data_8QGI
# 
_entry.id   8QGI 
# 
_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   8QGI         pdb_00008qgi 10.2210/pdb8qgi/pdb 
WWPDB D_1292133168 ?            ?                   
# 
_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                        8QGI 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8A9V 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gilles.labesse@cbs.cnrs.fr 
_pdbx_contact_author.name_first         Gilles 
_pdbx_contact_author.name_last          Labesse 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6861-3300 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gelin, M.'   1 ? 
'Labesse, G.' 2 ? 
'Lionne, C.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a di-adenosine derivative' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gelin, M.'      1 ? 
primary 'Labesse, G.'    2 ? 
primary 'Clement, D.'    3 ? 
primary 'Pochet, S.'     4 ? 
primary 'Lionne, C.'     5 ? 
primary 'Leseigneur, C.' 6 ? 
primary 'Huteau, V.'     7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'NAD kinase 1' 31045.279 1   2.7.1.23 ? ? ? 
2 non-polymer syn 'CITRIC ACID' 192.124   1   ?        ? ? ? 
3 non-polymer syn 
;1-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(3-azanylpropyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-(phenylmethyl)urea
;
758.787   1   ?        ? ? ? 
4 water       nat water 18.015    118 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ATP-dependent NAD kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 
;1-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(3-azanylpropyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-(phenylmethyl)urea
;
UZO 
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 
UZO non-polymer         . 
;1-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(3-azanylpropyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-(phenylmethyl)urea
;
? 'C34 H42 N14 O7' 758.787 
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        UZO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UZO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CIT 1   301 265 CIT CIT A . 
C 3 UZO 1   302 1   UZO XXX A . 
D 4 HOH 1   401 47  HOH HOH A . 
D 4 HOH 2   402 79  HOH HOH A . 
D 4 HOH 3   403 57  HOH HOH A . 
D 4 HOH 4   404 114 HOH HOH A . 
D 4 HOH 5   405 5   HOH HOH A . 
D 4 HOH 6   406 33  HOH HOH A . 
D 4 HOH 7   407 80  HOH HOH A . 
D 4 HOH 8   408 10  HOH HOH A . 
D 4 HOH 9   409 2   HOH HOH A . 
D 4 HOH 10  410 26  HOH HOH A . 
D 4 HOH 11  411 50  HOH HOH A . 
D 4 HOH 12  412 7   HOH HOH A . 
D 4 HOH 13  413 19  HOH HOH A . 
D 4 HOH 14  414 107 HOH HOH A . 
D 4 HOH 15  415 121 HOH HOH A . 
D 4 HOH 16  416 103 HOH HOH A . 
D 4 HOH 17  417 9   HOH HOH A . 
D 4 HOH 18  418 42  HOH HOH A . 
D 4 HOH 19  419 43  HOH HOH A . 
D 4 HOH 20  420 38  HOH HOH A . 
D 4 HOH 21  421 3   HOH HOH A . 
D 4 HOH 22  422 1   HOH HOH A . 
D 4 HOH 23  423 24  HOH HOH A . 
D 4 HOH 24  424 31  HOH HOH A . 
D 4 HOH 25  425 55  HOH HOH A . 
D 4 HOH 26  426 32  HOH HOH A . 
D 4 HOH 27  427 117 HOH HOH A . 
D 4 HOH 28  428 15  HOH HOH A . 
D 4 HOH 29  429 118 HOH HOH A . 
D 4 HOH 30  430 8   HOH HOH A . 
D 4 HOH 31  431 25  HOH HOH A . 
D 4 HOH 32  432 13  HOH HOH A . 
D 4 HOH 33  433 4   HOH HOH A . 
D 4 HOH 34  434 58  HOH HOH A . 
D 4 HOH 35  435 44  HOH HOH A . 
D 4 HOH 36  436 20  HOH HOH A . 
D 4 HOH 37  437 72  HOH HOH A . 
D 4 HOH 38  438 104 HOH HOH A . 
D 4 HOH 39  439 62  HOH HOH A . 
D 4 HOH 40  440 74  HOH HOH A . 
D 4 HOH 41  441 22  HOH HOH A . 
D 4 HOH 42  442 111 HOH HOH A . 
D 4 HOH 43  443 23  HOH HOH A . 
D 4 HOH 44  444 102 HOH HOH A . 
D 4 HOH 45  445 6   HOH HOH A . 
D 4 HOH 46  446 76  HOH HOH A . 
D 4 HOH 47  447 17  HOH HOH A . 
D 4 HOH 48  448 16  HOH HOH A . 
D 4 HOH 49  449 14  HOH HOH A . 
D 4 HOH 50  450 11  HOH HOH A . 
D 4 HOH 51  451 68  HOH HOH A . 
D 4 HOH 52  452 40  HOH HOH A . 
D 4 HOH 53  453 54  HOH HOH A . 
D 4 HOH 54  454 41  HOH HOH A . 
D 4 HOH 55  455 18  HOH HOH A . 
D 4 HOH 56  456 120 HOH HOH A . 
D 4 HOH 57  457 105 HOH HOH A . 
D 4 HOH 58  458 82  HOH HOH A . 
D 4 HOH 59  459 46  HOH HOH A . 
D 4 HOH 60  460 12  HOH HOH A . 
D 4 HOH 61  461 66  HOH HOH A . 
D 4 HOH 62  462 69  HOH HOH A . 
D 4 HOH 63  463 85  HOH HOH A . 
D 4 HOH 64  464 39  HOH HOH A . 
D 4 HOH 65  465 97  HOH HOH A . 
D 4 HOH 66  466 34  HOH HOH A . 
D 4 HOH 67  467 27  HOH HOH A . 
D 4 HOH 68  468 108 HOH HOH A . 
D 4 HOH 69  469 30  HOH HOH A . 
D 4 HOH 70  470 87  HOH HOH A . 
D 4 HOH 71  471 49  HOH HOH A . 
D 4 HOH 72  472 67  HOH HOH A . 
D 4 HOH 73  473 64  HOH HOH A . 
D 4 HOH 74  474 21  HOH HOH A . 
D 4 HOH 75  475 86  HOH HOH A . 
D 4 HOH 76  476 37  HOH HOH A . 
D 4 HOH 77  477 92  HOH HOH A . 
D 4 HOH 78  478 56  HOH HOH A . 
D 4 HOH 79  479 59  HOH HOH A . 
D 4 HOH 80  480 29  HOH HOH A . 
D 4 HOH 81  481 83  HOH HOH A . 
D 4 HOH 82  482 53  HOH HOH A . 
D 4 HOH 83  483 90  HOH HOH A . 
D 4 HOH 84  484 77  HOH HOH A . 
D 4 HOH 85  485 112 HOH HOH A . 
D 4 HOH 86  486 100 HOH HOH A . 
D 4 HOH 87  487 48  HOH HOH A . 
D 4 HOH 88  488 60  HOH HOH A . 
D 4 HOH 89  489 93  HOH HOH A . 
D 4 HOH 90  490 36  HOH HOH A . 
D 4 HOH 91  491 99  HOH HOH A . 
D 4 HOH 92  492 78  HOH HOH A . 
D 4 HOH 93  493 73  HOH HOH A . 
D 4 HOH 94  494 75  HOH HOH A . 
D 4 HOH 95  495 52  HOH HOH A . 
D 4 HOH 96  496 71  HOH HOH A . 
D 4 HOH 97  497 81  HOH HOH A . 
D 4 HOH 98  498 51  HOH HOH A . 
D 4 HOH 99  499 101 HOH HOH A . 
D 4 HOH 100 500 63  HOH HOH A . 
D 4 HOH 101 501 94  HOH HOH A . 
D 4 HOH 102 502 116 HOH HOH A . 
D 4 HOH 103 503 115 HOH HOH A . 
D 4 HOH 104 504 119 HOH HOH A . 
D 4 HOH 105 505 109 HOH HOH A . 
D 4 HOH 106 506 61  HOH HOH A . 
D 4 HOH 107 507 95  HOH HOH A . 
D 4 HOH 108 508 88  HOH HOH A . 
D 4 HOH 109 509 70  HOH HOH A . 
D 4 HOH 110 510 45  HOH HOH A . 
D 4 HOH 111 511 106 HOH HOH A . 
D 4 HOH 112 512 84  HOH HOH A . 
D 4 HOH 113 513 35  HOH HOH A . 
D 4 HOH 114 514 28  HOH HOH A . 
D 4 HOH 115 515 110 HOH HOH A . 
D 4 HOH 116 516 98  HOH HOH A . 
D 4 HOH 117 517 113 HOH HOH A . 
D 4 HOH 118 518 96  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 MET 1   ? CG  ? A MET 1   CG  
2  1 Y 1 A MET 1   ? SD  ? A MET 1   SD  
3  1 Y 1 A MET 1   ? CE  ? A MET 1   CE  
4  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
5  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
6  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
7  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
8  1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
9  1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
10 1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
11 1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
12 1 Y 1 A LYS 108 ? CG  ? A LYS 108 CG  
13 1 Y 1 A LYS 108 ? CD  ? A LYS 108 CD  
14 1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
15 1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
16 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
17 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
18 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
19 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                     8QGI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.915 
_cell.length_a_esd                 ? 
_cell.length_b                     75.306 
_cell.length_b_esd                 ? 
_cell.length_c                     118.523 
_cell.length_c_esd                 ? 
_cell.volume                       561547.413 
_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                         8QGI 
_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                   8QGI 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.60 
_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 EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-11-19 
_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   0.967697 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.967697 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          34.30 
_reflns.entry_id                                       8QGI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.506 
_reflns.d_resolution_low                               63.561 
_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                                     39441 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.096 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.087 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.934 
_reflns_shell.d_res_low                                     1.968 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           7991 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1293 
_reflns_shell.percent_possible_obs                          9.7 
_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                               6.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.044 
_reflns_shell.pdbx_Rpim_I_all                               0.411 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.955 
_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                               45.86 
_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                                 8QGI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.93 
_refine.ls_d_res_low                             59.26 
_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                     39441 
_refine.ls_number_reflns_R_free                  1951 
_refine.ls_number_reflns_R_work                  37490 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.99 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1889 
_refine.ls_R_factor_R_free                       0.2140 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1876 
_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                          1.33 
_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                 25.7616 
_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                            0.1856 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.93 
_refine_hist.d_res_low                        59.26 
_refine_hist.number_atoms_solvent             118 
_refine_hist.number_atoms_total               2257 
_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        2071 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_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' ? 0.0034  ? 2212 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6337  ? 3000 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0499  ? 323  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0041  ? 417  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0108 ? 837  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.93 1.98  . . 139 2693 97.59 . . . . 0.2708 . . . . . . . . . . . 0.3046 
'X-RAY DIFFRACTION' 1.98 2.04  . . 143 2701 97.53 . . . . 0.2514 . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 2.04 2.10  . . 132 2702 97.99 . . . . 0.2346 . . . . . . . . . . . 0.2868 
'X-RAY DIFFRACTION' 2.10 2.16  . . 131 2700 97.86 . . . . 0.2221 . . . . . . . . . . . 0.2403 
'X-RAY DIFFRACTION' 2.16 2.24  . . 137 2680 97.27 . . . . 0.2170 . . . . . . . . . . . 0.2406 
'X-RAY DIFFRACTION' 2.24 2.33  . . 146 2684 95.48 . . . . 0.2170 . . . . . . . . . . . 0.2583 
'X-RAY DIFFRACTION' 2.33 2.44  . . 133 2657 97.89 . . . . 0.2077 . . . . . . . . . . . 0.2172 
'X-RAY DIFFRACTION' 2.44 2.57  . . 131 2736 98.08 . . . . 0.1984 . . . . . . . . . . . 0.2356 
'X-RAY DIFFRACTION' 2.57 2.73  . . 144 2690 97.93 . . . . 0.2026 . . . . . . . . . . . 0.2168 
'X-RAY DIFFRACTION' 2.73 2.94  . . 160 2651 97.13 . . . . 0.2061 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 2.94 3.23  . . 158 2667 97.55 . . . . 0.2016 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 3.23 3.70  . . 126 2702 96.75 . . . . 0.1682 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 3.70 4.66  . . 146 2651 96.38 . . . . 0.1508 . . . . . . . . . . . 0.1899 
'X-RAY DIFFRACTION' 4.66 59.26 . . 125 2576 92.75 . . . . 0.1771 . . . . . . . . . . . 0.1639 
# 
_struct.entry_id                     8QGI 
_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        8QGI 
_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              8QGI 
_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 8QGI LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGI GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGI HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGI HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGI HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGI HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGI HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGI 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 62.9150000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 62.9150000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 58  ? ILE A 62  ? ARG A 58  ILE A 62  5 ? 5  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 8 ? 
AA3 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 2 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA2 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA2 7 ALA A 178 ? SER A 186 ? ALA A 178 SER A 186 
AA2 8 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA3 2 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA3 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA3 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA3 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA3 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA3 7 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 8 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 9 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA2 3 4 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA2 6 7 N SER A 155 ? N SER A 155 O GLN A 180 ? O GLN A 180 
AA2 7 8 N MET A 179 ? N MET A 179 O PHE A 201 ? O PHE A 201 
AA3 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA3 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA3 3 4 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA3 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA3 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 6 7 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 7 8 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 8 9 N PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QGI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 109 ? ? -123.96 -155.53 
2 1 ASN A 122 ? ? -96.81  -69.33  
3 1 ALA A 162 ? ? -108.00 -129.14 
4 1 ASN A 189 ? ? -144.37 -155.53 
5 1 HIS A 204 ? ? 75.04   -0.48   
6 1 ASN A 213 ? ? -124.11 -78.50  
7 1 ASP A 222 ? ? 53.69   -124.61 
8 1 GLU A 233 ? ? -170.85 144.61  
9 1 GLU A 263 ? ? -179.71 147.23  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 448 ? D HOH . 
2 1 A HOH 507 ? D HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 12.6511918936 23.7345752156 23.1818346171  0.422201480928 ? 0.090675769713  ? 0.0237695454029   ? 
0.436888999359 ? -0.0909120986654 ? 0.355616772491 ? 2.30731495265 ? -0.352924192064 ? -1.48474092993  ? 1.00556157017 ? 
0.796917055344   ? 2.85541910735 ? -0.0412861868238 ? -0.42054032951  ? 0.179941048974  ? 0.0563064420605  ? 0.0874402272195  ? 
0.0426873789926 ? -0.264121995524  ? 0.19070063058   ? -0.033975796527   ? 
2 'X-RAY DIFFRACTION' ? refined 19.4514939807 13.3916239145 -4.44276359003 0.235853291877 ? 0.0281160848601 ? -0.00944229714763 ? 
0.248510713674 ? 0.0123673110306  ? 0.276029526295 ? 1.74757277389 ? -0.119468092479 ? -0.270013801647 ? 1.58189590856 ? 
-0.0602125261298 ? 2.31037858723 ? 0.0505462133356  ? 0.122050064821  ? 0.0999346751933 ? -0.0801306008138 ? -0.03573678418   ? 
0.209784671911  ? -0.0167382439963 ? -0.273997646631 ? -0.00299665462013 ? 
3 'X-RAY DIFFRACTION' ? refined 19.0746003892 17.0459385078 7.29156018965  0.298704515197 ? 0.0290031591158 ? 0.0454333608558   ? 
0.301881675327 ? -0.0361257488433 ? 0.33505241491  ? 1.72218776878 ? -0.218297603844 ? 0.153475519721  ? 1.59655976431 ? 
-0.126744860816  ? 2.079521444   ? 0.0376557917905  ? -0.129069723676 ? 0.20984041814   ? 0.0721137598921  ? -0.0179579558536 ? 
0.196541397506  ? -0.184749968315  ? -0.254901234752 ? -0.0150183706432  ? 
# 
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 92  A 92  ? ? 
;chain 'A' and (resid    1  through   92 )
;
2 'X-RAY DIFFRACTION' 2 A 93  A 93  ? A 213 A 216 ? ? 
;chain 'A' and (resid   93  through  216 )
;
3 'X-RAY DIFFRACTION' 3 A 214 A 217 ? A 261 A 264 ? ? 
;chain 'A' and (resid  217  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 
UZO N1   N N N 393 
UZO C7   C Y N 394 
UZO C8   C Y N 395 
UZO N2   N Y N 396 
UZO C9   C Y N 397 
UZO O1   O N N 398 
UZO C1   C N N 399 
UZO O5   O N N 400 
UZO C5   C N N 401 
UZO C6   C Y N 402 
UZO N3   N N N 403 
UZO C4   C N N 404 
UZO O4   O N N 405 
UZO C3   C N N 406 
UZO O3   O N N 407 
UZO C2   C N N 408 
UZO N4   N Y N 409 
UZO N    N N N 410 
UZO C    C N N 411 
UZO O    O N N 412 
UZO C10  C Y N 413 
UZO C11  C N S 414 
UZO C12  C N R 415 
UZO C13  C N N 416 
UZO C14  C N N 417 
UZO C15  C N N 418 
UZO C16  C Y N 419 
UZO C17  C Y N 420 
UZO C18  C Y N 421 
UZO C19  C Y N 422 
UZO C20  C Y N 423 
UZO C21  C Y N 424 
UZO C22  C N S 425 
UZO C23  C N R 426 
UZO C24  C N N 427 
UZO C25  C N S 428 
UZO C26  C N S 429 
UZO C27  C N R 430 
UZO C28  C N S 431 
UZO C29  C Y N 432 
UZO C30  C Y N 433 
UZO C31  C Y N 434 
UZO C32  C Y N 435 
UZO C33  C Y N 436 
UZO N10  N Y N 437 
UZO N11  N N N 438 
UZO N12  N Y N 439 
UZO N13  N Y N 440 
UZO N5   N Y N 441 
UZO N6   N Y N 442 
UZO N7   N N N 443 
UZO N8   N N N 444 
UZO N9   N Y N 445 
UZO O2   O N N 446 
UZO O6   O N N 447 
UZO H20  H N N 448 
UZO H13  H N N 449 
UZO H12  H N N 450 
UZO H36  H N N 451 
UZO H18  H N N 452 
UZO H19  H N N 453 
UZO H17  H N N 454 
UZO H16  H N N 455 
UZO H33  H N N 456 
UZO H14  H N N 457 
UZO H15  H N N 458 
UZO H8   H N N 459 
UZO H43  H N N 460 
UZO H11  H N N 461 
UZO H10  H N N 462 
UZO H    H N N 463 
UZO H1   H N N 464 
UZO H22  H N N 465 
UZO H21  H N N 466 
UZO H26  H N N 467 
UZO H25  H N N 468 
UZO H27  H N N 469 
UZO H28  H N N 470 
UZO H29  H N N 471 
UZO H30  H N N 472 
UZO H31  H N N 473 
UZO H2   H N N 474 
UZO H3   H N N 475 
UZO H35  H N N 476 
UZO H34  H N N 477 
UZO H4   H N N 478 
UZO H5   H N N 479 
UZO H6   H N N 480 
UZO H7   H N N 481 
UZO H38  H N N 482 
UZO H41  H N N 483 
UZO H39  H N N 484 
UZO H40  H N N 485 
UZO H23  H N N 486 
UZO H24  H N N 487 
UZO H32  H N N 488 
UZO H37  H N N 489 
VAL N    N N N 490 
VAL CA   C N S 491 
VAL C    C N N 492 
VAL O    O N N 493 
VAL CB   C N N 494 
VAL CG1  C N N 495 
VAL CG2  C N N 496 
VAL OXT  O N N 497 
VAL H    H N N 498 
VAL H2   H N N 499 
VAL HA   H N N 500 
VAL HB   H N N 501 
VAL HG11 H N N 502 
VAL HG12 H N N 503 
VAL HG13 H N N 504 
VAL HG21 H N N 505 
VAL HG22 H N N 506 
VAL HG23 H N N 507 
VAL HXT  H N N 508 
# 
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 
UZO N   C    sing N N 378 
UZO C   C1   sing N N 379 
UZO C1  C2   sing N N 380 
UZO C2  N1   sing N N 381 
UZO N1  C3   sing N N 382 
UZO C3  C4   sing N N 383 
UZO C4  C5   trip N N 384 
UZO C5  C6   sing N N 385 
UZO C6  N2   doub Y N 386 
UZO N2  C7   sing Y N 387 
UZO C7  C8   doub Y N 388 
UZO N3  C8   sing N N 389 
UZO C8  N4   sing Y N 390 
UZO N4  C9   doub Y N 391 
UZO C9  N5   sing Y N 392 
UZO N5  C10  doub Y N 393 
UZO C7  C10  sing Y N 394 
UZO C10 N6   sing Y N 395 
UZO C6  N6   sing Y N 396 
UZO N6  C11  sing N N 397 
UZO C11 O    sing N N 398 
UZO O   C12  sing N N 399 
UZO C12 C13  sing N N 400 
UZO C13 N7   sing N N 401 
UZO N7  C14  sing N N 402 
UZO C14 O1   doub N N 403 
UZO N8  C14  sing N N 404 
UZO C15 N8   sing N N 405 
UZO C16 C15  sing N N 406 
UZO C16 C17  doub Y N 407 
UZO C17 C18  sing Y N 408 
UZO C18 C19  doub Y N 409 
UZO C19 C20  sing Y N 410 
UZO C20 C21  doub Y N 411 
UZO C21 C16  sing Y N 412 
UZO C22 C12  sing N N 413 
UZO O2  C22  sing N N 414 
UZO C23 C22  sing N N 415 
UZO C11 C23  sing N N 416 
UZO O3  C23  sing N N 417 
UZO C24 N1   sing N N 418 
UZO C25 C24  sing N N 419 
UZO C25 O4   sing N N 420 
UZO O4  C26  sing N N 421 
UZO C26 C27  sing N N 422 
UZO O5  C27  sing N N 423 
UZO C27 C28  sing N N 424 
UZO C28 C25  sing N N 425 
UZO O6  C28  sing N N 426 
UZO N9  C26  sing N N 427 
UZO N9  C29  sing Y N 428 
UZO C29 N10  doub Y N 429 
UZO N10 C30  sing Y N 430 
UZO C30 C31  doub Y N 431 
UZO N11 C31  sing N N 432 
UZO C31 N12  sing Y N 433 
UZO N12 C32  doub Y N 434 
UZO C32 N13  sing Y N 435 
UZO N13 C33  doub Y N 436 
UZO C33 N9   sing Y N 437 
UZO C30 C33  sing Y N 438 
UZO C9  H20  sing N N 439 
UZO C1  H13  sing N N 440 
UZO C1  H12  sing N N 441 
UZO O5  H36  sing N N 442 
UZO N3  H18  sing N N 443 
UZO N3  H19  sing N N 444 
UZO C3  H17  sing N N 445 
UZO C3  H16  sing N N 446 
UZO O3  H33  sing N N 447 
UZO C2  H14  sing N N 448 
UZO C2  H15  sing N N 449 
UZO N   H8   sing N N 450 
UZO N   H43  sing N N 451 
UZO C   H11  sing N N 452 
UZO C   H10  sing N N 453 
UZO C11 H    sing N N 454 
UZO C12 H1   sing N N 455 
UZO C13 H22  sing N N 456 
UZO C13 H21  sing N N 457 
UZO C15 H26  sing N N 458 
UZO C15 H25  sing N N 459 
UZO C17 H27  sing N N 460 
UZO C18 H28  sing N N 461 
UZO C19 H29  sing N N 462 
UZO C20 H30  sing N N 463 
UZO C21 H31  sing N N 464 
UZO C22 H2   sing N N 465 
UZO C23 H3   sing N N 466 
UZO C24 H35  sing N N 467 
UZO C24 H34  sing N N 468 
UZO C25 H4   sing N N 469 
UZO C26 H5   sing N N 470 
UZO C27 H6   sing N N 471 
UZO C28 H7   sing N N 472 
UZO C29 H38  sing N N 473 
UZO C32 H41  sing N N 474 
UZO N11 H39  sing N N 475 
UZO N11 H40  sing N N 476 
UZO N7  H23  sing N N 477 
UZO N8  H24  sing N N 478 
UZO O2  H32  sing N N 479 
UZO O6  H37  sing N N 480 
VAL N   CA   sing N N 481 
VAL N   H    sing N N 482 
VAL N   H2   sing N N 483 
VAL CA  C    sing N N 484 
VAL CA  CB   sing N N 485 
VAL CA  HA   sing N N 486 
VAL C   O    doub N N 487 
VAL C   OXT  sing N N 488 
VAL CB  CG1  sing N N 489 
VAL CB  CG2  sing N N 490 
VAL CB  HB   sing N N 491 
VAL CG1 HG11 sing N N 492 
VAL CG1 HG12 sing N N 493 
VAL CG1 HG13 sing N N 494 
VAL CG2 HG21 sing N N 495 
VAL CG2 HG22 sing N N 496 
VAL CG2 HG23 sing N N 497 
VAL OXT HXT  sing N N 498 
# 
_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                    8QGI 
_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]   0.015894 
_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]   0.013279 
_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]   0.008437 
_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   ? 12.07558 36.02237 24.25227  1.000 76.94653  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.76451 36.65925 24.17694  1.000 77.37833  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.65776  35.60918 24.12948  1.000 71.10301  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.34706  34.97544 25.14210  1.000 65.94166  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 10.67748 37.57398 22.94996  1.000 85.50254  ? 1   MET A CB  1 
ATOM   6    N N   . LYS A 1 2   ? 9.05451  35.44067 22.96087  1.000 64.83287  ? 2   LYS A N   1 
ATOM   7    C CA  . LYS A 1 2   ? 8.08508  34.37724 22.75681  1.000 59.50593  ? 2   LYS A CA  1 
ATOM   8    C C   . LYS A 1 2   ? 8.81726  33.06013 22.53655  1.000 54.98210  ? 2   LYS A C   1 
ATOM   9    O O   . LYS A 1 2   ? 9.83633  33.01228 21.84400  1.000 53.99012  ? 2   LYS A O   1 
ATOM   10   C CB  . LYS A 1 2   ? 7.17888  34.69169 21.56803  1.000 59.76307  ? 2   LYS A CB  1 
ATOM   11   C CG  . LYS A 1 2   ? 6.43244  36.01320 21.70168  1.000 62.21956  ? 2   LYS A CG  1 
ATOM   12   C CD  . LYS A 1 2   ? 5.18848  36.05354 20.82536  1.000 62.60108  ? 2   LYS A CD  1 
ATOM   13   C CE  . LYS A 1 2   ? 4.30854  37.24239 21.18270  1.000 65.92473  ? 2   LYS A CE  1 
ATOM   14   N NZ  . LYS A 1 2   ? 2.87416  36.96612 20.89430  1.000 68.97769  ? 2   LYS A NZ  1 
ATOM   15   N N   . TYR A 1 3   ? 8.29750  31.99159 23.13775  1.000 50.95639  ? 3   TYR A N   1 
ATOM   16   C CA  . TYR A 1 3   ? 8.93321  30.68857 23.05860  1.000 48.55644  ? 3   TYR A CA  1 
ATOM   17   C C   . TYR A 1 3   ? 7.86063  29.61463 23.13220  1.000 47.31561  ? 3   TYR A C   1 
ATOM   18   O O   . TYR A 1 3   ? 6.75060  29.84946 23.61589  1.000 47.12960  ? 3   TYR A O   1 
ATOM   19   C CB  . TYR A 1 3   ? 9.95643  30.48526 24.18698  1.000 47.86538  ? 3   TYR A CB  1 
ATOM   20   C CG  . TYR A 1 3   ? 9.31834  30.10135 25.50897  1.000 48.14658  ? 3   TYR A CG  1 
ATOM   21   C CD1 . TYR A 1 3   ? 8.75437  31.06348 26.33779  1.000 51.46454  ? 3   TYR A CD1 1 
ATOM   22   C CD2 . TYR A 1 3   ? 9.27620  28.77507 25.92145  1.000 45.75488  ? 3   TYR A CD2 1 
ATOM   23   C CE1 . TYR A 1 3   ? 8.16666  30.71564 27.54422  1.000 50.65234  ? 3   TYR A CE1 1 
ATOM   24   C CE2 . TYR A 1 3   ? 8.68793  28.41593 27.11864  1.000 46.55999  ? 3   TYR A CE2 1 
ATOM   25   C CZ  . TYR A 1 3   ? 8.13570  29.39010 27.92641  1.000 48.34275  ? 3   TYR A CZ  1 
ATOM   26   O OH  . TYR A 1 3   ? 7.55208  29.03067 29.11576  1.000 47.17681  ? 3   TYR A OH  1 
ATOM   27   N N   . MET A 1 4   ? 8.20794  28.42257 22.65300  1.000 43.76590  ? 4   MET A N   1 
ATOM   28   C CA  . MET A 1 4   ? 7.37499  27.25050 22.86070  1.000 43.30823  ? 4   MET A CA  1 
ATOM   29   C C   . MET A 1 4   ? 8.28285  26.04724 23.06101  1.000 41.09657  ? 4   MET A C   1 
ATOM   30   O O   . MET A 1 4   ? 9.48683  26.09891 22.80264  1.000 39.27994  ? 4   MET A O   1 
ATOM   31   C CB  . MET A 1 4   ? 6.39201  27.03605 21.70046  1.000 46.14893  ? 4   MET A CB  1 
ATOM   32   C CG  . MET A 1 4   ? 7.02842  26.63754 20.38404  1.000 43.78802  ? 4   MET A CG  1 
ATOM   33   S SD  . MET A 1 4   ? 7.21439  24.85216 20.22991  1.000 46.63831  ? 4   MET A SD  1 
ATOM   34   C CE  . MET A 1 4   ? 5.53512  24.32206 20.56565  1.000 47.26914  ? 4   MET A CE  1 
ATOM   35   N N   . ILE A 1 5   ? 7.69823  24.95729 23.55240  1.000 40.27779  ? 5   ILE A N   1 
ATOM   36   C CA  . ILE A 1 5   ? 8.44252  23.73240 23.82339  1.000 39.25407  ? 5   ILE A CA  1 
ATOM   37   C C   . ILE A 1 5   ? 7.61789  22.55599 23.32094  1.000 40.78679  ? 5   ILE A C   1 
ATOM   38   O O   . ILE A 1 5   ? 6.45720  22.39827 23.71504  1.000 38.23862  ? 5   ILE A O   1 
ATOM   39   C CB  . ILE A 1 5   ? 8.75872  23.55929 25.32178  1.000 39.84847  ? 5   ILE A CB  1 
ATOM   40   C CG1 . ILE A 1 5   ? 9.44588  24.80609 25.88399  1.000 36.10878  ? 5   ILE A CG1 1 
ATOM   41   C CG2 . ILE A 1 5   ? 9.63066  22.33256 25.54268  1.000 37.53068  ? 5   ILE A CG2 1 
ATOM   42   C CD1 . ILE A 1 5   ? 9.83959  24.68149 27.35313  1.000 42.87912  ? 5   ILE A CD1 1 
ATOM   43   N N   . THR A 1 6   ? 8.20459  21.73896 22.44941  1.000 38.16521  ? 6   THR A N   1 
ATOM   44   C CA  . THR A 1 6   ? 7.59485  20.48315 22.03830  1.000 39.50907  ? 6   THR A CA  1 
ATOM   45   C C   . THR A 1 6   ? 8.18034  19.34828 22.86481  1.000 39.43376  ? 6   THR A C   1 
ATOM   46   O O   . THR A 1 6   ? 9.31633  19.42609 23.34046  1.000 41.83436  ? 6   THR A O   1 
ATOM   47   C CB  . THR A 1 6   ? 7.81495  20.19600 20.54392  1.000 41.07755  ? 6   THR A CB  1 
ATOM   48   O OG1 . THR A 1 6   ? 9.21683  20.08689 20.27005  1.000 39.42223  ? 6   THR A OG1 1 
ATOM   49   C CG2 . THR A 1 6   ? 7.22696  21.29093 19.68059  1.000 43.93232  ? 6   THR A CG2 1 
ATOM   50   N N   . SER A 1 7   ? 7.39522  18.28894 23.03206  1.000 39.45868  ? 7   SER A N   1 
ATOM   51   C CA  . SER A 1 7   ? 7.80658  17.14220 23.82353  1.000 42.29650  ? 7   SER A CA  1 
ATOM   52   C C   . SER A 1 7   ? 7.63650  15.86103 23.02086  1.000 43.90931  ? 7   SER A C   1 
ATOM   53   O O   . SER A 1 7   ? 6.71265  15.73014 22.21436  1.000 44.40198  ? 7   SER A O   1 
ATOM   54   C CB  . SER A 1 7   ? 7.00462  17.04142 25.13201  1.000 44.62483  ? 7   SER A CB  1 
ATOM   55   O OG  . SER A 1 7   ? 7.31572  15.84759 25.82860  1.000 46.07127  ? 7   SER A OG  1 
ATOM   56   N N   . LYS A 1 8   ? 8.54794  14.91371 23.25893  1.000 43.43466  ? 8   LYS A N   1 
ATOM   57   C CA  . LYS A 1 8   ? 8.40103  13.57277 22.70422  1.000 46.58966  ? 8   LYS A CA  1 
ATOM   58   C C   . LYS A 1 8   ? 7.12101  12.90375 23.19288  1.000 49.28059  ? 8   LYS A C   1 
ATOM   59   O O   . LYS A 1 8   ? 6.55548  12.05205 22.49574  1.000 53.58344  ? 8   LYS A O   1 
ATOM   60   C CB  . LYS A 1 8   ? 9.62263  12.72780 23.06837  1.000 48.44378  ? 8   LYS A CB  1 
ATOM   61   C CG  . LYS A 1 8   ? 9.56031  11.29560 22.59587  1.000 52.13882  ? 8   LYS A CG  1 
ATOM   62   C CD  . LYS A 1 8   ? 10.68651 10.47796 23.19635  1.000 55.90386  ? 8   LYS A CD  1 
ATOM   63   C CE  . LYS A 1 8   ? 10.72519 9.10024  22.56495  1.000 59.97813  ? 8   LYS A CE  1 
ATOM   64   N NZ  . LYS A 1 8   ? 10.67637 9.20111  21.07862  1.000 62.30403  ? 8   LYS A NZ  1 
ATOM   65   N N   . GLY A 1 9   ? 6.65063  13.26756 24.38060  1.000 49.87049  ? 9   GLY A N   1 
ATOM   66   C CA  . GLY A 1 9   ? 5.37957  12.79291 24.87962  1.000 50.66815  ? 9   GLY A CA  1 
ATOM   67   C C   . GLY A 1 9   ? 5.46465  11.68768 25.90877  1.000 52.40864  ? 9   GLY A C   1 
ATOM   68   O O   . GLY A 1 9   ? 4.42440  11.28568 26.44548  1.000 55.99834  ? 9   GLY A O   1 
ATOM   69   N N   . ASP A 1 10  ? 6.65694  11.17292 26.18829  1.000 51.94136  ? 10  ASP A N   1 
ATOM   70   C CA  . ASP A 1 10  ? 6.81767  10.26988 27.31434  1.000 56.28668  ? 10  ASP A CA  1 
ATOM   71   C C   . ASP A 1 10  ? 6.86121  11.07168 28.61313  1.000 56.08918  ? 10  ASP A C   1 
ATOM   72   O O   . ASP A 1 10  ? 6.87965  12.30593 28.61049  1.000 54.06300  ? 10  ASP A O   1 
ATOM   73   C CB  . ASP A 1 10  ? 8.07903  9.42031  27.15400  1.000 58.46301  ? 10  ASP A CB  1 
ATOM   74   C CG  . ASP A 1 10  ? 9.34404  10.25367 27.10297  1.000 58.47275  ? 10  ASP A CG  1 
ATOM   75   O OD1 . ASP A 1 10  ? 9.26321  11.43284 26.70516  1.000 55.30472  ? 10  ASP A OD1 1 
ATOM   76   O OD2 . ASP A 1 10  ? 10.41995 9.72947  27.45753  1.000 65.49394  ? 10  ASP A OD2 1 
ATOM   77   N N   . GLU A 1 11  ? 6.87195  10.35312 29.73918  1.000 58.40241  ? 11  GLU A N   1 
ATOM   78   C CA  . GLU A 1 11  ? 6.82406  11.01740 31.03933  1.000 60.40462  ? 11  GLU A CA  1 
ATOM   79   C C   . GLU A 1 11  ? 8.03730  11.91574 31.24852  1.000 58.31122  ? 11  GLU A C   1 
ATOM   80   O O   . GLU A 1 11  ? 7.90617  13.05495 31.70849  1.000 57.98057  ? 11  GLU A O   1 
ATOM   81   C CB  . GLU A 1 11  ? 6.72439  9.98299  32.16276  1.000 65.44067  ? 11  GLU A CB  1 
ATOM   82   C CG  . GLU A 1 11  ? 5.36128  9.32611  32.29497  0.800 69.10835  ? 11  GLU A CG  1 
ATOM   83   C CD  . GLU A 1 11  ? 5.23193  8.50453  33.56453  0.600 71.70973  ? 11  GLU A CD  1 
ATOM   84   O OE1 . GLU A 1 11  ? 6.16882  8.52874  34.39150  0.600 72.24229  ? 11  GLU A OE1 1 
ATOM   85   O OE2 . GLU A 1 11  ? 4.19215  7.83514  33.73542  0.600 71.93558  ? 11  GLU A OE2 1 
ATOM   86   N N   . LYS A 1 12  ? 9.22939  11.41986 30.91247  1.000 58.14866  ? 12  LYS A N   1 
ATOM   87   C CA  . LYS A 1 12  ? 10.44814 12.18676 31.15533  1.000 57.33121  ? 12  LYS A CA  1 
ATOM   88   C C   . LYS A 1 12  ? 10.41465 13.52837 30.42997  1.000 53.70025  ? 12  LYS A C   1 
ATOM   89   O O   . LYS A 1 12  ? 10.74682 14.56960 31.00865  1.000 47.94337  ? 12  LYS A O   1 
ATOM   90   C CB  . LYS A 1 12  ? 11.67065 11.37147 30.72900  1.000 60.28930  ? 12  LYS A CB  1 
ATOM   91   C CG  . LYS A 1 12  ? 12.99858 12.03585 31.05366  1.000 65.77879  ? 12  LYS A CG  1 
ATOM   92   C CD  . LYS A 1 12  ? 14.17591 11.14001 30.70551  1.000 62.71512  ? 12  LYS A CD  1 
ATOM   93   C CE  . LYS A 1 12  ? 15.50176 11.80562 31.06012  1.000 61.59135  ? 12  LYS A CE  1 
ATOM   94   N NZ  . LYS A 1 12  ? 15.58987 12.14935 32.50759  1.000 68.40537  ? 12  LYS A NZ  1 
ATOM   95   N N   . SER A 1 13  ? 9.99514  13.52625 29.16313  1.000 53.92155  ? 13  SER A N   1 
