1 218 ? 7.59497  6.00683  -2.12565  1.000 48.83411  ? 218 GLN A CB  1 
ATOM   1674 C CG  . GLN A 1 218 ? 7.16548  6.05777  -0.66639  1.000 52.73726  ? 218 GLN A CG  1 
ATOM   1675 C CD  . GLN A 1 218 ? 5.65897  5.98340  -0.49299  1.000 58.57969  ? 218 GLN A CD  1 
ATOM   1676 O OE1 . GLN A 1 218 ? 5.04921  6.85536  0.12790   1.000 57.41056  ? 218 GLN A OE1 1 
ATOM   1677 N NE2 . GLN A 1 218 ? 5.05096  4.93329  -1.03666  1.000 61.64560  ? 218 GLN A NE2 1 
ATOM   1678 N N   . ILE A 1 219 ? 8.13252  9.55989  -2.23293  1.000 47.11320  ? 219 ILE A N   1 
ATOM   1679 C CA  . ILE A 1 219 ? 9.07051  10.62944 -1.90219  1.000 46.14609  ? 219 ILE A CA  1 
ATOM   1680 C C   . ILE A 1 219 ? 8.98987  10.90263 -0.40773  1.000 47.99870  ? 219 ILE A C   1 
ATOM   1681 O O   . ILE A 1 219 ? 7.90199  11.14414 0.13127   1.000 49.66076  ? 219 ILE A O   1 
ATOM   1682 C CB  . ILE A 1 219 ? 8.77148  11.90897 -2.70025  1.000 46.72858  ? 219 ILE A CB  1 
ATOM   1683 C CG1 . ILE A 1 219 ? 8.83551  11.63767 -4.20356  1.000 43.03175  ? 219 ILE A CG1 1 
ATOM   1684 C CG2 . ILE A 1 219 ? 9.75431  13.00261 -2.32847  1.000 44.09625  ? 219 ILE A CG2 1 
ATOM   1685 C CD1 . ILE A 1 219 ? 8.46753  12.83086 -5.04267  1.000 38.61439  ? 219 ILE A CD1 1 
ATOM   1686 N N   . SER A 1 220 ? 10.13368 10.86741 0.26360   1.000 43.60667  ? 220 SER A N   1 
ATOM   1687 C CA  . SER A 1 220 ? 10.20254 11.13662 1.68945   1.000 43.13826  ? 220 SER A CA  1 
ATOM   1688 C C   . SER A 1 220 ? 11.00980 12.39935 1.93862   1.000 38.81208  ? 220 SER A C   1 
ATOM   1689 O O   . SER A 1 220 ? 12.03971 12.62467 1.29732   1.000 41.63535  ? 220 SER A O   1 
ATOM   1690 C CB  . SER A 1 220 ? 10.83885 9.97973  2.45224   1.000 38.93781  ? 220 SER A CB  1 
ATOM   1691 O OG  . SER A 1 220 ? 12.20989 10.25029 2.68347   1.000 41.94896  ? 220 SER A OG  1 
ATOM   1692 N N   . VAL A 1 221 ? 10.54369 13.21621 2.87788   1.000 44.33931  ? 221 VAL A N   1 
ATOM   1693 C CA  . VAL A 1 221 ? 11.26861 14.39819 3.33572   1.000 44.36644  ? 221 VAL A CA  1 
ATOM   1694 C C   . VAL A 1 221 ? 11.40217 14.25404 4.84521   1.000 43.01383  ? 221 VAL A C   1 
ATOM   1695 O O   . VAL A 1 221 ? 10.45281 14.52519 5.58644   1.000 45.79824  ? 221 VAL A O   1 
ATOM   1696 C CB  . VAL A 1 221 ? 10.56834 15.70651 2.95847   1.000 41.93995  ? 221 VAL A CB  1 
ATOM   1697 C CG1 . VAL A 1 221 ? 11.33521 16.89531 3.50670   1.000 38.08271  ? 221 VAL A CG1 1 
ATOM   1698 C CG2 . VAL A 1 221 ? 10.43600 15.81807 1.44348   1.000 45.34728  ? 221 VAL A CG2 1 
ATOM   1699 N N   . ASP A 1 222 ? 12.57487 13.81824 5.30014   1.000 42.41206  ? 222 ASP A N   1 
ATOM   1700 C CA  . ASP A 1 222 ? 12.84771 13.51705 6.71589   1.000 48.76013  ? 222 ASP A CA  1 
ATOM   1701 C C   . ASP A 1 222 ? 11.94380 12.34906 7.10873   1.000 52.04931  ? 222 ASP A C   1 
ATOM   1702 O O   . ASP A 1 222 ? 11.96143 11.30469 6.43853   1.000 54.46523  ? 222 ASP A O   1 
ATOM   1703 C CB  . ASP A 1 222 ? 12.70332 14.78276 7.55415   1.000 40.26522  ? 222 ASP A CB  1 
ATOM   1704 C CG  . ASP A 1 222 ? 13.65254 15.87870 7.10539   1.000 36.71126  ? 222 ASP A CG  1 
ATOM   1705 O OD1 . ASP A 1 222 ? 14.74279 15.55643 6.58821   1.000 35.91546  ? 222 ASP A OD1 1 
ATOM   1706 O OD2 . ASP A 1 222 ? 13.31793 17.06721 7.26049   1.000 35.08701  ? 222 ASP A OD2 1 
ATOM   1707 N N   . HIS A 1 223 ? 11.14640 12.45993 8.16227   1.000 55.79901  ? 223 HIS A N   1 
ATOM   1708 C CA  . HIS A 1 223 ? 10.30236 11.34630 8.57495   1.000 68.59475  ? 223 HIS A CA  1 
ATOM   1709 C C   . HIS A 1 223 ? 9.04877  11.19568 7.72269   1.000 68.49501  ? 223 HIS A C   1 
ATOM   1710 O O   . HIS A 1 223 ? 8.38663  10.15517 7.79859   1.000 74.64100  ? 223 HIS A O   1 
ATOM   1711 C CB  . HIS A 1 223 ? 9.90276  11.51113 10.04637  1.000 70.74553  ? 223 HIS A CB  1 
ATOM   1712 C CG  . HIS A 1 223 ? 9.23351  12.81522 10.35697  0.800 73.81878  ? 223 HIS A CG  1 
ATOM   1713 N ND1 . HIS A 1 223 ? 9.82370  14.03532 10.10320  0.800 68.67794  ? 223 HIS A ND1 1 
ATOM   1714 C CD2 . HIS A 1 223 ? 8.02819  13.08871 10.90994  0.800 70.45835  ? 223 HIS A CD2 1 
ATOM   1715 C CE1 . HIS A 1 223 ? 9.00828  15.00374 10.47744  0.800 64.02776  ? 223 HIS A CE1 1 
ATOM   1716 N NE2 . HIS A 1 223 ? 7.91256  14.45638 10.97248  0.800 68.65837  ? 223 HIS A NE2 1 
ATOM   1717 N N   . LEU A 1 224 ? 8.72053  12.19070 6.90633   1.000 56.82352  ? 224 LEU A N   1 
ATOM   1718 C CA  . LEU A 1 224 ? 7.44718  12.24670 6.20487   1.000 51.35761  ? 224 LEU A CA  1 
ATOM   1719 C C   . LEU A 1 224 ? 7.61112  11.66170 4.80512   1.000 56.31166  ? 224 LEU A C   1 
ATOM   1720 O O   . LEU A 1 224 ? 8.46487  12.11214 4.03543   1.000 51.92922  ? 224 LEU A O   1 
ATOM   1721 C CB  . LEU A 1 224 ? 6.96036  13.69488 6.16335   1.000 49.64035  ? 224 LEU A CB  1 
ATOM   1722 C CG  . LEU A 1 224 ? 5.71358  14.14828 5.39709   1.000 57.67518  ? 224 LEU A CG  1 
ATOM   1723 C CD1 . LEU A 1 224 ? 6.04312  14.48070 3.93890   1.000 59.02462  ? 224 LEU A CD1 1 
ATOM   1724 C CD2 . LEU A 1 224 ? 4.58135  13.12796 5.49532   1.000 59.93017  ? 224 LEU A CD2 1 
ATOM   1725 N N   . SER A 1 225 ? 6.78833  10.66559 4.47800   1.000 52.77557  ? 225 SER A N   1 
ATOM   1726 C CA  . SER A 1 225 ? 6.82324  9.98319  3.19107   1.000 53.53981  ? 225 SER A CA  1 
ATOM   1727 C C   . SER A 1 225 ? 5.44980  10.06381 2.54165   1.000 52.59522  ? 225 SER A C   1 
ATOM   1728 O O   . SER A 1 225 ? 4.43371  9.80441  3.19516   1.000 58.47883  ? 225 SER A O   1 
ATOM   1729 C CB  . SER A 1 225 ? 7.24783  8.52075  3.35840   1.000 58.10708  ? 225 SER A CB  1 
ATOM   1730 O OG  . SER A 1 225 ? 7.33367  7.86308  2.10588   1.000 58.40684  ? 225 SER A OG  1 
ATOM   1731 N N   . ILE A 1 226 ? 5.42113  10.41364 1.25748   1.000 52.16944  ? 226 ILE A N   1 
ATOM   1732 C CA  . ILE A 1 226 ? 4.17403  10.62338 0.52692   1.000 56.76576  ? 226 ILE A CA  1 
ATOM   1733 C C   . ILE A 1 226 ? 4.28130  9.97447  -0.84574  1.000 53.57264  ? 226 ILE A C   1 
ATOM   1734 O O   . ILE A 1 226 ? 5.29572  10.12997 -1.53335  1.000 55.01446  ? 226 ILE A O   1 
ATOM   1735 C CB  . ILE A 1 226 ? 3.84483  12.12319 0.38040   1.000 60.21848  ? 226 ILE A CB  1 
ATOM   1736 C CG1 . ILE A 1 226 ? 3.56856  12.75461 1.74562   1.000 63.68643  ? 226 ILE A CG1 1 
ATOM   1737 C CG2 . ILE A 1 226 ? 2.65314  12.32528 -0.54285  1.000 65.63157  ? 226 ILE A CG2 1 
ATOM   1738 C CD1 . ILE A 1 226 ? 3.08568  14.18638 1.66450   1.000 69.75966  ? 226 ILE A CD1 1 
ATOM   1739 N N   . LEU A 1 227 ? 3.23615  9.25356  -1.24719  1.000 57.25060  ? 227 LEU A N   1 
ATOM   1740 C CA  . LEU A 1 227 ? 3.14725  8.73367  -2.60652  1.000 59.77167  ? 227 LEU A CA  1 
ATOM   1741 C C   . LEU A 1 227 ? 2.72377  9.85143  -3.55061  1.000 60.15752  ? 227 LEU A C   1 
ATOM   1742 O O   . LEU A 1 227 ? 1.65702  10.44877 -3.37513  1.000 71.56827  ? 227 LEU A O   1 
ATOM   1743 C CB  . LEU A 1 227 ? 2.15367  7.57788  -2.68663  1.000 59.83104  ? 227 LEU A CB  1 
ATOM   1744 C CG  . LEU A 1 227 ? 1.82818  7.13459  -4.11592  1.000 57.59647  ? 227 LEU A CG  1 
ATOM   1745 C CD1 . LEU A 1 227 ? 3.00262  6.39172  -4.73342  1.000 59.76127  ? 227 LEU A CD1 1 
ATOM   1746 C CD2 . LEU A 1 227 ? 0.57301  6.28423  -4.14591  1.000 60.91038  ? 227 LEU A CD2 1 
ATOM   1747 N N   . HIS A 1 228 ? 3.55009  10.13205 -4.55097  1.000 55.42755  ? 228 HIS A N   1 
ATOM   1748 C CA  . HIS A 1 228 ? 3.26127  11.16000 -5.54005  1.000 57.74990  ? 228 HIS A CA  1 
ATOM   1749 C C   . HIS A 1 228 ? 2.96922  10.49579 -6.87815  1.000 55.59652  ? 228 HIS A C   1 
ATOM   1750 O O   . HIS A 1 228 ? 3.79309  9.72977  -7.38690  1.000 55.81423  ? 228 HIS A O   1 
ATOM   1751 C CB  . HIS A 1 228 ? 4.42452  12.14169 -5.65738  1.000 55.01497  ? 228 HIS A CB  1 
ATOM   1752 C CG  . HIS A 1 228 ? 4.57611  13.03460 -4.46666  1.000 58.33035  ? 228 HIS A CG  1 
ATOM   1753 N ND1 . HIS A 1 228 ? 4.32574  14.38859 -4.51627  1.000 58.95764  ? 228 HIS A ND1 1 
ATOM   1754 C CD2 . HIS A 1 228 ? 4.93654  12.76515 -3.18920  1.000 58.76339  ? 228 HIS A CD2 1 
ATOM   1755 C CE1 . HIS A 1 228 ? 4.53200  14.91596 -3.32258  1.000 63.93214  ? 228 HIS A CE1 1 
ATOM   1756 N NE2 . HIS A 1 228 ? 4.90237  13.95224 -2.49866  1.000 60.52277  ? 228 HIS A NE2 1 
ATOM   1757 N N   . ARG A 1 229 ? 1.80168  10.79088 -7.44014  1.000 55.67059  ? 229 ARG A N   1 
ATOM   1758 C CA  . ARG A 1 229 ? 1.36605  10.21511 -8.70078  1.000 52.73550  ? 229 ARG A CA  1 
ATOM   1759 C C   . ARG A 1 229 ? 1.53134  11.21343 -9.83868  1.000 57.19247  ? 229 ARG A C   1 
ATOM   1760 O O   . ARG A 1 229 ? 1.55077  12.43061 -9.63556  1.000 54.19199  ? 229 ARG A O   1 
ATOM   1761 C CB  . ARG A 1 229 ? -0.09097 9.76289  -8.61690  1.000 50.16567  ? 229 ARG A CB  1 
ATOM   1762 C CG  . ARG A 1 229 ? -0.31066 8.52354  -7.77809  0.800 52.63156  ? 229 ARG A CG  1 
ATOM   1763 C CD  . ARG A 1 229 ? -1.71626 7.99787  -7.98217  0.700 57.34317  ? 229 ARG A CD  1 
ATOM   1764 N NE  . ARG A 1 229 ? -2.33341 7.61791  -6.71905  0.600 55.34184  ? 229 ARG A NE  1 
ATOM   1765 C CZ  . ARG A 1 229 ? -2.21153 6.42447  -6.15697  0.600 53.75818  ? 229 ARG A CZ  1 
ATOM   1766 N NH1 . ARG A 1 229 ? -1.49531 5.46497  -6.72094  0.600 51.09225  ? 229 ARG A NH1 1 
ATOM   1767 N NH2 . ARG A 1 229 ? -2.82222 6.18874  -4.99912  0.600 55.84525  ? 229 ARG A NH2 1 
ATOM   1768 N N   . ASP A 1 230 ? 1.62735  10.66776 -11.04746 1.000 55.60194  ? 230 ASP A N   1 
ATOM   1769 C CA  . ASP A 1 230 ? 1.87647  11.42155 -12.27395 1.000 55.26042  ? 230 ASP A CA  1 
ATOM   1770 C C   . ASP A 1 230 ? 2.94612  12.49502 -12.06365 1.000 58.38817  ? 230 ASP A C   1 
ATOM   1771 O O   . ASP A 1 230 ? 2.73225  13.68744 -12.28909 1.000 60.65350  ? 230 ASP A O   1 
ATOM   1772 C CB  . ASP A 1 230 ? 0.59043  12.03103 -12.81604 1.000 52.43044  ? 230 ASP A CB  1 
ATOM   1773 C CG  . ASP A 1 230 ? 0.47254  11.86936 -14.31242 0.700 59.03104  ? 230 ASP A CG  1 
ATOM   1774 O OD1 . ASP A 1 230 ? -0.05388 10.82870 -14.75477 0.700 63.78734  ? 230 ASP A OD1 1 
ATOM   1775 O OD2 . ASP A 1 230 ? 0.93639  12.76388 -15.04790 0.700 61.52953  ? 230 ASP A OD2 1 
ATOM   1776 N N   . VAL A 1 231 ? 4.11413  12.03639 -11.61679 1.000 58.87251  ? 231 VAL A N   1 
ATOM   1777 C CA  . VAL A 1 231 ? 5.26300  12.90835 -11.40509 1.000 53.39727  ? 231 VAL A CA  1 
ATOM   1778 C C   . VAL A 1 231 ? 5.90673  13.21384 -12.74835 1.000 53.18702  ? 231 VAL A C   1 
ATOM   1779 O O   . VAL A 1 231 ? 6.20982  12.30327 -13.52677 1.000 53.47903  ? 231 VAL A O   1 
ATOM   1780 C CB  . VAL A 1 231 ? 6.27032  12.25678 -10.44395 1.000 50.68423  ? 231 VAL A CB  1 
ATOM   1781 C CG1 . VAL A 1 231 ? 7.63647  12.89043 -10.59128 1.000 45.20395  ? 231 VAL A CG1 1 
ATOM   1782 C CG2 . VAL A 1 231 ? 5.78322  12.37474 -9.01533  1.000 53.49716  ? 231 VAL A CG2 1 
ATOM   1783 N N   . GLN A 1 232 ? 6.10917  14.49926 -13.02973 1.000 51.23354  ? 232 GLN A N   1 
ATOM   1784 C CA  . GLN A 1 232 ? 6.83978  14.90681 -14.22280 1.000 51.39503  ? 232 GLN A CA  1 
ATOM   1785 C C   . GLN A 1 232 ? 8.29887  15.22008 -13.94197 1.000 48.23592  ? 232 GLN A C   1 
ATOM   1786 O O   . GLN A 1 232 ? 9.13366  15.09159 -14.84641 1.000 43.31228  ? 232 GLN A O   1 
ATOM   1787 C CB  . GLN A 1 232 ? 6.18284  16.13054 -14.87072 1.000 52.72027  ? 232 GLN A CB  1 
ATOM   1788 N N   . GLU A 1 233 ? 8.62288  15.60776 -12.70903 1.000 48.05152  ? 233 GLU A N   1 
ATOM   1789 C CA  . GLU A 1 233 ? 9.96583  16.05571 -12.37850 1.000 42.31371  ? 233 GLU A CA  1 
ATOM   1790 C C   . GLU A 1 233 ? 10.09461 16.22708 -10.87548 1.000 42.70887  ? 233 GLU A C   1 
ATOM   1791 O O   . GLU A 1 233 ? 9.19050  16.75656 -10.22721 1.000 44.41997  ? 233 GLU A O   1 
ATOM   1792 C CB  . GLU A 1 233 ? 10.28666 17.38140 -13.07601 1.000 45.99495  ? 233 GLU A CB  1 
ATOM   1793 C CG  . GLU A 1 233 ? 11.65501 17.93093 -12.75192 1.000 46.57017  ? 233 GLU A CG  1 
ATOM   1794 C CD  . GLU A 1 233 ? 11.99448 19.13035 -13.59794 1.000 45.63981  ? 233 GLU A CD  1 
ATOM   1795 O OE1 . GLU A 1 233 ? 11.07734 19.65532 -14.25781 1.000 58.42694  ? 233 GLU A OE1 1 
ATOM   1796 O OE2 . GLU A 1 233 ? 13.17201 19.54140 -13.61689 1.000 44.78527  ? 233 GLU A OE2 1 
ATOM   1797 N N   . ILE A 1 234 ? 11.22259 15.77502 -10.33729 1.000 44.26993  ? 234 ILE A N   1 
ATOM   1798 C CA  . ILE A 1 234 ? 11.66146 16.10140 -8.98696  1.000 40.08552  ? 234 ILE A CA  1 
ATOM   1799 C C   . ILE A 1 234 ? 12.93547 16.92531 -9.11057  1.000 39.28054  ? 234 ILE A C   1 
ATOM   1800 O O   . ILE A 1 234 ? 13.89589 16.49223 -9.75803  1.000 41.01609  ? 234 ILE A O   1 
ATOM   1801 C CB  . ILE A 1 234 ? 11.90862 14.83418 -8.15059  1.000 38.23663  ? 234 ILE A CB  1 
ATOM   1802 C CG1 . ILE A 1 234 ? 10.75869 13.84124 -8.31270  1.000 32.46136  ? 234 ILE A CG1 1 
ATOM   1803 C CG2 . ILE A 1 234 ? 12.10172 15.19212 -6.68856  1.000 40.79988  ? 234 ILE A CG2 1 
ATOM   1804 C CD1 . ILE A 1 234 ? 11.06751 12.48256 -7.74230  1.000 33.73076  ? 234 ILE A CD1 1 
ATOM   1805 N N   . ARG A 1 235 ? 12.94764 18.10919 -8.50349  1.000 37.50234  ? 235 ARG A N   1 
ATOM   1806 C CA  . ARG A 1 235 ? 14.09260 19.00885 -8.57757  1.000 39.83290  ? 235 ARG A CA  1 
ATOM   1807 C C   . ARG A 1 235 ? 14.70716 19.21215 -7.20097  1.000 39.95053  ? 235 ARG A C   1 
ATOM   1808 O O   . ARG A 1 235 ? 13.99774 19.51608 -6.23712  1.000 40.33766  ? 235 ARG A O   1 
ATOM   1809 C CB  . ARG A 1 235 ? 13.70287 20.36344 -9.16003  1.000 41.48711  ? 235 ARG A CB  1 
ATOM   1810 C CG  . ARG A 1 235 ? 13.26462 20.31378 -10.60092 1.000 48.62522  ? 235 ARG A CG  1 
ATOM   1811 C CD  . ARG A 1 235 ? 13.53509 21.64259 -11.27694 1.000 56.47359  ? 235 ARG A CD  1 
ATOM   1812 N NE  . ARG A 1 235 ? 13.50959 22.74169 -10.31877 0.800 56.08124  ? 235 ARG A NE  1 
ATOM   1813 C CZ  . ARG A 1 235 ? 13.94112 23.96793 -10.57727 0.800 59.22672  ? 235 ARG A CZ  1 
ATOM   1814 N NH1 . ARG A 1 235 ? 14.43601 24.29043 -11.76217 0.700 58.32209  ? 235 ARG A NH1 1 
ATOM   1815 N NH2 . ARG A 1 235 ? 13.88005 24.89155 -9.62215  0.700 52.34009  ? 235 ARG A NH2 1 
ATOM   1816 N N   . TYR A 1 236 ? 16.02864 19.07859 -7.12751  1.000 39.38234  ? 236 TYR A N   1 
ATOM   1817 C CA  . TYR A 1 236 ? 16.79385 19.26550 -5.90249  1.000 38.58132  ? 236 TYR A CA  1 
ATOM   1818 C C   . TYR A 1 236 ? 17.71333 20.47121 -6.04626  1.000 40.54296  ? 236 TYR A C   1 
ATOM   1819 O O   . TYR A 1 236 ? 18.40901 20.61057 -7.05846  1.000 40.02455  ? 236 TYR A O   1 
ATOM   1820 C CB  . TYR A 1 236 ? 17.62060 18.01696 -5.58210  1.000 31.79820  ? 236 TYR A CB  1 
ATOM   1821 C CG  . TYR A 1 236 ? 16.79247 16.83264 -5.14977  1.000 34.01405  ? 236 TYR A CG  1 
ATOM   1822 C CD1 . TYR A 1 236 ? 15.98444 16.91003 -4.02376  1.000 35.83800  ? 236 TYR A CD1 1 
ATOM   1823 C CD2 . TYR A 1 236 ? 16.82174 15.63500 -5.85701  1.000 33.36197  ? 236 TYR A CD2 1 
ATOM   1824 C CE1 . TYR A 1 236 ? 15.22527 15.84085 -3.61644  1.000 36.14708  ? 236 TYR A CE1 1 
ATOM   1825 C CE2 . TYR A 1 236 ? 16.05796 14.54857 -5.45360  1.000 33.64899  ? 236 TYR A CE2 1 
ATOM   1826 C CZ  . TYR A 1 236 ? 15.26279 14.66296 -4.32769  1.000 39.84401  ? 236 TYR A CZ  1 
ATOM   1827 O OH  . TYR A 1 236 ? 14.49051 13.60882 -3.89425  1.000 40.05073  ? 236 TYR A OH  1 
ATOM   1828 N N   . GLU A 1 237 ? 17.71828 21.33442 -5.03498  1.000 38.86629  ? 237 GLU A N   1 
ATOM   1829 C CA  . GLU A 1 237 ? 18.67944 22.42607 -4.97635  1.000 40.34847  ? 237 GLU A CA  1 
ATOM   1830 C C   . GLU A 1 237 ? 18.80681 22.88343 -3.53158  1.000 38.23194  ? 237 GLU A C   1 
ATOM   1831 O O   . GLU A 1 237 ? 17.89751 22.69478 -2.71949  1.000 40.30755  ? 237 GLU A O   1 
ATOM   1832 C CB  . GLU A 1 237 ? 18.28011 23.58986 -5.89073  1.000 37.19649  ? 237 GLU A CB  1 
ATOM   1833 C CG  . GLU A 1 237 ? 16.86023 24.10431 -5.70592  1.000 45.47375  ? 237 GLU A CG  1 
ATOM   1834 C CD  . GLU A 1 237 ? 16.43891 25.06059 -6.81841  1.000 52.41777  ? 237 GLU A CD  1 
ATOM   1835 O OE1 . GLU A 1 237 ? 17.22974 25.96735 -7.16595  1.000 47.47479  ? 237 GLU A OE1 1 
ATOM   1836 O OE2 . GLU A 1 237 ? 15.32170 24.89453 -7.35464  1.000 49.22790  ? 237 GLU A OE2 1 
ATOM   1837 N N   . VAL A 1 238 ? 19.95795 23.47763 -3.21825  1.000 36.92034  ? 238 VAL A N   1 
ATOM   1838 C CA  . VAL A 1 238 ? 20.18369 23.99987 -1.87733  1.000 39.73399  ? 238 VAL A CA  1 
ATOM   1839 C C   . VAL A 1 238 ? 19.26288 25.18974 -1.64665  1.000 41.68161  ? 238 VAL A C   1 
ATOM   1840 O O   . VAL A 1 238 ? 19.22291 26.13094 -2.45063  1.000 46.27677  ? 238 VAL A O   1 
ATOM   1841 C CB  . VAL A 1 238 ? 21.66107 24.37373 -1.68336  1.000 33.60242  ? 238 VAL A CB  1 
ATOM   1842 C CG1 . VAL A 1 238 ? 21.86333 25.07256 -0.35183  1.000 39.32826  ? 238 VAL A CG1 1 
ATOM   1843 C CG2 . VAL A 1 238 ? 22.52602 23.13548 -1.76129  1.000 29.78475  ? 238 VAL A CG2 1 
ATOM   1844 N N   . SER A 1 239 ? 18.51274 25.14663 -0.54822  1.000 38.27566  ? 239 SER A N   1 
ATOM   1845 C CA  . SER A 1 239 ? 17.52461 26.17549 -0.25058  1.000 37.85167  ? 239 SER A CA  1 
ATOM   1846 C C   . SER A 1 239 ? 18.18112 27.52927 -0.00277  1.000 38.01091  ? 239 SER A C   1 
ATOM   1847 O O   . SER A 1 239 ? 19.33299 27.61790 0.42866   1.000 40.68166  ? 239 SER A O   1 
ATOM   1848 C CB  . SER A 1 239 ? 16.70213 25.77801 0.97825   1.000 39.88377  ? 239 SER A CB  1 
ATOM   1849 O OG  . SER A 1 239 ? 15.93179 26.86986 1.46000   1.000 39.94542  ? 239 SER A OG  1 
ATOM   1850 N N   . ALA A 1 240 ? 17.42847 28.59431 -0.28810  1.000 39.87125  ? 240 ALA A N   1 
ATOM   1851 C CA  . ALA A 1 240 ? 17.84367 29.92320 0.12975   1.000 39.81285  ? 240 ALA A CA  1 
ATOM   1852 C C   . ALA A 1 240 ? 17.63367 30.13197 1.62064   1.000 45.34955  ? 240 ALA A C   1 
ATOM   1853 O O   . ALA A 1 240 ? 18.31676 30.96943 2.22071   1.000 46.80046  ? 240 ALA A O   1 
ATOM   1854 C CB  . ALA A 1 240 ? 17.07876 30.98834 -0.66366  1.000 36.97035  ? 240 ALA A CB  1 
ATOM   1855 N N   . LYS A 1 241 ? 16.70919 29.38608 2.22245   1.000 45.90782  ? 241 LYS A N   1 
ATOM   1856 C CA  . LYS A 1 241 ? 16.41924 29.46791 3.64417   1.000 44.31012  ? 241 LYS A CA  1 
ATOM   1857 C C   . LYS A 1 241 ? 17.41334 28.63027 4.44563   1.000 40.90104  ? 241 LYS A C   1 
ATOM   1858 O O   . LYS A 1 241 ? 18.04128 27.70317 3.93000   1.000 41.52252  ? 241 LYS A O   1 
ATOM   1859 C CB  . LYS A 1 241 ? 14.99083 28.99285 3.91760   1.000 47.05091  ? 241 LYS A CB  1 
ATOM   1860 C CG  . LYS A 1 241 ? 13.92579 29.70904 3.09236   1.000 47.41978  ? 241 LYS A CG  1 
ATOM   1861 C CD  . LYS A 1 241 ? 12.63558 28.90265 3.00942   1.000 56.92046  ? 241 LYS A CD  1 
ATOM   1862 C CE  . LYS A 1 241 ? 11.59129 29.60094 2.14297   1.000 57.82694  ? 241 LYS A CE  1 
ATOM   1863 N NZ  . LYS A 1 241 ? 10.45460 28.69629 1.79660   1.000 54.00912  ? 241 LYS A NZ  1 
ATOM   1864 N N   . LYS A 1 242 ? 17.55013 28.96923 5.72804   1.000 43.69972  ? 242 LYS A N   1 
ATOM   1865 C CA  . LYS A 1 242 ? 18.44408 28.25673 6.62899   1.000 37.36693  ? 242 LYS A CA  1 
ATOM   1866 C C   . LYS A 1 242 ? 17.79042 28.11597 7.99515   1.000 42.92208  ? 242 LYS A C   1 
ATOM   1867 O O   . LYS A 1 242 ? 17.01582 28.97495 8.42289   1.000 44.46159  ? 242 LYS A O   1 
ATOM   1868 C CB  . LYS A 1 242 ? 19.79823 28.96881 6.78587   1.000 41.60645  ? 242 LYS A CB  1 
ATOM   1869 C CG  . LYS A 1 242 ? 20.56975 29.16091 5.48846   1.000 46.08766  ? 242 LYS A CG  1 
ATOM   1870 C CD  . LYS A 1 242 ? 22.01217 29.59270 5.73871   1.000 51.34549  ? 242 LYS A CD  1 
ATOM   1871 C CE  . LYS A 1 242 ? 22.92180 28.39311 5.99443   1.000 46.90894  ? 242 LYS A CE  1 
ATOM   1872 N NZ  . LYS A 1 242 ? 24.35531 28.78326 6.15860   1.000 49.69962  ? 242 LYS A NZ  1 
ATOM   1873 N N   . ILE A 1 243 ? 18.10687 27.02033 8.67626   1.000 46.12562  ? 243 ILE A N   1 
ATOM   1874 C CA  . ILE A 1 243 ? 17.70138 26.82877 10.06391  1.000 43.31547  ? 243 ILE A CA  1 
ATOM   1875 C C   . ILE A 1 243 ? 18.74637 27.48124 10.95417  1.000 43.16317  ? 243 ILE A C   1 
ATOM   1876 O O   . ILE A 1 243 ? 19.94682 27.44175 10.66002  1.000 40.19641  ? 243 ILE A O   1 
ATOM   1877 C CB  . ILE A 1 243 ? 17.52692 25.33359 10.39790  1.000 40.71004  ? 243 ILE A CB  1 
ATOM   1878 C CG1 . ILE A 1 243 ? 16.95404 25.16480 11.80723  1.000 41.45726  ? 243 ILE A CG1 1 
ATOM   1879 C CG2 . ILE A 1 243 ? 18.84320 24.58604 10.27115  1.000 36.77273  ? 243 ILE A CG2 1 
ATOM   1880 C CD1 . ILE A 1 243 ? 16.77944 23.72058 12.23247  1.000 37.03901  ? 243 ILE A CD1 1 
ATOM   1881 N N   . HIS A 1 244 ? 18.29163 28.11195 12.03079  1.000 45.00587  ? 244 HIS A N   1 
ATOM   1882 C CA  . HIS A 1 244 ? 19.16996 28.80556 12.95864  1.000 43.70944  ? 244 HIS A CA  1 
ATOM   1883 C C   . HIS A 1 244 ? 19.12529 28.10463 14.30288  1.000 39.36808  ? 244 HIS A C   1 
ATOM   1884 O O   . HIS A 1 244 ? 18.04101 27.81194 14.81733  1.000 42.01415  ? 244 HIS A O   1 
ATOM   1885 C CB  . HIS A 1 244 ? 18.76149 30.27062 13.10719  1.000 44.41354  ? 244 HIS A CB  1 
ATOM   1886 C CG  . HIS A 1 244 ? 18.62102 30.98820 11.80056  1.000 49.45792  ? 244 HIS A CG  1 
ATOM   1887 N ND1 . HIS A 1 244 ? 19.69669 31.52552 11.12611  1.000 50.21368  ? 244 HIS A ND1 1 
ATOM   1888 C CD2 . HIS A 1 244 ? 17.53102 31.25119 11.04027  1.000 53.56331  ? 244 HIS A CD2 1 
ATOM   1889 C CE1 . HIS A 1 244 ? 19.27466 32.09305 10.00983  1.000 55.30848  ? 244 HIS A CE1 1 
ATOM   1890 N NE2 . HIS A 1 244 ? 17.96467 31.94003 9.93320   1.000 54.51110  ? 244 HIS A NE2 1 
ATOM   1891 N N   . PHE A 1 245 ? 20.29960 27.83620 14.86301  1.000 44.89006  ? 245 PHE A N   1 
ATOM   1892 C CA  . PHE A 1 245 ? 20.43071 27.22363 16.17890  1.000 47.43733  ? 245 PHE A CA  1 
ATOM   1893 C C   . PHE A 1 245 ? 20.90411 28.26100 17.18737  1.000 48.52592  ? 245 PHE A C   1 
ATOM   1894 O O   . PHE A 1 245 ? 21.83519 29.02405 16.91076  1.000 49.25632  ? 245 PHE A O   1 
ATOM   1895 C CB  . PHE A 1 245 ? 21.42366 26.05991 16.15366  1.000 43.77833  ? 245 PHE A CB  1 
ATOM   1896 C CG  . PHE A 1 245 ? 20.95283 24.87319 15.37779  1.000 44.51014  ? 245 PHE A CG  1 
ATOM   1897 C CD1 . PHE A 1 245 ? 21.19790 24.77491 14.01634  1.000 43.30477  ? 245 PHE A CD1 1 
ATOM   1898 C CD2 . PHE A 1 245 ? 20.28051 23.84402 16.01107  1.000 40.25815  ? 245 PHE A CD2 1 
ATOM   1899 C CE1 . PHE A 1 245 ? 20.76977 23.67508 13.30198  1.000 39.01553  ? 245 PHE A CE1 1 
ATOM   1900 C CE2 . PHE A 1 245 ? 19.85116 22.74248 15.30192  1.000 43.80633  ? 245 PHE A CE2 1 
ATOM   1901 C CZ  . PHE A 1 245 ? 20.09476 22.65796 13.94490  1.000 39.88693  ? 245 PHE A CZ  1 
ATOM   1902 N N   . ALA A 1 246 ? 20.27650 28.28145 18.35693  1.000 49.84175  ? 246 ALA A N   1 
ATOM   1903 C CA  . ALA A 1 246 ? 20.80209 29.06108 19.46857  1.000 55.47780  ? 246 ALA A CA  1 
ATOM   1904 C C   . ALA A 1 246 ? 21.91743 28.25437 20.11956  1.000 58.30939  ? 246 ALA A C   1 
ATOM   1905 O O   . ALA A 1 246 ? 21.67250 27.17526 20.66865  1.000 61.38214  ? 246 ALA A O   1 
ATOM   1906 C CB  . ALA A 1 246 ? 19.70032 29.39636 20.46799  1.000 58.70037  ? 246 ALA A CB  1 
ATOM   1907 N N   . ARG A 1 247 ? 23.14514 28.75379 20.03243  1.000 63.08860  ? 247 ARG A N   1 
ATOM   1908 C CA  . ARG A 1 247 ? 24.28713 28.11220 20.66484  1.000 72.18533  ? 247 ARG A CA  1 
ATOM   1909 C C   . ARG A 1 247 ? 24.65785 28.87108 21.92909  1.000 71.71193  ? 247 ARG A C   1 
ATOM   1910 O O   . ARG A 1 247 ? 24.58571 30.10305 21.97174  1.000 75.45362  ? 247 ARG A O   1 
ATOM   1911 C CB  . ARG A 1 247 ? 25.49297 28.04784 19.72207  1.000 70.03657  ? 247 ARG A CB  1 
ATOM   1912 C CG  . ARG A 1 247 ? 26.03565 29.40434 19.29497  1.000 78.17032  ? 247 ARG A CG  1 
ATOM   1913 C CD  . ARG A 1 247 ? 27.53963 29.35619 19.02729  1.000 87.01843  ? 247 ARG A CD  1 
ATOM   1914 N NE  . ARG A 1 247 ? 28.32071 29.28699 20.25890  1.000 91.11023  ? 247 ARG A NE  1 
ATOM   1915 C CZ  . ARG A 1 247 ? 29.64469 29.21431 20.30622  1.000 81.50886  ? 247 ARG A CZ  1 
ATOM   1916 N NH1 . ARG A 1 247 ? 30.37499 29.18427 19.20355  1.000 79.74800  ? 247 ARG A NH1 1 
ATOM   1917 N NH2 . ARG A 1 247 ? 30.25108 29.17115 21.48967  1.000 78.55891  ? 247 ARG A NH2 1 
ATOM   1918 N N   . PHE A 1 248 ? 25.04088 28.12809 22.96357  1.000 71.78607  ? 248 PHE A N   1 
ATOM   1919 C CA  . PHE A 1 248 ? 25.47216 28.72516 24.21767  1.000 68.42543  ? 248 PHE A CA  1 
ATOM   1920 C C   . PHE A 1 248 ? 26.87229 28.29920 24.62547  1.000 67.01479  ? 248 PHE A C   1 
ATOM   1921 O O   . PHE A 1 248 ? 27.36430 28.75642 25.66277  1.000 72.70880  ? 248 PHE A O   1 
ATOM   1922 C CB  . PHE A 1 248 ? 24.47421 28.39322 25.33630  1.000 71.56251  ? 248 PHE A CB  1 
ATOM   1923 C CG  . PHE A 1 248 ? 23.18365 29.15812 25.23296  1.000 77.59804  ? 248 PHE A CG  1 
ATOM   1924 C CD1 . PHE A 1 248 ? 23.10360 30.46384 25.69217  1.000 72.59625  ? 248 PHE A CD1 1 
ATOM   1925 C CD2 . PHE A 1 248 ? 22.05662 28.58077 24.66348  1.000 70.94306  ? 248 PHE A CD2 1 
ATOM   1926 C CE1 . PHE A 1 248 ? 21.92479 31.17881 25.59317  1.000 72.57659  ? 248 PHE A CE1 1 
ATOM   1927 C CE2 . PHE A 1 248 ? 20.87219 29.29066 24.56397  1.000 66.92798  ? 248 PHE A CE2 1 
ATOM   1928 C CZ  . PHE A 1 248 ? 20.80733 30.59225 25.03006  1.000 68.30226  ? 248 PHE A CZ  1 
ATOM   1929 N N   . ARG A 1 249 ? 27.52645 27.45108 23.83885  1.000 67.92022  ? 249 ARG A N   1 
ATOM   1930 C CA  . ARG A 1 249 ? 28.89370 27.01495 24.09341  1.000 68.30919  ? 249 ARG A CA  1 
ATOM   1931 C C   . ARG A 1 249 ? 29.37226 26.25538 22.86453  1.000 66.27238  ? 249 ARG A C   1 
ATOM   1932 O O   . ARG A 1 249 ? 28.58998 25.92549 21.96950  1.000 63.04869  ? 249 ARG A O   1 
ATOM   1933 C CB  . ARG A 1 249 ? 28.99546 26.14578 25.35033  1.000 62.72852  ? 249 ARG A CB  1 
ATOM   1934 C CG  . ARG A 1 249 ? 27.95053 25.05190 25.41854  1.000 67.89111  ? 249 ARG A CG  1 
ATOM   1935 C CD  . ARG A 1 249 ? 28.15094 24.15369 26.62759  0.800 66.79864  ? 249 ARG A CD  1 
ATOM   1936 N NE  . ARG A 1 249 ? 27.05289 23.20444 26.76070  0.700 68.71400  ? 249 ARG A NE  1 
ATOM   1937 C CZ  . ARG A 1 249 ? 27.09764 22.10048 27.49229  0.700 70.13920  ? 249 ARG A CZ  1 
ATOM   1938 N NH1 . ARG A 1 249 ? 28.18073 21.76599 28.17410  0.700 70.52556  ? 249 ARG A NH1 1 
ATOM   1939 N NH2 . ARG A 1 249 ? 26.03211 21.30695 27.53201  0.700 72.22704  ? 249 ARG A NH2 1 
ATOM   1940 N N   . SER A 1 250 ? 30.66982 25.97752 22.83530  1.000 64.59766  ? 250 SER A N   1 
ATOM   1941 C CA  . SER A 1 250 ? 31.26733 25.29242 21.70006  1.000 60.91362  ? 250 SER A CA  1 
ATOM   1942 C C   . SER A 1 250 ? 30.95305 23.80340 21.77490  1.000 63.67608  ? 250 SER A C   1 
ATOM   1943 O O   . SER A 1 250 ? 31.29126 23.13423 22.75814  1.000 62.41084  ? 250 SER A O   1 
ATOM   1944 C CB  . SER A 1 250 ? 32.77499 25.52499 21.66475  1.000 60.05270  ? 250 SER A CB  1 
ATOM   1945 O OG  . SER A 1 250 ? 33.32575 25.08604 20.43427  1.000 56.08271  ? 250 SER A OG  1 
ATOM   1946 N N   . PHE A 1 251 ? 30.29173 23.29405 20.74078  1.000 59.96528  ? 251 PHE A N   1 
ATOM   1947 C CA  . PHE A 1 251 ? 30.09828 21.85807 20.54802  1.000 51.79339  ? 251 PHE A CA  1 
ATOM   1948 C C   . PHE A 1 251 ? 30.38834 21.58969 19.07838  1.000 49.67664  ? 251 PHE A C   1 
ATOM   1949 O O   . PHE A 1 251 ? 29.47124 21.46524 18.25664  1.000 50.16335  ? 251 PHE A O   1 
ATOM   1950 C CB  . PHE A 1 251 ? 28.68473 21.42994 20.95005  1.000 50.71692  ? 251 PHE A CB  1 
ATOM   1951 C CG  . PHE A 1 251 ? 28.54744 19.96145 21.23479  1.000 48.26451  ? 251 PHE A CG  1 
ATOM   1952 C CD1 . PHE A 1 251 ? 29.64775 19.12349 21.19272  1.000 48.27428  ? 251 PHE A CD1 1 
ATOM   1953 C CD2 . PHE A 1 251 ? 27.31123 19.41876 21.53911  1.000 51.37054  ? 251 PHE A CD2 1 
ATOM   1954 C CE1 . PHE A 1 251 ? 29.51912 17.77306 21.45157  1.000 46.72782  ? 251 PHE A CE1 1 
ATOM   1955 C CE2 . PHE A 1 251 ? 27.17486 18.06778 21.79925  1.000 52.71824  ? 251 PHE A CE2 1 
ATOM   1956 C CZ  . PHE A 1 251 ? 28.28036 17.24390 21.75494  1.000 53.44637  ? 251 PHE A CZ  1 
ATOM   1957 N N   . PRO A 1 252 ? 31.66983 21.51476 18.70656  1.000 48.50277  ? 252 PRO A N   1 
ATOM   1958 C CA  . PRO A 1 252 ? 32.03194 21.47098 17.28378  1.000 44.37289  ? 252 PRO A CA  1 
ATOM   1959 C C   . PRO A 1 252 ? 31.45030 20.25716 16.58174  1.000 43.19715  ? 252 PRO A C   1 
ATOM   1960 O O   . PRO A 1 252 ? 31.29814 19.18382 17.16737  1.000 46.71939  ? 252 PRO A O   1 
ATOM   1961 C CB  . PRO A 1 252 ? 33.56337 21.41071 17.30702  1.000 44.05067  ? 252 PRO A CB  1 
ATOM   1962 C CG  . PRO A 1 252 ? 33.95092 21.91466 18.64824  1.000 46.99517  ? 252 PRO A CG  1 
ATOM   1963 C CD  . PRO A 1 252 ? 32.85555 21.48885 19.57499  1.000 47.28880  ? 252 PRO A CD  1 
ATOM   1964 N N   . PHE A 1 253 ? 31.13536 20.44533 15.30029  1.000 47.47136  ? 253 PHE A N   1 
ATOM   1965 C CA  . PHE A 1 253 ? 30.51160 19.38996 14.51017  1.000 40.33052  ? 253 PHE A CA  1 
ATOM   1966 C C   . PHE A 1 253 ? 31.30116 18.09202 14.59357  1.000 35.73343  ? 253 PHE A C   1 
ATOM   1967 O O   . PHE A 1 253 ? 30.73744 17.02265 14.84947  1.000 37.48983  ? 253 PHE A O   1 
ATOM   1968 C CB  . PHE A 1 253 ? 30.37948 19.85040 13.06134  1.000 42.00746  ? 253 PHE A CB  1 
ATOM   1969 C CG  . PHE A 1 253 ? 29.70872 18.85738 12.16770  1.000 38.98403  ? 253 PHE A CG  1 
ATOM   1970 C CD1 . PHE A 1 253 ? 28.33082 18.76347 12.13206  1.000 40.65342  ? 253 PHE A CD1 1 
ATOM   1971 C CD2 . PHE A 1 253 ? 30.45596 18.02754 11.35173  1.000 33.73373  ? 253 PHE A CD2 1 
ATOM   1972 C CE1 . PHE A 1 253 ? 27.70763 17.85536 11.29865  1.000 40.30150  ? 253 PHE A CE1 1 
ATOM   1973 C CE2 . PHE A 1 253 ? 29.84289 17.11903 10.52470  1.000 35.54622  ? 253 PHE A CE2 1 
ATOM   1974 C CZ  . PHE A 1 253 ? 28.46356 17.03166 10.49559  1.000 37.62382  ? 253 PHE A CZ  1 
ATOM   1975 N N   . TRP A 1 254 ? 32.61722 18.16738 14.39594  1.000 36.62533  ? 254 TRP A N   1 
ATOM   1976 C CA  . TRP A 1 254 ? 33.41572 16.94740 14.41900  1.000 38.13680  ? 254 TRP A CA  1 
ATOM   1977 C C   . TRP A 1 254 ? 33.46961 16.33236 15.81022  1.000 37.31646  ? 254 TRP A C   1 
ATOM   1978 O O   . TRP A 1 254 ? 33.65149 15.11614 15.93578  1.000 37.63007  ? 254 TRP A O   1 
ATOM   1979 C CB  . TRP A 1 254 ? 34.82297 17.22971 13.89671  1.000 34.65790  ? 254 TRP A CB  1 
ATOM   1980 C CG  . TRP A 1 254 ? 34.82541 17.80676 12.51948  1.000 37.61406  ? 254 TRP A CG  1 
ATOM   1981 C CD1 . TRP A 1 254 ? 35.26844 19.04474 12.15110  1.000 39.17398  ? 254 TRP A CD1 1 
ATOM   1982 C CD2 . TRP A 1 254 ? 34.33948 17.18459 11.32715  1.000 32.10614  ? 254 TRP A CD2 1 
ATOM   1983 N NE1 . TRP A 1 254 ? 35.10413 19.22645 10.80005  1.000 33.44576  ? 254 TRP A NE1 1 
ATOM   1984 C CE2 . TRP A 1 254 ? 34.53472 18.09839 10.26945  1.000 35.73194  ? 254 TRP A CE2 1 
ATOM   1985 C CE3 . TRP A 1 254 ? 33.76703 15.94225 11.04753  1.000 33.97746  ? 254 TRP A CE3 1 
ATOM   1986 C CZ2 . TRP A 1 254 ? 34.17575 17.80673 8.95439   1.000 30.25283  ? 254 TRP A CZ2 1 
ATOM   1987 C CZ3 . TRP A 1 254 ? 33.41097 15.65451 9.73943   1.000 32.58797  ? 254 TRP A CZ3 1 
ATOM   1988 C CH2 . TRP A 1 254 ? 33.61573 16.58347 8.71275   1.000 30.31213  ? 254 TRP A CH2 1 
ATOM   1989 N N   . ARG A 1 255 ? 33.31132 17.14378 16.85915  1.000 37.39214  ? 255 ARG A N   1 
ATOM   1990 C CA  . ARG A 1 255 ? 33.20745 16.58884 18.20444  1.000 37.85415  ? 255 ARG A CA  1 
ATOM   1991 C C   . ARG A 1 255 ? 31.90426 15.81949 18.36648  1.000 36.28544  ? 255 ARG A C   1 
ATOM   1992 O O   . ARG A 1 255 ? 31.89246 14.69117 18.87360  1.000 36.44282  ? 255 ARG A O   1 
ATOM   1993 C CB  . ARG A 1 255 ? 33.31648 17.69840 19.25260  1.000 39.33787  ? 255 ARG A CB  1 
ATOM   1994 C CG  . ARG A 1 255 ? 32.87158 17.24906 20.62854  1.000 38.03496  ? 255 ARG A CG  1 
ATOM   1995 C CD  . ARG A 1 255 ? 33.33913 18.18105 21.73889  0.800 46.21754  ? 255 ARG A CD  1 
ATOM   1996 N NE  . ARG A 1 255 ? 34.78536 18.37026 21.74504  0.700 45.81764  ? 255 ARG A NE  1 
ATOM   1997 C CZ  . ARG A 1 255 ? 35.66959 17.43268 22.06046  0.700 45.92428  ? 255 ARG A CZ  1 
ATOM   1998 N NH1 . ARG A 1 255 ? 35.29576 16.19807 22.35752  0.700 46.30222  ? 255 ARG A NH1 1 
ATOM   1999 N NH2 . ARG A 1 255 ? 36.96267 17.74220 22.08219  0.700 45.23020  ? 255 ARG A NH2 1 
ATOM   2000 N N   . ARG A 1 256 ? 30.79482 16.42056 17.93434  1.000 36.56743  ? 256 ARG A N   1 
ATOM   2001 C CA  . ARG A 1 256 ? 29.51772 15.71706 17.91031  1.000 38.10122  ? 256 ARG A CA  1 
ATOM   2002 C C   . ARG A 1 256 ? 29.61486 14.41941 17.11126  1.000 40.59451  ? 256 ARG A C   1 
ATOM   2003 O O   . ARG A 1 256 ? 29.05100 13.39341 17.51289  1.000 38.47386  ? 256 ARG A O   1 
ATOM   2004 C CB  . ARG A 1 256 ? 28.44249 16.64000 17.33054  1.000 41.89382  ? 256 ARG A CB  1 
ATOM   2005 C CG  . ARG A 1 256 ? 27.09231 16.54440 18.00953  1.000 51.11258  ? 256 ARG A CG  1 
ATOM   2006 C CD  . ARG A 1 256 ? 26.35106 17.88086 17.97684  1.000 57.99100  ? 256 ARG A CD  1 
ATOM   2007 N NE  . ARG A 1 256 ? 26.08963 18.34978 16.62213  1.000 48.44069  ? 256 ARG A NE  1 
ATOM   2008 C CZ  . ARG A 1 256 ? 26.63109 19.43426 16.08422  1.000 48.70938  ? 256 ARG A CZ  1 
ATOM   2009 N NH1 . ARG A 1 256 ? 27.47041 20.19825 16.76400  1.000 48.39043  ? 256 ARG A NH1 1 
ATOM   2010 N NH2 . ARG A 1 256 ? 26.31616 19.76476 14.83386  1.000 50.80603  ? 256 ARG A NH2 1 
ATOM   2011 N N   . VAL A 1 257 ? 30.34029 14.44247 15.98381  1.000 39.38705  ? 257 VAL A N   1 
ATOM   2012 C CA  . VAL A 1 257 ? 30.50178 13.24125 15.16480  1.000 38.09796  ? 257 VAL A CA  1 
ATOM   2013 C C   . VAL A 1 257 ? 31.31846 12.19120 15.90819  1.000 34.39852  ? 257 VAL A C   1 
ATOM   2014 O O   . VAL A 1 257 ? 30.99717 10.99647 15.87448  1.000 35.03414  ? 257 VAL A O   1 
ATOM   2015 C CB  . VAL A 1 257 ? 31.14064 13.59270 13.80579  1.000 36.61073  ? 257 VAL A CB  1 
ATOM   2016 C CG1 . VAL A 1 257 ? 31.53465 12.32717 13.06241  1.000 27.29212  ? 257 VAL A CG1 1 
ATOM   2017 C CG2 . VAL A 1 257 ? 30.19233 14.43072 12.95811  1.000 31.88368  ? 257 VAL A CG2 1 
ATOM   2018 N N   . HIS A 1 258 ? 32.39315 12.61671 16.57801  1.000 37.29416  ? 258 HIS A N   1 
ATOM   2019 C CA  . HIS A 1 258 ? 33.20920 11.69335 17.36394  1.000 39.40608  ? 258 HIS A CA  1 
ATOM   2020 C C   . HIS A 1 258 ? 32.38630 11.01246 18.45216  1.000 40.60901  ? 258 HIS A C   1 
ATOM   2021 O O   . HIS A 1 258 ? 32.48174 9.79564  18.65360  1.000 40.81539  ? 258 HIS A O   1 
ATOM   2022 C CB  . HIS A 1 258 ? 34.39031 12.44174 17.98221  1.000 36.00532  ? 258 HIS A CB  1 
ATOM   2023 C CG  . HIS A 1 258 ? 35.12876 11.65786 19.02555  1.000 42.82646  ? 258 HIS A CG  1 
ATOM   2024 N ND1 . HIS A 1 258 ? 34.71973 11.59233 20.34181  1.000 44.42507  ? 258 HIS A ND1 1 
ATOM   2025 C CD2 . HIS A 1 258 ? 36.25957 10.91823 18.94814  1.000 38.62822  ? 258 HIS A CD2 1 
ATOM   2026 C CE1 . HIS A 1 258 ? 35.56194 10.83965 21.02584  1.000 40.50646  ? 258 HIS A CE1 1 
ATOM   2027 N NE2 . HIS A 1 258 ? 36.50563 10.41864 20.20327  1.000 41.24050  ? 258 HIS A NE2 1 
ATOM   2028 N N   . ASP A 1 259 ? 31.57340 11.78725 19.17034  1.000 40.22117  ? 259 ASP A N   1 
ATOM   2029 C CA  . ASP A 1 259 ? 30.83080 11.22878 20.29361  1.000 44.38701  ? 259 ASP A CA  1 
ATOM   2030 C C   . ASP A 1 259 ? 29.75245 10.26417 19.82037  1.000 42.86794  ? 259 ASP A C   1 
ATOM   2031 O O   . ASP A 1 259 ? 29.50869 9.23649  20.46041  1.000 47.73578  ? 259 ASP A O   1 
ATOM   2032 C CB  . ASP A 1 259 ? 30.22441 12.35651 21.12697  1.000 46.83083  ? 259 ASP A CB  1 
ATOM   2033 C CG  . ASP A 1 259 ? 31.27977 13.25957 21.74415  1.000 45.47882  ? 259 ASP A CG  1 
ATOM   2034 O OD1 . ASP A 1 259 ? 32.38422 12.76453 22.05427  1.000 45.89123  ? 259 ASP A OD1 1 
ATOM   2035 O OD2 . ASP A 1 259 ? 31.00475 14.46522 21.91864  1.000 45.02182  ? 259 ASP A OD2 1 
ATOM   2036 N N   . SER A 1 260 ? 29.11093 10.56602 18.69075  1.000 45.65706  ? 260 SER A N   1 
ATOM   2037 C CA  . SER A 1 260 ? 28.01289 9.73510  18.20689  1.000 47.92669  ? 260 SER A CA  1 
ATOM   2038 C C   . SER A 1 260 ? 28.49262 8.44063  17.56025  1.000 41.89196  ? 260 SER A C   1 
ATOM   2039 O O   . SER A 1 260 ? 27.77733 7.43307  17.61003  1.000 42.93125  ? 260 SER A O   1 
ATOM   2040 C CB  . SER A 1 260 ? 27.15893 10.51799 17.20767  1.000 40.57297  ? 260 SER A CB  1 
ATOM   2041 O OG  . SER A 1 260 ? 26.67784 11.72610 17.77135  1.000 46.49325  ? 260 SER A OG  1 
ATOM   2042 N N   . PHE A 1 261 ? 29.68541 8.43533  16.96173  1.000 36.04146  ? 261 PHE A N   1 
ATOM   2043 C CA  . PHE A 1 261 ? 30.13879 7.28540  16.18992  1.000 41.27709  ? 261 PHE A CA  1 
ATOM   2044 C C   . PHE A 1 261 ? 31.41489 6.63361  16.70661  1.000 38.67147  ? 261 PHE A C   1 
ATOM   2045 O O   . PHE A 1 261 ? 31.59108 5.42875  16.51055  1.000 39.41224  ? 261 PHE A O   1 
ATOM   2046 C CB  . PHE A 1 261 ? 30.34505 7.67951  14.71470  1.000 33.87471  ? 261 PHE A CB  1 
ATOM   2047 C CG  . PHE A 1 261 ? 29.10784 8.21872  14.05235  1.000 29.37125  ? 261 PHE A CG  1 
ATOM   2048 C CD1 . PHE A 1 261 ? 28.05826 7.37581  13.72547  1.000 30.98793  ? 261 PHE A CD1 1 
ATOM   2049 C CD2 . PHE A 1 261 ? 28.99490 9.56904  13.75896  1.000 30.71007  ? 261 PHE A CD2 1 
ATOM   2050 C CE1 . PHE A 1 261 ? 26.91327 7.86761  13.11540  1.000 32.83692  ? 261 PHE A CE1 1 
ATOM   2051 C CE2 . PHE A 1 261 ? 27.85588 10.06949 13.14711  1.000 33.46947  ? 261 PHE A CE2 1 
ATOM   2052 C CZ  . PHE A 1 261 ? 26.81261 9.21657  12.82453  1.000 30.65238  ? 261 PHE A CZ  1 
ATOM   2053 N N   . ILE A 1 262 ? 32.30933 7.37465  17.35350  1.000 37.28795  ? 262 ILE A N   1 
ATOM   2054 C CA  . ILE A 1 262 ? 33.57214 6.77529  17.76786  1.000 43.29802  ? 262 ILE A CA  1 
ATOM   2055 C C   . ILE A 1 262 ? 33.48364 6.29543  19.21162  1.000 39.87987  ? 262 ILE A C   1 
ATOM   2056 O O   . ILE A 1 262 ? 33.64998 5.10180  19.48267  1.000 40.14196  ? 262 ILE A O   1 
ATOM   2057 C CB  . ILE A 1 262 ? 34.74341 7.75139  17.57583  1.000 41.49444  ? 262 ILE A CB  1 
ATOM   2058 C CG1 . ILE A 1 262 ? 34.74642 8.30089  16.14452  1.000 40.72424  ? 262 ILE A CG1 1 
ATOM   2059 C CG2 . ILE A 1 262 ? 36.05894 7.05416  17.88996  1.000 37.93999  ? 262 ILE A CG2 1 
ATOM   2060 C CD1 . ILE A 1 262 ? 35.06272 7.26926  15.07445  1.000 30.69876  ? 262 ILE A CD1 1 
ATOM   2061 N N   . GLU A 1 263 ? 33.22083 7.21511  20.14421  1.000 42.17540  ? 263 GLU A N   1 
ATOM   2062 C CA  . GLU A 1 263 ? 33.17340 6.89461  21.57314  1.000 50.57079  ? 263 GLU A CA  1 
ATOM   2063 C C   . GLU A 1 263 ? 32.76928 8.10027  22.41573  1.000 53.14976  ? 263 GLU A C   1 
ATOM   2064 O O   . GLU A 1 263 ? 33.29733 9.20060  22.22779  1.000 56.91980  ? 263 GLU A O   1 
ATOM   2065 C CB  . GLU A 1 263 ? 34.53043 6.38321  22.06159  1.000 48.73281  ? 263 GLU A CB  1 
ATOM   2066 C CG  . GLU A 1 263 ? 35.70600 7.19172  21.52348  1.000 59.23168  ? 263 GLU A CG  1 
ATOM   2067 C CD  . GLU A 1 263 ? 36.92563 7.12966  22.41480  0.800 58.61502  ? 263 GLU A CD  1 
ATOM   2068 O OE1 . GLU A 1 263 ? 36.75211 6.92383  23.63569  0.800 59.67058  ? 263 GLU A OE1 1 
ATOM   2069 O OE2 . GLU A 1 263 ? 38.05199 7.29342  21.89276  0.800 50.21127  ? 263 GLU A OE2 1 
ATOM   2070 N N   . ASP A 1 264 ? 31.85597 7.90599  23.36113  1.000 64.86345  ? 264 ASP A N   1 
ATOM   2071 C CA  . ASP A 1 264 ? 31.47215 8.98134  24.27729  1.000 66.00653  ? 264 ASP A CA  1 
ATOM   2072 C C   . ASP A 1 264 ? 31.28916 8.45635  25.70282  1.000 73.79744  ? 264 ASP A C   1 
ATOM   2073 O O   . ASP A 1 264 ? 32.24647 8.37850  26.47801  1.000 75.43214  ? 264 ASP A O   1 
ATOM   2074 C CB  . ASP A 1 264 ? 30.18893 9.66524  23.79714  1.000 63.55779  ? 264 ASP A CB  1 
ATOM   2075 C CG  . ASP A 1 264 ? 29.87955 10.94201 24.56379  1.000 72.00869  ? 264 ASP A CG  1 
ATOM   2076 O OD1 . ASP A 1 264 ? 30.74513 11.40381 25.33957  1.000 78.62379  ? 264 ASP A OD1 1 
ATOM   2077 O OD2 . ASP A 1 264 ? 28.76691 11.48502 24.38747  1.000 68.26574  ? 264 ASP A OD2 1 
HETATM 2078 C C1  . CIT B 2 .   ? 31.72824 23.97449 14.20939  1.000 51.66862  ? 301 CIT A C1  1 
HETATM 2079 O O1  . CIT B 2 .   ? 31.36942 22.83327 13.85201  1.000 51.09423  ? 301 CIT A O1  1 
HETATM 2080 O O2  . CIT B 2 .   ? 32.94485 24.15970 14.43476  1.000 48.12018  ? 301 CIT A O2  1 
HETATM 2081 C C2  . CIT B 2 .   ? 30.73217 25.10954 14.35591  1.000 52.17179  ? 301 CIT A C2  1 
HETATM 2082 C C3  . CIT B 2 .   ? 29.60973 24.81583 15.36030  1.000 58.88212  ? 301 CIT A C3  1 
HETATM 2083 O O7  . CIT B 2 .   ? 30.19422 24.30907 16.58950  1.000 61.19468  ? 301 CIT A O7  1 
HETATM 2084 C C4  . CIT B 2 .   ? 28.82818 26.08705 15.68827  1.000 60.30375  ? 301 CIT A C4  1 
HETATM 2085 C C5  . CIT B 2 .   ? 29.32817 26.68056 16.98864  1.000 63.54481  ? 301 CIT A C5  1 
HETATM 2086 O O3  . CIT B 2 .   ? 29.82240 27.82879 17.01646  1.000 64.27952  ? 301 CIT A O3  1 
HETATM 2087 O O4  . CIT B 2 .   ? 29.24845 26.03332 18.05711  1.000 62.97215  ? 301 CIT A O4  1 
HETATM 2088 C C6  . CIT B 2 .   ? 28.64887 23.76165 14.82024  1.000 53.87819  ? 301 CIT A C6  1 
HETATM 2089 O O5  . CIT B 2 .   ? 27.95870 23.99522 13.80477  1.000 51.21638  ? 301 CIT A O5  1 
HETATM 2090 O O6  . CIT B 2 .   ? 28.54455 22.64660 15.37928  1.000 53.11055  ? 301 CIT A O6  1 
HETATM 2091 N N1  . UX6 C 3 .   ? 10.90698 7.44185  9.49373   1.000 52.96617  ? 302 UX6 A N1  1 
HETATM 2092 C C7  . UX6 C 3 .   ? 19.45777 9.45261  14.11984  1.000 33.36234  ? 302 UX6 A C7  1 
HETATM 2093 C C8  . UX6 C 3 .   ? 18.71624 9.52508  15.44683  1.000 36.52537  ? 302 UX6 A C8  1 
HETATM 2094 N N2  . UX6 C 3 .   ? 12.33839 5.53765  9.39682   1.000 54.54412  ? 302 UX6 A N2  1 
HETATM 2095 C C9  . UX6 C 3 .   ? 18.42699 8.04311  15.67010  1.000 39.28610  ? 302 UX6 A C9  1 
HETATM 2096 O O1  . UX6 C 3 .   ? 18.77510 8.47614  13.35783  1.000 34.83485  ? 302 UX6 A O1  1 
HETATM 2097 C C1  . UX6 C 3 .   ? 13.73320 5.15871  9.58970   1.000 59.16154  ? 302 UX6 A C1  1 
HETATM 2098 O O5  . UX6 C 3 .   ? 16.07340 8.51831  9.94419   1.000 37.87486  ? 302 UX6 A O5  1 
HETATM 2099 C C5  . UX6 C 3 .   ? 16.66181 7.43134  13.88570  1.000 36.09979  ? 302 UX6 A C5  1 
HETATM 2100 C C6  . UX6 C 3 .   ? 18.12933 7.54170  14.25492  1.000 36.08123  ? 302 UX6 A C6  1 
HETATM 2101 N N3  . UX6 C 3 .   ? 16.45114 6.73531  12.62391  1.000 40.54159  ? 302 UX6 A N3  1 
HETATM 2102 C C4  . UX6 C 3 .   ? 16.22529 5.42503  12.54240  1.000 43.17733  ? 302 UX6 A C4  1 
HETATM 2103 O O4  . UX6 C 3 .   ? 14.41354 9.39198  12.03095  1.000 44.09296  ? 302 UX6 A O4  1 
HETATM 2104 C C3  . UX6 C 3 .   ? 15.66138 4.93304  11.22879  1.000 42.63015  ? 302 UX6 A C3  1 
HETATM 2105 O O3  . UX6 C 3 .   ? 19.57419 7.39010  16.19769  1.000 40.38155  ? 302 UX6 A O3  1 
HETATM 2106 C C2  . UX6 C 3 .   ? 14.18259 5.26668  11.04153  1.000 47.66505  ? 302 UX6 A C2  1 
HETATM 2107 N N4  . UX6 C 3 .   ? 19.54959 10.69613 13.36879  1.000 31.42604  ? 302 UX6 A N4  1 
HETATM 2108 N N   . UX6 C 3 .   ? 12.83642 7.41298  8.02852   1.000 50.18601  ? 302 UX6 A N   1 
HETATM 2109 C C   . UX6 C 3 .   ? 11.96503 6.86414  8.98825   1.000 52.05486  ? 302 UX6 A C   1 
HETATM 2110 O O   . UX6 C 3 .   ? 16.46572 4.65129  13.46462  1.000 42.31481  ? 302 UX6 A O   1 
HETATM 2111 C C10 . UX6 C 3 .   ? 18.52319 11.51223 12.93327  1.000 30.85970  ? 302 UX6 A C10 1 
HETATM 2112 C C11 . UX6 C 3 .   ? 20.32819 12.49685 12.36427  1.000 30.25540  ? 302 UX6 A C11 1 
HETATM 2113 C C12 . UX6 C 3 .   ? 21.34997 13.31006 11.83770  1.000 28.47037  ? 302 UX6 A C12 1 
HETATM 2114 C C13 . UX6 C 3 .   ? 22.85101 11.73121 12.61476  1.000 29.91557  ? 302 UX6 A C13 1 
HETATM 2115 C C14 . UX6 C 3 .   ? 20.71885 11.32459 12.98951  1.000 31.92233  ? 302 UX6 A C14 1 
HETATM 2116 C C15 . UX6 C 3 .   ? 17.15900 11.13189 13.04164  1.000 35.21260  ? 302 UX6 A C15 1 
HETATM 2117 C C16 . UX6 C 3 .   ? 16.00603 10.83398 13.07655  1.000 35.29687  ? 302 UX6 A C16 1 
HETATM 2118 C C17 . UX6 C 3 .   ? 14.59709 10.44768 12.96834  1.000 31.97750  ? 302 UX6 A C17 1 
HETATM 2119 C C18 . UX6 C 3 .   ? 14.23349 9.88170  10.69915  1.000 38.86022  ? 302 UX6 A C18 1 
HETATM 2120 C C19 . UX6 C 3 .   ? 15.55233 9.86018  9.96547   1.000 36.11550  ? 302 UX6 A C19 1 
HETATM 2121 C C20 . UX6 C 3 .   ? 17.04990 8.45060  8.91947   1.000 37.47205  ? 302 UX6 A C20 1 
HETATM 2122 C C21 . UX6 C 3 .   ? 16.76828 9.59223  7.92594   1.000 35.84979  ? 302 UX6 A C21 1 
HETATM 2123 C C22 . UX6 C 3 .   ? 15.50578 10.25633 8.49247   1.000 38.68822  ? 302 UX6 A C22 1 
HETATM 2124 C C23 . UX6 C 3 .   ? 16.00970 6.57917  7.55980   1.000 35.95863  ? 302 UX6 A C23 1 
HETATM 2125 C C24 . UX6 C 3 .   ? 17.55044 5.11915  7.57567   1.000 33.13916  ? 302 UX6 A C24 1 
HETATM 2126 C C25 . UX6 C 3 .   ? 18.41183 4.01532  7.42768   1.000 31.28918  ? 302 UX6 A C25 1 
HETATM 2127 C C26 . UX6 C 3 .   ? 19.93029 5.16563  8.73850   1.000 31.33936  ? 302 UX6 A C26 1 
HETATM 2128 C C27 . UX6 C 3 .   ? 18.01628 6.18062  8.33369   1.000 34.82135  ? 302 UX6 A C27 1 
HETATM 2129 N N10 . UX6 C 3 .   ? 16.27664 5.38413  7.09250   1.000 34.37721  ? 302 UX6 A N10 1 
HETATM 2130 N N11 . UX6 C 3 .   ? 18.11037 2.92364  6.71388   1.000 34.58030  ? 302 UX6 A N11 1 
HETATM 2131 N N12 . UX6 C 3 .   ? 19.61689 4.07481  8.03546   1.000 29.71245  ? 302 UX6 A N12 1 
HETATM 2132 N N13 . UX6 C 3 .   ? 19.20241 6.26477  8.94567   1.000 32.64818  ? 302 UX6 A N13 1 
HETATM 2133 N N5  . UX6 C 3 .   ? 18.94220 12.61546 12.34219  1.000 30.70444  ? 302 UX6 A N5  1 
HETATM 2134 N N6  . UX6 C 3 .   ? 21.12860 14.45034 11.17240  1.000 32.72457  ? 302 UX6 A N6  1 
HETATM 2135 N N7  . UX6 C 3 .   ? 22.62420 12.88917 11.98845  1.000 29.18614  ? 302 UX6 A N7  1 
HETATM 2136 N N8  . UX6 C 3 .   ? 21.97062 10.88232 13.14860  1.000 33.27510  ? 302 UX6 A N8  1 
HETATM 2137 N N9  . UX6 C 3 .   ? 17.01653 7.12283  8.31451   1.000 36.65384  ? 302 UX6 A N9  1 
HETATM 2138 O O2  . UX6 C 3 .   ? 19.56479 10.04756 16.46079  1.000 38.83800  ? 302 UX6 A O2  1 
HETATM 2139 O O6  . UX6 C 3 .   ? 17.86850 10.49334 7.88775   1.000 39.69467  ? 302 UX6 A O6  1 
HETATM 2140 O O7  . UX6 C 3 .   ? 15.55017 11.66672 8.29132   1.000 30.73795  ? 302 UX6 A O7  1 
HETATM 2141 O O   . HOH D 4 .   ? 26.79547 -4.23729 -10.55255 1.000 43.15063  ? 401 HOH A O   1 
HETATM 2142 O O   . HOH D 4 .   ? 7.94364  31.60335 41.63324  1.000 39.05139  ? 402 HOH A O   1 
HETATM 2143 O O   . HOH D 4 .   ? 25.20139 31.96473 3.40065   1.000 53.34191  ? 403 HOH A O   1 
HETATM 2144 O O   . HOH D 4 .   ? 24.19715 8.30024  -8.84259  1.000 25.30528  ? 404 HOH A O   1 
HETATM 2145 O O   . HOH D 4 .   ? 14.17676 -0.73513 -9.34249  1.000 42.52190  ? 405 HOH A O   1 
HETATM 2146 O O   . HOH D 4 .   ? 24.64998 1.32100  -5.63742  1.000 34.60568  ? 406 HOH A O   1 
HETATM 2147 O O   . HOH D 4 .   ? 13.57600 19.36106 0.52172   1.000 34.69452  ? 407 HOH A O   1 
HETATM 2148 O O   . HOH D 4 .   ? 13.70106 22.02927 -6.11031  1.000 41.76605  ? 408 HOH A O   1 
HETATM 2149 O O   . HOH D 4 .   ? 23.27381 7.65943  11.03983  1.000 28.90664  ? 409 HOH A O   1 
HETATM 2150 O O   . HOH D 4 .   ? 25.89475 6.67334  -3.77378  1.000 32.30085  ? 410 HOH A O   1 
HETATM 2151 O O   . HOH D 4 .   ? 22.63904 8.64117  14.21476  1.000 34.06345  ? 411 HOH A O   1 
HETATM 2152 O O   . HOH D 4 .   ? 11.20971 7.82849  -0.40326  1.000 36.28333  ? 412 HOH A O   1 
HETATM 2153 O O   . HOH D 4 .   ? 29.20876 6.72005  4.64663   1.000 26.52611  ? 413 HOH A O   1 
HETATM 2154 O O   . HOH D 4 .   ? 22.92457 11.34741 0.31785   1.000 24.01463  ? 414 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 31.51000 5.33591  0.00000   0.50  34.73659  ? 415 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 15.58542 28.64053 12.06082  1.000 35.62618  ? 416 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 11.03612 39.83100 21.56852  1.000 56.88151  ? 417 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 22.64263 20.93232 6.92732   1.000 27.95812  ? 418 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 20.39207 26.75625 2.92700   1.000 40.38994  ? 419 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 24.34358 5.33125  9.78569   1.000 33.78244  ? 420 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 30.16423 4.64609  8.22029   1.000 33.89066  ? 421 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 14.447   -3.871   -5.471    1.000 40.32873  ? 422 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 12.01911 1.53841  -5.48868  1.000 42.33208  ? 423 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 25.52025 9.37966  -6.52635  1.000 26.48716  ? 424 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 14.97303 16.70739 20.72090  1.000 41.91889  ? 425 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 10.52671 3.94415  -12.24661 1.000 40.65920  ? 426 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 20.91054 22.48057 19.80264  1.000 43.44952  ? 427 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 28.40714 26.25261 -2.62279  1.000 35.54332  ? 428 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 32.95642 15.81773 23.96696  1.000 40.55355  ? 429 HOH A O   1 
HETATM 2170 O O   . HOH D 4 .   ? 4.69702  18.68059 28.75120  1.000 43.70668  ? 430 HOH A O   1 
HETATM 2171 O O   . HOH D 4 .   ? 20.56889 8.10192  10.74609  1.000 28.61715  ? 431 HOH A O   1 
HETATM 2172 O O   . HOH D 4 .   ? 5.63874  9.40355  8.41142   1.000 55.74728  ? 432 HOH A O   1 
HETATM 2173 O O   . HOH D 4 .   ? 7.33280  9.83494  10.51882  1.000 57.82858  ? 433 HOH A O   1 
HETATM 2174 O O   . HOH D 4 .   ? 13.30900 17.74806 35.80924  1.000 46.12114  ? 434 HOH A O   1 
HETATM 2175 O O   . HOH D 4 .   ? 29.88202 26.85060 0.87097   1.000 39.28025  ? 435 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 12.73164 11.27698 18.56870  1.000 36.88900  ? 436 HOH A O   1 
HETATM 2177 O O   . HOH D 4 .   ? 23.51738 0.73452  -1.51635  1.000 36.96093  ? 437 HOH A O   1 
HETATM 2178 O O   . HOH D 4 .   ? 0.01852  34.05972 24.14509  1.000 64.07819  ? 438 HOH A O   1 
HETATM 2179 O O   . HOH D 4 .   ? -3.09410 3.06121  -8.25863  1.000 53.00687  ? 439 HOH A O   1 
HETATM 2180 O O   . HOH D 4 .   ? 15.13305 9.48458  17.23588  1.000 38.32847  ? 440 HOH A O   1 
HETATM 2181 O O   . HOH D 4 .   ? 6.43038  14.49253 0.86221   1.000 54.99556  ? 441 HOH A O   1 
HETATM 2182 O O   . HOH D 4 .   ? 15.11381 -0.84497 -12.85460 1.000 40.31019  ? 442 HOH A O   1 
HETATM 2183 O O   . HOH D 4 .   ? 0.62267  14.37775 -2.46959  1.000 57.38084  ? 443 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   ? 1.19635 1.02262 1.06790 -0.00312 0.13969  -0.17798 1   MET A N   
2    C CA  . MET A 1   ? 1.15765 0.95594 1.03448 0.01693  0.14616  -0.16279 1   MET A CA  
3    C C   . MET A 1   ? 1.04633 0.87301 0.93526 0.03444  0.13519  -0.14581 1   MET A C   
4    O O   . MET A 1   ? 0.94968 0.80722 0.83872 0.03256  0.12797  -0.14757 1   MET A O   
5    C CB  . MET A 1   ? 1.20743 0.98356 1.08824 0.01568  0.14753  -0.15382 1   MET A CB  
6    C CG  . MET A 1   ? 1.17730 0.98483 1.06780 0.00684  0.13136  -0.14679 1   MET A CG  
7    S SD  . MET A 1   ? 1.48824 1.27747 1.37488 -0.01482 0.13715  -0.15603 1   MET A SD  
8    C CE  . MET A 1   ? 1.10861 0.94136 0.99267 -0.03766 0.12798  -0.17549 1   MET A CE  
9    N N   . LYS A 2   ? 1.04039 0.85734 0.93877 0.05118  0.13501  -0.12983 2   LYS A N   
10   C CA  . LYS A 2   ? 0.91657 0.76172 0.82842 0.06507  0.12565  -0.11577 2   LYS A CA  
11   C C   . LYS A 2   ? 0.78260 0.65800 0.70288 0.05706  0.11004  -0.10834 2   LYS A C   
12   O O   . LYS A 2   ? 0.74438 0.61648 0.66477 0.04796  0.10534  -0.10742 2   LYS A O   
13   C CB  . LYS A 2   ? 0.85467 0.68703 0.77445 0.08487  0.12921  -0.10266 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.93794 0.74719 0.85092 0.09974  0.14450  -0.10651 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.94706 0.74759 0.86654 0.12229  0.14762  -0.09225 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.95898 0.73554 0.87018 0.14039  0.16418  -0.09511 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.89595 0.66320 0.81021 0.16540  0.16842  -0.08035 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.76928 0.67276 0.69590 0.06071  0.10360  -0.10296 3   TYR A N   
19   C CA  . TYR A 3   ? 0.67786 0.60682 0.60947 0.05463  0.09141  -0.09599 3   TYR A CA  
20   C C   . TYR A 3   ? 0.68114 0.63011 0.62311 0.06332  0.08878  -0.08618 3   TYR A C   
21   O O   . TYR A 3   ? 0.68659 0.63696 0.62997 0.07095  0.09589  -0.08781 3   TYR A O   
22   C CB  . TYR A 3   ? 0.62658 0.56970 0.54596 0.04183  0.08879  -0.10580 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.68267 0.64143 0.59542 0.04437  0.09206  -0.10898 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.74407 0.69127 0.64794 0.04532  0.10275  -0.12099 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.60890 0.59154 0.52280 0.04646  0.08614  -0.09955 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.71382 0.67647 0.61080 0.04800  0.10631  -0.12377 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.65177 0.64747 0.55797 0.04924  0.09072  -0.10100 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.67868 0.66621 0.57672 0.04987  0.10022  -0.11326 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.65442 0.65633 0.54391 0.05294  0.10528  -0.11466 3   TYR A OH  
30   N N   . MET A 4   ? 0.56613 0.53038 0.51516 0.06126  0.07979  -0.07683 4   MET A N   
31   C CA  . MET A 4   ? 0.55719 0.53918 0.51447 0.06499  0.07885  -0.06898 4   MET A CA  
32   C C   . MET A 4   ? 0.52664 0.52032 0.48031 0.05893  0.07185  -0.06306 4   MET A C   
33   O O   . MET A 4   ? 0.52607 0.51797 0.47474 0.05373  0.06602  -0.06406 4   MET A O   
34   C CB  . MET A 4   ? 0.61147 0.59639 0.58561 0.07312  0.07814  -0.06241 4   MET A CB  
35   C CG  . MET A 4   ? 0.54377 0.52774 0.52485 0.07179  0.06969  -0.05611 4   MET A CG  
36   S SD  . MET A 4   ? 0.54658 0.54624 0.53356 0.06621  0.06429  -0.04826 4   MET A SD  
37   C CE  . MET A 4   ? 0.58271 0.59798 0.58297 0.06992  0.07126  -0.04770 4   MET A CE  
38   N N   . ILE A 5   ? 0.52395 0.52928 0.47971 0.06015  0.07389  -0.05658 5   ILE A N   
39   C CA  . ILE A 5   ? 0.52430 0.53736 0.47385 0.05766  0.07024  -0.04891 5   ILE A CA  
40   C C   . ILE A 5   ? 0.55957 0.57519 0.52060 0.05865  0.07305  -0.04029 5   ILE A C   
41   O O   . ILE A 5   ? 0.56391 0.58400 0.52990 0.05965  0.08084  -0.04045 5   ILE A O   
42   C CB  . ILE A 5   ? 0.53764 0.56013 0.46949 0.05742  0.07355  -0.05041 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.55432 0.57679 0.47558 0.05376  0.07258  -0.06340 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.52718 0.55710 0.45034 0.05868  0.06984  -0.04056 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.51074 0.54768 0.41398 0.05373  0.07547  -0.06741 5   ILE A CD1 
46   N N   . THR A 6   ? 0.54076 0.55412 0.50614 0.05732  0.06783  -0.03404 6   THR A N   
47   C CA  . THR A 6   ? 0.55288 0.56611 0.52708 0.05561  0.07183  -0.02755 6   THR A CA  
48   C C   . THR A 6   ? 0.53922 0.54950 0.49894 0.05644  0.07599  -0.01862 6   THR A C   
49   O O   . THR A 6   ? 0.59858 0.61111 0.54390 0.05970  0.07160  -0.01643 6   THR A O   
50   C CB  . THR A 6   ? 0.58763 0.59842 0.57437 0.05422  0.06525  -0.02688 6   THR A CB  
51   O OG1 . THR A 6   ? 0.62494 0.63179 0.60349 0.05522  0.05735  -0.02494 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.62723 0.64294 0.62770 0.05637  0.06293  -0.03315 6   THR A CG2 
53   N N   . SER A 7   ? 0.53873 0.54492 0.50197 0.05382  0.08553  -0.01349 7   SER A N   
54   C CA  . SER A 7   ? 0.61338 0.61168 0.56064 0.05660  0.09330  -0.00274 7   SER A CA  
55   C C   . SER A 7   ? 0.67618 0.66060 0.63035 0.05221  0.09924  0.00245  7   SER A C   
56   O O   . SER A 7   ? 0.70224 0.68826 0.67474 0.04416  0.10180  -0.00376 7   SER A O   
57   C CB  . SER A 7   ? 0.62645 0.62806 0.56512 0.05717  0.10484  -0.00088 7   SER A CB  
58   O OG  . SER A 7   ? 0.59480 0.58617 0.51582 0.06159  0.11452  0.01183  7   SER A OG  
59   N N   . LYS A 8   ? 0.63204 0.60423 0.57100 0.05808  0.10190  0.01310  8   LYS A N   
60   C CA  . LYS A 8   ? 0.61927 0.57171 0.56063 0.05415  0.11148  0.01837  8   LYS A CA  
61   C C   . LYS A 8   ? 0.67910 0.62304 0.62440 0.04539  0.12853  0.01890  8   LYS A C   
62   O O   . LYS A 8   ? 0.73913 0.67019 0.69463 0.03561  0.13725  0.01655  8   LYS A O   
63   C CB  . LYS A 8   ? 0.69456 0.63376 0.61484 0.06607  0.11351  0.03174  8   LYS A CB  
64   C CG  . LYS A 8   ? 0.76478 0.67504 0.68038 0.06434  0.12890  0.03977  8   LYS A CG  
65   C CD  . LYS A 8   ? 0.80161 0.70159 0.71108 0.07270  0.12397  0.04495  8   LYS A CD  
66   C CE  . LYS A 8   ? 0.94008 0.80500 0.84102 0.07232  0.14249  0.05338  8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.86838 0.72225 0.78830 0.05252  0.15281  0.04208  8   LYS A NZ  
68   N N   . GLY A 9   ? 0.70297 0.65527 0.64113 0.04719  0.13416  0.02030  9   GLY A N   
69   C CA  . GLY A 9   ? 0.67424 0.62233 0.61773 0.03784  0.15082  0.01986  9   GLY A CA  
70   C C   . GLY A 9   ? 0.69029 0.61552 0.61178 0.04180  0.16891  0.03486  9   GLY A C   
71   O O   . GLY A 9   ? 0.80832 0.72605 0.73360 0.03202  0.18593  0.03521  9   GLY A O   
72   N N   . ASP A 10  ? 0.65619 0.57111 0.55452 0.05643  0.16684  0.04769  10  ASP A N   
73   C CA  . ASP A 10  ? 0.75066 0.64503 0.62327 0.06529  0.18427  0.06483  10  ASP A CA  
74   C C   . ASP A 10  ? 0.83738 0.75166 0.69388 0.07467  0.18315  0.06844  10  ASP A C   
75   O O   . ASP A 10  ? 0.77090 0.71166 0.63629 0.07350  0.16926  0.05664  10  ASP A O   
76   C CB  . ASP A 10  ? 0.73511 0.61098 0.58927 0.07974  0.18383  0.07813  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.80737 0.70901 0.65307 0.09428  0.16340  0.07820  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.81326 0.74251 0.66915 0.09054  0.14939  0.06596  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.88282 0.77713 0.71144 0.10949  0.16250  0.09011  10  ASP A OD2 
80   N N   . GLU A 11  ? 0.86525 0.76521 0.69594 0.08475  0.19915  0.08501  11  GLU A N   
81   C CA  . GLU A 11  ? 0.85907 0.77946 0.67186 0.09419  0.19931  0.08857  11  GLU A CA  
82   C C   . GLU A 11  ? 0.81359 0.76263 0.61680 0.10721  0.17839  0.08517  11  GLU A C   
83   O O   . GLU A 11  ? 0.81059 0.78570 0.61431 0.10653  0.16989  0.07482  11  GLU A O   
84   C CB  . GLU A 11  ? 0.94425 0.84293 0.72776 0.10518  0.22126  0.10957  11  GLU A CB  
85   C CG  . GLU A 11  ? 0.93766 0.82266 0.72673 0.09120  0.24302  0.10979  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.00875 0.87566 0.76441 0.10439  0.26458  0.13155  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.03675 0.90652 0.76434 0.12671  0.26064  0.14630  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.07146 0.92338 0.82852 0.09309  0.28597  0.13422  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.85413 0.79950 0.64887 0.11837  0.17086  0.09251  12  LYS A N   
90   C CA  . LYS A 12  ? 0.81771 0.79425 0.60334 0.12973  0.15228  0.08889  12  LYS A CA  
91   C C   . LYS A 12  ? 0.78757 0.78462 0.59698 0.11645  0.13510  0.06726  12  LYS A C   
92   O O   . LYS A 12  ? 0.77428 0.79794 0.57886 0.11744  0.12606  0.05772  12  LYS A O   
93   C CB  . LYS A 12  ? 0.85188 0.82193 0.62781 0.14354  0.14824  0.10016  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.90721 0.91478 0.67063 0.15713  0.13145  0.09850  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.92886 0.93240 0.67834 0.17570  0.13090  0.11358  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.92674 0.96548 0.64872 0.19768  0.12594  0.12288  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.92695 1.01014 0.65533 0.18987  0.10831  0.10331  12  LYS A NZ  
98   N N   . SER A 13  ? 0.78813 0.77213 0.62204 0.10414  0.13161  0.05906  13  SER A N   
99   C CA  . SER A 13  ? 0.70757 0.70737 0.56133 0.09464  0.11627  0.04140  13  SER A CA  
100  C C   . SER A 13  ? 0.69205 0.70021 0.55517 0.08588  0.11897  0.02983  13  SER A C   
101  O O   . SER A 13  ? 0.67585 0.70133 0.54098 0.08420  0.10916  0.01765  13  SER A O   
102  C CB  . SER A 13  ? 0.64644 0.63194 0.52120 0.08654  0.11224  0.03750  13  SER A CB  
103  O OG  . SER A 13  ? 0.68024 0.65516 0.54518 0.09566  0.11231  0.04875  13  SER A OG  
104  N N   . ASP A 14  ? 0.67272 0.66847 0.54171 0.07986  0.13346  0.03269  14  ASP A N   
105  C CA  . ASP A 14  ? 0.67903 0.68528 0.55722 0.07338  0.13717  0.02229  14  ASP A CA  
106  C C   . ASP A 14  ? 0.66986 0.69383 0.52794 0.08102  0.13576  0.02035  14  ASP A C   
107  O O   . ASP A 14  ? 0.61985 0.65668 0.48389 0.07801  0.13030  0.00669  14  ASP A O   
108  C CB  . ASP A 14  ? 0.69192 0.68618 0.57695 0.06602  0.15513  0.02701  14  ASP A CB  
109  C CG  . ASP A 14  ? 0.73235 0.71962 0.64417 0.05403  0.15530  0.02038  14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.73190 0.72444 0.65671 0.05294  0.14101  0.01226  14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.75682 0.73483 0.67631 0.04511  0.17036  0.02270  14  ASP A OD2 
112  N N   . LEU A 15  ? 0.71672 0.74153 0.54940 0.09197  0.14134  0.03378  15  LEU A N   
113  C CA  . LEU A 15  ? 0.71344 0.75949 0.52461 0.09983  0.14054  0.03185  15  LEU A CA  
114  C C   . LEU A 15  ? 0.65670 0.72414 0.46588 0.10096  0.12304  0.01908  15  LEU A C   