ATOM   96   C CA  . SER A 1 13  ? 10.03892 14.74732 28.36518  1.000 50.63212  ? 13  SER A CA  1 
ATOM   97   C C   . SER A 1 13  ? 8.91798  15.71212 28.73329  1.000 48.99535  ? 13  SER A C   1 
ATOM   98   O O   . SER A 1 13  ? 9.12400  16.93095 28.73229  1.000 46.21710  ? 13  SER A O   1 
ATOM   99   C CB  . SER A 1 13  ? 9.97835  14.40096 26.87847  1.000 48.38288  ? 13  SER A CB  1 
ATOM   100  O OG  . SER A 1 13  ? 11.00954 13.48754 26.53376  1.000 48.07777  ? 13  SER A OG  1 
ATOM   101  N N   . ASP A 1 14  ? 7.72526  15.19437 29.03881  1.000 49.78426  ? 14  ASP A N   1 
ATOM   102  C CA  . ASP A 1 14  ? 6.63194  16.07233 29.44563  1.000 50.14129  ? 14  ASP A CA  1 
ATOM   103  C C   . ASP A 1 14  ? 6.97038  16.81189 30.73113  1.000 48.78404  ? 14  ASP A C   1 
ATOM   104  O O   . ASP A 1 14  ? 6.68136  18.00786 30.86711  1.000 45.84678  ? 14  ASP A O   1 
ATOM   105  C CB  . ASP A 1 14  ? 5.34470  15.27015 29.62490  1.000 51.28376  ? 14  ASP A CB  1 
ATOM   106  C CG  . ASP A 1 14  ? 4.69453  14.91565 28.31086  1.000 51.22588  ? 14  ASP A CG  1 
ATOM   107  O OD1 . ASP A 1 14  ? 5.21684  15.33584 27.25643  1.000 49.49084  ? 14  ASP A OD1 1 
ATOM   108  O OD2 . ASP A 1 14  ? 3.65730  14.22153 28.33554  1.000 52.97223  ? 14  ASP A OD2 1 
ATOM   109  N N   . LEU A 1 15  ? 7.58004  16.11645 31.68881  1.000 50.14697  ? 15  LEU A N   1 
ATOM   110  C CA  . LEU A 1 15  ? 7.86758  16.74915 32.96817  1.000 50.82489  ? 15  LEU A CA  1 
ATOM   111  C C   . LEU A 1 15  ? 9.02576  17.73034 32.85368  1.000 47.89252  ? 15  LEU A C   1 
ATOM   112  O O   . LEU A 1 15  ? 8.99478  18.80037 33.47058  1.000 43.69567  ? 15  LEU A O   1 
ATOM   113  C CB  . LEU A 1 15  ? 8.14409  15.68639 34.03068  1.000 53.55501  ? 15  LEU A CB  1 
ATOM   114  C CG  . LEU A 1 15  ? 6.87505  15.24091 34.77079  1.000 63.09008  ? 15  LEU A CG  1 
ATOM   115  C CD1 . LEU A 1 15  ? 6.11210  14.15923 34.00615  1.000 63.72801  ? 15  LEU A CD1 1 
ATOM   116  C CD2 . LEU A 1 15  ? 7.19329  14.79280 36.18670  1.000 62.21698  ? 15  LEU A CD2 1 
ATOM   117  N N   . LEU A 1 16  ? 10.04333 17.39817 32.05903  1.000 45.85855  ? 16  LEU A N   1 
ATOM   118  C CA  . LEU A 1 16  ? 11.09284 18.37352 31.78828  1.000 44.83813  ? 16  LEU A CA  1 
ATOM   119  C C   . LEU A 1 16  ? 10.51126 19.62119 31.13401  1.000 43.19726  ? 16  LEU A C   1 
ATOM   120  O O   . LEU A 1 16  ? 10.89389 20.74738 31.47441  1.000 41.32188  ? 16  LEU A O   1 
ATOM   121  C CB  . LEU A 1 16  ? 12.17725 17.75063 30.90915  1.000 43.84566  ? 16  LEU A CB  1 
ATOM   122  C CG  . LEU A 1 16  ? 13.45069 18.57817 30.73183  1.000 43.85157  ? 16  LEU A CG  1 
ATOM   123  C CD1 . LEU A 1 16  ? 14.00096 19.00291 32.09199  1.000 45.55763  ? 16  LEU A CD1 1 
ATOM   124  C CD2 . LEU A 1 16  ? 14.49390 17.79333 29.95341  1.000 45.22775  ? 16  LEU A CD2 1 
ATOM   125  N N   . ARG A 1 17  ? 9.55896  19.43836 30.21465  1.000 43.72269  ? 17  ARG A N   1 
ATOM   126  C CA  . ARG A 1 17  ? 8.91291  20.57704 29.56939  1.000 42.96772  ? 17  ARG A CA  1 
ATOM   127  C C   . ARG A 1 17  ? 8.18856  21.45415 30.58750  1.000 42.45193  ? 17  ARG A C   1 
ATOM   128  O O   . ARG A 1 17  ? 8.34023  22.68117 30.58402  1.000 41.31364  ? 17  ARG A O   1 
ATOM   129  C CB  . ARG A 1 17  ? 7.94494  20.08631 28.49310  1.000 40.37340  ? 17  ARG A CB  1 
ATOM   130  C CG  . ARG A 1 17  ? 7.04547  21.17562 27.93917  1.000 41.74903  ? 17  ARG A CG  1 
ATOM   131  C CD  . ARG A 1 17  ? 6.23136  20.67162 26.75106  1.000 39.18855  ? 17  ARG A CD  1 
ATOM   132  N NE  . ARG A 1 17  ? 5.34118  21.70172 26.23053  1.000 38.88311  ? 17  ARG A NE  1 
ATOM   133  C CZ  . ARG A 1 17  ? 4.16850  22.01305 26.76362  1.000 44.13731  ? 17  ARG A CZ  1 
ATOM   134  N NH1 . ARG A 1 17  ? 3.71835  21.40157 27.84845  1.000 41.93780  ? 17  ARG A NH1 1 
ATOM   135  N NH2 . ARG A 1 17  ? 3.43142  22.96550 26.19894  1.000 44.80457  ? 17  ARG A NH2 1 
ATOM   136  N N   . LEU A 1 18  ? 7.39383  20.84215 31.47027  1.000 43.07997  ? 18  LEU A N   1 
ATOM   137  C CA  . LEU A 1 18  ? 6.66583  21.62702 32.46723  1.000 44.91017  ? 18  LEU A CA  1 
ATOM   138  C C   . LEU A 1 18  ? 7.61988  22.35569 33.40651  1.000 41.97371  ? 18  LEU A C   1 
ATOM   139  O O   . LEU A 1 18  ? 7.35334  23.49225 33.81610  1.000 41.84699  ? 18  LEU A O   1 
ATOM   140  C CB  . LEU A 1 18  ? 5.71855  20.73145 33.26602  1.000 45.89655  ? 18  LEU A CB  1 
ATOM   141  C CG  . LEU A 1 18  ? 4.47820  20.17132 32.57008  1.000 48.08665  ? 18  LEU A CG  1 
ATOM   142  C CD1 . LEU A 1 18  ? 3.58465  19.48437 33.59613  1.000 47.38909  ? 18  LEU A CD1 1 
ATOM   143  C CD2 . LEU A 1 18  ? 3.72421  21.27202 31.83983  1.000 46.41599  ? 18  LEU A CD2 1 
ATOM   144  N N   . ASN A 1 19  ? 8.73588  21.71775 33.76015  1.000 43.43085  ? 19  ASN A N   1 
ATOM   145  C CA  . ASN A 1 19  ? 9.69737  22.35404 34.65447  1.000 42.72355  ? 19  ASN A CA  1 
ATOM   146  C C   . ASN A 1 19  ? 10.37149 23.54868 33.99178  1.000 42.83607  ? 19  ASN A C   1 
ATOM   147  O O   . ASN A 1 19  ? 10.62687 24.56535 34.64857  1.000 42.20207  ? 19  ASN A O   1 
ATOM   148  C CB  . ASN A 1 19  ? 10.74027 21.33933 35.11357  1.000 42.37217  ? 19  ASN A CB  1 
ATOM   149  C CG  . ASN A 1 19  ? 10.40845 20.74053 36.46059  1.000 44.55350  ? 19  ASN A CG  1 
ATOM   150  O OD1 . ASN A 1 19  ? 9.54336  21.24658 37.18415  1.000 43.44275  ? 19  ASN A OD1 1 
ATOM   151  N ND2 . ASN A 1 19  ? 11.10627 19.66860 36.81923  1.000 45.98222  ? 19  ASN A ND2 1 
ATOM   152  N N   . MET A 1 20  ? 10.66868 23.45024 32.69383  1.000 40.02888  ? 20  MET A N   1 
ATOM   153  C CA  . MET A 1 20  ? 11.27080 24.58586 32.00379  1.000 41.20485  ? 20  MET A CA  1 
ATOM   154  C C   . MET A 1 20  ? 10.27421 25.72867 31.86263  1.000 41.74919  ? 20  MET A C   1 
ATOM   155  O O   . MET A 1 20  ? 10.64417 26.90081 31.99946  1.000 44.02086  ? 20  MET A O   1 
ATOM   156  C CB  . MET A 1 20  ? 11.80678 24.15521 30.63607  1.000 42.28811  ? 20  MET A CB  1 
ATOM   157  C CG  . MET A 1 20  ? 13.03259 23.25611 30.71294  1.000 42.12470  ? 20  MET A CG  1 
ATOM   158  S SD  . MET A 1 20  ? 13.72843 22.85911 29.09360  1.000 42.40513  ? 20  MET A SD  1 
ATOM   159  C CE  . MET A 1 20  ? 14.61123 24.36884 28.70426  1.000 45.20300  ? 20  MET A CE  1 
ATOM   160  N N   . ILE A 1 21  ? 9.00346  25.40651 31.60125  1.000 42.28442  ? 21  ILE A N   1 
ATOM   161  C CA  . ILE A 1 21  ? 7.96856  26.43532 31.54987  1.000 43.87608  ? 21  ILE A CA  1 
ATOM   162  C C   . ILE A 1 21  ? 7.85935  27.14481 32.89166  1.000 43.52398  ? 21  ILE A C   1 
ATOM   163  O O   . ILE A 1 21  ? 7.78046  28.37786 32.95500  1.000 43.47118  ? 21  ILE A O   1 
ATOM   164  C CB  . ILE A 1 21  ? 6.62173  25.82271 31.12647  1.000 43.49113  ? 21  ILE A CB  1 
ATOM   165  C CG1 . ILE A 1 21  ? 6.69521  25.30598 29.68931  1.000 43.42224  ? 21  ILE A CG1 1 
ATOM   166  C CG2 . ILE A 1 21  ? 5.50771  26.84541 31.27911  1.000 43.99640  ? 21  ILE A CG2 1 
ATOM   167  C CD1 . ILE A 1 21  ? 5.42981  24.61930 29.23265  1.000 44.30001  ? 21  ILE A CD1 1 
ATOM   168  N N   . ALA A 1 22  ? 7.84785  26.38065 33.98496  1.000 43.70157  ? 22  ALA A N   1 
ATOM   169  C CA  . ALA A 1 22  ? 7.82393  27.00194 35.30369  1.000 45.40268  ? 22  ALA A CA  1 
ATOM   170  C C   . ALA A 1 22  ? 9.05597  27.87147 35.51225  1.000 45.68355  ? 22  ALA A C   1 
ATOM   171  O O   . ALA A 1 22  ? 8.95370  28.99841 36.00963  1.000 47.61863  ? 22  ALA A O   1 
ATOM   172  C CB  . ALA A 1 22  ? 7.71963  25.93117 36.39016  1.000 43.44768  ? 22  ALA A CB  1 
ATOM   173  N N   . GLY A 1 23  ? 10.22793 27.37618 35.11313  1.000 45.93521  ? 23  GLY A N   1 
ATOM   174  C CA  . GLY A 1 23  ? 11.43401 28.17756 35.24293  1.000 45.86653  ? 23  GLY A CA  1 
ATOM   175  C C   . GLY A 1 23  ? 11.40221 29.41261 34.36439  1.000 49.78476  ? 23  GLY A C   1 
ATOM   176  O O   . GLY A 1 23  ? 11.87663 30.48146 34.76139  1.000 50.36913  ? 23  GLY A O   1 
ATOM   177  N N   . PHE A 1 24  ? 10.83866 29.28435 33.16034  1.000 46.03124  ? 24  PHE A N   1 
ATOM   178  C CA  . PHE A 1 24  ? 10.69311 30.43737 32.27772  1.000 49.31486  ? 24  PHE A CA  1 
ATOM   179  C C   . PHE A 1 24  ? 9.73258  31.47106 32.85059  1.000 51.12421  ? 24  PHE A C   1 
ATOM   180  O O   . PHE A 1 24  ? 9.88648  32.66964 32.58914  1.000 54.54705  ? 24  PHE A O   1 
ATOM   181  C CB  . PHE A 1 24  ? 10.21638 29.98512 30.89854  1.000 46.68246  ? 24  PHE A CB  1 
ATOM   182  C CG  . PHE A 1 24  ? 11.32991 29.60473 29.96614  1.000 49.47232  ? 24  PHE A CG  1 
ATOM   183  C CD1 . PHE A 1 24  ? 12.43906 30.41967 29.82161  1.000 51.34761  ? 24  PHE A CD1 1 
ATOM   184  C CD2 . PHE A 1 24  ? 11.26502 28.43217 29.23299  1.000 47.30704  ? 24  PHE A CD2 1 
ATOM   185  C CE1 . PHE A 1 24  ? 13.46431 30.07350 28.95771  1.000 55.33710  ? 24  PHE A CE1 1 
ATOM   186  C CE2 . PHE A 1 24  ? 12.28676 28.07802 28.36759  1.000 47.62570  ? 24  PHE A CE2 1 
ATOM   187  C CZ  . PHE A 1 24  ? 13.38741 28.90015 28.23074  1.000 50.86740  ? 24  PHE A CZ  1 
ATOM   188  N N   . GLY A 1 25  ? 8.74217  31.03519 33.62795  1.000 50.35714  ? 25  GLY A N   1 
ATOM   189  C CA  . GLY A 1 25  ? 7.80291  31.95898 34.24093  1.000 53.87941  ? 25  GLY A CA  1 
ATOM   190  C C   . GLY A 1 25  ? 8.43738  32.99614 35.14513  1.000 57.08756  ? 25  GLY A C   1 
ATOM   191  O O   . GLY A 1 25  ? 7.77007  33.97703 35.49366  1.000 57.12371  ? 25  GLY A O   1 
ATOM   192  N N   . GLU A 1 26  ? 9.70100  32.81740 35.52007  1.000 57.98631  ? 26  GLU A N   1 
ATOM   193  C CA  . GLU A 1 26  ? 10.40297 33.75670 36.38294  1.000 59.18068  ? 26  GLU A CA  1 
ATOM   194  C C   . GLU A 1 26  ? 11.17317 34.81932 35.60266  1.000 65.81842  ? 26  GLU A C   1 
ATOM   195  O O   . GLU A 1 26  ? 11.93633 35.57896 36.20799  1.000 60.87064  ? 26  GLU A O   1 
ATOM   196  C CB  . GLU A 1 26  ? 11.34945 32.99267 37.31212  1.000 55.66840  ? 26  GLU A CB  1 
ATOM   197  C CG  . GLU A 1 26  ? 10.69468 31.81765 38.03765  1.000 52.51025  ? 26  GLU A CG  1 
ATOM   198  C CD  . GLU A 1 26  ? 9.66785  32.25200 39.07887  1.000 58.70260  ? 26  GLU A CD  1 
ATOM   199  O OE1 . GLU A 1 26  ? 9.59604  33.45942 39.39350  1.000 59.79718  ? 26  GLU A OE1 1 
ATOM   200  O OE2 . GLU A 1 26  ? 8.93038  31.38031 39.59048  1.000 59.05416  ? 26  GLU A OE2 1 
ATOM   201  N N   . TYR A 1 27  ? 10.97739 34.89948 34.28455  1.000 58.33668  ? 27  TYR A N   1 
ATOM   202  C CA  . TYR A 1 27  ? 11.64419 35.88000 33.43723  1.000 62.99547  ? 27  TYR A CA  1 
ATOM   203  C C   . TYR A 1 27  ? 10.62394 36.50429 32.49167  1.000 65.32495  ? 27  TYR A C   1 
ATOM   204  O O   . TYR A 1 27  ? 9.47355  36.06617 32.40417  1.000 63.71770  ? 27  TYR A O   1 
ATOM   205  C CB  . TYR A 1 27  ? 12.78469 35.24581 32.62614  1.000 64.44784  ? 27  TYR A CB  1 
ATOM   206  C CG  . TYR A 1 27  ? 13.84127 34.54472 33.45198  1.000 62.49852  ? 27  TYR A CG  1 
ATOM   207  C CD1 . TYR A 1 27  ? 13.72428 33.19632 33.76529  1.000 58.85560  ? 27  TYR A CD1 1 
ATOM   208  C CD2 . TYR A 1 27  ? 14.96588 35.22604 33.89992  1.000 64.41755  ? 27  TYR A CD2 1 
ATOM   209  C CE1 . TYR A 1 27  ? 14.69194 32.54904 34.51603  1.000 58.26254  ? 27  TYR A CE1 1 
ATOM   210  C CE2 . TYR A 1 27  ? 15.93776 34.58830 34.64869  1.000 63.44501  ? 27  TYR A CE2 1 
ATOM   211  C CZ  . TYR A 1 27  ? 15.79663 33.24956 34.95262  1.000 60.95501  ? 27  TYR A CZ  1 
ATOM   212  O OH  . TYR A 1 27  ? 16.76415 32.61251 35.69818  1.000 61.85472  ? 27  TYR A OH  1 
ATOM   213  N N   . ASP A 1 28  ? 11.06170 37.53394 31.76314  1.000 68.05998  ? 28  ASP A N   1 
ATOM   214  C CA  . ASP A 1 28  ? 10.22372 38.15255 30.73958  1.000 69.24599  ? 28  ASP A CA  1 
ATOM   215  C C   . ASP A 1 28  ? 10.12146 37.22832 29.53260  1.000 68.69607  ? 28  ASP A C   1 
ATOM   216  O O   . ASP A 1 28  ? 10.64164 37.53763 28.45524  1.000 69.68178  ? 28  ASP A O   1 
ATOM   217  C CB  . ASP A 1 28  ? 10.77943 39.51924 30.32702  1.000 74.04420  ? 28  ASP A CB  1 
ATOM   218  C CG  . ASP A 1 28  ? 9.82723  40.29670 29.42392  0.700 78.00528  ? 28  ASP A CG  1 
ATOM   219  O OD1 . ASP A 1 28  ? 8.72580  39.78612 29.12306  0.700 78.12818  ? 28  ASP A OD1 1 
ATOM   220  O OD2 . ASP A 1 28  ? 10.18233 41.42362 29.01564  0.700 80.64316  ? 28  ASP A OD2 1 
ATOM   221  N N   . MET A 1 29  ? 9.45761  36.08976 29.71215  1.000 66.70161  ? 29  MET A N   1 
ATOM   222  C CA  . MET A 1 29  ? 9.30122  35.08813 28.66975  1.000 64.77075  ? 29  MET A CA  1 
ATOM   223  C C   . MET A 1 29  ? 7.83164  34.71174 28.58137  1.000 62.94654  ? 29  MET A C   1 
ATOM   224  O O   . MET A 1 29  ? 7.17884  34.49620 29.60716  1.000 63.23884  ? 29  MET A O   1 
ATOM   225  C CB  . MET A 1 29  ? 10.16305 33.85148 28.95143  1.000 61.26290  ? 29  MET A CB  1 
ATOM   226  C CG  . MET A 1 29  ? 11.65821 34.13737 29.03798  1.000 64.13254  ? 29  MET A CG  1 
ATOM   227  S SD  . MET A 1 29  ? 12.41973 34.49929 27.44129  1.000 68.48326  ? 29  MET A SD  1 
ATOM   228  C CE  . MET A 1 29  ? 12.24678 32.91851 26.61111  1.000 64.29431  ? 29  MET A CE  1 
ATOM   229  N N   . GLU A 1 30  ? 7.31821  34.63704 27.35923  1.000 61.34941  ? 30  GLU A N   1 
ATOM   230  C CA  . GLU A 1 30  ? 5.90315  34.41167 27.09781  1.000 60.40035  ? 30  GLU A CA  1 
ATOM   231  C C   . GLU A 1 30  ? 5.75831  33.15135 26.25732  1.000 56.05538  ? 30  GLU A C   1 
ATOM   232  O O   . GLU A 1 30  ? 6.38030  33.03748 25.19591  1.000 54.82909  ? 30  GLU A O   1 
ATOM   233  C CB  . GLU A 1 30  ? 5.30109  35.62665 26.38599  1.000 62.50636  ? 30  GLU A CB  1 
ATOM   234  C CG  . GLU A 1 30  ? 3.92120  35.43161 25.79370  0.800 62.28513  ? 30  GLU A CG  1 
ATOM   235  C CD  . GLU A 1 30  ? 3.53542  36.57644 24.87044  0.700 65.99958  ? 30  GLU A CD  1 
ATOM   236  O OE1 . GLU A 1 30  ? 4.27771  37.58156 24.82917  0.700 65.39557  ? 30  GLU A OE1 1 
ATOM   237  O OE2 . GLU A 1 30  ? 2.49991  36.46994 24.17959  0.700 69.76490  ? 30  GLU A OE2 1 
ATOM   238  N N   . TYR A 1 31  ? 4.95582  32.20124 26.73528  1.000 53.65749  ? 31  TYR A N   1 
ATOM   239  C CA  . TYR A 1 31  ? 4.71028  30.98878 25.96343  1.000 52.07678  ? 31  TYR A CA  1 
ATOM   240  C C   . TYR A 1 31  ? 3.76686  31.30922 24.81370  1.000 52.63219  ? 31  TYR A C   1 
ATOM   241  O O   . TYR A 1 31  ? 2.63189  31.74368 25.03548  1.000 51.63503  ? 31  TYR A O   1 
ATOM   242  C CB  . TYR A 1 31  ? 4.12397  29.88326 26.84022  1.000 51.96660  ? 31  TYR A CB  1 
ATOM   243  C CG  . TYR A 1 31  ? 4.15604  28.52003 26.17539  1.000 49.34017  ? 31  TYR A CG  1 
ATOM   244  C CD1 . TYR A 1 31  ? 3.17604  28.13756 25.26248  1.000 48.81418  ? 31  TYR A CD1 1 
ATOM   245  C CD2 . TYR A 1 31  ? 5.17601  27.62039 26.45268  1.000 47.05542  ? 31  TYR A CD2 1 
ATOM   246  C CE1 . TYR A 1 31  ? 3.21520  26.89395 24.64512  1.000 47.84283  ? 31  TYR A CE1 1 
ATOM   247  C CE2 . TYR A 1 31  ? 5.22314  26.37826 25.84432  1.000 46.35097  ? 31  TYR A CE2 1 
ATOM   248  C CZ  . TYR A 1 31  ? 4.24128  26.01850 24.94224  1.000 46.36310  ? 31  TYR A CZ  1 
ATOM   249  O OH  . TYR A 1 31  ? 4.29630  24.77739 24.34568  1.000 41.89152  ? 31  TYR A OH  1 
ATOM   250  N N   . ASP A 1 32  ? 4.23732  31.09600 23.58731  1.000 50.92374  ? 32  ASP A N   1 
ATOM   251  C CA  . ASP A 1 32  ? 3.42898  31.33627 22.39565  1.000 51.64579  ? 32  ASP A CA  1 
ATOM   252  C C   . ASP A 1 32  ? 3.87679  30.33022 21.34746  1.000 51.48053  ? 32  ASP A C   1 
ATOM   253  O O   . ASP A 1 32  ? 5.01307  30.40237 20.87135  1.000 50.65515  ? 32  ASP A O   1 
ATOM   254  C CB  . ASP A 1 32  ? 3.59531  32.77323 21.90086  1.000 55.88934  ? 32  ASP A CB  1 
ATOM   255  C CG  . ASP A 1 32  ? 2.76907  33.07762 20.65320  1.000 57.84221  ? 32  ASP A CG  1 
ATOM   256  O OD1 . ASP A 1 32  ? 2.24729  32.14373 20.00774  1.000 55.50983  ? 32  ASP A OD1 1 
ATOM   257  O OD2 . ASP A 1 32  ? 2.63784  34.27258 20.31612  1.000 63.63040  ? 32  ASP A OD2 1 
ATOM   258  N N   . ASP A 1 33  ? 2.99522  29.39640 20.99384  1.000 51.16718  ? 33  ASP A N   1 
ATOM   259  C CA  . ASP A 1 33  ? 3.29880  28.40831 19.96957  1.000 52.14136  ? 33  ASP A CA  1 
ATOM   260  C C   . ASP A 1 33  ? 2.71394  28.78013 18.61218  1.000 53.12329  ? 33  ASP A C   1 
ATOM   261  O O   . ASP A 1 33  ? 2.65774  27.92978 17.71818  1.000 53.20825  ? 33  ASP A O   1 
ATOM   262  C CB  . ASP A 1 33  ? 2.81994  27.01753 20.40629  1.000 51.20986  ? 33  ASP A CB  1 
ATOM   263  C CG  . ASP A 1 33  ? 1.30770  26.91859 20.54281  1.000 53.71258  ? 33  ASP A CG  1 
ATOM   264  O OD1 . ASP A 1 33  ? 0.58948  27.88444 20.20746  1.000 54.67427  ? 33  ASP A OD1 1 
ATOM   265  O OD2 . ASP A 1 33  ? 0.83397  25.85306 20.99120  1.000 54.45023  ? 33  ASP A OD2 1 
ATOM   266  N N   . VAL A 1 34  ? 2.26766  30.02575 18.44483  1.000 52.84156  ? 34  VAL A N   1 
ATOM   267  C CA  . VAL A 1 34  ? 1.81000  30.51489 17.14877  1.000 55.16815  ? 34  VAL A CA  1 
ATOM   268  C C   . VAL A 1 34  ? 2.95839  31.25319 16.47587  1.000 56.21730  ? 34  VAL A C   1 
ATOM   269  O O   . VAL A 1 34  ? 3.36304  30.90903 15.36160  1.000 56.40455  ? 34  VAL A O   1 
ATOM   270  C CB  . VAL A 1 34  ? 0.57187  31.41917 17.28314  1.000 55.70450  ? 34  VAL A CB  1 
ATOM   271  C CG1 . VAL A 1 34  ? 0.18359  31.98451 15.92343  1.000 58.47794  ? 34  VAL A CG1 1 
ATOM   272  C CG2 . VAL A 1 34  ? -0.58579 30.64547 17.89131  1.000 55.80373  ? 34  VAL A CG2 1 
ATOM   273  N N   . GLU A 1 35  ? 3.50595  32.26168 17.15116  1.000 55.31848  ? 35  GLU A N   1 
ATOM   274  C CA  . GLU A 1 35  ? 4.64872  33.02219 16.64658  1.000 57.92134  ? 35  GLU A CA  1 
ATOM   275  C C   . GLU A 1 35  ? 5.80807  33.00715 17.64210  1.000 55.46610  ? 35  GLU A C   1 
ATOM   276  O O   . GLU A 1 35  ? 6.23691  34.06304 18.12184  1.000 56.68444  ? 35  GLU A O   1 
ATOM   277  C CB  . GLU A 1 35  ? 4.23510  34.45666 16.32709  1.000 60.80174  ? 35  GLU A CB  1 
ATOM   278  C CG  . GLU A 1 35  ? 3.08876  34.57088 15.33267  0.700 64.98966  ? 35  GLU A CG  1 
ATOM   279  C CD  . GLU A 1 35  ? 2.73117  36.01045 15.00816  0.700 70.33813  ? 35  GLU A CD  1 
ATOM   280  O OE1 . GLU A 1 35  ? 3.65594  36.83090 14.82170  0.700 70.56405  ? 35  GLU A OE1 1 
ATOM   281  O OE2 . GLU A 1 35  ? 1.52242  36.32018 14.94154  0.700 73.38945  ? 35  GLU A OE2 1 
ATOM   282  N N   . PRO A 1 36  ? 6.35449  31.83202 17.96170  1.000 53.51601  ? 36  PRO A N   1 
ATOM   283  C CA  . PRO A 1 36  ? 7.50919  31.79423 18.86314  1.000 52.17168  ? 36  PRO A CA  1 
ATOM   284  C C   . PRO A 1 36  ? 8.76632  32.31758 18.18664  1.000 51.87309  ? 36  PRO A C   1 
ATOM   285  O O   . PRO A 1 36  ? 8.91177  32.26976 16.96302  1.000 52.04103  ? 36  PRO A O   1 
ATOM   286  C CB  . PRO A 1 36  ? 7.64796  30.30651 19.20061  1.000 49.68396  ? 36  PRO A CB  1 
ATOM   287  C CG  . PRO A 1 36  ? 7.11652  29.61748 18.00122  1.000 50.58869  ? 36  PRO A CG  1 
ATOM   288  C CD  . PRO A 1 36  ? 5.99714  30.48228 17.48495  1.000 52.40323  ? 36  PRO A CD  1 
ATOM   289  N N   . GLU A 1 37  ? 9.67738  32.83656 19.00364  1.000 51.62942  ? 37  GLU A N   1 
ATOM   290  C CA  . GLU A 1 37  ? 11.00385 33.19776 18.53347  1.000 51.06148  ? 37  GLU A CA  1 
ATOM   291  C C   . GLU A 1 37  ? 12.05942 32.17426 18.92398  1.000 49.22327  ? 37  GLU A C   1 
ATOM   292  O O   . GLU A 1 37  ? 13.13406 32.13584 18.31070  1.000 48.52468  ? 37  GLU A O   1 
ATOM   293  C CB  . GLU A 1 37  ? 11.40277 34.57183 19.08111  1.000 54.16749  ? 37  GLU A CB  1 
ATOM   294  C CG  . GLU A 1 37  ? 10.50258 35.70680 18.63186  0.600 56.63034  ? 37  GLU A CG  1 
ATOM   295  C CD  . GLU A 1 37  ? 10.91247 37.02933 19.23291  0.600 61.08714  ? 37  GLU A CD  1 
ATOM   296  O OE1 . GLU A 1 37  ? 11.83989 37.03386 20.07199  0.600 62.37079  ? 37  GLU A OE1 1 
ATOM   297  O OE2 . GLU A 1 37  ? 10.30863 38.05966 18.86409  0.600 63.49579  ? 37  GLU A OE2 1 
ATOM   298  N N   . ILE A 1 38  ? 11.78367 31.36720 19.94294  1.000 48.35812  ? 38  ILE A N   1 
ATOM   299  C CA  . ILE A 1 38  ? 12.63131 30.25162 20.34095  1.000 46.15889  ? 38  ILE A CA  1 
ATOM   300  C C   . ILE A 1 38  ? 11.76989 29.00079 20.36592  1.000 43.86305  ? 38  ILE A C   1 
ATOM   301  O O   . ILE A 1 38  ? 10.67387 29.00873 20.93809  1.000 44.78420  ? 38  ILE A O   1 
ATOM   302  C CB  . ILE A 1 38  ? 13.28069 30.48572 21.71679  1.000 50.05889  ? 38  ILE A CB  1 
ATOM   303  C CG1 . ILE A 1 38  ? 14.16755 31.72860 21.67674  1.000 54.76473  ? 38  ILE A CG1 1 
ATOM   304  C CG2 . ILE A 1 38  ? 14.07476 29.26433 22.14850  1.000 48.25277  ? 38  ILE A CG2 1 
ATOM   305  C CD1 . ILE A 1 38  ? 14.45124 32.32313 23.04112  1.000 67.27006  ? 38  ILE A CD1 1 
ATOM   306  N N   . VAL A 1 39  ? 12.25749 27.93369 19.74521  1.000 41.75679  ? 39  VAL A N   1 
ATOM   307  C CA  . VAL A 1 39  ? 11.56680 26.65218 19.73004  1.000 40.45526  ? 39  VAL A CA  1 
ATOM   308  C C   . VAL A 1 39  ? 12.48473 25.62941 20.37880  1.000 39.29905  ? 39  VAL A C   1 
ATOM   309  O O   . VAL A 1 39  ? 13.57599 25.34540 19.86624  1.000 37.79262  ? 39  VAL A O   1 
ATOM   310  C CB  . VAL A 1 39  ? 11.16763 26.22702 18.31198  1.000 39.98467  ? 39  VAL A CB  1 
ATOM   311  C CG1 . VAL A 1 39  ? 10.79659 24.76040 18.29489  1.000 38.95752  ? 39  VAL A CG1 1 
ATOM   312  C CG2 . VAL A 1 39  ? 10.00040 27.07947 17.82842  1.000 40.82669  ? 39  VAL A CG2 1 
ATOM   313  N N   . ILE A 1 40  ? 12.05357 25.09477 21.51518  1.000 40.38207  ? 40  ILE A N   1 
ATOM   314  C CA  . ILE A 1 40  ? 12.79670 24.07915 22.24810  1.000 38.22594  ? 40  ILE A CA  1 
ATOM   315  C C   . ILE A 1 40  ? 12.15298 22.73131 21.97161  1.000 37.93324  ? 40  ILE A C   1 
ATOM   316  O O   . ILE A 1 40  ? 10.93912 22.56371 22.14659  1.000 37.55179  ? 40  ILE A O   1 
ATOM   317  C CB  . ILE A 1 40  ? 12.81969 24.38254 23.75557  1.000 39.52294  ? 40  ILE A CB  1 
ATOM   318  C CG1 . ILE A 1 40  ? 13.44116 25.75535 24.00724  1.000 41.62442  ? 40  ILE A CG1 1 
ATOM   319  C CG2 . ILE A 1 40  ? 13.58437 23.29793 24.50731  1.000 37.61107  ? 40  ILE A CG2 1 
ATOM   320  C CD1 . ILE A 1 40  ? 13.29269 26.23277 25.44102  1.000 40.88008  ? 40  ILE A CD1 1 
ATOM   321  N N   . SER A 1 41  ? 12.95895 21.78115 21.51955  1.000 34.47627  ? 41  SER A N   1 
ATOM   322  C CA  . SER A 1 41  ? 12.51770 20.42305 21.25923  1.000 37.41058  ? 41  SER A CA  1 
ATOM   323  C C   . SER A 1 41  ? 13.10567 19.50691 22.32164  1.000 37.66444  ? 41  SER A C   1 
ATOM   324  O O   . SER A 1 41  ? 14.32561 19.48178 22.51703  1.000 36.97112  ? 41  SER A O   1 
ATOM   325  C CB  . SER A 1 41  ? 12.95032 19.97580 19.85810  1.000 36.89097  ? 41  SER A CB  1 
ATOM   326  O OG  . SER A 1 41  ? 12.59291 18.63144 19.61408  1.000 38.96842  ? 41  SER A OG  1 
ATOM   327  N N   . ILE A 1 42  ? 12.24413 18.76397 23.01017  1.000 37.07159  ? 42  ILE A N   1 
ATOM   328  C CA  . ILE A 1 42  ? 12.66422 17.85971 24.07563  1.000 38.10523  ? 42  ILE A CA  1 
ATOM   329  C C   . ILE A 1 42  ? 12.32909 16.44015 23.64384  1.000 38.91779  ? 42  ILE A C   1 
ATOM   330  O O   . ILE A 1 42  ? 11.15064 16.07448 23.54085  1.000 38.49102  ? 42  ILE A O   1 
ATOM   331  C CB  . ILE A 1 42  ? 12.00515 18.19312 25.41922  1.000 37.36112  ? 42  ILE A CB  1 
ATOM   332  C CG1 . ILE A 1 42  ? 12.39788 19.60074 25.86845  1.000 37.79636  ? 42  ILE A CG1 1 
ATOM   333  C CG2 . ILE A 1 42  ? 12.41237 17.16957 26.46732  1.000 39.68762  ? 42  ILE A CG2 1 
ATOM   334  C CD1 . ILE A 1 42  ? 11.79173 20.00494 27.20626  1.000 37.34102  ? 42  ILE A CD1 1 
ATOM   335  N N   . GLY A 1 43  ? 13.36232 15.63503 23.40963  1.000 39.29615  ? 43  GLY A N   1 
ATOM   336  C CA  . GLY A 1 43  ? 13.17802 14.25998 22.99683  1.000 40.91159  ? 43  GLY A CA  1 
ATOM   337  C C   . GLY A 1 43  ? 14.37453 13.72317 22.24272  1.000 44.14119  ? 43  GLY A C   1 
ATOM   338  O O   . GLY A 1 43  ? 15.45095 13.54759 22.81763  1.000 48.57908  ? 43  GLY A O   1 
ATOM   339  N N   . GLY A 1 44  ? 14.19460 13.45005 20.95470  1.000 35.69441  ? 44  GLY A N   1 
ATOM   340  C CA  . GLY A 1 44  ? 15.27558 12.97278 20.11559  1.000 40.43377  ? 44  GLY A CA  1 
ATOM   341  C C   . GLY A 1 44  ? 15.33800 13.76056 18.82328  1.000 37.37507  ? 44  GLY A C   1 
ATOM   342  O O   . GLY A 1 44  ? 14.71969 14.82457 18.71893  1.000 33.87276  ? 44  GLY A O   1 
ATOM   343  N N   . ASP A 1 45  ? 16.07370 13.25343 17.83026  1.000 38.87724  ? 45  ASP A N   1 
ATOM   344  C CA  . ASP A 1 45  ? 16.16478 13.95076 16.55103  1.000 36.91108  ? 45  ASP A CA  1 
ATOM   345  C C   . ASP A 1 45  ? 14.83652 13.92759 15.80827  1.000 37.23146  ? 45  ASP A C   1 
ATOM   346  O O   . ASP A 1 45  ? 14.49462 14.89218 15.11284  1.000 37.25638  ? 45  ASP A O   1 
ATOM   347  C CB  . ASP A 1 45  ? 17.26582 13.33473 15.68891  1.000 37.67579  ? 45  ASP A CB  1 
ATOM   348  C CG  . ASP A 1 45  ? 18.65530 13.73081 16.14947  1.000 37.92848  ? 45  ASP A CG  1 
ATOM   349  O OD1 . ASP A 1 45  ? 18.81797 14.85334 16.67613  1.000 37.02352  ? 45  ASP A OD1 1 
ATOM   350  O OD2 . ASP A 1 45  ? 19.58824 12.92165 15.98146  1.000 39.45843  ? 45  ASP A OD2 1 
ATOM   351  N N   . GLY A 1 46  ? 14.08039 12.83194 15.92869  1.000 36.85241  ? 46  GLY A N   1 
ATOM   352  C CA  . GLY A 1 46  ? 12.75757 12.79799 15.32590  1.000 38.68529  ? 46  GLY A CA  1 
ATOM   353  C C   . GLY A 1 46  ? 11.85035 13.87881 15.87879  1.000 37.88526  ? 46  GLY A C   1 
ATOM   354  O O   . GLY A 1 46  ? 11.10176 14.51932 15.13500  1.000 34.53785  ? 46  GLY A O   1 
ATOM   355  N N   . THR A 1 47  ? 11.90981 14.09823 17.19561  1.000 37.59768  ? 47  THR A N   1 
ATOM   356  C CA  . THR A 1 47  ? 11.16765 15.19422 17.80670  1.000 37.46209  ? 47  THR A CA  1 
ATOM   357  C C   . THR A 1 47  ? 11.63216 16.53917 17.26309  1.000 34.22448  ? 47  THR A C   1 
ATOM   358  O O   . THR A 1 47  ? 10.81296 17.41888 16.97347  1.000 32.83667  ? 47  THR A O   1 
ATOM   359  C CB  . THR A 1 47  ? 11.33489 15.14552 19.32688  1.000 37.14498  ? 47  THR A CB  1 
ATOM   360  O OG1 . THR A 1 47  ? 11.04207 13.82373 19.79688  1.000 39.03891  ? 47  THR A OG1 1 
ATOM   361  C CG2 . THR A 1 47  ? 10.40699 16.14067 20.00860  1.000 38.60612  ? 47  THR A CG2 1 
ATOM   362  N N   . PHE A 1 48  ? 12.94712 16.71682 17.11848  1.000 34.56594  ? 48  PHE A N   1 
ATOM   363  C CA  . PHE A 1 48  ? 13.46387 17.97074 16.58162  1.000 36.80332  ? 48  PHE A CA  1 
ATOM   364  C C   . PHE A 1 48  ? 13.01721 18.17364 15.13982  1.000 35.29699  ? 48  PHE A C   1 
ATOM   365  O O   . PHE A 1 48  ? 12.63717 19.28529 14.75203  1.000 34.69101  ? 48  PHE A O   1 
ATOM   366  C CB  . PHE A 1 48  ? 14.99105 18.00262 16.68359  1.000 36.69762  ? 48  PHE A CB  1 
ATOM   367  C CG  . PHE A 1 48  ? 15.58930 19.32924 16.31221  1.000 38.41559  ? 48  PHE A CG  1 
ATOM   368  C CD1 . PHE A 1 48  ? 15.86687 19.64051 14.98553  1.000 35.56752  ? 48  PHE A CD1 1 
ATOM   369  C CD2 . PHE A 1 48  ? 15.86397 20.27103 17.28564  1.000 37.01227  ? 48  PHE A CD2 1 
ATOM   370  C CE1 . PHE A 1 48  ? 16.40528 20.86642 14.64477  1.000 37.65044  ? 48  PHE A CE1 1 
ATOM   371  C CE2 . PHE A 1 48  ? 16.40207 21.49733 16.95214  1.000 39.03382  ? 48  PHE A CE2 1 
ATOM   372  C CZ  . PHE A 1 48  ? 16.67480 21.79654 15.63161  1.000 35.97742  ? 48  PHE A CZ  1 
ATOM   373  N N   . LEU A 1 49  ? 13.05499 17.10642 14.33299  1.000 36.14130  ? 49  LEU A N   1 
ATOM   374  C CA  . LEU A 1 49  ? 12.60683 17.19271 12.94576  1.000 35.71230  ? 49  LEU A CA  1 
ATOM   375  C C   . LEU A 1 49  ? 11.15728 17.65928 12.85612  1.000 35.82594  ? 49  LEU A C   1 
ATOM   376  O O   . LEU A 1 49  ? 10.80986 18.46239 11.98263  1.000 36.58823  ? 49  LEU A O   1 
ATOM   377  C CB  . LEU A 1 49  ? 12.77273 15.83575 12.25390  1.000 37.21295  ? 49  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 49  ? 13.96570 15.52463 11.33570  1.000 36.87452  ? 49  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 49  ? 14.78119 16.76401 10.98830  1.000 36.12494  ? 49  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 49  ? 14.85693 14.43118 11.90817  1.000 36.31268  ? 49  LEU A CD2 1 
ATOM   381  N N   . SER A 1 50  ? 10.29414 17.16780 13.75000  1.000 38.04082  ? 50  SER A N   1 
ATOM   382  C CA  . SER A 1 50  ? 8.89775  17.59692 13.73128  1.000 37.95444  ? 50  SER A CA  1 
ATOM   383  C C   . SER A 1 50  ? 8.76349  19.05816 14.13498  1.000 37.31898  ? 50  SER A C   1 
ATOM   384  O O   . SER A 1 50  ? 7.92477  19.78370 13.58801  1.000 38.24359  ? 50  SER A O   1 
ATOM   385  C CB  . SER A 1 50  ? 8.05580  16.70761 14.64717  1.000 37.89662  ? 50  SER A CB  1 
ATOM   386  O OG  . SER A 1 50  ? 7.88610  15.42232 14.07058  1.000 39.77878  ? 50  SER A OG  1 
ATOM   387  N N   . ALA A 1 51  ? 9.58297  19.50730 15.08855  1.000 36.60241  ? 51  ALA A N   1 
ATOM   388  C CA  . ALA A 1 51  ? 9.56917  20.91269 15.47712  1.000 36.65365  ? 51  ALA A CA  1 
ATOM   389  C C   . ALA A 1 51  ? 9.96366  21.80660 14.31240  1.000 38.13076  ? 51  ALA A C   1 
ATOM   390  O O   . ALA A 1 51  ? 9.34586  22.85243 14.08390  1.000 37.01843  ? 51  ALA A O   1 
ATOM   391  C CB  . ALA A 1 51  ? 10.51128 21.13709 16.65805  1.000 36.59528  ? 51  ALA A CB  1 
ATOM   392  N N   . PHE A 1 52  ? 11.00522 21.41659 13.57676  1.000 32.98656  ? 52  PHE A N   1 
ATOM   393  C CA  . PHE A 1 52  ? 11.42142 22.17800 12.40477  1.000 38.60991  ? 52  PHE A CA  1 
ATOM   394  C C   . PHE A 1 52  ? 10.28974 22.28128 11.39137  1.000 37.56217  ? 52  PHE A C   1 
ATOM   395  O O   . PHE A 1 52  ? 9.98732  23.37018 10.88831  1.000 40.04861  ? 52  PHE A O   1 
ATOM   396  C CB  . PHE A 1 52  ? 12.65798 21.52590 11.78319  1.000 36.17274  ? 52  PHE A CB  1 
ATOM   397  C CG  . PHE A 1 52  ? 12.94573 21.97371 10.37736  1.000 37.54629  ? 52  PHE A CG  1 
ATOM   398  C CD1 . PHE A 1 52  ? 13.54447 23.19784 10.13335  1.000 38.20612  ? 52  PHE A CD1 1 
ATOM   399  C CD2 . PHE A 1 52  ? 12.63239 21.16270 9.30474   1.000 35.18433  ? 52  PHE A CD2 1 
ATOM   400  C CE1 . PHE A 1 52  ? 13.81627 23.60752 8.84074   1.000 37.64742  ? 52  PHE A CE1 1 
ATOM   401  C CE2 . PHE A 1 52  ? 12.90183 21.56588 8.00874   1.000 36.89554  ? 52  PHE A CE2 1 
ATOM   402  C CZ  . PHE A 1 52  ? 13.49135 22.79187 7.77838   1.000 37.19250  ? 52  PHE A CZ  1 
ATOM   403  N N   . HIS A 1 53  ? 9.63851  21.15501 11.09211  1.000 37.34050  ? 53  HIS A N   1 
ATOM   404  C CA  . HIS A 1 53  ? 8.58345  21.16420 10.08474  1.000 39.70012  ? 53  HIS A CA  1 
ATOM   405  C C   . HIS A 1 53  ? 7.31816  21.82596 10.60156  1.000 42.64122  ? 53  HIS A C   1 
ATOM   406  O O   . HIS A 1 53  ? 6.53418  22.36310 9.81060   1.000 42.44454  ? 53  HIS A O   1 
ATOM   407  C CB  . HIS A 1 53  ? 8.29920  19.74126 9.61167   1.000 39.41164  ? 53  HIS A CB  1 
ATOM   408  C CG  . HIS A 1 53  ? 9.36203  19.19822 8.70926   1.000 39.08882  ? 53  HIS A CG  1 
ATOM   409  N ND1 . HIS A 1 53  ? 9.53989  19.65207 7.42103   1.000 39.22172  ? 53  HIS A ND1 1 
ATOM   410  C CD2 . HIS A 1 53  ? 10.32371 18.26878 8.91807   1.000 37.77747  ? 53  HIS A CD2 1 
ATOM   411  C CE1 . HIS A 1 53  ? 10.55476 19.01122 6.86808   1.000 39.23423  ? 53  HIS A CE1 1 
ATOM   412  N NE2 . HIS A 1 53  ? 11.05146 18.17058 7.75762   1.000 37.42490  ? 53  HIS A NE2 1 
ATOM   413  N N   . GLN A 1 54  ? 7.10330  21.80498 11.91610  1.000 40.19132  ? 54  GLN A N   1 
ATOM   414  C CA  . GLN A 1 54  ? 5.96958  22.52746 12.47609  1.000 43.76494  ? 54  GLN A CA  1 
ATOM   415  C C   . GLN A 1 54  ? 6.07090  24.01742 12.18300  1.000 44.53925  ? 54  GLN A C   1 
ATOM   416  O O   . GLN A 1 54  ? 5.05160  24.67453 11.94520  1.000 46.05984  ? 54  GLN A O   1 
ATOM   417  C CB  . GLN A 1 54  ? 5.88591  22.27137 13.98346  1.000 45.15357  ? 54  GLN A CB  1 
ATOM   418  C CG  . GLN A 1 54  ? 4.69790  22.90713 14.68603  1.000 48.40445  ? 54  GLN A CG  1 
ATOM   419  C CD  . GLN A 1 54  ? 4.61236  22.49683 16.14860  1.000 55.68375  ? 54  GLN A CD  1 
ATOM   420  O OE1 . GLN A 1 54  ? 5.08959  21.42668 16.53223  1.000 61.16551  ? 54  GLN A OE1 1 
ATOM   421  N NE2 . GLN A 1 54  ? 4.00729  23.34933 16.97309  1.000 56.64397  ? 54  GLN A NE2 1 