115  O O   . LEU A 15  ? 0.61739 0.70188 0.42194 0.09891  0.11977  0.00586  15  LEU A O   
116  C CB  . LEU A 15  ? 0.71079 0.75427 0.49350 0.11391  0.15126  0.05151  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.85943 0.88966 0.63339 0.11382  0.17214  0.06216  15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.76748 0.82117 0.52483 0.11827  0.17427  0.05675  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.80951 0.82189 0.61144 0.09747  0.18103  0.05614  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.67529 0.74186 0.48800 0.10312  0.11288  0.02168  16  LEU A N   
121  C CA  . LEU A 16  ? 0.63384 0.72091 0.44774 0.10096  0.09749  0.00811  16  LEU A CA  
122  C C   . LEU A 16  ? 0.61230 0.69467 0.44636 0.08787  0.09343  -0.01008 16  LEU A C   
123  O O   . LEU A 16  ? 0.58120 0.67859 0.41159 0.08378  0.08760  -0.02514 16  LEU A O   
124  C CB  . LEU A 16  ? 0.65854 0.74483 0.47532 0.10517  0.08888  0.01479  16  LEU A CB  
125  C CG  . LEU A 16  ? 0.73871 0.85077 0.55502 0.10287  0.07417  0.00197  16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.75607 0.90116 0.54933 0.11006  0.07218  -0.00156 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.60972 0.72203 0.42999 0.10796  0.06694  0.00971  16  LEU A CD2 
128  N N   . ARG A 17  ? 0.63237 0.69424 0.48685 0.08168  0.09765  -0.00925 17  ARG A N   
129  C CA  . ARG A 17  ? 0.61306 0.66984 0.48560 0.07321  0.09497  -0.02369 17  ARG A CA  
130  C C   . ARG A 17  ? 0.56161 0.62532 0.42806 0.07256  0.10174  -0.03335 17  ARG A C   
131  O O   . ARG A 17  ? 0.55684 0.62332 0.42431 0.06872  0.09797  -0.04807 17  ARG A O   
132  C CB  . ARG A 17  ? 0.58870 0.62936 0.48304 0.06905  0.09836  -0.01981 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.55923 0.59647 0.47149 0.06443  0.09672  -0.03176 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.56423 0.59421 0.49740 0.06129  0.09958  -0.02820 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.51027 0.54151 0.45910 0.06081  0.09914  -0.03774 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.55811 0.59582 0.51239 0.06202  0.10771  -0.04186 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.56259 0.60551 0.50848 0.06177  0.11790  -0.03786 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.57205 0.61152 0.53967 0.06497  0.10691  -0.04933 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.61947 0.68409 0.47850 0.07606  0.11341  -0.02546 18  LEU A N   
140  C CA  . LEU A 18  ? 0.61453 0.68725 0.46667 0.07641  0.12086  -0.03431 18  LEU A CA  
141  C C   . LEU A 18  ? 0.59038 0.68090 0.42154 0.07846  0.11547  -0.04412 18  LEU A C   
142  O O   . LEU A 18  ? 0.59668 0.69083 0.42599 0.07550  0.11696  -0.05945 18  LEU A O   
143  C CB  . LEU A 18  ? 0.66188 0.73380 0.50804 0.07951  0.13552  -0.02256 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.60139 0.66580 0.46956 0.07424  0.14512  -0.02341 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.60768 0.66026 0.49745 0.06902  0.14064  -0.01997 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.66883 0.73411 0.52827 0.07546  0.16148  -0.01269 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.59687 0.70024 0.41192 0.08382  0.10958  -0.03654 19  ASN A N   
148  C CA  . ASN A 19  ? 0.60968 0.73803 0.40569 0.08485  0.10323  -0.04780 19  ASN A CA  
149  C C   . ASN A 19  ? 0.63416 0.76307 0.44021 0.07455  0.09311  -0.06612 19  ASN A C   
150  O O   . ASN A 19  ? 0.65833 0.80118 0.45467 0.06946  0.09166  -0.08365 19  ASN A O   
151  C CB  . ASN A 19  ? 0.62113 0.76881 0.39734 0.09602  0.09951  -0.03376 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.64605 0.80099 0.40064 0.10724  0.11102  -0.02054 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.65634 0.81153 0.40708 0.10518  0.11965  -0.02707 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.65874 0.81850 0.39782 0.12043  0.11247  -0.00106 19  ASN A ND2 
155  N N   . MET A 20  ? 0.57814 0.69131 0.40254 0.07053  0.08734  -0.06318 20  MET A N   
156  C CA  . MET A 20  ? 0.57055 0.67984 0.40411 0.06025  0.08034  -0.07933 20  MET A CA  
157  C C   . MET A 20  ? 0.59989 0.68924 0.44283 0.05484  0.08746  -0.09213 20  MET A C   
158  O O   . MET A 20  ? 0.65069 0.73875 0.49033 0.04674  0.08726  -0.11006 20  MET A O   
159  C CB  . MET A 20  ? 0.58717 0.68621 0.43571 0.05897  0.07292  -0.07122 20  MET A CB  
160  C CG  . MET A 20  ? 0.61273 0.73238 0.45163 0.06512  0.06542  -0.06109 20  MET A CG  
161  S SD  . MET A 20  ? 0.57934 0.68767 0.43537 0.06332  0.05722  -0.05390 20  MET A SD  
162  C CE  . MET A 20  ? 0.60134 0.70941 0.46509 0.04827  0.05217  -0.07566 20  MET A CE  
163  N N   . ILE A 21  ? 0.60730 0.68145 0.46180 0.05933  0.09488  -0.08374 21  ILE A N   
164  C CA  . ILE A 21  ? 0.64146 0.70067 0.50359 0.05848  0.10277  -0.09410 21  ILE A CA  
165  C C   . ILE A 21  ? 0.59716 0.66616 0.44155 0.05742  0.10887  -0.10833 21  ILE A C   
166  O O   . ILE A 21  ? 0.62865 0.68543 0.47244 0.05331  0.11290  -0.12433 21  ILE A O   
167  C CB  . ILE A 21  ? 0.62041 0.67284 0.49738 0.06425  0.10982  -0.08270 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.60169 0.64535 0.49647 0.06375  0.10375  -0.07218 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.62405 0.66653 0.50815 0.06679  0.11826  -0.09267 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.56825 0.61227 0.47677 0.06654  0.11012  -0.06137 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.63414 0.72388 0.46206 0.06176  0.11079  -0.10272 22  ALA A N   
172  C CA  . ALA A 22  ? 0.69181 0.79565 0.50047 0.06103  0.11594  -0.11683 22  ALA A CA  
173  C C   . ALA A 22  ? 0.64640 0.75963 0.44547 0.05111  0.10908  -0.13589 22  ALA A C   
174  O O   . ALA A 22  ? 0.70468 0.81501 0.49586 0.04534  0.11460  -0.15561 22  ALA A O   
175  C CB  . ALA A 22  ? 0.64226 0.76859 0.43297 0.06936  0.11904  -0.10440 22  ALA A CB  
176  N N   . GLY A 23  ? 0.63514 0.76013 0.43512 0.04820  0.09807  -0.13156 23  GLY A N   
177  C CA  . GLY A 23  ? 0.70604 0.84287 0.50048 0.03607  0.09189  -0.15097 23  GLY A CA  
178  C C   . GLY A 23  ? 0.70706 0.81191 0.51419 0.02543  0.09617  -0.16549 23  GLY A C   
179  O O   . GLY A 23  ? 0.73162 0.83588 0.53098 0.01370  0.09950  -0.18800 23  GLY A O   
180  N N   . PHE A 24  ? 0.69370 0.77108 0.51927 0.02956  0.09726  -0.15311 24  PHE A N   
181  C CA  . PHE A 24  ? 0.76685 0.81128 0.60243 0.02335  0.10283  -0.16332 24  PHE A CA  
182  C C   . PHE A 24  ? 0.76732 0.79332 0.59757 0.02579  0.11615  -0.17525 24  PHE A C   
183  O O   . PHE A 24  ? 0.82834 0.82850 0.65781 0.01896  0.12368  -0.19027 24  PHE A O   
184  C CB  . PHE A 24  ? 0.71688 0.74216 0.57200 0.02983  0.10005  -0.14610 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.68228 0.71644 0.54347 0.02521  0.08890  -0.13902 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.71365 0.74587 0.57286 0.01212  0.08661  -0.15267 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.64527 0.68878 0.51427 0.03320  0.08222  -0.11963 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.76665 0.80990 0.63218 0.00834  0.07685  -0.14634 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.61130 0.66263 0.48528 0.03037  0.07276  -0.11339 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.70634 0.75928 0.57897 0.01859  0.06959  -0.12635 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.77994 0.81693 0.60567 0.03573  0.12084  -0.16872 25  GLY A N   
192  C CA  . GLY A 25  ? 0.78236 0.80611 0.60177 0.03912  0.13384  -0.18078 25  GLY A CA  
193  C C   . GLY A 25  ? 0.81557 0.84129 0.61677 0.02728  0.13847  -0.20629 25  GLY A C   
194  O O   . GLY A 25  ? 0.86923 0.87202 0.66579 0.02745  0.15087  -0.22055 25  GLY A O   
195  N N   . GLU A 26  ? 0.84599 0.89996 0.63667 0.01714  0.12929  -0.21337 26  GLU A N   
196  C CA  . GLU A 26  ? 0.86075 0.92518 0.63437 0.00296  0.13245  -0.24049 26  GLU A CA  
197  C C   . GLU A 26  ? 0.94860 0.98559 0.72670 -0.01322 0.13623  -0.25807 26  GLU A C   
198  O O   . GLU A 26  ? 0.89953 0.94051 0.66472 -0.02850 0.14131  -0.28424 26  GLU A O   
199  C CB  . GLU A 26  ? 0.76999 0.88414 0.53065 -0.00004 0.12052  -0.24106 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.72770 0.86670 0.47944 0.01600  0.11924  -0.22320 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.93060 1.06361 0.67059 0.02063  0.13212  -0.23304 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.99064 1.12109 0.71920 0.00950  0.13856  -0.25953 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 0.90558 1.03626 0.64794 0.03449  0.13690  -0.21528 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.95969 0.96937 0.75471 -0.01105 0.13496  -0.24516 27  TYR A N   
205  C CA  . TYR A 27  ? 0.99121 0.96970 0.79042 -0.02507 0.14057  -0.25794 27  TYR A CA  
206  C C   . TYR A 27  ? 1.11325 1.04289 0.92138 -0.01370 0.15256  -0.24962 27  TYR A C   
207  O O   . TYR A 27  ? 1.06680 0.99271 0.88027 0.00415  0.15481  -0.23497 27  TYR A O   
208  C CB  . TYR A 27  ? 0.93521 0.93002 0.74475 -0.03255 0.12748  -0.24946 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.89184 0.93894 0.69345 -0.04097 0.11493  -0.25605 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.80746 0.88939 0.60851 -0.02693 0.10336  -0.23649 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.89528 0.95787 0.68969 -0.06257 0.11557  -0.28181 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.77118 0.90227 0.56313 -0.03045 0.09232  -0.24027 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.79046 0.90852 0.57804 -0.06821 0.10314  -0.28795 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.73349 0.88578 0.51915 -0.05021 0.09126  -0.26596 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.70913 0.91773 0.48607 -0.05171 0.07940  -0.26988 27  TYR A OH  
216  N N   . ASP A 28  ? 1.42987 1.32360 1.23941 -0.02388 0.16099  -0.25882 28  ASP A N   
217  C CA  . ASP A 28  ? 1.47290 1.31958 1.28917 -0.01122 0.17251  -0.24907 28  ASP A CA  
218  C C   . ASP A 28  ? 1.32677 1.17843 1.16090 0.00014  0.16088  -0.22284 28  ASP A C   
219  O O   . ASP A 28  ? 1.34691 1.17420 1.18680 -0.00252 0.16275  -0.21791 28  ASP A O   
220  C CB  . ASP A 28  ? 1.66832 1.47099 1.47615 -0.02618 0.18843  -0.26792 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.67981 1.43001 1.48802 -0.00924 0.20475  -0.25971 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.61548 1.36805 1.42826 0.01294  0.20539  -0.24614 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 1.65746 1.36524 1.46106 -0.01751 0.21775  -0.26640 28  ASP A OD2 
224  N N   . MET A 29  ? 1.19556 1.07919 1.03743 0.01225  0.14980  -0.20647 29  MET A N   
225  C CA  . MET A 29  ? 1.09727 0.98980 0.95575 0.02253  0.13890  -0.18331 29  MET A CA  
226  C C   . MET A 29  ? 1.02939 0.92140 0.89648 0.04231  0.14222  -0.16983 29  MET A C   
227  O O   . MET A 29  ? 1.05723 0.96772 0.91999 0.04688  0.14393  -0.17136 29  MET A O   
228  C CB  . MET A 29  ? 0.98769 0.92031 0.84851 0.01687  0.12319  -0.17605 29  MET A CB  
229  C CG  . MET A 29  ? 0.99498 0.93967 0.84907 -0.00188 0.11823  -0.18963 29  MET A CG  
230  S SD  . MET A 29  ? 1.08972 1.00785 0.95320 -0.01006 0.11839  -0.18727 29  MET A SD  
231  C CE  . MET A 29  ? 0.91257 0.86475 0.78801 -0.00569 0.10008  -0.16719 29  MET A CE  
232  N N   . GLU A 30  ? 0.94778 0.82180 0.82685 0.05401  0.14347  -0.15709 30  GLU A N   
233  C CA  . GLU A 30  ? 0.93711 0.81663 0.82771 0.07275  0.14565  -0.14458 30  GLU A CA  
234  C C   . GLU A 30  ? 0.89810 0.80038 0.80530 0.07613  0.13245  -0.12688 30  GLU A C   
235  O O   . GLU A 30  ? 0.82523 0.71987 0.73744 0.07302  0.12634  -0.12089 30  GLU A O   
236  C CB  . GLU A 30  ? 1.02902 0.87396 0.91943 0.08675  0.15836  -0.14430 30  GLU A CB  
237  C CG  . GLU A 30  ? 1.09341 0.95012 1.00038 0.10700  0.15678  -0.12829 30  GLU A CG  
238  C CD  . GLU A 30  ? 1.14844 0.97283 1.05337 0.12462  0.16886  -0.12541 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.11788 0.90478 1.00992 0.11930  0.17742  -0.13218 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 1.19593 1.03331 1.11180 0.14420  0.17075  -0.11626 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.86408 0.79315 0.77918 0.08149  0.12946  -0.11938 31  TYR A N   
242  C CA  . TYR A 31  ? 0.74478 0.69377 0.67549 0.08342  0.11941  -0.10462 31  TYR A CA  
243  C C   . TYR A 31  ? 0.79781 0.74222 0.74329 0.09755  0.12098  -0.09668 31  TYR A C   
244  O O   . TYR A 31  ? 0.78824 0.73567 0.73814 0.10979  0.12906  -0.09748 31  TYR A O   
245  C CB  . TYR A 31  ? 0.63658 0.61233 0.56963 0.08262  0.11882  -0.10012 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.64988 0.64235 0.59687 0.08124  0.11056  -0.08695 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.64050 0.64298 0.60582 0.08916  0.11119  -0.08020 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.66920 0.66868 0.61068 0.07234  0.10282  -0.08227 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.58412 0.60049 0.56182 0.08548  0.10502  -0.07104 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.61875 0.62830 0.57136 0.07105  0.09741  -0.07114 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.59766 0.61428 0.56832 0.07625  0.09890  -0.06651 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.61032 0.63588 0.59173 0.07261  0.09485  -0.05821 31  TYR A OH  
253  N N   . ASP A 32  ? 0.67090 0.61143 0.62362 0.09712  0.11325  -0.08905 32  ASP A N   
254  C CA  . ASP A 32  ? 0.70260 0.64443 0.66840 0.11149  0.11299  -0.08071 32  ASP A CA  
255  C C   . ASP A 32  ? 0.69975 0.65526 0.67627 0.10643  0.10094  -0.07160 32  ASP A C   
256  O O   . ASP A 32  ? 0.71764 0.65983 0.68827 0.09873  0.09612  -0.07096 32  ASP A O   
257  C CB  . ASP A 32  ? 0.81056 0.71942 0.76715 0.12059  0.12131  -0.08288 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.81995 0.73344 0.78707 0.14140  0.12336  -0.07379 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.82220 0.76842 0.80604 0.14579  0.11619  -0.06735 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.88375 0.76866 0.84167 0.15370  0.13312  -0.07344 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.64967 0.63232 0.64193 0.10945  0.09702  -0.06593 33  ASP A N   
262  C CA  . ASP A 33  ? 0.70025 0.69494 0.70272 0.10500  0.08695  -0.05893 33  ASP A CA  
263  C C   . ASP A 33  ? 0.72765 0.72698 0.73988 0.11831  0.08450  -0.05365 33  ASP A C   
264  O O   . ASP A 33  ? 0.72024 0.73446 0.74264 0.11607  0.07647  -0.04909 33  ASP A O   
265  C CB  . ASP A 33  ? 0.65024 0.66970 0.66313 0.09737  0.08513  -0.05716 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.70063 0.74451 0.72867 0.10530  0.09026  -0.05816 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.73750 0.78190 0.76787 0.11961  0.09447  -0.05944 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.68599 0.74895 0.72350 0.09733  0.09119  -0.05765 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.71312 0.69989 0.72094 0.13330  0.09196  -0.05408 34  VAL A N   
270  C CA  . VAL A 34  ? 0.72409 0.71435 0.73724 0.14993  0.09064  -0.04718 34  VAL A CA  
271  C C   . VAL A 34  ? 0.75165 0.70908 0.75098 0.14888  0.09071  -0.04377 34  VAL A C   
272  O O   . VAL A 34  ? 0.73410 0.69716 0.73720 0.14907  0.08301  -0.03753 34  VAL A O   
273  C CB  . VAL A 34  ? 0.69589 0.69000 0.71040 0.17076  0.10027  -0.04715 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.65602 0.65940 0.67507 0.19134  0.09830  -0.03812 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.72809 0.75671 0.75698 0.16931  0.10145  -0.05180 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.76785 0.69115 0.75090 0.14636  0.10038  -0.04896 35  GLU A N   
277  C CA  . GLU A 35  ? 0.76693 0.65639 0.73630 0.14151  0.10344  -0.04792 35  GLU A CA  
278  C C   . GLU A 35  ? 0.76138 0.63600 0.72027 0.12033  0.10484  -0.05870 35  GLU A C   
279  O O   . GLU A 35  ? 0.78608 0.62947 0.73084 0.11700  0.11604  -0.06616 35  GLU A O   
280  C CB  . GLU A 35  ? 0.80979 0.66771 0.76767 0.15990  0.11722  -0.04452 35  GLU A CB  
281  C CG  . GLU A 35  ? 0.82013 0.69305 0.78502 0.18379  0.11545  -0.03182 35  GLU A CG  
282  C CD  . GLU A 35  ? 0.99347 0.83207 0.94386 0.20577  0.13149  -0.02666 35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.00449 0.81463 0.94356 0.20431  0.14453  -0.03509 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.01244 0.85153 0.96116 0.22538  0.13199  -0.01410 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.72559 0.62261 0.69025 0.10599  0.09441  -0.06030 36  PRO A N   
286  C CA  . PRO A 36  ? 0.73440 0.62440 0.68879 0.08793  0.09429  -0.06985 36  PRO A CA  
287  C C   . PRO A 36  ? 0.71507 0.58465 0.66228 0.07911  0.09469  -0.07053 36  PRO A C   
288  O O   . PRO A 36  ? 0.74876 0.61365 0.69976 0.08543  0.09219  -0.06136 36  PRO A O   
289  C CB  . PRO A 36  ? 0.67732 0.59788 0.63977 0.08036  0.08337  -0.06722 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.68139 0.61674 0.65771 0.08870  0.07648  -0.05672 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.70559 0.63503 0.68531 0.10573  0.08325  -0.05384 36  PRO A CD  
292  N N   . GLU A 37  ? 0.72226 0.58190 0.65869 0.06375  0.09857  -0.08254 37  GLU A N   
293  C CA  . GLU A 37  ? 0.66897 0.51736 0.60043 0.05028  0.09835  -0.08584 37  GLU A CA  
294  C C   . GLU A 37  ? 0.66594 0.54334 0.59993 0.03664  0.08672  -0.08880 37  GLU A C   
295  O O   . GLU A 37  ? 0.68202 0.55992 0.61589 0.02687  0.08368  -0.08930 37  GLU A O   
296  C CB  . GLU A 37  ? 0.75032 0.56615 0.66776 0.04073  0.11332  -0.09974 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.86049 0.64443 0.77171 0.05637  0.12779  -0.09814 37  GLU A CG  
298  C CD  . GLU A 37  ? 0.93872 0.67900 0.83524 0.04749  0.14536  -0.10845 37  GLU A CD  
299  O OE1 . GLU A 37  ? 0.97379 0.70169 0.86835 0.03695  0.14703  -0.10756 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 0.97274 0.68980 0.85928 0.05034  0.15888  -0.11802 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.65426 0.55591 0.58963 0.03704  0.08128  -0.09000 38  ILE A N   
302  C CA  . ILE A 38  ? 0.54918 0.47935 0.48536 0.02946  0.07082  -0.08948 38  ILE A CA  
303  C C   . ILE A 38  ? 0.52345 0.47161 0.46782 0.03962  0.06479  -0.07823 38  ILE A C   
304  O O   . ILE A 38  ? 0.54377 0.49306 0.48842 0.04612  0.06932  -0.07850 38  ILE A O   
305  C CB  . ILE A 38  ? 0.59293 0.53463 0.51768 0.01812  0.07276  -0.10390 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.66904 0.59379 0.58686 0.00382  0.08000  -0.11799 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.59805 0.57281 0.52218 0.01581  0.06206  -0.10027 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.72988 0.65981 0.65259 -0.00394 0.07452  -0.11504 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.52949 0.49054 0.48049 0.04033  0.05608  -0.06911 39  VAL A N   
310  C CA  . VAL A 39  ? 0.50746 0.48268 0.46550 0.04695  0.05209  -0.05966 39  VAL A CA  
311  C C   . VAL A 39  ? 0.49961 0.49304 0.45136 0.04307  0.04669  -0.05768 39  VAL A C   
312  O O   . VAL A 39  ? 0.48682 0.48616 0.43787 0.03928  0.04099  -0.05652 39  VAL A O   
313  C CB  . VAL A 39  ? 0.48138 0.45458 0.45158 0.05279  0.04820  -0.05084 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.46592 0.45288 0.44234 0.05511  0.04513  -0.04368 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.55240 0.51423 0.52811 0.06121  0.05364  -0.05087 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.50660 0.50980 0.45276 0.04539  0.04928  -0.05666 40  ILE A N   
317  C CA  . ILE A 40  ? 0.48413 0.50442 0.42152 0.04606  0.04582  -0.05199 40  ILE A CA  
318  C C   . ILE A 40  ? 0.48136 0.50077 0.42439 0.05214  0.04701  -0.03998 40  ILE A C   
319  O O   . ILE A 40  ? 0.50122 0.51465 0.45146 0.05416  0.05255  -0.03861 40  ILE A O   
320  C CB  . ILE A 40  ? 0.54137 0.57322 0.46463 0.04489  0.04946  -0.05892 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.56343 0.59461 0.48146 0.03571  0.04991  -0.07426 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.47431 0.52626 0.38606 0.04957  0.04627  -0.05148 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.58910 0.63553 0.49240 0.03309  0.05277  -0.08412 40  ILE A CD1 
324  N N   . SER A 41  ? 0.48464 0.51023 0.42467 0.05472  0.04291  -0.03208 41  SER A N   
325  C CA  . SER A 41  ? 0.51150 0.53140 0.45513 0.05901  0.04599  -0.02155 41  SER A CA  
326  C C   . SER A 41  ? 0.47303 0.50109 0.40092 0.06540  0.04832  -0.01327 41  SER A C   
327  O O   . SER A 41  ? 0.48064 0.52199 0.39985 0.06838  0.04256  -0.01244 41  SER A O   
328  C CB  . SER A 41  ? 0.50171 0.51581 0.45555 0.05856  0.04083  -0.01860 41  SER A CB  
329  O OG  . SER A 41  ? 0.54356 0.55164 0.49685 0.06209  0.04436  -0.00952 41  SER A OG  
330  N N   . ILE A 42  ? 0.48208 0.50395 0.40587 0.06820  0.05753  -0.00684 42  ILE A N   
331  C CA  . ILE A 42  ? 0.54886 0.57497 0.45455 0.07686  0.06264  0.00363  42  ILE A CA  
332  C C   . ILE A 42  ? 0.52645 0.53345 0.43377 0.07954  0.07092  0.01493  42  ILE A C   
333  O O   . ILE A 42  ? 0.54877 0.54340 0.46435 0.07406  0.07996  0.01493  42  ILE A O   
334  C CB  . ILE A 42  ? 0.56733 0.60015 0.46220 0.07791  0.06957  0.00208  42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.53283 0.58004 0.42732 0.07278  0.06333  -0.01242 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.63839 0.67871 0.51108 0.08955  0.07415  0.01421  42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.52509 0.57984 0.40833 0.07377  0.07013  -0.01595 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.54715 0.55229 0.44659 0.08760  0.06899  0.02361  43  GLY A N   
339  C CA  . GLY A 43  ? 0.59401 0.57633 0.49300 0.09022  0.07829  0.03341  43  GLY A CA  
340  C C   . GLY A 43  ? 0.63184 0.61352 0.52869 0.09748  0.07241  0.03804  43  GLY A C   
341  O O   . GLY A 43  ? 0.70430 0.70155 0.58700 0.10932  0.06796  0.04403  43  GLY A O   
342  N N   . GLY A 44  ? 0.59637 0.56366 0.50715 0.09108  0.07234  0.03468  44  GLY A N   
343  C CA  . GLY A 44  ? 0.53422 0.50039 0.44420 0.09749  0.06726  0.03784  44  GLY A CA  
344  C C   . GLY A 44  ? 0.51267 0.48812 0.44016 0.08865  0.05562  0.02648  44  GLY A C   
345  O O   . GLY A 44  ? 0.47858 0.46365 0.41619 0.08002  0.05036  0.01709  44  GLY A O   
346  N N   . ASP A 45  ? 0.54984 0.52119 0.47956 0.09207  0.05268  0.02796  45  ASP A N   
347  C CA  . ASP A 45  ? 0.44692 0.42587 0.39153 0.08456  0.04298  0.01862  45  ASP A CA  
348  C C   . ASP A 45  ? 0.43705 0.40524 0.39656 0.07340  0.04589  0.01097  45  ASP A C   
349  O O   . ASP A 45  ? 0.47307 0.45089 0.44395 0.06726  0.03874  0.00310  45  ASP A O   
350  C CB  . ASP A 45  ? 0.46321 0.44259 0.40538 0.09192  0.03979  0.02222  45  ASP A CB  
351  C CG  . ASP A 45  ? 0.49877 0.50140 0.43115 0.10164  0.03324  0.02635  45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.51856 0.54077 0.45253 0.09675  0.02667  0.02048  45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.49728 0.49986 0.42041 0.11418  0.03532  0.03458  45  ASP A OD2 
354  N N   . GLY A 46  ? 0.45235 0.40183 0.41163 0.07081  0.05723  0.01291  46  GLY A N   
355  C CA  . GLY A 46  ? 0.44672 0.39402 0.42145 0.05898  0.06019  0.00369  46  GLY A CA  
356  C C   . GLY A 46  ? 0.49372 0.45462 0.47494 0.05472  0.05797  -0.00102 46  GLY A C   
357  O O   . GLY A 46  ? 0.48832 0.46061 0.48312 0.04977  0.05228  -0.00916 46  GLY A O   
358  N N   . THR A 47  ? 0.54001 0.50046 0.51010 0.05844  0.06297  0.00452  47  THR A N   
359  C CA  . THR A 47  ? 0.44938 0.42195 0.42324 0.05583  0.06158  -0.00021 47  THR A CA  
360  C C   . THR A 47  ? 0.42376 0.40955 0.40190 0.05678  0.04969  -0.00588 47  THR A C   
361  O O   . THR A 47  ? 0.46941 0.46185 0.45753 0.05363  0.04778  -0.01258 47  THR A O   
362  C CB  . THR A 47  ? 0.57228 0.54393 0.52984 0.06124  0.06808  0.00690  47  THR A CB  
363  O OG1 . THR A 47  ? 0.64609 0.60039 0.59776 0.06069  0.08191  0.01389  47  THR A OG1 
364  C CG2 . THR A 47  ? 0.45595 0.43883 0.41651 0.05843  0.06821  0.00084  47  THR A CG2 
365  N N   . PHE A 48  ? 0.44485 0.43430 0.41534 0.06147  0.04290  -0.00315 48  PHE A N   
366  C CA  . PHE A 48  ? 0.47406 0.47256 0.44834 0.06008  0.03405  -0.00885 48  PHE A CA  
367  C C   . PHE A 48  ? 0.49291 0.48976 0.48057 0.05728  0.03036  -0.01280 48  PHE A C   
368  O O   . PHE A 48  ? 0.52457 0.52428 0.51815 0.05598  0.02777  -0.01765 48  PHE A O   
369  C CB  . PHE A 48  ? 0.43065 0.43779 0.39542 0.06399  0.02850  -0.00612 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.51234 0.52725 0.47982 0.05971  0.02218  -0.01293 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.53235 0.54492 0.50784 0.05791  0.01792  -0.01440 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.50086 0.52390 0.46197 0.05668  0.02204  -0.01852 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.45735 0.47252 0.43391 0.05333  0.01495  -0.01970 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.55114 0.57648 0.51417 0.05045  0.01915  -0.02596 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.49105 0.51083 0.46163 0.04884  0.01627  -0.02575 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.44177 0.43366 0.43274 0.05746  0.03087  -0.01072 49  LEU A N   
377  C CA  . LEU A 49  ? 0.50726 0.50190 0.50989 0.05524  0.02711  -0.01529 49  LEU A CA  
378  C C   . LEU A 49  ? 0.50030 0.50100 0.51416 0.05214  0.02971  -0.02081 49  LEU A C   
379  O O   . LEU A 49  ? 0.46919 0.47800 0.49022 0.05385  0.02515  -0.02415 49  LEU A O   
380  C CB  . LEU A 49  ? 0.50763 0.49553 0.51096 0.05472  0.02902  -0.01429 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.43887 0.42505 0.43411 0.05999  0.02508  -0.00966 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.47488 0.44775 0.46668 0.06117  0.03153  -0.00751 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.44031 0.43530 0.44078 0.06015  0.01700  -0.01263 49  LEU A CD2 
384  N N   . SER A 50  ? 0.50533 0.50362 0.52033 0.04870  0.03786  -0.02117 50  SER A N   
385  C CA  . SER A 50  ? 0.49565 0.50499 0.52246 0.04601  0.04083  -0.02698 50  SER A CA  
386  C C   . SER A 50  ? 0.49426 0.50876 0.51987 0.05140  0.03774  -0.02785 50  SER A C   
387  O O   . SER A 50  ? 0.52240 0.54853 0.55785 0.05419  0.03629  -0.03188 50  SER A O   
388  C CB  . SER A 50  ? 0.51657 0.52160 0.54328 0.04044  0.05199  -0.02666 50  SER A CB  
389  O OG  . SER A 50  ? 0.59985 0.60085 0.63279 0.03274  0.05780  -0.02973 50  SER A OG  
390  N N   . ALA A 51  ? 0.49041 0.49723 0.50334 0.05350  0.03744  -0.02468 51  ALA A N   
391  C CA  . ALA A 51  ? 0.51120 0.51809 0.52119 0.05682  0.03694  -0.02736 51  ALA A CA  
392  C C   . ALA A 51  ? 0.51017 0.51521 0.52184 0.06032  0.03121  -0.02799 51  ALA A C   
393  O O   . ALA A 51  ? 0.50749 0.51215 0.52176 0.06521  0.03253  -0.03010 51  ALA A O   
394  C CB  . ALA A 51  ? 0.52203 0.52432 0.51775 0.05587  0.03850  -0.02648 51  ALA A CB  
395  N N   . PHE A 52  ? 0.48085 0.48361 0.48981 0.05913  0.02613  -0.02533 52  PHE A N   
396  C CA  . PHE A 52  ? 0.51537 0.51568 0.52489 0.06213  0.02201  -0.02473 52  PHE A CA  
397  C C   . PHE A 52  ? 0.48742 0.49666 0.50730 0.06789  0.02091  -0.02533 52  PHE A C   
398  O O   . PHE A 52  ? 0.50907 0.51531 0.52811 0.07461  0.02136  -0.02436 52  PHE A O   
399  C CB  . PHE A 52  ? 0.50463 0.50473 0.51067 0.05984  0.01731  -0.02190 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.51018 0.51002 0.51795 0.06291  0.01368  -0.02034 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.52756 0.51847 0.52909 0.06265  0.01482  -0.01988 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.51783 0.52597 0.53241 0.06529  0.01033  -0.01992 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.51301 0.50173 0.51411 0.06620  0.01324  -0.01673 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.47417 0.48399 0.48839 0.06947  0.00714  -0.01773 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.45489 0.45423 0.46187 0.07067  0.00886  -0.01498 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.50659 0.52757 0.53561 0.06565  0.02044  -0.02728 53  HIS A N   
407  C CA  . HIS A 53  ? 0.50672 0.54488 0.54684 0.07039  0.01833  -0.02999 53  HIS A CA  
408  C C   . HIS A 53  ? 0.56426 0.61207 0.61045 0.07587  0.02240  -0.03228 53  HIS A C   
409  O O   . HIS A 53  ? 0.57490 0.63909 0.62801 0.08458  0.02034  -0.03305 53  HIS A O   
410  C CB  . HIS A 53  ? 0.43960 0.48879 0.48831 0.06317  0.01782  -0.03459 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.50347 0.54657 0.54738 0.06121  0.01357  -0.03299 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.50128 0.55138 0.54472 0.06717  0.00763  -0.03183 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.56556 0.59630 0.60370 0.05575  0.01522  -0.03156 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.50608 0.54946 0.54483 0.06409  0.00553  -0.03093 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.52917 0.56064 0.56481 0.05781  0.01006  -0.03071 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.56714 0.60761 0.61014 0.07257  0.02826  -0.03313 54  GLN A N   
417  C CA  . GLN A 54  ? 0.52188 0.57103 0.56986 0.07874  0.03308  -0.03546 54  GLN A CA  
418  C C   . GLN A 54  ? 0.51083 0.54891 0.55128 0.09041  0.03383  -0.03238 54  GLN A C   
419  O O   . GLN A 54  ? 0.57991 0.62826 0.62532 0.10120  0.03662  -0.03286 54  GLN A O   
420  C CB  . GLN A 54  ? 0.54057 0.58336 0.58462 0.07224  0.03992  -0.03698 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.57226 0.62716 0.62302 0.07700  0.04618  -0.04041 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.70936 0.75780 0.75403 0.07038  0.05345  -0.04126 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.72086 0.76145 0.75971 0.06201  0.05432  -0.03899 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.70890 0.76044 0.75328 0.07588  0.05947  -0.04382 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.54260 0.55985 0.57097 0.08877  0.03263  -0.02924 55  TYR A N   
426  C CA  . TYR A 55  ? 0.55229 0.55102 0.57096 0.09694  0.03673  -0.02683 55  TYR A CA  
427  C C   . TYR A 55  ? 0.61387 0.60393 0.62715 0.09913  0.03320  -0.02169 55  TYR A C   
428  O O   . TYR A 55  ? 0.64678 0.61411 0.64895 0.09970  0.03801  -0.01999 55  TYR A O   
429  C CB  . TYR A 55  ? 0.61817 0.59738 0.62569 0.08987  0.04256  -0.03071 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.61821 0.60419 0.62830 0.08970  0.04762  -0.03525 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.62778 0.61298 0.63917 0.10106  0.05416  -0.03629 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.60424 0.59727 0.61420 0.07987  0.04696  -0.03750 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.68198 0.67510 0.69592 0.10106  0.05944  -0.04069 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.65832 0.65760 0.66940 0.07978  0.05274  -0.04090 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.67806 0.67826 0.69183 0.08959  0.05875  -0.04310 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.66114 0.66916 0.67621 0.08964  0.06515  -0.04678 55  TYR A OH  
437  N N   . GLU A 56  ? 0.70261 0.70996 0.72315 0.09943  0.02611  -0.02000 56  GLU A N   
438  C CA  . GLU A 56  ? 0.75720 0.75874 0.77211 0.10257  0.02309  -0.01469 56  GLU A CA  
439  C C   . GLU A 56  ? 0.66203 0.65623 0.67095 0.11858  0.02750  -0.00827 56  GLU A C   
440  O O   . GLU A 56  ? 0.69381 0.67684 0.69442 0.12197  0.02802  -0.00231 56  GLU A O   
441  C CB  . GLU A 56  ? 0.62490 0.64823 0.64825 0.10021  0.01509  -0.01577 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.64481 0.69679 0.68136 0.10533  0.01262  -0.01984 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.71688 0.78770 0.76157 0.09809  0.00651  -0.02473 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.61548 0.67594 0.65437 0.09236  0.00399  -0.02317 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.85684 0.95367 0.91400 0.09752  0.00506  -0.03127 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.66625 0.66589 0.67809 0.12975  0.03184  -0.00844 57  GLU A N   
447  C CA  . GLU A 57  ? 0.74900 0.73869 0.75270 0.14874  0.03815  -0.00072 57  GLU A CA  
448  C C   . GLU A 57  ? 0.72364 0.67332 0.71260 0.14796  0.05026  0.00036  57  GLU A C   
449  O O   . GLU A 57  ? 0.79253 0.72456 0.77140 0.16419  0.05893  0.00766  57  GLU A O   
450  C CB  . GLU A 57  ? 0.74248 0.76045 0.75654 0.16375  0.03779  -0.00148 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.82845 0.87464 0.84553 0.18178  0.03250  0.00479  57  GLU A CG  
452  C CD  . GLU A 57  ? 0.83410 0.91228 0.86296 0.17150  0.02084  -0.00068 57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.80458 0.87095 0.82704 0.16357  0.01767  0.00148  57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.83861 0.95398 0.88332 0.17062  0.01590  -0.00820 57  GLU A OE2 
455  N N   . ARG A 58  ? 0.68016 0.61545 0.66664 0.13007  0.05198  -0.00709 58  ARG A N   
456  C CA  . ARG A 58  ? 0.72748 0.62780 0.70085 0.12535  0.06381  -0.01022 58  ARG A CA  
457  C C   . ARG A 58  ? 0.71624 0.60754 0.68572 0.10458  0.06223  -0.01617 58  ARG A C   
458  O O   . ARG A 58  ? 0.75523 0.63362 0.71941 0.09323  0.06761  -0.02485 58  ARG A O   
459  C CB  . ARG A 58  ? 0.74259 0.64180 0.71725 0.12763  0.06953  -0.01688 58  ARG A CB  
460  C CG  . ARG A 58  ? 0.79171 0.69463 0.76738 0.15050  0.07502  -0.01132 58  ARG A CG  
461  C CD  . ARG A 58  ? 0.82994 0.72948 0.80568 0.15264  0.08244  -0.01859 58  ARG A CD  
462  N NE  . ARG A 58  ? 0.82442 0.68415 0.78449 0.14611  0.09539  -0.02443 58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.81169 0.66590 0.76881 0.12758  0.09628  -0.03570 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.73435 0.61679 0.70135 0.11584  0.08587  -0.03993 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.81248 0.63197 0.75525 0.12100  0.10892  -0.04317 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.70461 0.60605 0.67662 0.09992  0.05479  -0.01235 59  LEU A N   
467  C CA  . LEU A 59  ? 0.68657 0.58806 0.65712 0.08200  0.05188  -0.01780 59  LEU A CA  
468  C C   . LEU A 59  ? 0.74661 0.61862 0.70521 0.07242  0.06339  -0.02214 59  LEU A C   
469  O O   . LEU A 59  ? 0.73845 0.61194 0.69548 0.05668  0.06370  -0.03164 59  LEU A O   
470  C CB  . LEU A 59  ? 0.60230 0.51964 0.57739 0.08128  0.04306  -0.01245 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.62749 0.57303 0.61449 0.08527  0.03280  -0.01198 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.55067 0.50894 0.54052 0.08455  0.02551  -0.00823 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.56830 0.52295 0.55912 0.07578  0.03044  -0.01888 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.75998 0.60559 0.70931 0.08173  0.07399  -0.01571 60  ASP A N   
475  C CA  . ASP A 60  ? 0.81072 0.62266 0.74780 0.07077  0.08829  -0.02052 60  ASP A CA  
476  C C   . ASP A 60  ? 0.79538 0.58991 0.72698 0.06525  0.09784  -0.03188 60  ASP A C   
477  O O   . ASP A 60  ? 0.85146 0.62111 0.77404 0.05061  0.10968  -0.04091 60  ASP A O   
478  C CB  . ASP A 60  ? 0.87293 0.65633 0.79884 0.08437  0.09961  -0.00822 60  ASP A CB  
479  C CG  . ASP A 60  ? 0.95785 0.72018 0.87567 0.06905  0.10886  -0.00922 60  ASP A CG  
480  O OD1 . ASP A 60  ? 0.97335 0.75914 0.89867 0.05609  0.09932  -0.01218 60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.02776 0.74932 0.93141 0.07025  0.12699  -0.00690 60  ASP A OD2 
482  N N   . GLU A 61  ? 0.75973 0.56775 0.69665 0.07512  0.09382  -0.03304 61  GLU A N   
483  C CA  . GLU A 61  ? 0.76804 0.56075 0.69903 0.07217  0.10320  -0.04366 61  GLU A CA  
484  C C   . GLU A 61  ? 0.75177 0.57279 0.68945 0.06041  0.09388  -0.05411 61  GLU A C   
485  O O   . GLU A 61  ? 0.74086 0.55641 0.67459 0.05964  0.09966  -0.06275 61  GLU A O   
486  C CB  . GLU A 61  ? 0.83363 0.61702 0.76303 0.09530  0.10941  -0.03647 61  GLU A CB  
487  C CG  . GLU A 61  ? 0.90051 0.65024 0.81827 0.11104  0.12240  -0.02526 61  GLU A CG  
488  C CD  . GLU A 61  ? 0.90347 0.67551 0.82790 0.13074  0.11318  -0.00970 61  GLU A CD  
489  O OE1 . GLU A 61  ? 0.87495 0.68580 0.81384 0.13524  0.09936  -0.00914 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 0.90645 0.65759 0.82093 0.14119  0.12064  0.00143  61  GLU A OE2 
491  N N   . ILE A 62  ? 0.73166 0.58160 0.67763 0.05262  0.08074  -0.05297 62  ILE A N   
492  C CA  . ILE A 62  ? 0.65576 0.53332 0.60664 0.04632  0.07206  -0.05866 62  ILE A CA  
493  C C   . ILE A 62  ? 0.64795 0.54220 0.59905 0.03110  0.06536  -0.06326 62  ILE A C   
494  O O   . ILE A 62  ? 0.60055 0.49831 0.55489 0.02980  0.06119  -0.05732 62  ILE A O   
495  C CB  . ILE A 62  ? 0.62536 0.52585 0.58751 0.05849  0.06288  -0.04965 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.66148 0.55492 0.62515 0.07326  0.06908  -0.04730 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.55370 0.47883 0.51884 0.05183  0.05541  -0.05273 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.64242 0.56074 0.61896 0.08314  0.06145  -0.04039 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.59299 0.50071 0.54021 0.02088  0.06435  -0.07385 63  ALA A N   
500  C CA  . ALA A 63  ? 0.54535 0.47955 0.49345 0.01040  0.05611  -0.07748 63  ALA A CA  
501  C C   . ALA A 63  ? 0.54283 0.50210 0.49351 0.01715  0.04764  -0.07283 63  ALA A C   
502  O O   . ALA A 63  ? 0.59351 0.55367 0.54038 0.01989  0.05063  -0.07645 63  ALA A O   
503  C CB  . ALA A 63  ? 0.65661 0.59196 0.59673 -0.00672 0.06191  -0.09413 63  ALA A CB  
504  N N   . PHE A 64  ? 0.51608 0.49332 0.47200 0.02019  0.03876  -0.06458 64  PHE A N   
505  C CA  . PHE A 64  ? 0.50212 0.49648 0.45927 0.02771  0.03325  -0.05779 64  PHE A CA  
506  C C   . PHE A 64  ? 0.54032 0.55976 0.48998 0.02337  0.02929  -0.06211 64  PHE A C   
507  O O   . PHE A 64  ? 0.54612 0.57796 0.49389 0.01480  0.02720  -0.06864 64  PHE A O   
508  C CB  . PHE A 64  ? 0.51898 0.51556 0.48440 0.03495  0.02771  -0.04646 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.49900 0.48042 0.47195 0.04182  0.03002  -0.04175 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.52161 0.48920 0.49607 0.04183  0.03211  -0.04119 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.46156 0.44507 0.43973 0.04858  0.03079  -0.03783 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.49308 0.45210 0.47315 0.05111  0.03362  -0.03606 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.45597 0.43383 0.44224 0.05536  0.03203  -0.03487 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.49935 0.46644 0.48611 0.05796  0.03277  -0.03360 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.53111 0.56029 0.47616 0.02980  0.02895  -0.05832 65  ILE A N   
516  C CA  . ILE A 65  ? 0.54771 0.60330 0.48367 0.03142  0.02494  -0.05805 65  ILE A CA  
517  C C   . ILE A 65  ? 0.49119 0.54714 0.42588 0.04324  0.02491  -0.04453 65  ILE A C   
518  O O   . ILE A 65  ? 0.52067 0.56178 0.45862 0.04649  0.02994  -0.04109 65  ILE A O   
519  C CB  . ILE A 65  ? 0.50887 0.57575 0.43410 0.02553  0.02810  -0.07044 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.56866 0.63318 0.49425 0.01083  0.03042  -0.08623 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.54044 0.63928 0.45458 0.03101  0.02351  -0.06803 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.68582 0.72311 0.61052 0.00647  0.03978  -0.09465 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.54107 0.61381 0.47086 0.04979  0.02060  -0.03706 66  GLY A N   
524  C CA  . GLY A 66  ? 0.53488 0.60325 0.46023 0.06089  0.02355  -0.02400 66  GLY A CA  
525  C C   . GLY A 66  ? 0.61310 0.70338 0.52233 0.06954  0.02349  -0.01939 66  GLY A C   
526  O O   . GLY A 66  ? 0.63851 0.75454 0.54248 0.07131  0.01750  -0.02168 66  GLY A O   
527  N N   . ILE A 67  ? 0.59969 0.68265 0.50064 0.07562  0.03059  -0.01266 67  ILE A N   
528  C CA  . ILE A 67  ? 0.54703 0.64753 0.42957 0.08747  0.03256  -0.00444 67  ILE A CA  
529  C C   . ILE A 67  ? 0.63241 0.71419 0.51074 0.09911  0.03945  0.01266  67  ILE A C   
530  O O   . ILE A 67  ? 0.70123 0.75654 0.58791 0.09521  0.04669  0.01557  67  ILE A O   
531  C CB  . ILE A 67  ? 0.60420 0.70873 0.47729 0.08570  0.03795  -0.00937 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.54990 0.66732 0.42667 0.07278  0.03331  -0.02837 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.63702 0.76080 0.48833 0.10017  0.04067  0.00101  67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.50176 0.61507 0.37317 0.06918  0.03988  -0.03546 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.66632 0.76217 0.53172 0.11340  0.03819  0.02330  68  HIS A N   
536  C CA  . HIS A 68  ? 0.68389 0.75710 0.54219 0.12587  0.04719  0.04008  68  HIS A CA  
537  C C   . HIS A 68  ? 0.79376 0.86748 0.63017 0.13904  0.05693  0.05248  68  HIS A C   
538  O O   . HIS A 68  ? 0.81136 0.91509 0.63133 0.15165  0.05307  0.05640  68  HIS A O   
539  C CB  . HIS A 68  ? 0.80852 0.89119 0.66583 0.13630  0.04183  0.04604  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.81982 0.94121 0.66131 0.15117  0.03591  0.05014  68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.93172 1.05506 0.75110 0.17270  0.04338  0.06746  68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.82190 0.98414 0.66623 0.14788  0.02387  0.03883  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.90066 1.06887 0.71002 0.18395  0.03464  0.06696  68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.87099 1.06484 0.69631 0.16761  0.02261  0.04843  68  HIS A NE2 
545  N N   . THR A 69  ? 0.80078 0.84415 0.63688 0.13582  0.06997  0.05816  69  THR A N   
546  C CA  . THR A 69  ? 0.89019 0.92699 0.70429 0.14843  0.08267  0.07251  69  THR A CA  
547  C C   . THR A 69  ? 1.04910 1.06343 0.84845 0.16548  0.09360  0.09184  69  THR A C   
548  O O   . THR A 69  ? 1.02719 1.03830 0.80289 0.18152  0.10427  0.10738  69  THR A O   
549  C CB  . THR A 69  ? 0.82665 0.84217 0.64683 0.13613  0.09399  0.06946  69  THR A CB  
550  O OG1 . THR A 69  ? 0.73728 0.72850 0.57971 0.12186  0.09614  0.06294  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.83482 0.87476 0.65829 0.12735  0.08692  0.05494  69  THR A CG2 
552  N N   . GLY A 70  ? 1.02886 1.02605 0.83993 0.16335  0.09240  0.09155  70  GLY A N   
553  C CA  . GLY A 70  ? 1.03971 1.01632 0.83633 0.18111  0.10195  0.10829  70  GLY A CA  
554  C C   . GLY A 70  ? 1.04886 1.05669 0.84256 0.19500  0.08862  0.10938  70  GLY A C   
555  O O   . GLY A 70  ? 0.99118 1.04135 0.77925 0.20057  0.07701  0.10553  70  GLY A O   
556  N N   . HIS A 71  ? 1.25206 1.24208 1.05015 0.19976  0.09046  0.11302  71  HIS A N   
557  C CA  . HIS A 71  ? 1.28248 1.30414 1.08034 0.21238  0.07822  0.11328  71  HIS A CA  
558  C C   . HIS A 71  ? 1.23455 1.28804 1.05513 0.19336  0.06017  0.09282  71  HIS A C   
559  O O   . HIS A 71  ? 1.17502 1.21971 1.01144 0.17229  0.05796  0.07974  71  HIS A O   
560  C CB  . HIS A 71  ? 1.23157 1.22301 1.02843 0.22192  0.08627  0.12150  71  HIS A CB  
561  C CG  . HIS A 71  ? 1.27560 1.24086 1.09535 0.19987  0.08605  0.10810  71  HIS A CG  
562  N ND1 . HIS A 71  ? 1.22317 1.21138 1.06408 0.18555  0.07046  0.09229  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 1.28303 1.20337 1.10708 0.18970  0.10008  0.10772  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 1.13180 1.09224 0.98794 0.16986  0.07387  0.08398  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.23556 1.15683 1.08288 0.17110  0.09118  0.09178  71  HIS A NE2 
566  N N   . LEU A 72  ? 1.04950 1.14051 0.87110 0.20172  0.04843  0.09053  72  LEU A N   
567  C CA  . LEU A 72  ? 0.95548 1.07286 0.79753 0.18356  0.03394  0.07201  72  LEU A CA  
568  C C   . LEU A 72  ? 0.95443 1.04071 0.81531 0.16888  0.03484  0.06529  72  LEU A C   
569  O O   . LEU A 72  ? 0.99465 1.06026 0.85433 0.17769  0.04035  0.07302  72  LEU A O   
570  C CB  . LEU A 72  ? 0.84824 1.01322 0.68818 0.19525  0.02324  0.07120  72  LEU A CB  
571  C CG  . LEU A 72  ? 0.82585 1.01489 0.68661 0.17721  0.01102  0.05367  72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.73119 0.93096 0.60070 0.15507  0.00578  0.03655  72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.72158 0.95970 0.58031 0.19023  0.00261  0.05413  72  LEU A CD2 
574  N N   . GLY A 73  ? 0.83317 0.91604 0.70999 0.14770  0.03020  0.05091  73  GLY A N   
575  C CA  . GLY A 73  ? 0.72153 0.78426 0.61601 0.13449  0.02878  0.04338  73  GLY A CA  
576  C C   . GLY A 73  ? 0.64356 0.73310 0.55019 0.12534  0.01702  0.03185  73  GLY A C   
577  O O   . GLY A 73  ? 0.67902 0.80043 0.58333 0.12314  0.01058  0.02563  73  GLY A O   
578  N N   . PHE A 74  ? 0.56608 0.64394 0.48511 0.11903  0.01506  0.02809  74  PHE A N   
579  C CA  . PHE A 74  ? 0.54753 0.64776 0.47720 0.10976  0.00614  0.01823  74  PHE A CA  
580  C C   . PHE A 74  ? 0.53422 0.63439 0.47177 0.09269  0.00373  0.00624  74  PHE A C   
581  O O   . PHE A 74  ? 0.58543 0.70954 0.52552 0.08475  -0.00135 -0.00273 74  PHE A O   
582  C CB  . PHE A 74  ? 0.47927 0.56666 0.41784 0.10912  0.00569  0.01857  74  PHE A CB  
583  C CG  . PHE A 74  ? 0.44400 0.55271 0.37917 0.12149  0.00303  0.02344  74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.46226 0.56313 0.38536 0.14023  0.00904  0.03564  74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.45238 0.58941 0.39560 0.11510  -0.00402 0.01611  74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.51407 0.63663 0.43340 0.15481  0.00711  0.04090  74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.46548 0.62771 0.40677 0.12728  -0.00641 0.02020  74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.48526 0.64141 0.41462 0.14843  -0.00136 0.03285  74  PHE A CZ  
589  N N   . TYR A 75  ? 0.52860 0.60248 0.47002 0.08680  0.00843  0.00523  75  TYR A N   
590  C CA  . TYR A 75  ? 0.55194 0.62242 0.49950 0.07379  0.00777  -0.00487 75  TYR A CA  
591  C C   . TYR A 75  ? 0.54835 0.62658 0.48683 0.07358  0.01017  -0.00714 75  TYR A C   
592  O O   . TYR A 75  ? 0.60644 0.69353 0.54569 0.06408  0.00865  -0.01749 75  TYR A O   
593  C CB  . TYR A 75  ? 0.56966 0.61449 0.52683 0.06925  0.01102  -0.00547 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.52573 0.56488 0.49102 0.06892  0.00838  -0.00472 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.46093 0.50933 0.43074 0.06320  0.00394  -0.00965 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.46812 0.49230 0.43587 0.07321  0.01160  -0.00006 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.42717 0.47155 0.40287 0.06367  0.00202  -0.00843 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.48623 0.50731 0.46025 0.07296  0.00912  -0.00071 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.47394 0.50586 0.45150 0.06914  0.00394  -0.00414 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.47136 0.50126 0.45368 0.06973  0.00195  -0.00417 75  TYR A OH  
601  N N   . ALA A 76  ? 0.58320 0.65628 0.51178 0.08373  0.01536  0.00217  76  ALA A N   
602  C CA  . ALA A 76  ? 0.66858 0.75140 0.58558 0.08607  0.01823  0.00190  76  ALA A CA  
603  C C   . ALA A 76  ? 0.62956 0.74382 0.53382 0.09692  0.01418  0.00579  76  ALA A C   
604  O O   . ALA A 76  ? 0.67561 0.78932 0.56780 0.11228  0.01827  0.01889  76  ALA A O   
605  C CB  . ALA A 76  ? 0.65748 0.71710 0.56988 0.09093  0.02799  0.01063  76  ALA A CB  
606  N N   . ASP A 77  ? 0.57931 0.72223 0.48574 0.08920  0.00705  -0.00589 77  ASP A N   
607  C CA  . ASP A 77  ? 0.68167 0.86415 0.57979 0.09835  0.00125  -0.00481 77  ASP A CA  
608  C C   . ASP A 77  ? 0.72702 0.94131 0.61458 0.09599  -0.00102 -0.01389 77  ASP A C   
609  O O   . ASP A 77  ? 0.75192 1.00794 0.63744 0.09589  -0.00775 -0.02114 77  ASP A O   
610  C CB  . ASP A 77  ? 0.65678 0.85557 0.56718 0.09080  -0.00520 -0.01217 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.73543 0.92915 0.65727 0.06894  -0.00604 -0.02900 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.75381 0.93174 0.67397 0.06100  -0.00206 -0.03525 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.67929 0.88324 0.61091 0.06034  -0.00928 -0.03550 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.65389 0.85259 0.53479 0.09391  0.00468  -0.01467 78  TRP A N   
615  C CA  . TRP A 78  ? 0.74829 0.97584 0.61644 0.09330  0.00360  -0.02279 78  TRP A CA  
616  C C   . TRP A 78  ? 0.72489 0.94114 0.57648 0.10879  0.01119  -0.00792 78  TRP A C   
617  O O   . TRP A 78  ? 0.71456 0.89249 0.56922 0.11002  0.01924  0.00122  78  TRP A O   
618  C CB  . TRP A 78  ? 0.72312 0.94359 0.59873 0.07222  0.00461  -0.04264 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.78424 0.99800 0.67656 0.05628  0.00175  -0.05391 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.84149 1.01779 0.74608 0.04646  0.00601  -0.05632 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.86046 1.10719 0.75825 0.04947  -0.00495 -0.06313 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.81718 0.99697 0.73254 0.03446  0.00332  -0.06521 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.80798 1.03039 0.72038 0.03457  -0.00304 -0.07023 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.82350 1.12103 0.71525 0.05506  -0.01197 -0.06611 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.77719 1.02085 0.69841 0.02317  -0.00660 -0.08020 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.77329 1.09668 0.67595 0.04335  -0.01667 -0.07748 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.74436 1.03903 0.66167 0.02654  -0.01332 -0.08449 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.70120 0.95359 0.53471 0.12053  0.00920  -0.00576 79  ARG A N   
629  C CA  . ARG A 79  ? 0.76392 1.01017 0.57730 0.14017  0.01715  0.01257  79  ARG A CA  
630  C C   . ARG A 79  ? 0.77828 1.01334 0.58454 0.13363  0.02400  0.00745  79  ARG A C   
631  O O   . ARG A 79  ? 0.75609 1.00354 0.56748 0.11757  0.02045  -0.01199 79  ARG A O   
632  C CB  . ARG A 79  ? 0.81901 1.11349 0.61396 0.16013  0.01173  0.01964  79  ARG A CB  
633  C CG  . ARG A 79  ? 0.82098 1.12188 0.61732 0.17572  0.00891  0.03248  79  ARG A CG  
634  C CD  . ARG A 79  ? 0.83007 1.19468 0.61581 0.18924  -0.00101 0.03030  79  ARG A CD  
635  N NE  . ARG A 79  ? 0.80492 1.19721 0.56738 0.20188  0.00055  0.03401  79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.85716 1.31259 0.61157 0.20479  -0.00929 0.02258  79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.88321 1.38139 0.65233 0.19398  -0.02080 0.00556  79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.69648 1.17508 0.42753 0.21796  -0.00703 0.02737  79  ARG A NH2 
639  N N   . PRO A 80  ? 0.74508 0.95531 0.53882 0.14559  0.03546  0.02435  80  PRO A N   
640  C CA  . PRO A 80  ? 0.76887 0.96827 0.55683 0.13939  0.04323  0.01995  80  PRO A CA  
641  C C   . PRO A 80  ? 0.82772 1.06960 0.59889 0.14160  0.03880  0.00984  80  PRO A C   
642  O O   . PRO A 80  ? 0.79805 1.03859 0.57084 0.12898  0.04087  -0.00455 80  PRO A O   
643  C CB  . PRO A 80  ? 0.78680 0.95457 0.56292 0.15330  0.05771  0.04238  80  PRO A CB  
644  C CG  . PRO A 80  ? 0.82415 0.97227 0.60722 0.16008  0.05828  0.05421  80  PRO A CG  
645  C CD  . PRO A 80  ? 0.75873 0.94487 0.54387 0.16352  0.04407  0.04737  80  PRO A CD  
646  N N   . ALA A 81  ? 0.78184 1.06373 0.53615 0.15837  0.03304  0.01648  81  ALA A N   
647  C CA  . ALA A 81  ? 0.73160 1.06115 0.46902 0.16076  0.02795  0.00534  81  ALA A CA  
648  C C   . ALA A 81  ? 0.70314 1.05890 0.45505 0.13775  0.01760  -0.02407 81  ALA A C   
649  O O   . ALA A 81  ? 0.79692 1.18590 0.53819 0.13251  0.01489  -0.03982 81  ALA A O   
650  C CB  . ALA A 81  ? 0.82867 1.20014 0.54434 0.18701  0.02387  0.02052  81  ALA A CB  
651  N N   . GLU A 82  ? 0.72073 1.06113 0.49539 0.12338  0.01315  -0.03232 82  GLU A N   
652  C CA  . GLU A 82  ? 0.68063 1.03579 0.46936 0.09956  0.00690  -0.05943 82  GLU A CA  
653  C C   . GLU A 82  ? 0.69703 1.00762 0.49831 0.08125  0.01442  -0.07056 82  GLU A C   
654  O O   . GLU A 82  ? 0.72274 1.03016 0.53714 0.06141  0.01248  -0.09035 82  GLU A O   
655  C CB  . GLU A 82  ? 0.74885 1.11481 0.55367 0.09489  -0.00103 -0.06178 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.75904 1.16926 0.55314 0.11609  -0.00815 -0.04905 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.77088 1.18836 0.58205 0.11267  -0.01454 -0.04966 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.73617 1.11042 0.55823 0.11435  -0.01043 -0.03734 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.80948 1.27845 0.62369 0.10724  -0.02342 -0.06385 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.71206 0.98881 0.50909 0.08806  0.02415  -0.05808 83  ALA A N   
661  C CA  . ALA A 83  ? 0.64780 0.88438 0.45790 0.07442  0.03142  -0.06620 83  ALA A CA  
662  C C   . ALA A 83  ? 0.72437 0.97173 0.53054 0.05971  0.03286  -0.09043 83  ALA A C   
663  O O   . ALA A 83  ? 0.67345 0.89378 0.49258 0.04536  0.03657  -0.10311 83  ALA A O   
664  C CB  . ALA A 83  ? 0.67543 0.88202 0.48194 0.08479  0.04194  -0.04871 83  ALA A CB  
665  N N   . ASP A 84  ? 0.70107 0.98697 0.48804 0.06397  0.03092  -0.09721 84  ASP A N   
666  C CA  . ASP A 84  ? 0.65402 0.95056 0.43535 0.04923  0.03342  -0.12247 84  ASP A CA  
667  C C   . ASP A 84  ? 0.69239 0.99975 0.48516 0.02868  0.02832  -0.14572 84  ASP A C   
668  O O   . ASP A 84  ? 0.73640 1.01673 0.53693 0.01213  0.03477  -0.16301 84  ASP A O   
669  C CB  . ASP A 84  ? 0.72720 1.06778 0.48383 0.05936  0.03195  -0.12454 84  ASP A CB  
670  C CG  . ASP A 84  ? 0.72929 1.05179 0.47309 0.07405  0.04180  -0.10764 84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.71460 0.99688 0.46794 0.06813  0.05100  -0.10858 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.79759 1.14704 0.52148 0.09226  0.04115  -0.09285 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.65919 1.00562 0.45271 0.02981  0.01817  -0.14629 85  LYS A N   
674  C CA  . LYS A 85  ? 0.65807 1.01624 0.46404 0.00835  0.01459  -0.16827 85  LYS A CA  
675  C C   . LYS A 85  ? 0.69598 1.00198 0.52183 -0.00128 0.01973  -0.16534 85  LYS A C   
676  O O   . LYS A 85  ? 0.73625 1.03023 0.57076 -0.02209 0.02348  -0.18526 85  LYS A O   
677  C CB  . LYS A 85  ? 0.62490 1.03754 0.43032 0.01397  0.00273  -0.16636 85  LYS A CB  
678  N N   . LEU A 86  ? 0.70428 0.97857 0.53637 0.01341  0.02113  -0.14113 86  LEU A N   
679  C CA  . LEU A 86  ? 0.62449 0.85149 0.47364 0.00699  0.02601  -0.13735 86  LEU A CA  
680  C C   . LEU A 86  ? 0.72373 0.91490 0.57319 -0.00210 0.03692  -0.14918 86  LEU A C   
681  O O   . LEU A 86  ? 0.75189 0.91708 0.61045 -0.01599 0.04205  -0.16070 86  LEU A O   
682  C CB  . LEU A 86  ? 0.64070 0.84747 0.49519 0.02440  0.02524  -0.11106 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.63443 0.80589 0.50672 0.02069  0.02648  -0.10480 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.65521 0.84430 0.53544 0.01112  0.02013  -0.11189 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.64120 0.79603 0.51686 0.03658  0.02678  -0.08192 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.70946 0.89802 0.54786 0.00686  0.04187  -0.14570 87  VAL A N   
687  C CA  . VAL A 87  ? 0.71811 0.87520 0.55582 0.00142  0.05291  -0.15615 87  VAL A CA  
688  C C   . VAL A 87  ? 0.77808 0.93784 0.61186 -0.01847 0.05715  -0.18420 87  VAL A C   
689  O O   . VAL A 87  ? 0.74562 0.86796 0.58532 -0.02738 0.06653  -0.19361 87  VAL A O   
690  C CB  . VAL A 87  ? 0.76567 0.92931 0.59019 0.01382  0.05735  -0.14934 87  VAL A CB  
691  C CG1 . VAL A 87  ? 0.75349 0.89437 0.57423 0.00746  0.06872  -0.16514 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.71061 0.85855 0.54176 0.02941  0.05803  -0.12386 87  VAL A CG2 
693  N N   . LYS A 88  ? 0.81871 1.02339 0.64157 -0.02536 0.05128  -0.19835 88  LYS A N   
694  C CA  . LYS A 88  ? 0.75609 0.96868 0.57482 -0.04760 0.05590  -0.22862 88  LYS A CA  
695  C C   . LYS A 88  ? 0.81270 0.99838 0.64613 -0.06377 0.05954  -0.23606 88  LYS A C   
696  O O   . LYS A 88  ? 0.83063 0.97464 0.66570 -0.07500 0.07219  -0.24848 88  LYS A O   
697  C CB  . LYS A 88  ? 0.71852 0.99496 0.52593 -0.05183 0.04622  -0.24150 88  LYS A CB  
698  C CG  . LYS A 88  ? 0.88298 1.18813 0.67076 -0.03985 0.04537  -0.24140 88  LYS A CG  
699  C CD  . LYS A 88  ? 0.87583 1.24675 0.65189 -0.04790 0.03696  -0.26127 88  LYS A CD  
700  C CE  . LYS A 88  ? 0.89975 1.27059 0.67865 -0.07832 0.04348  -0.29749 88  LYS A CE  
701  N NZ  . LYS A 88  ? 0.90829 1.34991 0.67685 -0.08885 0.03527  -0.32108 88  LYS A NZ  
702  N N   . LEU A 89  ? 0.82720 1.03544 0.67017 -0.06391 0.04978  -0.22781 89  LEU A N   
703  C CA  . LEU A 89  ? 0.81533 1.00519 0.67106 -0.08083 0.05333  -0.23587 89  LEU A CA  
704  C C   . LEU A 89  ? 0.81797 0.94660 0.68230 -0.07597 0.06283  -0.22331 89  LEU A C   
705  O O   . LEU A 89  ? 0.94153 1.03682 0.80948 -0.09123 0.07375  -0.23530 89  LEU A O   
706  C CB  . LEU A 89  ? 0.79400 1.02223 0.65840 -0.07777 0.04065  -0.22614 89  LEU A CB  
707  C CG  . LEU A 89  ? 0.76935 1.06605 0.62518 -0.07556 0.02918  -0.23323 89  LEU A CG  
708  C CD1 . LEU A 89  ? 0.71961 1.04777 0.58385 -0.06431 0.01733  -0.21647 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 0.62834 0.95479 0.48045 -0.10196 0.03261  -0.26738 89  LEU A CD2 
710  N N   . LEU A 90  ? 0.78601 0.89988 0.65290 -0.05469 0.05992  -0.19949 90  LEU A N   
711  C CA  . LEU A 90  ? 0.84879 0.91264 0.72378 -0.04774 0.06779  -0.18772 90  LEU A CA  
712  C C   . LEU A 90  ? 0.91327 0.94175 0.78114 -0.05294 0.08254  -0.20182 90  LEU A C   
713  O O   . LEU A 90  ? 0.99185 0.97810 0.86422 -0.05407 0.09245  -0.20067 90  LEU A O   
714  C CB  . LEU A 90  ? 0.78796 0.85044 0.66731 -0.02616 0.06208  -0.16303 90  LEU A CB  
715  C CG  . LEU A 90  ? 0.82032 0.87403 0.71301 -0.01907 0.05621  -0.14485 90  LEU A CG  
716  C CD1 . LEU A 90  ? 0.77262 0.82814 0.66819 -0.00098 0.05205  -0.12451 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 0.89076 0.90318 0.79082 -0.02318 0.06487  -0.14566 90  LEU A CD2 
718  N N   . ALA A 91  ? 0.90931 0.95409 0.76458 -0.05441 0.08497  -0.21456 91  ALA A N   
719  C CA  . ALA A 91  ? 0.98187 0.99327 0.82886 -0.05831 0.10003  -0.22919 91  ALA A CA  
720  C C   . ALA A 91  ? 1.07262 1.06577 0.91603 -0.08193 0.11103  -0.25405 91  ALA A C   
721  O O   . ALA A 91  ? 1.11771 1.06211 0.95956 -0.08406 0.12626  -0.25897 91  ALA A O   
722  C CB  . ALA A 91  ? 0.96006 0.99660 0.79353 -0.05321 0.09967  -0.23619 91  ALA A CB  
723  N N   . LYS A 92  ? 1.03039 1.06258 0.87205 -0.09965 0.10474  -0.27023 92  LYS A N   
724  C CA  . LYS A 92  ? 1.13045 1.14770 0.97104 -0.12603 0.11596  -0.29502 92  LYS A CA  
725  C C   . LYS A 92  ? 1.20530 1.18203 1.05696 -0.12780 0.12214  -0.28339 92  LYS A C   
726  O O   . LYS A 92  ? 1.31336 1.24493 1.16163 -0.14133 0.13967  -0.29611 92  LYS A O   
727  C CB  . LYS A 92  ? 1.18225 1.26010 1.02229 -0.14396 0.10573  -0.31327 92  LYS A CB  
728  C CG  . LYS A 92  ? 1.22786 1.29775 1.07309 -0.17289 0.11493  -0.33473 92  LYS A CG  
729  C CD  . LYS A 92  ? 1.17105 1.30925 1.01615 -0.19187 0.10522  -0.35718 92  LYS A CD  
730  C CE  . LYS A 92  ? 1.24933 1.37840 1.10004 -0.22505 0.11763  -0.38278 92  LYS A CE  
731  N NZ  . LYS A 92  ? 1.24521 1.44345 1.09481 -0.24765 0.11095  -0.41247 92  LYS A NZ  
732  N N   . GLY A 93  ? 1.16997 1.15992 1.03326 -0.11356 0.10933  -0.25895 93  GLY A N   
733  C CA  . GLY A 93  ? 1.23306 1.19255 1.10615 -0.11460 0.11333  -0.24735 93  GLY A CA  
734  C C   . GLY A 93  ? 1.29992 1.28446 1.17872 -0.13746 0.11154  -0.26094 93  GLY A C   
735  O O   . GLY A 93  ? 1.21002 1.25068 1.09073 -0.14259 0.09848  -0.26746 93  GLY A O   
736  N N   . GLU A 94  ? 1.46465 1.40925 1.34571 -0.15040 0.12551  -0.26477 94  GLU A N   
737  C CA  . GLU A 94  ? 1.50619 1.46985 1.39383 -0.17509 0.12736  -0.27884 94  GLU A CA  
738  C C   . GLU A 94  ? 1.47411 1.48866 1.37420 -0.16690 0.10771  -0.26378 94  GLU A C   
739  O O   . GLU A 94  ? 1.41314 1.47100 1.31922 -0.18464 0.10286  -0.27775 94  GLU A O   
740  C CB  . GLU A 94  ? 1.39607 1.38554 1.27739 -0.20304 0.13347  -0.31340 94  GLU A CB  
741  N N   . TYR A 95  ? 1.34652 1.35746 1.25069 -0.14015 0.09709  -0.23628 95  TYR A N   
742  C CA  . TYR A 95  ? 1.23067 1.28125 1.14508 -0.12973 0.08059  -0.22033 95  TYR A CA  
743  C C   . TYR A 95  ? 1.23584 1.26428 1.15906 -0.13384 0.08524  -0.21090 95  TYR A C   
744  O O   . TYR A 95  ? 1.26497 1.24371 1.18522 -0.14067 0.10107  -0.21236 95  TYR A O   
745  C CB  . TYR A 95  ? 1.15257 1.20754 1.06670 -0.10153 0.06907  -0.19711 95  TYR A CB  
746  C CG  . TYR A 95  ? 1.17138 1.17440 1.08331 -0.08703 0.07740  -0.18377 95  TYR A CG  
747  C CD1 . TYR A 95  ? 1.17227 1.14418 1.09060 -0.07948 0.08048  -0.16805 95  TYR A CD1 
748  C CD2 . TYR A 95  ? 1.18965 1.17918 1.09295 -0.07966 0.08200  -0.18695 95  TYR A CD2 
749  C CE1 . TYR A 95  ? 1.12451 1.05645 1.04104 -0.06439 0.08724  -0.15612 95  TYR A CE1 