ATOM   422  N N   . TYR A 1 55  ? 7.28867  24.55940 12.15302  1.000 44.51605  ? 55  TYR A N   1 
ATOM   423  C CA  . TYR A 1 55  ? 7.50192  25.99546 12.02492  1.000 46.17442  ? 55  TYR A CA  1 
ATOM   424  C C   . TYR A 1 55  ? 8.33418  26.35047 10.79506  1.000 46.82324  ? 55  TYR A C   1 
ATOM   425  O O   . TYR A 1 55  ? 9.00599  27.38375 10.77290  1.000 46.87856  ? 55  TYR A O   1 
ATOM   426  C CB  . TYR A 1 55  ? 8.15621  26.54412 13.29100  1.000 45.69243  ? 55  TYR A CB  1 
ATOM   427  C CG  . TYR A 1 55  ? 7.28051  26.43116 14.52027  1.000 47.34616  ? 55  TYR A CG  1 
ATOM   428  C CD1 . TYR A 1 55  ? 6.28634  27.36844 14.77487  1.000 48.69462  ? 55  TYR A CD1 1 
ATOM   429  C CD2 . TYR A 1 55  ? 7.44609  25.38928 15.42517  1.000 46.38035  ? 55  TYR A CD2 1 
ATOM   430  C CE1 . TYR A 1 55  ? 5.47805  27.27225 15.89713  1.000 49.04369  ? 55  TYR A CE1 1 
ATOM   431  C CE2 . TYR A 1 55  ? 6.64173  25.28546 16.55100  1.000 48.39521  ? 55  TYR A CE2 1 
ATOM   432  C CZ  . TYR A 1 55  ? 5.66021  26.22946 16.78076  1.000 49.49119  ? 55  TYR A CZ  1 
ATOM   433  O OH  . TYR A 1 55  ? 4.85940  26.13105 17.89917  1.000 50.57464  ? 55  TYR A OH  1 
ATOM   434  N N   . GLU A 1 56  ? 8.28597  25.51991 9.75125   1.000 45.88494  ? 56  GLU A N   1 
ATOM   435  C CA  . GLU A 1 56  ? 9.14557  25.76493 8.59705   1.000 47.87057  ? 56  GLU A CA  1 
ATOM   436  C C   . GLU A 1 56  ? 8.72918  26.98485 7.78686   1.000 49.60739  ? 56  GLU A C   1 
ATOM   437  O O   . GLU A 1 56  ? 9.45009  27.35878 6.85724   1.000 51.45456  ? 56  GLU A O   1 
ATOM   438  C CB  . GLU A 1 56  ? 9.19931  24.53496 7.68683   1.000 45.53352  ? 56  GLU A CB  1 
ATOM   439  C CG  . GLU A 1 56  ? 7.85963  23.95747 7.28715   1.000 47.10735  ? 56  GLU A CG  1 
ATOM   440  C CD  . GLU A 1 56  ? 7.99354  22.94716 6.15492   1.000 51.94818  ? 56  GLU A CD  1 
ATOM   441  O OE1 . GLU A 1 56  ? 8.09238  23.37357 4.98336   1.000 55.79225  ? 56  GLU A OE1 1 
ATOM   442  O OE2 . GLU A 1 56  ? 8.02096  21.72896 6.43362   1.000 47.67288  ? 56  GLU A OE2 1 
ATOM   443  N N   . GLU A 1 57  ? 7.60681  27.61738 8.11286   1.000 51.75182  ? 57  GLU A N   1 
ATOM   444  C CA  . GLU A 1 57  ? 7.20796  28.85157 7.45217   1.000 56.22920  ? 57  GLU A CA  1 
ATOM   445  C C   . GLU A 1 57  ? 7.67292  30.09965 8.19443   1.000 55.42454  ? 57  GLU A C   1 
ATOM   446  O O   . GLU A 1 57  ? 7.43032  31.21130 7.71556   1.000 55.43759  ? 57  GLU A O   1 
ATOM   447  C CB  . GLU A 1 57  ? 5.68682  28.88207 7.26826   1.000 59.83309  ? 57  GLU A CB  1 
ATOM   448  C CG  . GLU A 1 57  ? 5.19344  27.94579 6.16752   1.000 64.65228  ? 57  GLU A CG  1 
ATOM   449  C CD  . GLU A 1 57  ? 3.68201  27.85258 6.10132   0.700 71.88431  ? 57  GLU A CD  1 
ATOM   450  O OE1 . GLU A 1 57  ? 3.04142  27.77820 7.17041   0.600 75.19907  ? 57  GLU A OE1 1 
ATOM   451  O OE2 . GLU A 1 57  ? 3.13364  27.85784 4.97917   0.600 76.69095  ? 57  GLU A OE2 1 
ATOM   452  N N   . ARG A 1 58  ? 8.33951  29.94820 9.33803   1.000 53.66003  ? 58  ARG A N   1 
ATOM   453  C CA  . ARG A 1 58  ? 8.88348  31.06999 10.09696  1.000 54.90619  ? 58  ARG A CA  1 
ATOM   454  C C   . ARG A 1 58  ? 10.33742 30.81345 10.47110  1.000 52.90716  ? 58  ARG A C   1 
ATOM   455  O O   . ARG A 1 58  ? 10.79067 31.17657 11.56207  1.000 51.76925  ? 58  ARG A O   1 
ATOM   456  C CB  . ARG A 1 58  ? 8.05768  31.34153 11.35523  1.000 56.87256  ? 58  ARG A CB  1 
ATOM   457  C CG  . ARG A 1 58  ? 6.56203  31.48473 11.12068  1.000 60.24753  ? 58  ARG A CG  1 
ATOM   458  C CD  . ARG A 1 58  ? 5.85567  32.05513 12.34619  1.000 67.25404  ? 58  ARG A CD  1 
ATOM   459  N NE  . ARG A 1 58  ? 6.17320  33.46378 12.55713  1.000 64.17385  ? 58  ARG A NE  1 
ATOM   460  C CZ  . ARG A 1 58  ? 6.98336  33.92192 13.50234  1.000 63.97656  ? 58  ARG A CZ  1 
ATOM   461  N NH1 . ARG A 1 58  ? 7.56264  33.10924 14.37261  1.000 58.88843  ? 58  ARG A NH1 1 
ATOM   462  N NH2 . ARG A 1 58  ? 7.21497  35.22943 13.57907  1.000 69.29074  ? 58  ARG A NH2 1 
ATOM   463  N N   . LEU A 1 59  ? 11.09488 30.18582 9.56867   1.000 51.90894  ? 59  LEU A N   1 
ATOM   464  C CA  . LEU A 1 59  ? 12.46220 29.79406 9.89624   1.000 50.79284  ? 59  LEU A CA  1 
ATOM   465  C C   . LEU A 1 59  ? 13.36339 30.99446 10.14340  1.000 52.79996  ? 59  LEU A C   1 
ATOM   466  O O   . LEU A 1 59  ? 14.29996 30.90600 10.94467  1.000 52.83302  ? 59  LEU A O   1 
ATOM   467  C CB  . LEU A 1 59  ? 13.04374 28.93004 8.78358   1.000 49.21734  ? 59  LEU A CB  1 
ATOM   468  C CG  . LEU A 1 59  ? 12.46759 27.52075 8.71578   1.000 47.47199  ? 59  LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 59  ? 13.14757 26.74934 7.61054   1.000 44.43024  ? 59  LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 59  ? 12.63424 26.82200 10.06397  1.000 43.98628  ? 59  LEU A CD2 1 
ATOM   471  N N   . ASP A 1 60  ? 13.10722 32.11528 9.47494   1.000 54.34808  ? 60  ASP A N   1 
ATOM   472  C CA  . ASP A 1 60  ? 13.95574 33.28543 9.64710   1.000 58.33841  ? 60  ASP A CA  1 
ATOM   473  C C   . ASP A 1 60  ? 13.69016 34.02713 10.95053  1.000 57.85384  ? 60  ASP A C   1 
ATOM   474  O O   . ASP A 1 60  ? 14.49102 34.88946 11.32689  1.000 60.20447  ? 60  ASP A O   1 
ATOM   475  C CB  . ASP A 1 60  ? 13.77979 34.23833 8.46320   1.000 63.69834  ? 60  ASP A CB  1 
ATOM   476  C CG  . ASP A 1 60  ? 15.10366 34.62706 7.82936   1.000 76.26346  ? 60  ASP A CG  1 
ATOM   477  O OD1 . ASP A 1 60  ? 15.83379 33.71933 7.37322   1.000 68.23211  ? 60  ASP A OD1 1 
ATOM   478  O OD2 . ASP A 1 60  ? 15.41178 35.83834 7.78318   1.000 84.46249  ? 60  ASP A OD2 1 
ATOM   479  N N   . GLU A 1 61  ? 12.60232 33.71183 11.64904  1.000 55.72351  ? 61  GLU A N   1 
ATOM   480  C CA  . GLU A 1 61  ? 12.25467 34.37816 12.89590  1.000 55.07818  ? 61  GLU A CA  1 
ATOM   481  C C   . GLU A 1 61  ? 12.48025 33.50582 14.12421  1.000 52.51127  ? 61  GLU A C   1 
ATOM   482  O O   . GLU A 1 61  ? 12.15131 33.93113 15.23822  1.000 51.82872  ? 61  GLU A O   1 
ATOM   483  C CB  . GLU A 1 61  ? 10.78962 34.83560 12.86175  1.000 56.99633  ? 61  GLU A CB  1 
ATOM   484  C CG  . GLU A 1 61  ? 10.49665 35.98210 11.90852  1.000 60.19012  ? 61  GLU A CG  1 
ATOM   485  C CD  . GLU A 1 61  ? 9.94101  35.51515 10.57996  0.700 61.05236  ? 61  GLU A CD  1 
ATOM   486  O OE1 . GLU A 1 61  ? 9.92684  34.29155 10.33442  0.700 59.36556  ? 61  GLU A OE1 1 
ATOM   487  O OE2 . GLU A 1 61  ? 9.51113  36.37273 9.78099   0.700 65.20622  ? 61  GLU A OE2 1 
ATOM   488  N N   . ILE A 1 62  ? 13.03293 32.30642 13.95874  1.000 51.19979  ? 62  ILE A N   1 
ATOM   489  C CA  . ILE A 1 62  ? 13.07611 31.30825 15.01939  1.000 48.99334  ? 62  ILE A CA  1 
ATOM   490  C C   . ILE A 1 62  ? 14.50216 30.80908 15.20034  1.000 47.42273  ? 62  ILE A C   1 
ATOM   491  O O   . ILE A 1 62  ? 15.21362 30.56290 14.22111  1.000 45.38561  ? 62  ILE A O   1 
ATOM   492  C CB  . ILE A 1 62  ? 12.12372 30.13346 14.70783  1.000 47.12832  ? 62  ILE A CB  1 
ATOM   493  C CG1 . ILE A 1 62  ? 10.67103 30.61021 14.75618  1.000 48.04088  ? 62  ILE A CG1 1 
ATOM   494  C CG2 . ILE A 1 62  ? 12.35679 28.96622 15.65711  1.000 44.26729  ? 62  ILE A CG2 1 
ATOM   495  C CD1 . ILE A 1 62  ? 9.66496  29.51510 14.52449  1.000 47.58963  ? 62  ILE A CD1 1 
ATOM   496  N N   . ALA A 1 63  ? 14.91944 30.66795 16.45644  1.000 45.03843  ? 63  ALA A N   1 
ATOM   497  C CA  . ALA A 1 63  ? 16.13378 29.94709 16.81398  1.000 44.18581  ? 63  ALA A CA  1 
ATOM   498  C C   . ALA A 1 63  ? 15.73722 28.66125 17.52628  1.000 42.87102  ? 63  ALA A C   1 
ATOM   499  O O   . ALA A 1 63  ? 14.97140 28.69747 18.49494  1.000 43.99823  ? 63  ALA A O   1 
ATOM   500  C CB  . ALA A 1 63  ? 17.04696 30.79277 17.70393  1.000 47.21877  ? 63  ALA A CB  1 
ATOM   501  N N   . PHE A 1 64  ? 16.24935 27.53356 17.04068  1.000 41.69118  ? 64  PHE A N   1 
ATOM   502  C CA  . PHE A 1 64  ? 15.90367 26.22237 17.57060  1.000 41.29285  ? 64  PHE A CA  1 
ATOM   503  C C   . PHE A 1 64  ? 16.92521 25.76151 18.60530  1.000 41.05137  ? 64  PHE A C   1 
ATOM   504  O O   . PHE A 1 64  ? 18.11090 26.09323 18.52546  1.000 40.62842  ? 64  PHE A O   1 
ATOM   505  C CB  . PHE A 1 64  ? 15.82415 25.18760 16.44441  1.000 38.31714  ? 64  PHE A CB  1 
ATOM   506  C CG  . PHE A 1 64  ? 14.64398 25.36142 15.52774  1.000 38.93094  ? 64  PHE A CG  1 
ATOM   507  C CD1 . PHE A 1 64  ? 14.71458 26.20754 14.43054  1.000 39.25857  ? 64  PHE A CD1 1 
ATOM   508  C CD2 . PHE A 1 64  ? 13.47293 24.65387 15.74682  1.000 37.80972  ? 64  PHE A CD2 1 
ATOM   509  C CE1 . PHE A 1 64  ? 13.63095 26.35512 13.57915  1.000 40.71544  ? 64  PHE A CE1 1 
ATOM   510  C CE2 . PHE A 1 64  ? 12.38715 24.79906 14.90238  1.000 37.59536  ? 64  PHE A CE2 1 
ATOM   511  C CZ  . PHE A 1 64  ? 12.46582 25.65013 13.81761  1.000 40.30341  ? 64  PHE A CZ  1 
ATOM   512  N N   . ILE A 1 65  ? 16.44898 24.98668 19.58388  1.000 39.32938  ? 65  ILE A N   1 
ATOM   513  C CA  . ILE A 1 65  ? 17.30212 24.32244 20.56874  1.000 40.55240  ? 65  ILE A CA  1 
ATOM   514  C C   . ILE A 1 65  ? 16.75617 22.92242 20.81501  1.000 39.44168  ? 65  ILE A C   1 
ATOM   515  O O   . ILE A 1 65  ? 15.55178 22.75123 21.03027  1.000 40.60609  ? 65  ILE A O   1 
ATOM   516  C CB  . ILE A 1 65  ? 17.37015 25.08926 21.90577  1.000 43.21053  ? 65  ILE A CB  1 
ATOM   517  C CG1 . ILE A 1 65  ? 17.74468 26.54976 21.68239  1.000 46.77244  ? 65  ILE A CG1 1 
ATOM   518  C CG2 . ILE A 1 65  ? 18.37223 24.43118 22.84347  1.000 46.16883  ? 65  ILE A CG2 1 
ATOM   519  C CD1 . ILE A 1 65  ? 17.73511 27.34754 22.93351  1.000 54.65589  ? 65  ILE A CD1 1 
ATOM   520  N N   . GLY A 1 66  ? 17.63653 21.92602 20.81899  1.000 37.32003  ? 66  GLY A N   1 
ATOM   521  C CA  . GLY A 1 66  ? 17.24865 20.54615 21.06284  1.000 38.77633  ? 66  GLY A CA  1 
ATOM   522  C C   . GLY A 1 66  ? 17.82404 20.02257 22.36989  1.000 43.30989  ? 66  GLY A C   1 
ATOM   523  O O   . GLY A 1 66  ? 19.00673 20.21406 22.66232  1.000 41.29596  ? 66  GLY A O   1 
ATOM   524  N N   . ILE A 1 67  ? 16.96861 19.35796 23.14296  1.000 40.52706  ? 67  ILE A N   1 
ATOM   525  C CA  . ILE A 1 67  ? 17.36048 18.66527 24.36535  1.000 42.26518  ? 67  ILE A CA  1 
ATOM   526  C C   . ILE A 1 67  ? 17.08324 17.18456 24.15862  1.000 42.05767  ? 67  ILE A C   1 
ATOM   527  O O   . ILE A 1 67  ? 15.95958 16.80782 23.80617  1.000 41.08194  ? 67  ILE A O   1 
ATOM   528  C CB  . ILE A 1 67  ? 16.59374 19.19675 25.59096  1.000 40.12007  ? 67  ILE A CB  1 
ATOM   529  C CG1 . ILE A 1 67  ? 16.94594 20.66237 25.84770  1.000 39.83753  ? 67  ILE A CG1 1 
ATOM   530  C CG2 . ILE A 1 67  ? 16.86988 18.33333 26.81920  1.000 43.20731  ? 67  ILE A CG2 1 
ATOM   531  C CD1 . ILE A 1 67  ? 16.08631 21.30849 26.90359  1.000 44.51257  ? 67  ILE A CD1 1 
ATOM   532  N N   . HIS A 1 68  ? 18.09638 16.34627 24.36348  1.000 42.50770  ? 68  HIS A N   1 
ATOM   533  C CA  . HIS A 1 68  ? 17.94536 14.91159 24.15108  1.000 48.04383  ? 68  HIS A CA  1 
ATOM   534  C C   . HIS A 1 68  ? 17.73541 14.23345 25.49875  1.000 51.10466  ? 68  HIS A C   1 
ATOM   535  O O   . HIS A 1 68  ? 18.62266 14.24543 26.35762  1.000 51.76686  ? 68  HIS A O   1 
ATOM   536  C CB  . HIS A 1 68  ? 19.13968 14.32077 23.39885  1.000 51.57400  ? 68  HIS A CB  1 
ATOM   537  C CG  . HIS A 1 68  ? 20.42968 14.37293 24.15378  1.000 53.75826  ? 68  HIS A CG  1 
ATOM   538  N ND1 . HIS A 1 68  ? 20.81520 13.38400 25.03292  1.000 56.58970  ? 68  HIS A ND1 1 
ATOM   539  C CD2 . HIS A 1 68  ? 21.42710 15.28828 24.15506  1.000 54.44635  ? 68  HIS A CD2 1 
ATOM   540  C CE1 . HIS A 1 68  ? 21.99268 13.69014 25.54758  1.000 56.34798  ? 68  HIS A CE1 1 
ATOM   541  N NE2 . HIS A 1 68  ? 22.38583 14.84141 25.03248  1.000 55.33744  ? 68  HIS A NE2 1 
ATOM   542  N N   . THR A 1 69  ? 16.54982 13.66001 25.68798  1.000 50.14806  ? 69  THR A N   1 
ATOM   543  C CA  . THR A 1 69  ? 16.25901 12.90452 26.89791  1.000 53.40240  ? 69  THR A CA  1 
ATOM   544  C C   . THR A 1 69  ? 16.63429 11.43451 26.77329  1.000 55.60541  ? 69  THR A C   1 
ATOM   545  O O   . THR A 1 69  ? 16.66506 10.72959 27.78748  1.000 56.85198  ? 69  THR A O   1 
ATOM   546  C CB  . THR A 1 69  ? 14.77754 13.04717 27.27515  1.000 51.61483  ? 69  THR A CB  1 
ATOM   547  O OG1 . THR A 1 69  ? 13.95345 12.81148 26.12702  1.000 51.67574  ? 69  THR A OG1 1 
ATOM   548  C CG2 . THR A 1 69  ? 14.50909 14.44541 27.80270  1.000 49.80985  ? 69  THR A CG2 1 
ATOM   549  N N   . GLY A 1 70  ? 16.92585 10.96594 25.56854  1.000 57.90454  ? 70  GLY A N   1 
ATOM   550  C CA  . GLY A 1 70  ? 17.57932 9.68781  25.33725  1.000 59.35641  ? 70  GLY A CA  1 
ATOM   551  C C   . GLY A 1 70  ? 19.05195 9.87526  25.04179  1.000 62.15352  ? 70  GLY A C   1 
ATOM   552  O O   . GLY A 1 70  ? 19.70928 10.76063 25.60039  1.000 60.11986  ? 70  GLY A O   1 
ATOM   553  N N   . HIS A 1 71  ? 19.57967 9.03931  24.15236  1.000 66.47080  ? 71  HIS A N   1 
ATOM   554  C CA  A HIS A 1 71  ? 20.96475 9.16928  23.72465  0.500 67.76516  ? 71  HIS A CA  1 
ATOM   555  C CA  B HIS A 1 71  ? 20.97141 9.18451  23.75764  0.500 67.75931  ? 71  HIS A CA  1 
ATOM   556  C C   . HIS A 1 71  ? 21.18256 10.51324 23.03394  1.000 67.18966  ? 71  HIS A C   1 
ATOM   557  O O   . HIS A 1 71  ? 20.23602 11.18495 22.61124  1.000 65.52151  ? 71  HIS A O   1 
ATOM   558  C CB  A HIS A 1 71  ? 21.34038 8.02979  22.77740  0.500 67.04472  ? 71  HIS A CB  1 
ATOM   559  C CB  B HIS A 1 71  ? 21.40413 8.01615  22.87189  0.500 67.06757  ? 71  HIS A CB  1 
ATOM   560  C CG  A HIS A 1 71  ? 20.59676 8.05735  21.47755  0.500 66.93009  ? 71  HIS A CG  1 
ATOM   561  C CG  B HIS A 1 71  ? 21.18512 6.67403  23.49804  0.500 68.64686  ? 71  HIS A CG  1 
ATOM   562  N ND1 A HIS A 1 71  ? 20.98032 8.84929  20.41620  0.500 64.19214  ? 71  HIS A ND1 1 
ATOM   563  N ND1 B HIS A 1 71  ? 21.94646 6.20848  24.54855  0.500 70.47319  ? 71  HIS A ND1 1 
ATOM   564  C CD2 A HIS A 1 71  ? 19.48838 7.39466  21.07008  0.500 66.47997  ? 71  HIS A CD2 1 
ATOM   565  C CD2 B HIS A 1 71  ? 20.28636 5.69899  23.22421  0.500 70.04343  ? 71  HIS A CD2 1 
ATOM   566  C CE1 A HIS A 1 71  ? 20.14211 8.67172  19.41071  0.500 61.77071  ? 71  HIS A CE1 1 
ATOM   567  C CE1 B HIS A 1 71  ? 21.52582 5.00500  24.89540  0.500 71.24251  ? 71  HIS A CE1 1 
ATOM   568  N NE2 A HIS A 1 71  ? 19.22771 7.79353  19.78132  0.500 63.85156  ? 71  HIS A NE2 1 
ATOM   569  N NE2 B HIS A 1 71  ? 20.52002 4.67213  24.10664  0.500 71.22690  ? 71  HIS A NE2 1 
ATOM   570  N N   . LEU A 1 72  ? 22.45224 10.89797 22.91261  1.000 61.60074  ? 72  LEU A N   1 
ATOM   571  C CA  . LEU A 1 72  ? 22.79239 12.15689 22.26286  1.000 58.86763  ? 72  LEU A CA  1 
ATOM   572  C C   . LEU A 1 72  ? 22.24012 12.18920 20.84338  1.000 58.04601  ? 72  LEU A C   1 
ATOM   573  O O   . LEU A 1 72  ? 22.38223 11.22679 20.08405  1.000 56.22876  ? 72  LEU A O   1 
ATOM   574  C CB  . LEU A 1 72  ? 24.30962 12.35456 22.24314  1.000 58.61877  ? 72  LEU A CB  1 
ATOM   575  C CG  . LEU A 1 72  ? 24.84731 13.53110 21.41910  1.000 57.43073  ? 72  LEU A CG  1 
ATOM   576  C CD1 . LEU A 1 72  ? 24.35249 14.86787 21.96688  1.000 55.56845  ? 72  LEU A CD1 1 
ATOM   577  C CD2 . LEU A 1 72  ? 26.36730 13.49557 21.36980  1.000 53.57644  ? 72  LEU A CD2 1 
ATOM   578  N N   . GLY A 1 73  ? 21.57864 13.28933 20.50146  1.000 53.59095  ? 73  GLY A N   1 
ATOM   579  C CA  . GLY A 1 73  ? 21.10082 13.49099 19.15134  1.000 48.47928  ? 73  GLY A CA  1 
ATOM   580  C C   . GLY A 1 73  ? 21.96329 14.50701 18.43722  1.000 49.92844  ? 73  GLY A C   1 
ATOM   581  O O   . GLY A 1 73  ? 22.63741 15.31342 19.08554  1.000 48.40362  ? 73  GLY A O   1 
ATOM   582  N N   . PHE A 1 74  ? 21.96491 14.48088 17.10648  1.000 39.47920  ? 74  PHE A N   1 
ATOM   583  C CA  . PHE A 1 74  ? 22.77558 15.44172 16.37373  1.000 41.64348  ? 74  PHE A CA  1 
ATOM   584  C C   . PHE A 1 74  ? 22.14855 16.82096 16.35106  1.000 39.95899  ? 74  PHE A C   1 
ATOM   585  O O   . PHE A 1 74  ? 22.86276 17.82027 16.20601  1.000 42.16256  ? 74  PHE A O   1 
ATOM   586  C CB  . PHE A 1 74  ? 23.01827 14.95454 14.94633  1.000 37.40421  ? 74  PHE A CB  1 
ATOM   587  C CG  . PHE A 1 74  ? 24.37958 14.40871 14.74913  1.000 38.74040  ? 74  PHE A CG  1 
ATOM   588  C CD1 . PHE A 1 74  ? 24.65786 13.09620 15.06815  1.000 38.65239  ? 74  PHE A CD1 1 
ATOM   589  C CD2 . PHE A 1 74  ? 25.39892 15.21771 14.28699  1.000 39.28510  ? 74  PHE A CD2 1 
ATOM   590  C CE1 . PHE A 1 74  ? 25.91884 12.58926 14.89603  1.000 39.77800  ? 74  PHE A CE1 1 
ATOM   591  C CE2 . PHE A 1 74  ? 26.66340 14.72089 14.11539  1.000 39.30937  ? 74  PHE A CE2 1 
ATOM   592  C CZ  . PHE A 1 74  ? 26.92835 13.40235 14.42116  1.000 45.29752  ? 74  PHE A CZ  1 
ATOM   593  N N   . TYR A 1 75  ? 20.82809 16.89748 16.47257  1.000 34.92484  ? 75  TYR A N   1 
ATOM   594  C CA  . TYR A 1 75  ? 20.15483 18.17760 16.59863  1.000 36.96109  ? 75  TYR A CA  1 
ATOM   595  C C   . TYR A 1 75  ? 19.81867 18.49759 18.04586  1.000 42.57175  ? 75  TYR A C   1 
ATOM   596  O O   . TYR A 1 75  ? 20.04708 19.62147 18.49841  1.000 41.12798  ? 75  TYR A O   1 
ATOM   597  C CB  . TYR A 1 75  ? 18.88870 18.19190 15.74574  1.000 37.63981  ? 75  TYR A CB  1 
ATOM   598  C CG  . TYR A 1 75  ? 19.18791 17.97820 14.28813  1.000 35.46464  ? 75  TYR A CG  1 
ATOM   599  C CD1 . TYR A 1 75  ? 20.02864 18.84772 13.60301  1.000 34.15373  ? 75  TYR A CD1 1 
ATOM   600  C CD2 . TYR A 1 75  ? 18.64637 16.90374 13.59607  1.000 36.18144  ? 75  TYR A CD2 1 
ATOM   601  C CE1 . TYR A 1 75  ? 20.31707 18.65478 12.25972  1.000 34.19769  ? 75  TYR A CE1 1 
ATOM   602  C CE2 . TYR A 1 75  ? 18.92849 16.70512 12.25223  1.000 32.53715  ? 75  TYR A CE2 1 
ATOM   603  C CZ  . TYR A 1 75  ? 19.76334 17.58281 11.59175  1.000 32.53507  ? 75  TYR A CZ  1 
ATOM   604  O OH  . TYR A 1 75  ? 20.04633 17.38083 10.25335  1.000 31.56829  ? 75  TYR A OH  1 
ATOM   605  N N   . ALA A 1 76  ? 19.27879 17.52324 18.77586  1.000 41.72192  ? 76  ALA A N   1 
ATOM   606  C CA  . ALA A 1 76  ? 19.03267 17.65272 20.21085  1.000 45.66226  ? 76  ALA A CA  1 
ATOM   607  C C   . ALA A 1 76  ? 20.33267 17.32710 20.92911  1.000 45.37815  ? 76  ALA A C   1 
ATOM   608  O O   . ALA A 1 76  ? 20.58512 16.18797 21.32580  1.000 44.32867  ? 76  ALA A O   1 
ATOM   609  C CB  . ALA A 1 76  ? 17.89805 16.73811 20.65369  1.000 44.35187  ? 76  ALA A CB  1 
ATOM   610  N N   . ASP A 1 77  ? 21.17868 18.34468 21.09264  1.000 45.34148  ? 77  ASP A N   1 
ATOM   611  C CA  . ASP A 1 77  ? 22.54010 18.15008 21.57367  1.000 52.18977  ? 77  ASP A CA  1 
ATOM   612  C C   . ASP A 1 77  ? 22.76351 18.69891 22.98449  1.000 53.19370  ? 77  ASP A C   1 
ATOM   613  O O   . ASP A 1 77  ? 23.91375 18.88686 23.39357  1.000 59.87523  ? 77  ASP A O   1 
ATOM   614  C CB  . ASP A 1 77  ? 23.52585 18.77633 20.58798  1.000 50.01446  ? 77  ASP A CB  1 
ATOM   615  C CG  . ASP A 1 77  ? 23.13413 20.18707 20.19324  1.000 51.37123  ? 77  ASP A CG  1 
ATOM   616  O OD1 . ASP A 1 77  ? 22.04877 20.64150 20.61538  1.000 56.00392  ? 77  ASP A OD1 1 
ATOM   617  O OD2 . ASP A 1 77  ? 23.91063 20.84187 19.46629  1.000 53.08266  ? 77  ASP A OD2 1 
ATOM   618  N N   . TRP A 1 78  ? 21.69201 18.94514 23.73902  1.000 52.43051  ? 78  TRP A N   1 
ATOM   619  C CA  . TRP A 1 78  ? 21.76533 19.39421 25.12421  1.000 53.57635  ? 78  TRP A CA  1 
ATOM   620  C C   . TRP A 1 78  ? 21.23977 18.30496 26.05386  1.000 51.83982  ? 78  TRP A C   1 
ATOM   621  O O   . TRP A 1 78  ? 20.24806 17.63984 25.74088  1.000 48.67805  ? 78  TRP A O   1 
ATOM   622  C CB  . TRP A 1 78  ? 20.94767 20.67466 25.33300  1.000 55.20552  ? 78  TRP A CB  1 
ATOM   623  C CG  . TRP A 1 78  ? 21.65572 21.94247 24.96565  0.700 59.48846  ? 78  TRP A CG  1 
ATOM   624  C CD1 . TRP A 1 78  ? 21.85269 22.44307 23.71039  0.700 59.38208  ? 78  TRP A CD1 1 
ATOM   625  C CD2 . TRP A 1 78  ? 22.24378 22.88466 25.87094  0.700 61.77862  ? 78  TRP A CD2 1 
ATOM   626  N NE1 . TRP A 1 78  ? 22.53712 23.63471 23.77961  0.700 66.77558  ? 78  TRP A NE1 1 
ATOM   627  C CE2 . TRP A 1 78  ? 22.78854 23.92722 25.09524  0.700 63.27754  ? 78  TRP A CE2 1 
ATOM   628  C CE3 . TRP A 1 78  ? 22.36985 22.94265 27.26184  0.700 61.76483  ? 78  TRP A CE3 1 
ATOM   629  C CZ2 . TRP A 1 78  ? 23.44820 25.01640 25.66596  0.700 64.60040  ? 78  TRP A CZ2 1 
ATOM   630  C CZ3 . TRP A 1 78  ? 23.02526 24.02372 27.82691  0.700 62.49798  ? 78  TRP A CZ3 1 
ATOM   631  C CH2 . TRP A 1 78  ? 23.55577 25.04575 27.02993  0.700 63.02894  ? 78  TRP A CH2 1 
ATOM   632  N N   . ARG A 1 79  ? 21.91653 18.12337 27.23394  1.000 54.99282  ? 79  ARG A N   1 
ATOM   633  C CA  . ARG A 1 79  ? 21.43253 17.13267 28.19036  1.000 54.36434  ? 79  ARG A CA  1 
ATOM   634  C C   . ARG A 1 79  ? 20.35240 17.72630 29.08978  1.000 53.57999  ? 79  ARG A C   1 
ATOM   635  O O   . ARG A 1 79  ? 20.31849 18.94029 29.31174  1.000 54.25159  ? 79  ARG A O   1 
ATOM   636  C CB  . ARG A 1 79  ? 22.57995 16.61034 29.05566  1.000 57.72075  ? 79  ARG A CB  1 
ATOM   637  C CG  . ARG A 1 79  ? 23.56623 15.71182 28.32370  0.800 60.45950  ? 79  ARG A CG  1 
ATOM   638  C CD  . ARG A 1 79  ? 24.45877 14.93426 29.29236  0.700 60.06594  ? 79  ARG A CD  1 
ATOM   639  N NE  . ARG A 1 79  ? 25.20657 15.80070 30.19638  0.700 62.46692  ? 79  ARG A NE  1 
ATOM   640  C CZ  . ARG A 1 79  ? 24.99792 15.88441 31.50424  0.700 64.00901  ? 79  ARG A CZ  1 
ATOM   641  N NH1 . ARG A 1 79  ? 24.07450 15.15254 32.10673  0.700 64.59004  ? 79  ARG A NH1 1 
ATOM   642  N NH2 . ARG A 1 79  ? 25.73772 16.72061 32.22687  0.700 63.94394  ? 79  ARG A NH2 1 
ATOM   643  N N   . PRO A 1 80  ? 19.45644 16.88636 29.61691  1.000 52.74410  ? 80  PRO A N   1 
ATOM   644  C CA  . PRO A 1 80  ? 18.40328 17.40343 30.51083  1.000 54.86469  ? 80  PRO A CA  1 
ATOM   645  C C   . PRO A 1 80  ? 18.93138 18.08906 31.75947  1.000 58.21061  ? 80  PRO A C   1 
ATOM   646  O O   . PRO A 1 80  ? 18.26017 18.98157 32.29265  1.000 57.51299  ? 80  PRO A O   1 
ATOM   647  C CB  . PRO A 1 80  ? 17.59904 16.14277 30.85836  1.000 51.15175  ? 80  PRO A CB  1 
ATOM   648  C CG  . PRO A 1 80  ? 17.80903 15.23966 29.67356  1.000 52.55844  ? 80  PRO A CG  1 
ATOM   649  C CD  . PRO A 1 80  ? 19.23100 15.47591 29.25422  1.000 51.21820  ? 80  PRO A CD  1 
ATOM   650  N N   . ALA A 1 81  ? 20.11209 17.69797 32.24687  1.000 59.67385  ? 81  ALA A N   1 
ATOM   651  C CA  . ALA A 1 81  ? 20.67345 18.31890 33.44111  1.000 63.93209  ? 81  ALA A CA  1 
ATOM   652  C C   . ALA A 1 81  ? 21.01170 19.78734 33.22775  1.000 62.23428  ? 81  ALA A C   1 
ATOM   653  O O   . ALA A 1 81  ? 21.08304 20.54180 34.20210  1.000 68.89959  ? 81  ALA A O   1 
ATOM   654  C CB  . ALA A 1 81  ? 21.92207 17.55942 33.89038  1.000 64.62575  ? 81  ALA A CB  1 
ATOM   655  N N   . GLU A 1 82  ? 21.21843 20.20809 31.98434  1.000 61.61006  ? 82  GLU A N   1 
ATOM   656  C CA  . GLU A 1 82  ? 21.52811 21.59507 31.67080  1.000 62.72631  ? 82  GLU A CA  1 
ATOM   657  C C   . GLU A 1 82  ? 20.28181 22.42823 31.39685  1.000 59.31541  ? 82  GLU A C   1 
ATOM   658  O O   . GLU A 1 82  ? 20.40520 23.58034 30.96730  1.000 57.82065  ? 82  GLU A O   1 
ATOM   659  C CB  . GLU A 1 82  ? 22.47974 21.65558 30.47180  1.000 64.37113  ? 82  GLU A CB  1 
ATOM   660  C CG  . GLU A 1 82  ? 23.91248 21.26589 30.80883  1.000 67.58489  ? 82  GLU A CG  1 
ATOM   661  C CD  . GLU A 1 82  ? 24.58559 20.45711 29.71486  1.000 66.80221  ? 82  GLU A CD  1 
ATOM   662  O OE1 . GLU A 1 82  ? 23.95575 20.21831 28.66118  1.000 65.11362  ? 82  GLU A OE1 1 
ATOM   663  O OE2 . GLU A 1 82  ? 25.74926 20.05175 29.91525  1.000 77.46688  ? 82  GLU A OE2 1 
ATOM   664  N N   . ALA A 1 83  ? 19.09040 21.87728 31.65004  1.000 58.21240  ? 83  ALA A N   1 
ATOM   665  C CA  . ALA A 1 83  ? 17.85643 22.58184 31.31435  1.000 58.00357  ? 83  ALA A CA  1 
ATOM   666  C C   . ALA A 1 83  ? 17.72605 23.87862 32.10352  1.000 58.07875  ? 83  ALA A C   1 
ATOM   667  O O   . ALA A 1 83  ? 17.36428 24.92172 31.54645  1.000 56.72066  ? 83  ALA A O   1 
ATOM   668  C CB  . ALA A 1 83  ? 16.64955 21.67648 31.56044  1.000 57.14699  ? 83  ALA A CB  1 
ATOM   669  N N   . ASP A 1 84  ? 18.01895 23.83430 33.40651  1.000 59.39667  ? 84  ASP A N   1 
ATOM   670  C CA  . ASP A 1 84  ? 17.96105 25.05182 34.20938  1.000 60.17307  ? 84  ASP A CA  1 
ATOM   671  C C   . ASP A 1 84  ? 18.97186 26.08187 33.71743  1.000 59.67670  ? 84  ASP A C   1 
ATOM   672  O O   . ASP A 1 84  ? 18.65440 27.27296 33.61162  1.000 59.26153  ? 84  ASP A O   1 
ATOM   673  C CB  . ASP A 1 84  ? 18.19193 24.72335 35.68555  1.000 61.77003  ? 84  ASP A CB  1 
ATOM   674  C CG  . ASP A 1 84  ? 17.08404 23.86424 36.27376  1.000 64.92781  ? 84  ASP A CG  1 
ATOM   675  O OD1 . ASP A 1 84  ? 15.99072 23.80206 35.67189  1.000 62.13271  ? 84  ASP A OD1 1 
ATOM   676  O OD2 . ASP A 1 84  ? 17.30234 23.25809 37.34495  1.000 71.09147  ? 84  ASP A OD2 1 
ATOM   677  N N   . LYS A 1 85  ? 20.19233 25.64121 33.39865  1.000 59.52847  ? 85  LYS A N   1 
ATOM   678  C CA  . LYS A 1 85  ? 21.17720 26.55657 32.83096  1.000 60.34037  ? 85  LYS A CA  1 
ATOM   679  C C   . LYS A 1 85  ? 20.69461 27.11518 31.50144  1.000 60.99249  ? 85  LYS A C   1 
ATOM   680  O O   . LYS A 1 85  ? 20.91148 28.29388 31.19467  1.000 62.30567  ? 85  LYS A O   1 
ATOM   681  C CB  . LYS A 1 85  ? 22.51964 25.84565 32.65786  1.000 60.95161  ? 85  LYS A CB  1 
ATOM   682  N N   . LEU A 1 86  ? 20.02390 26.28034 30.70622  1.000 59.11431  ? 86  LEU A N   1 
ATOM   683  C CA  . LEU A 1 86  ? 19.49859 26.71751 29.41921  1.000 59.41725  ? 86  LEU A CA  1 
ATOM   684  C C   . LEU A 1 86  ? 18.42134 27.77874 29.59717  1.000 58.90068  ? 86  LEU A C   1 
ATOM   685  O O   . LEU A 1 86  ? 18.41685 28.79964 28.89839  1.000 60.06617  ? 86  LEU A O   1 
ATOM   686  C CB  . LEU A 1 86  ? 18.94826 25.51049 28.66330  1.000 57.79855  ? 86  LEU A CB  1 
ATOM   687  C CG  . LEU A 1 86  ? 18.80192 25.64289 27.15650  1.000 58.60396  ? 86  LEU A CG  1 
ATOM   688  C CD1 . LEU A 1 86  ? 20.09718 26.15914 26.57053  1.000 62.46348  ? 86  LEU A CD1 1 
ATOM   689  C CD2 . LEU A 1 86  ? 18.45163 24.28937 26.57630  1.000 55.48172  ? 86  LEU A CD2 1 
ATOM   690  N N   . VAL A 1 87  ? 17.48759 27.53990 30.52414  1.000 57.95303  ? 87  VAL A N   1 
ATOM   691  C CA  . VAL A 1 87  ? 16.44676 28.52015 30.83264  1.000 57.62698  ? 87  VAL A CA  1 
ATOM   692  C C   . VAL A 1 87  ? 17.07198 29.87337 31.14101  1.000 60.36750  ? 87  VAL A C   1 
ATOM   693  O O   . VAL A 1 87  ? 16.69483 30.90261 30.56786  1.000 61.46835  ? 87  VAL A O   1 
ATOM   694  C CB  . VAL A 1 87  ? 15.58238 28.02318 32.00673  1.000 55.31080  ? 87  VAL A CB  1 
ATOM   695  C CG1 . VAL A 1 87  ? 14.71545 29.15236 32.55925  1.000 52.67870  ? 87  VAL A CG1 1 
ATOM   696  C CG2 . VAL A 1 87  ? 14.73185 26.83632 31.57740  1.000 52.86998  ? 87  VAL A CG2 1 
ATOM   697  N N   . LYS A 1 88  ? 18.05575 29.87925 32.04345  1.000 62.04090  ? 88  LYS A N   1 
ATOM   698  C CA  . LYS A 1 88  ? 18.68280 31.12294 32.47870  1.000 64.21762  ? 88  LYS A CA  1 
ATOM   699  C C   . LYS A 1 88  ? 19.35368 31.84076 31.31394  1.000 65.39338  ? 88  LYS A C   1 
ATOM   700  O O   . LYS A 1 88  ? 19.15576 33.04449 31.11256  1.000 66.63183  ? 88  LYS A O   1 
ATOM   701  C CB  . LYS A 1 88  ? 19.69052 30.82101 33.58833  1.000 66.47395  ? 88  LYS A CB  1 
ATOM   702  C CG  . LYS A 1 88  ? 20.27985 32.04077 34.27408  1.000 69.12684  ? 88  LYS A CG  1 
ATOM   703  C CD  . LYS A 1 88  ? 21.10189 31.63066 35.48818  1.000 71.22244  ? 88  LYS A CD  1 
ATOM   704  C CE  . LYS A 1 88  ? 21.64200 32.84292 36.22824  1.000 76.24953  ? 88  LYS A CE  1 
ATOM   705  N NZ  . LYS A 1 88  ? 22.23297 32.48030 37.54890  1.000 72.58657  ? 88  LYS A NZ  1 
ATOM   706  N N   . LEU A 1 89  ? 20.14578 31.11189 30.52560  1.000 66.13070  ? 89  LEU A N   1 
ATOM   707  C CA  . LEU A 1 89  ? 20.86136 31.74392 29.42279  1.000 67.32321  ? 89  LEU A CA  1 
ATOM   708  C C   . LEU A 1 89  ? 19.90477 32.19283 28.32565  1.000 69.33331  ? 89  LEU A C   1 
ATOM   709  O O   . LEU A 1 89  ? 20.09528 33.25867 27.72810  1.000 71.72920  ? 89  LEU A O   1 
ATOM   710  C CB  . LEU A 1 89  ? 21.91612 30.78833 28.87090  1.000 69.66547  ? 89  LEU A CB  1 
ATOM   711  C CG  . LEU A 1 89  ? 23.06449 30.45565 29.82305  1.000 69.70778  ? 89  LEU A CG  1 
ATOM   712  C CD1 . LEU A 1 89  ? 24.13825 29.64978 29.10758  1.000 66.95424  ? 89  LEU A CD1 1 
ATOM   713  C CD2 . LEU A 1 89  ? 23.64471 31.72845 30.42851  1.000 66.79816  ? 89  LEU A CD2 1 
ATOM   714  N N   . LEU A 1 90  ? 18.86807 31.39749 28.05233  1.000 67.38335  ? 90  LEU A N   1 
ATOM   715  C CA  . LEU A 1 90  ? 17.87255 31.78450 27.05707  1.000 69.34613  ? 90  LEU A CA  1 
ATOM   716  C C   . LEU A 1 90  ? 17.15782 33.06396 27.46133  1.000 72.39540  ? 90  LEU A C   1 
ATOM   717  O O   . LEU A 1 90  ? 16.96944 33.97162 26.64253  1.000 75.26355  ? 90  LEU A O   1 
ATOM   718  C CB  . LEU A 1 90  ? 16.85627 30.66312 26.86951  1.000 65.21998  ? 90  LEU A CB  1 
ATOM   719  C CG  . LEU A 1 90  ? 17.09797 29.69000 25.72908  1.000 66.39399  ? 90  LEU A CG  1 
ATOM   720  C CD1 . LEU A 1 90  ? 15.97956 28.66802 25.71489  1.000 61.97603  ? 90  LEU A CD1 1 
ATOM   721  C CD2 . LEU A 1 90  ? 17.16767 30.45883 24.42115  1.000 68.86397  ? 90  LEU A CD2 1 
ATOM   722  N N   . ALA A 1 91  ? 16.72951 33.13839 28.72255  1.000 70.89338  ? 91  ALA A N   1 
ATOM   723  C CA  . ALA A 1 91  ? 15.97827 34.29564 29.19164  1.000 75.59235  ? 91  ALA A CA  1 
ATOM   724  C C   . ALA A 1 91  ? 16.78127 35.57636 29.01771  1.000 82.19527  ? 91  ALA A C   1 
ATOM   725  O O   . ALA A 1 91  ? 16.28189 36.56789 28.47176  1.000 84.93791  ? 91  ALA A O   1 
ATOM   726  C CB  . ALA A 1 91  ? 15.58721 34.09592 30.65321  1.000 76.41354  ? 91  ALA A CB  1 
ATOM   727  N N   . LYS A 1 92  ? 18.03432 35.56959 29.47810  1.000 79.31100  ? 92  LYS A N   1 
ATOM   728  C CA  . LYS A 1 92  ? 18.91170 36.71753 29.27793  1.000 82.85083  ? 92  LYS A CA  1 
ATOM   729  C C   . LYS A 1 92  ? 19.04100 37.05554 27.79915  1.000 82.94562  ? 92  LYS A C   1 
ATOM   730  O O   . LYS A 1 92  ? 18.95965 38.22481 27.40545  1.000 86.06003  ? 92  LYS A O   1 
ATOM   731  C CB  . LYS A 1 92  ? 20.28453 36.43109 29.88479  1.000 83.87998  ? 92  LYS A CB  1 
ATOM   732  C CG  . LYS A 1 92  ? 21.38665 37.33836 29.37497  1.000 89.78274  ? 92  LYS A CG  1 
ATOM   733  C CD  . LYS A 1 92  ? 22.72104 36.97845 30.00027  1.000 93.86693  ? 92  LYS A CD  1 
ATOM   734  C CE  . LYS A 1 92  ? 23.78841 37.99272 29.63619  1.000 99.74130  ? 92  LYS A CE  1 
ATOM   735  N NZ  . LYS A 1 92  ? 25.05615 37.74500 30.37468  1.000 107.61616 ? 92  LYS A NZ  1 
ATOM   736  N N   . GLY A 1 93  ? 19.22772 36.04030 26.96376  1.000 82.60710  ? 93  GLY A N   1 
ATOM   737  C CA  . GLY A 1 93  ? 19.41486 36.26479 25.54675  1.000 83.84649  ? 93  GLY A CA  1 
ATOM   738  C C   . GLY A 1 93  ? 20.85987 36.54555 25.20062  1.000 85.57352  ? 93  GLY A C   1 
ATOM   739  O O   . GLY A 1 93  ? 21.77175 35.96047 25.79479  1.000 83.93765  ? 93  GLY A O   1 
ATOM   740  N N   . GLU A 1 94  ? 21.07725 37.44580 24.23959  1.000 88.66412  ? 94  GLU A N   1 
ATOM   741  C CA  . GLU A 1 94  ? 22.41398 37.78107 23.74673  1.000 91.75880  ? 94  GLU A CA  1 
ATOM   742  C C   . GLU A 1 94  ? 23.16361 36.54283 23.26266  1.000 92.37059  ? 94  GLU A C   1 
ATOM   743  O O   . GLU A 1 94  ? 24.39755 36.50497 23.27072  1.000 93.58168  ? 94  GLU A O   1 
ATOM   744  C CB  . GLU A 1 94  ? 23.23055 38.52560 24.80964  1.000 86.81051  ? 94  GLU A CB  1 
ATOM   745  N N   . TYR A 1 95  ? 22.42649 35.51891 22.84202  1.000 93.92365  ? 95  TYR A N   1 
ATOM   746  C CA  . TYR A 1 95  ? 23.03705 34.30361 22.33076  1.000 87.71041  ? 95  TYR A CA  1 
ATOM   747  C C   . TYR A 1 95  ? 23.36242 34.45671 20.85298  1.000 85.12445  ? 95  TYR A C   1 