750  C CE2 . TYR A 95  ? 1.18847 1.13689 1.09104 -0.06504 0.08936  -0.17515 95  TYR A CE2 
751  C CZ  . TYR A 95  ? 1.19224 1.11365 1.10165 -0.05708 0.09157  -0.15980 95  TYR A CZ  
752  O OH  . TYR A 95  ? 1.34536 1.23270 1.25425 -0.04076 0.09813  -0.14820 95  TYR A OH  
753  N N   . GLN A 96  ? 1.13723 1.20246 1.06983 -0.12807 0.07225  -0.20035 96  GLN A N   
754  C CA  . GLN A 96  ? 1.06369 1.11350 1.00451 -0.12801 0.07437  -0.18836 96  GLN A CA  
755  C C   . GLN A 96  ? 0.96077 0.99388 0.90392 -0.10113 0.06660  -0.16167 96  GLN A C   
756  O O   . GLN A 96  ? 0.93151 0.97955 0.87303 -0.08403 0.05649  -0.15229 96  GLN A O   
757  C CB  . GLN A 96  ? 1.05552 1.15742 1.00595 -0.13912 0.06622  -0.19490 96  GLN A CB  
758  C CG  . GLN A 96  ? 1.06815 1.18467 1.01988 -0.17084 0.07675  -0.22268 96  GLN A CG  
759  C CD  . GLN A 96  ? 1.15457 1.32283 1.11850 -0.18129 0.06988  -0.22761 96  GLN A CD  
760  O OE1 . GLN A 96  ? 1.12953 1.34485 1.09805 -0.16537 0.05354  -0.21790 96  GLN A OE1 
761  N NE2 . GLN A 96  ? 1.20896 1.36758 1.17776 -0.20754 0.08382  -0.24228 96  GLN A NE2 
762  N N   . LYS A 97  ? 0.89953 0.90147 0.84584 -0.09834 0.07258  -0.15013 97  LYS A N   
763  C CA  . LYS A 97  ? 0.81627 0.80354 0.76534 -0.07536 0.06622  -0.12738 97  LYS A CA  
764  C C   . LYS A 97  ? 0.77292 0.78029 0.73055 -0.07324 0.05912  -0.11774 97  LYS A C   
765  O O   . LYS A 97  ? 0.73017 0.73855 0.69051 -0.08901 0.06587  -0.12466 97  LYS A O   
766  C CB  . LYS A 97  ? 0.82733 0.76164 0.77066 -0.06845 0.07894  -0.12001 97  LYS A CB  
767  C CG  . LYS A 97  ? 0.86488 0.77914 0.80031 -0.06349 0.08472  -0.12535 97  LYS A CG  
768  C CD  . LYS A 97  ? 0.86858 0.73820 0.79955 -0.04849 0.09422  -0.11308 97  LYS A CD  
769  C CE  . LYS A 97  ? 0.95167 0.77926 0.87144 -0.05874 0.11397  -0.12517 97  LYS A CE  
770  N NZ  . LYS A 97  ? 0.98238 0.76860 0.89622 -0.03937 0.12354  -0.11135 97  LYS A NZ  
771  N N   . VAL A 98  ? 0.71352 0.73574 0.67510 -0.05442 0.04691  -0.10249 98  VAL A N   
772  C CA  . VAL A 98  ? 0.64087 0.68584 0.60972 -0.04928 0.03886  -0.09337 98  VAL A CA  
773  C C   . VAL A 98  ? 0.63814 0.66007 0.60828 -0.03147 0.03650  -0.07574 98  VAL A C   
774  O O   . VAL A 98  ? 0.60685 0.62499 0.57602 -0.01763 0.03156  -0.06845 98  VAL A O   
775  C CB  . VAL A 98  ? 0.58051 0.67165 0.55159 -0.04342 0.02655  -0.09385 98  VAL A CB  
776  C CG1 . VAL A 98  ? 0.65242 0.76154 0.62990 -0.03394 0.01930  -0.08256 98  VAL A CG1 
777  C CG2 . VAL A 98  ? 0.63069 0.75437 0.60133 -0.06110 0.02765  -0.11266 98  VAL A CG2 
778  N N   . SER A 99  ? 0.65236 0.66148 0.62459 -0.03256 0.04050  -0.06972 99  SER A N   
779  C CA  . SER A 99  ? 0.57819 0.56810 0.55080 -0.01684 0.03890  -0.05489 99  SER A CA  
780  C C   . SER A 99  ? 0.52849 0.54254 0.50702 -0.00856 0.02908  -0.04682 99  SER A C   
781  O O   . SER A 99  ? 0.58724 0.62244 0.56922 -0.01648 0.02822  -0.05021 99  SER A O   
782  C CB  . SER A 99  ? 0.60757 0.56389 0.57517 -0.02017 0.05128  -0.05170 99  SER A CB  
783  O OG  . SER A 99  ? 0.66558 0.59219 0.62593 -0.02278 0.06179  -0.05666 99  SER A OG  
784  N N   . TYR A 100 ? 0.56276 0.57416 0.54272 0.00690  0.02265  -0.03724 100 TYR A N   
785  C CA  . TYR A 100 ? 0.50500 0.53068 0.48895 0.01660  0.01521  -0.02945 100 TYR A CA  
786  C C   . TYR A 100 ? 0.51544 0.52298 0.49897 0.02538  0.01648  -0.02098 100 TYR A C   
787  O O   . TYR A 100 ? 0.52817 0.51731 0.50963 0.03060  0.01934  -0.01883 100 TYR A O   
788  C CB  . TYR A 100 ? 0.46091 0.49899 0.44594 0.02615  0.00810  -0.02705 100 TYR A CB  
789  C CG  . TYR A 100 ? 0.46118 0.52586 0.44523 0.02321  0.00477  -0.03188 100 TYR A CG  
790  C CD1 . TYR A 100 ? 0.48991 0.57130 0.47441 0.01045  0.00696  -0.04077 100 TYR A CD1 
791  C CD2 . TYR A 100 ? 0.45237 0.52708 0.43444 0.03351  0.00030  -0.02762 100 TYR A CD2 
792  C CE1 . TYR A 100 ? 0.50300 0.61678 0.48673 0.00927  0.00280  -0.04585 100 TYR A CE1 
793  C CE2 . TYR A 100 ? 0.51724 0.61902 0.49621 0.03459  -0.00273 -0.03011 100 TYR A CE2 
794  C CZ  . TYR A 100 ? 0.50246 0.62693 0.48265 0.02314  -0.00249 -0.03945 100 TYR A CZ  
795  O OH  . TYR A 100 ? 0.56232 0.72130 0.53955 0.02573  -0.00657 -0.04250 100 TYR A OH  
796  N N   . PRO A 101 ? 0.50051 0.51596 0.48555 0.02838  0.01435  -0.01630 101 PRO A N   
797  C CA  . PRO A 101 ? 0.50467 0.50812 0.48801 0.03780  0.01471  -0.00878 101 PRO A CA  
798  C C   . PRO A 101 ? 0.47514 0.48061 0.46164 0.04858  0.00845  -0.00670 101 PRO A C   
799  O O   . PRO A 101 ? 0.47517 0.49130 0.46482 0.04978  0.00390  -0.00888 101 PRO A O   
800  C CB  . PRO A 101 ? 0.45596 0.47284 0.44005 0.03753  0.01337  -0.00610 101 PRO A CB  
801  C CG  . PRO A 101 ? 0.42676 0.46045 0.41341 0.02591  0.01462  -0.01253 101 PRO A CG  
802  C CD  . PRO A 101 ? 0.48399 0.52319 0.47203 0.02460  0.01150  -0.01792 101 PRO A CD  
803  N N   . LEU A 102 ? 0.48701 0.48308 0.47211 0.05668  0.00929  -0.00242 102 LEU A N   
804  C CA  . LEU A 102 ? 0.46966 0.47160 0.45934 0.06500  0.00414  -0.00238 102 LEU A CA  
805  C C   . LEU A 102 ? 0.49736 0.50748 0.48652 0.07216  0.00091  0.00092  102 LEU A C   
806  O O   . LEU A 102 ? 0.43197 0.44023 0.41581 0.07255  0.00345  0.00512  102 LEU A O   
807  C CB  . LEU A 102 ? 0.43377 0.42616 0.42370 0.06945  0.00706  -0.00230 102 LEU A CB  
808  C CG  . LEU A 102 ? 0.49610 0.47796 0.48430 0.06269  0.01186  -0.00625 102 LEU A CG  
809  C CD1 . LEU A 102 ? 0.49250 0.46330 0.47962 0.06955  0.01629  -0.00523 102 LEU A CD1 
810  C CD2 . LEU A 102 ? 0.42986 0.42205 0.42201 0.05830  0.00814  -0.01075 102 LEU A CD2 
811  N N   . LEU A 103 ? 0.43336 0.45347 0.42777 0.07681  -0.00386 -0.00198 103 LEU A N   
812  C CA  . LEU A 103 ? 0.49369 0.52590 0.48799 0.08256  -0.00768 -0.00207 103 LEU A CA  
813  C C   . LEU A 103 ? 0.47308 0.51416 0.46990 0.09057  -0.00961 -0.00273 103 LEU A C   
814  O O   . LEU A 103 ? 0.43423 0.47856 0.43802 0.08945  -0.01021 -0.00734 103 LEU A O   
815  C CB  . LEU A 103 ? 0.42233 0.46170 0.42063 0.07950  -0.01069 -0.00790 103 LEU A CB  
816  C CG  . LEU A 103 ? 0.39424 0.44675 0.39302 0.08362  -0.01422 -0.01187 103 LEU A CG  
817  C CD1 . LEU A 103 ? 0.41334 0.46972 0.40470 0.08733  -0.01423 -0.00695 103 LEU A CD1 
818  C CD2 . LEU A 103 ? 0.37978 0.43201 0.38236 0.07952  -0.01415 -0.01927 103 LEU A CD2 
819  N N   . LYS A 104 ? 0.45233 0.50039 0.44326 0.09939  -0.01029 0.00207  104 LYS A N   
820  C CA  . LYS A 104 ? 0.47330 0.53784 0.46580 0.11005  -0.01314 0.00188  104 LYS A CA  
821  C C   . LYS A 104 ? 0.43578 0.52470 0.43169 0.11097  -0.01958 -0.00580 104 LYS A C   
822  O O   . LYS A 104 ? 0.44110 0.53205 0.43109 0.11095  -0.02046 -0.00479 104 LYS A O   
823  C CB  . LYS A 104 ? 0.47883 0.53617 0.45981 0.12272  -0.00855 0.01356  104 LYS A CB  
824  C CG  . LYS A 104 ? 0.58817 0.67080 0.56863 0.13803  -0.01275 0.01474  104 LYS A CG  
825  C CD  . LYS A 104 ? 0.56124 0.63277 0.53346 0.15282  -0.00629 0.02577  104 LYS A CD  
826  C CE  . LYS A 104 ? 0.56486 0.62837 0.51996 0.16592  -0.00110 0.03930  104 LYS A CE  
827  N NZ  . LYS A 104 ? 0.62213 0.70808 0.57164 0.18841  -0.00288 0.04605  104 LYS A NZ  
828  N N   . THR A 105 ? 0.46488 0.57337 0.47062 0.11061  -0.02325 -0.01486 105 THR A N   
829  C CA  . THR A 105 ? 0.48483 0.62006 0.49493 0.10974  -0.02868 -0.02567 105 THR A CA  
830  C C   . THR A 105 ? 0.47776 0.64343 0.48971 0.12214  -0.03281 -0.02614 105 THR A C   
831  O O   . THR A 105 ? 0.51336 0.68340 0.53173 0.12536  -0.03174 -0.02551 105 THR A O   
832  C CB  . THR A 105 ? 0.45261 0.58751 0.47399 0.09546  -0.02782 -0.03910 105 THR A CB  
833  O OG1 . THR A 105 ? 0.44597 0.55381 0.46396 0.08790  -0.02359 -0.03641 105 THR A OG1 
834  C CG2 . THR A 105 ? 0.44403 0.60398 0.46931 0.09161  -0.03158 -0.05315 105 THR A CG2 
835  N N   . THR A 106 ? 0.49638 0.68591 0.50222 0.13045  -0.03746 -0.02716 106 THR A N   
836  C CA  . THR A 106 ? 0.54372 0.77043 0.54999 0.14501  -0.04254 -0.02767 106 THR A CA  
837  C C   . THR A 106 ? 0.46814 0.73254 0.48195 0.13835  -0.04922 -0.04597 106 THR A C   
838  O O   . THR A 106 ? 0.43448 0.69764 0.44243 0.13338  -0.05028 -0.05073 106 THR A O   
839  C CB  . THR A 106 ? 0.51464 0.73930 0.50302 0.16490  -0.04116 -0.01037 106 THR A CB  
840  O OG1 . THR A 106 ? 0.51321 0.69799 0.49432 0.16732  -0.03257 0.00421  106 THR A OG1 
841  C CG2 . THR A 106 ? 0.50762 0.77264 0.49502 0.18434  -0.04605 -0.00854 106 THR A CG2 
842  N N   . VAL A 107 ? 0.49369 0.79266 0.52091 0.13729  -0.05292 -0.05761 107 VAL A N   
843  C CA  . VAL A 107 ? 0.50951 0.84866 0.54631 0.12772  -0.05834 -0.07890 107 VAL A CA  
844  C C   . VAL A 107 ? 0.57514 0.96759 0.61082 0.14651  -0.06617 -0.07893 107 VAL A C   
845  O O   . VAL A 107 ? 0.60279 1.01269 0.64490 0.15706  -0.06684 -0.07433 107 VAL A O   
846  C CB  . VAL A 107 ? 0.51688 0.85642 0.57254 0.10653  -0.05471 -0.09621 107 VAL A CB  
847  C CG1 . VAL A 107 ? 0.44836 0.81694 0.51186 0.09082  -0.05686 -0.12054 107 VAL A CG1 
848  C CG2 . VAL A 107 ? 0.50921 0.79515 0.56372 0.09485  -0.04616 -0.08982 107 VAL A CG2 
849  N N   . LYS A 108 ? 0.52669 0.94722 0.55347 0.15228  -0.07190 -0.08395 108 LYS A N   
850  C CA  . LYS A 108 ? 0.57143 1.05014 0.59556 0.17133  -0.08033 -0.08529 108 LYS A CA  
851  C C   . LYS A 108 ? 0.61541 1.14618 0.65643 0.15492  -0.08629 -0.11479 108 LYS A C   
852  O O   . LYS A 108 ? 0.59231 1.10910 0.63971 0.13107  -0.08326 -0.13269 108 LYS A O   
853  C CB  . LYS A 108 ? 0.48264 0.96370 0.48368 0.19018  -0.08252 -0.07129 108 LYS A CB  
854  N N   . TYR A 109 ? 0.66893 1.26027 0.71705 0.16788  -0.09370 -0.12032 109 TYR A N   
855  C CA  . TYR A 109 ? 0.57438 1.22494 0.64048 0.15159  -0.09947 -0.15064 109 TYR A CA  
856  C C   . TYR A 109 ? 0.69668 1.41548 0.75367 0.17246  -0.11079 -0.15383 109 TYR A C   
857  O O   . TYR A 109 ? 0.70400 1.41557 0.73813 0.19464  -0.11285 -0.13501 109 TYR A O   
858  C CB  . TYR A 109 ? 0.60959 1.28237 0.69912 0.14296  -0.09785 -0.16035 109 TYR A CB  
859  C CG  . TYR A 109 ? 0.67954 1.29056 0.77686 0.12604  -0.08672 -0.15523 109 TYR A CG  
860  C CD1 . TYR A 109 ? 0.65252 1.22763 0.74342 0.14257  -0.08245 -0.13049 109 TYR A CD1 
861  C CD2 . TYR A 109 ? 0.58392 1.17307 0.69379 0.09420  -0.07941 -0.17547 109 TYR A CD2 
862  C CE1 . TYR A 109 ? 0.65389 1.17794 0.75088 0.12793  -0.07298 -0.12664 109 TYR A CE1 
863  C CE2 . TYR A 109 ? 0.68191 1.21762 0.79677 0.08131  -0.06909 -0.16934 109 TYR A CE2 
864  C CZ  . TYR A 109 ? 0.72186 1.22786 0.83050 0.09825  -0.06679 -0.14528 109 TYR A CZ  
865  O OH  . TYR A 109 ? 0.72290 1.17997 0.83543 0.08584  -0.05710 -0.14007 109 TYR A OH  
866  N N   . GLY A 110 ? 0.75897 1.54776 0.83383 0.16525  -0.11769 -0.17826 110 GLY A N   
867  C CA  . GLY A 110 ? 0.64322 1.50528 0.71095 0.18483  -0.12808 -0.18343 110 GLY A CA  
868  C C   . GLY A 110 ? 0.62849 1.54510 0.71419 0.17914  -0.12721 -0.20065 110 GLY A C   
869  O O   . GLY A 110 ? 0.61614 1.56019 0.69204 0.20515  -0.12706 -0.18661 110 GLY A O   
870  N N   . LYS A 114 ? 0.75576 1.46946 0.79863 0.25541  -0.10624 -0.08293 114 LYS A N   
871  C CA  . LYS A 114 ? 0.76533 1.42926 0.81581 0.24998  -0.09671 -0.07330 114 LYS A CA  
872  C C   . LYS A 114 ? 0.85900 1.44378 0.90083 0.23136  -0.08770 -0.06592 114 LYS A C   
873  O O   . LYS A 114 ? 0.86841 1.44187 0.90341 0.21884  -0.08903 -0.07259 114 LYS A O   
874  C CB  . LYS A 114 ? 0.69888 1.39655 0.77897 0.22858  -0.09782 -0.09700 114 LYS A CB  
875  C CG  . LYS A 114 ? 0.83027 1.50175 0.91810 0.23376  -0.09009 -0.08600 114 LYS A CG  
876  C CD  . LYS A 114 ? 0.83051 1.50599 0.90144 0.27378  -0.08900 -0.05983 114 LYS A CD  
877  C CE  . LYS A 114 ? 0.84259 1.43647 0.89712 0.27911  -0.07694 -0.03641 114 LYS A CE  
878  N NZ  . LYS A 114 ? 0.85944 1.43848 0.88684 0.31464  -0.07352 -0.00931 114 LYS A NZ  
879  N N   . GLU A 115 ? 0.72210 1.25530 0.76393 0.23031  -0.07854 -0.05285 115 GLU A N   
880  C CA  . GLU A 115 ? 0.68260 1.14650 0.71566 0.21562  -0.07037 -0.04466 115 GLU A CA  
881  C C   . GLU A 115 ? 0.69093 1.11910 0.73580 0.20224  -0.06281 -0.04491 115 GLU A C   
882  O O   . GLU A 115 ? 0.70220 1.13787 0.75097 0.21585  -0.06037 -0.03805 115 GLU A O   
883  C CB  . GLU A 115 ? 0.66009 1.08837 0.66731 0.23721  -0.06516 -0.01907 115 GLU A CB  
884  C CG  . GLU A 115 ? 0.71516 1.11450 0.71021 0.22634  -0.06390 -0.01774 115 GLU A CG  
885  C CD  . GLU A 115 ? 0.78553 1.14831 0.75598 0.24514  -0.05633 0.00727  115 GLU A CD  
886  O OE1 . GLU A 115 ? 0.74887 1.07016 0.71440 0.24969  -0.04693 0.02123  115 GLU A OE1 
887  O OE2 . GLU A 115 ? 0.74917 1.12431 0.70466 0.25454  -0.05862 0.01222  115 GLU A OE2 
888  N N   . ALA A 116 ? 0.64517 1.03511 0.69427 0.17744  -0.05864 -0.05214 116 ALA A N   
889  C CA  . ALA A 116 ? 0.58039 0.93285 0.63717 0.16459  -0.05104 -0.05114 116 ALA A CA  
890  C C   . ALA A 116 ? 0.55367 0.84967 0.59829 0.15553  -0.04516 -0.04185 116 ALA A C   
891  O O   . ALA A 116 ? 0.56665 0.85577 0.60673 0.14607  -0.04683 -0.04667 116 ALA A O   
892  C CB  . ALA A 116 ? 0.61146 0.98291 0.68953 0.14135  -0.05092 -0.07266 116 ALA A CB  
893  N N   . THR A 117 ? 0.56266 0.82119 0.60223 0.15854  -0.03804 -0.02968 117 THR A N   
894  C CA  . THR A 117 ? 0.59598 0.80644 0.62537 0.14990  -0.03236 -0.02174 117 THR A CA  
895  C C   . THR A 117 ? 0.59104 0.77756 0.62920 0.13421  -0.02722 -0.02645 117 THR A C   
896  O O   . THR A 117 ? 0.52093 0.71853 0.56909 0.13476  -0.02562 -0.03017 117 THR A O   
897  C CB  . THR A 117 ? 0.57639 0.76052 0.58821 0.16648  -0.02680 -0.00304 117 THR A CB  
898  O OG1 . THR A 117 ? 0.66778 0.84357 0.68070 0.17581  -0.02145 0.00273  117 THR A OG1 
899  C CG2 . THR A 117 ? 0.54992 0.75819 0.55050 0.18532  -0.03055 0.00421  117 THR A CG2 
900  N N   . TYR A 118 ? 0.58982 0.74615 0.62357 0.12145  -0.02445 -0.02593 118 TYR A N   
901  C CA  . TYR A 118 ? 0.47649 0.61036 0.51529 0.10781  -0.01962 -0.02912 118 TYR A CA  
902  C C   . TYR A 118 ? 0.47542 0.57530 0.50278 0.10466  -0.01582 -0.02038 118 TYR A C   
903  O O   . TYR A 118 ? 0.51447 0.60937 0.53340 0.10661  -0.01716 -0.01612 118 TYR A O   
904  C CB  . TYR A 118 ? 0.47358 0.61527 0.52239 0.09223  -0.02003 -0.04264 118 TYR A CB  
905  C CG  . TYR A 118 ? 0.51865 0.69853 0.58024 0.09070  -0.02347 -0.05536 118 TYR A CG  
906  C CD1 . TYR A 118 ? 0.56903 0.77507 0.63014 0.09348  -0.02939 -0.06177 118 TYR A CD1 
907  C CD2 . TYR A 118 ? 0.53058 0.72404 0.60507 0.08567  -0.02056 -0.06226 118 TYR A CD2 
908  C CE1 . TYR A 118 ? 0.56347 0.81074 0.63719 0.09052  -0.03293 -0.07609 118 TYR A CE1 
909  C CE2 . TYR A 118 ? 0.56556 0.79954 0.65379 0.08227  -0.02336 -0.07596 118 TYR A CE2 
910  C CZ  . TYR A 118 ? 0.58215 0.84425 0.67029 0.08428  -0.02985 -0.08356 118 TYR A CZ  
911  O OH  . TYR A 118 ? 0.52226 0.83074 0.62509 0.07935  -0.03297 -0.09979 118 TYR A OH  
912  N N   . LEU A 119 ? 0.46441 0.54447 0.49190 0.09922  -0.01091 -0.01878 119 LEU A N   
913  C CA  . LEU A 119 ? 0.44643 0.50037 0.46508 0.09413  -0.00735 -0.01332 119 LEU A CA  
914  C C   . LEU A 119 ? 0.43723 0.48490 0.45937 0.08237  -0.00656 -0.01857 119 LEU A C   
915  O O   . LEU A 119 ? 0.46071 0.51174 0.48991 0.07801  -0.00464 -0.02356 119 LEU A O   
916  C CB  . LEU A 119 ? 0.49606 0.53304 0.50962 0.09788  -0.00154 -0.00811 119 LEU A CB  
917  C CG  . LEU A 119 ? 0.52670 0.54228 0.52828 0.09880  0.00315  -0.00081 119 LEU A CG  
918  C CD1 . LEU A 119 ? 0.48955 0.51055 0.48475 0.10858  0.00193  0.00565  119 LEU A CD1 
919  C CD2 . LEU A 119 ? 0.53097 0.52836 0.52779 0.10202  0.01078  0.00158  119 LEU A CD2 
920  N N   . ALA A 120 ? 0.40393 0.44321 0.42048 0.07848  -0.00704 -0.01671 120 ALA A N   
921  C CA  . ALA A 120 ? 0.42254 0.45564 0.43963 0.07137  -0.00556 -0.01945 120 ALA A CA  
922  C C   . ALA A 120 ? 0.45560 0.47715 0.46578 0.06891  -0.00352 -0.01491 120 ALA A C   
923  O O   . ALA A 120 ? 0.44365 0.46269 0.44870 0.06980  -0.00378 -0.01119 120 ALA A O   
924  C CB  . ALA A 120 ? 0.37731 0.41519 0.39413 0.07058  -0.00758 -0.02263 120 ALA A CB  
925  N N   . LEU A 121 ? 0.36330 0.48490 0.43110 0.08189  0.05125  -0.01537 121 LEU A N   
926  C CA  . LEU A 121 ? 0.38111 0.48208 0.43397 0.07582  0.05178  -0.01846 121 LEU A CA  
927  C C   . LEU A 121 ? 0.40412 0.50340 0.45684 0.06221  0.04724  -0.01507 121 LEU A C   
928  O O   . LEU A 121 ? 0.38395 0.46554 0.42842 0.05733  0.04398  -0.01608 121 LEU A O   
929  C CB  . LEU A 121 ? 0.34062 0.44618 0.38612 0.07868  0.05895  -0.02331 121 LEU A CB  
930  C CG  . LEU A 121 ? 0.39263 0.47887 0.42081 0.07247  0.05829  -0.02736 121 LEU A CG  
931  C CD1 . LEU A 121 ? 0.40287 0.46210 0.42115 0.07553  0.05493  -0.03125 121 LEU A CD1 
932  C CD2 . LEU A 121 ? 0.42001 0.51208 0.43819 0.07587  0.06594  -0.03187 121 LEU A CD2 
933  N N   . ASN A 122 ? 0.36180 0.47925 0.42407 0.05607  0.04684  -0.01127 122 ASN A N   
934  C CA  . ASN A 122 ? 0.33146 0.44539 0.39296 0.04524  0.04233  -0.00784 122 ASN A CA  
935  C C   . ASN A 122 ? 0.38474 0.49878 0.45353 0.04465  0.03698  -0.00459 122 ASN A C   
936  O O   . ASN A 122 ? 0.36785 0.46740 0.43235 0.04387  0.03371  -0.00407 122 ASN A O   
937  C CB  . ASN A 122 ? 0.35196 0.47944 0.41543 0.03773  0.04518  -0.00550 122 ASN A CB  
938  C CG  . ASN A 122 ? 0.39451 0.51274 0.44374 0.03383  0.04717  -0.00661 122 ASN A CG  
939  O OD1 . ASN A 122 ? 0.35701 0.46173 0.39597 0.03726  0.04653  -0.01067 122 ASN A OD1 
940  N ND2 . ASN A 122 ? 0.38293 0.50710 0.43006 0.02616  0.04910  -0.00294 122 ASN A ND2 
941  N N   . GLU A 123 ? 0.35827 0.48944 0.43789 0.04472  0.03614  -0.00269 123 GLU A N   
942  C CA  . GLU A 123 ? 0.33640 0.46730 0.41991 0.04354  0.03031  -0.00019 123 GLU A CA  
943  C C   . GLU A 123 ? 0.34928 0.50144 0.44525 0.04674  0.02872  0.00015  123 GLU A C   
944  O O   . GLU A 123 ? 0.34818 0.51842 0.45266 0.04777  0.03279  -0.00101 123 GLU A O   
945  C CB  . GLU A 123 ? 0.31231 0.43756 0.39287 0.03330  0.02727  0.00181  123 GLU A CB  
946  C CG  . GLU A 123 ? 0.34601 0.48392 0.43161 0.02485  0.02841  0.00293  123 GLU A CG  
947  C CD  . GLU A 123 ? 0.40460 0.54413 0.48572 0.02256  0.03455  0.00256  123 GLU A CD  
948  O OE1 . GLU A 123 ? 0.35190 0.47700 0.42212 0.02075  0.03443  0.00269  123 GLU A OE1 
949  O OE2 . GLU A 123 ? 0.37420 0.53084 0.46258 0.02302  0.03949  0.00205  123 GLU A OE2 
950  N N   . SER A 124 ? 0.38025 0.53155 0.47725 0.04839  0.02269  0.00159  124 SER A N   
951  C CA  . SER A 124 ? 0.31537 0.48727 0.42389 0.04941  0.01803  0.00163  124 SER A CA  
952  C C   . SER A 124 ? 0.27553 0.44347 0.38166 0.03983  0.01216  0.00238  124 SER A C   
953  O O   . SER A 124 ? 0.31062 0.45989 0.40549 0.04012  0.01020  0.00343  124 SER A O   
954  C CB  . SER A 124 ? 0.31737 0.49028 0.42562 0.06321  0.01482  0.00213  124 SER A CB  
955  O OG  . SER A 124 ? 0.41286 0.60660 0.53170 0.06420  0.00797  0.00192  124 SER A OG  
956  N N   . THR A 125 ? 0.29506 0.47984 0.41140 0.03091  0.00997  0.00156  125 THR A N   
957  C CA  . THR A 125 ? 0.35327 0.53145 0.46562 0.02138  0.00408  0.00119  125 THR A CA  
958  C C   . THR A 125 ? 0.31144 0.50945 0.43422 0.02040  -0.00383 -0.00084 125 THR A C   
959  O O   . THR A 125 ? 0.28570 0.50822 0.42330 0.02468  -0.00396 -0.00158 125 THR A O   
960  C CB  . THR A 125 ? 0.29881 0.47193 0.40995 0.00814  0.00744  0.00191  125 THR A CB  
961  O OG1 . THR A 125 ? 0.33900 0.53503 0.46499 -0.00026 0.00808  0.00131  125 THR A OG1 
962  C CG2 . THR A 125 ? 0.33488 0.49722 0.43918 0.00993  0.01498  0.00360  125 THR A CG2 
963  N N   . VAL A 126 ? 0.34413 0.53196 0.45879 0.01547  -0.01089 -0.00229 126 VAL A N   
964  C CA  . VAL A 126 ? 0.34099 0.54457 0.46225 0.01294  -0.02066 -0.00532 126 VAL A CA  
965  C C   . VAL A 126 ? 0.31658 0.51108 0.43392 -0.00243 -0.02436 -0.00789 126 VAL A C   
966  O O   . VAL A 126 ? 0.36505 0.53353 0.46635 -0.00438 -0.02293 -0.00758 126 VAL A O   
967  C CB  . VAL A 126 ? 0.33608 0.53196 0.44524 0.02504  -0.02732 -0.00538 126 VAL A CB  
968  C CG1 . VAL A 126 ? 0.35254 0.56954 0.46964 0.02421  -0.03893 -0.00888 126 VAL A CG1 
969  C CG2 . VAL A 126 ? 0.32139 0.51530 0.42858 0.04001  -0.02246 -0.00189 126 VAL A CG2 
970  N N   . LYS A 127 ? 0.34031 0.55615 0.47276 -0.01334 -0.02893 -0.01055 127 LYS A N   
971  C CA  . LYS A 127 ? 0.39070 0.59694 0.51914 -0.02919 -0.03415 -0.01387 127 LYS A CA  
972  C C   . LYS A 127 ? 0.44653 0.67789 0.58811 -0.03412 -0.04557 -0.01878 127 LYS A C   
973  O O   . LYS A 127 ? 0.46296 0.72274 0.61990 -0.02551 -0.04819 -0.01873 127 LYS A O   
974  C CB  . LYS A 127 ? 0.42314 0.62680 0.55703 -0.04380 -0.02619 -0.01143 127 LYS A CB  
975  C CG  . LYS A 127 ? 0.43983 0.61859 0.55948 -0.03985 -0.01682 -0.00693 127 LYS A CG  
976  C CD  . LYS A 127 ? 0.44247 0.61606 0.56352 -0.05454 -0.01024 -0.00393 127 LYS A CD  
977  C CE  . LYS A 127 ? 0.57149 0.72408 0.67886 -0.04912 -0.00207 0.00071  127 LYS A CE  
978  N NZ  . LYS A 127 ? 0.47479 0.61974 0.57958 -0.06238 0.00431  0.00480  127 LYS A NZ  
979  N N   . SER A 128 ? 0.49179 0.71244 0.62709 -0.04768 -0.05312 -0.02349 128 SER A N   
980  C CA  . SER A 128 ? 0.55248 0.79707 0.69991 -0.05433 -0.06589 -0.02935 128 SER A CA  
981  C C   . SER A 128 ? 0.61091 0.88709 0.78653 -0.07052 -0.06378 -0.02948 128 SER A C   
982  O O   . SER A 128 ? 0.56429 0.83438 0.74349 -0.08076 -0.05303 -0.02561 128 SER A O   
983  C CB  . SER A 128 ? 0.58314 0.80214 0.71056 -0.06270 -0.07596 -0.03585 128 SER A CB  
984  O OG  . SER A 128 ? 0.65228 0.86139 0.78232 -0.08379 -0.07490 -0.03780 128 SER A OG  
985  N N   . SER A 129 ? 0.63040 0.94199 0.82607 -0.07264 -0.07430 -0.03378 129 SER A N   
986  C CA  . SER A 129 ? 0.57581 0.92439 0.80251 -0.08867 -0.07287 -0.03451 129 SER A CA  
987  C C   . SER A 129 ? 0.67579 1.00746 0.89974 -0.11472 -0.07305 -0.03698 129 SER A C   
988  O O   . SER A 129 ? 0.73946 1.08995 0.98353 -0.13056 -0.06519 -0.03456 129 SER A O   
989  C CB  . SER A 129 ? 0.63107 1.02213 0.87992 -0.08490 -0.08668 -0.03955 129 SER A CB  
990  O OG  . SER A 129 ? 0.63712 1.01706 0.87367 -0.09279 -0.10287 -0.04717 129 SER A OG  
991  N N   . GLY A 130 ? 0.75304 1.04823 0.95124 -0.11935 -0.08120 -0.04166 130 GLY A N   
992  C CA  . GLY A 130 ? 0.82728 1.09948 1.01851 -0.14313 -0.08262 -0.04472 130 GLY A CA  
993  C C   . GLY A 130 ? 0.90697 1.13861 1.06680 -0.14231 -0.09288 -0.05138 130 GLY A C   
994  O O   . GLY A 130 ? 1.00626 1.19796 1.14551 -0.15132 -0.08917 -0.05133 130 GLY A O   
995  N N   . GLY A 131 ? 0.76635 1.00699 0.92047 -0.13017 -0.10567 -0.05707 131 GLY A N   
996  C CA  . GLY A 131 ? 0.80678 1.01088 0.92875 -0.12591 -0.11470 -0.06374 131 GLY A CA  
997  C C   . GLY A 131 ? 0.73888 0.90872 0.83471 -0.10712 -0.10470 -0.05862 131 GLY A C   
998  O O   . GLY A 131 ? 0.69551 0.86697 0.79727 -0.09931 -0.09149 -0.05019 131 GLY A O   
999  N N   . PRO A 132 ? 0.72159 0.86075 0.78805 -0.09990 -0.11083 -0.06416 132 PRO A N   
1000 C CA  . PRO A 132 ? 0.65662 0.76797 0.70056 -0.08157 -0.10136 -0.05964 132 PRO A CA  
1001 C C   . PRO A 132 ? 0.58583 0.71971 0.63784 -0.06222 -0.09686 -0.05301 132 PRO A C   
1002 O O   . PRO A 132 ? 0.61466 0.77902 0.67981 -0.05791 -0.10481 -0.05396 132 PRO A O   
1003 C CB  . PRO A 132 ? 0.64966 0.73145 0.66265 -0.07798 -0.11047 -0.06846 132 PRO A CB  
1004 C CG  . PRO A 132 ? 0.66682 0.76908 0.68691 -0.08888 -0.12702 -0.07713 132 PRO A CG  
1005 C CD  . PRO A 132 ? 0.69105 0.81929 0.74278 -0.10868 -0.12639 -0.07543 132 PRO A CD  
1006 N N   . PHE A 133 ? 0.52555 0.64314 0.56896 -0.05029 -0.08457 -0.04639 133 PHE A N   
1007 C CA  . PHE A 133 ? 0.49931 0.63156 0.54816 -0.03323 -0.07857 -0.03969 133 PHE A CA  
1008 C C   . PHE A 133 ? 0.43815 0.54910 0.46087 -0.01817 -0.07866 -0.04023 133 PHE A C   
1009 O O   . PHE A 133 ? 0.39912 0.48392 0.40650 -0.01434 -0.07088 -0.03896 133 PHE A O   
1010 C CB  . PHE A 133 ? 0.50014 0.63191 0.55956 -0.03226 -0.06484 -0.03215 133 PHE A CB  
1011 C CG  . PHE A 133 ? 0.42720 0.56998 0.49110 -0.01626 -0.05845 -0.02601 133 PHE A CG  
1012 C CD1 . PHE A 133 ? 0.46884 0.64241 0.55123 -0.01159 -0.06100 -0.02439 133 PHE A CD1 
1013 C CD2 . PHE A 133 ? 0.40562 0.52787 0.45586 -0.00603 -0.04989 -0.02207 133 PHE A CD2 
1014 C CE1 . PHE A 133 ? 0.41216 0.59071 0.49604 0.00329  -0.05509 -0.01901 133 PHE A CE1 
1015 C CE2 . PHE A 133 ? 0.38362 0.51285 0.43710 0.00656  -0.04412 -0.01678 133 PHE A CE2 
1016 C CZ  . PHE A 133 ? 0.35483 0.50970 0.42357 0.01133  -0.04668 -0.01526 133 PHE A CZ  
1017 N N   . VAL A 134 ? 0.47272 0.59582 0.49012 -0.00933 -0.08741 -0.04192 134 VAL A N   
1018 C CA  . VAL A 134 ? 0.46423 0.57028 0.45636 0.00567  -0.08650 -0.04101 134 VAL A CA  
1019 C C   . VAL A 134 ? 0.46652 0.59105 0.46534 0.01958  -0.08534 -0.03420 134 VAL A C   
1020 O O   . VAL A 134 ? 0.54520 0.69634 0.55894 0.01989  -0.09425 -0.03481 134 VAL A O   
1021 C CB  . VAL A 134 ? 0.42997 0.52515 0.39972 0.00428  -0.09916 -0.04985 134 VAL A CB  
1022 C CG1 . VAL A 134 ? 0.46517 0.53990 0.40607 0.01968  -0.09487 -0.04810 134 VAL A CG1 
1023 C CG2 . VAL A 134 ? 0.52342 0.59924 0.48736 -0.01092 -0.10187 -0.05765 134 VAL A CG2 
1024 N N   . VAL A 135 ? 0.44297 0.55346 0.43122 0.03107  -0.07451 -0.02778 135 VAL A N   
1025 C CA  . VAL A 135 ? 0.46330 0.58418 0.45465 0.04427  -0.07188 -0.02058 135 VAL A CA  
1026 C C   . VAL A 135 ? 0.44794 0.54556 0.41498 0.05515  -0.06385 -0.01618 135 VAL A C   
1027 O O   . VAL A 135 ? 0.45247 0.53154 0.41094 0.05258  -0.05540 -0.01672 135 VAL A O   
1028 C CB  . VAL A 135 ? 0.37014 0.50486 0.38622 0.04273  -0.06357 -0.01572 135 VAL A CB  
1029 C CG1 . VAL A 135 ? 0.36322 0.47891 0.37613 0.04220  -0.04992 -0.01199 135 VAL A CG1 
1030 C CG2 . VAL A 135 ? 0.42779 0.57793 0.45056 0.05532  -0.06498 -0.01057 135 VAL A CG2 
1031 N N   . ASP A 136 ? 0.44404 0.54298 0.39951 0.06760  -0.06644 -0.01159 136 ASP A N   
1032 C CA  . ASP A 136 ? 0.45478 0.53303 0.38837 0.07725  -0.05694 -0.00557 136 ASP A CA  
1033 C C   . ASP A 136 ? 0.45914 0.53655 0.40488 0.08090  -0.04538 0.00239  136 ASP A C   
1034 O O   . ASP A 136 ? 0.46185 0.55328 0.42159 0.08503  -0.04811 0.00533  136 ASP A O   
1035 C CB  . ASP A 136 ? 0.46760 0.54278 0.37755 0.08872  -0.06500 -0.00361 136 ASP A CB  
1036 C CG  . ASP A 136 ? 0.49487 0.56148 0.38295 0.08634  -0.07338 -0.01158 136 ASP A CG  
1037 O OD1 . ASP A 136 ? 0.50033 0.55260 0.38232 0.08011  -0.06693 -0.01587 136 ASP A OD1 
1038 O OD2 . ASP A 136 ? 0.51935 0.59324 0.39575 0.09135  -0.08699 -0.01406 136 ASP A OD2 
1039 N N   . VAL A 137 ? 0.40980 0.47132 0.35037 0.07968  -0.03279 0.00526  137 VAL A N   
1040 C CA  . VAL A 137 ? 0.48182 0.54024 0.43284 0.08093  -0.02200 0.01164  137 VAL A CA  
1041 C C   . VAL A 137 ? 0.44166 0.48452 0.37283 0.09004  -0.01543 0.01930  137 VAL A C   
1042 O O   . VAL A 137 ? 0.51579 0.54566 0.42975 0.09080  -0.00940 0.02013  137 VAL A O   
1043 C CB  . VAL A 137 ? 0.45714 0.51136 0.41892 0.07233  -0.01315 0.00981  137 VAL A CB  
1044 C CG1 . VAL A 137 ? 0.43703 0.48899 0.40948 0.07261  -0.00382 0.01525  137 VAL A CG1 
1045 C CG2 . VAL A 137 ? 0.38634 0.45192 0.36359 0.06308  -0.01927 0.00339  137 VAL A CG2 
1046 N N   . VAL A 138 ? 0.44682 0.48994 0.37957 0.09721  -0.01573 0.02513  138 VAL A N   
1047 C CA  . VAL A 138 ? 0.50229 0.52777 0.41445 0.10594  -0.01008 0.03376  138 VAL A CA  
1048 C C   . VAL A 138 ? 0.53735 0.55428 0.45970 0.10410  0.00046  0.03891  138 VAL A C   
1049 O O   . VAL A 138 ? 0.53060 0.55650 0.47036 0.10435  -0.00192 0.03760  138 VAL A O   
1050 C CB  . VAL A 138 ? 0.51447 0.54292 0.41427 0.11817  -0.02141 0.03657  138 VAL A CB  
1051 C CG1 . VAL A 138 ? 0.50875 0.51467 0.37992 0.12716  -0.01592 0.04601  138 VAL A CG1 
1052 C CG2 . VAL A 138 ? 0.47116 0.51422 0.36825 0.11730  -0.03497 0.02882  138 VAL A CG2 
1053 N N   . ILE A 139 ? 0.52918 0.52934 0.44070 0.10175  0.01234  0.04424  139 ILE A N   
1054 C CA  . ILE A 139 ? 0.50664 0.49693 0.42693 0.09737  0.02241  0.04836  139 ILE A CA  
1055 C C   . ILE A 139 ? 0.51479 0.48279 0.41323 0.10436  0.02772  0.05835  139 ILE A C   
1056 O O   . ILE A 139 ? 0.54278 0.49936 0.42210 0.10459  0.03443  0.06323  139 ILE A O   
1057 C CB  . ILE A 139 ? 0.44539 0.43722 0.37594 0.08629  0.03221  0.04605  139 ILE A CB  
1058 C CG1 . ILE A 139 ? 0.41485 0.42435 0.36152 0.08097  0.02642  0.03716  139 ILE A CG1 
1059 C CG2 . ILE A 139 ? 0.47014 0.45498 0.41266 0.08015  0.03996  0.04847  139 ILE A CG2 
1060 C CD1 . ILE A 139 ? 0.37496 0.38741 0.33237 0.07252  0.03438  0.03472  139 ILE A CD1 
1061 N N   . ASN A 140 ? 0.50933 0.46963 0.40904 0.11057  0.02545  0.06164  140 ASN A N   
1062 C CA  . ASN A 140 ? 0.56114 0.49568 0.43851 0.11822  0.02978  0.07184  140 ASN A CA  
1063 C C   . ASN A 140 ? 0.57999 0.50871 0.43015 0.12772  0.02552  0.07681  140 ASN A C   
1064 O O   . ASN A 140 ? 0.64772 0.55593 0.47512 0.12797  0.03437  0.08526  140 ASN A O   
1065 C CB  . ASN A 140 ? 0.50152 0.41720 0.37718 0.10747  0.04458  0.07693  140 ASN A CB  
1066 C CG  . ASN A 140 ? 0.52648 0.44511 0.42549 0.09892  0.04723  0.07187  140 ASN A CG  
1067 O OD1 . ASN A 140 ? 0.52431 0.44284 0.42994 0.10527  0.04136  0.06960  140 ASN A OD1 
1068 N ND2 . ASN A 140 ? 0.52253 0.44500 0.43381 0.08528  0.05587  0.06970  140 ASN A ND2 
1069 N N   . ASP A 141 ? 0.57648 0.52442 0.42894 0.13462  0.01185  0.07117  141 ASP A N   
1070 C CA  . ASP A 141 ? 0.65559 0.60267 0.48343 0.14455  0.00337  0.07334  141 ASP A CA  
1071 C C   . ASP A 141 ? 0.61747 0.56294 0.43136 0.13820  0.00901  0.07159  141 ASP A C   
1072 O O   . ASP A 141 ? 0.65207 0.59342 0.44072 0.14594  0.00332  0.07326  141 ASP A O   
1073 C CB  . ASP A 141 ? 0.67968 0.60215 0.48002 0.15799  0.00353  0.08506  141 ASP A CB  
1074 C CG  . ASP A 141 ? 0.76656 0.69001 0.57829 0.16796  -0.00316 0.08621  141 ASP A CG  
1075 O OD1 . ASP A 141 ? 0.72729 0.67771 0.56005 0.17093  -0.01492 0.07811  141 ASP A OD1 
1076 O OD2 . ASP A 141 ? 0.85204 0.74914 0.65210 0.17245  0.00397  0.09492  141 ASP A OD2 
1077 N N   . ILE A 142 ? 0.62425 0.57361 0.45326 0.12552  0.01943  0.06773  142 ILE A N   
1078 C CA  . ILE A 142 ? 0.58626 0.53705 0.40580 0.12067  0.02510  0.06439  142 ILE A CA  
1079 C C   . ILE A 142 ? 0.57910 0.55102 0.41696 0.11583  0.01555  0.05224  142 ILE A C   
1080 O O   . ILE A 142 ? 0.54375 0.52748 0.40875 0.10853  0.01517  0.04751  142 ILE A O   
1081 C CB  . ILE A 142 ? 0.57797 0.52127 0.40365 0.11081  0.04280  0.06809  142 ILE A CB  