ATOM   748  O O   . TYR A 1 95  ? 22.70210 35.20027 20.12093  1.000 90.48063  ? 95  TYR A O   1 
ATOM   749  C CB  . TYR A 1 95  ? 22.11239 33.10331 22.54164  1.000 84.36445  ? 95  TYR A CB  1 
ATOM   750  C CG  . TYR A 1 95  ? 20.66674 33.34586 22.15020  1.000 84.83159  ? 95  TYR A CG  1 
ATOM   751  C CD1 . TYR A 1 95  ? 20.26578 33.29894 20.82002  1.000 82.80872  ? 95  TYR A CD1 1 
ATOM   752  C CD2 . TYR A 1 95  ? 19.70141 33.60309 23.11488  1.000 85.14412  ? 95  TYR A CD2 1 
ATOM   753  C CE1 . TYR A 1 95  ? 18.94657 33.51386 20.46178  1.000 81.52344  ? 95  TYR A CE1 1 
ATOM   754  C CE2 . TYR A 1 95  ? 18.38083 33.81621 22.76660  1.000 84.92747  ? 95  TYR A CE2 1 
ATOM   755  C CZ  . TYR A 1 95  ? 18.00868 33.77123 21.43952  1.000 81.77100  ? 95  TYR A CZ  1 
ATOM   756  O OH  . TYR A 1 95  ? 16.69376 33.98469 21.09193  1.000 80.45196  ? 95  TYR A OH  1 
ATOM   757  N N   . GLN A 1 96  ? 24.39926 33.74943 20.41929  1.000 79.75926  ? 96  GLN A N   1 
ATOM   758  C CA  . GLN A 1 96  ? 24.73234 33.71566 19.00655  1.000 74.59396  ? 96  GLN A CA  1 
ATOM   759  C C   . GLN A 1 96  ? 23.88674 32.67386 18.28532  1.000 68.13580  ? 96  GLN A C   1 
ATOM   760  O O   . GLN A 1 96  ? 23.43542 31.68656 18.87428  1.000 65.66346  ? 96  GLN A O   1 
ATOM   761  C CB  . GLN A 1 96  ? 26.21499 33.40760 18.80489  1.000 75.78976  ? 96  GLN A CB  1 
ATOM   762  C CG  . GLN A 1 96  ? 27.15160 34.53756 19.17683  0.700 78.51829  ? 96  GLN A CG  1 
ATOM   763  C CD  . GLN A 1 96  ? 28.60073 34.16728 18.94673  0.600 80.47125  ? 96  GLN A CD  1 
ATOM   764  O OE1 . GLN A 1 96  ? 28.94535 32.98756 18.86783  0.600 78.97172  ? 96  GLN A OE1 1 
ATOM   765  N NE2 . GLN A 1 96  ? 29.45781 35.17309 18.82762  0.600 83.49368  ? 96  GLN A NE2 1 
ATOM   766  N N   . LYS A 1 97  ? 23.67389 32.90566 16.99527  1.000 62.39480  ? 97  LYS A N   1 
ATOM   767  C CA  . LYS A 1 97  ? 22.95323 31.97921 16.13771  1.000 56.75194  ? 97  LYS A CA  1 
ATOM   768  C C   . LYS A 1 97  ? 23.91832 31.35630 15.14161  1.000 54.22800  ? 97  LYS A C   1 
ATOM   769  O O   . LYS A 1 97  ? 24.81819 32.03141 14.63284  1.000 55.02129  ? 97  LYS A O   1 
ATOM   770  C CB  . LYS A 1 97  ? 21.81673 32.68350 15.39252  1.000 55.31103  ? 97  LYS A CB  1 
ATOM   771  C CG  . LYS A 1 97  ? 20.80577 33.36006 16.30612  1.000 59.44453  ? 97  LYS A CG  1 
ATOM   772  C CD  . LYS A 1 97  ? 19.74796 34.11220 15.51409  1.000 58.11360  ? 97  LYS A CD  1 
ATOM   773  C CE  . LYS A 1 97  ? 19.45759 35.46172 16.14932  1.000 60.48407  ? 97  LYS A CE  1 
ATOM   774  N NZ  . LYS A 1 97  ? 18.34622 36.17532 15.46335  1.000 67.90126  ? 97  LYS A NZ  1 
ATOM   775  N N   . VAL A 1 98  ? 23.73726 30.06423 14.88360  1.000 50.58110  ? 98  VAL A N   1 
ATOM   776  C CA  . VAL A 1 98  ? 24.43023 29.36199 13.81230  1.000 48.54664  ? 98  VAL A CA  1 
ATOM   777  C C   . VAL A 1 98  ? 23.37726 28.83264 12.85172  1.000 46.82970  ? 98  VAL A C   1 
ATOM   778  O O   . VAL A 1 98  ? 22.27726 28.45280 13.26831  1.000 44.32541  ? 98  VAL A O   1 
ATOM   779  C CB  . VAL A 1 98  ? 25.32590 28.22012 14.34018  1.000 51.52687  ? 98  VAL A CB  1 
ATOM   780  C CG1 . VAL A 1 98  ? 26.36452 28.76808 15.30071  1.000 53.79237  ? 98  VAL A CG1 1 
ATOM   781  C CG2 . VAL A 1 98  ? 24.49447 27.13906 15.01260  1.000 51.49552  ? 98  VAL A CG2 1 
ATOM   782  N N   . SER A 1 99  ? 23.70667 28.82990 11.56546  1.000 44.04020  ? 99  SER A N   1 
ATOM   783  C CA  . SER A 1 99  ? 22.77040 28.45255 10.52034  1.000 44.31318  ? 99  SER A CA  1 
ATOM   784  C C   . SER A 1 99  ? 23.29933 27.24760 9.75536   1.000 42.33333  ? 99  SER A C   1 
ATOM   785  O O   . SER A 1 99  ? 24.48997 27.17393 9.43347   1.000 40.54402  ? 99  SER A O   1 
ATOM   786  C CB  . SER A 1 99  ? 22.52225 29.62155 9.55975   1.000 46.30696  ? 99  SER A CB  1 
ATOM   787  O OG  . SER A 1 99  ? 22.06798 30.76447 10.26107  1.000 48.55465  ? 99  SER A OG  1 
ATOM   788  N N   . TYR A 1 100 ? 22.40506 26.29821 9.47760   1.000 40.10102  ? 100 TYR A N   1 
ATOM   789  C CA  . TYR A 1 100 ? 22.68750 25.12625 8.66867   1.000 38.51587  ? 100 TYR A CA  1 
ATOM   790  C C   . TYR A 1 100 ? 21.92004 25.19846 7.35066   1.000 38.52073  ? 100 TYR A C   1 
ATOM   791  O O   . TYR A 1 100 ? 20.79258 25.70250 7.31980   1.000 36.19894  ? 100 TYR A O   1 
ATOM   792  C CB  . TYR A 1 100 ? 22.30251 23.83432 9.39895   1.000 38.17184  ? 100 TYR A CB  1 
ATOM   793  C CG  . TYR A 1 100 ? 23.27705 23.38398 10.46949  1.000 38.15654  ? 100 TYR A CG  1 
ATOM   794  C CD1 . TYR A 1 100 ? 24.40795 24.13233 10.77867  1.000 40.31716  ? 100 TYR A CD1 1 
ATOM   795  C CD2 . TYR A 1 100 ? 23.07203 22.19284 11.15586  1.000 39.23625  ? 100 TYR A CD2 1 
ATOM   796  C CE1 . TYR A 1 100 ? 25.29860 23.71331 11.75885  1.000 42.46784  ? 100 TYR A CE1 1 
ATOM   797  C CE2 . TYR A 1 100 ? 23.95494 21.76543 12.13334  1.000 39.88490  ? 100 TYR A CE2 1 
ATOM   798  C CZ  . TYR A 1 100 ? 25.06437 22.52809 12.42896  1.000 42.62326  ? 100 TYR A CZ  1 
ATOM   799  O OH  . TYR A 1 100 ? 25.94291 22.10147 13.39659  1.000 46.03799  ? 100 TYR A OH  1 
ATOM   800  N N   . PRO A 1 101 ? 22.49565 24.70826 6.25485   1.000 36.37827  ? 101 PRO A N   1 
ATOM   801  C CA  . PRO A 1 101 ? 21.79125 24.74710 4.96908   1.000 35.62696  ? 101 PRO A CA  1 
ATOM   802  C C   . PRO A 1 101 ? 20.66696 23.72599 4.92480   1.000 35.66674  ? 101 PRO A C   1 
ATOM   803  O O   . PRO A 1 101 ? 20.65223 22.73591 5.66248   1.000 33.06118  ? 101 PRO A O   1 
ATOM   804  C CB  . PRO A 1 101 ? 22.88353 24.40628 3.94557   1.000 34.90854  ? 101 PRO A CB  1 
ATOM   805  C CG  . PRO A 1 101 ? 24.18763 24.51510 4.69581   1.000 38.04824  ? 101 PRO A CG  1 
ATOM   806  C CD  . PRO A 1 101 ? 23.84990 24.15884 6.11070   1.000 34.77146  ? 101 PRO A CD  1 
ATOM   807  N N   . LEU A 1 102 ? 19.71615 23.98090 4.02810   1.000 31.17035  ? 102 LEU A N   1 
ATOM   808  C CA  . LEU A 1 102 ? 18.55358 23.12674 3.85138   1.000 32.44405  ? 102 LEU A CA  1 
ATOM   809  C C   . LEU A 1 102 ? 18.41732 22.75855 2.38065   1.000 32.85130  ? 102 LEU A C   1 
ATOM   810  O O   . LEU A 1 102 ? 19.00352 23.39416 1.50232   1.000 29.23410  ? 102 LEU A O   1 
ATOM   811  C CB  . LEU A 1 102 ? 17.26903 23.80889 4.33642   1.000 33.98013  ? 102 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 102 ? 17.25849 24.30631 5.78741   1.000 35.05058  ? 102 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 102 ? 16.03244 25.16036 6.03304   1.000 36.74971  ? 102 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 102 ? 17.30718 23.13861 6.76231   1.000 33.54286  ? 102 LEU A CD2 1 
ATOM   815  N N   . LEU A 1 103 ? 17.62258 21.72457 2.12874   1.000 30.43133  ? 103 LEU A N   1 
ATOM   816  C CA  . LEU A 1 103 ? 17.41471 21.17938 0.79362   1.000 33.96240  ? 103 LEU A CA  1 
ATOM   817  C C   . LEU A 1 103 ? 15.99837 21.48450 0.32520   1.000 35.40815  ? 103 LEU A C   1 
ATOM   818  O O   . LEU A 1 103 ? 15.03260 21.24310 1.05648   1.000 33.53146  ? 103 LEU A O   1 
ATOM   819  C CB  . LEU A 1 103 ? 17.64407 19.66944 0.78937   1.000 32.77154  ? 103 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 103 ? 17.25108 18.93368 -0.49293  1.000 33.85933  ? 103 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 103 ? 18.21511 19.28546 -1.61556  1.000 32.16109  ? 103 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 103 ? 17.20316 17.43299 -0.25812  1.000 33.58693  ? 103 LEU A CD2 1 
ATOM   823  N N   . LYS A 1 104 ? 15.87432 22.00305 -0.89319  1.000 34.59842  ? 104 LYS A N   1 
ATOM   824  C CA  . LYS A 1 104 ? 14.57539 22.26409 -1.49883  1.000 34.98925  ? 104 LYS A CA  1 
ATOM   825  C C   . LYS A 1 104 ? 14.26369 21.17465 -2.51913  1.000 37.67237  ? 104 LYS A C   1 
ATOM   826  O O   . LYS A 1 104 ? 15.09268 20.86946 -3.38504  1.000 34.98988  ? 104 LYS A O   1 
ATOM   827  C CB  . LYS A 1 104 ? 14.55155 23.64368 -2.15771  1.000 38.12886  ? 104 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 104 ? 13.26069 23.99104 -2.89128  1.000 40.44044  ? 104 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 104 ? 13.45204 25.27074 -3.70894  1.000 43.20247  ? 104 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 104 ? 12.26002 25.57018 -4.60388  1.000 47.83794  ? 104 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 104 ? 11.21544 26.36704 -3.91261  1.000 54.00667  ? 104 LYS A NZ  1 
ATOM   832  N N   . THR A 1 105 ? 13.07788 20.58163 -2.39966  1.000 37.32425  ? 105 THR A N   1 
ATOM   833  C CA  . THR A 1 105 ? 12.58897 19.56388 -3.32119  1.000 37.56170  ? 105 THR A CA  1 
ATOM   834  C C   . THR A 1 105 ? 11.33974 20.09287 -4.00796  1.000 39.32558  ? 105 THR A C   1 
ATOM   835  O O   . THR A 1 105 ? 10.39362 20.51318 -3.33599  1.000 38.47031  ? 105 THR A O   1 
ATOM   836  C CB  . THR A 1 105 ? 12.25662 18.25505 -2.59410  1.000 38.10648  ? 105 THR A CB  1 
ATOM   837  O OG1 . THR A 1 105 ? 13.40033 17.79620 -1.86411  1.000 38.38425  ? 105 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 105 ? 11.83205 17.18487 -3.58465  1.000 37.96355  ? 105 THR A CG2 1 
ATOM   839  N N   . THR A 1 106 ? 11.33447 20.07743 -5.33650  1.000 37.50580  ? 106 THR A N   1 
ATOM   840  C CA  . THR A 1 106 ? 10.16458 20.46574 -6.11140  1.000 39.46162  ? 106 THR A CA  1 
ATOM   841  C C   . THR A 1 106 ? 9.64330  19.25372 -6.86828  1.000 40.97310  ? 106 THR A C   1 
ATOM   842  O O   . THR A 1 106 ? 10.40159 18.58870 -7.58276  1.000 40.34944  ? 106 THR A O   1 
ATOM   843  C CB  . THR A 1 106 ? 10.49107 21.59687 -7.08747  1.000 41.87260  ? 106 THR A CB  1 
ATOM   844  O OG1 . THR A 1 106 ? 11.07813 22.68985 -6.37280  1.000 41.39908  ? 106 THR A OG1 1 
ATOM   845  C CG2 . THR A 1 106 ? 9.21948  22.07935 -7.78466  1.000 43.23072  ? 106 THR A CG2 1 
ATOM   846  N N   . VAL A 1 107 ? 8.35701  18.96588 -6.70627  1.000 41.22323  ? 107 VAL A N   1 
ATOM   847  C CA  . VAL A 1 107 ? 7.70672  17.85738 -7.39233  1.000 43.99365  ? 107 VAL A CA  1 
ATOM   848  C C   . VAL A 1 107 ? 6.71721  18.44398 -8.38777  1.000 46.77521  ? 107 VAL A C   1 
ATOM   849  O O   . VAL A 1 107 ? 5.77487  19.14663 -7.99917  1.000 48.54741  ? 107 VAL A O   1 
ATOM   850  C CB  . VAL A 1 107 ? 7.00993  16.90635 -6.40870  1.000 44.13915  ? 107 VAL A CB  1 
ATOM   851  C CG1 . VAL A 1 107 ? 6.49679  15.67491 -7.13955  1.000 46.44968  ? 107 VAL A CG1 1 
ATOM   852  C CG2 . VAL A 1 107 ? 7.96503  16.50690 -5.29118  1.000 43.41742  ? 107 VAL A CG2 1 
ATOM   853  N N   . LYS A 1 108 ? 6.93219  18.16122 -9.66713  1.000 47.70474  ? 108 LYS A N   1 
ATOM   854  C CA  . LYS A 1 108 ? 6.05767  18.63212 -10.73079 1.000 51.38934  ? 108 LYS A CA  1 
ATOM   855  C C   . LYS A 1 108 ? 5.18050  17.49034 -11.22916 1.000 54.09610  ? 108 LYS A C   1 
ATOM   856  O O   . LYS A 1 108 ? 5.61328  16.33493 -11.27485 1.000 52.67814  ? 108 LYS A O   1 
ATOM   857  C CB  . LYS A 1 108 ? 6.87287  19.21425 -11.88836 1.000 49.70745  ? 108 LYS A CB  1 
ATOM   858  N N   . TYR A 1 109 ? 3.94249  17.82391 -11.59938 1.000 57.70085  ? 109 TYR A N   1 
ATOM   859  C CA  . TYR A 1 109 ? 2.98965  16.84268 -12.10669 1.000 60.08393  ? 109 TYR A CA  1 
ATOM   860  C C   . TYR A 1 109 ? 2.46955  17.24379 -13.48178 1.000 65.16890  ? 109 TYR A C   1 
ATOM   861  O O   . TYR A 1 109 ? 3.12972  17.98883 -14.21351 1.000 65.53185  ? 109 TYR A O   1 
ATOM   862  C CB  . TYR A 1 109 ? 1.80718  16.68182 -11.14761 1.000 61.98711  ? 109 TYR A CB  1 
ATOM   863  C CG  . TYR A 1 109 ? 2.18208  16.56551 -9.68564  1.000 58.30313  ? 109 TYR A CG  1 
ATOM   864  C CD1 . TYR A 1 109 ? 2.28512  17.69516 -8.88417  1.000 58.48522  ? 109 TYR A CD1 1 
ATOM   865  C CD2 . TYR A 1 109 ? 2.41381  15.32701 -9.10403  1.000 55.08522  ? 109 TYR A CD2 1 
ATOM   866  C CE1 . TYR A 1 109 ? 2.61855  17.59818 -7.54885  1.000 55.70947  ? 109 TYR A CE1 1 
ATOM   867  C CE2 . TYR A 1 109 ? 2.74651  15.21838 -7.76649  1.000 55.07660  ? 109 TYR A CE2 1 
ATOM   868  C CZ  . TYR A 1 109 ? 2.84808  16.35818 -6.99475  1.000 54.41619  ? 109 TYR A CZ  1 
ATOM   869  O OH  . TYR A 1 109 ? 3.17999  16.25835 -5.66415  1.000 55.57998  ? 109 TYR A OH  1 
ATOM   870  N N   . GLY A 1 110 ? 1.28165  16.75790 -13.83292 1.000 70.09527  ? 110 GLY A N   1 
ATOM   871  C CA  . GLY A 1 110 ? 0.63057  17.12274 -15.07704 1.000 68.25771  ? 110 GLY A CA  1 
ATOM   872  C C   . GLY A 1 110 ? -0.84280 17.43647 -14.89105 1.000 72.57306  ? 110 GLY A C   1 
ATOM   873  O O   . GLY A 1 110 ? -1.52248 17.88912 -15.81646 1.000 68.65945  ? 110 GLY A O   1 
ATOM   874  N N   . LYS A 1 114 ? 0.84379  21.46057 -12.15234 1.000 79.52841  ? 114 LYS A N   1 
ATOM   875  C CA  . LYS A 1 114 ? 0.83395  21.72097 -10.71630 1.000 75.70746  ? 114 LYS A CA  1 
ATOM   876  C C   . LYS A 1 114 ? 2.18923  21.37063 -10.09679 1.000 78.10554  ? 114 LYS A C   1 
ATOM   877  O O   . LYS A 1 114 ? 2.95039  20.57555 -10.65424 1.000 70.51130  ? 114 LYS A O   1 
ATOM   878  C CB  . LYS A 1 114 ? -0.29624 20.93984 -10.04110 1.000 74.06685  ? 114 LYS A CB  1 
ATOM   879  C CG  . LYS A 1 114 ? -0.30760 19.45865 -10.37500 1.000 76.47357  ? 114 LYS A CG  1 
ATOM   880  C CD  . LYS A 1 114 ? -1.54127 18.75737 -9.82329  1.000 79.31028  ? 114 LYS A CD  1 
ATOM   881  C CE  . LYS A 1 114 ? -2.75687 19.00167 -10.70218 1.000 86.47837  ? 114 LYS A CE  1 
ATOM   882  N NZ  . LYS A 1 114 ? -2.51811 18.56032 -12.10500 1.000 87.82212  ? 114 LYS A NZ  1 
ATOM   883  N N   . GLU A 1 115 ? 2.48697  21.96975 -8.94420  1.000 62.98766  ? 115 GLU A N   1 
ATOM   884  C CA  . GLU A 1 115 ? 3.81330  21.87416 -8.35284  1.000 57.45016  ? 115 GLU A CA  1 
ATOM   885  C C   . GLU A 1 115 ? 3.70470  21.87098 -6.83542  1.000 54.63681  ? 115 GLU A C   1 
ATOM   886  O O   . GLU A 1 115 ? 2.90209  22.61187 -6.26031  1.000 53.76800  ? 115 GLU A O   1 
ATOM   887  C CB  . GLU A 1 115 ? 4.70040  23.03976 -8.80100  1.000 57.17139  ? 115 GLU A CB  1 
ATOM   888  C CG  . GLU A 1 115 ? 6.03225  22.63428 -9.38852  1.000 58.10979  ? 115 GLU A CG  1 
ATOM   889  C CD  . GLU A 1 115 ? 6.90488  23.83309 -9.71250  1.000 62.19134  ? 115 GLU A CD  1 
ATOM   890  O OE1 . GLU A 1 115 ? 7.04339  24.71832 -8.83926  1.000 61.73014  ? 115 GLU A OE1 1 
ATOM   891  O OE2 . GLU A 1 115 ? 7.44295  23.89483 -10.84011 1.000 64.02480  ? 115 GLU A OE2 1 
ATOM   892  N N   . ALA A 1 116 ? 4.52400  21.04116 -6.19622  1.000 50.34397  ? 116 ALA A N   1 
ATOM   893  C CA  . ALA A 1 116 ? 4.65433  21.02508 -4.74791  1.000 48.33742  ? 116 ALA A CA  1 
ATOM   894  C C   . ALA A 1 116 ? 6.12188  21.17335 -4.38241  1.000 46.08083  ? 116 ALA A C   1 
ATOM   895  O O   . ALA A 1 116 ? 6.99320  20.58480 -5.03080  1.000 44.29930  ? 116 ALA A O   1 
ATOM   896  C CB  . ALA A 1 116 ? 4.08983  19.73504 -4.14619  1.000 48.99791  ? 116 ALA A CB  1 
ATOM   897  N N   . THR A 1 117 ? 6.39507  21.96273 -3.34624  1.000 45.05012  ? 117 THR A N   1 
ATOM   898  C CA  . THR A 1 117 ? 7.75214  22.17025 -2.86320  1.000 43.44404  ? 117 THR A CA  1 
ATOM   899  C C   . THR A 1 117 ? 7.84427  21.79515 -1.38964  1.000 44.04305  ? 117 THR A C   1 
ATOM   900  O O   . THR A 1 117 ? 6.91386  22.04273 -0.61411  1.000 42.26272  ? 117 THR A O   1 
ATOM   901  C CB  . THR A 1 117 ? 8.20696  23.62111 -3.06705  1.000 45.07086  ? 117 THR A CB  1 
ATOM   902  O OG1 . THR A 1 117 ? 7.37558  24.50215 -2.30267  1.000 49.41803  ? 117 THR A OG1 1 
ATOM   903  C CG2 . THR A 1 117 ? 8.12473  24.00446 -4.53289  1.000 46.30015  ? 117 THR A CG2 1 
ATOM   904  N N   . TYR A 1 118 ? 8.97155  21.19075 -1.01476  1.000 42.58731  ? 118 TYR A N   1 
ATOM   905  C CA  . TYR A 1 118 ? 9.21774  20.73932 0.34644   1.000 41.16585  ? 118 TYR A CA  1 
ATOM   906  C C   . TYR A 1 118 ? 10.61442 21.15914 0.77373   1.000 40.30424  ? 118 TYR A C   1 
ATOM   907  O O   . TYR A 1 118 ? 11.51913 21.30134 -0.05308  1.000 39.70948  ? 118 TYR A O   1 
ATOM   908  C CB  . TYR A 1 118 ? 9.08138  19.21140 0.47581   1.000 40.85457  ? 118 TYR A CB  1 
ATOM   909  C CG  . TYR A 1 118 ? 7.80313  18.67050 -0.11617  1.000 43.89660  ? 118 TYR A CG  1 
ATOM   910  C CD1 . TYR A 1 118 ? 7.72429  18.34024 -1.46402  1.000 44.08629  ? 118 TYR A CD1 1 
ATOM   911  C CD2 . TYR A 1 118 ? 6.66937  18.50296 0.66711   1.000 44.52219  ? 118 TYR A CD2 1 
ATOM   912  C CE1 . TYR A 1 118 ? 6.54424  17.85459 -2.01433  1.000 45.65656  ? 118 TYR A CE1 1 
ATOM   913  C CE2 . TYR A 1 118 ? 5.49034  18.01734 0.12798   1.000 46.43867  ? 118 TYR A CE2 1 
ATOM   914  C CZ  . TYR A 1 118 ? 5.43247  17.69382 -1.21083  1.000 47.10366  ? 118 TYR A CZ  1 
ATOM   915  O OH  . TYR A 1 118 ? 4.25786  17.21016 -1.74594  1.000 49.81605  ? 118 TYR A OH  1 
ATOM   916  N N   . LEU A 1 119 ? 10.78266 21.34266 2.07954   1.000 39.03267  ? 119 LEU A N   1 
ATOM   917  C CA  . LEU A 1 119 ? 12.05603 21.71655 2.67658   1.000 38.63448  ? 119 LEU A CA  1 
ATOM   918  C C   . LEU A 1 119 ? 12.52393 20.56940 3.56074   1.000 36.37165  ? 119 LEU A C   1 
ATOM   919  O O   . LEU A 1 119 ? 11.73132 20.01751 4.32833   1.000 37.60313  ? 119 LEU A O   1 
ATOM   920  C CB  . LEU A 1 119 ? 11.90123 23.00378 3.48873   1.000 41.23442  ? 119 LEU A CB  1 
ATOM   921  C CG  . LEU A 1 119 ? 13.03969 24.01843 3.53881   1.000 41.10524  ? 119 LEU A CG  1 
ATOM   922  C CD1 . LEU A 1 119 ? 13.45460 24.42481 2.14684   1.000 41.00024  ? 119 LEU A CD1 1 
ATOM   923  C CD2 . LEU A 1 119 ? 12.58442 25.23467 4.33259   1.000 44.79914  ? 119 LEU A CD2 1 
ATOM   924  N N   . ALA A 1 120 ? 13.79592 20.19498 3.44543   1.000 33.20442  ? 120 ALA A N   1 
ATOM   925  C CA  . ALA A 1 120 ? 14.33812 19.08663 4.21927   1.000 33.13461  ? 120 ALA A CA  1 
ATOM   926  C C   . ALA A 1 120 ? 15.50328 19.56180 5.07594   1.000 33.69742  ? 120 ALA A C   1 
ATOM   927  O O   . ALA A 1 120 ? 16.34611 20.33977 4.61764   1.000 30.77546  ? 120 ALA A O   1 
ATOM   928  C CB  . ALA A 1 120 ? 14.79358 17.93666 3.30890   1.000 33.91304  ? 120 ALA A CB  1 
ATOM   929  N N   . LEU A 1 121 ? 15.52915 19.10545 6.33110   1.000 31.33432  ? 121 LEU A N   1 
ATOM   930  C CA  . LEU A 1 121 ? 16.67375 19.30674 7.21137   1.000 31.44687  ? 121 LEU A CA  1 
ATOM   931  C C   . LEU A 1 121 ? 17.64199 18.13530 7.16461   1.000 29.13421  ? 121 LEU A C   1 
ATOM   932  O O   . LEU A 1 121 ? 18.85787 18.33581 7.27514   1.000 30.25892  ? 121 LEU A O   1 
ATOM   933  C CB  . LEU A 1 121 ? 16.20336 19.52859 8.65880   1.000 30.34727  ? 121 LEU A CB  1 
ATOM   934  C CG  . LEU A 1 121 ? 17.28338 19.65264 9.74136   1.000 32.72637  ? 121 LEU A CG  1 
ATOM   935  C CD1 . LEU A 1 121 ? 18.22881 20.79136 9.41967   1.000 32.26963  ? 121 LEU A CD1 1 
ATOM   936  C CD2 . LEU A 1 121 ? 16.66093 19.83890 11.14285  1.000 31.67963  ? 121 LEU A CD2 1 
ATOM   937  N N   . ASN A 1 122 ? 17.13386 16.91473 7.00011   1.000 27.02436  ? 122 ASN A N   1 
ATOM   938  C CA  . ASN A 1 122 ? 18.00227 15.75635 6.82731   1.000 28.46234  ? 122 ASN A CA  1 
ATOM   939  C C   . ASN A 1 122 ? 18.17431 15.41868 5.34786   1.000 28.71885  ? 122 ASN A C   1 
ATOM   940  O O   . ASN A 1 122 ? 19.26802 15.58353 4.79961   1.000 27.28938  ? 122 ASN A O   1 
ATOM   941  C CB  . ASN A 1 122 ? 17.45417 14.54684 7.58423   1.000 28.49769  ? 122 ASN A CB  1 
ATOM   942  C CG  . ASN A 1 122 ? 18.02881 14.42201 8.99217   1.000 32.96323  ? 122 ASN A CG  1 
ATOM   943  O OD1 . ASN A 1 122 ? 18.82875 15.25137 9.43774   1.000 30.39836  ? 122 ASN A OD1 1 
ATOM   944  N ND2 . ASN A 1 122 ? 17.62606 13.37453 9.69140   1.000 32.71540  ? 122 ASN A ND2 1 
ATOM   945  N N   . GLU A 1 123 ? 17.12062 14.93513 4.69490   1.000 27.30020  ? 123 GLU A N   1 
ATOM   946  C CA  . GLU A 1 123 ? 17.25898 14.50078 3.30683   1.000 29.92331  ? 123 GLU A CA  1 
ATOM   947  C C   . GLU A 1 123 ? 15.88424 14.31691 2.68265   1.000 31.63516  ? 123 GLU A C   1 
ATOM   948  O O   . GLU A 1 123 ? 14.85692 14.30748 3.36718   1.000 29.75606  ? 123 GLU A O   1 
ATOM   949  C CB  . GLU A 1 123 ? 18.05350 13.19433 3.19433   1.000 28.39794  ? 123 GLU A CB  1 
ATOM   950  C CG  . GLU A 1 123 ? 17.26486 11.95226 3.59824   1.000 27.44525  ? 123 GLU A CG  1 
ATOM   951  C CD  . GLU A 1 123 ? 17.06227 11.85408 5.10760   1.000 31.91990  ? 123 GLU A CD  1 
ATOM   952  O OE1 . GLU A 1 123 ? 18.07004 11.73388 5.83483   1.000 26.07466  ? 123 GLU A OE1 1 
ATOM   953  O OE2 . GLU A 1 123 ? 15.89889 11.90903 5.56337   1.000 30.17097  ? 123 GLU A OE2 1 
ATOM   954  N N   . SER A 1 124 ? 15.88886 14.17084 1.35850   1.000 30.05957  ? 124 SER A N   1 
ATOM   955  C CA  . SER A 1 124 ? 14.73644 13.72837 0.58762   1.000 32.56731  ? 124 SER A CA  1 
ATOM   956  C C   . SER A 1 124 ? 15.14367 12.51044 -0.22769  1.000 32.49886  ? 124 SER A C   1 
ATOM   957  O O   . SER A 1 124 ? 16.21155 12.50856 -0.84940  1.000 32.37091  ? 124 SER A O   1 
ATOM   958  C CB  . SER A 1 124 ? 14.22381 14.83315 -0.33875  1.000 35.24338  ? 124 SER A CB  1 
ATOM   959  O OG  . SER A 1 124 ? 13.16855 14.35758 -1.15820  1.000 35.97266  ? 124 SER A OG  1 
ATOM   960  N N   . THR A 1 125 ? 14.30978 11.47405 -0.21842  1.000 31.70285  ? 125 THR A N   1 
ATOM   961  C CA  . THR A 1 125 ? 14.60134 10.26230 -0.96931  1.000 33.20547  ? 125 THR A CA  1 
ATOM   962  C C   . THR A 1 125 ? 13.47232 9.97280  -1.94806  1.000 34.70312  ? 125 THR A C   1 
ATOM   963  O O   . THR A 1 125 ? 12.33158 10.40526 -1.76333  1.000 33.66945  ? 125 THR A O   1 
ATOM   964  C CB  . THR A 1 125 ? 14.80544 9.04356  -0.05466  1.000 33.38323  ? 125 THR A CB  1 
ATOM   965  O OG1 . THR A 1 125 ? 13.53291 8.56099  0.38649   1.000 34.28005  ? 125 THR A OG1 1 
ATOM   966  C CG2 . THR A 1 125 ? 15.65813 9.40699  1.15960   1.000 32.21908  ? 125 THR A CG2 1 
ATOM   967  N N   . VAL A 1 126 ? 13.80925 9.23687  -3.00347  1.000 35.89936  ? 126 VAL A N   1 
ATOM   968  C CA  . VAL A 1 126 ? 12.84362 8.80425  -4.00649  1.000 34.05015  ? 126 VAL A CA  1 
ATOM   969  C C   . VAL A 1 126 ? 12.98235 7.30127  -4.18364  1.000 34.90245  ? 126 VAL A C   1 
ATOM   970  O O   . VAL A 1 126 ? 14.09631 6.79299  -4.35687  1.000 32.56637  ? 126 VAL A O   1 
ATOM   971  C CB  . VAL A 1 126 ? 13.04083 9.51495  -5.35759  1.000 36.78847  ? 126 VAL A CB  1 
ATOM   972  C CG1 . VAL A 1 126 ? 11.92318 9.12550  -6.31180  1.000 35.50735  ? 126 VAL A CG1 1 
ATOM   973  C CG2 . VAL A 1 126 ? 13.07571 11.01155 -5.17455  1.000 37.85285  ? 126 VAL A CG2 1 
ATOM   974  N N   . LYS A 1 127 ? 11.85459 6.59817  -4.12337  1.000 35.84898  ? 127 LYS A N   1 
ATOM   975  C CA  . LYS A 1 127 ? 11.76376 5.17222  -4.39695  1.000 38.73025  ? 127 LYS A CA  1 
ATOM   976  C C   . LYS A 1 127 ? 10.53869 4.95159  -5.27752  1.000 41.61165  ? 127 LYS A C   1 
ATOM   977  O O   . LYS A 1 127 ? 9.71820  5.85397  -5.46539  1.000 40.71531  ? 127 LYS A O   1 
ATOM   978  C CB  . LYS A 1 127 ? 11.67659 4.35163  -3.09707  1.000 40.09027  ? 127 LYS A CB  1 
ATOM   979  C CG  . LYS A 1 127 ? 12.84135 4.58608  -2.12943  1.000 38.83345  ? 127 LYS A CG  1 
ATOM   980  C CD  . LYS A 1 127 ? 12.63691 3.89630  -0.77655  1.000 42.10106  ? 127 LYS A CD  1 
ATOM   981  C CE  . LYS A 1 127 ? 13.81155 4.18980  0.16618   1.000 48.01532  ? 127 LYS A CE  1 
ATOM   982  N NZ  . LYS A 1 127 ? 13.62904 3.68882  1.56746   1.000 42.96152  ? 127 LYS A NZ  1 
ATOM   983  N N   . SER A 1 128 ? 10.41171 3.74445  -5.82412  1.000 43.51892  ? 128 SER A N   1 
ATOM   984  C CA  . SER A 1 128 ? 9.27694  3.45291  -6.68766  1.000 48.17285  ? 128 SER A CA  1 
ATOM   985  C C   . SER A 1 128 ? 8.05569  3.05599  -5.85876  1.000 52.37618  ? 128 SER A C   1 
ATOM   986  O O   . SER A 1 128 ? 8.14011  2.79742  -4.65495  1.000 51.75627  ? 128 SER A O   1 
ATOM   987  C CB  . SER A 1 128 ? 9.61788  2.34088  -7.67803  1.000 50.83621  ? 128 SER A CB  1 
ATOM   988  O OG  . SER A 1 128 ? 9.57906  1.07185  -7.04651  1.000 54.85960  ? 128 SER A OG  1 
ATOM   989  N N   . SER A 1 129 ? 6.90147  3.00258  -6.53163  1.000 55.14762  ? 129 SER A N   1 
ATOM   990  C CA  . SER A 1 129 ? 5.66007  2.60456  -5.87699  1.000 60.02641  ? 129 SER A CA  1 
ATOM   991  C C   . SER A 1 129 ? 5.59327  1.10554  -5.61270  1.000 66.30473  ? 129 SER A C   1 
ATOM   992  O O   . SER A 1 129 ? 4.79300  0.67200  -4.77763  1.000 77.45383  ? 129 SER A O   1 
ATOM   993  C CB  . SER A 1 129 ? 4.45951  3.02765  -6.72383  1.000 60.36535  ? 129 SER A CB  1 
ATOM   994  O OG  . SER A 1 129 ? 4.45575  2.35031  -7.96793  1.000 63.27239  ? 129 SER A OG  1 
ATOM   995  N N   . GLY A 1 130 ? 6.40146  0.30801  -6.30475  1.000 67.91719  ? 130 GLY A N   1 
ATOM   996  C CA  . GLY A 1 130 ? 6.40533  -1.12677 -6.09961  1.000 71.46821  ? 130 GLY A CA  1 
ATOM   997  C C   . GLY A 1 130 ? 7.27488  -1.86238 -7.09691  1.000 74.03657  ? 130 GLY A C   1 
ATOM   998  O O   . GLY A 1 130 ? 8.01803  -2.78026 -6.73500  1.000 73.68467  ? 130 GLY A O   1 
ATOM   999  N N   . GLY A 1 131 ? 7.19143  -1.46077 -8.36169  1.000 65.67547  ? 131 GLY A N   1 
ATOM   1000 C CA  . GLY A 1 131 ? 7.97721  -2.06935 -9.40510  1.000 61.81767  ? 131 GLY A CA  1 
ATOM   1001 C C   . GLY A 1 131 ? 9.38535  -1.51613 -9.45575  1.000 57.51522  ? 131 GLY A C   1 
ATOM   1002 O O   . GLY A 1 131 ? 9.90611  -0.98203 -8.47025  1.000 55.91615  ? 131 GLY A O   1 
ATOM   1003 N N   . PRO A 1 132 ? 10.03151 -1.63439 -10.61355 1.000 54.46964  ? 132 PRO A N   1 
ATOM   1004 C CA  . PRO A 1 132 ? 11.40843 -1.14700 -10.73800 1.000 51.90547  ? 132 PRO A CA  1 
ATOM   1005 C C   . PRO A 1 132 ? 11.47285 0.37239  -10.71247 1.000 48.72074  ? 132 PRO A C   1 
ATOM   1006 O O   . PRO A 1 132 ? 10.58525 1.06921  -11.21247 1.000 48.48414  ? 132 PRO A O   1 
ATOM   1007 C CB  . PRO A 1 132 ? 11.85746 -1.69868 -12.09545 1.000 52.39217  ? 132 PRO A CB  1 
ATOM   1008 C CG  . PRO A 1 132 ? 10.59012 -1.83172 -12.86965 1.000 54.52821  ? 132 PRO A CG  1 
ATOM   1009 C CD  . PRO A 1 132 ? 9.53174  -2.21712 -11.86984 1.000 55.38640  ? 132 PRO A CD  1 
ATOM   1010 N N   . PHE A 1 133 ? 12.54947 0.88248  -10.12268 1.000 43.08531  ? 133 PHE A N   1 
ATOM   1011 C CA  . PHE A 1 133 ? 12.81660 2.31331  -10.07189 1.000 41.85381  ? 133 PHE A CA  1 
ATOM   1012 C C   . PHE A 1 133 ? 13.82946 2.64834  -11.15687 1.000 39.64919  ? 133 PHE A C   1 
ATOM   1013 O O   . PHE A 1 133 ? 14.95931 2.15113  -11.12865 1.000 37.60405  ? 133 PHE A O   1 
ATOM   1014 C CB  . PHE A 1 133 ? 13.33508 2.72495  -8.69338  1.000 39.37330  ? 133 PHE A CB  1 
ATOM   1015 C CG  . PHE A 1 133 ? 13.68803 4.18375  -8.57862  1.000 37.91559  ? 133 PHE A CG  1 
ATOM   1016 C CD1 . PHE A 1 133 ? 12.69944 5.14973  -8.54410  1.000 38.09072  ? 133 PHE A CD1 1 
ATOM   1017 C CD2 . PHE A 1 133 ? 15.00916 4.58590  -8.48119  1.000 36.63100  ? 133 PHE A CD2 1 
ATOM   1018 C CE1 . PHE A 1 133 ? 13.02430 6.48949  -8.43016  1.000 36.88654  ? 133 PHE A CE1 1 
ATOM   1019 C CE2 . PHE A 1 133 ? 15.33882 5.92800  -8.36436  1.000 35.10991  ? 133 PHE A CE2 1 
ATOM   1020 C CZ  . PHE A 1 133 ? 14.34410 6.87781  -8.33558  1.000 35.22292  ? 133 PHE A CZ  1 
ATOM   1021 N N   . VAL A 1 134 ? 13.41406 3.46793  -12.12106 1.000 38.65185  ? 134 VAL A N   1 
ATOM   1022 C CA  . VAL A 1 134 ? 14.27211 3.91185  -13.21554 1.000 38.26482  ? 134 VAL A CA  1 
ATOM   1023 C C   . VAL A 1 134 ? 14.01825 5.39710  -13.42478 1.000 37.97974  ? 134 VAL A C   1 
ATOM   1024 O O   . VAL A 1 134 ? 12.88795 5.79726  -13.72473 1.000 39.53950  ? 134 VAL A O   1 
ATOM   1025 C CB  . VAL A 1 134 ? 14.00793 3.14720  -14.52536 1.000 40.79734  ? 134 VAL A CB  1 
ATOM   1026 C CG1 . VAL A 1 134 ? 14.99213 3.59354  -15.59722 1.000 38.28155  ? 134 VAL A CG1 1 
ATOM   1027 C CG2 . VAL A 1 134 ? 14.08119 1.64241  -14.30921 1.000 40.37505  ? 134 VAL A CG2 1 
ATOM   1028 N N   . VAL A 1 135 ? 15.05400 6.21704  -13.26228 1.000 35.37971  ? 135 VAL A N   1 
ATOM   1029 C CA  . VAL A 1 135 ? 14.94128 7.64174  -13.54537 1.000 38.03116  ? 135 VAL A CA  1 
ATOM   1030 C C   . VAL A 1 135 ? 16.16957 8.09869  -14.31319 1.000 36.45886  ? 135 VAL A C   1 
ATOM   1031 O O   . VAL A 1 135 ? 17.26303 7.54215  -14.16981 1.000 36.98618  ? 135 VAL A O   1 
ATOM   1032 C CB  . VAL A 1 135 ? 14.76668 8.49630  -12.26861 1.000 35.81287  ? 135 VAL A CB  1 
ATOM   1033 C CG1 . VAL A 1 135 ? 13.45113 8.17167  -11.58365 1.000 38.04425  ? 135 VAL A CG1 1 
ATOM   1034 C CG2 . VAL A 1 135 ? 15.94367 8.29872  -11.31579 1.000 36.96861  ? 135 VAL A CG2 1 
ATOM   1035 N N   . ASP A 1 136 ? 15.97330 9.11773  -15.14392 1.000 35.92090  ? 136 ASP A N   1 
ATOM   1036 C CA  . ASP A 1 136 ? 17.07382 9.83357  -15.77032 1.000 36.79361  ? 136 ASP A CA  1 
ATOM   1037 C C   . ASP A 1 136 ? 17.51695 10.95400 -14.84128 1.000 34.90931  ? 136 ASP A C   1 
ATOM   1038 O O   . ASP A 1 136 ? 16.68968 11.74110 -14.37024 1.000 35.04997  ? 136 ASP A O   1 
ATOM   1039 C CB  . ASP A 1 136 ? 16.65506 10.40016 -17.12671 1.000 37.98007  ? 136 ASP A CB  1 
ATOM   1040 C CG  . ASP A 1 136 ? 16.67971 9.35558  -18.22286 1.000 39.33923  ? 136 ASP A CG  1 
ATOM   1041 O OD1 . ASP A 1 136 ? 17.58007 8.49352  -18.18768 1.000 39.60399  ? 136 ASP A OD1 1 
ATOM   1042 O OD2 . ASP A 1 136 ? 15.80284 9.39030  -19.11392 1.000 41.64274  ? 136 ASP A OD2 1 
ATOM   1043 N N   . VAL A 1 137 ? 18.81363 11.01559 -14.57060 1.000 32.71801  ? 137 VAL A N   1 
ATOM   1044 C CA  . VAL A 1 137 ? 19.38001 12.02223 -13.68300 1.000 34.89190  ? 137 VAL A CA  1 
ATOM   1045 C C   . VAL A 1 137 ? 19.96252 13.12923 -14.54674 1.000 34.50538  ? 137 VAL A C   1 
ATOM   1046 O O   . VAL A 1 137 ? 20.86825 12.88689 -15.35330 1.000 33.84732  ? 137 VAL A O   1 
ATOM   1047 C CB  . VAL A 1 137 ? 20.44327 11.42186 -12.75190 1.000 33.38648  ? 137 VAL A CB  1 
ATOM   1048 C CG1 . VAL A 1 137 ? 20.95889 12.48379 -11.79540 1.000 32.82670  ? 137 VAL A CG1 1 
ATOM   1049 C CG2 . VAL A 1 137 ? 19.86631 10.23913 -11.98703 1.000 31.59437  ? 137 VAL A CG2 1 
ATOM   1050 N N   . VAL A 1 138 ? 19.43921 14.33985 -14.37684 1.000 33.54909  ? 138 VAL A N   1 
ATOM   1051 C CA  . VAL A 1 138 ? 19.79961 15.49901 -15.18519 1.000 35.26484  ? 138 VAL A CA  1 
ATOM   1052 C C   . VAL A 1 138 ? 20.37942 16.55985 -14.25679 1.000 36.97571  ? 138 VAL A C   1 
ATOM   1053 O O   . VAL A 1 138 ? 19.70714 17.00439 -13.31678 1.000 35.55301  ? 138 VAL A O   1 
ATOM   1054 C CB  . VAL A 1 138 ? 18.58760 16.04488 -15.95375 1.000 37.66829  ? 138 VAL A CB  1 
ATOM   1055 C CG1 . VAL A 1 138 ? 18.96284 17.28309 -16.73481 1.000 39.25499  ? 138 VAL A CG1 1 
ATOM   1056 C CG2 . VAL A 1 138 ? 18.02132 14.98042 -16.88032 1.000 37.99983  ? 138 VAL A CG2 1 
ATOM   1057 N N   . ILE A 1 139 ? 21.61757 16.96716 -14.52204 1.000 33.78330  ? 139 ILE A N   1 
ATOM   1058 C CA  . ILE A 1 139 ? 22.33473 17.94027 -13.70215 1.000 33.58372  ? 139 ILE A CA  1 
ATOM   1059 C C   . ILE A 1 139 ? 22.49981 19.21101 -14.52378 1.000 37.81847  ? 139 ILE A C   1 
ATOM   1060 O O   . ILE A 1 139 ? 23.21484 19.21361 -15.53290 1.000 33.87191  ? 139 ILE A O   1 
ATOM   1061 C CB  . ILE A 1 139 ? 23.69997 17.40881 -13.24669 1.000 32.73428  ? 139 ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 139 ? 23.55396 16.06646 -12.52617 1.000 32.83415  ? 139 ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 139 ? 24.39572 18.43143 -12.35291 1.000 36.27549  ? 139 ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 139 ? 24.88518 15.42975 -12.16573 1.000 32.37417  ? 139 ILE A CD1 1 
ATOM   1065 N N   . ASN A 1 140 ? 21.85545 20.29477 -14.08936 1.000 34.55578  ? 140 ASN A N   1 
ATOM   1066 C CA  . ASN A 1 140 ? 21.90832 21.58091 -14.79093 1.000 36.46346  ? 140 ASN A CA  1 
ATOM   1067 C C   . ASN A 1 140 ? 21.60502 21.41212 -16.28124 1.000 39.84103  ? 140 ASN A C   1 
ATOM   1068 O O   . ASN A 1 140 ? 22.30345 21.94098 -17.15052 1.000 36.91854  ? 140 ASN A O   1 
ATOM   1069 C CB  . ASN A 1 140 ? 23.26211 22.26457 -14.57768 1.000 34.55343  ? 140 ASN A CB  1 
ATOM   1070 C CG  . ASN A 1 140 ? 23.55212 22.52963 -13.10907 1.000 37.54531  ? 140 ASN A CG  1 
ATOM   1071 O OD1 . ASN A 1 140 ? 22.65667 22.89116 -12.34636 1.000 34.60670  ? 140 ASN A OD1 1 
ATOM   1072 N ND2 . ASN A 1 140 ? 24.80268 22.33690 -12.70312 1.000 36.03140  ? 140 ASN A ND2 1 
ATOM   1073 N N   . ASP A 1 141 ? 20.54928 20.64885 -16.56718 1.000 40.08172  ? 141 ASP A N   1 
ATOM   1074 C CA  . ASP A 1 141 ? 20.00918 20.35922 -17.89682 1.000 41.70417  ? 141 ASP A CA  1 
ATOM   1075 C C   . ASP A 1 141 ? 20.86774 19.38826 -18.70057 1.000 40.88522  ? 141 ASP A C   1 
ATOM   1076 O O   . ASP A 1 141 ? 20.53455 19.10859 -19.85923 1.000 45.52893  ? 141 ASP A O   1 
ATOM   1077 C CB  . ASP A 1 141 ? 19.77808 21.62613 -18.73475 1.000 44.48684  ? 141 ASP A CB  1 
ATOM   1078 C CG  . ASP A 1 141 ? 18.80890 22.59315 -18.07739 1.000 50.96691  ? 141 ASP A CG  1 
ATOM   1079 O OD1 . ASP A 1 141 ? 17.95449 22.14519 -17.27821 1.000 49.01114  ? 141 ASP A OD1 1 
ATOM   1080 O OD2 . ASP A 1 141 ? 18.90260 23.80600 -18.35960 1.000 60.84472  ? 141 ASP A OD2 1 
ATOM   1081 N N   . ILE A 1 142 ? 21.94259 18.85476 -18.13242 1.000 39.17922  ? 142 ILE A N   1 
ATOM   1082 C CA  . ILE A 1 142 ? 22.80119 17.88236 -18.80145 1.000 41.52989  ? 142 ILE A CA  1 
ATOM   1083 C C   . ILE A 1 142 ? 22.38566 16.48892 -18.34878 1.000 41.37383  ? 142 ILE A C   1 
ATOM   1084 O O   . ILE A 1 142 ? 22.37134 16.20144 -17.14346 1.000 34.26011  ? 142 ILE A O   1 
ATOM   1085 C CB  . ILE A 1 142 ? 24.28251 18.12970 -18.47624 1.000 45.60330  ? 142 ILE A CB  1 
ATOM   1086 C CG1 . ILE A 1 142 ? 24.67311 19.58060 -18.76623 1.000 51.78775  ? 142 ILE A CG1 1 
ATOM   1087 C CG2 . ILE A 1 142 ? 25.17032 17.15290 -19.23921 1.000 47.72837  ? 142 ILE A CG2 1 
ATOM   1088 C CD1 . ILE A 1 142 ? 25.90052 20.03475 -17.98466 1.000 55.71563  ? 142 ILE A CD1 1 
ATOM   1089 N N   . HIS A 1 143 ? 22.06113 15.60999 -19.29806 1.000 38.23149  ? 143 HIS A N   1 
ATOM   1090 C CA  A HIS A 1 143 ? 21.74475 14.22910 -18.94312 0.500 39.72895  ? 143 HIS A CA  1 
ATOM   1091 C CA  B HIS A 1 143 ? 21.74127 14.23532 -18.94321 0.500 40.79642  ? 143 HIS A CA  1 
ATOM   1092 C C   . HIS A 1 143 ? 23.00233 13.53717 -18.44412 1.000 40.26960  ? 143 HIS A C   1 
ATOM   1093 O O   . HIS A 1 143 ? 23.97131 13.37732 -19.19420 1.000 36.92371  ? 143 HIS A O   1 
ATOM   1094 C CB  A HIS A 1 143 ? 21.16296 13.45095 -20.12112 0.500 41.55323  ? 143 HIS A CB  1 
ATOM   1095 C CB  B HIS A 1 143 ? 21.13075 13.51333 -20.14226 0.500 39.78636  ? 143 HIS A CB  1 
ATOM   1096 C CG  A HIS A 1 143 ? 20.97501 11.99108 -19.82734 0.500 40.76512  ? 143 HIS A CG  1 
ATOM   1097 C CG  B HIS A 1 143 ? 19.74974 13.98533 -20.48171 0.500 41.65106  ? 143 HIS A CG  1 
ATOM   1098 N ND1 A HIS A 1 143 ? 22.01473 11.08524 -19.85582 0.500 40.30841  ? 143 HIS A ND1 1 
ATOM   1099 N ND1 B HIS A 1 143 ? 18.66299 13.13889 -20.53810 0.500 43.71789  ? 143 HIS A ND1 1 
ATOM   1100 C CD2 A HIS A 1 143 ? 19.87685 11.28738 -19.46016 0.500 40.15832  ? 143 HIS A CD2 1 
ATOM   1101 C CD2 B HIS A 1 143 ? 19.27468 15.22338 -20.75639 0.500 42.61594  ? 143 HIS A CD2 1 
ATOM   1102 C CE1 A HIS A 1 143 ? 21.56244 9.88496  -19.53876 0.500 40.65399  ? 143 HIS A CE1 1 
ATOM   1103 C CE1 B HIS A 1 143 ? 17.58278 13.83212 -20.85238 0.500 44.79585  ? 143 HIS A CE1 1 
ATOM   1104 N NE2 A HIS A 1 143 ? 20.26823 9.97983  -19.29320 0.500 39.84409  ? 143 HIS A NE2 1 
ATOM   1105 N NE2 B HIS A 1 143 ? 17.92635 15.09985 -20.98794 0.500 43.92087  ? 143 HIS A NE2 1 
ATOM   1106 N N   . PHE A 1 144 ? 22.98668 13.12746 -17.17856 1.000 32.86390  ? 144 PHE A N   1 
ATOM   1107 C CA  . PHE A 1 144 ? 24.15061 12.54774 -16.52133 1.000 35.13415  ? 144 PHE A CA  1 
ATOM   1108 C C   . PHE A 1 144 ? 24.14451 11.02592 -16.50022 1.000 34.05003  ? 144 PHE A C   1 
ATOM   1109 O O   . PHE A 1 144 ? 25.17242 10.40691 -16.78522 1.000 33.20137  ? 144 PHE A O   1 
ATOM   1110 C CB  . PHE A 1 144 ? 24.25086 13.07543 -15.08777 1.000 32.13617  ? 144 PHE A CB  1 
ATOM   1111 C CG  . PHE A 1 144 ? 25.41961 12.53209 -14.32896 1.000 30.92769  ? 144 PHE A CG  1 
ATOM   1112 C CD1 . PHE A 1 144 ? 26.70069 13.00129 -14.57761 1.000 30.68707  ? 144 PHE A CD1 1 
ATOM   1113 C CD2 . PHE A 1 144 ? 25.24393 11.55193 -13.37014 1.000 31.09065  ? 144 PHE A CD2 1 
ATOM   1114 C CE1 . PHE A 1 144 ? 27.78830 12.49655 -13.88257 1.000 31.48598  ? 144 PHE A CE1 1 
ATOM   1115 C CE2 . PHE A 1 144 ? 26.32381 11.05167 -12.65955 1.000 32.31418  ? 144 PHE A CE2 1 
ATOM   1116 C CZ  . PHE A 1 144 ? 27.59589 11.51860 -12.91886 1.000 31.33299  ? 144 PHE A CZ  1 
ATOM   1117 N N   . GLU A 1 145 ? 23.01845 10.40167 -16.17485 1.000 32.03494  ? 145 GLU A N   1 
ATOM   1118 C CA  . GLU A 1 145 ? 22.97179 8.94942  -16.08807 1.000 33.30535  ? 145 GLU A CA  1 
ATOM   1119 C C   . GLU A 1 145 ? 21.51580 8.51881  -16.05687 1.000 32.17389  ? 145 GLU A C   1 
ATOM   1120 O O   . GLU A 1 145 ? 20.62711 9.30145  -15.70662 1.000 33.47663  ? 145 GLU A O   1 
ATOM   1121 C CB  . GLU A 1 145 ? 23.69861 8.43627  -14.83671 1.000 31.71021  ? 145 GLU A CB  1 
ATOM   1122 C CG  . GLU A 1 145 ? 22.95617 8.80037  -13.54376 1.000 30.14814  ? 145 GLU A CG  1 
ATOM   1123 C CD  . GLU A 1 145 ? 23.68870 8.40410  -12.28096 1.000 31.00214  ? 145 GLU A CD  1 
ATOM   1124 O OE1 . GLU A 1 145 ? 24.77621 7.80032  -12.36860 1.000 30.06475  ? 145 GLU A OE1 1 
ATOM   1125 O OE2 . GLU A 1 145 ? 23.16720 8.70944  -11.19136 1.000 27.51912  ? 145 GLU A OE2 1 
ATOM   1126 N N   . ARG A 1 146 ? 21.28319 7.26512  -16.43888 1.000 32.28421  ? 146 ARG A N   1 
ATOM   1127 C CA  . ARG A 1 146 ? 20.01228 6.59595  -16.19504 1.000 36.62136  ? 146 ARG A CA  1 
ATOM   1128 C C   . ARG A 1 146 ? 20.18301 5.65524  -15.00806 1.000 34.25164  ? 146 ARG A C   1 
ATOM   1129 O O   . ARG A 1 146 ? 20.94009 4.67986  -15.08620 1.000 34.44050  ? 146 ARG A O   1 
ATOM   1130 C CB  . ARG A 1 146 ? 19.53097 5.82415  -17.41801 1.000 38.90619  ? 146 ARG A CB  1 
ATOM   1131 C CG  . ARG A 1 146 ? 18.22021 5.08688  -17.17974 1.000 39.94908  ? 146 ARG A CG  1 
ATOM   1132 C CD  . ARG A 1 146 ? 17.50755 4.75665  -18.48494 1.000 44.01991  ? 146 ARG A CD  1 
ATOM   1133 N NE  . ARG A 1 146 ? 16.98467 5.94890  -19.14172 1.000 41.57956  ? 146 ARG A NE  1 
ATOM   1134 C CZ  . ARG A 1 146 ? 16.27950 5.93481  -20.26419 1.000 46.44993  ? 146 ARG A CZ  1 
ATOM   1135 N NH1 . ARG A 1 146 ? 16.00709 4.80347  -20.89538 1.000 47.21117  ? 146 ARG A NH1 1 
ATOM   1136 N NH2 . ARG A 1 146 ? 15.83599 7.08410  -20.76641 1.000 44.66635  ? 146 ARG A NH2 1 
ATOM   1137 N N   . PHE A 1 147 ? 19.48738 5.95228  -13.91613 1.000 34.32110  ? 147 PHE A N   1 
ATOM   1138 C CA  . PHE A 1 147 ? 19.64371 5.21395  -12.66846 1.000 31.20824  ? 147 PHE A CA  1 
ATOM   1139 C C   . PHE A 1 147 ? 18.59031 4.11881  -12.56295 1.000 31.31488  ? 147 PHE A C   1 
ATOM   1140 O O   . PHE A 1 147 ? 17.38685 4.39841  -12.61300 1.000 33.92288  ? 147 PHE A O   1 
ATOM   1141 C CB  . PHE A 1 147 ? 19.55245 6.13722  -11.45497 1.000 32.59259  ? 147 PHE A CB  1 
ATOM   1142 C CG  . PHE A 1 147 ? 19.74908 5.41193  -10.14956 1.000 28.80323  ? 147 PHE A CG  1 
ATOM   1143 C CD1 . PHE A 1 147 ? 21.01646 5.23565  -9.63353  1.000 30.23337  ? 147 PHE A CD1 1 
ATOM   1144 C CD2 . PHE A 1 147 ? 18.67081 4.86859  -9.46876  1.000 31.90302  ? 147 PHE A CD2 1 
ATOM   1145 C CE1 . PHE A 1 147 ? 21.20727 4.55552  -8.44780  1.000 31.99166  ? 147 PHE A CE1 1 
ATOM   1146 C CE2 . PHE A 1 147 ? 18.86055 4.17906  -8.27572  1.000 31.02059  ? 147 PHE A CE2 1 
ATOM   1147 C CZ  . PHE A 1 147 ? 20.13034 4.02716  -7.77376  1.000 29.84031  ? 147 PHE A CZ  1 
ATOM   1148 N N   . ARG A 1 148 ? 19.04971 2.88201  -12.38718 1.000 27.07155  ? 148 ARG A N   1 
ATOM   1149 C CA  . ARG A 1 148 ? 18.19757 1.74340  -12.07958 1.000 33.47823  ? 148 ARG A CA  1 
ATOM   1150 C C   . ARG A 1 148 ? 18.64132 1.16697  -10.74703 1.000 35.32712  ? 148 ARG A C   1 
ATOM   1151 O O   . ARG A 1 148 ? 19.82569 0.86875  -10.56586 1.000 36.11143  ? 148 ARG A O   1 
ATOM   1152 C CB  . ARG A 1 148 ? 18.28465 0.65325  -13.14632 1.000 38.47056  ? 148 ARG A CB  1 
ATOM   1153 C CG  . ARG A 1 148 ? 17.77339 1.02115  -14.50377 1.000 40.83703  ? 148 ARG A CG  1 
ATOM   1154 C CD  . ARG A 1 148 ? 17.93839 -0.16220 -15.44102 0.700 45.83055  ? 148 ARG A CD  1 
ATOM   1155 N NE  . ARG A 1 148 ? 17.33865 0.10057  -16.74085 0.700 48.86283  ? 148 ARG A NE  1 
ATOM   1156 C CZ  . ARG A 1 148 ? 17.85960 0.91183  -17.64910 0.700 48.30364  ? 148 ARG A CZ  1 
ATOM   1157 N NH1 . ARG A 1 148 ? 18.98244 1.57482  -17.42087 0.700 47.00967  ? 148 ARG A NH1 1 
ATOM   1158 N NH2 . ARG A 1 148 ? 17.23838 1.06276  -18.81420 0.700 48.81098  ? 148 ARG A NH2 1 
ATOM   1159 N N   . GLY A 1 149 ? 17.69997 1.00842  -9.82349  1.000 33.66270  ? 149 GLY A N   1 
ATOM   1160 C CA  . GLY A 1 149 ? 18.04134 0.48123  -8.51206  1.000 34.53453  ? 149 GLY A CA  1 
ATOM   1161 C C   . GLY A 1 149 ? 16.89148 0.67141  -7.54371  1.000 33.76744  ? 149 GLY A C   1 
ATOM   1162 O O   . GLY A 1 149 ? 15.73697 0.79193  -7.95200  1.000 35.49218  ? 149 GLY A O   1 
ATOM   1163 N N   . ASP A 1 150 ? 17.22994 0.69752  -6.25150  1.000 33.23612  ? 150 ASP A N   1 
ATOM   1164 C CA  . ASP A 1 150 ? 16.20888 0.85277  -5.21897  1.000 34.69678  ? 150 ASP A CA  1 
ATOM   1165 C C   . ASP A 1 150 ? 15.75150 2.29716  -5.07150  1.000 34.05667  ? 150 ASP A C   1 
ATOM   1166 O O   . ASP A 1 150 ? 14.58633 2.54026  -4.73625  1.000 36.50442  ? 150 ASP A O   1 
ATOM   1167 C CB  . ASP A 1 150 ? 16.72641 0.34197  -3.87133  1.000 31.26997  ? 150 ASP A CB  1 
ATOM   1168 C CG  . ASP A 1 150 ? 16.74910 -1.16581 -3.79373  1.000 34.54250  ? 150 ASP A CG  1 
ATOM   1169 O OD1 . ASP A 1 150 ? 16.33064 -1.80791 -4.77324  1.000 34.26833  ? 150 ASP A OD1 1 
ATOM   1170 O OD2 . ASP A 1 150 ? 17.18375 -1.71110 -2.75791  1.000 33.36786  ? 150 ASP A OD2 1 
ATOM   1171 N N   . GLY A 1 151 ? 16.63625 3.25650  -5.29925  1.000 28.81375  ? 151 GLY A N   1 
ATOM   1172 C CA  . GLY A 1 151 ? 16.26567 4.64772  -5.16203  1.000 31.67799  ? 151 GLY A CA  1 
ATOM   1173 C C   . GLY A 1 151 ? 17.48240 5.52622  -4.94911  1.000 30.29512  ? 151 GLY A C   1 
ATOM   1174 O O   . GLY A 1 151 ? 18.62796 5.08886  -5.07565  1.000 29.68700  ? 151 GLY A O   1 
ATOM   1175 N N   . LEU A 1 152 ? 17.19292 6.78289  -4.61896  1.000 29.11650  ? 152 LEU A N   1 
ATOM   1176 C CA  . LEU A 1 152 ? 18.18907 7.83471  -4.50374  1.000 27.98674  ? 152 LEU A CA  1 
ATOM   1177 C C   . LEU A 1 152 ? 17.90375 8.65789  -3.25521  1.000 30.40436  ? 152 LEU A C   1 
ATOM   1178 O O   . LEU A 1 152 ? 16.75222 8.80065  -2.83728  1.000 30.54119  ? 152 LEU A O   1 
ATOM   1179 C CB  . LEU A 1 152 ? 18.18264 8.74026  -5.74213  1.000 29.50207  ? 152 LEU A CB  1 
ATOM   1180 C CG  . LEU A 1 152 ? 18.71733 8.11005  -7.02908  1.000 28.21052  ? 152 LEU A CG  1 
ATOM   1181 C CD1 . LEU A 1 152 ? 18.27102 8.90207  -8.25546  1.000 29.63433  ? 152 LEU A CD1 1 
ATOM   1182 C CD2 . LEU A 1 152 ? 20.22411 8.01990  -6.97359  1.000 28.00828  ? 152 LEU A CD2 1 
ATOM   1183 N N   . CYS A 1 153 ? 18.96469 9.21300  -2.67662  1.000 26.22549  ? 153 CYS A N   1 
ATOM   1184 C CA  . CYS A 1 153 ? 18.87663 10.01326 -1.46188  1.000 30.04989  ? 153 CYS A CA  1 
ATOM   1185 C C   . CYS A 1 153 ? 19.65244 11.30568 -1.66444  1.000 29.10741  ? 153 CYS A C   1 
ATOM   1186 O O   . CYS A 1 153 ? 20.82742 11.27339 -2.04497  1.000 29.66070  ? 153 CYS A O   1 
ATOM   1187 C CB  . CYS A 1 153 ? 19.42459 9.23209  -0.25744  1.000 27.98890  ? 153 CYS A CB  1 
ATOM   1188 S SG  . CYS A 1 153 ? 19.62285 10.18059 1.28054   1.000 28.20033  ? 153 CYS A SG  1 
ATOM   1189 N N   . MET A 1 154 ? 18.99721 12.44019 -1.42948  1.000 27.73797  ? 154 MET A N   1 
ATOM   1190 C CA  . MET A 1 154 ? 19.64884 13.74271 -1.50138  1.000 29.09259  ? 154 MET A CA  1 
ATOM   1191 C C   . MET A 1 154 ? 19.66932 14.34423 -0.10374  1.000 28.66001  ? 154 MET A C   1 
ATOM   1192 O O   . MET A 1 154 ? 18.61069 14.61272 0.47221   1.000 27.13032  ? 154 MET A O   1 
ATOM   1193 C CB  . MET A 1 154 ? 18.94295 14.68355 -2.47204  1.000 29.42203  ? 154 MET A CB  1 
ATOM   1194 C CG  . MET A 1 154 ? 19.70897 15.97817 -2.68979  1.000 31.21459  ? 154 MET A CG  1 
ATOM   1195 S SD  . MET A 1 154 ? 21.27324 15.72613 -3.57520  1.000 30.29952  ? 154 MET A SD  1 
ATOM   1196 C CE  . MET A 1 154 ? 20.74453 15.96146 -5.26969  1.000 30.97404  ? 154 MET A CE  1 
ATOM   1197 N N   . SER A 1 155 ? 20.86921 14.58184 0.41867   1.000 28.86063  ? 155 SER A N   1 
ATOM   1198 C CA  . SER A 1 155 ? 21.07569 14.92485 1.81954   1.000 27.04847  ? 155 SER A CA  1 
ATOM   1199 C C   . SER A 1 155 ? 21.59487 16.35107 1.95845   1.000 30.16940  ? 155 SER A C   1 
ATOM   1200 O O   . SER A 1 155 ? 22.37424 16.82649 1.12417   1.000 28.33270  ? 155 SER A O   1 
ATOM   1201 C CB  . SER A 1 155 ? 22.06662 13.94813 2.46348   1.000 26.99109  ? 155 SER A CB  1 
ATOM   1202 O OG  . SER A 1 155 ? 22.32027 14.27774 3.82391   1.000 29.44512  ? 155 SER A OG  1 
ATOM   1203 N N   . THR A 1 156 ? 21.14331 17.03082 3.01257   1.000 25.37578  ? 156 THR A N   1 
ATOM   1204 C CA  . THR A 1 156 ? 21.75590 18.26288 3.47295   1.000 27.76864  ? 156 THR A CA  1 
ATOM   1205 C C   . THR A 1 156 ? 23.09940 17.94962 4.13100   1.000 28.15334  ? 156 THR A C   1 
ATOM   1206 O O   . THR A 1 156 ? 23.40896 16.78976 4.41523   1.000 28.30471  ? 156 THR A O   1 
ATOM   1207 C CB  . THR A 1 156 ? 20.85478 18.95394 4.49601   1.000 30.01303  ? 156 THR A CB  1 
ATOM   1208 O OG1 . THR A 1 156 ? 20.81434 18.15109 5.68192   1.000 26.63519  ? 156 THR A OG1 1 
ATOM   1209 C CG2 . THR A 1 156 ? 19.44662 19.14039 3.96636   1.000 30.44889  ? 156 THR A CG2 1 
ATOM   1210 N N   . PRO A 1 157 ? 23.91203 18.97141 4.41343   1.000 27.74319  ? 157 PRO A N   1 
ATOM   1211 C CA  . PRO A 1 157 ? 25.13707 18.71799 5.19797   1.000 29.42742  ? 157 PRO A CA  1 
ATOM   1212 C C   . PRO A 1 157 ? 24.86899 18.09578 6.56206   1.000 27.99166  ? 157 PRO A C   1 
ATOM   1213 O O   . PRO A 1 157 ? 25.48233 17.07508 6.90357   1.000 25.43600  ? 157 PRO A O   1 
ATOM   1214 C CB  . PRO A 1 157 ? 25.76222 20.11310 5.31059   1.000 30.94302  ? 157 PRO A CB  1 
ATOM   1215 C CG  . PRO A 1 157 ? 25.26716 20.83154 4.10473   1.000 32.02587  ? 157 PRO A CG  1 
ATOM   1216 C CD  . PRO A 1 157 ? 23.86593 20.35320 3.90051   1.000 29.18743  ? 157 PRO A CD  1 
ATOM   1217 N N   . SER A 1 158 ? 23.96489 18.67374 7.35810   1.000 28.45592  ? 158 SER A N   1 
ATOM   1218 C CA  . SER A 1 158 ? 23.69169 18.07548 8.66162   1.000 30.59166  ? 158 SER A CA  1 
ATOM   1219 C C   . SER A 1 158 ? 23.01130 16.72134 8.50923   1.000 28.54096  ? 158 SER A C   1 
ATOM   1220 O O   . SER A 1 158 ? 23.14295 15.85607 9.37965   1.000 30.13919  ? 158 SER A O   1 
ATOM   1221 C CB  . SER A 1 158 ? 22.85771 19.02142 9.53430   1.000 30.78119  ? 158 SER A CB  1 
ATOM   1222 O OG  . SER A 1 158 ? 21.60918 19.33803 8.94471   1.000 29.49206  ? 158 SER A OG  1 
ATOM   1223 N N   . GLY A 1 159 ? 22.32178 16.50045 7.39394   1.000 29.62091  ? 159 GLY A N   1 
ATOM   1224 C CA  . GLY A 1 159 ? 21.77948 15.18428 7.12114   1.000 28.59361  ? 159 GLY A CA  1 
ATOM   1225 C C   . GLY A 1 159 ? 22.81197 14.13379 6.75960   1.000 27.19120  ? 159 GLY A C   1 
ATOM   1226 O O   . GLY A 1 159 ? 22.46773 12.94535 6.73827   1.000 28.09960  ? 159 GLY A O   1 
ATOM   1227 N N   . THR A 1 160 ? 24.06414 14.52751 6.48451   1.000 27.41021  ? 160 THR A N   1 
ATOM   1228 C CA  . THR A 1 160 ? 25.01858 13.54524 5.97828   1.000 26.27358  ? 160 THR A CA  1 
ATOM   1229 C C   . THR A 1 160 ? 25.34225 12.46970 7.00416   1.000 29.74276  ? 160 THR A C   1 
ATOM   1230 O O   . THR A 1 160 ? 25.77372 11.38168 6.61297   1.000 27.77360  ? 160 THR A O   1 
ATOM   1231 C CB  . THR A 1 160 ? 26.32375 14.20113 5.48476   1.000 28.25094  ? 160 THR A CB  1 
ATOM   1232 O OG1 . THR A 1 160 ? 26.93329 14.99463 6.51141   1.000 25.95083  ? 160 THR A OG1 1 
ATOM   1233 C CG2 . THR A 1 160 ? 26.06058 15.05923 4.25310   1.000 30.35929  ? 160 THR A CG2 1 
ATOM   1234 N N   . THR A 1 161 ? 25.12175 12.73619 8.29723   1.000 27.08776  ? 161 THR A N   1 
ATOM   1235 C CA  . THR A 1 161 ? 25.33468 11.73657 9.33757   1.000 31.09864  ? 161 THR A CA  1 
ATOM   1236 C C   . THR A 1 161 ? 24.13264 10.82312 9.54973   1.000 31.40251  ? 161 THR A C   1 
ATOM   1237 O O   . THR A 1 161 ? 24.17082 9.98165  10.45296  1.000 32.18540  ? 161 THR A O   1 
ATOM   1238 C CB  . THR A 1 161 ? 25.69475 12.41846 10.66569  1.000 30.43797  ? 161 THR A CB  1 
ATOM   1239 O OG1 . THR A 1 161 ? 24.80529 13.51333 10.90199  1.000 28.85950  ? 161 THR A OG1 1 
ATOM   1240 C CG2 . THR A 1 161 ? 27.11970 12.94016 10.62818  1.000 32.41021  ? 161 THR A CG2 1 
ATOM   1241 N N   . ALA A 1 162 ? 23.09054 10.94695 8.74022   1.000 31.50667  ? 162 ALA A N   1 
ATOM   1242 C CA  . ALA A 1 162 ? 21.84919 10.19563 8.91214   1.000 31.65028  ? 162 ALA A CA  1 
ATOM   1243 C C   . ALA A 1 162 ? 21.75844 9.13638  7.81240   1.000 31.36877  ? 162 ALA A C   1 
ATOM   1244 O O   . ALA A 1 162 ? 22.72383 8.38378  7.63858   1.000 28.32011  ? 162 ALA A O   1 
ATOM   1245 C CB  . ALA A 1 162 ? 20.67847 11.16782 8.95544   1.000 32.89302  ? 162 ALA A CB  1 
ATOM   1246 N N   . TYR A 1 163 ? 20.64429 9.04167  7.07589   1.000 31.02752  ? 163 TYR A N   1 
ATOM   1247 C CA  . TYR A 1 163 ? 20.48366 8.04744  6.01621   1.000 31.16067  ? 163 TYR A CA  1 
ATOM   1248 C C   . TYR A 1 163 ? 21.66782 8.05838  5.05274   1.000 27.94666  ? 163 TYR A C   1 
ATOM   1249 O O   . TYR A 1 163 ? 22.16582 7.00038  4.65361   1.000 26.94143  ? 163 TYR A O   1 
ATOM   1250 C CB  . TYR A 1 163 ? 19.17574 8.33735  5.26871   1.000 33.30137  ? 163 TYR A CB  1 
ATOM   1251 C CG  . TYR A 1 163 ? 18.52146 7.18364  4.53682   1.000 33.70292  ? 163 TYR A CG  1 
ATOM   1252 C CD1 . TYR A 1 163 ? 19.15860 5.96038  4.37478   1.000 34.00702  ? 163 TYR A CD1 1 
ATOM   1253 C CD2 . TYR A 1 163 ? 17.24969 7.33308  3.99770   1.000 35.99920  ? 163 TYR A CD2 1 
ATOM   1254 C CE1 . TYR A 1 163 ? 18.53759 4.91216  3.68927   1.000 33.52607  ? 163 TYR A CE1 1 
ATOM   1255 C CE2 . TYR A 1 163 ? 16.62744 6.30201  3.31497   1.000 37.36351  ? 163 TYR A CE2 1 
ATOM   1256 C CZ  . TYR A 1 163 ? 17.27186 5.09580  3.16083   1.000 36.34050  ? 163 TYR A CZ  1 
ATOM   1257 O OH  . TYR A 1 163 ? 16.63663 4.07487  2.48332   1.000 36.74410  ? 163 TYR A OH  1 
ATOM   1258 N N   . ASN A 1 164 ? 22.12635 9.25497  4.67688   1.000 27.15825  ? 164 ASN A N   1 
ATOM   1259 C CA  . ASN A 1 164 ? 23.26119 9.41049  3.77043   1.000 28.67425  ? 164 ASN A CA  1 
ATOM   1260 C C   . ASN A 1 164 ? 24.46707 8.59778  4.22600   1.000 29.36011  ? 164 ASN A C   1 
ATOM   1261 O O   . ASN A 1 164 ? 25.14622 7.96374  3.40890   1.000 26.36610  ? 164 ASN A O   1 
ATOM   1262 C CB  . ASN A 1 164 ? 23.61494 10.89842 3.67253   1.000 26.32834  ? 164 ASN A CB  1 
ATOM   1263 C CG  . ASN A 1 164 ? 24.95195 11.14540 3.01447   1.000 29.18219  ? 164 ASN A CG  1 
ATOM   1264 O OD1 . ASN A 1 164 ? 25.02784 11.34343 1.80215   1.000 27.21341  ? 164 ASN A OD1 1 
ATOM   1265 N ND2 . ASN A 1 164 ? 26.02055 11.15603 3.81332   1.000 26.86524  ? 164 ASN A ND2 1 
ATOM   1266 N N   . LYS A 1 165 ? 24.75191 8.61003  5.53154   1.000 24.30090  ? 165 LYS A N   1 
ATOM   1267 C CA  . LYS A 1 165 ? 25.89284 7.86229  6.05070   1.000 27.06822  ? 165 LYS A CA  1 
ATOM   1268 C C   . LYS A 1 165 ? 25.72003 6.36545  5.82854   1.000 27.28779  ? 165 LYS A C   1 
ATOM   1269 O O   . LYS A 1 165 ? 26.66582 5.67551  5.42666   1.000 23.79224  ? 165 LYS A O   1 
ATOM   1270 C CB  . LYS A 1 165 ? 26.08216 8.16592  7.54213   1.000 27.04424  ? 165 LYS A CB  1 
ATOM   1271 C CG  . LYS A 1 165 ? 27.27389 7.44431  8.15867   1.000 29.10498  ? 165 LYS A CG  1 
ATOM   1272 C CD  . LYS A 1 165 ? 27.64327 8.01232  9.52653   1.000 30.61029  ? 165 LYS A CD  1 
ATOM   1273 C CE  . LYS A 1 165 ? 28.98976 7.46173  9.98046   1.000 32.64893  ? 165 LYS A CE  1 
ATOM   1274 N NZ  . LYS A 1 165 ? 28.94174 5.99585  10.27847  1.000 35.40894  ? 165 LYS A NZ  1 
ATOM   1275 N N   . SER A 1 166 ? 24.51523 5.84506  6.07965   1.000 26.42092  ? 166 SER A N   1 
ATOM   1276 C CA  . SER A 1 166 ? 24.26315 4.42123  5.89447   1.000 28.13018  ? 166 SER A CA  1 
ATOM   1277 C C   . SER A 1 166 ? 24.37623 4.00056  4.43443   1.000 28.13343  ? 166 SER A C   1 
ATOM   1278 O O   . SER A 1 166 ? 24.57143 2.81236  4.15576   1.000 27.69110  ? 166 SER A O   1 
ATOM   1279 C CB  . SER A 1 166 ? 22.87867 4.06030  6.43804   1.000 30.37499  ? 166 SER A CB  1 
ATOM   1280 O OG  . SER A 1 166 ? 22.79636 4.36894  7.81891   1.000 33.24823  ? 166 SER A OG  1 
ATOM   1281 N N   . LEU A 1 167 ? 24.26984 4.94136  3.50039   1.000 28.50834  ? 167 LEU A N   1 
ATOM   1282 C CA  . LEU A 1 167 ? 24.36185 4.64115  2.07955   1.000 25.48764  ? 167 LEU A CA  1 
ATOM   1283 C C   . LEU A 1 167 ? 25.76473 4.84673  1.52097   1.000 29.49732  ? 167 LEU A C   1 
ATOM   1284 O O   . LEU A 1 167 ? 25.95406 4.76830  0.30248   1.000 27.54118  ? 167 LEU A O   1 
ATOM   1285 C CB  . LEU A 1 167 ? 23.35485 5.49062  1.30054   1.000 26.79651  ? 167 LEU A CB  1 
ATOM   1286 C CG  . LEU A 1 167 ? 21.89116 5.20634  1.64804   1.000 28.30854  ? 167 LEU A CG  1 
ATOM   1287 C CD1 . LEU A 1 167 ? 20.97544 6.25681  1.04162   1.000 30.82980  ? 167 LEU A CD1 1 
ATOM   1288 C CD2 . LEU A 1 167 ? 21.49051 3.81062  1.18704   1.000 29.08148  ? 167 LEU A CD2 1 
ATOM   1289 N N   . GLY A 1 168 ? 26.74918 5.10468  2.37604   1.000 27.41034  ? 168 GLY A N   1 
ATOM   1290 C CA  . GLY A 1 168 ? 28.11259 5.28470  1.93080   1.000 29.49056  ? 168 GLY A CA  1 
ATOM   1291 C C   . GLY A 1 168 ? 28.50771 6.71520  1.64786   1.000 30.42434  ? 168 GLY A C   1 
ATOM   1292 O O   . GLY A 1 168 ? 29.63523 6.94876  1.19245   1.000 29.60110  ? 168 GLY A O   1 
ATOM   1293 N N   . GLY A 1 169 ? 27.62571 7.67910  1.90531   1.000 29.22899  ? 169 GLY A N   1 
ATOM   1294 C CA  . GLY A 1 169 ? 27.94353 9.06126  1.62163   1.000 26.85550  ? 169 GLY A CA  1 
ATOM   1295 C C   . GLY A 1 169 ? 29.01150 9.61570  2.54635   1.000 29.42014  ? 169 GLY A C   1 
ATOM   1296 O O   . GLY A 1 169 ? 29.32812 9.05706  3.59987   1.000 27.32010  ? 169 GLY A O   1 
ATOM   1297 N N   . ALA A 1 170 ? 29.58295 10.74199 2.12928   1.000 25.45624  ? 170 ALA A N   1 
ATOM   1298 C CA  . ALA A 1 170 ? 30.56740 11.43355 2.94357   1.000 29.38405  ? 170 ALA A CA  1 
ATOM   1299 C C   . ALA A 1 170 ? 29.88105 12.27614 4.01342   1.000 27.42870  ? 170 ALA A C   1 
ATOM   1300 O O   . ALA A 1 170 ? 28.75746 12.74989 3.83419   1.000 27.60714  ? 170 ALA A O   1 
ATOM   1301 C CB  . ALA A 1 170 ? 31.44986 12.32760 2.07508   1.000 28.32355  ? 170 ALA A CB  1 
ATOM   1302 N N   . LEU A 1 171 ? 30.57218 12.46098 5.13383   1.000 29.44401  ? 171 LEU A N   1 
ATOM   1303 C CA  . LEU A 1 171 ? 30.13003 13.38555 6.17205   1.000 28.24770  ? 171 LEU A CA  1 
ATOM   1304 C C   . LEU A 1 171 ? 30.67438 14.76950 5.83610   1.000 28.58872  ? 171 LEU A C   1 
ATOM   1305 O O   . LEU A 1 171 ? 31.88640 14.93539 5.65819   1.000 32.44231  ? 171 LEU A O   1 
ATOM   1306 C CB  . LEU A 1 171 ? 30.61352 12.93006 7.54853   1.000 27.81499  ? 171 LEU A CB  1 
ATOM   1307 C CG  . LEU A 1 171 ? 30.37150 11.46356 7.92365   1.000 29.02311  ? 171 LEU A CG  1 
ATOM   1308 C CD1 . LEU A 1 171 ? 30.76997 11.19701 9.38536   1.000 28.08193  ? 171 LEU A CD1 1 
ATOM   1309 C CD2 . LEU A 1 171 ? 28.92173 11.06947 7.67800   1.000 28.63472  ? 171 LEU A CD2 1 
ATOM   1310 N N   . MET A 1 172 ? 29.78732 15.75523 5.72680   1.000 26.92752  ? 172 MET A N   1 
ATOM   1311 C CA  . MET A 1 172 ? 30.16951 17.10985 5.34669   1.000 31.78093  ? 172 MET A CA  1 
ATOM   1312 C C   . MET A 1 172 ? 29.94011 18.06573 6.50802   1.000 33.45614  ? 172 MET A C   1 
ATOM   1313 O O   . MET A 1 172 ? 28.90800 17.99688 7.18135   1.000 35.34794  ? 172 MET A O   1 
ATOM   1314 C CB  . MET A 1 172 ? 29.36764 17.61116 4.14117   1.000 30.58031  ? 172 MET A CB  1 
ATOM   1315 C CG  . MET A 1 172 ? 29.24531 16.65792 2.98600   1.000 33.95205  ? 172 MET A CG  1 
ATOM   1316 S SD  . MET A 1 172 ? 28.27320 17.44001 1.67980   1.000 38.72148  ? 172 MET A SD  1 
ATOM   1317 C CE  . MET A 1 172 ? 29.08970 19.02700 1.60028   1.000 35.97572  ? 172 MET A CE  1 
ATOM   1318 N N   . HIS A 1 173 ? 30.89262 18.96768 6.72666   1.000 34.68717  ? 173 HIS A N   1 
ATOM   1319 C CA  . HIS A 1 173 ? 30.68912 20.00097 7.72793   1.000 34.32523  ? 173 HIS A CA  1 
ATOM   1320 C C   . HIS A 1 173 ? 29.55389 20.92447 7.29189   1.000 36.34847  ? 173 HIS A C   1 
ATOM   1321 O O   . HIS A 1 173 ? 29.49185 21.32522 6.12185   1.000 37.82802  ? 173 HIS A O   1 
ATOM   1322 C CB  . HIS A 1 173 ? 31.95714 20.81624 7.95674   1.000 34.98953  ? 173 HIS A CB  1 
ATOM   1323 C CG  . HIS A 1 173 ? 31.87068 21.70879 9.15389   1.000 37.67936  ? 173 HIS A CG  1 
ATOM   1324 N ND1 . HIS A 1 173 ? 31.35438 22.98475 9.09473   1.000 38.41619  ? 173 HIS A ND1 1 
ATOM   1325 C CD2 . HIS A 1 173 ? 32.19555 21.49347 10.44993  1.000 36.29560  ? 173 HIS A CD2 1 
ATOM   1326 C CE1 . HIS A 1 173 ? 31.38384 23.52518 10.29954  1.000 39.78171  ? 173 HIS A CE1 1 
ATOM   1327 N NE2 . HIS A 1 173 ? 31.89220 22.64182 11.13946  1.000 39.16451  ? 173 HIS A NE2 1 
ATOM   1328 N N   . PRO A 1 174 ? 28.64731 21.29154 8.20344   1.000 36.21332  ? 174 PRO A N   1 
ATOM   1329 C CA  . PRO A 1 174 ? 27.44127 22.02911 7.79513   1.000 36.14274  ? 174 PRO A CA  1 
ATOM   1330 C C   . PRO A 1 174 ? 27.69788 23.46331 7.36855   1.000 38.02674  ? 174 PRO A C   1 
ATOM   1331 O O   . PRO A 1 174 ? 26.75988 24.12015 6.90420   1.000 39.94196  ? 174 PRO A O   1 
ATOM   1332 C CB  . PRO A 1 174 ? 26.55537 21.97958 9.04946   1.000 37.84684  ? 174 PRO A CB  1 
ATOM   1333 C CG  . PRO A 1 174 ? 27.16717 20.93920 9.94048   1.000 38.03948  ? 174 PRO A CG  1 
ATOM   1334 C CD  . PRO A 1 174 ? 28.62627 20.95740 9.63619   1.000 37.09650  ? 174 PRO A CD  1 
ATOM   1335 N N   . SER A 1 175 ? 28.91590 23.98296 7.51841   1.000 36.98161  ? 175 SER A N   1 
ATOM   1336 C CA  . SER A 1 175 ? 29.21525 25.29377 6.96140   1.000 38.22609  ? 175 SER A CA  1 
ATOM   1337 C C   . SER A 1 175 ? 29.31878 25.26977 5.44062   1.000 39.32571  ? 175 SER A C   1 
ATOM   1338 O O   . SER A 1 175 ? 29.39564 26.33741 4.82130   1.000 40.02967  ? 175 SER A O   1 
ATOM   1339 C CB  . SER A 1 175 ? 30.51319 25.83152 7.55961   1.000 40.08317  ? 175 SER A CB  1 
ATOM   1340 O OG  . SER A 1 175 ? 31.57823 24.92637 7.33685   1.000 40.67782  ? 175 SER A OG  1 
ATOM   1341 N N   . ILE A 1 176 ? 29.32793 24.09001 4.82940   1.000 37.99583  ? 176 ILE A N   1 
ATOM   1342 C CA  . ILE A 1 176 ? 29.42142 23.95958 3.38030   1.000 37.27728  ? 176 ILE A CA  1 
ATOM   1343 C C   . ILE A 1 176 ? 28.01100 23.94810 2.80453   1.000 36.52383  ? 176 ILE A C   1 
ATOM   1344 O O   . ILE A 1 176 ? 27.22001 23.04664 3.09814   1.000 35.93581  ? 176 ILE A O   1 
ATOM   1345 C CB  . ILE A 1 176 ? 30.18667 22.68795 2.98908   1.000 36.31994  ? 176 ILE A CB  1 
ATOM   1346 C CG1 . ILE A 1 176 ? 31.55918 22.66726 3.66524   1.000 35.26720  ? 176 ILE A CG1 1 
ATOM   1347 C CG2 . ILE A 1 176 ? 30.32876 22.60075 1.48113   1.000 36.17258  ? 176 ILE A CG2 1 
ATOM   1348 C CD1 . ILE A 1 176 ? 32.31051 21.35947 3.48824   1.000 34.82146  ? 176 ILE A CD1 1 
ATOM   1349 N N   . GLU A 1 177 ? 27.69282 24.94702 1.98471   1.000 34.56466  ? 177 GLU A N   1 
ATOM   1350 C CA  . GLU A 1 177 ? 26.36001 25.05423 1.39315   1.000 36.49979  ? 177 GLU A CA  1 
ATOM   1351 C C   . GLU A 1 177 ? 26.30127 24.11179 0.20013   1.000 36.24124  ? 177 GLU A C   1 
ATOM   1352 O O   . GLU A 1 177 ? 26.69001 24.45901 -0.91632  1.000 35.00276  ? 177 GLU A O   1 
ATOM   1353 C CB  . GLU A 1 177 ? 26.05793 26.48994 0.98823   1.000 39.29815  ? 177 GLU A CB  1 
ATOM   1354 C CG  . GLU A 1 177 ? 26.32432 27.51333 2.08140   1.000 41.85166  ? 177 GLU A CG  1 
ATOM   1355 C CD  . GLU A 1 177 ? 25.80925 28.88738 1.71547   0.700 45.46730  ? 177 GLU A CD  1 
ATOM   1356 O OE1 . GLU A 1 177 ? 24.62419 29.16795 1.99046   0.700 48.97519  ? 177 GLU A OE1 1 
ATOM   1357 O OE2 . GLU A 1 177 ? 26.58069 29.67789 1.13216   0.700 44.30365  ? 177 GLU A OE2 1 
ATOM   1358 N N   . ALA A 1 178 ? 25.80132 22.90439 0.44013   1.000 33.59838  ? 178 ALA A N   1 
ATOM   1359 C CA  . ALA A 1 178 ? 25.83852 21.85678 -0.56747  1.000 32.41175  ? 178 ALA A CA  1 
ATOM   1360 C C   . ALA A 1 178 ? 24.73624 20.85081 -0.27640  1.000 31.74098  ? 178 ALA A C   1 
ATOM   1361 O O   . ALA A 1 178 ? 24.07330 20.90183 0.76265   1.000 32.03205  ? 178 ALA A O   1 
ATOM   1362 C CB  . ALA A 1 178 ? 27.20845 21.17045 -0.60243  1.000 32.58542  ? 178 ALA A CB  1 
ATOM   1363 N N   . MET A 1 179 ? 24.53898 19.94330 -1.23004  1.000 30.21195  ? 179 MET A N   1 
ATOM   1364 C CA  . MET A 1 179 ? 23.67903 18.78323 -1.06359  1.000 29.30477  ? 179 MET A CA  1 
ATOM   1365 C C   . MET A 1 179 ? 24.40540 17.58299 -1.64921  1.000 31.59788  ? 179 MET A C   1 
ATOM   1366 O O   . MET A 1 179 ? 25.23430 17.72431 -2.55584  1.000 27.66249  ? 179 MET A O   1 
ATOM   1367 C CB  . MET A 1 179 ? 22.31202 18.98180 -1.73921  1.000 27.22801  ? 179 MET A CB  1 
ATOM   1368 C CG  . MET A 1 179 ? 22.42133 19.23384 -3.26197  1.000 30.66914  ? 179 MET A CG  1 
ATOM   1369 S SD  . MET A 1 179 ? 20.83673 19.54490 -4.03793  1.000 29.14524  ? 179 MET A SD  1 
ATOM   1370 C CE  . MET A 1 179 ? 21.36715 19.77528 -5.73973  1.000 30.63126  ? 179 MET A CE  1 
ATOM   1371 N N   . GLN A 1 180 ? 24.10707 16.39869 -1.11914  1.000 27.90199  ? 180 GLN A N   1 
ATOM   1372 C CA  . GLN A 1 180 ? 24.82877 15.19445 -1.50710  1.000 28.32733  ? 180 GLN A CA  1 
ATOM   1373 C C   . GLN A 1 180 ? 23.85632 14.11341 -1.95126  1.000 29.46867  ? 180 GLN A C   1 
ATOM   1374 O O   . GLN A 1 180 ? 22.89550 13.80616 -1.23742  1.000 27.46046  ? 180 GLN A O   1 
ATOM   1375 C CB  . GLN A 1 180 ? 25.70326 14.67857 -0.35765  1.000 27.21452  ? 180 GLN A CB  1 
ATOM   1376 C CG  . GLN A 1 180 ? 26.49587 13.44913 -0.75318  1.000 25.51562  ? 180 GLN A CG  1 
ATOM   1377 C CD  . GLN A 1 180 ? 27.50380 13.01806 0.28401   1.000 28.98376  ? 180 GLN A CD  1 
ATOM   1378 O OE1 . GLN A 1 180 ? 28.24497 12.06061 0.06697   1.000 25.72763  ? 180 GLN A OE1 1 
ATOM   1379 N NE2 . GLN A 1 180 ? 27.52973 13.71200 1.43336   1.000 23.81214  ? 180 GLN A NE2 1 
ATOM   1380 N N   . LEU A 1 181 ? 24.12431 13.52182 -3.11603  1.000 26.31073  ? 181 LEU A N   1 
ATOM   1381 C CA  . LEU A 1 181 ? 23.25745 12.51760 -3.72298  1.000 27.73009  ? 181 LEU A CA  1 
ATOM   1382 C C   . LEU A 1 181 ? 23.92050 11.15001 -3.62041  1.000 29.01341  ? 181 LEU A C   1 
ATOM   1383 O O   . LEU A 1 181 ? 25.01566 10.94822 -4.15783  1.000 26.55185  ? 181 LEU A O   1 
ATOM   1384 C CB  . LEU A 1 181 ? 22.97447 12.86049 -5.18861  1.000 28.10592  ? 181 LEU A CB  1 
ATOM   1385 C CG  . LEU A 1 181 ? 22.16128 11.85419 -6.00771  1.000 29.41047  ? 181 LEU A CG  1 
ATOM   1386 C CD1 . LEU A 1 181 ? 20.68605 11.90498 -5.61687  1.000 26.18621  ? 181 LEU A CD1 1 
ATOM   1387 C CD2 . LEU A 1 181 ? 22.34202 12.11459 -7.51928  1.000 25.30627  ? 181 LEU A CD2 1 
ATOM   1388 N N   . THR A 1 182 ? 23.25493 10.20789 -2.95083  1.000 25.37879  ? 182 THR A N   1 
ATOM   1389 C CA  . THR A 1 182 ? 23.76426 8.84884  -2.83037  1.000 25.73362  ? 182 THR A CA  1 
ATOM   1390 C C   . THR A 1 182 ? 22.80822 7.85376  -3.47371  1.000 29.30511  ? 182 THR A C   1 
ATOM   1391 O O   . THR A 1 182 ? 21.59146 8.07229  -3.51714  1.000 28.33306  ? 182 THR A O   1 
ATOM   1392 C CB  . THR A 1 182 ? 23.98957 8.46183  -1.36498  1.000 30.34792  ? 182 THR A CB  1 
ATOM   1393 O OG1 . THR A 1 182 ? 22.80019 8.72952  -0.61642  1.000 28.49355  ? 182 THR A OG1 1 
ATOM   1394 C CG2 . THR A 1 182 ? 25.14979 9.25852  -0.78177  1.000 24.51974  ? 182 THR A CG2 1 
ATOM   1395 N N   . GLU A 1 183 ? 23.37645 6.74528  -3.95008  1.000 27.21252  ? 183 GLU A N   1 
ATOM   1396 C CA  . GLU A 1 183 ? 22.62597 5.67686  -4.59679  1.000 28.95656  ? 183 GLU A CA  1 
ATOM   1397 C C   . GLU A 1 183 ? 22.17427 4.62708  -3.58649  1.000 30.97458  ? 183 GLU A C   1 
ATOM   1398 O O   . GLU A 1 183 ? 22.88197 4.31805  -2.62647  1.000 27.90191  ? 183 GLU A O   1 