1082 C CG1 . ILE A 142 ? 0.64842 0.56847 0.45740 0.11273  0.05298  0.08060  142 ILE A CG1 
1083 C CG2 . ILE A 142 ? 0.62903 0.57612 0.44609 0.10813  0.04932  0.06410  142 ILE A CG2 
1084 C CD1 . ILE A 142 ? 0.72734 0.63118 0.49931 0.12364  0.05204  0.08823  142 ILE A CD1 
1085 N N   . HIS A 143 ? 0.58013 0.55475 0.40130 0.11938  0.00790  0.04711  143 HIS A N   
1086 C CA  . HIS A 143 ? 0.58399 0.57406 0.41946 0.11348  -0.00090 0.03559  143 HIS A CA  
1087 C C   . HIS A 143 ? 0.57613 0.56562 0.42126 0.10511  0.01055  0.03188  143 HIS A C   
1088 O O   . HIS A 143 ? 0.56813 0.54796 0.39524 0.10686  0.01959  0.03292  143 HIS A O   
1089 C CB  . HIS A 143 ? 0.63647 0.62695 0.44954 0.11887  -0.01323 0.03005  143 HIS A CB  
1090 C CG  . HIS A 143 ? 0.82087 0.82266 0.64625 0.11112  -0.02182 0.01809  143 HIS A CG  
1091 N ND1 . HIS A 143 ? 0.84426 0.83853 0.66045 0.10761  -0.01670 0.01184  143 HIS A ND1 
1092 C CD2 . HIS A 143 ? 0.73376 0.75261 0.57992 0.10585  -0.03432 0.01153  143 HIS A CD2 
1093 C CE1 . HIS A 143 ? 0.67523 0.67783 0.50385 0.10038  -0.02638 0.00206  143 HIS A CE1 
1094 N NE2 . HIS A 143 ? 0.75383 0.77224 0.60132 0.09813  -0.03685 0.00194  143 HIS A NE2 
1095 N N   . PHE A 144 ? 0.54847 0.54922 0.42134 0.09707  0.01004  0.02750  144 PHE A N   
1096 C CA  . PHE A 144 ? 0.47672 0.47859 0.36208 0.09031  0.01985  0.02480  144 PHE A CA  
1097 C C   . PHE A 144 ? 0.46463 0.46932 0.34987 0.08754  0.01419  0.01500  144 PHE A C   
1098 O O   . PHE A 144 ? 0.46643 0.46624 0.34619 0.08779  0.02214  0.01271  144 PHE A O   
1099 C CB  . PHE A 144 ? 0.44078 0.45043 0.35326 0.08374  0.02269  0.02624  144 PHE A CB  
1100 C CG  . PHE A 144 ? 0.42468 0.43754 0.35136 0.07761  0.03121  0.02397  144 PHE A CG  
1101 C CD1 . PHE A 144 ? 0.42842 0.43711 0.35356 0.07687  0.04432  0.02892  144 PHE A CD1 
1102 C CD2 . PHE A 144 ? 0.41483 0.43559 0.35661 0.07258  0.02606  0.01731  144 PHE A CD2 
1103 C CE1 . PHE A 144 ? 0.45376 0.46937 0.39428 0.07232  0.05101  0.02655  144 PHE A CE1 
1104 C CE2 . PHE A 144 ? 0.41757 0.44130 0.37128 0.06895  0.03261  0.01560  144 PHE A CE2 
1105 C CZ  . PHE A 144 ? 0.44171 0.46451 0.39589 0.06937  0.04454  0.01986  144 PHE A CZ  
1106 N N   . GLU A 145 ? 0.42830 0.44062 0.32015 0.08474  0.00103  0.00911  145 GLU A N   
1107 C CA  . GLU A 145 ? 0.42095 0.43227 0.31264 0.08016  -0.00470 -0.00016 145 GLU A CA  
1108 C C   . GLU A 145 ? 0.41914 0.43979 0.31492 0.07673  -0.02009 -0.00512 145 GLU A C   
1109 O O   . GLU A 145 ? 0.43482 0.46646 0.33912 0.07841  -0.02520 -0.00133 145 GLU A O   
1110 C CB  . GLU A 145 ? 0.48596 0.49992 0.39830 0.07355  0.00122  -0.00170 145 GLU A CB  
1111 C CG  . GLU A 145 ? 0.39504 0.42167 0.33205 0.06727  -0.00186 0.00020  145 GLU A CG  
1112 C CD  . GLU A 145 ? 0.43504 0.46309 0.38896 0.06189  0.00399  -0.00029 145 GLU A CD  
1113 O OE1 . GLU A 145 ? 0.49825 0.51883 0.44712 0.06345  0.00954  -0.00236 145 GLU A OE1 
1114 O OE2 . GLU A 145 ? 0.38682 0.42385 0.35837 0.05717  0.00295  0.00133  145 GLU A OE2 
1115 N N   . ARG A 146 ? 0.45526 0.47154 0.34534 0.07195  -0.02736 -0.01393 146 ARG A N   
1116 C CA  . ARG A 146 ? 0.49364 0.52059 0.39276 0.06446  -0.04149 -0.01992 146 ARG A CA  
1117 C C   . ARG A 146 ? 0.45328 0.47997 0.37013 0.05376  -0.04014 -0.02356 146 ARG A C   
1118 O O   . ARG A 146 ? 0.47337 0.48439 0.37985 0.05153  -0.03882 -0.02912 146 ARG A O   
1119 C CB  . ARG A 146 ? 0.51390 0.53310 0.38898 0.06577  -0.05261 -0.02770 146 ARG A CB  
1120 C CG  . ARG A 146 ? 0.54684 0.57654 0.43238 0.05487  -0.06735 -0.03553 146 ARG A CG  
1121 C CD  . ARG A 146 ? 0.56242 0.58842 0.42416 0.05709  -0.08099 -0.04278 146 ARG A CD  
1122 N NE  . ARG A 146 ? 0.54348 0.58076 0.39800 0.06783  -0.08569 -0.03697 146 ARG A NE  
1123 C CZ  . ARG A 146 ? 0.60719 0.64758 0.44375 0.07147  -0.09985 -0.04152 146 ARG A CZ  
1124 N NH1 . ARG A 146 ? 0.61741 0.65066 0.44142 0.06397  -0.11117 -0.05303 146 ARG A NH1 
1125 N NH2 . ARG A 146 ? 0.53645 0.58577 0.36604 0.08313  -0.10344 -0.03451 146 ARG A NH2 
1126 N N   . PHE A 147 ? 0.45075 0.49302 0.39214 0.04813  -0.04011 -0.02029 147 PHE A N   
1127 C CA  . PHE A 147 ? 0.39883 0.43991 0.35533 0.03856  -0.03736 -0.02177 147 PHE A CA  
1128 C C   . PHE A 147 ? 0.37683 0.41977 0.33629 0.02701  -0.04816 -0.02895 147 PHE A C   
1129 O O   . PHE A 147 ? 0.38041 0.44188 0.35064 0.02287  -0.05671 -0.03002 147 PHE A O   
1130 C CB  . PHE A 147 ? 0.41054 0.46616 0.38928 0.03716  -0.03182 -0.01553 147 PHE A CB  
1131 C CG  . PHE A 147 ? 0.38293 0.43598 0.37372 0.02836  -0.02839 -0.01597 147 PHE A CG  
1132 C CD1 . PHE A 147 ? 0.38997 0.45248 0.39311 0.01735  -0.03406 -0.01844 147 PHE A CD1 
1133 C CD2 . PHE A 147 ? 0.32677 0.36835 0.31592 0.03099  -0.01965 -0.01369 147 PHE A CD2 
1134 C CE1 . PHE A 147 ? 0.37783 0.43487 0.38819 0.00938  -0.03036 -0.01774 147 PHE A CE1 
1135 C CE2 . PHE A 147 ? 0.37671 0.41430 0.37383 0.02435  -0.01755 -0.01351 147 PHE A CE2 
1136 C CZ  . PHE A 147 ? 0.32092 0.36438 0.32692 0.01365  -0.02259 -0.01513 147 PHE A CZ  
1137 N N   . ARG A 148 ? 0.38874 0.41267 0.33959 0.02168  -0.04761 -0.03377 148 ARG A N   
1138 C CA  . ARG A 148 ? 0.44172 0.46210 0.39589 0.00784  -0.05583 -0.03990 148 ARG A CA  
1139 C C   . ARG A 148 ? 0.41314 0.42572 0.37767 0.00141  -0.04877 -0.03683 148 ARG A C   
1140 O O   . ARG A 148 ? 0.45080 0.44566 0.40603 0.00768  -0.04150 -0.03574 148 ARG A O   
1141 C CB  . ARG A 148 ? 0.46448 0.46223 0.39366 0.00714  -0.06263 -0.04908 148 ARG A CB  
1142 C CG  . ARG A 148 ? 0.53278 0.53425 0.44540 0.01492  -0.06975 -0.05244 148 ARG A CG  
1143 C CD  . ARG A 148 ? 0.56650 0.54236 0.45139 0.01434  -0.07589 -0.06269 148 ARG A CD  
1144 N NE  . ARG A 148 ? 0.54876 0.53219 0.42120 0.01499  -0.08879 -0.06829 148 ARG A NE  
1145 C CZ  . ARG A 148 ? 0.57301 0.55845 0.42843 0.02841  -0.08819 -0.06621 148 ARG A CZ  
1146 N NH1 . ARG A 148 ? 0.56992 0.55046 0.41966 0.04096  -0.07438 -0.05884 148 ARG A NH1 
1147 N NH2 . ARG A 148 ? 0.61205 0.60496 0.45562 0.02873  -0.10196 -0.07139 148 ARG A NH2 
1148 N N   . GLY A 149 ? 0.40028 0.42721 0.38370 -0.01033 -0.05070 -0.03517 149 GLY A N   
1149 C CA  . GLY A 149 ? 0.38650 0.40646 0.37785 -0.01615 -0.04382 -0.03100 149 GLY A CA  
1150 C C   . GLY A 149 ? 0.43432 0.47584 0.44706 -0.02840 -0.04478 -0.02848 149 GLY A C   
1151 O O   . GLY A 149 ? 0.52333 0.58166 0.54461 -0.03601 -0.05266 -0.03205 149 GLY A O   
1152 N N   . ASP A 150 ? 0.37543 0.41796 0.39685 -0.02994 -0.03665 -0.02245 150 ASP A N   
1153 C CA  . ASP A 150 ? 0.36477 0.42782 0.40534 -0.04089 -0.03497 -0.01944 150 ASP A CA  
1154 C C   . ASP A 150 ? 0.34519 0.43712 0.40205 -0.03298 -0.03211 -0.01613 150 ASP A C   
1155 O O   . ASP A 150 ? 0.39834 0.51533 0.47235 -0.03934 -0.03415 -0.01641 150 ASP A O   
1156 C CB  . ASP A 150 ? 0.38417 0.43284 0.42278 -0.04646 -0.02765 -0.01443 150 ASP A CB  
1157 C CG  . ASP A 150 ? 0.43118 0.45190 0.45595 -0.05760 -0.03086 -0.01707 150 ASP A CG  
1158 O OD1 . ASP A 150 ? 0.47037 0.48448 0.48871 -0.06289 -0.03903 -0.02381 150 ASP A OD1 
1159 O OD2 . ASP A 150 ? 0.39087 0.39417 0.40924 -0.06077 -0.02573 -0.01252 150 ASP A OD2 
1160 N N   . GLY A 151 ? 0.34781 0.43684 0.40014 -0.01928 -0.02727 -0.01320 151 GLY A N   
1161 C CA  . GLY A 151 ? 0.29607 0.40673 0.36052 -0.01104 -0.02468 -0.01039 151 GLY A CA  
1162 C C   . GLY A 151 ? 0.30680 0.40759 0.36434 0.00080  -0.01816 -0.00692 151 GLY A C   
1163 O O   . GLY A 151 ? 0.29138 0.37264 0.33672 0.00332  -0.01595 -0.00683 151 GLY A O   
1164 N N   . LEU A 152 ? 0.32004 0.43518 0.38636 0.00801  -0.01511 -0.00434 152 LEU A N   
1165 C CA  . LEU A 152 ? 0.31141 0.41867 0.37279 0.01780  -0.00936 -0.00130 152 LEU A CA  
1166 C C   . LEU A 152 ? 0.25286 0.37019 0.32474 0.01912  -0.00353 0.00109  152 LEU A C   
1167 O O   . LEU A 152 ? 0.25028 0.38533 0.33395 0.01659  -0.00390 0.00065  152 LEU A O   
1168 C CB  . LEU A 152 ? 0.28758 0.39479 0.34212 0.02775  -0.01206 -0.00088 152 LEU A CB  
1169 C CG  . LEU A 152 ? 0.33011 0.42411 0.36904 0.02923  -0.01613 -0.00317 152 LEU A CG  
1170 C CD1 . LEU A 152 ? 0.30881 0.40476 0.33970 0.03897  -0.01916 -0.00182 152 LEU A CD1 
1171 C CD2 . LEU A 152 ? 0.28219 0.35838 0.31195 0.03033  -0.01011 -0.00233 152 LEU A CD2 
1172 N N   . CYS A 153 ? 0.26601 0.37293 0.33369 0.02316  0.00192  0.00308  153 CYS A N   
1173 C CA  . CYS A 153 ? 0.27796 0.38969 0.35142 0.02445  0.00729  0.00425  153 CYS A CA  
1174 C C   . CYS A 153 ? 0.26101 0.36454 0.33017 0.03256  0.01036  0.00553  153 CYS A C   
1175 O O   . CYS A 153 ? 0.28517 0.37642 0.34774 0.03307  0.01159  0.00632  153 CYS A O   
1176 C CB  . CYS A 153 ? 0.28932 0.39433 0.36068 0.01767  0.01001  0.00485  153 CYS A CB  
1177 S SG  . CYS A 153 ? 0.36531 0.47151 0.43784 0.01930  0.01603  0.00542  153 CYS A SG  
1178 N N   . MET A 154 ? 0.26650 0.37660 0.33961 0.03886  0.01194  0.00571  154 MET A N   
1179 C CA  . MET A 154 ? 0.31486 0.41373 0.38276 0.04552  0.01527  0.00697  154 MET A CA  
1180 C C   . MET A 154 ? 0.30198 0.40045 0.37221 0.04527  0.01978  0.00535  154 MET A C   
1181 O O   . MET A 154 ? 0.30443 0.41477 0.38056 0.04795  0.02099  0.00396  154 MET A O   
1182 C CB  . MET A 154 ? 0.29806 0.39885 0.36415 0.05510  0.01312  0.00848  154 MET A CB  
1183 C CG  . MET A 154 ? 0.30134 0.38444 0.35839 0.06089  0.01674  0.01094  154 MET A CG  
1184 S SD  . MET A 154 ? 0.41138 0.47937 0.45905 0.05627  0.01865  0.01350  154 MET A SD  
1185 C CE  . MET A 154 ? 0.31608 0.37986 0.35247 0.06493  0.01537  0.01739  154 MET A CE  
1186 N N   . SER A 155 ? 0.35097 0.43720 0.41665 0.04233  0.02219  0.00507  155 SER A N   
1187 C CA  . SER A 155 ? 0.34231 0.42698 0.40743 0.04013  0.02499  0.00258  155 SER A CA  
1188 C C   . SER A 155 ? 0.34530 0.41627 0.40533 0.04355  0.02755  0.00124  155 SER A C   
1189 O O   . SER A 155 ? 0.34375 0.40406 0.40089 0.04347  0.02777  0.00307  155 SER A O   
1190 C CB  . SER A 155 ? 0.31114 0.39396 0.37500 0.03269  0.02373  0.00255  155 SER A CB  
1191 O OG  . SER A 155 ? 0.36216 0.44075 0.42245 0.03099  0.02516  0.00007  155 SER A OG  
1192 N N   . THR A 156 ? 0.35867 0.42895 0.41656 0.04612  0.03011  -0.00212 156 THR A N   
1193 C CA  . THR A 156 ? 0.33565 0.38968 0.38655 0.04728  0.03204  -0.00508 156 THR A CA  
1194 C C   . THR A 156 ? 0.32469 0.37374 0.37426 0.03831  0.03017  -0.00656 156 THR A C   
1195 O O   . THR A 156 ? 0.34738 0.40555 0.40010 0.03357  0.02789  -0.00537 156 THR A O   
1196 C CB  . THR A 156 ? 0.38920 0.44379 0.43614 0.05331  0.03530  -0.00948 156 THR A CB  
1197 O OG1 . THR A 156 ? 0.37252 0.43869 0.41986 0.04888  0.03589  -0.01111 156 THR A OG1 
1198 C CG2 . THR A 156 ? 0.38020 0.44314 0.43107 0.06407  0.03687  -0.00827 156 THR A CG2 
1199 N N   . PRO A 157 ? 0.34677 0.38100 0.39177 0.03581  0.03055  -0.00925 157 PRO A N   
1200 C CA  . PRO A 157 ? 0.33827 0.37191 0.38388 0.02739  0.02744  -0.01186 157 PRO A CA  
1201 C C   . PRO A 157 ? 0.37887 0.41995 0.42020 0.02655  0.02562  -0.01496 157 PRO A C   
1202 O O   . PRO A 157 ? 0.36704 0.41656 0.41112 0.02255  0.02221  -0.01345 157 PRO A O   
1203 C CB  . PRO A 157 ? 0.35810 0.37372 0.39874 0.02453  0.02825  -0.01550 157 PRO A CB  
1204 C CG  . PRO A 157 ? 0.44448 0.44940 0.48281 0.03051  0.03212  -0.01188 157 PRO A CG  
1205 C CD  . PRO A 157 ? 0.38903 0.40557 0.42818 0.03988  0.03316  -0.00973 157 PRO A CD  
1206 N N   . SER A 158 ? 0.39669 0.43396 0.42977 0.03131  0.02832  -0.01894 158 SER A N   
1207 C CA  A SER A 158 ? 0.40259 0.44621 0.42870 0.03050  0.02787  -0.02125 158 SER A CA  
1208 C CA  B SER A 158 ? 0.47684 0.52044 0.50270 0.03101  0.02825  -0.02135 158 SER A CA  
1209 C C   . SER A 158 ? 0.38974 0.44860 0.42077 0.03029  0.02880  -0.01596 158 SER A C   
1210 O O   . SER A 158 ? 0.40896 0.47187 0.43410 0.02736  0.02760  -0.01550 158 SER A O   
1211 C CB  A SER A 158 ? 0.40421 0.44134 0.41942 0.03678  0.03230  -0.02687 158 SER A CB  
1212 C CB  B SER A 158 ? 0.39273 0.43116 0.40918 0.03826  0.03333  -0.02628 158 SER A CB  
1213 O OG  A SER A 158 ? 0.37662 0.42081 0.39663 0.04501  0.03766  -0.02488 158 SER A OG  
1214 O OG  B SER A 158 ? 0.40356 0.43628 0.40666 0.03635  0.03209  -0.03199 158 SER A OG  
1215 N N   . GLY A 159 ? 0.37437 0.44011 0.41450 0.03277  0.03034  -0.01189 159 GLY A N   
1216 C CA  . GLY A 159 ? 0.34810 0.42628 0.39313 0.03050  0.03044  -0.00755 159 GLY A CA  
1217 C C   . GLY A 159 ? 0.35714 0.43436 0.40429 0.02521  0.02579  -0.00429 159 GLY A C   
1218 O O   . GLY A 159 ? 0.32125 0.40409 0.36927 0.02231  0.02540  -0.00106 159 GLY A O   
1219 N N   . THR A 160 ? 0.37815 0.44828 0.42639 0.02382  0.02264  -0.00519 160 THR A N   
1220 C CA  . THR A 160 ? 0.34082 0.41193 0.39264 0.02111  0.01890  -0.00241 160 THR A CA  
1221 C C   . THR A 160 ? 0.36500 0.43701 0.41056 0.01884  0.01589  -0.00128 160 THR A C   
1222 O O   . THR A 160 ? 0.36910 0.44120 0.41559 0.01827  0.01347  0.00184  160 THR A O   
1223 C CB  . THR A 160 ? 0.33145 0.39887 0.38803 0.01974  0.01722  -0.00377 160 THR A CB  
1224 O OG1 . THR A 160 ? 0.31005 0.37327 0.36265 0.01755  0.01563  -0.00825 160 THR A OG1 
1225 C CG2 . THR A 160 ? 0.36630 0.43003 0.42672 0.02185  0.02067  -0.00259 160 THR A CG2 
1226 N N   . THR A 161 ? 0.31846 0.38899 0.35517 0.01838  0.01606  -0.00369 161 THR A N   
1227 C CA  . THR A 161 ? 0.35404 0.42345 0.38088 0.01692  0.01344  -0.00157 161 THR A CA  
1228 C C   . THR A 161 ? 0.38273 0.45431 0.40533 0.01524  0.01793  0.00248  161 THR A C   
1229 O O   . THR A 161 ? 0.37005 0.43786 0.38203 0.01347  0.01690  0.00572  161 THR A O   
1230 C CB  . THR A 161 ? 0.37252 0.43864 0.38832 0.01702  0.01148  -0.00596 161 THR A CB  
1231 O OG1 . THR A 161 ? 0.40708 0.47254 0.41994 0.01878  0.01726  -0.00987 161 THR A OG1 
1232 C CG2 . THR A 161 ? 0.37900 0.44440 0.40008 0.01605  0.00505  -0.00962 161 THR A CG2 
1233 N N   . ALA A 162 ? 0.37195 0.44971 0.40262 0.01538  0.02249  0.00275  162 ALA A N   
1234 C CA  . ALA A 162 ? 0.35886 0.44303 0.38930 0.01212  0.02731  0.00578  162 ALA A CA  
1235 C C   . ALA A 162 ? 0.33884 0.42238 0.37554 0.00870  0.02498  0.00916  162 ALA A C   
1236 O O   . ALA A 162 ? 0.31188 0.38589 0.34405 0.00805  0.02047  0.01123  162 ALA A O   
1237 C CB  . ALA A 162 ? 0.34355 0.43818 0.37951 0.01546  0.03327  0.00272  162 ALA A CB  
1238 N N   . TYR A 163 ? 0.38823 0.48146 0.43444 0.00705  0.02726  0.00931  163 TYR A N   
1239 C CA  . TYR A 163 ? 0.32494 0.41618 0.37525 0.00319  0.02408  0.01111  163 TYR A CA  
1240 C C   . TYR A 163 ? 0.34775 0.42980 0.39795 0.00748  0.01912  0.01009  163 TYR A C   
1241 O O   . TYR A 163 ? 0.35011 0.42260 0.39626 0.00569  0.01589  0.01161  163 TYR A O   
1242 C CB  . TYR A 163 ? 0.35117 0.45789 0.41345 0.00223  0.02572  0.00986  163 TYR A CB  
1243 C CG  . TYR A 163 ? 0.34491 0.45284 0.41072 -0.00557 0.02318  0.01121  163 TYR A CG  
1244 C CD1 . TYR A 163 ? 0.33984 0.43098 0.39646 -0.01020 0.01991  0.01326  163 TYR A CD1 
1245 C CD2 . TYR A 163 ? 0.34626 0.47187 0.42450 -0.00793 0.02337  0.00988  163 TYR A CD2 
1246 C CE1 . TYR A 163 ? 0.36613 0.45461 0.42396 -0.01822 0.01721  0.01350  163 TYR A CE1 
1247 C CE2 . TYR A 163 ? 0.39354 0.52054 0.47534 -0.01676 0.01990  0.01003  163 TYR A CE2 
1248 C CZ  . TYR A 163 ? 0.43026 0.53694 0.50089 -0.02253 0.01696  0.01161  163 TYR A CZ  
1249 O OH  . TYR A 163 ? 0.38938 0.49392 0.46168 -0.03226 0.01313  0.01082  163 TYR A OH  
1250 N N   . ASN A 164 ? 0.29738 0.38120 0.35123 0.01321  0.01923  0.00756  164 ASN A N   
1251 C CA  . ASN A 164 ? 0.28305 0.36075 0.33795 0.01663  0.01648  0.00700  164 ASN A CA  
1252 C C   . ASN A 164 ? 0.35609 0.42583 0.40580 0.01650  0.01348  0.00823  164 ASN A C   
1253 O O   . ASN A 164 ? 0.36246 0.42766 0.41251 0.01863  0.01148  0.00855  164 ASN A O   
1254 C CB  . ASN A 164 ? 0.32047 0.39905 0.37845 0.02062  0.01817  0.00482  164 ASN A CB  
1255 C CG  . ASN A 164 ? 0.33992 0.41399 0.39987 0.02243  0.01697  0.00478  164 ASN A CG  
1256 O OD1 . ASN A 164 ? 0.35480 0.42805 0.41643 0.02461  0.01763  0.00549  164 ASN A OD1 
1257 N ND2 . ASN A 164 ? 0.34154 0.41422 0.40130 0.02158  0.01529  0.00394  164 ASN A ND2 
1258 N N   . LYS A 165 ? 0.32417 0.39233 0.36793 0.01529  0.01303  0.00883  165 LYS A N   
1259 C CA  . LYS A 165 ? 0.30270 0.36446 0.34118 0.01705  0.00882  0.01026  165 LYS A CA  
1260 C C   . LYS A 165 ? 0.30919 0.36100 0.34130 0.01602  0.00715  0.01355  165 LYS A C   
1261 O O   . LYS A 165 ? 0.31129 0.35722 0.34220 0.02042  0.00378  0.01414  165 LYS A O   
1262 C CB  . LYS A 165 ? 0.36585 0.42731 0.39612 0.01644  0.00778  0.01022  165 LYS A CB  
1263 C CG  . LYS A 165 ? 0.27773 0.33446 0.30220 0.01978  0.00172  0.01176  165 LYS A CG  
1264 C CD  . LYS A 165 ? 0.32795 0.38667 0.34508 0.01990  -0.00083 0.00988  165 LYS A CD  
1265 C CE  . LYS A 165 ? 0.30614 0.36312 0.31864 0.02445  -0.00875 0.01121  165 LYS A CE  
1266 N NZ  . LYS A 165 ? 0.35826 0.40332 0.36062 0.02680  -0.01017 0.01721  165 LYS A NZ  
1267 N N   . SER A 166 ? 0.31846 0.36812 0.34676 0.01016  0.00970  0.01549  166 SER A N   
1268 C CA  . SER A 166 ? 0.36470 0.40087 0.38513 0.00710  0.00814  0.01844  166 SER A CA  
1269 C C   . SER A 166 ? 0.37541 0.40789 0.39976 0.00877  0.00638  0.01603  166 SER A C   
1270 O O   . SER A 166 ? 0.33280 0.35008 0.34896 0.00828  0.00408  0.01716  166 SER A O   
1271 C CB  . SER A 166 ? 0.37445 0.41095 0.39138 -0.00221 0.01204  0.02115  166 SER A CB  
1272 O OG  . SER A 166 ? 0.40030 0.43691 0.40881 -0.00326 0.01446  0.02402  166 SER A OG  
1273 N N   . LEU A 167 ? 0.35465 0.39814 0.38866 0.01122  0.00746  0.01278  167 LEU A N   
1274 C CA  . LEU A 167 ? 0.35871 0.39903 0.39367 0.01352  0.00611  0.01036  167 LEU A CA  
1275 C C   . LEU A 167 ? 0.36713 0.40664 0.40368 0.02186  0.00586  0.00918  167 LEU A C   
1276 O O   . LEU A 167 ? 0.37794 0.41711 0.41491 0.02509  0.00638  0.00711  167 LEU A O   
1277 C CB  . LEU A 167 ? 0.30430 0.35661 0.34662 0.01164  0.00735  0.00842  167 LEU A CB  
1278 C CG  . LEU A 167 ? 0.30531 0.36482 0.35065 0.00355  0.00803  0.00906  167 LEU A CG  
1279 C CD1 . LEU A 167 ? 0.30823 0.38367 0.36303 0.00522  0.00904  0.00737  167 LEU A CD1 
1280 C CD2 . LEU A 167 ? 0.32252 0.37197 0.36235 -0.00351 0.00496  0.00868  167 LEU A CD2 
1281 N N   . GLY A 168 ? 0.36238 0.40310 0.39987 0.02533  0.00511  0.01040  168 GLY A N   
1282 C CA  . GLY A 168 ? 0.31446 0.35919 0.35720 0.03244  0.00516  0.00930  168 GLY A CA  
1283 C C   . GLY A 168 ? 0.28017 0.33783 0.33343 0.03243  0.00824  0.00794  168 GLY A C   
1284 O O   . GLY A 168 ? 0.30073 0.36436 0.36065 0.03665  0.00953  0.00721  168 GLY A O   
1285 N N   . GLY A 169 ? 0.30703 0.36885 0.36207 0.02795  0.00996  0.00767  169 GLY A N   
1286 C CA  . GLY A 169 ? 0.29287 0.36164 0.35512 0.02774  0.01296  0.00664  169 GLY A CA  
1287 C C   . GLY A 169 ? 0.35534 0.42980 0.42337 0.02709  0.01153  0.00565  169 GLY A C   
1288 O O   . GLY A 169 ? 0.31058 0.38486 0.37588 0.02728  0.00752  0.00583  169 GLY A O   
1289 N N   . ALA A 170 ? 0.28672 0.36560 0.36196 0.02582  0.01444  0.00470  170 ALA A N   
1290 C CA  . ALA A 170 ? 0.28208 0.36725 0.36428 0.02295  0.01247  0.00268  170 ALA A CA  
1291 C C   . ALA A 170 ? 0.34795 0.42891 0.42488 0.01936  0.01140  0.00049  170 ALA A C   
1292 O O   . ALA A 170 ? 0.36036 0.43564 0.43212 0.01949  0.01438  0.00073  170 ALA A O   
1293 C CB  . ALA A 170 ? 0.30532 0.39576 0.39756 0.02078  0.01685  0.00259  170 ALA A CB  
1294 N N   . LEU A 171 ? 0.24581 0.33035 0.32362 0.01710  0.00675  -0.00211 171 LEU A N   
1295 C CA  . LEU A 171 ? 0.29291 0.37232 0.36402 0.01400  0.00590  -0.00560 171 LEU A CA  
1296 C C   . LEU A 171 ? 0.27126 0.34949 0.34926 0.00886  0.00733  -0.00874 171 LEU A C   
1297 O O   . LEU A 171 ? 0.29577 0.38263 0.38400 0.00537  0.00437  -0.01015 171 LEU A O   
1298 C CB  . LEU A 171 ? 0.28428 0.36573 0.34841 0.01411  -0.00068 -0.00722 171 LEU A CB  
1299 C CG  . LEU A 171 ? 0.26047 0.34234 0.31880 0.01845  -0.00353 -0.00309 171 LEU A CG  
1300 C CD1 . LEU A 171 ? 0.32969 0.41179 0.37826 0.01895  -0.01044 -0.00428 171 LEU A CD1 
1301 C CD2 . LEU A 171 ? 0.25879 0.33391 0.30959 0.01932  0.00146  0.00003  171 LEU A CD2 
1302 N N   . MET A 172 ? 0.30093 0.36860 0.37386 0.00833  0.01179  -0.00975 172 MET A N   
1303 C CA  . MET A 172 ? 0.33093 0.39171 0.40734 0.00272  0.01372  -0.01227 172 MET A CA  
1304 C C   . MET A 172 ? 0.35379 0.40268 0.41950 0.00124  0.01234  -0.01799 172 MET A C   
1305 O O   . MET A 172 ? 0.37279 0.41820 0.42820 0.00647  0.01306  -0.01885 172 MET A O   
1306 C CB  . MET A 172 ? 0.33751 0.39104 0.41486 0.00426  0.02066  -0.00802 172 MET A CB  
1307 C CG  . MET A 172 ? 0.40942 0.45740 0.47820 0.01183  0.02348  -0.00563 172 MET A CG  
1308 S SD  . MET A 172 ? 0.43913 0.48109 0.50769 0.01482  0.02950  0.00025  172 MET A SD  
1309 C CE  . MET A 172 ? 0.33636 0.37894 0.39772 0.02393  0.02925  0.00167  172 MET A CE  
1310 N N   . HIS A 173 ? 0.38471 0.42764 0.45302 -0.00641 0.01076  -0.02228 173 HIS A N   
1311 C CA  . HIS A 173 ? 0.45101 0.47984 0.50787 -0.00898 0.00852  -0.02948 173 HIS A CA  
1312 C C   . HIS A 173 ? 0.49018 0.49954 0.53684 -0.00403 0.01517  -0.02927 173 HIS A C   
1313 O O   . HIS A 173 ? 0.47032 0.47316 0.52089 -0.00417 0.02027  -0.02467 173 HIS A O   
1314 C CB  . HIS A 173 ? 0.39759 0.42582 0.46181 -0.02065 0.00393  -0.03453 173 HIS A CB  
1315 C CG  . HIS A 173 ? 0.43343 0.44575 0.48395 -0.02425 -0.00009 -0.04357 173 HIS A CG  
1316 N ND1 . HIS A 173 ? 0.49003 0.47746 0.52989 -0.02505 0.00446  -0.04666 173 HIS A ND1 
1317 C CD2 . HIS A 173 ? 0.44927 0.46496 0.49251 -0.02647 -0.00855 -0.05056 173 HIS A CD2 
1318 C CE1 . HIS A 173 ? 0.54196 0.51744 0.56866 -0.02787 -0.00065 -0.05598 173 HIS A CE1 
1319 N NE2 . HIS A 173 ? 0.53656 0.52957 0.56473 -0.02908 -0.00877 -0.05858 173 HIS A NE2 
1320 N N   . PRO A 174 ? 0.49408 0.49371 0.52652 0.00143  0.01546  -0.03410 174 PRO A N   
1321 C CA  . PRO A 174 ? 0.45161 0.43650 0.47539 0.01004  0.02177  -0.03337 174 PRO A CA  
1322 C C   . PRO A 174 ? 0.47530 0.43596 0.49419 0.00652  0.02417  -0.03540 174 PRO A C   
1323 O O   . PRO A 174 ? 0.46666 0.41336 0.47810 0.01523  0.02908  -0.03376 174 PRO A O   
1324 C CB  . PRO A 174 ? 0.49622 0.47981 0.50670 0.01664  0.02183  -0.03903 174 PRO A CB  
1325 C CG  . PRO A 174 ? 0.46130 0.46068 0.47297 0.01237  0.01615  -0.03991 174 PRO A CG  
1326 C CD  . PRO A 174 ? 0.48403 0.48738 0.50673 0.00188  0.01052  -0.03985 174 PRO A CD  
1327 N N   . SER A 175 ? 0.47827 0.43300 0.50095 -0.00591 0.02070  -0.03883 175 SER A N   
1328 C CA  . SER A 175 ? 0.49020 0.41967 0.50849 -0.01135 0.02405  -0.03916 175 SER A CA  
1329 C C   . SER A 175 ? 0.49982 0.43055 0.52650 -0.01150 0.02983  -0.02916 175 SER A C   
1330 O O   . SER A 175 ? 0.50416 0.41147 0.52474 -0.01456 0.03417  -0.02702 175 SER A O   
1331 C CB  . SER A 175 ? 0.49653 0.42043 0.51785 -0.02710 0.01854  -0.04623 175 SER A CB  
1332 O OG  . SER A 175 ? 0.51504 0.46624 0.55512 -0.03530 0.01449  -0.04388 175 SER A OG  
1333 N N   . ILE A 176 ? 0.48114 0.43597 0.51903 -0.00814 0.03013  -0.02306 176 ILE A N   
1334 C CA  . ILE A 176 ? 0.52645 0.48350 0.56921 -0.00636 0.03559  -0.01398 176 ILE A CA  
1335 C C   . ILE A 176 ? 0.49547 0.44618 0.52819 0.00823  0.03839  -0.01019 176 ILE A C   
1336 O O   . ILE A 176 ? 0.44422 0.41051 0.47828 0.01615  0.03624  -0.01066 176 ILE A O   
1337 C CB  . ILE A 176 ? 0.46619 0.45058 0.52405 -0.00878 0.03420  -0.01046 176 ILE A CB  
1338 C CG1 . ILE A 176 ? 0.44469 0.44036 0.51539 -0.02161 0.03042  -0.01447 176 ILE A CG1 
1339 C CG2 . ILE A 176 ? 0.42117 0.40643 0.48060 -0.00602 0.04031  -0.00188 176 ILE A CG2 
1340 C CD1 . ILE A 176 ? 0.42810 0.45010 0.51391 -0.02197 0.02942  -0.01115 176 ILE A CD1 
1341 N N   . GLU A 177 ? 0.49115 0.41943 0.51403 0.01158  0.04298  -0.00610 177 GLU A N   
1342 C CA  . GLU A 177 ? 0.48595 0.40951 0.50011 0.02669  0.04457  -0.00215 177 GLU A CA  
1343 C C   . GLU A 177 ? 0.47899 0.41910 0.49910 0.02941  0.04553  0.00548  177 GLU A C   
1344 O O   . GLU A 177 ? 0.49430 0.42435 0.51050 0.02735  0.04958  0.01206  177 GLU A O   
1345 C CB  . GLU A 177 ? 0.52883 0.41910 0.52735 0.03105  0.04816  -0.00055 177 GLU A CB  
1346 C CG  . GLU A 177 ? 0.52554 0.39772 0.51463 0.03254  0.04684  -0.00963 177 GLU A CG  
1347 C CD  . GLU A 177 ? 0.60401 0.43785 0.57541 0.03703  0.05035  -0.00847 177 GLU A CD  
1348 O OE1 . GLU A 177 ? 0.60477 0.42259 0.57184 0.03219  0.05413  -0.00081 177 GLU A OE1 
1349 O OE2 . GLU A 177 ? 0.65329 0.47136 0.61348 0.04594  0.04991  -0.01506 177 GLU A OE2 
1350 N N   . ALA A 178 ? 0.45100 0.41497 0.47884 0.03349  0.04210  0.00450  178 ALA A N   
1351 C CA  . ALA A 178 ? 0.37154 0.35144 0.40481 0.03438  0.04188  0.00962  178 ALA A CA  
1352 C C   . ALA A 178 ? 0.39538 0.39445 0.43295 0.04112  0.03783  0.00792  178 ALA A C   
1353 O O   . ALA A 178 ? 0.41751 0.41983 0.45515 0.04438  0.03632  0.00337  178 ALA A O   
1354 C CB  . ALA A 178 ? 0.36510 0.35493 0.40836 0.02322  0.04263  0.00972  178 ALA A CB  
1355 N N   . MET A 179 ? 0.40544 0.41659 0.44578 0.04258  0.03662  0.01144  179 MET A N   
1356 C CA  . MET A 179 ? 0.35430 0.38308 0.39937 0.04615  0.03268  0.01026  179 MET A CA  
1357 C C   . MET A 179 ? 0.36018 0.39815 0.40882 0.04188  0.03158  0.01192  179 MET A C   
1358 O O   . MET A 179 ? 0.37425 0.40639 0.41986 0.04035  0.03443  0.01523  179 MET A O   
1359 C CB  . MET A 179 ? 0.41643 0.44710 0.45757 0.05668  0.03095  0.01229  179 MET A CB  
1360 C CG  . MET A 179 ? 0.36474 0.38607 0.39684 0.06119  0.03155  0.01802  179 MET A CG  
1361 S SD  . MET A 179 ? 0.44953 0.47772 0.47779 0.07469  0.02657  0.02023  179 MET A SD  
1362 C CE  . MET A 179 ? 0.35631 0.36896 0.36879 0.07799  0.02780  0.02752  179 MET A CE  
1363 N N   . GLN A 180 ? 0.32729 0.37825 0.38115 0.04017  0.02822  0.00972  180 GLN A N   
1364 C CA  . GLN A 180 ? 0.29559 0.35219 0.35169 0.03665  0.02698  0.01017  180 GLN A CA  
1365 C C   . GLN A 180 ? 0.33003 0.39481 0.38556 0.03847  0.02300  0.00992  180 GLN A C   
1366 O O   . GLN A 180 ? 0.32226 0.39455 0.38127 0.03769  0.02095  0.00815  180 GLN A O   
1367 C CB  . GLN A 180 ? 0.30899 0.36918 0.37053 0.03105  0.02614  0.00767  180 GLN A CB  
1368 C CG  . GLN A 180 ? 0.29568 0.36007 0.35916 0.02964  0.02496  0.00813  180 GLN A CG  
1369 C CD  . GLN A 180 ? 0.34157 0.40962 0.41031 0.02597  0.02333  0.00628  180 GLN A CD  
1370 O OE1 . GLN A 180 ? 0.33970 0.41115 0.41025 0.02645  0.02177  0.00642  180 GLN A OE1 
1371 N NE2 . GLN A 180 ? 0.32520 0.39177 0.39516 0.02324  0.02306  0.00414  180 GLN A NE2 
1372 N N   . LEU A 181 ? 0.31900 0.38228 0.36969 0.04007  0.02228  0.01138  181 LEU A N   
1373 C CA  . LEU A 181 ? 0.30928 0.37800 0.35786 0.04051  0.01749  0.01023  181 LEU A CA  
1374 C C   . LEU A 181 ? 0.29354 0.36091 0.34170 0.03666  0.01645  0.00860  181 LEU A C   
1375 O O   . LEU A 181 ? 0.26664 0.32928 0.31263 0.03753  0.01948  0.00922  181 LEU A O   
1376 C CB  . LEU A 181 ? 0.36129 0.42665 0.40064 0.04608  0.01621  0.01208  181 LEU A CB  
1377 C CG  . LEU A 181 ? 0.32317 0.39407 0.35900 0.04634  0.00955  0.00990  181 LEU A CG  
1378 C CD1 . LEU A 181 ? 0.26303 0.34724 0.30763 0.04628  0.00518  0.00863  181 LEU A CD1 
1379 C CD2 . LEU A 181 ? 0.28059 0.34501 0.30280 0.05228  0.00858  0.01163  181 LEU A CD2 
1380 N N   . THR A 182 ? 0.26940 0.34073 0.31969 0.03264  0.01270  0.00677  182 THR A N   
1381 C CA  . THR A 182 ? 0.27794 0.34376 0.32517 0.02971  0.01105  0.00548  182 THR A CA  
1382 C C   . THR A 182 ? 0.26652 0.33184 0.30965 0.02662  0.00596  0.00336  182 THR A C   
1383 O O   . THR A 182 ? 0.25737 0.33196 0.30459 0.02491  0.00334  0.00290  182 THR A O   
1384 C CB  . THR A 182 ? 0.32432 0.39045 0.37556 0.02582  0.01154  0.00590  182 THR A CB  
1385 O OG1 . THR A 182 ? 0.32107 0.39466 0.37638 0.02180  0.01093  0.00595  182 THR A OG1 
1386 C CG2 . THR A 182 ? 0.27626 0.34330 0.33155 0.02775  0.01483  0.00672  182 THR A CG2 
1387 N N   . GLU A 183 ? 0.33068 0.38533 0.36608 0.02609  0.00429  0.00159  183 GLU A N   
1388 C CA  . GLU A 183 ? 0.28028 0.32964 0.30902 0.02205  -0.00116 -0.00160 183 GLU A CA  
1389 C C   . GLU A 183 ? 0.33076 0.37608 0.36117 0.01348  -0.00300 -0.00159 183 GLU A C   
1390 O O   . GLU A 183 ? 0.34276 0.38411 0.37438 0.01310  -0.00027 0.00083  183 GLU A O   
1391 C CB  . GLU A 183 ? 0.31066 0.34613 0.32629 0.02710  -0.00144 -0.00430 183 GLU A CB  
1392 C CG  . GLU A 183 ? 0.38010 0.41774 0.39075 0.03499  0.00168  -0.00363 183 GLU A CG  
1393 C CD  . GLU A 183 ? 0.35194 0.37675 0.34825 0.04071  0.00288  -0.00669 183 GLU A CD  
1394 O OE1 . GLU A 183 ? 0.32229 0.33520 0.31325 0.03993  0.00137  -0.00953 183 GLU A OE1 
1395 O OE2 . GLU A 183 ? 0.42234 0.44746 0.41104 0.04666  0.00590  -0.00608 183 GLU A OE2 
1396 N N   . MET A 184 ? 0.37871 0.42483 0.40839 0.00602  -0.00800 -0.00415 184 MET A N   
1397 C CA  . MET A 184 ? 0.34096 0.37847 0.36898 -0.00416 -0.00961 -0.00412 184 MET A CA  
1398 C C   . MET A 184 ? 0.35578 0.37518 0.37047 -0.00675 -0.01500 -0.00898 184 MET A C   
1399 O O   . MET A 184 ? 0.40630 0.43131 0.42050 -0.00965 -0.02046 -0.01305 184 MET A O   
1400 C CB  . MET A 184 ? 0.29874 0.35446 0.33977 -0.01377 -0.01008 -0.00316 184 MET A CB  
1401 C CG  . MET A 184 ? 0.28028 0.35451 0.33319 -0.00985 -0.00492 0.00011  184 MET A CG  
1402 S SD  . MET A 184 ? 0.41171 0.51008 0.48084 -0.02012 -0.00440 0.00051  184 MET A SD  
1403 C CE  . MET A 184 ? 0.29965 0.41446 0.37784 -0.01062 0.00204  0.00293  184 MET A CE  
1404 N N   . ALA A 185 ? 0.33717 0.33440 0.34005 -0.00467 -0.01409 -0.00897 185 ALA A N   
1405 C CA  . ALA A 185 ? 0.42126 0.39482 0.40829 -0.00699 -0.01866 -0.01400 185 ALA A CA  
1406 C C   . ALA A 185 ? 0.46516 0.44050 0.44539 -0.00361 -0.02321 -0.02016 185 ALA A C   
1407 O O   . ALA A 185 ? 0.43240 0.40629 0.40976 -0.01266 -0.02996 -0.02488 185 ALA A O   
1408 C CB  . ALA A 185 ? 0.37877 0.34298 0.36496 -0.02241 -0.02177 -0.01395 185 ALA A CB  
1409 N N   . SER A 186 ? 0.41176 0.39094 0.38900 0.00909  -0.01950 -0.01997 186 SER A N   
1410 C CA  . SER A 186 ? 0.44921 0.42683 0.41507 0.01417  -0.02274 -0.02509 186 SER A CA  
1411 C C   . SER A 186 ? 0.48308 0.43333 0.42828 0.01594  -0.02552 -0.03168 186 SER A C   
1412 O O   . SER A 186 ? 0.55755 0.49114 0.49688 0.02069  -0.02181 -0.03107 186 SER A O   
1413 C CB  . SER A 186 ? 0.44552 0.43310 0.41243 0.02639  -0.01610 -0.02198 186 SER A CB  