ATOM   1399 C CB  . GLU A 1 183 ? 23.47707 4.99345  -5.67069  1.000 31.73825  ? 183 GLU A CB  1 
ATOM   1400 C CG  . GLU A 1 183 ? 24.06369 5.92974  -6.71280  1.000 29.23820  ? 183 GLU A CG  1 
ATOM   1401 C CD  . GLU A 1 183 ? 24.82057 5.18366  -7.79926  1.000 32.75786  ? 183 GLU A CD  1 
ATOM   1402 O OE1 . GLU A 1 183 ? 25.07527 3.97351  -7.62523  1.000 33.99071  ? 183 GLU A OE1 1 
ATOM   1403 O OE2 . GLU A 1 183 ? 25.16165 5.80813  -8.82542  1.000 30.53432  ? 183 GLU A OE2 1 
ATOM   1404 N N   . MET A 1 184 ? 20.98949 4.06333  -3.82757  1.000 27.74508  ? 184 MET A N   1 
ATOM   1405 C CA  . MET A 1 184 ? 20.50564 2.87911  -3.12187  1.000 30.71820  ? 184 MET A CA  1 
ATOM   1406 C C   . MET A 1 184 ? 20.54438 1.70270  -4.08951  1.000 31.23321  ? 184 MET A C   1 
ATOM   1407 O O   . MET A 1 184 ? 19.74060 1.64790  -5.02570  1.000 35.07760  ? 184 MET A O   1 
ATOM   1408 C CB  . MET A 1 184 ? 19.08181 3.07148  -2.60458  1.000 32.33735  ? 184 MET A CB  1 
ATOM   1409 C CG  . MET A 1 184 ? 18.83676 4.30852  -1.76644  1.000 33.03289  ? 184 MET A CG  1 
ATOM   1410 S SD  . MET A 1 184 ? 17.08885 4.38902  -1.31899  1.000 39.28266  ? 184 MET A SD  1 
ATOM   1411 C CE  . MET A 1 184 ? 17.06081 5.90262  -0.36744  1.000 35.50801  ? 184 MET A CE  1 
ATOM   1412 N N   . ALA A 1 185 ? 21.45484 0.75643  -3.84552  1.000 28.61296  ? 185 ALA A N   1 
ATOM   1413 C CA  . ALA A 1 185 ? 21.54488 -0.49957 -4.58879  1.000 32.99952  ? 185 ALA A CA  1 
ATOM   1414 C C   . ALA A 1 185 ? 21.32799 -0.34232 -6.09116  1.000 33.72536  ? 185 ALA A C   1 
ATOM   1415 O O   . ALA A 1 185 ? 20.30693 -0.78759 -6.62029  1.000 30.40002  ? 185 ALA A O   1 
ATOM   1416 C CB  . ALA A 1 185 ? 20.53581 -1.51010 -4.04291  1.000 29.93974  ? 185 ALA A CB  1 
ATOM   1417 N N   . SER A 1 186 ? 22.27136 0.28089  -6.78508  1.000 34.24587  ? 186 SER A N   1 
ATOM   1418 C CA  . SER A 1 186 ? 22.15872 0.42779  -8.22799  1.000 36.40243  ? 186 SER A CA  1 
ATOM   1419 C C   . SER A 1 186 ? 22.59821 -0.84539 -8.94035  1.000 37.08700  ? 186 SER A C   1 
ATOM   1420 O O   . SER A 1 186 ? 23.50157 -1.55845 -8.48905  1.000 37.49875  ? 186 SER A O   1 
ATOM   1421 C CB  . SER A 1 186 ? 23.00986 1.59871  -8.71143  1.000 37.60049  ? 186 SER A CB  1 
ATOM   1422 O OG  . SER A 1 186 ? 24.38339 1.34178  -8.47599  1.000 43.74024  ? 186 SER A OG  1 
ATOM   1423 N N   . ILE A 1 187 ? 21.95754 -1.12492 -10.07312 1.000 39.42687  ? 187 ILE A N   1 
ATOM   1424 C CA  . ILE A 1 187 ? 22.39684 -2.20451 -10.94717 1.000 39.99404  ? 187 ILE A CA  1 
ATOM   1425 C C   . ILE A 1 187 ? 23.46063 -1.65964 -11.89117 1.000 40.28560  ? 187 ILE A C   1 
ATOM   1426 O O   . ILE A 1 187 ? 23.29564 -0.59114 -12.49306 1.000 40.67999  ? 187 ILE A O   1 
ATOM   1427 C CB  . ILE A 1 187 ? 21.21552 -2.82587 -11.71607 1.000 41.81819  ? 187 ILE A CB  1 
ATOM   1428 C CG1 . ILE A 1 187 ? 21.65814 -4.10768 -12.42416 1.000 39.56852  ? 187 ILE A CG1 1 
ATOM   1429 C CG2 . ILE A 1 187 ? 20.63458 -1.86952 -12.73429 1.000 46.06981  ? 187 ILE A CG2 1 
ATOM   1430 C CD1 . ILE A 1 187 ? 20.50470 -4.96861 -12.91211 1.000 51.85849  ? 187 ILE A CD1 1 
ATOM   1431 N N   . ASN A 1 188 ? 24.57453 -2.37318 -11.99058 1.000 41.49341  ? 188 ASN A N   1 
ATOM   1432 C CA  . ASN A 1 188 ? 25.65032 -2.00698 -12.90066 1.000 43.74780  ? 188 ASN A CA  1 
ATOM   1433 C C   . ASN A 1 188 ? 26.11325 -3.26368 -13.61045 1.000 45.35531  ? 188 ASN A C   1 
ATOM   1434 O O   . ASN A 1 188 ? 26.58429 -4.20675 -12.96667 1.000 42.80017  ? 188 ASN A O   1 
ATOM   1435 C CB  . ASN A 1 188 ? 26.81213 -1.34023 -12.16166 1.000 44.23402  ? 188 ASN A CB  1 
ATOM   1436 C CG  . ASN A 1 188 ? 26.56508 0.12884  -11.90335 1.000 42.38203  ? 188 ASN A CG  1 
ATOM   1437 O OD1 . ASN A 1 188 ? 26.93452 0.98316  -12.70897 1.000 41.57583  ? 188 ASN A OD1 1 
ATOM   1438 N ND2 . ASN A 1 188 ? 25.93332 0.43248  -10.77748 1.000 38.84669  ? 188 ASN A ND2 1 
ATOM   1439 N N   . ASN A 1 189 ? 25.95619 -3.28288 -14.92634 1.000 46.68884  ? 189 ASN A N   1 
ATOM   1440 C CA  . ASN A 1 189 ? 26.42786 -4.39003 -15.73872 1.000 48.71244  ? 189 ASN A CA  1 
ATOM   1441 C C   . ASN A 1 189 ? 26.91961 -3.80749 -17.06015 1.000 52.33601  ? 189 ASN A C   1 
ATOM   1442 O O   . ASN A 1 189 ? 27.29451 -2.63172 -17.13368 1.000 53.83522  ? 189 ASN A O   1 
ATOM   1443 C CB  . ASN A 1 189 ? 25.31954 -5.44450 -15.90194 1.000 48.11270  ? 189 ASN A CB  1 
ATOM   1444 C CG  . ASN A 1 189 ? 23.99707 -4.84455 -16.34774 1.000 50.41885  ? 189 ASN A CG  1 
ATOM   1445 O OD1 . ASN A 1 189 ? 23.96483 -3.89406 -17.12909 1.000 52.45162  ? 189 ASN A OD1 1 
ATOM   1446 N ND2 . ASN A 1 189 ? 22.89691 -5.39242 -15.83950 1.000 48.15936  ? 189 ASN A ND2 1 
ATOM   1447 N N   . ARG A 1 190 ? 26.91797 -4.63079 -18.10649 1.000 57.95033  ? 190 ARG A N   1 
ATOM   1448 C CA  . ARG A 1 190 ? 27.33428 -4.15977 -19.42375 1.000 58.92506  ? 190 ARG A CA  1 
ATOM   1449 C C   . ARG A 1 190 ? 26.41961 -3.05069 -19.93095 1.000 58.06114  ? 190 ARG A C   1 
ATOM   1450 O O   . ARG A 1 190 ? 26.88953 -2.02400 -20.43502 1.000 65.82789  ? 190 ARG A O   1 
ATOM   1451 C CB  . ARG A 1 190 ? 27.34764 -5.32685 -20.40685 1.000 58.89995  ? 190 ARG A CB  1 
ATOM   1452 C CG  . ARG A 1 190 ? 28.71920 -5.87269 -20.73181 0.700 58.42959  ? 190 ARG A CG  1 
ATOM   1453 C CD  . ARG A 1 190 ? 28.63110 -6.86896 -21.87440 0.700 57.75533  ? 190 ARG A CD  1 
ATOM   1454 N NE  . ARG A 1 190 ? 27.64907 -6.46882 -22.87618 0.600 63.60557  ? 190 ARG A NE  1 
ATOM   1455 C CZ  . ARG A 1 190 ? 26.46821 -7.04965 -23.04335 0.600 63.35936  ? 190 ARG A CZ  1 
ATOM   1456 N NH1 . ARG A 1 190 ? 26.09575 -8.08267 -22.30494 0.600 60.21547  ? 190 ARG A NH1 1 
ATOM   1457 N NH2 . ARG A 1 190 ? 25.63899 -6.57851 -23.97027 0.600 63.71138  ? 190 ARG A NH2 1 
ATOM   1458 N N   . VAL A 1 191 ? 25.10506 -3.23996 -19.80014 1.000 57.03482  ? 191 VAL A N   1 
ATOM   1459 C CA  . VAL A 1 191 ? 24.14527 -2.32640 -20.40930 1.000 58.00827  ? 191 VAL A CA  1 
ATOM   1460 C C   . VAL A 1 191 ? 23.67280 -1.20489 -19.48341 1.000 55.50337  ? 191 VAL A C   1 
ATOM   1461 O O   . VAL A 1 191 ? 23.11308 -0.21271 -19.97143 1.000 55.74605  ? 191 VAL A O   1 
ATOM   1462 C CB  . VAL A 1 191 ? 22.92587 -3.11123 -20.92532 1.000 61.95383  ? 191 VAL A CB  1 
ATOM   1463 C CG1 . VAL A 1 191 ? 23.34774 -4.09438 -22.00688 1.000 64.18655  ? 191 VAL A CG1 1 
ATOM   1464 C CG2 . VAL A 1 191 ? 22.23911 -3.84039 -19.78091 1.000 58.85415  ? 191 VAL A CG2 1 
ATOM   1465 N N   . TYR A 1 192 ? 23.86886 -1.32763 -18.17090 1.000 53.85156  ? 192 TYR A N   1 
ATOM   1466 C CA  . TYR A 1 192 ? 23.38806 -0.33572 -17.21473 1.000 51.03044  ? 192 TYR A CA  1 
ATOM   1467 C C   . TYR A 1 192 ? 24.56853 0.20823  -16.41933 1.000 49.11745  ? 192 TYR A C   1 
ATOM   1468 O O   . TYR A 1 192 ? 25.31166 -0.56299 -15.80215 1.000 47.68556  ? 192 TYR A O   1 
ATOM   1469 C CB  . TYR A 1 192 ? 22.33276 -0.93840 -16.28147 1.000 50.05457  ? 192 TYR A CB  1 
ATOM   1470 C CG  . TYR A 1 192 ? 21.17513 -1.60091 -17.00244 0.700 51.45579  ? 192 TYR A CG  1 
ATOM   1471 C CD1 . TYR A 1 192 ? 20.67200 -1.07721 -18.18702 0.700 52.65756  ? 192 TYR A CD1 1 
ATOM   1472 C CD2 . TYR A 1 192 ? 20.58911 -2.75528 -16.49712 0.700 51.06011  ? 192 TYR A CD2 1 
ATOM   1473 C CE1 . TYR A 1 192 ? 19.61912 -1.68259 -18.84813 0.700 52.74768  ? 192 TYR A CE1 1 
ATOM   1474 C CE2 . TYR A 1 192 ? 19.53443 -3.36706 -17.14961 0.700 52.49657  ? 192 TYR A CE2 1 
ATOM   1475 C CZ  . TYR A 1 192 ? 19.05278 -2.82566 -18.32366 0.700 53.10750  ? 192 TYR A CZ  1 
ATOM   1476 O OH  . TYR A 1 192 ? 18.00509 -3.43190 -18.97871 0.700 57.17585  ? 192 TYR A OH  1 
ATOM   1477 N N   . ARG A 1 193 ? 24.72766 1.53501  -16.42254 1.000 45.77009  ? 193 ARG A N   1 
ATOM   1478 C CA  . ARG A 1 193 ? 25.89408 2.20436  -15.85004 1.000 43.28182  ? 193 ARG A CA  1 
ATOM   1479 C C   . ARG A 1 193 ? 25.44018 3.39256  -15.01770 1.000 41.43544  ? 193 ARG A C   1 
ATOM   1480 O O   . ARG A 1 193 ? 24.77290 4.29039  -15.54050 1.000 36.28657  ? 193 ARG A O   1 
ATOM   1481 C CB  . ARG A 1 193 ? 26.84653 2.69479  -16.94876 1.000 47.23833  ? 193 ARG A CB  1 
ATOM   1482 C CG  . ARG A 1 193 ? 27.25238 1.66816  -17.99712 0.800 52.90444  ? 193 ARG A CG  1 
ATOM   1483 C CD  . ARG A 1 193 ? 28.14354 0.60651  -17.39017 0.700 55.45281  ? 193 ARG A CD  1 
ATOM   1484 N NE  . ARG A 1 193 ? 28.98022 1.15837  -16.33266 0.700 54.53437  ? 193 ARG A NE  1 
ATOM   1485 C CZ  . ARG A 1 193 ? 29.62305 0.42873  -15.43218 0.700 57.96643  ? 193 ARG A CZ  1 
ATOM   1486 N NH1 . ARG A 1 193 ? 29.57095 -0.89313 -15.45043 0.700 58.73845  ? 193 ARG A NH1 1 
ATOM   1487 N NH2 . ARG A 1 193 ? 30.33093 1.04047  -14.48669 0.700 53.10587  ? 193 ARG A NH2 1 
ATOM   1488 N N   . THR A 1 194 ? 25.82270 3.41554  -13.73958 1.000 34.14080  ? 194 THR A N   1 
ATOM   1489 C CA  . THR A 1 194 ? 25.68703 4.59617  -12.89639 1.000 33.47742  ? 194 THR A CA  1 
ATOM   1490 C C   . THR A 1 194 ? 27.06144 5.00202  -12.37803 1.000 32.50312  ? 194 THR A C   1 
ATOM   1491 O O   . THR A 1 194 ? 28.03979 4.26457  -12.50686 1.000 31.16806  ? 194 THR A O   1 
ATOM   1492 C CB  . THR A 1 194 ? 24.72995 4.35621  -11.71727 1.000 35.30754  ? 194 THR A CB  1 
ATOM   1493 O OG1 . THR A 1 194 ? 25.35604 3.51369  -10.74122 1.000 34.06918  ? 194 THR A OG1 1 
ATOM   1494 C CG2 . THR A 1 194 ? 23.44860 3.70470  -12.19687 1.000 35.12654  ? 194 THR A CG2 1 
ATOM   1495 N N   . ILE A 1 195 ? 27.13087 6.19087  -11.77355 1.000 28.64065  ? 195 ILE A N   1 
ATOM   1496 C CA  . ILE A 1 195 ? 28.42842 6.68416  -11.32502 1.000 31.40935  ? 195 ILE A CA  1 
ATOM   1497 C C   . ILE A 1 195 ? 28.89272 5.92635  -10.08458 1.000 29.98563  ? 195 ILE A C   1 
ATOM   1498 O O   . ILE A 1 195 ? 30.09829 5.74424  -9.87479  1.000 29.84407  ? 195 ILE A O   1 
ATOM   1499 C CB  . ILE A 1 195 ? 28.37524 8.20683  -11.08778 1.000 27.86398  ? 195 ILE A CB  1 
ATOM   1500 C CG1 . ILE A 1 195 ? 29.77109 8.75187  -10.78283 1.000 28.30046  ? 195 ILE A CG1 1 
ATOM   1501 C CG2 . ILE A 1 195 ? 27.41408 8.55744  -9.95745  1.000 28.98040  ? 195 ILE A CG2 1 
ATOM   1502 C CD1 . ILE A 1 195 ? 30.76310 8.56984  -11.92234 1.000 32.03436  ? 195 ILE A CD1 1 
ATOM   1503 N N   . GLY A 1 196 ? 27.96017 5.44560  -9.26492  1.000 30.48962  ? 196 GLY A N   1 
ATOM   1504 C CA  . GLY A 1 196 ? 28.31365 4.73806  -8.05021  1.000 30.18670  ? 196 GLY A CA  1 
ATOM   1505 C C   . GLY A 1 196 ? 28.62321 5.68832  -6.91272  1.000 31.56299  ? 196 GLY A C   1 
ATOM   1506 O O   . GLY A 1 196 ? 27.94780 5.68043  -5.87875  1.000 31.86783  ? 196 GLY A O   1 
ATOM   1507 N N   . SER A 1 197 ? 29.62258 6.53909  -7.11912  1.000 30.60859  ? 197 SER A N   1 
ATOM   1508 C CA  . SER A 1 197 ? 30.10240 7.42431  -6.07173  1.000 29.60938  ? 197 SER A CA  1 
ATOM   1509 C C   . SER A 1 197 ? 29.00964 8.38929  -5.61624  1.000 28.67308  ? 197 SER A C   1 
ATOM   1510 O O   . SER A 1 197 ? 28.13808 8.77637  -6.39880  1.000 26.79323  ? 197 SER A O   1 
ATOM   1511 C CB  . SER A 1 197 ? 31.30334 8.22587  -6.57138  1.000 26.93035  ? 197 SER A CB  1 
ATOM   1512 O OG  . SER A 1 197 ? 32.26867 7.36612  -7.14326  1.000 29.07808  ? 197 SER A OG  1 
ATOM   1513 N N   . PRO A 1 198 ? 29.03335 8.79104  -4.34772  1.000 29.52486  ? 198 PRO A N   1 
ATOM   1514 C CA  . PRO A 1 198 ? 28.23040 9.94421  -3.93270  1.000 27.92812  ? 198 PRO A CA  1 
ATOM   1515 C C   . PRO A 1 198 ? 28.64090 11.17550 -4.72573  1.000 25.61903  ? 198 PRO A C   1 
ATOM   1516 O O   . PRO A 1 198 ? 29.80182 11.33058 -5.10938  1.000 26.73466  ? 198 PRO A O   1 
ATOM   1517 C CB  . PRO A 1 198 ? 28.56820 10.10104 -2.44402  1.000 27.86024  ? 198 PRO A CB  1 
ATOM   1518 C CG  . PRO A 1 198 ? 29.11266 8.76485  -2.02141  1.000 29.47045  ? 198 PRO A CG  1 
ATOM   1519 C CD  . PRO A 1 198 ? 29.80092 8.20535  -3.23674  1.000 28.24388  ? 198 PRO A CD  1 
ATOM   1520 N N   . LEU A 1 199 ? 27.67273 12.05334 -4.97963  1.000 23.94045  ? 199 LEU A N   1 
ATOM   1521 C CA  . LEU A 1 199 ? 27.91144 13.30291 -5.69064  1.000 28.02447  ? 199 LEU A CA  1 
ATOM   1522 C C   . LEU A 1 199 ? 27.57317 14.46380 -4.77065  1.000 25.85893  ? 199 LEU A C   1 
ATOM   1523 O O   . LEU A 1 199 ? 26.49975 14.48089 -4.16302  1.000 27.60192  ? 199 LEU A O   1 
ATOM   1524 C CB  . LEU A 1 199 ? 27.07000 13.38933 -6.97506  1.000 26.04153  ? 199 LEU A CB  1 
ATOM   1525 C CG  . LEU A 1 199 ? 27.21073 12.27203 -8.00097  1.000 26.57869  ? 199 LEU A CG  1 
ATOM   1526 C CD1 . LEU A 1 199 ? 26.43733 12.62883 -9.27897  1.000 27.43394  ? 199 LEU A CD1 1 
ATOM   1527 C CD2 . LEU A 1 199 ? 28.67689 12.00248 -8.31297  1.000 27.43252  ? 199 LEU A CD2 1 
ATOM   1528 N N   . VAL A 1 200 ? 28.47562 15.43581 -4.68085  1.000 26.55094  ? 200 VAL A N   1 
ATOM   1529 C CA  . VAL A 1 200 ? 28.29182 16.61089 -3.83234  1.000 29.58266  ? 200 VAL A CA  1 
ATOM   1530 C C   . VAL A 1 200 ? 28.14492 17.82994 -4.73420  1.000 30.31665  ? 200 VAL A C   1 
ATOM   1531 O O   . VAL A 1 200 ? 29.03320 18.12249 -5.54773  1.000 30.91485  ? 200 VAL A O   1 
ATOM   1532 C CB  . VAL A 1 200 ? 29.45414 16.78359 -2.84157  1.000 28.93617  ? 200 VAL A CB  1 
ATOM   1533 C CG1 . VAL A 1 200 ? 29.35219 18.12950 -2.13082  1.000 31.21967  ? 200 VAL A CG1 1 
ATOM   1534 C CG2 . VAL A 1 200 ? 29.45188 15.64538 -1.82541  1.000 29.36418  ? 200 VAL A CG2 1 
ATOM   1535 N N   . PHE A 1 201 ? 27.01659 18.55095 -4.58145  1.000 30.25502  ? 201 PHE A N   1 
ATOM   1536 C CA  . PHE A 1 201 ? 26.59406 19.65657 -5.43297  1.000 31.26563  ? 201 PHE A CA  1 
ATOM   1537 C C   . PHE A 1 201 ? 26.61519 20.97866 -4.68139  1.000 33.56198  ? 201 PHE A C   1 
ATOM   1538 O O   . PHE A 1 201 ? 26.12936 21.04827 -3.54914  1.000 32.55825  ? 201 PHE A O   1 
ATOM   1539 C CB  . PHE A 1 201 ? 25.17868 19.41384 -5.96259  1.000 30.49189  ? 201 PHE A CB  1 
ATOM   1540 C CG  . PHE A 1 201 ? 25.06954 18.21182 -6.84579  1.000 32.38504  ? 201 PHE A CG  1 
ATOM   1541 C CD1 . PHE A 1 201 ? 25.39196 18.29747 -8.19119  1.000 31.15869  ? 201 PHE A CD1 1 
ATOM   1542 C CD2 . PHE A 1 201 ? 24.66054 16.99249 -6.33260  1.000 31.24061  ? 201 PHE A CD2 1 
ATOM   1543 C CE1 . PHE A 1 201 ? 25.30439 17.18673 -9.01154  1.000 30.81674  ? 201 PHE A CE1 1 
ATOM   1544 C CE2 . PHE A 1 201 ? 24.56884 15.87964 -7.14400  1.000 29.78256  ? 201 PHE A CE2 1 
ATOM   1545 C CZ  . PHE A 1 201 ? 24.89152 15.97711 -8.48760  1.000 30.51312  ? 201 PHE A CZ  1 
ATOM   1546 N N   . PRO A 1 202 ? 27.13089 22.04216 -5.28509  1.000 34.45657  ? 202 PRO A N   1 
ATOM   1547 C CA  . PRO A 1 202 ? 27.13962 23.35151 -4.62907  1.000 34.53904  ? 202 PRO A CA  1 
ATOM   1548 C C   . PRO A 1 202 ? 25.78816 24.04018 -4.78482  1.000 35.55413  ? 202 PRO A C   1 
ATOM   1549 O O   . PRO A 1 202 ? 24.86715 23.52664 -5.42199  1.000 32.59518  ? 202 PRO A O   1 
ATOM   1550 C CB  . PRO A 1 202 ? 28.23796 24.10384 -5.38164  1.000 37.27348  ? 202 PRO A CB  1 
ATOM   1551 C CG  . PRO A 1 202 ? 28.14032 23.55627 -6.77587  1.000 34.18364  ? 202 PRO A CG  1 
ATOM   1552 C CD  . PRO A 1 202 ? 27.74452 22.09704 -6.62650  1.000 34.34393  ? 202 PRO A CD  1 
ATOM   1553 N N   . LYS A 1 203 ? 25.68279 25.21915 -4.17162  1.000 36.04500  ? 203 LYS A N   1 
ATOM   1554 C CA  . LYS A 1 203 ? 24.51794 26.06842 -4.37346  1.000 39.21868  ? 203 LYS A CA  1 
ATOM   1555 C C   . LYS A 1 203 ? 24.34270 26.36136 -5.85543  1.000 37.63356  ? 203 LYS A C   1 
ATOM   1556 O O   . LYS A 1 203 ? 25.31421 26.45277 -6.60895  1.000 39.48571  ? 203 LYS A O   1 
ATOM   1557 C CB  . LYS A 1 203 ? 24.66371 27.39040 -3.61543  1.000 39.83510  ? 203 LYS A CB  1 
ATOM   1558 C CG  . LYS A 1 203 ? 24.15397 27.39272 -2.19177  0.800 40.65639  ? 203 LYS A CG  1 
ATOM   1559 C CD  . LYS A 1 203 ? 24.05380 28.82213 -1.67087  0.700 44.01365  ? 203 LYS A CD  1 
ATOM   1560 C CE  . LYS A 1 203 ? 25.32464 29.60781 -1.97573  0.700 44.76885  ? 203 LYS A CE  1 
ATOM   1561 N NZ  . LYS A 1 203 ? 25.18172 31.06040 -1.67037  0.700 49.47787  ? 203 LYS A NZ  1 
ATOM   1562 N N   . HIS A 1 204 ? 23.08309 26.49313 -6.26602  1.000 38.77491  ? 204 HIS A N   1 
ATOM   1563 C CA  . HIS A 1 204 ? 22.61694 26.88045 -7.59935  1.000 39.75610  ? 204 HIS A CA  1 
ATOM   1564 C C   . HIS A 1 204 ? 22.75349 25.76525 -8.63446  1.000 38.23236  ? 204 HIS A C   1 
ATOM   1565 O O   . HIS A 1 204 ? 22.38447 25.98201 -9.79030  1.000 39.33537  ? 204 HIS A O   1 
ATOM   1566 C CB  . HIS A 1 204 ? 23.31754 28.14473 -8.12407  1.000 40.95664  ? 204 HIS A CB  1 
ATOM   1567 C CG  . HIS A 1 204 ? 23.17437 29.32479 -7.21410  1.000 41.69889  ? 204 HIS A CG  1 
ATOM   1568 N ND1 . HIS A 1 204 ? 24.23324 29.85838 -6.51159  1.000 43.26203  ? 204 HIS A ND1 1 
ATOM   1569 C CD2 . HIS A 1 204 ? 22.08891 30.05775 -6.87163  1.000 43.79520  ? 204 HIS A CD2 1 
ATOM   1570 C CE1 . HIS A 1 204 ? 23.80936 30.87861 -5.78782  1.000 43.81228  ? 204 HIS A CE1 1 
ATOM   1571 N NE2 . HIS A 1 204 ? 22.51147 31.02004 -5.98689  1.000 44.50192  ? 204 HIS A NE2 1 
ATOM   1572 N N   . HIS A 1 205 ? 23.26563 24.59349 -8.27382  1.000 37.34105  ? 205 HIS A N   1 
ATOM   1573 C CA  . HIS A 1 205 ? 23.16655 23.43625 -9.14954  1.000 36.78377  ? 205 HIS A CA  1 
ATOM   1574 C C   . HIS A 1 205 ? 21.82308 22.75072 -8.93289  1.000 37.70624  ? 205 HIS A C   1 
ATOM   1575 O O   . HIS A 1 205 ? 21.38503 22.55833 -7.79649  1.000 34.06307  ? 205 HIS A O   1 
ATOM   1576 C CB  . HIS A 1 205 ? 24.30744 22.45083 -8.88725  1.000 35.60938  ? 205 HIS A CB  1 
ATOM   1577 C CG  . HIS A 1 205 ? 25.61785 22.86362 -9.48111  1.000 35.25338  ? 205 HIS A CG  1 
ATOM   1578 N ND1 . HIS A 1 205 ? 26.57358 21.95222 -9.87419  1.000 33.53630  ? 205 HIS A ND1 1 
ATOM   1579 C CD2 . HIS A 1 205 ? 26.13490 24.08753 -9.74272  1.000 37.66280  ? 205 HIS A CD2 1 
ATOM   1580 C CE1 . HIS A 1 205 ? 27.62348 22.59640 -10.35171 1.000 37.05403  ? 205 HIS A CE1 1 
ATOM   1581 N NE2 . HIS A 1 205 ? 27.38275 23.89340 -10.28424 1.000 38.56897  ? 205 HIS A NE2 1 
ATOM   1582 N N   . VAL A 1 206 ? 21.16430 22.38967 -10.02909 1.000 32.27015  ? 206 VAL A N   1 
ATOM   1583 C CA  . VAL A 1 206 ? 19.84960 21.76017 -9.98832  1.000 34.52542  ? 206 VAL A CA  1 
ATOM   1584 C C   . VAL A 1 206 ? 19.98952 20.32144 -10.46411 1.000 35.76641  ? 206 VAL A C   1 
ATOM   1585 O O   . VAL A 1 206 ? 20.42535 20.07133 -11.59432 1.000 34.59882  ? 206 VAL A O   1 
ATOM   1586 C CB  . VAL A 1 206 ? 18.82711 22.51989 -10.84543 1.000 37.09107  ? 206 VAL A CB  1 
ATOM   1587 C CG1 . VAL A 1 206 ? 17.50618 21.76523 -10.87854 1.000 38.27045  ? 206 VAL A CG1 1 
ATOM   1588 C CG2 . VAL A 1 206 ? 18.62992 23.92901 -10.31690 1.000 38.59274  ? 206 VAL A CG2 1 
ATOM   1589 N N   . VAL A 1 207 ? 19.61217 19.37865 -9.60964  1.000 33.34153  ? 207 VAL A N   1 
ATOM   1590 C CA  . VAL A 1 207 ? 19.54328 17.97027 -9.97498  1.000 33.67699  ? 207 VAL A CA  1 
ATOM   1591 C C   . VAL A 1 207 ? 18.08220 17.62037 -10.20778 1.000 36.76324  ? 207 VAL A C   1 
ATOM   1592 O O   . VAL A 1 207 ? 17.23824 17.81354 -9.32265  1.000 33.13868  ? 207 VAL A O   1 
ATOM   1593 C CB  . VAL A 1 207 ? 20.16210 17.07401 -8.89389  1.000 33.30780  ? 207 VAL A CB  1 
ATOM   1594 C CG1 . VAL A 1 207 ? 20.06503 15.61520 -9.31185  1.000 33.03265  ? 207 VAL A CG1 1 
ATOM   1595 C CG2 . VAL A 1 207 ? 21.60528 17.47571 -8.64460  1.000 32.63485  ? 207 VAL A CG2 1 
ATOM   1596 N N   . SER A 1 208 ? 17.78313 17.11390 -11.39965 1.000 32.47250  ? 208 SER A N   1 
ATOM   1597 C CA  . SER A 1 208 ? 16.42404 16.80783 -11.82032 1.000 37.52222  ? 208 SER A CA  1 
ATOM   1598 C C   . SER A 1 208 ? 16.31031 15.31552 -12.09139 1.000 38.73285  ? 208 SER A C   1 
ATOM   1599 O O   . SER A 1 208 ? 17.14189 14.74691 -12.80536 1.000 38.86030  ? 208 SER A O   1 
ATOM   1600 C CB  . SER A 1 208 ? 16.05145 17.61153 -13.07096 1.000 40.14307  ? 208 SER A CB  1 
ATOM   1601 O OG  . SER A 1 208 ? 14.78978 17.22288 -13.57841 1.000 43.68523  ? 208 SER A OG  1 
ATOM   1602 N N   . LEU A 1 209 ? 15.29772 14.68353 -11.50855 1.000 36.80966  ? 209 LEU A N   1 
ATOM   1603 C CA  . LEU A 1 209 ? 14.99556 13.28253 -11.76198 1.000 38.56542  ? 209 LEU A CA  1 
ATOM   1604 C C   . LEU A 1 209 ? 13.77846 13.21493 -12.66783 1.000 40.66544  ? 209 LEU A C   1 
ATOM   1605 O O   . LEU A 1 209 ? 12.75163 13.83771 -12.38091 1.000 41.72567  ? 209 LEU A O   1 
ATOM   1606 C CB  . LEU A 1 209 ? 14.73091 12.52189 -10.46071 1.000 38.20297  ? 209 LEU A CB  1 
ATOM   1607 C CG  . LEU A 1 209 ? 15.80901 12.55845 -9.37965  1.000 35.45671  ? 209 LEU A CG  1 
ATOM   1608 C CD1 . LEU A 1 209 ? 15.39623 11.67710 -8.20423  1.000 36.05801  ? 209 LEU A CD1 1 
ATOM   1609 C CD2 . LEU A 1 209 ? 17.15686 12.12632 -9.93870  1.000 33.06717  ? 209 LEU A CD2 1 
ATOM   1610 N N   . GLN A 1 210 ? 13.89623 12.47360 -13.76418 1.000 39.88205  ? 210 GLN A N   1 
ATOM   1611 C CA  . GLN A 1 210 ? 12.83645 12.42613 -14.75186 1.000 43.67638  ? 210 GLN A CA  1 
ATOM   1612 C C   . GLN A 1 210 ? 12.45565 10.97321 -15.00904 1.000 43.64994  ? 210 GLN A C   1 
ATOM   1613 O O   . GLN A 1 210 ? 13.33811 10.13466 -15.26566 1.000 42.39567  ? 210 GLN A O   1 
ATOM   1614 C CB  . GLN A 1 210 ? 13.27720 13.13745 -16.03991 1.000 44.24072  ? 210 GLN A CB  1 
ATOM   1615 C CG  . GLN A 1 210 ? 13.46465 14.63952 -15.82592 1.000 45.18981  ? 210 GLN A CG  1 
ATOM   1616 C CD  . GLN A 1 210 ? 14.22403 15.32826 -16.94367 1.000 48.45951  ? 210 GLN A CD  1 
ATOM   1617 O OE1 . GLN A 1 210 ? 14.28656 14.83363 -18.06752 1.000 49.56117  ? 210 GLN A OE1 1 
ATOM   1618 N NE2 . GLN A 1 210 ? 14.80758 16.48251 -16.63574 1.000 49.12043  ? 210 GLN A NE2 1 
ATOM   1619 N N   . PRO A 1 211 ? 11.17095 10.63362 -14.93479 1.000 45.52422  ? 211 PRO A N   1 
ATOM   1620 C CA  . PRO A 1 211 ? 10.76571 9.23250  -15.07705 1.000 45.97962  ? 211 PRO A CA  1 
ATOM   1621 C C   . PRO A 1 211 ? 11.05318 8.70693  -16.47036 1.000 48.31591  ? 211 PRO A C   1 
ATOM   1622 O O   . PRO A 1 211 ? 11.06757 9.45252  -17.45219 1.000 46.22244  ? 211 PRO A O   1 
ATOM   1623 C CB  . PRO A 1 211 ? 9.25608  9.26732  -14.80872 1.000 49.41900  ? 211 PRO A CB  1 
ATOM   1624 C CG  . PRO A 1 211 ? 9.01112  10.58154 -14.11522 1.000 51.92262  ? 211 PRO A CG  1 
ATOM   1625 C CD  . PRO A 1 211 ? 10.02094 11.51857 -14.69083 1.000 49.05745  ? 211 PRO A CD  1 
ATOM   1626 N N   . VAL A 1 212 ? 11.27657 7.40038  -16.54490 1.000 49.71494  ? 212 VAL A N   1 
ATOM   1627 C CA  . VAL A 1 212 ? 11.50100 6.71301  -17.81098 1.000 50.87655  ? 212 VAL A CA  1 
ATOM   1628 C C   . VAL A 1 212 ? 10.25860 5.95786  -18.25909 1.000 55.02455  ? 212 VAL A C   1 
ATOM   1629 O O   . VAL A 1 212 ? 9.81421  6.09805  -19.39780 1.000 56.60354  ? 212 VAL A O   1 
ATOM   1630 C CB  . VAL A 1 212 ? 12.72401 5.77682  -17.69596 1.000 48.07256  ? 212 VAL A CB  1 
ATOM   1631 C CG1 . VAL A 1 212 ? 12.87477 4.94249  -18.95501 1.000 50.59153  ? 212 VAL A CG1 1 
ATOM   1632 C CG2 . VAL A 1 212 ? 13.97947 6.59657  -17.43709 1.000 44.40982  ? 212 VAL A CG2 1 
ATOM   1633 N N   . ASN A 1 213 ? 9.67643  5.15816  -17.36821 1.000 54.86427  ? 213 ASN A N   1 
ATOM   1634 C CA  . ASN A 1 213 ? 8.43391  4.45863  -17.66718 1.000 58.66604  ? 213 ASN A CA  1 
ATOM   1635 C C   . ASN A 1 213 ? 7.37336  4.79270  -16.62598 1.000 58.53280  ? 213 ASN A C   1 
ATOM   1636 O O   . ASN A 1 213 ? 6.48410  5.61335  -16.87738 1.000 59.98789  ? 213 ASN A O   1 
ATOM   1637 C CB  . ASN A 1 213 ? 8.66870  2.94794  -17.73553 1.000 61.10842  ? 213 ASN A CB  1 
ATOM   1638 C CG  . ASN A 1 213 ? 9.34604  2.52248  -19.02531 0.700 63.85319  ? 213 ASN A CG  1 
ATOM   1639 O OD1 . ASN A 1 213 ? 8.96962  2.96323  -20.11212 0.600 66.30906  ? 213 ASN A OD1 1 
ATOM   1640 N ND2 . ASN A 1 213 ? 10.35700 1.66837  -18.91036 0.600 64.45028  ? 213 ASN A ND2 1 
ATOM   1641 N N   . ASP A 1 214 ? 7.46054  4.16487  -15.45745 1.000 58.72559  ? 214 ASP A N   1 
ATOM   1642 C CA  . ASP A 1 214 ? 6.51321  4.43863  -14.38575 1.000 59.01315  ? 214 ASP A CA  1 
ATOM   1643 C C   . ASP A 1 214 ? 6.67987  5.86690  -13.87961 1.000 55.50759  ? 214 ASP A C   1 
ATOM   1644 O O   . ASP A 1 214 ? 7.79922  6.35993  -13.71717 1.000 53.45202  ? 214 ASP A O   1 
ATOM   1645 C CB  . ASP A 1 214 ? 6.71086  3.44212  -13.24180 1.000 60.53399  ? 214 ASP A CB  1 
ATOM   1646 C CG  . ASP A 1 214 ? 5.56572  3.45797  -12.24427 1.000 66.51396  ? 214 ASP A CG  1 
ATOM   1647 O OD1 . ASP A 1 214 ? 5.30959  4.51813  -11.63658 1.000 62.31622  ? 214 ASP A OD1 1 
ATOM   1648 O OD2 . ASP A 1 214 ? 4.91296  2.40623  -12.07443 1.000 85.84280  ? 214 ASP A OD2 1 
ATOM   1649 N N   . LYS A 1 215 ? 5.55341  6.53331  -13.62764 1.000 54.95172  ? 215 LYS A N   1 
ATOM   1650 C CA  . LYS A 1 215 ? 5.55423  7.90912  -13.14624 1.000 54.18385  ? 215 LYS A CA  1 
ATOM   1651 C C   . LYS A 1 215 ? 5.09515  8.03786  -11.69488 1.000 52.29507  ? 215 LYS A C   1 
ATOM   1652 O O   . LYS A 1 215 ? 4.87967  9.16001  -11.22626 1.000 51.84071  ? 215 LYS A O   1 
ATOM   1653 C CB  . LYS A 1 215 ? 4.67792  8.78574  -14.04648 1.000 55.87243  ? 215 LYS A CB  1 
ATOM   1654 C CG  . LYS A 1 215 ? 5.10453  8.84076  -15.51089 0.800 58.02170  ? 215 LYS A CG  1 
ATOM   1655 C CD  . LYS A 1 215 ? 4.16801  9.74572  -16.31102 0.700 61.42364  ? 215 LYS A CD  1 
ATOM   1656 C CE  . LYS A 1 215 ? 4.45197  9.69140  -17.80805 0.600 64.46618  ? 215 LYS A CE  1 
ATOM   1657 N NZ  . LYS A 1 215 ? 5.74506  10.33551 -18.17094 0.600 66.43829  ? 215 LYS A NZ  1 
ATOM   1658 N N   . ASP A 1 216 ? 4.93281  6.92903  -10.97456 1.000 51.95252  ? 216 ASP A N   1 
ATOM   1659 C CA  . ASP A 1 216 ? 4.54661  6.95606  -9.56650  1.000 51.21740  ? 216 ASP A CA  1 
ATOM   1660 C C   . ASP A 1 216 ? 5.76959  6.69997  -8.69440  1.000 49.00799  ? 216 ASP A C   1 
ATOM   1661 O O   . ASP A 1 216 ? 6.53678  5.76675  -8.95478  1.000 49.27349  ? 216 ASP A O   1 
ATOM   1662 C CB  . ASP A 1 216 ? 3.46578  5.91583  -9.26873  1.000 51.68286  ? 216 ASP A CB  1 
ATOM   1663 C CG  . ASP A 1 216 ? 2.16863  6.19866  -9.99754  1.000 53.72161  ? 216 ASP A CG  1 
ATOM   1664 O OD1 . ASP A 1 216 ? 2.11652  7.19185  -10.75307 1.000 52.11308  ? 216 ASP A OD1 1 
ATOM   1665 O OD2 . ASP A 1 216 ? 1.20201  5.42774  -9.81543  1.000 53.85939  ? 216 ASP A OD2 1 
ATOM   1666 N N   . PHE A 1 217 ? 5.94383  7.52151  -7.65692  1.000 46.65787  ? 217 PHE A N   1 
ATOM   1667 C CA  . PHE A 1 217 ? 7.12020  7.44026  -6.80172  1.000 44.22273  ? 217 PHE A CA  1 
ATOM   1668 C C   . PHE A 1 217 ? 6.74907  7.68197  -5.34831  1.000 44.60257  ? 217 PHE A C   1 
ATOM   1669 O O   . PHE A 1 217 ? 5.92011  8.54297  -5.04212  1.000 43.89056  ? 217 PHE A O   1 
ATOM   1670 C CB  . PHE A 1 217 ? 8.18915  8.46149  -7.20739  1.000 42.75341  ? 217 PHE A CB  1 
ATOM   1671 C CG  . PHE A 1 217 ? 8.65582  8.31807  -8.61972  1.000 44.41845  ? 217 PHE A CG  1 
ATOM   1672 C CD1 . PHE A 1 217 ? 9.71994  7.48850  -8.92877  1.000 43.48579  ? 217 PHE A CD1 1 
ATOM   1673 C CD2 . PHE A 1 217 ? 8.03484  9.01635  -9.63837  1.000 46.92576  ? 217 PHE A CD2 1 
ATOM   1674 C CE1 . PHE A 1 217 ? 10.15411 7.35587  -10.23261 1.000 42.44057  ? 217 PHE A CE1 1 
ATOM   1675 C CE2 . PHE A 1 217 ? 8.46219  8.88590  -10.94704 1.000 47.87836  ? 217 PHE A CE2 1 
ATOM   1676 C CZ  . PHE A 1 217 ? 9.52313  8.05401  -11.24296 1.000 46.58805  ? 217 PHE A CZ  1 
ATOM   1677 N N   . GLN A 1 218 ? 7.39001  6.93384  -4.45889  1.000 43.33932  ? 218 GLN A N   1 
ATOM   1678 C CA  . GLN A 1 218 ? 7.30853  7.18607  -3.02619  1.000 42.42816  ? 218 GLN A CA  1 
ATOM   1679 C C   . GLN A 1 218 ? 8.41966  8.16966  -2.67979  1.000 39.96182  ? 218 GLN A C   1 
ATOM   1680 O O   . GLN A 1 218 ? 9.60500  7.84257  -2.79897  1.000 37.09857  ? 218 GLN A O   1 
ATOM   1681 C CB  . GLN A 1 218 ? 7.44054  5.88378  -2.24049  1.000 43.38676  ? 218 GLN A CB  1 
ATOM   1682 C CG  . GLN A 1 218 ? 7.08182  5.99802  -0.76266  1.000 45.94419  ? 218 GLN A CG  1 
ATOM   1683 C CD  . GLN A 1 218 ? 5.58313  5.93686  -0.51816  1.000 48.11520  ? 218 GLN A CD  1 
ATOM   1684 O OE1 . GLN A 1 218 ? 4.83112  5.39206  -1.32657  1.000 49.36232  ? 218 GLN A OE1 1 
ATOM   1685 N NE2 . GLN A 1 218 ? 5.14312  6.49577  0.60326   1.000 49.86667  ? 218 GLN A NE2 1 
ATOM   1686 N N   . ILE A 1 219 ? 8.04372  9.38305  -2.28298  1.000 39.54270  ? 219 ILE A N   1 
ATOM   1687 C CA  . ILE A 1 219 ? 8.99765  10.44656 -1.98551  1.000 38.51822  ? 219 ILE A CA  1 
ATOM   1688 C C   . ILE A 1 219 ? 8.96618  10.72732 -0.49255  1.000 41.65501  ? 219 ILE A C   1 
ATOM   1689 O O   . ILE A 1 219 ? 7.89662  10.97524 0.07749   1.000 41.51530  ? 219 ILE A O   1 
ATOM   1690 C CB  . ILE A 1 219 ? 8.69472  11.72454 -2.78440  1.000 41.23194  ? 219 ILE A CB  1 
ATOM   1691 C CG1 . ILE A 1 219 ? 8.67774  11.42263 -4.28349  1.000 38.83986  ? 219 ILE A CG1 1 
ATOM   1692 C CG2 . ILE A 1 219 ? 9.72450  12.79837 -2.47362  1.000 39.10993  ? 219 ILE A CG2 1 
ATOM   1693 C CD1 . ILE A 1 219 ? 8.31507  12.61566 -5.12931  1.000 42.69157  ? 219 ILE A CD1 1 
ATOM   1694 N N   . SER A 1 220 ? 10.13652 10.69525 0.13718   1.000 37.02406  ? 220 SER A N   1 
ATOM   1695 C CA  . SER A 1 220 ? 10.26551 11.02567 1.54627   1.000 39.16920  ? 220 SER A CA  1 
ATOM   1696 C C   . SER A 1 220 ? 10.95055 12.37488 1.70225   1.000 39.88712  ? 220 SER A C   1 
ATOM   1697 O O   . SER A 1 220 ? 11.82512 12.74444 0.91322   1.000 42.86143  ? 220 SER A O   1 
ATOM   1698 C CB  . SER A 1 220 ? 11.06861 9.96900  2.29778   1.000 36.89643  ? 220 SER A CB  1 
ATOM   1699 O OG  . SER A 1 220 ? 12.45564 10.13935 2.04663   1.000 36.75227  ? 220 SER A OG  1 
ATOM   1700 N N   . VAL A 1 221 ? 10.52805 13.11406 2.72231   1.000 37.04133  ? 221 VAL A N   1 
ATOM   1701 C CA  . VAL A 1 221 ? 11.19350 14.33568 3.15541   1.000 35.74275  ? 221 VAL A CA  1 
ATOM   1702 C C   . VAL A 1 221 ? 11.33433 14.21731 4.66177   1.000 39.98319  ? 221 VAL A C   1 
ATOM   1703 O O   . VAL A 1 221 ? 10.33495 14.29796 5.38728   1.000 35.92727  ? 221 VAL A O   1 
ATOM   1704 C CB  . VAL A 1 221 ? 10.41025 15.59969 2.77322   1.000 38.52124  ? 221 VAL A CB  1 
ATOM   1705 C CG1 . VAL A 1 221 ? 11.05125 16.82885 3.39393   1.000 38.21173  ? 221 VAL A CG1 1 
ATOM   1706 C CG2 . VAL A 1 221 ? 10.33282 15.73482 1.25472   1.000 39.05988  ? 221 VAL A CG2 1 
ATOM   1707 N N   . ASP A 1 222 ? 12.56185 14.00318 5.13154   1.000 36.63751  ? 222 ASP A N   1 
ATOM   1708 C CA  . ASP A 1 222 ? 12.80596 13.71877 6.54218   1.000 37.91534  ? 222 ASP A CA  1 
ATOM   1709 C C   . ASP A 1 222 ? 11.92652 12.53830 6.96348   1.000 41.06477  ? 222 ASP A C   1 
ATOM   1710 O O   . ASP A 1 222 ? 11.98811 11.48264 6.32576   1.000 39.13307  ? 222 ASP A O   1 
ATOM   1711 C CB  . ASP A 1 222 ? 12.59413 14.99456 7.37031   1.000 36.01121  ? 222 ASP A CB  1 
ATOM   1712 C CG  . ASP A 1 222 ? 13.60193 16.09616 6.99970   1.000 34.32318  ? 222 ASP A CG  1 
ATOM   1713 O OD1 . ASP A 1 222 ? 14.67437 15.75778 6.45878   1.000 33.89955  ? 222 ASP A OD1 1 
ATOM   1714 O OD2 . ASP A 1 222 ? 13.33581 17.29327 7.23467   1.000 34.77956  ? 222 ASP A OD2 1 
ATOM   1715 N N   . HIS A 1 223 ? 11.09438 12.67309 8.00003   1.000 41.00565  ? 223 HIS A N   1 
ATOM   1716 C CA  . HIS A 1 223 ? 10.28860 11.51355 8.39016   1.000 48.78362  ? 223 HIS A CA  1 
ATOM   1717 C C   . HIS A 1 223 ? 9.14373  11.25066 7.41125   1.000 54.26344  ? 223 HIS A C   1 
ATOM   1718 O O   . HIS A 1 223 ? 8.75562  10.09516 7.20792   1.000 57.22123  ? 223 HIS A O   1 
ATOM   1719 C CB  . HIS A 1 223 ? 9.73314  11.68740 9.80458   1.000 57.26371  ? 223 HIS A CB  1 
ATOM   1720 C CG  . HIS A 1 223 ? 8.89405  10.53395 10.26170  0.700 59.87995  ? 223 HIS A CG  1 
ATOM   1721 N ND1 . HIS A 1 223 ? 9.38396  9.24827  10.35060  0.700 59.69797  ? 223 HIS A ND1 1 
ATOM   1722 C CD2 . HIS A 1 223 ? 7.59453  10.46770 10.63777  0.700 59.97282  ? 223 HIS A CD2 1 
ATOM   1723 C CE1 . HIS A 1 223 ? 8.42532  8.44165  10.77058  0.700 60.97726  ? 223 HIS A CE1 1 
ATOM   1724 N NE2 . HIS A 1 223 ? 7.32932  9.15641  10.95215  0.700 60.93662  ? 223 HIS A NE2 1 
ATOM   1725 N N   . LEU A 1 224 ? 8.61342  12.29669 6.78614   1.000 46.98238  ? 224 LEU A N   1 