1414 O OG  . SER A 186 ? 0.56830 0.54894 0.53539 0.03362  -0.00925 -0.01961 186 SER A OG  
1415 N N   . ILE A 187 ? 0.47741 0.42225 0.41043 0.01302  -0.03273 -0.03845 187 ILE A N   
1416 C CA  . ILE A 187 ? 0.50884 0.42544 0.41840 0.01605  -0.03556 -0.04635 187 ILE A CA  
1417 C C   . ILE A 187 ? 0.51880 0.43454 0.41523 0.03171  -0.03002 -0.04782 187 ILE A C   
1418 O O   . ILE A 187 ? 0.49391 0.42490 0.38966 0.03480  -0.03095 -0.04724 187 ILE A O   
1419 C CB  . ILE A 187 ? 0.53316 0.44222 0.43414 0.00336  -0.04716 -0.05424 187 ILE A CB  
1420 C CG1 . ILE A 187 ? 0.58206 0.46431 0.45432 0.00992  -0.05041 -0.06398 187 ILE A CG1 
1421 C CG2 . ILE A 187 ? 0.54312 0.48145 0.45732 -0.00136 -0.05275 -0.05308 187 ILE A CG2 
1422 C CD1 . ILE A 187 ? 0.58105 0.43391 0.43987 -0.00198 -0.05797 -0.07160 187 ILE A CD1 
1423 N N   . ASN A 188 ? 0.56456 0.46315 0.45070 0.04228  -0.02359 -0.04904 188 ASN A N   
1424 C CA  . ASN A 188 ? 0.57942 0.47832 0.45439 0.05740  -0.01575 -0.05006 188 ASN A CA  
1425 C C   . ASN A 188 ? 0.56762 0.43658 0.41680 0.06465  -0.01644 -0.05921 188 ASN A C   
1426 O O   . ASN A 188 ? 0.59636 0.44667 0.44295 0.06672  -0.01563 -0.06037 188 ASN A O   
1427 C CB  . ASN A 188 ? 0.54197 0.45608 0.43405 0.06569  -0.00508 -0.04226 188 ASN A CB  
1428 C CG  . ASN A 188 ? 0.57675 0.51760 0.48475 0.06425  -0.00152 -0.03514 188 ASN A CG  
1429 O OD1 . ASN A 188 ? 0.56910 0.51706 0.47122 0.07186  0.00456  -0.03399 188 ASN A OD1 
1430 N ND2 . ASN A 188 ? 0.49263 0.44661 0.41909 0.05464  -0.00469 -0.03023 188 ASN A ND2 
1431 N N   . ASN A 189 ? 0.64979 0.51231 0.47777 0.06947  -0.01810 -0.06573 189 ASN A N   
1432 C CA  . ASN A 189 ? 0.71653 0.54984 0.51643 0.07868  -0.01760 -0.07558 189 ASN A CA  
1433 C C   . ASN A 189 ? 0.79407 0.63249 0.57579 0.08999  -0.01221 -0.07813 189 ASN A C   
1434 O O   . ASN A 189 ? 0.78316 0.64642 0.57657 0.09282  -0.00578 -0.07032 189 ASN A O   
1435 C CB  . ASN A 189 ? 0.71376 0.52061 0.49858 0.06607  -0.03075 -0.08475 189 ASN A CB  
1436 C CG  . ASN A 189 ? 0.68511 0.50533 0.47144 0.05257  -0.04221 -0.08675 189 ASN A CG  
1437 O OD1 . ASN A 189 ? 0.71963 0.55751 0.50291 0.05743  -0.04142 -0.08519 189 ASN A OD1 
1438 N ND2 . ASN A 189 ? 0.64541 0.45783 0.43676 0.03555  -0.05290 -0.08977 189 ASN A ND2 
1439 N N   . ARG A 190 ? 0.93244 0.74485 0.68312 0.09629  -0.01459 -0.08912 190 ARG A N   
1440 C CA  . ARG A 190 ? 1.03918 0.85276 0.76707 0.10841  -0.00834 -0.09213 190 ARG A CA  
1441 C C   . ARG A 190 ? 0.98730 0.81869 0.71373 0.10144  -0.01520 -0.08911 190 ARG A C   
1442 O O   . ARG A 190 ? 0.92455 0.76810 0.64317 0.11031  -0.00686 -0.08473 190 ARG A O   
1443 C CB  . ARG A 190 ? 1.03092 0.80941 0.72274 0.11577  -0.01126 -0.10616 190 ARG A CB  
1444 C CG  . ARG A 190 ? 1.11900 0.89432 0.78134 0.13004  -0.00365 -0.11066 190 ARG A CG  
1445 C CD  . ARG A 190 ? 1.20239 0.95950 0.83342 0.12395  -0.01812 -0.12180 190 ARG A CD  
1446 N NE  . ARG A 190 ? 1.28732 1.01863 0.91383 0.11126  -0.03258 -0.13123 190 ARG A NE  
1447 C CZ  . ARG A 190 ? 1.29260 0.98717 0.89296 0.11664  -0.03408 -0.14353 190 ARG A CZ  
1448 N NH1 . ARG A 190 ? 1.22516 0.90561 0.80119 0.13623  -0.02196 -0.14882 190 ARG A NH1 
1449 N NH2 . ARG A 190 ? 1.37082 1.04146 0.96897 0.10198  -0.04742 -0.15073 190 ARG A NH2 
1450 N N   . VAL A 191 ? 0.87641 0.71044 0.61085 0.08597  -0.02990 -0.09071 191 VAL A N   
1451 C CA  . VAL A 191 ? 0.81803 0.66877 0.55061 0.08058  -0.03898 -0.08898 191 VAL A CA  
1452 C C   . VAL A 191 ? 0.77965 0.66058 0.54574 0.07470  -0.03705 -0.07652 191 VAL A C   
1453 O O   . VAL A 191 ? 0.78564 0.68358 0.55213 0.07769  -0.03688 -0.07052 191 VAL A O   
1454 C CB  . VAL A 191 ? 0.89755 0.73583 0.61831 0.06768  -0.05739 -0.09986 191 VAL A CB  
1455 C CG1 . VAL A 191 ? 0.97492 0.83367 0.69461 0.06405  -0.06828 -0.09825 191 VAL A CG1 
1456 C CG2 . VAL A 191 ? 0.96928 0.77319 0.65358 0.07358  -0.05962 -0.11352 191 VAL A CG2 
1457 N N   . TYR A 192 ? 0.72977 0.61533 0.52162 0.06720  -0.03543 -0.07248 192 TYR A N   
1458 C CA  . TYR A 192 ? 0.72116 0.63273 0.54350 0.06041  -0.03491 -0.06249 192 TYR A CA  
1459 C C   . TYR A 192 ? 0.63617 0.55672 0.47477 0.06768  -0.02040 -0.05374 192 TYR A C   
1460 O O   . TYR A 192 ? 0.60174 0.51093 0.44273 0.07044  -0.01504 -0.05492 192 TYR A O   
1461 C CB  . TYR A 192 ? 0.67310 0.58576 0.51244 0.04473  -0.04452 -0.06429 192 TYR A CB  
1462 C CG  . TYR A 192 ? 0.66374 0.57021 0.49103 0.03474  -0.05975 -0.07360 192 TYR A CG  
1463 C CD1 . TYR A 192 ? 0.69046 0.60316 0.50173 0.03903  -0.06671 -0.07667 192 TYR A CD1 
1464 C CD2 . TYR A 192 ? 0.64764 0.54159 0.47878 0.02043  -0.06759 -0.07919 192 TYR A CD2 
1465 C CE1 . TYR A 192 ? 0.72464 0.63406 0.52573 0.02948  -0.08240 -0.08604 192 TYR A CE1 
1466 C CE2 . TYR A 192 ? 0.67882 0.56860 0.50090 0.00911  -0.08217 -0.08840 192 TYR A CE2 
1467 C CZ  . TYR A 192 ? 0.67474 0.57366 0.48262 0.01378  -0.09019 -0.09229 192 TYR A CZ  
1468 O OH  . TYR A 192 ? 0.76873 0.66583 0.56847 0.00211  -0.10642 -0.10226 192 TYR A OH  
1469 N N   . ARG A 193 ? 0.58841 0.52880 0.43810 0.07063  -0.01489 -0.04509 193 ARG A N   
1470 C CA  . ARG A 193 ? 0.54785 0.49759 0.41045 0.07722  -0.00112 -0.03748 193 ARG A CA  
1471 C C   . ARG A 193 ? 0.52739 0.49769 0.41296 0.07211  -0.00033 -0.02859 193 ARG A C   
1472 O O   . ARG A 193 ? 0.49255 0.47061 0.37402 0.07295  -0.00271 -0.02521 193 ARG A O   
1473 C CB  . ARG A 193 ? 0.69686 0.64312 0.53989 0.08910  0.00903  -0.03683 193 ARG A CB  
1474 C CG  . ARG A 193 ? 0.73449 0.69310 0.59242 0.09437  0.02382  -0.02921 193 ARG A CG  
1475 C CD  . ARG A 193 ? 0.71583 0.66580 0.56416 0.10477  0.03353  -0.03357 193 ARG A CD  
1476 N NE  . ARG A 193 ? 0.71844 0.67864 0.59125 0.10542  0.03987  -0.03028 193 ARG A NE  
1477 C CZ  . ARG A 193 ? 0.69858 0.65073 0.57884 0.10402  0.03456  -0.03398 193 ARG A CZ  
1478 N NH1 . ARG A 193 ? 0.66780 0.60017 0.53393 0.10031  0.02378  -0.04116 193 ARG A NH1 
1479 N NH2 . ARG A 193 ? 0.72506 0.68852 0.62664 0.10596  0.03980  -0.03025 193 ARG A NH2 
1480 N N   . THR A 194 ? 0.49895 0.47635 0.40644 0.06790  0.00268  -0.02500 194 THR A N   
1481 C CA  . THR A 194 ? 0.46221 0.45666 0.39005 0.06469  0.00574  -0.01721 194 THR A CA  
1482 C C   . THR A 194 ? 0.40949 0.40915 0.34863 0.06883  0.01708  -0.01287 194 THR A C   
1483 O O   . THR A 194 ? 0.46046 0.45322 0.39495 0.07439  0.02187  -0.01575 194 THR A O   
1484 C CB  . THR A 194 ? 0.49410 0.49535 0.43856 0.05462  -0.00189 -0.01707 194 THR A CB  
1485 O OG1 . THR A 194 ? 0.40224 0.39733 0.35413 0.05204  -0.00049 -0.01820 194 THR A OG1 
1486 C CG2 . THR A 194 ? 0.40545 0.40420 0.34179 0.04890  -0.01361 -0.02252 194 THR A CG2 
1487 N N   . ILE A 195 ? 0.37607 0.38846 0.33049 0.06640  0.02103  -0.00636 195 ILE A N   
1488 C CA  . ILE A 195 ? 0.39369 0.41383 0.36089 0.06841  0.03084  -0.00251 195 ILE A CA  
1489 C C   . ILE A 195 ? 0.38680 0.40864 0.36786 0.06606  0.02885  -0.00412 195 ILE A C   
1490 O O   . ILE A 195 ? 0.33583 0.36165 0.32346 0.07050  0.03483  -0.00395 195 ILE A O   
1491 C CB  . ILE A 195 ? 0.37004 0.39941 0.34691 0.06537  0.03492  0.00420  195 ILE A CB  
1492 C CG1 . ILE A 195 ? 0.33000 0.36801 0.31930 0.06582  0.04528  0.00769  195 ILE A CG1 
1493 C CG2 . ILE A 195 ? 0.33099 0.36535 0.32036 0.05876  0.02788  0.00505  195 ILE A CG2 
1494 C CD1 . ILE A 195 ? 0.34385 0.38074 0.32211 0.07228  0.05509  0.00833  195 ILE A CD1 
1495 N N   . GLY A 196 ? 0.36917 0.38883 0.35448 0.05963  0.02065  -0.00543 196 GLY A N   
1496 C CA  . GLY A 196 ? 0.39944 0.41851 0.39470 0.05757  0.01885  -0.00568 196 GLY A CA  
1497 C C   . GLY A 196 ? 0.38520 0.41774 0.39806 0.05482  0.02181  -0.00124 196 GLY A C   
1498 O O   . GLY A 196 ? 0.39509 0.42956 0.41502 0.04914  0.01769  -0.00024 196 GLY A O   
1499 N N   . SER A 197 ? 0.30629 0.34801 0.32559 0.05797  0.02917  0.00122  197 SER A N   
1500 C CA  . SER A 197 ? 0.31536 0.36893 0.35072 0.05409  0.03128  0.00438  197 SER A CA  
1501 C C   . SER A 197 ? 0.33854 0.39320 0.37591 0.04791  0.02855  0.00635  197 SER A C   
1502 O O   . SER A 197 ? 0.31086 0.36145 0.33934 0.04821  0.02766  0.00679  197 SER A O   
1503 C CB  . SER A 197 ? 0.27954 0.34271 0.32159 0.05637  0.04022  0.00661  197 SER A CB  
1504 O OG  . SER A 197 ? 0.29392 0.36094 0.33820 0.06336  0.04352  0.00464  197 SER A OG  
1505 N N   . PRO A 198 ? 0.34644 0.40662 0.39437 0.04344  0.02674  0.00719  198 PRO A N   
1506 C CA  . PRO A 198 ? 0.31460 0.37614 0.36477 0.03946  0.02604  0.00871  198 PRO A CA  
1507 C C   . PRO A 198 ? 0.33291 0.39451 0.38313 0.03989  0.03215  0.01157  198 PRO A C   
1508 O O   . PRO A 198 ? 0.30509 0.37010 0.35915 0.04045  0.03772  0.01265  198 PRO A O   
1509 C CB  . PRO A 198 ? 0.27756 0.34375 0.33679 0.03556  0.02380  0.00816  198 PRO A CB  
1510 C CG  . PRO A 198 ? 0.27383 0.33897 0.33258 0.03746  0.02084  0.00685  198 PRO A CG  
1511 C CD  . PRO A 198 ? 0.31137 0.37543 0.36717 0.04302  0.02439  0.00642  198 PRO A CD  
1512 N N   . LEU A 199 ? 0.29839 0.35627 0.34444 0.03978  0.03148  0.01315  199 LEU A N   
1513 C CA  . LEU A 199 ? 0.31815 0.37090 0.36071 0.04029  0.03700  0.01691  199 LEU A CA  
1514 C C   . LEU A 199 ? 0.29577 0.34615 0.34336 0.03728  0.03650  0.01714  199 LEU A C   
1515 O O   . LEU A 199 ? 0.30059 0.35239 0.34851 0.03835  0.03181  0.01537  199 LEU A O   
1516 C CB  . LEU A 199 ? 0.34328 0.38960 0.37142 0.04587  0.03626  0.01904  199 LEU A CB  
1517 C CG  . LEU A 199 ? 0.31321 0.35915 0.33200 0.04952  0.03524  0.01721  199 LEU A CG  
1518 C CD1 . LEU A 199 ? 0.33267 0.37233 0.33535 0.05497  0.03296  0.01895  199 LEU A CD1 
1519 C CD2 . LEU A 199 ? 0.29029 0.33797 0.31081 0.04966  0.04304  0.01796  199 LEU A CD2 
1520 N N   . VAL A 200 ? 0.32651 0.37327 0.37791 0.03319  0.04179  0.01892  200 VAL A N   
1521 C CA  . VAL A 200 ? 0.33221 0.37224 0.38580 0.03003  0.04182  0.01833  200 VAL A CA  
1522 C C   . VAL A 200 ? 0.36350 0.38864 0.40678 0.03184  0.04677  0.02327  200 VAL A C   
1523 O O   . VAL A 200 ? 0.39135 0.41298 0.43277 0.02891  0.05331  0.02707  200 VAL A O   
1524 C CB  . VAL A 200 ? 0.33014 0.37551 0.39563 0.02213  0.04250  0.01558  200 VAL A CB  
1525 C CG1 . VAL A 200 ? 0.34167 0.37626 0.40620 0.01846  0.04230  0.01381  200 VAL A CG1 
1526 C CG2 . VAL A 200 ? 0.29232 0.35000 0.36460 0.02225  0.03690  0.01177  200 VAL A CG2 
1527 N N   . PHE A 201 ? 0.36405 0.38045 0.40008 0.03736  0.04416  0.02369  201 PHE A N   
1528 C CA  . PHE A 201 ? 0.35281 0.35221 0.37569 0.04201  0.04744  0.02909  201 PHE A CA  
1529 C C   . PHE A 201 ? 0.42248 0.40577 0.44386 0.03950  0.04945  0.02849  201 PHE A C   
1530 O O   . PHE A 201 ? 0.43656 0.42283 0.46338 0.03968  0.04582  0.02316  201 PHE A O   
1531 C CB  . PHE A 201 ? 0.36039 0.36163 0.37487 0.05294  0.04199  0.03022  201 PHE A CB  
1532 C CG  . PHE A 201 ? 0.38521 0.39825 0.39779 0.05502  0.03908  0.03004  201 PHE A CG  
1533 C CD1 . PHE A 201 ? 0.37575 0.38197 0.37533 0.05766  0.04246  0.03489  201 PHE A CD1 
1534 C CD2 . PHE A 201 ? 0.34588 0.37454 0.36749 0.05395  0.03337  0.02493  201 PHE A CD2 
1535 C CE1 . PHE A 201 ? 0.39639 0.41100 0.39151 0.05997  0.03947  0.03345  201 PHE A CE1 
1536 C CE2 . PHE A 201 ? 0.38747 0.42308 0.40548 0.05516  0.03027  0.02390  201 PHE A CE2 
1537 C CZ  . PHE A 201 ? 0.38261 0.41107 0.38706 0.05856  0.03299  0.02757  201 PHE A CZ  
1538 N N   . PRO A 202 ? 0.46555 0.42972 0.47773 0.03700  0.05558  0.03376  202 PRO A N   
1539 C CA  . PRO A 202 ? 0.46115 0.40452 0.46923 0.03396  0.05748  0.03282  202 PRO A CA  
1540 C C   . PRO A 202 ? 0.52402 0.45356 0.51955 0.04736  0.05433  0.03392  202 PRO A C   
1541 O O   . PRO A 202 ? 0.50478 0.44290 0.49608 0.05818  0.05042  0.03603  202 PRO A O   
1542 C CB  . PRO A 202 ? 0.46151 0.38887 0.46349 0.02544  0.06607  0.03937  202 PRO A CB  
1543 C CG  . PRO A 202 ? 0.47966 0.41153 0.47230 0.03216  0.06828  0.04605  202 PRO A CG  
1544 C CD  . PRO A 202 ? 0.44313 0.40167 0.44614 0.03629  0.06191  0.04103  202 PRO A CD  
1545 N N   . LYS A 203 ? 0.53921 0.44739 0.52900 0.04680  0.05561  0.03189  203 LYS A N   
1546 C CA  . LYS A 203 ? 0.58441 0.47471 0.56047 0.06098  0.05398  0.03365  203 LYS A CA  
1547 C C   . LYS A 203 ? 0.56790 0.44472 0.52806 0.06844  0.05616  0.04367  203 LYS A C   
1548 O O   . LYS A 203 ? 0.61358 0.48562 0.57002 0.05992  0.06167  0.04940  203 LYS A O   
1549 C CB  . LYS A 203 ? 0.63803 0.49978 0.60648 0.05771  0.05657  0.03028  203 LYS A CB  
1550 C CG  . LYS A 203 ? 0.59289 0.45026 0.55790 0.07077  0.05299  0.02428  203 LYS A CG  
1551 C CD  . LYS A 203 ? 0.68486 0.51030 0.64003 0.06552  0.05580  0.01974  203 LYS A CD  
1552 C CE  . LYS A 203 ? 0.75582 0.54689 0.69551 0.05982  0.06148  0.02791  203 LYS A CE  
1553 N NZ  . LYS A 203 ? 0.76549 0.52229 0.69537 0.05090  0.06414  0.02319  203 LYS A NZ  
1554 N N   . HIS A 204 ? 0.62637 0.49877 0.57696 0.08519  0.05184  0.04587  204 HIS A N   
1555 C CA  . HIS A 204 ? 0.68234 0.53974 0.61396 0.09636  0.05173  0.05545  204 HIS A CA  
1556 C C   . HIS A 204 ? 0.59314 0.47152 0.52530 0.09649  0.04952  0.05898  204 HIS A C   
1557 O O   . HIS A 204 ? 0.61352 0.48155 0.52814 0.10594  0.04851  0.06675  204 HIS A O   
1558 C CB  . HIS A 204 ? 0.70955 0.52867 0.62232 0.09076  0.05995  0.06327  204 HIS A CB  
1559 C CG  . HIS A 204 ? 0.75038 0.54046 0.65650 0.09210  0.06168  0.06027  204 HIS A CG  
1560 N ND1 . HIS A 204 ? 0.76259 0.54980 0.66632 0.10884  0.05625  0.05622  204 HIS A ND1 
1561 C CD2 . HIS A 204 ? 0.77373 0.53592 0.67475 0.07868  0.06828  0.06006  204 HIS A CD2 
1562 C CE1 . HIS A 204 ? 0.75319 0.50929 0.64826 0.10688  0.05960  0.05335  204 HIS A CE1 
1563 N NE2 . HIS A 204 ? 0.85635 0.59594 0.74940 0.08775  0.06639  0.05546  204 HIS A NE2 
1564 N N   . HIS A 205 ? 0.56962 0.47489 0.51893 0.08716  0.04838  0.05340  205 HIS A N   
1565 C CA  . HIS A 205 ? 0.53020 0.45467 0.47939 0.08863  0.04510  0.05465  205 HIS A CA  
1566 C C   . HIS A 205 ? 0.54478 0.49190 0.50184 0.09901  0.03493  0.05005  205 HIS A C   
1567 O O   . HIS A 205 ? 0.52136 0.48093 0.49308 0.09895  0.03220  0.04352  205 HIS A O   
1568 C CB  . HIS A 205 ? 0.50300 0.44311 0.46564 0.07468  0.04883  0.05091  205 HIS A CB  
1569 C CG  . HIS A 205 ? 0.51435 0.44131 0.46923 0.06580  0.05865  0.05685  205 HIS A CG  
1570 N ND1 . HIS A 205 ? 0.45514 0.39597 0.41410 0.05968  0.06218  0.05661  205 HIS A ND1 
1571 C CD2 . HIS A 205 ? 0.54831 0.44955 0.49173 0.06175  0.06652  0.06331  205 HIS A CD2 
1572 C CE1 . HIS A 205 ? 0.48095 0.40876 0.43317 0.05235  0.07242  0.06270  205 HIS A CE1 
1573 N NE2 . HIS A 205 ? 0.44638 0.34953 0.38909 0.05232  0.07524  0.06715  205 HIS A NE2 
1574 N N   . VAL A 206 ? 0.55215 0.50526 0.49906 0.10738  0.02943  0.05340  206 VAL A N   
1575 C CA  . VAL A 206 ? 0.47734 0.45429 0.43260 0.11599  0.01888  0.04924  206 VAL A CA  
1576 C C   . VAL A 206 ? 0.48160 0.47729 0.44146 0.10897  0.01542  0.04568  206 VAL A C   
1577 O O   . VAL A 206 ? 0.53173 0.51961 0.47625 0.10848  0.01698  0.04957  206 VAL A O   
1578 C CB  . VAL A 206 ? 0.44381 0.41382 0.38357 0.13287  0.01238  0.05486  206 VAL A CB  
1579 C CG1 . VAL A 206 ? 0.44207 0.44248 0.39562 0.14028  0.00089  0.04958  206 VAL A CG1 
1580 C CG2 . VAL A 206 ? 0.50608 0.45118 0.43742 0.14123  0.01644  0.05890  206 VAL A CG2 
1581 N N   . VAL A 207 ? 0.46739 0.48567 0.44634 0.10368  0.01135  0.03837  207 VAL A N   
1582 C CA  . VAL A 207 ? 0.47168 0.50595 0.45482 0.09760  0.00666  0.03408  207 VAL A CA  
1583 C C   . VAL A 207 ? 0.48288 0.53796 0.47286 0.10414  -0.00444 0.03096  207 VAL A C   
1584 O O   . VAL A 207 ? 0.45079 0.51959 0.45609 0.10643  -0.00640 0.02819  207 VAL A O   
1585 C CB  . VAL A 207 ? 0.40201 0.44386 0.40026 0.08513  0.01058  0.02884  207 VAL A CB  
1586 C CG1 . VAL A 207 ? 0.37536 0.43116 0.37728 0.07994  0.00475  0.02403  207 VAL A CG1 
1587 C CG2 . VAL A 207 ? 0.35769 0.38379 0.35099 0.07874  0.02015  0.03156  207 VAL A CG2 
1588 N N   . SER A 208 ? 0.52298 0.58163 0.50167 0.10716  -0.01163 0.03107  208 SER A N   
1589 C CA  . SER A 208 ? 0.50232 0.58169 0.48644 0.11362  -0.02389 0.02834  208 SER A CA  
1590 C C   . SER A 208 ? 0.49265 0.58516 0.48034 0.10401  -0.03044 0.02180  208 SER A C   
1591 O O   . SER A 208 ? 0.54216 0.62209 0.51344 0.10099  -0.02932 0.02173  208 SER A O   
1592 C CB  . SER A 208 ? 0.52425 0.59420 0.48787 0.12812  -0.02945 0.03441  208 SER A CB  
1593 O OG  . SER A 208 ? 0.61641 0.70975 0.58603 0.13395  -0.04319 0.03100  208 SER A OG  
1594 N N   . LEU A 209 ? 0.46819 0.58491 0.47650 0.09904  -0.03659 0.01622  209 LEU A N   
1595 C CA  . LEU A 209 ? 0.47710 0.60534 0.48914 0.08894  -0.04416 0.00962  209 LEU A CA  
1596 C C   . LEU A 209 ? 0.47244 0.61853 0.48364 0.09556  -0.05837 0.00764  209 LEU A C   
1597 O O   . LEU A 209 ? 0.48025 0.64402 0.50376 0.10439  -0.06257 0.00911  209 LEU A O   
1598 C CB  . LEU A 209 ? 0.40667 0.54932 0.44137 0.07653  -0.04151 0.00513  209 LEU A CB  
1599 C CG  . LEU A 209 ? 0.41974 0.54782 0.45657 0.07149  -0.02903 0.00708  209 LEU A CG  
1600 C CD1 . LEU A 209 ? 0.35279 0.49372 0.40816 0.05992  -0.02692 0.00343  209 LEU A CD1 
1601 C CD2 . LEU A 209 ? 0.41500 0.52036 0.43401 0.06891  -0.02422 0.00796  209 LEU A CD2 
1602 N N   . GLN A 210 ? 0.47654 0.61825 0.47260 0.09234  -0.06617 0.00388  210 GLN A N   
1603 C CA  . GLN A 210 ? 0.51200 0.66886 0.50317 0.09875  -0.08140 0.00154  210 GLN A CA  
1604 C C   . GLN A 210 ? 0.50286 0.66940 0.49762 0.08494  -0.09104 -0.00781 210 GLN A C   
1605 O O   . GLN A 210 ? 0.44895 0.59522 0.42829 0.07745  -0.08750 -0.01093 210 GLN A O   
1606 C CB  . GLN A 210 ? 0.47767 0.61336 0.43688 0.11197  -0.08272 0.00713  210 GLN A CB  
1607 C CG  . GLN A 210 ? 0.50972 0.63501 0.46447 0.12584  -0.07534 0.01670  210 GLN A CG  
1608 C CD  . GLN A 210 ? 0.64280 0.74210 0.56348 0.13701  -0.07349 0.02399  210 GLN A CD  
1609 O OE1 . GLN A 210 ? 0.55302 0.64766 0.45247 0.13836  -0.08119 0.02182  210 GLN A OE1 
1610 N NE2 . GLN A 210 ? 0.67429 0.75481 0.58782 0.14458  -0.06285 0.03271  210 GLN A NE2 
1611 N N   . PRO A 211 ? 0.53075 0.72748 0.54527 0.08134  -0.10327 -0.01275 211 PRO A N   
1612 C CA  . PRO A 211 ? 0.53307 0.73827 0.55375 0.06481  -0.11201 -0.02211 211 PRO A CA  
1613 C C   . PRO A 211 ? 0.59879 0.78719 0.58950 0.06605  -0.12189 -0.02678 211 PRO A C   
1614 O O   . PRO A 211 ? 0.64025 0.82082 0.60901 0.08066  -0.12614 -0.02298 211 PRO A O   
1615 C CB  . PRO A 211 ? 0.53894 0.78493 0.58958 0.06254  -0.12295 -0.02521 211 PRO A CB  
1616 C CG  . PRO A 211 ? 0.55201 0.80946 0.61373 0.07893  -0.11711 -0.01731 211 PRO A CG  
1617 C CD  . PRO A 211 ? 0.50505 0.72982 0.53652 0.09298  -0.11038 -0.01019 211 PRO A CD  
1618 N N   . VAL A 212 ? 0.63724 0.81744 0.62474 0.05061  -0.12513 -0.03509 212 VAL A N   
1619 C CA  . VAL A 212 ? 0.69357 0.85580 0.65162 0.04968  -0.13453 -0.04198 212 VAL A CA  
1620 C C   . VAL A 212 ? 0.71697 0.90163 0.68479 0.03868  -0.15353 -0.05199 212 VAL A C   
1621 O O   . VAL A 212 ? 0.75533 0.94186 0.70427 0.04488  -0.16774 -0.05604 212 VAL A O   
1622 C CB  . VAL A 212 ? 0.56229 0.69161 0.50348 0.04230  -0.12369 -0.04480 212 VAL A CB  
1623 C CG1 . VAL A 212 ? 0.59494 0.70528 0.50540 0.04065  -0.13365 -0.05398 212 VAL A CG1 
1624 C CG2 . VAL A 212 ? 0.48869 0.59879 0.41945 0.05352  -0.10656 -0.03546 212 VAL A CG2 
1625 N N   . ASN A 213 ? 0.69169 0.89385 0.68857 0.02152  -0.15415 -0.05604 213 ASN A N   
1626 C CA  . ASN A 213 ? 0.67872 0.90747 0.69170 0.00814  -0.17153 -0.06523 213 ASN A CA  
1627 C C   . ASN A 213 ? 0.64126 0.91112 0.69642 0.00308  -0.17077 -0.06226 213 ASN A C   
1628 O O   . ASN A 213 ? 0.64967 0.94877 0.71792 0.01607  -0.17726 -0.05877 213 ASN A O   
1629 C CB  . ASN A 213 ? 0.70422 0.91169 0.70902 -0.01231 -0.17398 -0.07503 213 ASN A CB  
1630 C CG  . ASN A 213 ? 0.75026 0.92193 0.71327 -0.00719 -0.17828 -0.08093 213 ASN A CG  
1631 O OD1 . ASN A 213 ? 0.84948 1.01948 0.79064 0.00855  -0.18485 -0.07979 213 ASN A OD1 
1632 N ND2 . ASN A 213 ? 0.81945 0.96090 0.76921 -0.01964 -0.17425 -0.08716 213 ASN A ND2 
1633 N N   . ASP A 214 ? 0.65142 0.92287 0.72656 -0.01477 -0.16230 -0.06332 214 ASP A N   
1634 C CA  . ASP A 214 ? 0.63807 0.94758 0.75241 -0.02061 -0.15840 -0.06027 214 ASP A CA  
1635 C C   . ASP A 214 ? 0.58716 0.90190 0.70748 -0.00128 -0.14574 -0.04989 214 ASP A C   
1636 O O   . ASP A 214 ? 0.58642 0.86979 0.68737 0.00688  -0.13306 -0.04432 214 ASP A O   
1637 C CB  . ASP A 214 ? 0.65541 0.95720 0.78264 -0.04328 -0.14930 -0.06200 214 ASP A CB  
1638 C CG  . ASP A 214 ? 0.68819 1.02360 0.85153 -0.04785 -0.13972 -0.05691 214 ASP A CG  
1639 O OD1 . ASP A 214 ? 0.68209 1.06060 0.87191 -0.04502 -0.14756 -0.05782 214 ASP A OD1 
1640 O OD2 . ASP A 214 ? 0.74699 1.06657 0.91185 -0.05362 -0.12432 -0.05213 214 ASP A OD2 
1641 N N   . LYS A 215 ? 0.61765 0.97273 0.76528 0.00625  -0.14962 -0.04783 215 LYS A N   
1642 C CA  . LYS A 215 ? 0.60737 0.96818 0.76044 0.02596  -0.13950 -0.03911 215 LYS A CA  
1643 C C   . LYS A 215 ? 0.53177 0.91568 0.71622 0.01973  -0.12674 -0.03631 215 LYS A C   
1644 O O   . LYS A 215 ? 0.46337 0.85906 0.65724 0.03574  -0.11987 -0.03074 215 LYS A O   
1645 C CB  . LYS A 215 ? 0.55549 0.94075 0.71061 0.04543  -0.15308 -0.03807 215 LYS A CB  
1646 C CG  . LYS A 215 ? 0.60972 0.97610 0.73289 0.05138  -0.16744 -0.04119 215 LYS A CG  
1647 C CD  . LYS A 215 ? 0.69006 1.07666 0.81122 0.07374  -0.18012 -0.03813 215 LYS A CD  
1648 C CE  . LYS A 215 ? 0.83635 1.20294 0.92174 0.07969  -0.19452 -0.04102 215 LYS A CE  
1649 N NZ  . LYS A 215 ? 0.80482 1.12108 0.85301 0.08038  -0.18249 -0.03779 215 LYS A NZ  
1650 N N   . ASP A 216 ? 0.52142 0.91005 0.72009 -0.00277 -0.12301 -0.03994 216 ASP A N   
1651 C CA  . ASP A 216 ? 0.50391 0.91037 0.72785 -0.01023 -0.10900 -0.03675 216 ASP A CA  
1652 C C   . ASP A 216 ? 0.52194 0.88858 0.72691 -0.01375 -0.09328 -0.03230 216 ASP A C   
1653 O O   . ASP A 216 ? 0.54701 0.88158 0.73145 -0.02432 -0.09402 -0.03456 216 ASP A O   
1654 C CB  . ASP A 216 ? 0.54544 0.98217 0.79685 -0.03396 -0.11340 -0.04218 216 ASP A CB  
1655 C CG  . ASP A 216 ? 0.52368 1.00580 0.79835 -0.03179 -0.13014 -0.04733 216 ASP A CG  
1656 O OD1 . ASP A 216 ? 0.55893 1.04501 0.82421 -0.01067 -0.13943 -0.04651 216 ASP A OD1 
1657 O OD2 . ASP A 216 ? 0.50674 1.02078 0.80905 -0.05142 -0.13414 -0.05188 216 ASP A OD2 
1658 N N   . PHE A 217 ? 0.48922 0.85814 0.70064 -0.00414 -0.07970 -0.02655 217 PHE A N   
1659 C CA  . PHE A 217 ? 0.48410 0.81814 0.67796 -0.00486 -0.06603 -0.02225 217 PHE A CA  
1660 C C   . PHE A 217 ? 0.48741 0.83702 0.69928 -0.00728 -0.05218 -0.01883 217 PHE A C   
1661 O O   . PHE A 217 ? 0.48843 0.86650 0.71809 0.00411  -0.04981 -0.01768 217 PHE A O   
1662 C CB  . PHE A 217 ? 0.47201 0.77911 0.64214 0.01438  -0.06398 -0.01844 217 PHE A CB  
1663 C CG  . PHE A 217 ? 0.50592 0.79486 0.65395 0.01830  -0.07521 -0.02087 217 PHE A CG  
1664 C CD1 . PHE A 217 ? 0.52553 0.78409 0.65347 0.00837  -0.07540 -0.02316 217 PHE A CD1 
1665 C CD2 . PHE A 217 ? 0.51827 0.81955 0.66364 0.03331  -0.08540 -0.02078 217 PHE A CD2 
1666 C CE1 . PHE A 217 ? 0.54148 0.78301 0.64690 0.01285  -0.08460 -0.02593 217 PHE A CE1 
1667 C CE2 . PHE A 217 ? 0.54720 0.83079 0.66878 0.03735  -0.09528 -0.02278 217 PHE A CE2 
1668 C CZ  . PHE A 217 ? 0.55921 0.81325 0.66070 0.02688  -0.09440 -0.02567 217 PHE A CZ  
1669 N N   . GLN A 218 ? 0.48482 0.81451 0.69003 -0.02085 -0.04298 -0.01719 218 GLN A N   
1670 C CA  . GLN A 218 ? 0.40816 0.74487 0.62267 -0.02247 -0.02867 -0.01336 218 GLN A CA  
1671 C C   . GLN A 218 ? 0.37471 0.68598 0.57087 -0.00646 -0.02119 -0.00974 218 GLN A C   
1672 O O   . GLN A 218 ? 0.35862 0.63623 0.53367 -0.00835 -0.01920 -0.00834 218 GLN A O   
1673 C CB  . GLN A 218 ? 0.43966 0.76386 0.65196 -0.04370 -0.02300 -0.01243 218 GLN A CB  
1674 C CG  . GLN A 218 ? 0.47978 0.81930 0.70469 -0.04897 -0.00892 -0.00868 218 GLN A CG  
1675 C CD  . GLN A 218 ? 0.52760 0.91376 0.78440 -0.05675 -0.00854 -0.01037 218 GLN A CD  
1676 O OE1 . GLN A 218 ? 0.49848 0.91191 0.77096 -0.04646 -0.00094 -0.00928 218 GLN A OE1 
1677 N NE2 . GLN A 218 ? 0.55973 0.95578 0.82674 -0.07516 -0.01662 -0.01355 218 GLN A NE2 
1678 N N   . ILE A 219 ? 0.41947 0.74672 0.62390 0.00956  -0.01744 -0.00861 219 ILE A N   
1679 C CA  . ILE A 219 ? 0.42057 0.72421 0.60856 0.02425  -0.01103 -0.00591 219 ILE A CA  
1680 C C   . ILE A 219 ? 0.44066 0.74926 0.63381 0.02366  0.00219  -0.00440 219 ILE A C   
1681 O O   . ILE A 219 ? 0.44459 0.78458 0.65771 0.02537  0.00646  -0.00524 219 ILE A O   
1682 C CB  . ILE A 219 ? 0.42591 0.73590 0.61366 0.04422  -0.01643 -0.00575 219 ILE A CB  
1683 C CG1 . ILE A 219 ? 0.38374 0.68837 0.56289 0.04541  -0.02976 -0.00696 219 ILE A CG1 
1684 C CG2 . ILE A 219 ? 0.40765 0.68999 0.57781 0.05678  -0.00934 -0.00310 219 ILE A CG2 
1685 C CD1 . ILE A 219 ? 0.32671 0.63698 0.50348 0.06526  -0.03609 -0.00573 219 ILE A CD1 
1686 N N   . SER A 220 ? 0.40078 0.68013 0.57595 0.02179  0.00861  -0.00245 220 SER A N   
1687 C CA  . SER A 220 ? 0.39517 0.67437 0.56951 0.02177  0.02037  -0.00133 220 SER A CA  
1688 C C   . SER A 220 ? 0.35201 0.61071 0.51197 0.03658  0.02375  -0.00128 220 SER A C   
1689 O O   . SER A 220 ? 0.40105 0.63476 0.54614 0.03975  0.01940  -0.00054 220 SER A O   
1690 C CB  . SER A 220 ? 0.35091 0.61327 0.51528 0.00612  0.02456  0.00083  220 SER A CB  
1691 O OG  . SER A 220 ? 0.40627 0.63732 0.55028 0.01017  0.02560  0.00192  220 SER A OG  
1692 N N   . VAL A 221 ? 0.41722 0.68617 0.58130 0.04505  0.03207  -0.00237 221 VAL A N   
1693 C CA  . VAL A 221 ? 0.42974 0.67703 0.57895 0.05713  0.03621  -0.00332 221 VAL A CA  
1694 C C   . VAL A 221 ? 0.41527 0.66034 0.55873 0.05238  0.04645  -0.00393 221 VAL A C   
1695 O O   . VAL A 221 ? 0.44004 0.70676 0.59332 0.05655  0.05405  -0.00547 221 VAL A O   
1696 C CB  . VAL A 221 ? 0.39397 0.65071 0.54884 0.07569  0.03573  -0.00507 221 VAL A CB  
1697 C CG1 . VAL A 221 ? 0.36000 0.58962 0.49735 0.08609  0.04039  -0.00664 221 VAL A CG1 
1698 C CG2 . VAL A 221 ? 0.43594 0.69381 0.59325 0.08087  0.02478  -0.00363 221 VAL A CG2 
1699 N N   . ASP A 222 ? 0.42135 0.64158 0.54853 0.04446  0.04668  -0.00272 222 ASP A N   
1700 C CA  . ASP A 222 ? 0.50691 0.72157 0.62418 0.03877  0.05462  -0.00260 222 ASP A CA  
1701 C C   . ASP A 222 ? 0.53746 0.77400 0.66618 0.02639  0.05888  0.00010  222 ASP A C   
1702 O O   . ASP A 222 ? 0.56627 0.80336 0.69980 0.01545  0.05324  0.00260  222 ASP A O   
1703 C CB  . ASP A 222 ? 0.40241 0.61451 0.51298 0.05154  0.06147  -0.00665 222 ASP A CB  
1704 C CG  . ASP A 222 ? 0.36993 0.55647 0.46847 0.06069  0.05679  -0.00897 222 ASP A CG  
1705 O OD1 . ASP A 222 ? 0.36848 0.53652 0.45963 0.05478  0.05054  -0.00716 222 ASP A OD1 
1706 O OD2 . ASP A 222 ? 0.35084 0.53513 0.44717 0.07379  0.05984  -0.01256 222 ASP A OD2 
1707 N N   . HIS A 223 ? 0.57794 0.83169 0.71048 0.02693  0.06920  -0.00036 223 HIS A N   
1708 C CA  . HIS A 223 ? 0.72956 1.00379 0.87294 0.01300  0.07481  0.00308  223 HIS A CA  
1709 C C   . HIS A 223 ? 0.70794 1.01601 0.87855 0.01161  0.07246  0.00240  223 HIS A C   
1710 O O   . HIS A 223 ? 0.77632 1.10101 0.95869 -0.00334 0.07478  0.00521  223 HIS A O   
1711 C CB  . HIS A 223 ? 0.75653 1.03841 0.89307 0.01369  0.08842  0.00331  223 HIS A CB  
1712 C CG  . HIS A 223 ? 0.78805 1.08606 0.93066 0.03080  0.09494  -0.00181 223 HIS A CG  
1713 N ND1 . HIS A 223 ? 0.73234 1.01216 0.86494 0.04630  0.09064  -0.00643 223 HIS A ND1 
1714 C CD2 . HIS A 223 ? 0.73004 1.05980 0.88725 0.03529  0.10603  -0.00313 223 HIS A CD2 
1715 C CE1 . HIS A 223 ? 0.66573 0.96233 0.80470 0.06059  0.09814  -0.01062 223 HIS A CE1 
1716 N NE2 . HIS A 223 ? 0.70843 1.03718 0.86309 0.05508  0.10776  -0.00889 223 HIS A NE2 
1717 N N   . LEU A 224 ? 0.55362 0.87146 0.73395 0.02630  0.06726  -0.00106 224 LEU A N   
1718 C CA  . LEU A 224 ? 0.46312 0.81787 0.67036 0.02875  0.06464  -0.00241 224 LEU A CA  
1719 C C   . LEU A 224 ? 0.52563 0.87656 0.73739 0.02244  0.05065  -0.00200 224 LEU A C   
1720 O O   . LEU A 224 ? 0.48293 0.80919 0.68095 0.03009  0.04265  -0.00250 224 LEU A O   
1721 C CB  . LEU A 224 ? 0.43573 0.80197 0.64841 0.05103  0.06672  -0.00618 224 LEU A CB  
1722 C CG  . LEU A 224 ? 0.51607 0.92002 0.75530 0.06169  0.06253  -0.00824 224 LEU A CG  
1723 C CD1 . LEU A 224 ? 0.53811 0.93011 0.77445 0.06907  0.04758  -0.00834 224 LEU A CD1 
1724 C CD2 . LEU A 224 ? 0.52198 0.96670 0.78839 0.04643  0.06524  -0.00723 224 LEU A CD2 
1725 N N   . SER A 225 ? 0.46661 0.84175 0.69687 0.00790  0.04808  -0.00135 225 SER A N   
1726 C CA  . SER A 225 ? 0.47583 0.84871 0.70973 0.00009  0.03459  -0.00210 225 SER A CA  
1727 C C   . SER A 225 ? 0.43959 0.85588 0.70291 0.00130  0.02921  -0.00477 225 SER A C   
1728 O O   . SER A 225 ? 0.49576 0.94565 0.78052 -0.00569 0.03704  -0.00465 225 SER A O   
1729 C CB  . SER A 225 ? 0.54248 0.89756 0.76777 -0.02165 0.03421  0.00040  225 SER A CB  
1730 O OG  . SER A 225 ? 0.54829 0.89725 0.77365 -0.02850 0.02108  -0.00155 225 SER A OG  
1731 N N   . ILE A 226 ? 0.43359 0.85064 0.69798 0.01011  0.01589  -0.00699 226 ILE A N   
1732 C CA  . ILE A 226 ? 0.46900 0.92764 0.76020 0.01476  0.00782  -0.00990 226 ILE A CA  
1733 C C   . ILE A 226 ? 0.43191 0.88404 0.71957 0.00752  -0.00852 -0.01204 226 ILE A C   
1734 O O   . ILE A 226 ? 0.47005 0.88710 0.73315 0.01315  -0.01452 -0.01146 226 ILE A O   
1735 C CB  . ILE A 226 ? 0.50779 0.97765 0.80258 0.04137  0.00782  -0.01072 226 ILE A CB  
1736 C CG1 . ILE A 226 ? 0.54675 1.02676 0.84628 0.04917  0.02413  -0.01021 226 ILE A CG1 
1737 C CG2 . ILE A 226 ? 0.55395 1.06525 0.87449 0.04851  -0.00373 -0.01350 226 ILE A CG2 
1738 C CD1 . ILE A 226 ? 0.61769 1.11038 0.92247 0.07591  0.02483  -0.01177 226 ILE A CD1 
1739 N N   . LEU A 227 ? 0.45890 0.94548 0.77088 -0.00534 -0.01550 -0.01491 227 LEU A N   
1740 C CA  . LEU A 227 ? 0.49187 0.97740 0.80178 -0.01056 -0.03277 -0.01851 227 LEU A CA  
1741 C C   . LEU A 227 ? 0.48978 0.99196 0.80397 0.01252  -0.04359 -0.01990 227 LEU A C   
1742 O O   . LEU A 227 ? 0.61165 1.15547 0.95215 0.02235  -0.04331 -0.02085 227 LEU A O   
1743 C CB  . LEU A 227 ? 0.47390 0.99067 0.80874 -0.03403 -0.03753 -0.02190 227 LEU A CB  
1744 C CG  . LEU A 227 ? 0.44297 0.96638 0.77905 -0.03842 -0.05741 -0.02741 227 LEU A CG  
1745 C CD1 . LEU A 227 ? 0.49852 0.97144 0.80070 -0.04610 -0.06283 -0.02825 227 LEU A CD1 
1746 C CD2 . LEU A 227 ? 0.45940 1.02626 0.82866 -0.05930 -0.06273 -0.03164 227 LEU A CD2 
1747 N N   . HIS A 228 ? 0.44934 0.91940 0.73725 0.02193  -0.05270 -0.01962 228 HIS A N   
1748 C CA  . HIS A 228 ? 0.47694 0.95512 0.76217 0.04401  -0.06362 -0.01965 228 HIS A CA  
1749 C C   . HIS A 228 ? 0.44853 0.93258 0.73130 0.03724  -0.08200 -0.02397 228 HIS A C   
1750 O O   . HIS A 228 ? 0.46967 0.92120 0.72982 0.02614  -0.08562 -0.02519 228 HIS A O   
1751 C CB  . HIS A 228 ? 0.46660 0.90253 0.72119 0.06122  -0.05870 -0.01515 228 HIS A CB  
1752 C CG  . HIS A 228 ? 0.50912 0.94151 0.76566 0.07186  -0.04350 -0.01219 228 HIS A CG  
1753 N ND1 . HIS A 228 ? 0.51641 0.95179 0.77192 0.09575  -0.04256 -0.01022 228 HIS A ND1 
1754 C CD2 . HIS A 228 ? 0.51701 0.94145 0.77428 0.06234  -0.02906 -0.01124 228 HIS A CD2 
1755 C CE1 . HIS A 228 ? 0.58157 1.01045 0.83711 0.10002  -0.02811 -0.00910 228 HIS A CE1 
1756 N NE2 . HIS A 228 ? 0.53995 0.96322 0.79642 0.08002  -0.01990 -0.00965 228 HIS A NE2 
1757 N N   . ARG A 229 ? 0.42794 0.95384 0.73344 0.04481  -0.09390 -0.02677 229 ARG A N   
1758 C CA  . ARG A 229 ? 0.38707 0.92442 0.69222 0.03904  -0.11343 -0.03194 229 ARG A CA  
1759 C C   . ARG A 229 ? 0.45418 0.98035 0.73853 0.06376  -0.12507 -0.02977 229 ARG A C   
1760 O O   . ARG A 229 ? 0.41765 0.94224 0.69916 0.08641  -0.11983 -0.02475 229 ARG A O   
1761 C CB  . ARG A 229 ? 0.32139 0.91700 0.66768 0.02851  -0.12124 -0.03710 229 ARG A CB  
1762 C CG  . ARG A 229 ? 0.34377 0.94834 0.70765 -0.00125 -0.11301 -0.03967 229 ARG A CG  
1763 C CD  . ARG A 229 ? 0.37125 1.03294 0.77459 -0.01451 -0.12399 -0.04562 229 ARG A CD  
1764 N NE  . ARG A 229 ? 0.32556 1.01720 0.75997 -0.02997 -0.10852 -0.04439 229 ARG A NE  
1765 C CZ  . ARG A 229 ? 0.30855 0.98914 0.74488 -0.05862 -0.10135 -0.04522 229 ARG A CZ  
1766 N NH1 . ARG A 229 ? 0.29722 0.93699 0.70706 -0.07457 -0.10848 -0.04806 229 ARG A NH1 
1767 N NH2 . ARG A 229 ? 0.31612 1.02578 0.77996 -0.07087 -0.08603 -0.04292 229 ARG A NH2 
1768 N N   . ASP A 230 ? 0.44268 0.95939 0.71055 0.05901  -0.14105 -0.03372 230 ASP A N   
1769 C CA  . ASP A 230 ? 0.45269 0.95309 0.69386 0.07966  -0.15307 -0.03144 230 ASP A CA  
1770 C C   . ASP A 230 ? 0.51506 0.97455 0.72887 0.09772  -0.13992 -0.02306 230 ASP A C   
1771 O O   . ASP A 230 ? 0.54437 1.00620 0.75399 0.12120  -0.14140 -0.01805 230 ASP A O   
1772 C CB  . ASP A 230 ? 0.39391 0.94091 0.65730 0.09544  -0.16862 -0.03287 230 ASP A CB  
1773 C CG  . ASP A 230 ? 0.48580 1.02900 0.72811 0.10043  -0.18984 -0.03606 230 ASP A CG  
1774 O OD1 . ASP A 230 ? 0.53583 1.09890 0.78890 0.08191  -0.20305 -0.04439 230 ASP A OD1 
1775 O OD2 . ASP A 230 ? 0.53588 1.05350 0.74846 0.12193  -0.19309 -0.03027 230 ASP A OD2 
1776 N N   . VAL A 231 ? 0.54014 0.96133 0.73542 0.08594  -0.12720 -0.02167 231 VAL A N   
1777 C CA  . VAL A 231 ? 0.49267 0.87373 0.66245 0.09821  -0.11456 -0.01460 231 VAL A CA  
1778 C C   . VAL A 231 ? 0.51148 0.86304 0.64635 0.10877  -0.12286 -0.01206 231 VAL A C   
1779 O O   . VAL A 231 ? 0.52398 0.86417 0.64382 0.09782  -0.13059 -0.01636 231 VAL A O   
1780 C CB  . VAL A 231 ? 0.46858 0.82380 0.63339 0.08174  -0.09927 -0.01440 231 VAL A CB  
1781 C CG1 . VAL A 231 ? 0.42403 0.73523 0.55828 0.09024  -0.09011 -0.00867 231 VAL A CG1 
1782 C CG2 . VAL A 231 ? 0.48780 0.86501 0.67983 0.07766  -0.08751 -0.01413 231 VAL A CG2 
1783 N N   . GLN A 232 ? 0.49649 0.83374 0.61642 0.13024  -0.12079 -0.00501 232 GLN A N   
1784 C CA  . GLN A 232 ? 0.52164 0.82620 0.60494 0.14062  -0.12511 -0.00053 232 GLN A CA  
1785 C C   . GLN A 232 ? 0.50386 0.76501 0.56387 0.13882  -0.10898 0.00484  232 GLN A C   
1786 O O   . GLN A 232 ? 0.46069 0.69370 0.49128 0.13896  -0.10951 0.00686  232 GLN A O   
1787 C CB  . GLN A 232 ? 0.53831 0.84991 0.61491 0.16567  -0.13392 0.00510  232 GLN A CB  
1788 N N   . GLU A 233 ? 0.49872 0.75552 0.57150 0.13676  -0.09475 0.00673  233 GLU A N   
1789 C CA  . GLU A 233 ? 0.44490 0.66409 0.49874 0.13586  -0.08031 0.01175  233 GLU A CA  
1790 C C   . GLU A 233 ? 0.44223 0.66516 0.51535 0.13035  -0.06753 0.01102  233 GLU A C   
1791 O O   . GLU A 233 ? 0.44984 0.69534 0.54257 0.13829  -0.06734 0.01046  233 GLU A O   
1792 C CB  . GLU A 233 ? 0.50789 0.70243 0.53728 0.15479  -0.07940 0.02012  233 GLU A CB  
1793 C CG  . GLU A 233 ? 0.53335 0.69082 0.54529 0.15252  -0.06448 0.02538  233 GLU A CG  
1794 C CD  . GLU A 233 ? 0.53990 0.66977 0.52443 0.16846  -0.06368 0.03428  233 GLU A CD  
1795 O OE1 . GLU A 233 ? 0.69989 0.83977 0.68030 0.18417  -0.07449 0.03676  233 GLU A OE1 
1796 O OE2 . GLU A 233 ? 0.54530 0.64393 0.51241 0.16518  -0.05248 0.03912  233 GLU A OE2 
1797 N N   . ILE A 234 ? 0.47131 0.67279 0.53795 0.11781  -0.05707 0.01082  234 ILE A N   
1798 C CA  . ILE A 234 ? 0.41728 0.61259 0.49320 0.11404  -0.04431 0.01122  234 ILE A CA  
1799 C C   . ILE A 234 ? 0.42643 0.58576 0.48029 0.11818  -0.03549 0.01666  234 ILE A C   
1800 O O   . ILE A 234 ? 0.46021 0.60059 0.49762 0.11219  -0.03427 0.01786  234 ILE A O   
1801 C CB  . ILE A 234 ? 0.38742 0.58976 0.47564 0.09515  -0.04031 0.00646  234 ILE A CB  
1802 C CG1 . ILE A 234 ? 0.29758 0.53163 0.40417 0.08708  -0.04998 0.00125  234 ILE A CG1 
1803 C CG2 . ILE A 234 ? 0.41655 0.61834 0.51532 0.09285  -0.02891 0.00647  234 ILE A CG2 
1804 C CD1 . ILE A 234 ? 0.31188 0.54546 0.42428 0.06772  -0.04721 -0.00257 234 ILE A CD1 
1805 N N   . ARG A 235 ? 0.40717 0.55708 0.46067 0.12813  -0.02902 0.01958  235 ARG A N   
1806 C CA  . ARG A 235 ? 0.45457 0.57028 0.48862 0.13080  -0.02065 0.02471  235 ARG A CA  
1807 C C   . ARG A 235 ? 0.45619 0.56404 0.49771 0.12342  -0.01013 0.02251  235 ARG A C   
1808 O O   . ARG A 235 ? 0.45192 0.57338 0.50735 0.12729  -0.00812 0.01955  235 ARG A O   
1809 C CB  . ARG A 235 ? 0.48452 0.58666 0.50515 0.14921  -0.02260 0.03050  235 ARG A CB  
1810 C CG  . ARG A 235 ? 0.57890 0.68298 0.58565 0.15817  -0.03319 0.03405  235 ARG A CG  
1811 C CD  . ARG A 235 ? 0.69653 0.77033 0.67888 0.17273  -0.03127 0.04257  235 ARG A CD  
1812 N NE  . ARG A 235 ? 0.69493 0.75549 0.68042 0.17978  -0.02368 0.04349  235 ARG A NE  
1813 C CZ  . ARG A 235 ? 0.75300 0.77974 0.71761 0.18901  -0.01868 0.05043  235 ARG A CZ  
1814 N NH1 . ARG A 235 ? 0.75787 0.76128 0.69683 0.19244  -0.01950 0.05831  235 ARG A NH1 
1815 N NH2 . ARG A 235 ? 0.66900 0.68302 0.63667 0.19455  -0.01224 0.04944  235 ARG A NH2 
1816 N N   . TYR A 236 ? 0.45925 0.54609 0.49101 0.11366  -0.00351 0.02379  236 TYR A N   
1817 C CA  . TYR A 236 ? 0.45076 0.52823 0.48692 0.10587  0.00507  0.02163  236 TYR A CA  
1818 C C   . TYR A 236 ? 0.49093 0.53804 0.51147 0.10884  0.01142  0.02604  236 TYR A C   
1819 O O   . TYR A 236 ? 0.49434 0.52587 0.50055 0.10827  0.01231  0.03090  236 TYR A O   
1820 C CB  . TYR A 236 ? 0.36199 0.44330 0.40290 0.09082  0.00675  0.01885  236 TYR A CB  
1821 C CG  . TYR A 236 ? 0.37657 0.48314 0.43267 0.08480  0.00231  0.01438  236 TYR A CG  
1822 C CD1 . TYR A 236 ? 0.38975 0.51218 0.45975 0.08535  0.00412  0.01130  236 TYR A CD1 
1823 C CD2 . TYR A 236 ? 0.36636 0.47951 0.42173 0.07801  -0.00293 0.01312  236 TYR A CD2 
1824 C CE1 . TYR A 236 ? 0.38137 0.52663 0.46543 0.07803  0.00144  0.00809  236 TYR A CE1 
1825 C CE2 . TYR A 236 ? 0.35881 0.49221 0.42749 0.07044  -0.00678 0.00920  236 TYR A CE2 
1826 C CZ  . TYR A 236 ? 0.42676 0.57671 0.51042 0.06982  -0.00423 0.00721  236 TYR A CZ  
1827 O OH  . TYR A 236 ? 0.41809 0.58827 0.51539 0.06065  -0.00660 0.00419  236 TYR A OH  
1828 N N   . GLU A 237 ? 0.47219 0.51009 0.49447 0.11131  0.01632  0.02414  237 GLU A N   
1829 C CA  . GLU A 237 ? 0.50561 0.51300 0.51445 0.11021  0.02269  0.02703  237 GLU A CA  
1830 C C   . GLU A 237 ? 0.47843 0.48136 0.49285 0.10732  0.02722  0.02138  237 GLU A C   
1831 O O   . GLU A 237 ? 0.49530 0.51589 0.52030 0.11189  0.02610  0.01669  237 GLU A O   
1832 C CB  . GLU A 237 ? 0.47792 0.46515 0.47024 0.12430  0.02170  0.03336  237 GLU A CB  
1833 C CG  . GLU A 237 ? 0.57790 0.57563 0.57427 0.14131  0.01714  0.03204  237 GLU A CG  
1834 C CD  . GLU A 237 ? 0.67804 0.65731 0.65629 0.15709  0.01396  0.03955  237 GLU A CD  
1835 O OE1 . GLU A 237 ? 0.63297 0.57826 0.59260 0.15638  0.01921  0.04496  237 GLU A OE1 
1836 O OE2 . GLU A 237 ? 0.62971 0.62860 0.61212 0.16980  0.00591  0.04034  237 GLU A OE2 
1837 N N   . VAL A 238 ? 0.47190 0.45197 0.47893 0.09903  0.03254  0.02157  238 VAL A N   
1838 C CA  . VAL A 238 ? 0.50976 0.48163 0.51832 0.09575  0.03596  0.01545  238 VAL A CA  
1839 C C   . VAL A 238 ? 0.54187 0.49963 0.54221 0.11099  0.03670  0.01450  238 VAL A C   
1840 O O   . VAL A 238 ? 0.61238 0.54710 0.59882 0.11899  0.03729  0.01987  238 VAL A O   
1841 C CB  . VAL A 238 ? 0.44038 0.39233 0.44403 0.08209  0.04010  0.01546  238 VAL A CB  
1842 C CG1 . VAL A 238 ? 0.51775 0.45723 0.51931 0.07935  0.04222  0.00836  238 VAL A CG1 
1843 C CG2 . VAL A 238 ? 0.38268 0.35233 0.39667 0.06959  0.03931  0.01540  238 VAL A CG2 
1844 N N   . SER A 239 ? 0.49204 0.46270 0.49956 0.11598  0.03723  0.00797  239 SER A N   
1845 C CA  . SER A 239 ? 0.49165 0.45333 0.49321 0.13306  0.03839  0.00591  239 SER A CA  
1846 C C   . SER A 239 ? 0.51338 0.43426 0.49660 0.13373  0.04232  0.00489  239 SER A C   
1847 O O   . SER A 239 ? 0.55355 0.45928 0.53288 0.11879  0.04456  0.00266  239 SER A O   
1848 C CB  . SER A 239 ? 0.50558 0.49114 0.51868 0.13657  0.04017  -0.00150 239 SER A CB  
1849 O OG  . SER A 239 ? 0.51282 0.48635 0.51857 0.15308  0.04306  -0.00516 239 SER A OG  
1850 N N   . ALA A 240 ? 0.54672 0.44949 0.51871 0.15142  0.04263  0.00643  240 ALA A N   
1851 C CA  . ALA A 240 ? 0.56612 0.42737 0.51922 0.15386  0.04656  0.00383  240 ALA A CA  
1852 C C   . ALA A 240 ? 0.63592 0.49759 0.58956 0.15496  0.04973  -0.00722 240 ALA A C   
1853 O O   . ALA A 240 ? 0.66995 0.49896 0.60930 0.14920  0.05246  -0.01208 240 ALA A O   
1854 C CB  . ALA A 240 ? 0.54274 0.38103 0.48094 0.17468  0.04569  0.00943  240 ALA A CB  
1855 N N   . LYS A 241 ? 0.62597 0.52351 0.59481 0.16140  0.04963  -0.01138 241 LYS A N   
1856 C CA  . LYS A 241 ? 0.60432 0.50643 0.57283 0.16336  0.05368  -0.02148 241 LYS A CA  
1857 C C   . LYS A 241 ? 0.55660 0.46759 0.52985 0.14224  0.05362  -0.02544 241 LYS A C   
1858 O O   . LYS A 241 ? 0.55624 0.48193 0.53950 0.12864  0.05051  -0.02045 241 LYS A O   
1859 C CB  . LYS A 241 ? 0.62145 0.56100 0.60527 0.17848  0.05496  -0.02316 241 LYS A CB  
1860 C CG  . LYS A 241 ? 0.62675 0.56529 0.60970 0.20147  0.05339  -0.01904 241 LYS A CG  
1861 C CD  . LYS A 241 ? 0.72304 0.71027 0.72940 0.21115  0.05232  -0.01833 241 LYS A CD  
1862 C CE  . LYS A 241 ? 0.73337 0.72323 0.74056 0.23520  0.04888  -0.01411 241 LYS A CE  
1863 N NZ  . LYS A 241 ? 0.65903 0.70042 0.69264 0.24070  0.04527  -0.01223 241 LYS A NZ  
1864 N N   . LYS A 242 ? 0.59829 0.49945 0.56265 0.14091  0.05677  -0.03480 242 LYS A N   
1865 C CA  . LYS A 242 ? 0.51505 0.42356 0.48116 0.12327  0.05576  -0.03924 242 LYS A CA  
1866 C C   . LYS A 242 ? 0.58239 0.50319 0.54526 0.12929  0.06007  -0.04780 242 LYS A C   
1867 O O   . LYS A 242 ? 0.60909 0.51838 0.56187 0.14510  0.06450  -0.05325 242 LYS A O   
1868 C CB  . LYS A 242 ? 0.58463 0.45886 0.53737 0.10940  0.05362  -0.04235 242 LYS A CB  
1869 C CG  . LYS A 242 ? 0.64530 0.50597 0.59986 0.10147  0.05134  -0.03365 242 LYS A CG  
1870 C CD  . LYS A 242 ? 0.72194 0.55910 0.66986 0.08305  0.04943  -0.03672 242 LYS A CD  
1871 C CE  . LYS A 242 ? 0.65194 0.51581 0.61458 0.06668  0.04579  -0.03615 242 LYS A CE  
1872 N NZ  . LYS A 242 ? 0.69349 0.54067 0.65420 0.04854  0.04323  -0.03884 242 LYS A NZ  
1873 N N   . ILE A 243 ? 0.61311 0.55641 0.58305 0.11751  0.05927  -0.04870 243 ILE A N   
1874 C CA  . ILE A 243 ? 0.57686 0.52915 0.53978 0.12007  0.06373  -0.05636 243 ILE A CA  
1875 C C   . ILE A 243 ? 0.59148 0.51384 0.53469 0.11145  0.06130  -0.06501 243 ILE A C   
1876 O O   . ILE A 243 ? 0.55793 0.46819 0.50116 0.09679  0.05519  -0.06359 243 ILE A O   
1877 C CB  . ILE A 243 ? 0.52755 0.51501 0.50423 0.11148  0.06401  -0.05233 243 ILE A CB  
1878 C CG1 . ILE A 243 ? 0.53682 0.53409 0.50428 0.11571  0.07056  -0.05898 243 ILE A CG1 
1879 C CG2 . ILE A 243 ? 0.47739 0.46320 0.45660 0.09327  0.05707  -0.04921 243 ILE A CG2 
1880 C CD1 . ILE A 243 ? 0.46755 0.49483 0.44493 0.10650  0.07182  -0.05436 243 ILE A CD1 
1881 N N   . HIS A 244 ? 0.62419 0.53518 0.55065 0.12071  0.06604  -0.07456 244 HIS A N   
1882 C CA  . HIS A 244 ? 0.62496 0.50602 0.52978 0.11357  0.06306  -0.08478 244 HIS A CA  
1883 C C   . HIS A 244 ? 0.56753 0.46432 0.46396 0.11034  0.06473  -0.09022 244 HIS A C   
1884 O O   . HIS A 244 ? 0.59454 0.51071 0.49110 0.12211  0.07284  -0.09105 244 HIS A O   
1885 C CB  . HIS A 244 ? 0.65219 0.49778 0.53754 0.12774  0.06668  -0.09293 244 HIS A CB  
1886 C CG  . HIS A 244 ? 0.72014 0.54854 0.61050 0.13425  0.06615  -0.08633 244 HIS A CG  
1887 N ND1 . HIS A 244 ? 0.74005 0.54073 0.62711 0.12133  0.06052  -0.08401 244 HIS A ND1 
1888 C CD2 . HIS A 244 ? 0.76721 0.60289 0.66506 0.15247  0.07045  -0.08102 244 HIS A CD2 
1889 C CE1 . HIS A 244 ? 0.80784 0.59639 0.69724 0.13143  0.06197  -0.07699 244 HIS A CE1 
1890 N NE2 . HIS A 244 ? 0.78863 0.59811 0.68443 0.15105  0.06711  -0.07522 244 HIS A NE2 
1891 N N   . PHE A 245 ? 0.64221 0.53191 0.53150 0.09457  0.05718  -0.09352 245 PHE A N   
1892 C CA  . PHE A 245 ? 0.67547 0.57508 0.55186 0.09079  0.05692  -0.09863 245 PHE A CA  
1893 C C   . PHE A 245 ? 0.70945 0.57647 0.55784 0.09053  0.05412  -0.11263 245 PHE A C   
1894 O O   . PHE A 245 ? 0.72888 0.56977 0.57287 0.08141  0.04679  -0.11687 245 PHE A O   
1895 C CB  . PHE A 245 ? 0.61953 0.53690 0.50694 0.07450  0.04869  -0.09232 245 PHE A CB  
1896 C CG  . PHE A 245 ? 0.61084 0.55907 0.52127 0.07401  0.05128  -0.08001 245 PHE A CG  
1897 C CD1 . PHE A 245 ? 0.58790 0.53957 0.51792 0.07057  0.04867  -0.07209 245 PHE A CD1 
1898 C CD2 . PHE A 245 ? 0.54891 0.52109 0.45962 0.07609  0.05647  -0.07644 245 PHE A CD2 
1899 C CE1 . PHE A 245 ? 0.51849 0.49642 0.46750 0.06974  0.05018  -0.06207 245 PHE A CE1 
1900 C CE2 . PHE A 245 ? 0.57851 0.57638 0.50955 0.07392  0.05830  -0.06586 245 PHE A CE2 
1901 C CZ  . PHE A 245 ? 0.52167 0.52217 0.47168 0.07095  0.05460  -0.05928 245 PHE A CZ  
1902 N N   . ALA A 246 ? 0.73223 0.60051 0.56102 0.09961  0.06019  -0.12002 246 ALA A N   
1903 C CA  . ALA A 246 ? 0.82328 0.66258 0.62204 0.09781  0.05613  -0.13427 246 ALA A CA  
1904 C C   . ALA A 246 ? 0.85741 0.70570 0.65238 0.08127  0.04526  -0.13439 246 ALA A C   
1905 O O   . ALA A 246 ? 0.88784 0.76142 0.68298 0.08108  0.04760  -0.12919 246 ALA A O   
1906 C CB  . ALA A 246 ? 0.87219 0.70926 0.64890 0.11530  0.06761  -0.14249 246 ALA A CB  
1907 N N   . ARG A 247 ? 0.92535 0.75383 0.71790 0.06720  0.03327  -0.13963 247 ARG A N   
1908 C CA  . ARG A 247 ? 1.03879 0.87573 0.82819 0.05247  0.02097  -0.14110 247 ARG A CA  
1909 C C   . ARG A 247 ? 1.05260 0.86353 0.80859 0.05122  0.01510  -0.15733 247 ARG A C   
1910 O O   . ARG A 247 ? 1.11589 0.89405 0.85695 0.05407  0.01588  -0.16801 247 ARG A O   
1911 C CB  . ARG A 247 ? 1.00282 0.84226 0.81599 0.03611  0.01066  -0.13596 247 ARG A CB  
1912 C CG  . ARG A 247 ? 1.11825 0.92401 0.92785 0.02934  0.00692  -0.14398 247 ARG A CG  
1913 C CD  . ARG A 247 ? 1.22451 1.03317 1.04862 0.00894  -0.00632 -0.14424 247 ARG A CD  
1914 N NE  . ARG A 247 ? 1.28253 1.08987 1.08937 0.00058  -0.01830 -0.15505 247 ARG A NE  
1915 C CZ  . ARG A 247 ? 1.15503 0.96913 0.97280 -0.01665 -0.03171 -0.15760 247 ARG A CZ  
1916 N NH1 . ARG A 247 ? 1.12017 0.94336 0.96652 -0.02800 -0.03352 -0.14995 247 ARG A NH1 
1917 N NH2 . ARG A 247 ? 1.12401 0.93730 0.92357 -0.02228 -0.04357 -0.16817 247 ARG A NH2 
1918 N N   . PHE A 248 ? 1.05407 0.87750 0.79597 0.04751  0.00891  -0.15923 248 PHE A N   
1919 C CA  . PHE A 248 ? 1.03028 0.83134 0.73824 0.04549  0.00120  -0.17486 248 PHE A CA  
1920 C C   . PHE A 248 ? 1.00941 0.81808 0.71877 0.02889  -0.01700 -0.17704 248 PHE A C   
1921 O O   . PHE A 248 ? 1.09644 0.88812 0.77805 0.02519  -0.02652 -0.19055 248 PHE A O   
1922 C CB  . PHE A 248 ? 1.07805 0.88334 0.75766 0.06025  0.01160  -0.17774 248 PHE A CB  
1923 C CG  . PHE A 248 ? 1.16186 0.95376 0.83275 0.07789  0.02799  -0.18167 248 PHE A CG  
1924 C CD1 . PHE A 248 ? 1.11992 0.87445 0.76395 0.08349  0.02815  -0.19794 248 PHE A CD1 
1925 C CD2 . PHE A 248 ? 1.06292 0.87958 0.75301 0.08916  0.04268  -0.16959 248 PHE A CD2 
1926 C CE1 . PHE A 248 ? 1.12649 0.86856 0.76253 0.10220  0.04318  -0.20175 248 PHE A CE1 
1927 C CE2 . PHE A 248 ? 1.01665 0.82495 0.70135 0.10684  0.05713  -0.17333 248 PHE A CE2 
1928 C CZ  . PHE A 248 ? 1.05558 0.82651 0.71309 0.11448  0.05764  -0.18924 248 PHE A CZ  
1929 N N   . ARG A 249 ? 1.00204 0.83612 0.74250 0.01963  -0.02250 -0.16480 249 ARG A N   
1930 C CA  . ARG A 249 ? 1.00043 0.84672 0.74829 0.00510  -0.03992 -0.16578 249 ARG A CA  
1931 C C   . ARG A 249 ? 0.95317 0.82482 0.74007 -0.00150 -0.04065 -0.15134 249 ARG A C   
1932 O O   . ARG A 249 ? 0.90395 0.78420 0.70742 0.00558  -0.02840 -0.14060 249 ARG A O   
1933 C CB  . ARG A 249 ? 0.93364 0.79205 0.65772 0.00881  -0.04608 -0.16647 249 ARG A CB  
1934 C CG  . ARG A 249 ? 0.99324 0.87033 0.71598 0.02130  -0.03265 -0.15352 249 ARG A CG  
1935 C CD  . ARG A 249 ? 0.98456 0.87125 0.68223 0.02382  -0.03904 -0.15237 249 ARG A CD  
1936 N NE  . ARG A 249 ? 1.00578 0.90613 0.69891 0.03451  -0.02406 -0.14049 249 ARG A NE  
1937 C CZ  . ARG A 249 ? 1.02460 0.93726 0.70311 0.03680  -0.02612 -0.13284 249 ARG A CZ  
1938 N NH1 . ARG A 249 ? 1.03293 0.94745 0.69926 0.03133  -0.04349 -0.13555 249 ARG A NH1 
1939 N NH2 . ARG A 249 ? 1.04816 0.97168 0.72446 0.04453  -0.01068 -0.12183 249 ARG A NH2 
1940 N N   . SER A 250 ? 0.92278 0.80755 0.72409 -0.01465 -0.05548 -0.15174 250 SER A N   
1941 C CA  . SER A 250 ? 0.85608 0.76483 0.69353 -0.02091 -0.05667 -0.13949 250 SER A CA  
1942 C C   . SER A 250 ? 0.88103 0.81545 0.72293 -0.01248 -0.05400 -0.12664 250 SER A C   
1943 O O   . SER A 250 ? 0.86715 0.81043 0.69375 -0.01089 -0.06273 -0.12754 250 SER A O   
1944 C CB  . SER A 250 ? 0.83711 0.75413 0.69048 -0.03729 -0.07279 -0.14483 250 SER A CB  
1945 O OG  . SER A 250 ? 0.76831 0.70547 0.65712 -0.04311 -0.07124 -0.13409 250 SER A OG  
1946 N N   . PHE A 251 ? 0.82450 0.76864 0.68527 -0.00712 -0.04233 -0.11476 251 PHE A N   
1947 C CA  . PHE A 251 ? 0.71027 0.67721 0.58043 -0.00185 -0.03997 -0.10174 251 PHE A CA  
1948 C C   . PHE A 251 ? 0.66844 0.64761 0.57144 -0.00571 -0.03678 -0.09260 251 PHE A C   
1949 O O   . PHE A 251 ? 0.67165 0.65119 0.58314 0.00007  -0.02499 -0.08569 251 PHE A O   
1950 C CB  . PHE A 251 ? 0.70299 0.66797 0.55605 0.01013  -0.02678 -0.09735 251 PHE A CB  
1951 C CG  . PHE A 251 ? 0.66666 0.64897 0.51821 0.01394  -0.02655 -0.08636 251 PHE A CG  
1952 C CD1 . PHE A 251 ? 0.65856 0.65492 0.52073 0.00932  -0.03848 -0.08162 251 PHE A CD1 
1953 C CD2 . PHE A 251 ? 0.70924 0.69353 0.54907 0.02222  -0.01399 -0.08057 251 PHE A CD2 
1954 C CE1 . PHE A 251 ? 0.63668 0.64403 0.49473 0.01364  -0.03828 -0.07115 251 PHE A CE1 
1955 C CE2 . PHE A 251 ? 0.72335 0.71963 0.56008 0.02417  -0.01321 -0.06990 251 PHE A CE2 
1956 C CZ  . PHE A 251 ? 0.72698 0.73243 0.57131 0.02024  -0.02556 -0.06509 251 PHE A CZ  
1957 N N   . PRO A 252 ? 0.64332 0.63405 0.56552 -0.01535 -0.04720 -0.09274 252 PRO A N   
1958 C CA  . PRO A 252 ? 0.57820 0.57806 0.52971 -0.01981 -0.04323 -0.08565 252 PRO A CA  
1959 C C   . PRO A 252 ? 0.55509 0.56931 0.51690 -0.01182 -0.03573 -0.07300 252 PRO A C   
1960 O O   . PRO A 252 ? 0.59930 0.62299 0.55284 -0.00621 -0.03793 -0.06833 252 PRO A O   
1961 C CB  . PRO A 252 ? 0.56324 0.57872 0.53176 -0.03058 -0.05651 -0.08848 252 PRO A CB  
1962 C CG  . PRO A 252 ? 0.61032 0.61750 0.55778 -0.03428 -0.06789 -0.10026 252 PRO A CG  
1963 C CD  . PRO A 252 ? 0.62686 0.62477 0.54512 -0.02238 -0.06319 -0.09975 252 PRO A CD  
1964 N N   . PHE A 253 ? 0.60390 0.61756 0.58224 -0.01179 -0.02714 -0.06746 253 PHE A N   
1965 C CA  . PHE A 253 ? 0.50661 0.53146 0.49431 -0.00511 -0.02006 -0.05668 253 PHE A CA  
1966 C C   . PHE A 253 ? 0.43931 0.48287 0.43553 -0.00482 -0.02719 -0.05097 253 PHE A C   
1967 O O   . PHE A 253 ? 0.46240 0.51054 0.45150 0.00152  -0.02512 -0.04485 253 PHE A O   
1968 C CB  . PHE A 253 ? 0.52309 0.54542 0.52759 -0.00657 -0.01276 -0.05253 253 PHE A CB  
1969 C CG  . PHE A 253 ? 0.47866 0.51086 0.49170 -0.00034 -0.00629 -0.04288 253 PHE A CG  
1970 C CD1 . PHE A 253 ? 0.50396 0.53199 0.50869 0.00726  0.00168  -0.04051 253 PHE A CD1 
1971 C CD2 . PHE A 253 ? 0.40185 0.44823 0.43164 -0.00207 -0.00827 -0.03686 253 PHE A CD2 
1972 C CE1 . PHE A 253 ? 0.49360 0.53100 0.50667 0.01129  0.00640  -0.03257 253 PHE A CE1 
1973 C CE2 . PHE A 253 ? 0.42093 0.47350 0.45617 0.00313  -0.00307 -0.02925 253 PHE A CE2 
1974 C CZ  . PHE A 253 ? 0.45160 0.49942 0.47851 0.00896  0.00371  -0.02722 253 PHE A CZ  
1975 N N   . TRP A 254 ? 0.44184 0.49627 0.45348 -0.01158 -0.03552 -0.05285 254 TRP A N   
1976 C CA  . TRP A 254 ? 0.45168 0.52461 0.47273 -0.00892 -0.04247 -0.04751 254 TRP A CA  
1977 C C   . TRP A 254 ? 0.44785 0.52131 0.44870 -0.00452 -0.05112 -0.04892 254 TRP A C   
1978 O O   . TRP A 254 ? 0.44925 0.53122 0.44930 0.00170  -0.05427 -0.04215 254 TRP A O   
1979 C CB  . TRP A 254 ? 0.39442 0.48307 0.43935 -0.01660 -0.04886 -0.04965 254 TRP A CB  
1980 C CG  . TRP A 254 ? 0.42660 0.51373 0.48883 -0.02119 -0.03944 -0.04710 254 TRP A CG  
1981 C CD1 . TRP A 254 ? 0.44553 0.52668 0.51622 -0.03175 -0.03810 -0.05220 254 TRP A CD1 
1982 C CD2 . TRP A 254 ? 0.35354 0.44257 0.42378 -0.01568 -0.03001 -0.03865 254 TRP A CD2 
1983 N NE1 . TRP A 254 ? 0.36959 0.44894 0.45226 -0.03248 -0.02789 -0.04643 254 TRP A NE1 
1984 C CE2 . TRP A 254 ? 0.39677 0.48168 0.47920 -0.02233 -0.02324 -0.03855 254 TRP A CE2 
1985 C CE3 . TRP A 254 ? 0.37738 0.46946 0.44415 -0.00645 -0.02693 -0.03135 254 TRP A CE3 
1986 C CZ2 . TRP A 254 ? 0.32481 0.40989 0.41477 -0.01880 -0.01400 -0.03150 254 TRP A CZ2 
1987 C CZ3 . TRP A 254 ? 0.35680 0.44901 0.43238 -0.00389 -0.01834 -0.02545 254 TRP A CZ3 
1988 C CH2 . TRP A 254 ? 0.32530 0.41469 0.41174 -0.00944 -0.01220 -0.02562 254 TRP A CH2 
1989 N N   . ARG A 255 ? 0.45895 0.52100 0.44078 -0.00700 -0.05495 -0.05752 255 ARG A N   
1990 C CA  . ARG A 255 ? 0.47387 0.53353 0.43088 -0.00186 -0.06173 -0.05838 255 ARG A CA  
1991 C C   . ARG A 255 ? 0.46207 0.51376 0.40286 0.00608  -0.05089 -0.05072 255 ARG A C   
1992 O O   . ARG A 255 ? 0.46662 0.52138 0.39665 0.01158  -0.05367 -0.04397 255 ARG A O   
1993 C CB  . ARG A 255 ? 0.50305 0.55062 0.44100 -0.00637 -0.06787 -0.07062 255 ARG A CB  
1994 C CG  . ARG A 255 ? 0.49988 0.54000 0.40527 0.00024  -0.07099 -0.07140 255 ARG A CG  
1995 C CD  . ARG A 255 ? 0.61301 0.64422 0.49882 -0.00420 -0.08178 -0.08457 255 ARG A CD  
1996 N NE  . ARG A 255 ? 0.59721 0.64350 0.50015 -0.01201 -0.09787 -0.08984 255 ARG A NE  
1997 C CZ  . ARG A 255 ? 0.59081 0.65544 0.49866 -0.00883 -0.11024 -0.08548 255 ARG A CZ  
1998 N NH1 . ARG A 255 ? 0.59917 0.66561 0.49449 0.00173  -0.10834 -0.07493 255 ARG A NH1 
1999 N NH2 . ARG A 255 ? 0.57030 0.65187 0.49637 -0.01643 -0.12496 -0.09172 255 ARG A NH2 
2000 N N   . ARG A 256 ? 0.46953 0.51109 0.40878 0.00666  -0.03847 -0.05139 256 ARG A N   
2001 C CA  . ARG A 256 ? 0.49279 0.53162 0.42325 0.01252  -0.02715 -0.04399 256 ARG A CA  
2002 C C   . ARG A 256 ? 0.51640 0.56501 0.46100 0.01433  -0.02615 -0.03327 256 ARG A C   
2003 O O   . ARG A 256 ? 0.49389 0.54130 0.42664 0.01784  -0.02294 -0.02621 256 ARG A O   
2004 C CB  . ARG A 256 ? 0.54216 0.57348 0.47614 0.01345  -0.01534 -0.04668 256 ARG A CB  
2005 C CG  . ARG A 256 ? 0.66662 0.69323 0.58220 0.01908  -0.00493 -0.04576 256 ARG A CG  
2006 C CD  . ARG A 256 ? 0.75870 0.77467 0.67002 0.02177  0.00242  -0.05375 256 ARG A CD  
2007 N NE  . ARG A 256 ? 0.63023 0.64724 0.56305 0.02161  0.00712  -0.05181 256 ARG A NE  
2008 C CZ  . ARG A 256 ? 0.63444 0.64170 0.57459 0.01839  0.00430  -0.05748 256 ARG A CZ  
2009 N NH1 . ARG A 256 ? 0.63739 0.63374 0.56748 0.01369  -0.00360 -0.06651 256 ARG A NH1 
2010 N NH2 . ARG A 256 ? 0.65543 0.66281 0.61216 0.01930  0.00930  -0.05395 256 ARG A NH2 
2011 N N   . VAL A 257 ? 0.49044 0.54721 0.45888 0.01167  -0.02839 -0.03202 257 VAL A N   
2012 C CA  . VAL A 257 ? 0.46760 0.53170 0.44825 0.01427  -0.02762 -0.02323 257 VAL A CA  
2013 C C   . VAL A 257 ? 0.42214 0.49021 0.39464 0.01807  -0.03764 -0.01961 257 VAL A C   
2014 O O   . VAL A 257 ? 0.43314 0.49829 0.39971 0.02219  -0.03577 -0.01161 257 VAL A O   
2015 C CB  . VAL A 257 ? 0.43775 0.50969 0.44360 0.01136  -0.02685 -0.02345 257 VAL A CB  
2016 C CG1 . VAL A 257 ? 0.31390 0.39301 0.33007 0.01528  -0.02773 -0.01602 257 VAL A CG1 
2017 C CG2 . VAL A 257 ? 0.37826 0.44384 0.38933 0.00978  -0.01659 -0.02447 257 VAL A CG2 
2018 N N   . HIS A 258 ? 0.45706 0.53110 0.42885 0.01675  -0.04907 -0.02546 258 HIS A N   
2019 C CA  . HIS A 258 ? 0.48521 0.56402 0.44802 0.02217  -0.06053 -0.02233 258 HIS A CA  
2020 C C   . HIS A 258 ? 0.51519 0.58031 0.44745 0.02659  -0.05842 -0.01745 258 HIS A C   
2021 O O   . HIS A 258 ? 0.52184 0.58363 0.44532 0.03258  -0.06086 -0.00907 258 HIS A O   
2022 C CB  . HIS A 258 ? 0.43728 0.52666 0.40410 0.01888  -0.07405 -0.03109 258 HIS A CB  
2023 C CG  . HIS A 258 ? 0.52698 0.62078 0.47945 0.02562  -0.08767 -0.02906 258 HIS A CG  
2024 N ND1 . HIS A 258 ? 0.56193 0.64364 0.48238 0.02832  -0.09128 -0.02987 258 HIS A ND1 
2025 C CD2 . HIS A 258 ? 0.46457 0.57380 0.42933 0.03147  -0.09876 -0.02612 258 HIS A CD2 
2026 C CE1 . HIS A 258 ? 0.51295 0.60098 0.42513 0.03539  -0.10477 -0.02697 258 HIS A CE1 
2027 N NE2 . HIS A 258 ? 0.50727 0.61265 0.44703 0.03794  -0.10985 -0.02478 258 HIS A NE2 
2028 N N   . ASP A 259 ? 0.51938 0.57506 0.43379 0.02401  -0.05316 -0.02241 259 ASP A N   
2029 C CA  . ASP A 259 ? 0.58630 0.63025 0.46995 0.02760  -0.05003 -0.01806 259 ASP A CA  
2030 C C   . ASP A 259 ? 0.56939 0.60742 0.45197 0.02837  -0.03752 -0.00784 259 ASP A C   
2031 O O   . ASP A 259 ? 0.64048 0.66999 0.50328 0.03151  -0.03700 0.00038  259 ASP A O   
2032 C CB  . ASP A 259 ? 0.62587 0.66225 0.49124 0.02550  -0.04606 -0.02700 259 ASP A CB  
2033 C CG  . ASP A 259 ? 0.60904 0.64807 0.47087 0.02334  -0.05992 -0.03802 259 ASP A CG  
2034 O OD1 . ASP A 259 ? 0.61132 0.65820 0.47414 0.02542  -0.07395 -0.03702 259 ASP A OD1 
2035 O OD2 . ASP A 259 ? 0.60646 0.63956 0.46460 0.01974  -0.05726 -0.04801 259 ASP A OD2 
2036 N N   . SER A 260 ? 0.59668 0.63838 0.49970 0.02502  -0.02792 -0.00799 260 SER A N   
2037 C CA  . SER A 260 ? 0.62632 0.66438 0.53029 0.02397  -0.01665 0.00024  260 SER A CA  
2038 C C   . SER A 260 ? 0.54794 0.58431 0.45945 0.02596  -0.02042 0.00848  260 SER A C   
2039 O O   . SER A 260 ? 0.56700 0.59491 0.46928 0.02497  -0.01439 0.01660  260 SER A O   
2040 C CB  . SER A 260 ? 0.52513 0.56875 0.44771 0.02079  -0.00683 -0.00324 260 SER A CB  
2041 O OG  . SER A 260 ? 0.60303 0.64565 0.51785 0.02074  -0.00275 -0.01112 260 SER A OG  
2042 N N   . PHE A 261 ? 0.46595 0.50971 0.39376 0.02858  -0.02973 0.00642  261 PHE A N   
2043 C CA  . PHE A 261 ? 0.52989 0.57194 0.46651 0.03217  -0.03221 0.01290  261 PHE A CA  
2044 C C   . PHE A 261 ? 0.49834 0.54138 0.42962 0.03989  -0.04519 0.01505  261 PHE A C   
2045 O O   . PHE A 261 ? 0.51229 0.54637 0.43883 0.04510  -0.04681 0.02237  261 PHE A O   
2046 C CB  . PHE A 261 ? 0.42377 0.47562 0.38770 0.03038  -0.02931 0.00974  261 PHE A CB  
2047 C CG  . PHE A 261 ? 0.36473 0.41621 0.33503 0.02476  -0.01798 0.00848  261 PHE A CG  
2048 C CD1 . PHE A 261 ? 0.38917 0.43311 0.35513 0.02255  -0.01053 0.01437  261 PHE A CD1 
2049 C CD2 . PHE A 261 ? 0.37597 0.43432 0.35656 0.02171  -0.01538 0.00138  261 PHE A CD2 
2050 C CE1 . PHE A 261 ? 0.40872 0.45627 0.38267 0.01813  -0.00143 0.01295  261 PHE A CE1 
2051 C CE2 . PHE A 261 ? 0.40897 0.46756 0.39516 0.01885  -0.00592 0.00055  261 PHE A CE2 
2052 C CZ  . PHE A 261 ? 0.37511 0.43048 0.35906 0.01744  0.00067  0.00622  261 PHE A CZ  
2053 N N   . ILE A 262 ? 0.47725 0.53051 0.40901 0.04117  -0.05512 0.00867  262 ILE A N   
2054 C CA  . ILE A 262 ? 0.55173 0.61090 0.48250 0.04961  -0.06890 0.01030  262 ILE A CA  
2055 C C   . ILE A 262 ? 0.52347 0.57024 0.42154 0.05414  -0.07500 0.01449  262 ILE A C   
2056 O O   . ILE A 262 ? 0.53541 0.57060 0.41920 0.06195  -0.07849 0.02330  262 ILE A O   
2057 C CB  . ILE A 262 ? 0.51402 0.59518 0.46741 0.04794  -0.07814 0.00110  262 ILE A CB  
2058 C CG1 . ILE A 262 ? 0.49138 0.58229 0.47367 0.04254  -0.06995 -0.00207 262 ILE A CG1 
2059 C CG2 . ILE A 262 ? 0.46380 0.55646 0.42129 0.05796  -0.09263 0.00297  262 ILE A CG2 
2060 C CD1 . ILE A 262 ? 0.35933 0.45188 0.35521 0.04903  -0.06748 0.00384  262 ILE A CD1 
2061 N N   . GLU A 263 ? 0.55747 0.60409 0.44092 0.04989  -0.07614 0.00832  263 GLU A N   
2062 C CA  . GLU A 263 ? 0.67905 0.71430 0.52811 0.05426  -0.08215 0.01132  263 GLU A CA  
2063 C C   . GLU A 263 ? 0.71663 0.75155 0.55126 0.04863  -0.08092 0.00203  263 GLU A C   
2064 O O   . GLU A 263 ? 0.75471 0.80231 0.60567 0.04414  -0.08610 -0.00877 263 GLU A O   
2065 C CB  . GLU A 263 ? 0.65391 0.69709 0.50063 0.06415  -0.10035 0.01246  263 GLU A CB  
2066 C CG  . GLU A 263 ? 0.76757 0.83653 0.64642 0.06254  -0.11073 0.00252  263 GLU A CG  
2067 C CD  . GLU A 263 ? 0.75761 0.83905 0.63044 0.06992  -0.13053 -0.00031 263 GLU A CD  
2068 O OE1 . GLU A 263 ? 0.78642 0.85543 0.62536 0.07397  -0.13643 0.00188  263 GLU A OE1 
2069 O OE2 . GLU A 263 ? 0.63356 0.73864 0.53560 0.07168  -0.14010 -0.00469 263 GLU A OE2 
2070 N N   . ASP A 264 ? 0.88077 0.90011 0.68364 0.04870  -0.07373 0.00594  264 ASP A N   
2071 C CA  . ASP A 264 ? 0.90253 0.91914 0.68627 0.04557  -0.07235 -0.00324 264 ASP A CA  
2072 C C   . ASP A 264 ? 1.02020 1.02230 0.76146 0.05091  -0.07505 0.00194  264 ASP A C   
2073 O O   . ASP A 264 ? 1.04532 1.04891 0.77185 0.05650  -0.09132 -0.00003 264 ASP A O   
2074 C CB  . ASP A 264 ? 0.86977 0.88427 0.66087 0.03905  -0.05442 -0.00623 264 ASP A CB  
2075 C CG  . ASP A 264 ? 0.98286 0.99459 0.75855 0.03701  -0.05291 -0.01807 264 ASP A CG  
2076 O OD1 . ASP A 264 ? 1.07073 1.08305 0.83357 0.03856  -0.06692 -0.02563 264 ASP A OD1 
2077 O OD2 . ASP A 264 ? 0.93614 0.94521 0.71244 0.03437  -0.03813 -0.02035 264 ASP A OD2 
# 