ATOM   1726 C CA  . LEU A 1 224 ? 7.37219  12.20040 6.02668   1.000 47.39262  ? 224 LEU A CA  1 
ATOM   1727 C C   . LEU A 1 224 ? 7.59065  11.47407 4.69808   1.000 46.86621  ? 224 LEU A C   1 
ATOM   1728 O O   . LEU A 1 224 ? 8.53216  11.78025 3.96260   1.000 44.18057  ? 224 LEU A O   1 
ATOM   1729 C CB  . LEU A 1 224 ? 6.83346  13.61330 5.79858   1.000 48.12378  ? 224 LEU A CB  1 
ATOM   1730 C CG  . LEU A 1 224 ? 5.77441  13.95598 4.75274   1.000 51.79462  ? 224 LEU A CG  1 
ATOM   1731 C CD1 . LEU A 1 224 ? 4.38541  13.60380 5.24553   1.000 54.71757  ? 224 LEU A CD1 1 
ATOM   1732 C CD2 . LEU A 1 224 ? 5.86727  15.43729 4.40539   1.000 51.86731  ? 224 LEU A CD2 1 
ATOM   1733 N N   . SER A 1 225 ? 6.72010  10.50960 4.38813   1.000 46.67144  ? 225 SER A N   1 
ATOM   1734 C CA  . SER A 1 225 ? 6.80856  9.73588  3.15049   1.000 46.96709  ? 225 SER A CA  1 
ATOM   1735 C C   . SER A 1 225 ? 5.44085  9.68029  2.48388   1.000 49.19737  ? 225 SER A C   1 
ATOM   1736 O O   . SER A 1 225 ? 4.46843  9.22408  3.09465   1.000 48.19722  ? 225 SER A O   1 
ATOM   1737 C CB  . SER A 1 225 ? 7.32841  8.31976  3.41495   1.000 46.87092  ? 225 SER A CB  1 
ATOM   1738 O OG  . SER A 1 225 ? 7.56147  7.63406  2.19171   1.000 46.52063  ? 225 SER A OG  1 
ATOM   1739 N N   . ILE A 1 226 ? 5.37423  10.11608 1.22405   1.000 47.68706  ? 226 ILE A N   1 
ATOM   1740 C CA  . ILE A 1 226 ? 4.11845  10.27376 0.49813   1.000 49.26196  ? 226 ILE A CA  1 
ATOM   1741 C C   . ILE A 1 226 ? 4.24412  9.62972  -0.87587  1.000 49.53088  ? 226 ILE A C   1 
ATOM   1742 O O   . ILE A 1 226 ? 5.26137  9.79505  -1.55817  1.000 46.21274  ? 226 ILE A O   1 
ATOM   1743 C CB  . ILE A 1 226 ? 3.74017  11.76290 0.34668   1.000 52.97077  ? 226 ILE A CB  1 
ATOM   1744 C CG1 . ILE A 1 226 ? 3.73332  12.46244 1.70640   1.000 56.43995  ? 226 ILE A CG1 1 
ATOM   1745 C CG2 . ILE A 1 226 ? 2.39037  11.91158 -0.35110  1.000 55.39537  ? 226 ILE A CG2 1 
ATOM   1746 C CD1 . ILE A 1 226 ? 3.95038  13.95589 1.61281   1.000 60.16457  ? 226 ILE A CD1 1 
ATOM   1747 N N   . LEU A 1 227 ? 3.20281  8.91135  -1.29094  1.000 50.66068  ? 227 LEU A N   1 
ATOM   1748 C CA  . LEU A 1 227 ? 3.13460  8.40639  -2.65614  1.000 50.95122  ? 227 LEU A CA  1 
ATOM   1749 C C   . LEU A 1 227 ? 2.68158  9.53056  -3.57762  1.000 51.98884  ? 227 LEU A C   1 
ATOM   1750 O O   . LEU A 1 227 ? 1.57678  10.06127 -3.42240  1.000 55.15074  ? 227 LEU A O   1 
ATOM   1751 C CB  . LEU A 1 227 ? 2.18308  7.21634  -2.75778  1.000 50.82146  ? 227 LEU A CB  1 
ATOM   1752 C CG  . LEU A 1 227 ? 1.93321  6.72037  -4.18746  1.000 53.35403  ? 227 LEU A CG  1 
ATOM   1753 C CD1 . LEU A 1 227 ? 3.23297  6.26634  -4.83573  1.000 51.37123  ? 227 LEU A CD1 1 
ATOM   1754 C CD2 . LEU A 1 227 ? 0.89871  5.60538  -4.21897  1.000 53.62609  ? 227 LEU A CD2 1 
ATOM   1755 N N   . HIS A 1 228 ? 3.53310  9.90220  -4.52631  1.000 50.69301  ? 228 HIS A N   1 
ATOM   1756 C CA  . HIS A 1 228 ? 3.19086  10.89768 -5.53151  1.000 51.36805  ? 228 HIS A CA  1 
ATOM   1757 C C   . HIS A 1 228 ? 2.85597  10.19759 -6.83937  1.000 51.47582  ? 228 HIS A C   1 
ATOM   1758 O O   . HIS A 1 228 ? 3.56293  9.27261  -7.25365  1.000 50.44498  ? 228 HIS A O   1 
ATOM   1759 C CB  . HIS A 1 228 ? 4.33572  11.89049 -5.73355  1.000 50.68152  ? 228 HIS A CB  1 
ATOM   1760 C CG  . HIS A 1 228 ? 4.53905  12.81269 -4.57337  1.000 50.71409  ? 228 HIS A CG  1 
ATOM   1761 N ND1 . HIS A 1 228 ? 4.14485  14.13319 -4.59502  1.000 51.40135  ? 228 HIS A ND1 1 
ATOM   1762 C CD2 . HIS A 1 228 ? 5.07788  12.60048 -3.34994  1.000 50.04801  ? 228 HIS A CD2 1 
ATOM   1763 C CE1 . HIS A 1 228 ? 4.44106  14.69745 -3.43758  1.000 51.80752  ? 228 HIS A CE1 1 
ATOM   1764 N NE2 . HIS A 1 228 ? 5.00735  13.78912 -2.66397  1.000 51.17359  ? 228 HIS A NE2 1 
ATOM   1765 N N   . ARG A 1 229 ? 1.77716  10.63490 -7.47989  1.000 52.44572  ? 229 ARG A N   1 
ATOM   1766 C CA  . ARG A 1 229 ? 1.30793  10.04082 -8.71994  1.000 53.76518  ? 229 ARG A CA  1 
ATOM   1767 C C   . ARG A 1 229 ? 1.41574  11.04062 -9.86230  1.000 54.54672  ? 229 ARG A C   1 
ATOM   1768 O O   . ARG A 1 229 ? 1.29232  12.25256 -9.66416  1.000 55.37780  ? 229 ARG A O   1 
ATOM   1769 C CB  . ARG A 1 229 ? -0.13602 9.54748  -8.58104  1.000 54.28285  ? 229 ARG A CB  1 
ATOM   1770 C CG  . ARG A 1 229 ? -0.21674 8.13946  -8.01910  1.000 55.46529  ? 229 ARG A CG  1 
ATOM   1771 C CD  . ARG A 1 229 ? -1.60717 7.76039  -7.54809  0.800 57.38113  ? 229 ARG A CD  1 
ATOM   1772 N NE  . ARG A 1 229 ? -1.61030 6.39714  -7.03195  0.700 58.62663  ? 229 ARG A NE  1 
ATOM   1773 C CZ  . ARG A 1 229 ? -2.44866 5.94178  -6.11216  0.600 60.36422  ? 229 ARG A CZ  1 
ATOM   1774 N NH1 . ARG A 1 229 ? -3.37436 6.71907  -5.57491  0.600 60.82968  ? 229 ARG A NH1 1 
ATOM   1775 N NH2 . ARG A 1 229 ? -2.34820 4.67713  -5.71325  0.600 61.97541  ? 229 ARG A NH2 1 
ATOM   1776 N N   . ASP A 1 230 ? 1.66549  10.50905 -11.06079 1.000 55.50084  ? 230 ASP A N   1 
ATOM   1777 C CA  . ASP A 1 230 ? 1.76767  11.30354 -12.28494 1.000 56.88936  ? 230 ASP A CA  1 
ATOM   1778 C C   . ASP A 1 230 ? 2.88121  12.34691 -12.17788 1.000 56.12610  ? 230 ASP A C   1 
ATOM   1779 O O   . ASP A 1 230 ? 2.70192  13.52394 -12.49952 1.000 57.52487  ? 230 ASP A O   1 
ATOM   1780 C CB  . ASP A 1 230 ? 0.42492  11.95406 -12.62605 1.000 59.09846  ? 230 ASP A CB  1 
ATOM   1781 C CG  . ASP A 1 230 ? 0.42139  12.59116 -13.99859 1.000 63.34538  ? 230 ASP A CG  1 
ATOM   1782 O OD1 . ASP A 1 230 ? 1.00469  11.99289 -14.92816 1.000 64.79107  ? 230 ASP A OD1 1 
ATOM   1783 O OD2 . ASP A 1 230 ? -0.16147 13.68755 -14.14406 1.000 66.47604  ? 230 ASP A OD2 1 
ATOM   1784 N N   . VAL A 1 231 ? 4.04739  11.89894 -11.72512 1.000 54.31198  ? 231 VAL A N   1 
ATOM   1785 C CA  . VAL A 1 231 ? 5.19755  12.78112 -11.56630 1.000 52.53327  ? 231 VAL A CA  1 
ATOM   1786 C C   . VAL A 1 231 ? 5.87481  12.97098 -12.91544 1.000 53.20108  ? 231 VAL A C   1 
ATOM   1787 O O   . VAL A 1 231 ? 6.14870  12.00044 -13.63198 1.000 53.77722  ? 231 VAL A O   1 
ATOM   1788 C CB  . VAL A 1 231 ? 6.17889  12.21483 -10.52897 1.000 51.23358  ? 231 VAL A CB  1 
ATOM   1789 C CG1 . VAL A 1 231 ? 7.52231  12.91821 -10.63080 1.000 48.42919  ? 231 VAL A CG1 1 
ATOM   1790 C CG2 . VAL A 1 231 ? 5.60745  12.36608 -9.12974  1.000 52.01979  ? 231 VAL A CG2 1 
ATOM   1791 N N   . GLN A 1 232 ? 6.13497  14.22759 -13.27185 1.000 52.86528  ? 232 GLN A N   1 
ATOM   1792 C CA  . GLN A 1 232 ? 6.92012  14.53885 -14.45648 1.000 51.49763  ? 232 GLN A CA  1 
ATOM   1793 C C   . GLN A 1 232 ? 8.36835  14.87608 -14.13759 1.000 49.92956  ? 232 GLN A C   1 
ATOM   1794 O O   . GLN A 1 232 ? 9.22324  14.75650 -15.02396 1.000 45.75107  ? 232 GLN A O   1 
ATOM   1795 C CB  . GLN A 1 232 ? 6.29215  15.70997 -15.22142 1.000 54.67638  ? 232 GLN A CB  1 
ATOM   1796 N N   . GLU A 1 233 ? 8.66572  15.27419 -12.90040 1.000 47.12136  ? 233 GLU A N   1 
ATOM   1797 C CA  . GLU A 1 233 ? 10.00687 15.72763 -12.56128 1.000 45.24103  ? 233 GLU A CA  1 
ATOM   1798 C C   . GLU A 1 233 ? 10.12283 15.90194 -11.05460 1.000 44.50079  ? 233 GLU A C   1 
ATOM   1799 O O   . GLU A 1 233 ? 9.16100  16.31103 -10.39952 1.000 43.27636  ? 233 GLU A O   1 
ATOM   1800 C CB  . GLU A 1 233 ? 10.32447 17.05223 -13.26687 1.000 46.53286  ? 233 GLU A CB  1 
ATOM   1801 C CG  . GLU A 1 233 ? 11.74090 17.54289 -13.06805 1.000 49.91611  ? 233 GLU A CG  1 
ATOM   1802 C CD  . GLU A 1 233 ? 11.98714 18.87891 -13.73323 1.000 50.27741  ? 233 GLU A CD  1 
ATOM   1803 O OE1 . GLU A 1 233 ? 11.01010 19.62542 -13.94320 1.000 52.08912  ? 233 GLU A OE1 1 
ATOM   1804 O OE2 . GLU A 1 233 ? 13.15791 19.18673 -14.04515 1.000 51.90363  ? 233 GLU A OE2 1 
ATOM   1805 N N   . ILE A 1 234 ? 11.30358 15.59282 -10.51991 1.000 40.96704  ? 234 ILE A N   1 
ATOM   1806 C CA  . ILE A 1 234 ? 11.67143 15.89378 -9.14031  1.000 40.28913  ? 234 ILE A CA  1 
ATOM   1807 C C   . ILE A 1 234 ? 12.95114 16.71690 -9.19117  1.000 39.94197  ? 234 ILE A C   1 
ATOM   1808 O O   . ILE A 1 234 ? 13.95303 16.27468 -9.76744  1.000 39.87210  ? 234 ILE A O   1 
ATOM   1809 C CB  . ILE A 1 234 ? 11.87091 14.61824 -8.30399  1.000 39.92003  ? 234 ILE A CB  1 
ATOM   1810 C CG1 . ILE A 1 234 ? 10.62485 13.73266 -8.36601  1.000 41.89461  ? 234 ILE A CG1 1 
ATOM   1811 C CG2 . ILE A 1 234 ? 12.21858 14.96932 -6.86271  1.000 39.65255  ? 234 ILE A CG2 1 
ATOM   1812 C CD1 . ILE A 1 234 ? 10.83329 12.34106 -7.81226  1.000 41.58481  ? 234 ILE A CD1 1 
ATOM   1813 N N   . ARG A 1 235 ? 12.92100 17.91021 -8.60116  1.000 37.00428  ? 235 ARG A N   1 
ATOM   1814 C CA  . ARG A 1 235 ? 14.03222 18.85024 -8.68500  1.000 36.24190  ? 235 ARG A CA  1 
ATOM   1815 C C   . ARG A 1 235 ? 14.62908 19.09437 -7.30771  1.000 36.24153  ? 235 ARG A C   1 
ATOM   1816 O O   . ARG A 1 235 ? 13.90730 19.43881 -6.36562  1.000 35.07753  ? 235 ARG A O   1 
ATOM   1817 C CB  . ARG A 1 235 ? 13.59157 20.18160 -9.29366  1.000 36.55583  ? 235 ARG A CB  1 
ATOM   1818 C CG  . ARG A 1 235 ? 13.20877 20.09627 -10.74689 0.900 43.15237  ? 235 ARG A CG  1 
ATOM   1819 C CD  . ARG A 1 235 ? 13.33171 21.45294 -11.41526 0.800 45.40827  ? 235 ARG A CD  1 
ATOM   1820 N NE  . ARG A 1 235 ? 13.47400 21.30934 -12.85779 0.700 49.39813  ? 235 ARG A NE  1 
ATOM   1821 C CZ  . ARG A 1 235 ? 14.17978 22.12604 -13.62568 0.700 50.43537  ? 235 ARG A CZ  1 
ATOM   1822 N NH1 . ARG A 1 235 ? 14.83231 23.15850 -13.11730 0.700 50.99734  ? 235 ARG A NH1 1 
ATOM   1823 N NH2 . ARG A 1 235 ? 14.23746 21.89683 -14.93529 0.700 52.49632  ? 235 ARG A NH2 1 
ATOM   1824 N N   . TYR A 1 236 ? 15.94951 18.95303 -7.21072  1.000 32.52085  ? 236 TYR A N   1 
ATOM   1825 C CA  . TYR A 1 236 ? 16.69702 19.17713 -5.98029  1.000 34.45860  ? 236 TYR A CA  1 
ATOM   1826 C C   . TYR A 1 236 ? 17.64392 20.35636 -6.15054  1.000 34.66654  ? 236 TYR A C   1 
ATOM   1827 O O   . TYR A 1 236 ? 18.31704 20.47761 -7.17949  1.000 34.21794  ? 236 TYR A O   1 
ATOM   1828 C CB  . TYR A 1 236 ? 17.50796 17.93693 -5.59286  1.000 32.78290  ? 236 TYR A CB  1 
ATOM   1829 C CG  . TYR A 1 236 ? 16.66291 16.76709 -5.16358  1.000 34.83818  ? 236 TYR A CG  1 
ATOM   1830 C CD1 . TYR A 1 236 ? 15.85775 16.85501 -4.03676  1.000 34.54264  ? 236 TYR A CD1 1 
ATOM   1831 C CD2 . TYR A 1 236 ? 16.67223 15.57429 -5.87308  1.000 35.37259  ? 236 TYR A CD2 1 
ATOM   1832 C CE1 . TYR A 1 236 ? 15.08138 15.79068 -3.63153  1.000 35.07524  ? 236 TYR A CE1 1 
ATOM   1833 C CE2 . TYR A 1 236 ? 15.89980 14.49916 -5.46766  1.000 37.51300  ? 236 TYR A CE2 1 
ATOM   1834 C CZ  . TYR A 1 236 ? 15.10837 14.61652 -4.34795  1.000 38.27089  ? 236 TYR A CZ  1 
ATOM   1835 O OH  . TYR A 1 236 ? 14.33007 13.56061 -3.93466  1.000 48.68175  ? 236 TYR A OH  1 
ATOM   1836 N N   . GLU A 1 237 ? 17.70392 21.21173 -5.13121  1.000 34.33127  ? 237 GLU A N   1 
ATOM   1837 C CA  . GLU A 1 237 ? 18.67934 22.29256 -5.08014  1.000 33.17455  ? 237 GLU A CA  1 
ATOM   1838 C C   . GLU A 1 237 ? 18.81903 22.74666 -3.63222  1.000 34.03481  ? 237 GLU A C   1 
ATOM   1839 O O   . GLU A 1 237 ? 17.89349 22.59124 -2.82969  1.000 33.01087  ? 237 GLU A O   1 
ATOM   1840 C CB  . GLU A 1 237 ? 18.27283 23.46757 -5.97670  1.000 35.91091  ? 237 GLU A CB  1 
ATOM   1841 C CG  . GLU A 1 237 ? 16.89785 24.02103 -5.67964  1.000 37.18120  ? 237 GLU A CG  1 
ATOM   1842 C CD  . GLU A 1 237 ? 16.30934 24.78539 -6.85419  1.000 50.01496  ? 237 GLU A CD  1 
ATOM   1843 O OE1 . GLU A 1 237 ? 16.99268 25.68227 -7.39436  1.000 43.08737  ? 237 GLU A OE1 1 
ATOM   1844 O OE2 . GLU A 1 237 ? 15.16385 24.47510 -7.24560  1.000 43.79882  ? 237 GLU A OE2 1 
ATOM   1845 N N   . VAL A 1 238 ? 19.98980 23.29763 -3.30114  1.000 31.38164  ? 238 VAL A N   1 
ATOM   1846 C CA  . VAL A 1 238 ? 20.17250 23.86681 -1.97035  1.000 33.14397  ? 238 VAL A CA  1 
ATOM   1847 C C   . VAL A 1 238 ? 19.21492 25.03374 -1.79931  1.000 35.13397  ? 238 VAL A C   1 
ATOM   1848 O O   . VAL A 1 238 ? 19.14230 25.93194 -2.64829  1.000 33.85899  ? 238 VAL A O   1 
ATOM   1849 C CB  . VAL A 1 238 ? 21.62756 24.30478 -1.75223  1.000 32.92492  ? 238 VAL A CB  1 
ATOM   1850 C CG1 . VAL A 1 238 ? 21.79042 24.94524 -0.36477  1.000 32.96614  ? 238 VAL A CG1 1 
ATOM   1851 C CG2 . VAL A 1 238 ? 22.55935 23.13161 -1.91642  1.000 31.62145  ? 238 VAL A CG2 1 
ATOM   1852 N N   . SER A 1 239 ? 18.46261 25.01955 -0.70317  1.000 31.83834  ? 239 SER A N   1 
ATOM   1853 C CA  . SER A 1 239 ? 17.50013 26.07929 -0.44453  1.000 35.71269  ? 239 SER A CA  1 
ATOM   1854 C C   . SER A 1 239 ? 18.21231 27.39765 -0.16349  1.000 36.99399  ? 239 SER A C   1 
ATOM   1855 O O   . SER A 1 239 ? 19.37212 27.42860 0.26148   1.000 35.83828  ? 239 SER A O   1 
ATOM   1856 C CB  . SER A 1 239 ? 16.60231 25.70617 0.74041   1.000 36.43486  ? 239 SER A CB  1 
ATOM   1857 O OG  . SER A 1 239 ? 15.64205 26.71987 1.00974   1.000 38.59212  ? 239 SER A OG  1 
ATOM   1858 N N   . ALA A 1 240 ? 17.50637 28.49957 -0.42654  1.000 38.56855  ? 240 ALA A N   1 
ATOM   1859 C CA  . ALA A 1 240 ? 17.95096 29.80267 0.05014   1.000 38.61266  ? 240 ALA A CA  1 
ATOM   1860 C C   . ALA A 1 240 ? 17.63876 30.00224 1.52522   1.000 40.64936  ? 240 ALA A C   1 
ATOM   1861 O O   . ALA A 1 240 ? 18.22156 30.89033 2.15716   1.000 41.75211  ? 240 ALA A O   1 
ATOM   1862 C CB  . ALA A 1 240 ? 17.30229 30.92239 -0.76422  1.000 40.11354  ? 240 ALA A CB  1 
ATOM   1863 N N   . LYS A 1 241 ? 16.73359 29.20094 2.07681   1.000 39.69649  ? 241 LYS A N   1 
ATOM   1864 C CA  . LYS A 1 241 ? 16.36318 29.28088 3.47961   1.000 42.29146  ? 241 LYS A CA  1 
ATOM   1865 C C   . LYS A 1 241 ? 17.31991 28.44516 4.31581   1.000 41.63393  ? 241 LYS A C   1 
ATOM   1866 O O   . LYS A 1 241 ? 17.83904 27.42121 3.86335   1.000 38.22940  ? 241 LYS A O   1 
ATOM   1867 C CB  . LYS A 1 241 ? 14.93116 28.79183 3.69324   1.000 43.65161  ? 241 LYS A CB  1 
ATOM   1868 C CG  . LYS A 1 241 ? 13.89070 29.45610 2.80306   1.000 45.80627  ? 241 LYS A CG  1 
ATOM   1869 C CD  . LYS A 1 241 ? 12.62352 28.61249 2.75813   1.000 50.16634  ? 241 LYS A CD  1 
ATOM   1870 C CE  . LYS A 1 241 ? 11.50365 29.29823 1.99393   1.000 54.26246  ? 241 LYS A CE  1 
ATOM   1871 N NZ  . LYS A 1 241 ? 10.27895 28.45146 1.98254   1.000 59.34499  ? 241 LYS A NZ  1 
ATOM   1872 N N   . LYS A 1 242 ? 17.54504 28.89185 5.54811   1.000 41.01093  ? 242 LYS A N   1 
ATOM   1873 C CA  . LYS A 1 242 ? 18.43401 28.21201 6.47501   1.000 41.07404  ? 242 LYS A CA  1 
ATOM   1874 C C   . LYS A 1 242 ? 17.73460 28.04911 7.81508   1.000 41.75531  ? 242 LYS A C   1 
ATOM   1875 O O   . LYS A 1 242 ? 16.88305 28.86053 8.19136   1.000 41.81750  ? 242 LYS A O   1 
ATOM   1876 C CB  . LYS A 1 242 ? 19.75038 28.98690 6.66536   1.000 44.87548  ? 242 LYS A CB  1 
ATOM   1877 C CG  . LYS A 1 242 ? 20.36094 29.51145 5.36867   1.000 48.98239  ? 242 LYS A CG  1 
ATOM   1878 C CD  . LYS A 1 242 ? 21.82355 29.89120 5.54013   1.000 53.13113  ? 242 LYS A CD  1 
ATOM   1879 C CE  . LYS A 1 242 ? 22.70102 28.64929 5.67705   1.000 56.65277  ? 242 LYS A CE  1 
ATOM   1880 N NZ  . LYS A 1 242 ? 24.15460 28.96413 5.54831   1.000 58.46804  ? 242 LYS A NZ  1 
ATOM   1881 N N   . ILE A 1 243 ? 18.09191 26.99064 8.53114   1.000 39.63500  ? 243 ILE A N   1 
ATOM   1882 C CA  . ILE A 1 243 ? 17.62296 26.81170 9.89972   1.000 40.03651  ? 243 ILE A CA  1 
ATOM   1883 C C   . ILE A 1 243 ? 18.64266 27.44054 10.83640  1.000 42.03437  ? 243 ILE A C   1 
ATOM   1884 O O   . ILE A 1 243 ? 19.85462 27.34962 10.61134  1.000 41.89048  ? 243 ILE A O   1 
ATOM   1885 C CB  . ILE A 1 243 ? 17.39500 25.32429 10.22935  1.000 36.78675  ? 243 ILE A CB  1 
ATOM   1886 C CG1 . ILE A 1 243 ? 16.89953 25.17591 11.67700  1.000 39.94634  ? 243 ILE A CG1 1 
ATOM   1887 C CG2 . ILE A 1 243 ? 18.66357 24.52320 9.99667   1.000 36.43266  ? 243 ILE A CG2 1 
ATOM   1888 C CD1 . ILE A 1 243 ? 16.63589 23.74906 12.10502  1.000 36.31080  ? 243 ILE A CD1 1 
ATOM   1889 N N   . HIS A 1 244 ? 18.15265 28.09725 11.88099  1.000 41.39243  ? 244 HIS A N   1 
ATOM   1890 C CA  . HIS A 1 244 ? 18.99463 28.80748 12.83225  1.000 43.44254  ? 244 HIS A CA  1 
ATOM   1891 C C   . HIS A 1 244 ? 18.92198 28.12582 14.18965  1.000 42.12407  ? 244 HIS A C   1 
ATOM   1892 O O   . HIS A 1 244 ? 17.82780 27.82109 14.67725  1.000 41.73436  ? 244 HIS A O   1 
ATOM   1893 C CB  . HIS A 1 244 ? 18.56368 30.26928 12.95788  1.000 45.39922  ? 244 HIS A CB  1 
ATOM   1894 C CG  . HIS A 1 244 ? 18.49495 30.99147 11.64896  1.000 48.16768  ? 244 HIS A CG  1 
ATOM   1895 N ND1 . HIS A 1 244 ? 19.61973 31.39336 10.96106  1.000 46.69300  ? 244 HIS A ND1 1 
ATOM   1896 C CD2 . HIS A 1 244 ? 17.43597 31.38392 10.90199  1.000 49.12677  ? 244 HIS A CD2 1 
ATOM   1897 C CE1 . HIS A 1 244 ? 19.25625 32.00701 9.84913   1.000 49.41395  ? 244 HIS A CE1 1 
ATOM   1898 N NE2 . HIS A 1 244 ? 17.93665 32.01361 9.78868   1.000 51.20201  ? 244 HIS A NE2 1 
ATOM   1899 N N   . PHE A 1 245 ? 20.08369 27.89895 14.79498  1.000 42.83105  ? 245 PHE A N   1 
ATOM   1900 C CA  . PHE A 1 245 ? 20.18902 27.34216 16.13662  1.000 43.75990  ? 245 PHE A CA  1 
ATOM   1901 C C   . PHE A 1 245 ? 20.67620 28.41140 17.10605  1.000 46.05310  ? 245 PHE A C   1 
ATOM   1902 O O   . PHE A 1 245 ? 21.57050 29.19617 16.77964  1.000 48.15918  ? 245 PHE A O   1 
ATOM   1903 C CB  . PHE A 1 245 ? 21.16280 26.16038 16.17740  1.000 42.29288  ? 245 PHE A CB  1 
ATOM   1904 C CG  . PHE A 1 245 ? 20.76779 25.00226 15.31131  1.000 42.82233  ? 245 PHE A CG  1 
ATOM   1905 C CD1 . PHE A 1 245 ? 21.07390 24.98996 13.95788  1.000 39.91519  ? 245 PHE A CD1 1 
ATOM   1906 C CD2 . PHE A 1 245 ? 20.11834 23.90866 15.85566  1.000 40.81528  ? 245 PHE A CD2 1 
ATOM   1907 C CE1 . PHE A 1 245 ? 20.72302 23.91404 13.16067  1.000 41.03788  ? 245 PHE A CE1 1 
ATOM   1908 C CE2 . PHE A 1 245 ? 19.76603 22.82841 15.06457  1.000 41.11964  ? 245 PHE A CE2 1 
ATOM   1909 C CZ  . PHE A 1 245 ? 20.06774 22.83087 13.71520  1.000 38.97288  ? 245 PHE A CZ  1 
ATOM   1910 N N   . ALA A 1 246 ? 20.09633 28.44091 18.30065  1.000 49.11688  ? 246 ALA A N   1 
ATOM   1911 C CA  . ALA A 1 246 ? 20.69101 29.20356 19.38769  1.000 52.45751  ? 246 ALA A CA  1 
ATOM   1912 C C   . ALA A 1 246 ? 21.89592 28.43129 19.90931  1.000 53.77601  ? 246 ALA A C   1 
ATOM   1913 O O   . ALA A 1 246 ? 21.77658 27.25222 20.26056  1.000 53.34778  ? 246 ALA A O   1 
ATOM   1914 C CB  . ALA A 1 246 ? 19.67274 29.44549 20.49925  1.000 59.12254  ? 246 ALA A CB  1 
ATOM   1915 N N   . ARG A 1 247 ? 23.06196 29.06947 19.92456  1.000 56.74870  ? 247 ARG A N   1 
ATOM   1916 C CA  . ARG A 1 247 ? 24.26954 28.45269 20.45801  1.000 61.64344  ? 247 ARG A CA  1 
ATOM   1917 C C   . ARG A 1 247 ? 24.62970 29.13615 21.76939  1.000 66.26595  ? 247 ARG A C   1 
ATOM   1918 O O   . ARG A 1 247 ? 24.61243 30.36882 21.86193  1.000 68.40762  ? 247 ARG A O   1 
ATOM   1919 C CB  . ARG A 1 247 ? 25.43598 28.51930 19.46037  1.000 62.95780  ? 247 ARG A CB  1 
ATOM   1920 C CG  . ARG A 1 247 ? 26.13965 29.86707 19.34584  1.000 68.34445  ? 247 ARG A CG  1 
ATOM   1921 C CD  . ARG A 1 247 ? 27.44450 29.78150 18.55275  1.000 71.47543  ? 247 ARG A CD  1 
ATOM   1922 N NE  . ARG A 1 247 ? 28.39790 28.83502 19.12234  1.000 72.35923  ? 247 ARG A NE  1 
ATOM   1923 C CZ  . ARG A 1 247 ? 29.19232 29.09384 20.15290  1.000 74.68979  ? 247 ARG A CZ  1 
ATOM   1924 N NH1 . ARG A 1 247 ? 29.14883 30.25556 20.78648  1.000 73.73392  ? 247 ARG A NH1 1 
ATOM   1925 N NH2 . ARG A 1 247 ? 30.05127 28.16278 20.55927  1.000 68.59402  ? 247 ARG A NH2 1 
ATOM   1926 N N   . PHE A 1 248 ? 24.91754 28.33161 22.79033  1.000 65.90040  ? 248 PHE A N   1 
ATOM   1927 C CA  . PHE A 1 248 ? 25.30890 28.84813 24.09090  1.000 68.96097  ? 248 PHE A CA  1 
ATOM   1928 C C   . PHE A 1 248 ? 26.69668 28.41616 24.52857  1.000 70.65633  ? 248 PHE A C   1 
ATOM   1929 O O   . PHE A 1 248 ? 27.27526 29.06746 25.40483  1.000 72.48105  ? 248 PHE A O   1 
ATOM   1930 C CB  . PHE A 1 248 ? 24.28985 28.43270 25.16190  1.000 74.66756  ? 248 PHE A CB  1 
ATOM   1931 C CG  . PHE A 1 248 ? 22.99454 29.18234 25.07204  1.000 82.11922  ? 248 PHE A CG  1 
ATOM   1932 C CD1 . PHE A 1 248 ? 22.89105 30.46541 25.58364  1.000 77.84854  ? 248 PHE A CD1 1 
ATOM   1933 C CD2 . PHE A 1 248 ? 21.88712 28.61712 24.46052  1.000 79.57903  ? 248 PHE A CD2 1 
ATOM   1934 C CE1 . PHE A 1 248 ? 21.70601 31.16859 25.49800  1.000 78.33494  ? 248 PHE A CE1 1 
ATOM   1935 C CE2 . PHE A 1 248 ? 20.69649 29.31699 24.37329  1.000 78.33071  ? 248 PHE A CE2 1 
ATOM   1936 C CZ  . PHE A 1 248 ? 20.60849 30.59436 24.89464  1.000 78.77808  ? 248 PHE A CZ  1 
ATOM   1937 N N   . ARG A 1 249 ? 27.24491 27.35181 23.94952  1.000 64.37663  ? 249 ARG A N   1 
ATOM   1938 C CA  . ARG A 1 249 ? 28.62638 26.97100 24.18849  1.000 61.89033  ? 249 ARG A CA  1 
ATOM   1939 C C   . ARG A 1 249 ? 29.15664 26.27859 22.94231  1.000 60.00332  ? 249 ARG A C   1 
ATOM   1940 O O   . ARG A 1 249 ? 28.41451 25.99124 21.99884  1.000 57.31351  ? 249 ARG A O   1 
ATOM   1941 C CB  . ARG A 1 249 ? 28.76473 26.07362 25.42545  1.000 61.16151  ? 249 ARG A CB  1 
ATOM   1942 C CG  . ARG A 1 249 ? 27.63770 25.07079 25.60994  0.800 62.83379  ? 249 ARG A CG  1 
ATOM   1943 C CD  . ARG A 1 249 ? 28.08886 23.89973 26.47219  0.700 62.40217  ? 249 ARG A CD  1 
ATOM   1944 N NE  . ARG A 1 249 ? 26.97646 23.07766 26.93611  0.600 63.60787  ? 249 ARG A NE  1 
ATOM   1945 C CZ  . ARG A 1 249 ? 26.30754 22.21408 26.18281  0.600 63.14664  ? 249 ARG A CZ  1 
ATOM   1946 N NH1 . ARG A 1 249 ? 26.57254 22.06649 24.89371  0.600 62.93898  ? 249 ARG A NH1 1 
ATOM   1947 N NH2 . ARG A 1 249 ? 25.34552 21.48114 26.73611  0.600 63.49366  ? 249 ARG A NH2 1 
ATOM   1948 N N   . SER A 1 250 ? 30.45901 26.01951 22.94282  1.000 57.94871  ? 250 SER A N   1 
ATOM   1949 C CA  . SER A 1 250 ? 31.08402 25.33177 21.82230  1.000 54.42978  ? 250 SER A CA  1 
ATOM   1950 C C   . SER A 1 250 ? 30.75996 23.84686 21.89403  1.000 52.11778  ? 250 SER A C   1 
ATOM   1951 O O   . SER A 1 250 ? 31.05348 23.18373 22.89511  1.000 50.69180  ? 250 SER A O   1 
ATOM   1952 C CB  . SER A 1 250 ? 32.59416 25.55142 21.82515  1.000 54.63598  ? 250 SER A CB  1 
ATOM   1953 O OG  . SER A 1 250 ? 33.20820 24.83595 20.76492  1.000 54.31869  ? 250 SER A OG  1 
ATOM   1954 N N   . PHE A 1 251 ? 30.12940 23.33630 20.84446  1.000 49.00142  ? 251 PHE A N   1 
ATOM   1955 C CA  . PHE A 1 251 ? 29.97477 21.89903 20.63389  1.000 47.87542  ? 251 PHE A CA  1 
ATOM   1956 C C   . PHE A 1 251 ? 30.25342 21.66808 19.15752  1.000 45.75712  ? 251 PHE A C   1 
ATOM   1957 O O   . PHE A 1 251 ? 29.33261 21.61133 18.33285  1.000 45.25415  ? 251 PHE A O   1 
ATOM   1958 C CB  . PHE A 1 251 ? 28.57951 21.41832 21.04133  1.000 49.87586  ? 251 PHE A CB  1 
ATOM   1959 C CG  . PHE A 1 251 ? 28.47429 19.92734 21.22111  1.000 51.91936  ? 251 PHE A CG  1 
ATOM   1960 C CD1 . PHE A 1 251 ? 29.59329 19.11626 21.11624  1.000 49.68703  ? 251 PHE A CD1 1 
ATOM   1961 C CD2 . PHE A 1 251 ? 27.25098 19.33649 21.48954  1.000 54.57098  ? 251 PHE A CD2 1 
ATOM   1962 C CE1 . PHE A 1 251 ? 29.49410 17.74396 21.28173  1.000 49.36134  ? 251 PHE A CE1 1 
ATOM   1963 C CE2 . PHE A 1 251 ? 27.14505 17.96521 21.65450  1.000 55.01192  ? 251 PHE A CE2 1 
ATOM   1964 C CZ  . PHE A 1 251 ? 28.26877 17.16922 21.55201  1.000 52.12512  ? 251 PHE A CZ  1 
ATOM   1965 N N   . PRO A 1 252 ? 31.52915 21.56921 18.78131  1.000 44.67858  ? 252 PRO A N   1 
ATOM   1966 C CA  . PRO A 1 252 ? 31.88097 21.49834 17.35715  1.000 43.84905  ? 252 PRO A CA  1 
ATOM   1967 C C   . PRO A 1 252 ? 31.27318 20.28520 16.67204  1.000 40.24823  ? 252 PRO A C   1 
ATOM   1968 O O   . PRO A 1 252 ? 31.11647 19.21808 17.26699  1.000 36.42114  ? 252 PRO A O   1 
ATOM   1969 C CB  . PRO A 1 252 ? 33.41179 21.41474 17.37368  1.000 42.99005  ? 252 PRO A CB  1 
ATOM   1970 C CG  . PRO A 1 252 ? 33.80872 22.01909 18.67634  1.000 45.37295  ? 252 PRO A CG  1 
ATOM   1971 C CD  . PRO A 1 252 ? 32.72060 21.64741 19.64364  1.000 45.69535  ? 252 PRO A CD  1 
ATOM   1972 N N   . PHE A 1 253 ? 30.94247 20.46652 15.39123  1.000 42.01790  ? 253 PHE A N   1 
ATOM   1973 C CA  . PHE A 1 253 ? 30.32263 19.40417 14.60576  1.000 37.38388  ? 253 PHE A CA  1 
ATOM   1974 C C   . PHE A 1 253 ? 31.15176 18.12361 14.63297  1.000 32.40311  ? 253 PHE A C   1 
ATOM   1975 O O   . PHE A 1 253 ? 30.61607 17.02803 14.82825  1.000 31.19059  ? 253 PHE A O   1 
ATOM   1976 C CB  . PHE A 1 253 ? 30.12236 19.88808 13.16911  1.000 38.94817  ? 253 PHE A CB  1 
ATOM   1977 C CG  . PHE A 1 253 ? 29.57999 18.84339 12.24567  1.000 34.77852  ? 253 PHE A CG  1 
ATOM   1978 C CD1 . PHE A 1 253 ? 28.22968 18.53647 12.24448  1.000 36.53676  ? 253 PHE A CD1 1 
ATOM   1979 C CD2 . PHE A 1 253 ? 30.41543 18.18516 11.35893  1.000 36.29894  ? 253 PHE A CD2 1 
ATOM   1980 C CE1 . PHE A 1 253 ? 27.72376 17.57974 11.38330  1.000 37.41232  ? 253 PHE A CE1 1 
ATOM   1981 C CE2 . PHE A 1 253 ? 29.91800 17.23071 10.48949  1.000 33.68639  ? 253 PHE A CE2 1 
ATOM   1982 C CZ  . PHE A 1 253 ? 28.57009 16.92639 10.50247  1.000 33.80104  ? 253 PHE A CZ  1 
ATOM   1983 N N   . TRP A 1 254 ? 32.46927 18.24317 14.44983  1.000 34.54803  ? 254 TRP A N   1 
ATOM   1984 C CA  . TRP A 1 254 ? 33.31052 17.04954 14.40725  1.000 34.56590  ? 254 TRP A CA  1 
ATOM   1985 C C   . TRP A 1 254 ? 33.42247 16.38610 15.77426  1.000 33.99233  ? 254 TRP A C   1 
ATOM   1986 O O   . TRP A 1 254 ? 33.62861 15.16822 15.85393  1.000 30.77313  ? 254 TRP A O   1 
ATOM   1987 C CB  . TRP A 1 254 ? 34.70392 17.38798 13.87318  1.000 34.32814  ? 254 TRP A CB  1 
ATOM   1988 C CG  . TRP A 1 254 ? 34.72159 17.88592 12.45685  1.000 33.27364  ? 254 TRP A CG  1 
ATOM   1989 C CD1 . TRP A 1 254 ? 35.19077 19.08862 12.02153  1.000 34.47963  ? 254 TRP A CD1 1 
ATOM   1990 C CD2 . TRP A 1 254 ? 34.24227 17.19641 11.29271  1.000 32.54334  ? 254 TRP A CD2 1 
ATOM   1991 N NE1 . TRP A 1 254 ? 35.03929 19.19049 10.65512  1.000 32.30219  ? 254 TRP A NE1 1 
ATOM   1992 C CE2 . TRP A 1 254 ? 34.45908 18.04234 10.18725  1.000 33.63863  ? 254 TRP A CE2 1 
ATOM   1993 C CE3 . TRP A 1 254 ? 33.65665 15.94494 11.07758  1.000 33.13359  ? 254 TRP A CE3 1 
ATOM   1994 C CZ2 . TRP A 1 254 ? 34.11257 17.67753 8.88720   1.000 31.80754  ? 254 TRP A CZ2 1 
ATOM   1995 C CZ3 . TRP A 1 254 ? 33.31366 15.58468 9.78548   1.000 31.31500  ? 254 TRP A CZ3 1 
ATOM   1996 C CH2 . TRP A 1 254 ? 33.54197 16.44869 8.70954   1.000 31.79720  ? 254 TRP A CH2 1 
ATOM   1997 N N   . ARG A 1 255 ? 33.30843 17.15955 16.85715  1.000 34.79450  ? 255 ARG A N   1 
ATOM   1998 C CA  . ARG A 1 255 ? 33.20146 16.54178 18.17447  1.000 36.50548  ? 255 ARG A CA  1 
ATOM   1999 C C   . ARG A 1 255 ? 31.86076 15.83600 18.32577  1.000 35.84592  ? 255 ARG A C   1 
ATOM   2000 O O   . ARG A 1 255 ? 31.79017 14.73023 18.87308  1.000 37.84147  ? 255 ARG A O   1 
ATOM   2001 C CB  . ARG A 1 255 ? 33.40297 17.59541 19.27199  1.000 37.74519  ? 255 ARG A CB  1 
ATOM   2002 C CG  . ARG A 1 255 ? 33.02166 17.13489 20.66847  1.000 43.05473  ? 255 ARG A CG  1 
ATOM   2003 C CD  . ARG A 1 255 ? 33.81580 17.89113 21.73310  0.800 43.46578  ? 255 ARG A CD  1 
ATOM   2004 N NE  . ARG A 1 255 ? 35.15444 17.33137 21.87718  0.700 45.68940  ? 255 ARG A NE  1 
ATOM   2005 C CZ  . ARG A 1 255 ? 36.20966 17.99770 22.32456  0.600 49.12779  ? 255 ARG A CZ  1 
ATOM   2006 N NH1 . ARG A 1 255 ? 36.13472 19.27908 22.64465  0.600 50.48320  ? 255 ARG A NH1 1 
ATOM   2007 N NH2 . ARG A 1 255 ? 37.37138 17.36262 22.45055  0.600 48.63380  ? 255 ARG A NH2 1 
ATOM   2008 N N   . ARG A 1 256 ? 30.79234 16.45271 17.81670  1.000 33.69936  ? 256 ARG A N   1 
ATOM   2009 C CA  . ARG A 1 256 ? 29.48375 15.80947 17.79448  1.000 36.57703  ? 256 ARG A CA  1 
ATOM   2010 C C   . ARG A 1 256 ? 29.52008 14.50649 16.99956  1.000 37.48486  ? 256 ARG A C   1 
ATOM   2011 O O   . ARG A 1 256 ? 28.93723 13.49761 17.41803  1.000 35.33044  ? 256 ARG A O   1 
ATOM   2012 C CB  . ARG A 1 256 ? 28.45754 16.77935 17.20729  1.000 41.79610  ? 256 ARG A CB  1 
ATOM   2013 C CG  . ARG A 1 256 ? 27.02841 16.49536 17.59277  1.000 50.50491  ? 256 ARG A CG  1 
ATOM   2014 C CD  . ARG A 1 256 ? 26.24336 17.79189 17.75869  1.000 51.26475  ? 256 ARG A CD  1 
ATOM   2015 N NE  . ARG A 1 256 ? 25.95235 18.43702 16.48393  1.000 43.41498  ? 256 ARG A NE  1 
ATOM   2016 C CZ  . ARG A 1 256 ? 26.55988 19.52719 16.03495  1.000 46.70561  ? 256 ARG A CZ  1 
ATOM   2017 N NH1 . ARG A 1 256 ? 27.52901 20.11181 16.72021  1.000 51.16804  ? 256 ARG A NH1 1 
ATOM   2018 N NH2 . ARG A 1 256 ? 26.18131 20.04705 14.87083  1.000 46.92971  ? 256 ARG A NH2 1 
ATOM   2019 N N   . VAL A 1 257 ? 30.20168 14.51020 15.84750  1.000 32.39626  ? 257 VAL A N   1 
ATOM   2020 C CA  . VAL A 1 257 ? 30.40139 13.27523 15.09460  1.000 33.41046  ? 257 VAL A CA  1 
ATOM   2021 C C   . VAL A 1 257 ? 31.18211 12.26828 15.92439  1.000 34.08906  ? 257 VAL A C   1 
ATOM   2022 O O   . VAL A 1 257 ? 30.82438 11.08438 15.99138  1.000 33.41409  ? 257 VAL A O   1 
ATOM   2023 C CB  . VAL A 1 257 ? 31.10785 13.57050 13.75803  1.000 32.50935  ? 257 VAL A CB  1 
ATOM   2024 C CG1 . VAL A 1 257 ? 31.49169 12.27071 13.05761  1.000 30.06609  ? 257 VAL A CG1 1 
ATOM   2025 C CG2 . VAL A 1 257 ? 30.22074 14.43342 12.87222  1.000 31.37236  ? 257 VAL A CG2 1 
ATOM   2026 N N   . HIS A 1 258 ? 32.26342 12.71871 16.56487  1.000 32.32222  ? 258 HIS A N   1 
ATOM   2027 C CA  . HIS A 1 258 ? 33.06562 11.81917 17.38821  1.000 36.76074  ? 258 HIS A CA  1 
ATOM   2028 C C   . HIS A 1 258 ? 32.22931 11.20386 18.50299  1.000 38.82578  ? 258 HIS A C   1 
ATOM   2029 O O   . HIS A 1 258 ? 32.25715 9.98601  18.71728  1.000 38.57849  ? 258 HIS A O   1 
ATOM   2030 C CB  . HIS A 1 258 ? 34.26450 12.56854 17.97023  1.000 36.10137  ? 258 HIS A CB  1 
ATOM   2031 C CG  . HIS A 1 258 ? 34.97373 11.82320 19.05790  1.000 37.98681  ? 258 HIS A CG  1 
ATOM   2032 N ND1 . HIS A 1 258 ? 34.56496 11.86101 20.37504  1.000 41.39760  ? 258 HIS A ND1 1 
ATOM   2033 C CD2 . HIS A 1 258 ? 36.07064 11.03017 19.02843  1.000 38.02007  ? 258 HIS A CD2 1 
ATOM   2034 C CE1 . HIS A 1 258 ? 35.37481 11.11748 21.10775  1.000 40.93202  ? 258 HIS A CE1 1 
ATOM   2035 N NE2 . HIS A 1 258 ? 36.29730 10.60197 20.31541  1.000 43.70175  ? 258 HIS A NE2 1 
ATOM   2036 N N   . ASP A 1 259 ? 31.47518 12.03739 19.22437  1.000 38.63393  ? 259 ASP A N   1 
ATOM   2037 C CA  . ASP A 1 259 ? 30.71179 11.54893 20.36756  1.000 43.50707  ? 259 ASP A CA  1 
ATOM   2038 C C   . ASP A 1 259 ? 29.64436 10.54749 19.94884  1.000 45.08813  ? 259 ASP A C   1 
ATOM   2039 O O   . ASP A 1 259 ? 29.32129 9.63276  20.71391  1.000 46.20234  ? 259 ASP A O   1 
ATOM   2040 C CB  . ASP A 1 259 ? 30.08027 12.72575 21.11338  1.000 44.38307  ? 259 ASP A CB  1 
ATOM   2041 C CG  . ASP A 1 259 ? 31.11263 13.59436 21.81109  1.000 44.61456  ? 259 ASP A CG  1 
ATOM   2042 O OD1 . ASP A 1 259 ? 32.29965 13.20677 21.84135  1.000 40.80815  ? 259 ASP A OD1 1 
ATOM   2043 O OD2 . ASP A 1 259 ? 30.73922 14.66599 22.32928  1.000 44.68534  ? 259 ASP A OD2 1 
ATOM   2044 N N   . SER A 1 260 ? 29.10172 10.68720 18.74007  1.000 39.15124  ? 260 SER A N   1 
ATOM   2045 C CA  . SER A 1 260 ? 27.99880 9.83698  18.30555  1.000 39.93391  ? 260 SER A CA  1 
ATOM   2046 C C   . SER A 1 260 ? 28.46084 8.52357  17.68706  1.000 41.68391  ? 260 SER A C   1 
ATOM   2047 O O   . SER A 1 260 ? 27.79380 7.49814  17.85931  1.000 42.83436  ? 260 SER A O   1 
ATOM   2048 C CB  . SER A 1 260 ? 27.12102 10.57933 17.29836  1.000 39.70055  ? 260 SER A CB  1 
ATOM   2049 O OG  . SER A 1 260 ? 26.51948 11.72401 17.87278  1.000 43.74001  ? 260 SER A OG  1 
ATOM   2050 N N   . PHE A 1 261 ? 29.57886 8.52734  16.95157  1.000 38.15320  ? 261 PHE A N   1 
ATOM   2051 C CA  . PHE A 1 261 ? 29.99786 7.34476  16.21059  1.000 38.58477  ? 261 PHE A CA  1 
ATOM   2052 C C   . PHE A 1 261 ? 31.28081 6.69775  16.71934  1.000 38.25313  ? 261 PHE A C   1 
ATOM   2053 O O   . PHE A 1 261 ? 31.47759 5.50168  16.48580  1.000 37.86180  ? 261 PHE A O   1 
ATOM   2054 C CB  . PHE A 1 261 ? 30.16603 7.68502  14.71886  1.000 34.07125  ? 261 PHE A CB  1 
ATOM   2055 C CG  . PHE A 1 261 ? 28.89372 8.14810  14.05819  1.000 34.45684  ? 261 PHE A CG  1 
ATOM   2056 C CD1 . PHE A 1 261 ? 27.91265 7.23453  13.69126  1.000 35.71807  ? 261 PHE A CD1 1 
ATOM   2057 C CD2 . PHE A 1 261 ? 28.67224 9.49477  13.81041  1.000 34.17386  ? 261 PHE A CD2 1 
ATOM   2058 C CE1 . PHE A 1 261 ? 26.73774 7.65639  13.09242  1.000 35.02198  ? 261 PHE A CE1 1 
ATOM   2059 C CE2 . PHE A 1 261 ? 27.49907 9.92242  13.20945  1.000 35.38710  ? 261 PHE A CE2 1 
ATOM   2060 C CZ  . PHE A 1 261 ? 26.53142 9.00032  12.84788  1.000 34.07479  ? 261 PHE A CZ  1 
ATOM   2061 N N   . ILE A 1 262 ? 32.15230 7.43364  17.40589  1.000 35.98436  ? 262 ILE A N   1 
ATOM   2062 C CA  . ILE A 1 262 ? 33.40948 6.84188  17.85042  1.000 40.37515  ? 262 ILE A CA  1 
ATOM   2063 C C   . ILE A 1 262 ? 33.28417 6.40810  19.30781  1.000 44.13658  ? 262 ILE A C   1 
ATOM   2064 O O   . ILE A 1 262 ? 33.52017 5.23878  19.63309  1.000 43.62178  ? 262 ILE A O   1 
ATOM   2065 C CB  . ILE A 1 262 ? 34.59311 7.80687  17.65169  1.000 38.14241  ? 262 ILE A CB  1 
ATOM   2066 C CG1 . ILE A 1 262 ? 34.66700 8.26122  16.19456  1.000 38.13514  ? 262 ILE A CG1 1 
ATOM   2067 C CG2 . ILE A 1 262 ? 35.90228 7.13673  18.04972  1.000 40.87197  ? 262 ILE A CG2 1 
ATOM   2068 C CD1 . ILE A 1 262 ? 34.93089 7.14003  15.20781  1.000 35.72851  ? 262 ILE A CD1 1 
ATOM   2069 N N   . GLU A 1 263 ? 32.90225 7.33790  20.18900  1.000 44.84540  ? 263 GLU A N   1 
ATOM   2070 C CA  . GLU A 1 263 ? 32.81633 7.06684  21.62501  1.000 53.82653  ? 263 GLU A CA  1 
ATOM   2071 C C   . GLU A 1 263 ? 32.35023 8.29126  22.40438  1.000 57.47920  ? 263 GLU A C   1 
ATOM   2072 O O   . GLU A 1 263 ? 32.67409 9.42412  22.03476  1.000 55.95644  ? 263 GLU A O   1 
ATOM   2073 C CB  . GLU A 1 263 ? 34.17221 6.62163  22.17401  1.000 56.79797  ? 263 GLU A CB  1 
ATOM   2074 C CG  . GLU A 1 263 ? 35.31209 7.52463  21.73245  1.000 59.54241  ? 263 GLU A CG  1 
ATOM   2075 C CD  . GLU A 1 263 ? 36.48339 7.50617  22.68636  1.000 62.51127  ? 263 GLU A CD  1 
ATOM   2076 O OE1 . GLU A 1 263 ? 36.26510 7.26243  23.89381  1.000 59.83341  ? 263 GLU A OE1 1 
ATOM   2077 O OE2 . GLU A 1 263 ? 37.62222 7.73791  22.22155  1.000 64.46232  ? 263 GLU A OE2 1 
ATOM   2078 N N   . ASP A 1 264 ? 31.61340 8.07989  23.49293  1.000 70.18362  ? 264 ASP A N   1 
ATOM   2079 C CA  . ASP A 1 264 ? 31.21148 9.18021  24.36930  1.000 74.08339  ? 264 ASP A CA  1 
ATOM   2080 C C   . ASP A 1 264 ? 31.29787 8.76505  25.83754  1.000 87.72394  ? 264 ASP A C   1 
ATOM   2081 O O   . ASP A 1 264 ? 32.08221 7.88829  26.20420  1.000 94.78625  ? 264 ASP A O   1 
ATOM   2082 C CB  . ASP A 1 264 ? 29.79000 9.65243  24.03695  1.000 78.75167  ? 264 ASP A CB  1 
ATOM   2083 C CG  . ASP A 1 264 ? 29.42574 10.96312 24.73141  1.000 81.99612  ? 264 ASP A CG  1 
ATOM   2084 O OD1 . ASP A 1 264 ? 30.28280 11.52778 25.44412  1.000 81.25218  ? 264 ASP A OD1 1 
ATOM   2085 O OD2 . ASP A 1 264 ? 28.27974 11.43377 24.56072  1.000 75.56484  ? 264 ASP A OD2 1 
HETATM 2086 C C1  . CIT B 2 .   ? 31.59873 24.01819 14.25805  1.000 48.68481  ? 301 CIT A C1  1 
HETATM 2087 O O1  . CIT B 2 .   ? 31.38593 22.81930 13.97915  1.000 44.34928  ? 301 CIT A O1  1 
HETATM 2088 O O2  . CIT B 2 .   ? 32.78405 24.38367 14.40811  1.000 51.32152  ? 301 CIT A O2  1 
HETATM 2089 C C2  . CIT B 2 .   ? 30.47466 25.02317 14.40736  1.000 52.07222  ? 301 CIT A C2  1 
HETATM 2090 C C3  . CIT B 2 .   ? 29.32523 24.56359 15.31005  1.000 52.36110  ? 301 CIT A C3  1 
HETATM 2091 O O7  . CIT B 2 .   ? 29.86112 24.04727 16.55879  1.000 55.36722  ? 301 CIT A O7  1 
HETATM 2092 C C4  . CIT B 2 .   ? 28.39459 25.73540 15.60934  1.000 56.48881  ? 301 CIT A C4  1 
HETATM 2093 C C5  . CIT B 2 .   ? 29.06692 26.72003 16.54086  1.000 60.82845  ? 301 CIT A C5  1 
HETATM 2094 O O3  . CIT B 2 .   ? 29.47406 27.81940 16.10284  1.000 60.90555  ? 301 CIT A O3  1 
HETATM 2095 O O4  . CIT B 2 .   ? 29.21396 26.45554 17.75821  1.000 59.46188  ? 301 CIT A O4  1 
HETATM 2096 C C6  . CIT B 2 .   ? 28.50727 23.46061 14.64932  1.000 50.01635  ? 301 CIT A C6  1 
HETATM 2097 O O5  . CIT B 2 .   ? 28.11411 23.58932 13.46711  1.000 48.54804  ? 301 CIT A O5  1 
HETATM 2098 O O6  . CIT B 2 .   ? 28.22846 22.41003 15.27589  1.000 48.22019  ? 301 CIT A O6  1 
HETATM 2099 N N1  . UZO C 3 .   ? 14.13867 9.43533  11.96804  1.000 43.61054  ? 302 UZO A N1  1 
HETATM 2100 C C7  . UZO C 3 .   ? 20.29583 12.38825 12.27301  1.000 35.70766  ? 302 UZO A C7  1 
HETATM 2101 C C8  . UZO C 3 .   ? 21.34376 13.17448 11.75758  1.000 34.93675  ? 302 UZO A C8  1 
HETATM 2102 N N2  . UZO C 3 .   ? 18.91623 12.49203 12.16102  1.000 35.72933  ? 302 UZO A N2  1 
HETATM 2103 C C9  . UZO C 3 .   ? 22.80095 11.67156 12.74246  1.000 34.49022  ? 302 UZO A C9  1 
HETATM 2104 O O1  . UZO C 3 .   ? 15.91353 5.04605  13.08957  1.000 46.36218  ? 302 UZO A O1  1 
HETATM 2105 C C1  . UZO C 3 .   ? 11.75666 9.26815  12.75024  1.000 54.72600  ? 302 UZO A C1  1 
HETATM 2106 O O5  . UZO C 3 .   ? 17.79962 10.38485 7.90237   1.000 30.57018  ? 302 UZO A O5  1 
HETATM 2107 C C5  . UZO C 3 .   ? 17.08815 11.07323 12.88895  1.000 38.11658  ? 302 UZO A C5  1 
HETATM 2108 C C6  . UZO C 3 .   ? 18.45857 11.44325 12.81665  1.000 37.50244  ? 302 UZO A C6  1 
HETATM 2109 N N3  . UZO C 3 .   ? 21.15866 14.27767 11.02369  1.000 32.35241  ? 302 UZO A N3  1 
HETATM 2110 C C4  . UZO C 3 .   ? 15.91094 10.87321 12.87112  1.000 39.31926  ? 302 UZO A C4  1 
HETATM 2111 O O4  . UZO C 3 .   ? 15.84567 8.43945  9.85538   1.000 39.92799  ? 302 UZO A O4  1 
HETATM 2112 C C3  . UZO C 3 .   ? 14.48406 10.51246 12.89197  1.000 41.06401  ? 302 UZO A C3  1 
HETATM 2113 O O3  . UZO C 3 .   ? 19.31163 10.21488 16.50964  1.000 40.16250  ? 302 UZO A O3  1 
HETATM 2114 C C2  . UZO C 3 .   ? 13.04864 8.55220  12.40383  1.000 48.24216  ? 302 UZO A C2  1 
HETATM 2115 N N4  . UZO C 3 .   ? 22.60905 12.77734 12.01693  1.000 33.40009  ? 302 UZO A N4  1 
HETATM 2116 N N   . UZO C 3 .   ? 11.28363 7.53281  14.46179  1.000 66.29060  ? 302 UZO A N   1 
HETATM 2117 C C   . UZO C 3 .   ? 10.72813 8.33471  13.36202  1.000 62.13117  ? 302 UZO A C   1 
HETATM 2118 O O   . UZO C 3 .   ? 18.66795 8.45785  13.44338  1.000 40.51366  ? 302 UZO A O   1 
HETATM 2119 C C10 . UZO C 3 .   ? 20.65023 11.27218 13.01091  1.000 35.56876  ? 302 UZO A C10 1 
HETATM 2120 C C11 . UZO C 3 .   ? 19.32509 9.46963  14.18493  1.000 39.26844  ? 302 UZO A C11 1 
HETATM 2121 C C12 . UZO C 3 .   ? 17.89269 7.63065  14.34479  1.000 43.09503  ? 302 UZO A C12 1 
HETATM 2122 C C13 . UZO C 3 .   ? 16.42619 7.65049  13.95899  1.000 43.54715  ? 302 UZO A C13 1 
HETATM 2123 C C14 . UZO C 3 .   ? 15.83494 5.96486  12.27697  1.000 44.96939  ? 302 UZO A C14 1 
HETATM 2124 C C15 . UZO C 3 .   ? 14.83966 4.50571  10.56980  1.000 47.91949  ? 302 UZO A C15 1 
HETATM 2125 C C16 . UZO C 3 .   ? 13.45570 4.62383  9.97822   1.000 51.40690  ? 302 UZO A C16 1 
HETATM 2126 C C17 . UZO C 3 .   ? 12.47240 5.36852  10.61422  1.000 55.73796  ? 302 UZO A C17 1 
HETATM 2127 C C18 . UZO C 3 .   ? 11.20778 5.49145  10.06082  1.000 58.41026  ? 302 UZO A C18 1 
HETATM 2128 C C19 . UZO C 3 .   ? 10.91019 4.87135  8.86763   1.000 58.29472  ? 302 UZO A C19 1 
HETATM 2129 C C20 . UZO C 3 .   ? 11.87502 4.12601  8.22731   1.000 55.46196  ? 302 UZO A C20 1 
HETATM 2130 C C21 . UZO C 3 .   ? 13.14000 4.00157  8.77890   1.000 52.28010  ? 302 UZO A C21 1 
HETATM 2131 C C22 . UZO C 3 .   ? 18.20166 8.15096  15.74832  1.000 43.47011  ? 302 UZO A C22 1 
HETATM 2132 C C23 . UZO C 3 .   ? 18.53016 9.61825  15.47848  1.000 42.30354  ? 302 UZO A C23 1 
HETATM 2133 C C24 . UZO C 3 .   ? 14.01433 9.84933  10.56347  1.000 40.27364  ? 302 UZO A C24 1 
HETATM 2134 C C25 . UZO C 3 .   ? 15.35561 9.79247  9.85582   1.000 40.22835  ? 302 UZO A C25 1 
HETATM 2135 C C26 . UZO C 3 .   ? 16.89486 8.37107  8.90621   1.000 38.08826  ? 302 UZO A C26 1 
HETATM 2136 C C27 . UZO C 3 .   ? 16.67679 9.50693  7.88791   1.000 34.54088  ? 302 UZO A C27 1 
HETATM 2137 C C28 . UZO C 3 .   ? 15.38600 10.18169 8.38322   1.000 35.13505  ? 302 UZO A C28 1 
HETATM 2138 C C29 . UZO C 3 .   ? 15.91885 6.43845  7.58098   1.000 39.71182  ? 302 UZO A C29 1 
HETATM 2139 C C30 . UZO C 3 .   ? 17.54473 5.07417  7.55608   1.000 37.72610  ? 302 UZO A C30 1 
HETATM 2140 C C31 . UZO C 3 .   ? 18.47242 4.02953  7.37767   1.000 36.49221  ? 302 UZO A C31 1 
HETATM 2141 C C32 . UZO C 3 .   ? 19.94801 5.27049  8.65293   1.000 36.02072  ? 302 UZO A C32 1 
HETATM 2142 C C33 . UZO C 3 .   ? 17.96262 6.15922  8.30978   1.000 37.63071  ? 302 UZO A C33 1 
HETATM 2143 N N10 . UZO C 3 .   ? 16.24803 5.26312  7.10188   1.000 39.09981  ? 302 UZO A N10 1 
HETATM 2144 N N11 . UZO C 3 .   ? 18.22001 2.91856  6.67865   1.000 35.00159  ? 302 UZO A N11 1 
HETATM 2145 N N12 . UZO C 3 .   ? 19.68879 4.16643  7.94746   1.000 33.42995  ? 302 UZO A N12 1 
HETATM 2146 N N13 . UZO C 3 .   ? 19.15434 6.31661  8.89299   1.000 35.68933  ? 302 UZO A N13 1 
HETATM 2147 N N5  . UZO C 3 .   ? 21.89197 10.85746 13.28589  1.000 33.92057  ? 302 UZO A N5  1 
HETATM 2148 N N6  . UZO C 3 .   ? 19.46134 10.66704 13.37019  1.000 38.07394  ? 302 UZO A N6  1 
HETATM 2149 N N7  . UZO C 3 .   ? 16.17858 7.23214  12.58566  1.000 43.69845  ? 302 UZO A N7  1 
HETATM 2150 N N8  . UZO C 3 .   ? 15.37400 5.78328  11.02064  1.000 45.53477  ? 302 UZO A N8  1 
HETATM 2151 N N9  . UZO C 3 .   ? 16.90925 7.03963  8.31296   1.000 38.43318  ? 302 UZO A N9  1 
HETATM 2152 O O2  . UZO C 3 .   ? 19.31957 7.46097  16.29574  1.000 47.72860  ? 302 UZO A O2  1 
HETATM 2153 O O6  . UZO C 3 .   ? 15.43720 11.59600 8.22479   1.000 33.43219  ? 302 UZO A O6  1 
HETATM 2154 O O   . HOH D 4 .   ? 18.87184 26.68255 -6.79909  1.000 44.39405  ? 401 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 11.03633 35.13718 39.77499  1.000 54.08472  ? 402 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 16.82648 2.03583  -20.98865 1.000 52.45076  ? 403 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 16.88209 11.58160 22.76715  1.000 52.73418  ? 404 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 24.16672 8.22379  -8.96494  1.000 28.41766  ? 405 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 32.09721 15.75574 24.12252  1.000 48.91839  ? 406 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 35.29949 23.61567 21.44362  1.000 53.23721  ? 407 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 10.44387 5.92085  -14.44628 1.000 48.00945  ? 408 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 13.63329 10.96289 4.44356   1.000 30.10893  ? 409 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 30.86772 5.24930  11.78424  1.000 35.10584  ? 410 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 9.71445  6.52889  1.36569   1.000 43.34200  ? 411 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 23.58154 5.75682  -17.30691 1.000 36.87410  ? 412 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 20.19523 22.13824 19.57951  1.000 44.05599  ? 413 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 14.27063 -1.09728 -9.01402  1.000 44.97484  ? 414 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 13.67752 36.07695 22.16654  1.000 72.64353  ? 415 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 17.45102 10.69434 18.30933  1.000 42.11249  ? 416 HOH A O   1 
HETATM 2170 O O   . HOH D 4 .   ? 20.11201 26.50037 2.61606   1.000 35.66398  ? 417 HOH A O   1 
HETATM 2171 O O   . HOH D 4 .   ? 18.76447 -0.73484 -0.88099  1.000 41.57381  ? 418 HOH A O   1 
HETATM 2172 O O   . HOH D 4 .   ? 8.53344  21.13904 3.63431   1.000 41.65476  ? 419 HOH A O   1 
HETATM 2173 O O   . HOH D 4 .   ? 27.44806 5.57785  -1.73050  1.000 35.45355  ? 420 HOH A O   1 
HETATM 2174 O O   . HOH D 4 .   ? 22.24811 21.10077 7.03468   1.000 32.57539  ? 421 HOH A O   1 
HETATM 2175 O O   . HOH D 4 .   ? 22.74559 11.22039 0.42104   1.000 24.79324  ? 422 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 25.32592 3.42716  -1.92269  1.000 35.00298  ? 423 HOH A O   1 
HETATM 2177 O O   . HOH D 4 .   ? 13.47553 26.75074 -0.56185  1.000 44.37195  ? 424 HOH A O   1 
HETATM 2178 O O   . HOH D 4 .   ? 13.36704 18.94641 0.55797   1.000 40.66242  ? 425 HOH A O   1 
HETATM 2179 O O   . HOH D 4 .   ? 14.50696 4.07075  5.43526   1.000 44.00009  ? 426 HOH A O   1 
HETATM 2180 O O   . HOH D 4 .   ? 5.73236  18.80106 12.37420  1.000 47.25422  ? 427 HOH A O   1 
HETATM 2181 O O   . HOH D 4 .   ? 33.49622 21.16471 13.67714  1.000 38.96229  ? 428 HOH A O   1 
HETATM 2182 O O   . HOH D 4 .   ? 32.03916 26.76673 25.01472  1.000 59.82409  ? 429 HOH A O   1 
HETATM 2183 O O   . HOH D 4 .   ? 25.47776 9.28945  -6.58461  1.000 28.47905  ? 430 HOH A O   1 
HETATM 2184 O O   . HOH D 4 .   ? 13.74852 22.32355 -6.03119  1.000 39.43179  ? 431 HOH A O   1 
HETATM 2185 O O   . HOH D 4 .   ? 11.24117 7.53184  -0.65203  1.000 36.67014  ? 432 HOH A O   1 
HETATM 2186 O O   . HOH D 4 .   ? 20.62547 11.63239 4.90903   1.000 30.24284  ? 433 HOH A O   1 
HETATM 2187 O O   . HOH D 4 .   ? 21.31446 1.52857  -13.05670 1.000 40.86907  ? 434 HOH A O   1 
HETATM 2188 O O   . HOH D 4 .   ? 25.82444 27.20362 6.78525   1.000 45.48434  ? 435 HOH A O   1 
HETATM 2189 O O   . HOH D 4 .   ? 22.15012 23.22923 -5.26453  1.000 34.11136  ? 436 HOH A O   1 
HETATM 2190 O O   . HOH D 4 .   ? 33.96547 20.92745 22.86909  1.000 51.25850  ? 437 HOH A O   1 
HETATM 2191 O O   . HOH D 4 .   ? 15.24352 28.53699 -1.96224  1.000 46.94504  ? 438 HOH A O   1 
HETATM 2192 O O   . HOH D 4 .   ? 6.76619  11.16296 19.91642  1.000 52.21196  ? 439 HOH A O   1 
HETATM 2193 O O   . HOH D 4 .   ? 16.25918 34.51604 14.82901  1.000 57.64134  ? 440 HOH A O   1 
HETATM 2194 O O   . HOH D 4 .   ? 23.13259 7.54580  11.18063  1.000 39.37153  ? 441 HOH A O   1 
HETATM 2195 O O   . HOH D 4 .   ? 10.12285 13.60191 12.73639  1.000 42.33970  ? 442 HOH A O   1 
HETATM 2196 O O   . HOH D 4 .   ? 27.97532 26.23096 -2.58212  1.000 39.37231  ? 443 HOH A O   1 
HETATM 2197 O O   . HOH D 4 .   ? 24.39558 16.46865 11.75376  1.000 36.26495  ? 444 HOH A O   1 
HETATM 2198 O O   . HOH D 4 .   ? 29.21410 6.59951  4.83723   1.000 28.59401  ? 445 HOH A O   1 
HETATM 2199 O O   . HOH D 4 .   ? 15.56968 30.93656 6.94487   1.000 51.93807  ? 446 HOH A O   1 
HETATM 2200 O O   . HOH D 4 .   ? 14.74085 17.10263 20.42199  1.000 42.00867  ? 447 HOH A O   1 
HETATM 2201 O O   . HOH D 4 .   ? 31.45750 5.24400  0.00000   0.50  35.19419  ? 448 HOH A O   1 
HETATM 2202 O O   . HOH D 4 .   ? 15.28535 28.61317 12.15982  1.000 42.33174  ? 449 HOH A O   1 
HETATM 2203 O O   . HOH D 4 .   ? 12.10096 1.53582  -5.46130  1.000 41.50233  ? 450 HOH A O   1 
HETATM 2204 O O   . HOH D 4 .   ? 28.60850 2.35484  -10.56642 1.000 37.18587  ? 451 HOH A O   1 
HETATM 2205 O O   . HOH D 4 .   ? 4.67895  18.85215 29.12728  1.000 44.73321  ? 452 HOH A O   1 
HETATM 2206 O O   . HOH D 4 .   ? 3.79725  32.80368 29.19423  1.000 51.75378  ? 453 HOH A O   1 
HETATM 2207 O O   . HOH D 4 .   ? 11.01587 26.83358 -0.16251  1.000 48.56082  ? 454 HOH A O   1 
HETATM 2208 O O   . HOH D 4 .   ? 20.62328 26.86220 -4.81736  1.000 36.34148  ? 455 HOH A O   1 
HETATM 2209 O O   . HOH D 4 .   ? 4.67221  18.81890 22.75033  1.000 56.23309  ? 456 HOH A O   1 
HETATM 2210 O O   . HOH D 4 .   ? 29.24889 28.99008 1.56621   1.000 56.54670  ? 457 HOH A O   1 
HETATM 2211 O O   . HOH D 4 .   ? 10.59326 29.88369 6.49092   1.000 53.89607  ? 458 HOH A O   1 
HETATM 2212 O O   . HOH D 4 .   ? 24.22871 5.43917  9.97757   1.000 37.75610  ? 459 HOH A O   1 
HETATM 2213 O O   . HOH D 4 .   ? 26.17336 6.81446  -3.73797  1.000 29.68527  ? 460 HOH A O   1 
HETATM 2214 O O   . HOH D 4 .   ? 9.69521  2.79699  -14.42552 1.000 55.03338  ? 461 HOH A O   1 
HETATM 2215 O O   . HOH D 4 .   ? 28.92512 -4.35342 -24.22821 1.000 66.50756  ? 462 HOH A O   1 
HETATM 2216 O O   . HOH D 4 .   ? 27.62934 27.44172 -7.87238  1.000 53.34448  ? 463 HOH A O   1 
HETATM 2217 O O   . HOH D 4 .   ? 12.27853 -0.83997 -6.95718  1.000 47.96684  ? 464 HOH A O   1 
HETATM 2218 O O   . HOH D 4 .   ? 0.72918  17.17314 -4.59561  1.000 57.09667  ? 465 HOH A O   1 
HETATM 2219 O O   . HOH D 4 .   ? 20.13591 8.08753  11.04419  1.000 34.26786  ? 466 HOH A O   1 
HETATM 2220 O O   . HOH D 4 .   ? 23.49014 0.59125  -1.87026  1.000 36.61261  ? 467 HOH A O   1 
HETATM 2221 O O   . HOH D 4 .   ? 6.62237  14.13923 -0.34105  1.000 49.59890  ? 468 HOH A O   1 
HETATM 2222 O O   . HOH D 4 .   ? 25.52876 -0.85868 -6.60571  1.000 45.66297  ? 469 HOH A O   1 
HETATM 2223 O O   . HOH D 4 .   ? 26.91537 3.33971  -4.59759  1.000 44.37912  ? 470 HOH A O   1 
HETATM 2224 O O   . HOH D 4 .   ? 26.24694 29.99627 10.91664  1.000 46.64238  ? 471 HOH A O   1 
HETATM 2225 O O   . HOH D 4 .   ? 34.49833 14.70527 22.91945  1.000 45.80124  ? 472 HOH A O   1 
HETATM 2226 O O   . HOH D 4 .   ? 7.868    18.267   36.060    1.000 51.51532  ? 473 HOH A O   1 
HETATM 2227 O O   . HOH D 4 .   ? 29.69223 26.82958 1.10535   1.000 40.93153  ? 474 HOH A O   1 
HETATM 2228 O O   . HOH D 4 .   ? 25.62132 14.38769 -21.34251 1.000 45.52238  ? 475 HOH A O   1 
HETATM 2229 O O   . HOH D 4 .   ? 8.23335  18.11686 18.10380  1.000 41.42061  ? 476 HOH A O   1 
HETATM 2230 O O   . HOH D 4 .   ? 10.08792 25.23878 -7.34607  1.000 52.93613  ? 477 HOH A O   1 
HETATM 2231 O O   . HOH D 4 .   ? 21.23963 21.18226 1.33936   1.000 32.00341  ? 478 HOH A O   1 
HETATM 2232 O O   . HOH D 4 .   ? 29.80146 4.52206  7.90721   1.000 36.20238  ? 479 HOH A O   1 
HETATM 2233 O O   . HOH D 4 .   ? 24.58603 1.49054  -5.46719  1.000 38.40535  ? 480 HOH A O   1 
HETATM 2234 O O   . HOH D 4 .   ? 8.36270  13.25096 -17.39816 1.000 54.54451  ? 481 HOH A O   1 
HETATM 2235 O O   . HOH D 4 .   ? 5.26780  26.94481 9.80700   1.000 52.82670  ? 482 HOH A O   1 
HETATM 2236 O O   . HOH D 4 .   ? 22.46096 32.84547 8.18381   1.000 55.40934  ? 483 HOH A O   1 
HETATM 2237 O O   . HOH D 4 .   ? 8.15942  13.00728 15.85162  1.000 44.47177  ? 484 HOH A O   1 
HETATM 2238 O O   . HOH D 4 .   ? 10.08109 14.85287 9.82751   1.000 44.36067  ? 485 HOH A O   1 
HETATM 2239 O O   . HOH D 4 .   ? 12.85983 11.55172 18.53117  1.000 40.25926  ? 486 HOH A O   1 
HETATM 2240 O O   . HOH D 4 .   ? 27.13211 21.72380 -14.54557 1.000 39.95938  ? 487 HOH A O   1 
HETATM 2241 O O   . HOH D 4 .   ? 10.43763 4.08602  -12.22904 1.000 45.79885  ? 488 HOH A O   1 
HETATM 2242 O O   . HOH D 4 .   ? 0.50411  23.78834 26.39244  1.000 57.20086  ? 489 HOH A O   1 
HETATM 2243 O O   . HOH D 4 .   ? 18.69514 19.89944 -14.26560 1.000 39.20007  ? 490 HOH A O   1 
HETATM 2244 O O   . HOH D 4 .   ? 34.62866 8.19008  27.86524  1.000 62.07599  ? 491 HOH A O   1 
HETATM 2245 O O   . HOH D 4 .   ? 21.06635 14.61876 32.22350  1.000 55.40463  ? 492 HOH A O   1 
HETATM 2246 O O   . HOH D 4 .   ? 10.93817 32.79427 7.41962   1.000 57.37257  ? 493 HOH A O   1 
HETATM 2247 O O   . HOH D 4 .   ? 28.83278 25.95467 11.59743  1.000 49.57165  ? 494 HOH A O   1 
HETATM 2248 O O   . HOH D 4 .   ? 25.05922 16.41993 24.99917  1.000 52.12773  ? 495 HOH A O   1 
HETATM 2249 O O   . HOH D 4 .   ? 6.76198  16.36264 19.14219  1.000 49.04873  ? 496 HOH A O   1 
HETATM 2250 O O   . HOH D 4 .   ? 16.14035 19.27182 -16.06306 1.000 46.13254  ? 497 HOH A O   1 
HETATM 2251 O O   . HOH D 4 .   ? 23.08253 7.96301  13.83648  1.000 42.71941  ? 498 HOH A O   1 
HETATM 2252 O O   . HOH D 4 .   ? 14.76704 9.86108  16.84163  1.000 42.30164  ? 499 HOH A O   1 
HETATM 2253 O O   . HOH D 4 .   ? 27.67546 26.99195 9.88557   1.000 43.75883  ? 500 HOH A O   1 
HETATM 2254 O O   . HOH D 4 .   ? 24.78055 31.41769 7.55565   1.000 56.52794  ? 501 HOH A O   1 
HETATM 2255 O O   . HOH D 4 .   ? 29.302   26.096   -11.704   1.000 53.62046  ? 502 HOH A O   1 
HETATM 2256 O O   . HOH D 4 .   ? 35.765   10.516   24.016    1.000 52.19474  ? 503 HOH A O   1 
HETATM 2257 O O   . HOH D 4 .   ? 30.91319 30.06215 23.67168  1.000 63.73175  ? 504 HOH A O   1 
HETATM 2258 O O   . HOH D 4 .   ? 10.21749 10.40176 16.22830  1.000 53.44273  ? 505 HOH A O   1 
HETATM 2259 O O   . HOH D 4 .   ? 11.87540 8.10936  7.99562   1.000 52.44727  ? 506 HOH A O   1 
HETATM 2260 O O   . HOH D 4 .   ? 0.00000  37.65300 26.50391  0.50  65.15571  ? 507 HOH A O   1 
HETATM 2261 O O   . HOH D 4 .   ? 25.88432 14.48865 25.97741  1.000 60.12098  ? 508 HOH A O   1 
HETATM 2262 O O   . HOH D 4 .   ? 12.85288 31.39495 5.90204   1.000 52.76596  ? 509 HOH A O   1 
HETATM 2263 O O   . HOH D 4 .   ? 29.95273 4.82615  -1.93240  1.000 38.95349  ? 510 HOH A O   1 
HETATM 2264 O O   . HOH D 4 .   ? 25.20347 26.10773 -13.14839 1.000 47.71963  ? 511 HOH A O   1 
HETATM 2265 O O   . HOH D 4 .   ? 13.07574 6.06472  4.54196   1.000 48.78212  ? 512 HOH A O   1 
HETATM 2266 O O   . HOH D 4 .   ? 13.70554 8.09418  5.52027   1.000 41.76982  ? 513 HOH A O   1 
HETATM 2267 O O   . HOH D 4 .   ? 31.75271 4.65417  -4.22674  1.000 37.66318  ? 514 HOH A O   1 
HETATM 2268 O O   . HOH D 4 .   ? 0.56337  14.40424 -2.59832  1.000 56.92333  ? 515 HOH A O   1 
HETATM 2269 O O   . HOH D 4 .   ? 4.52625  28.77428 11.14703  1.000 56.17472  ? 516 HOH A O   1 
HETATM 2270 O O   . HOH D 4 .   ? 15.82107 28.87808 -4.67084  1.000 58.00579  ? 517 HOH A O   1 
HETATM 2271 O O   . HOH D 4 .   ? 0.47176  25.99457 27.50208  1.000 62.50962  ? 518 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   ? 1.08724 0.87366 0.96271 0.05501  0.09152  -0.18918 1   MET A N   
2    C CA  . MET A 1   ? 1.10383 0.86218 0.97402 0.07363  0.09629  -0.18318 1   MET A CA  
3    C C   . MET A 1   ? 1.01266 0.79839 0.89053 0.09232  0.08323  -0.16777 1   MET A C   
4    O O   . MET A 1   ? 0.93344 0.75337 0.81868 0.09408  0.07718  -0.17251 1   MET A O   
5    C CB  . MET A 1   ? 1.22804 0.93472 1.08595 0.07852  0.10691  -0.17355 1   MET A CB  
6    N N   . LYS A 2   ? 0.93874 0.71030 0.81431 0.10579  0.07992  -0.15012 2   LYS A N   
7    C CA  . LYS A 2   ? 0.85880 0.65881 0.74335 0.12015  0.06817  -0.13716 2   LYS A CA  
8    C C   . LYS A 2   ? 0.78841 0.62001 0.68065 0.11033  0.05839  -0.13183 2   LYS A C   
9    O O   . LYS A 2   ? 0.77967 0.60319 0.66852 0.09920  0.05910  -0.13004 2   LYS A O   
10   C CB  . LYS A 2   ? 0.87085 0.64963 0.75025 0.13838  0.06782  -0.12218 2   LYS A CB  
11   C CG  . LYS A 2   ? 0.91655 0.66069 0.78682 0.15226  0.07861  -0.12496 2   LYS A CG  
12   C CD  . LYS A 2   ? 0.92250 0.66443 0.79163 0.17674  0.07445  -0.10996 2   LYS A CD  
13   C CE  . LYS A 2   ? 0.97596 0.69055 0.83833 0.19439  0.08459  -0.11307 2   LYS A CE  
14   N NZ  . LYS A 2   ? 1.00477 0.74177 0.87430 0.21877  0.07698  -0.10388 2   LYS A NZ  
15   N N   . TYR A 3   ? 0.72256 0.58876 0.62480 0.11464  0.05081  -0.12933 3   TYR A N   
16   C CA  . TYR A 3   ? 0.68059 0.57481 0.58953 0.10738  0.04347  -0.12401 3   TYR A CA  
17   C C   . TYR A 3   ? 0.65381 0.57173 0.57224 0.11777  0.03770  -0.11540 3   TYR A C   
18   O O   . TYR A 3   ? 0.64936 0.57071 0.57064 0.12808  0.03906  -0.11712 3   TYR A O   
19   C CB  . TYR A 3   ? 0.66472 0.57993 0.57402 0.09509  0.04404  -0.13535 3   TYR A CB  
20   C CG  . TYR A 3   ? 0.65884 0.59896 0.57155 0.10053  0.04328  -0.13986 3   TYR A CG  
21   C CD1 . TYR A 3   ? 0.70479 0.63664 0.61399 0.10380  0.04921  -0.15123 3   TYR A CD1 
22   C CD2 . TYR A 3   ? 0.61684 0.58655 0.53509 0.10273  0.03826  -0.13243 3   TYR A CD2 
23   C CE1 . TYR A 3   ? 0.68587 0.64155 0.59713 0.10867  0.04918  -0.15542 3   TYR A CE1 
24   C CE2 . TYR A 3   ? 0.61970 0.61048 0.53889 0.10789  0.03920  -0.13509 3   TYR A CE2 
25   C CZ  . TYR A 3   ? 0.64525 0.63055 0.56100 0.11062  0.04417  -0.14675 3   TYR A CZ  
26   O OH  . TYR A 3   ? 0.62311 0.63054 0.53885 0.11560  0.04567  -0.14946 3   TYR A OH  
27   N N   . MET A 4   ? 0.60158 0.53583 0.52549 0.11421  0.03257  -0.10718 4   MET A N   
28   C CA  . MET A 4   ? 0.58483 0.54238 0.51830 0.11964  0.02970  -0.10116 4   MET A CA  
29   C C   . MET A 4   ? 0.55014 0.52519 0.48615 0.11189  0.02800  -0.09725 4   MET A C   
30   O O   . MET A 4   ? 0.52964 0.50120 0.46162 0.10376  0.02724  -0.09824 4   MET A O   
31   C CB  . MET A 4   ? 0.61986 0.57509 0.55850 0.12789  0.02670  -0.09362 4   MET A CB  
32   C CG  . MET A 4   ? 0.59269 0.54117 0.52988 0.12318  0.02336  -0.08660 4   MET A CG  
33   S SD  . MET A 4   ? 0.61769 0.58935 0.56500 0.11700  0.02154  -0.08100 4   MET A SD  
34   C CE  . MET A 4   ? 0.61522 0.60642 0.57437 0.12523  0.02247  -0.08174 4   MET A CE  
35   N N   . ILE A 5   ? 0.53132 0.52512 0.47393 0.11490  0.02874  -0.09284 5   ILE A N   
36   C CA  . ILE A 5   ? 0.51326 0.52123 0.45699 0.11091  0.02921  -0.08711 5   ILE A CA  
37   C C   . ILE A 5   ? 0.52765 0.54159 0.48047 0.11286  0.03102  -0.07960 5   ILE A C   
38   O O   . ILE A 5   ? 0.49114 0.51229 0.44946 0.11723  0.03405  -0.08054 5   ILE A O   
39   C CB  . ILE A 5   ? 0.51683 0.54168 0.45555 0.11206  0.03195  -0.09010 5   ILE A CB  
40   C CG1 . ILE A 5   ? 0.47287 0.49510 0.40399 0.10832  0.03105  -0.10183 5   ILE A CG1 
41   C CG2 . ILE A 5   ? 0.48354 0.52145 0.42100 0.11125  0.03283  -0.08203 5   ILE A CG2 
42   C CD1 . ILE A 5   ? 0.55324 0.59782 0.47815 0.10941  0.03265  -0.10664 5   ILE A CD1 
43   N N   . THR A 6   ? 0.49438 0.50616 0.44957 0.10864  0.03022  -0.07379 6   THR A N   
44   C CA  . THR A 6   ? 0.50678 0.52384 0.47054 0.10780  0.03421  -0.06854 6   THR A CA  
45   C C   . THR A 6   ? 0.50432 0.52830 0.46568 0.10784  0.04043  -0.06215 6   THR A C   
46   O O   . THR A 6   ? 0.53626 0.56321 0.49005 0.10843  0.03892  -0.06067 6   THR A O   
47   C CB  . THR A 6   ? 0.52785 0.53771 0.49520 0.10356  0.03116  -0.06673 6   THR A CB  
48   O OG1 . THR A 6   ? 0.51052 0.51521 0.47214 0.09975  0.02952  -0.06406 6   THR A OG1 
49   C CG2 . THR A 6   ? 0.56641 0.56959 0.53323 0.10648  0.02547  -0.07053 6   THR A CG2 
50   N N   . SER A 7   ? 0.50143 0.52879 0.46903 0.10762  0.04839  -0.05853 7   SER A N   
51   C CA  . SER A 7   ? 0.53814 0.56743 0.50151 0.10982  0.05726  -0.05008 7   SER A CA  
52   C C   . SER A 7   ? 0.55880 0.57996 0.52959 0.10492  0.06515  -0.04586 7   SER A C   
53   O O   . SER A 7   ? 0.56155 0.58248 0.54304 0.09917  0.06613  -0.05140 7   SER A O   
54   C CB  . SER A 7   ? 0.56580 0.60338 0.52637 0.11413  0.06442  -0.04922 7   SER A CB  
55   O OG  . SER A 7   ? 0.58667 0.62273 0.54111 0.11763  0.07523  -0.03865 7   SER A OG  
56   N N   . LYS A 8   ? 0.55646 0.57249 0.52137 0.10787  0.07126  -0.03679 8   LYS A N   
57   C CA  . LYS A 8   ? 0.59853 0.60272 0.56894 0.10377  0.08277  -0.03246 8   LYS A CA  
58   C C   . LYS A 8   ? 0.63135 0.63367 0.60741 0.10018  0.09592  -0.03298 8   LYS A C   
59   O O   . LYS A 8   ? 0.68518 0.67974 0.67101 0.09162  0.10513  -0.03611 8   LYS A O   
60   C CB  . LYS A 8   ? 0.62724 0.62532 0.58808 0.11154  0.08837  -0.02092 8   LYS A CB  
61   C CG  . LYS A 8   ? 0.67871 0.65910 0.64323 0.10875  0.10329  -0.01559 8   LYS A CG  
62   C CD  . LYS A 8   ? 0.73236 0.70675 0.68498 0.12131  0.11042  -0.00165 8   LYS A CD  
63   C CE  . LYS A 8   ? 0.79040 0.74190 0.74660 0.11861  0.12633  0.00281  8   LYS A CE  
64   N NZ  . LYS A 8   ? 0.81656 0.76537 0.78534 0.10612  0.12085  -0.00889 8   LYS A NZ  
65   N N   . GLY A 9   ? 0.63797 0.64845 0.60843 0.10532  0.09802  -0.03141 9   GLY A N   
66   C CA  . GLY A 9   ? 0.64571 0.65727 0.62218 0.10094  0.11049  -0.03342 9   GLY A CA  
67   C C   . GLY A 9   ? 0.67487 0.67542 0.64101 0.10562  0.12803  -0.02080 9   GLY A C   
68   O O   . GLY A 9   ? 0.71916 0.71963 0.68889 0.10129  0.14077  -0.02191 9   GLY A O   
69   N N   . ASP A 10  ? 0.67622 0.66799 0.62932 0.11506  0.13006  -0.00847 10  ASP A N   
70   C CA  . ASP A 10  ? 0.73930 0.72169 0.67765 0.12450  0.14587  0.00645  10  ASP A CA  
71   C C   . ASP A 10  ? 0.73474 0.73624 0.66015 0.13459  0.13978  0.00890  10  ASP A C   
72   O O   . ASP A 10  ? 0.70218 0.72143 0.63054 0.13377  0.12387  -0.00156 10  ASP A O   
73   C CB  . ASP A 10  ? 0.77470 0.74361 0.70301 0.13440  0.15024  0.01958  10  ASP A CB  
74   C CG  . ASP A 10  ? 0.77076 0.75771 0.69323 0.14323  0.13147  0.01916  10  ASP A CG  
75   O OD1 . ASP A 10  ? 0.72316 0.72495 0.65322 0.13694  0.11556  0.00633  10  ASP A OD1 
76   O OD2 . ASP A 10  ? 0.86386 0.85044 0.77417 0.15673  0.13361  0.03143  10  ASP A OD2 
77   N N   . GLU A 11  ? 0.77098 0.76741 0.68063 0.14443  0.15400  0.02285  11  GLU A N   
78   C CA  . GLU A 11  ? 0.79424 0.81070 0.69017 0.15378  0.15017  0.02474  11  GLU A CA  
79   C C   . GLU A 11  ? 0.76311 0.80147 0.65098 0.16305  0.13137  0.02244  11  GLU A C   
80   O O   . GLU A 11  ? 0.75242 0.81079 0.63979 0.16235  0.11995  0.01173  11  GLU A O   
81   C CB  . GLU A 11  ? 0.86775 0.87390 0.74480 0.16466  0.17001  0.04277  11  GLU A CB  
82   C CG  . GLU A 11  ? 0.91749 0.90710 0.80121 0.15354  0.19036  0.04224  11  GLU A CG  
83   C CD  . GLU A 11  ? 0.96102 0.94116 0.82247 0.16502  0.21044  0.06052  11  GLU A CD  
84   O OE1 . GLU A 11  ? 0.97130 0.96233 0.81124 0.18358  0.20629  0.07344  11  GLU A OE1 
85   O OE2 . GLU A 11  ? 0.96824 0.93169 0.83329 0.15551  0.23096  0.06170  11  GLU A OE2 
86   N N   . LYS A 12  ? 0.76384 0.79940 0.64615 0.17121  0.12900  0.03103  12  LYS A N   
87   C CA  . LYS A 12  ? 0.74738 0.80809 0.62285 0.17927  0.11266  0.02786  12  LYS A CA  
88   C C   . LYS A 12  ? 0.69359 0.76364 0.58313 0.16656  0.09607  0.00865  12  LYS A C   
89   O O   . LYS A 12  ? 0.61483 0.70692 0.49988 0.16777  0.08520  -0.00054 12  LYS A O   
90   C CB  . LYS A 12  ? 0.78771 0.84429 0.65872 0.18928  0.11368  0.03907  12  LYS A CB  
91   C CG  . LYS A 12  ? 0.84884 0.93718 0.71327 0.19821  0.09827  0.03566  12  LYS A CG  
92   C CD  . LYS A 12  ? 0.81176 0.89924 0.67188 0.21090  0.10056  0.04783  12  LYS A CD  
93   C CE  . LYS A 12  ? 0.78609 0.91249 0.64161 0.21915  0.08515  0.04230  12  LYS A CE  
94   N NZ  . LYS A 12  ? 0.86777 1.02499 0.70634 0.23112  0.08250  0.04427  12  LYS A NZ  
95   N N   . SER A 13  ? 0.69678 0.74961 0.60238 0.15436  0.09511  0.00207  13  SER A N   
96   C CA  . SER A 13  ? 0.64998 0.70750 0.56631 0.14453  0.08082  -0.01321 13  SER A CA  
97   C C   . SER A 13  ? 0.62623 0.68860 0.54677 0.13943  0.07841  -0.02416 13  SER A C   
98   O O   . SER A 13  ? 0.58786 0.65909 0.50908 0.13682  0.06761  -0.03541 13  SER A O   
99   C CB  . SER A 13  ? 0.62286 0.66298 0.55249 0.13534  0.08055  -0.01549 13  SER A CB  
100  O OG  . SER A 13  ? 0.62196 0.65663 0.54814 0.14065  0.08396  -0.00593 13  SER A OG  
101  N N   . ASP A 14  ? 0.63725 0.69323 0.56109 0.13768  0.08966  -0.02180 14  ASP A N   
102  C CA  . ASP A 14  ? 0.63772 0.70122 0.56620 0.13465  0.08816  -0.03218 14  ASP A CA  
103  C C   . ASP A 14  ? 0.61906 0.70056 0.53395 0.14201  0.08437  -0.03484 14  ASP A C   
104  O O   . ASP A 14  ? 0.57871 0.66719 0.49607 0.13990  0.07679  -0.04734 14  ASP A O   
105  C CB  . ASP A 14  ? 0.65201 0.70953 0.58701 0.13091  0.10273  -0.02952 14  ASP A CB  
106  C CG  . ASP A 14  ? 0.64885 0.69607 0.60143 0.12058  0.10423  -0.03466 14  ASP A CG  
107  O OD1 . ASP A 14  ? 0.62622 0.66994 0.58426 0.11765  0.09342  -0.03908 14  ASP A OD1 
108  O OD2 . ASP A 14  ? 0.66915 0.71364 0.62991 0.11473  0.11681  -0.03519 14  ASP A OD2 
109  N N   . LEU A 15  ? 0.63881 0.72823 0.53831 0.15154  0.09025  -0.02342 15  LEU A N   
110  C CA  . LEU A 15  ? 0.64473 0.75630 0.53008 0.15875  0.08704  -0.02681 15  LEU A CA  
111  C C   . LEU A 15  ? 0.60342 0.72956 0.48671 0.15798  0.07260  -0.03721 15  LEU A C   
112  O O   . LEU A 15  ? 0.54662 0.68702 0.42660 0.15659  0.06698  -0.05016 15  LEU A O   
113  C CB  . LEU A 15  ? 0.68314 0.80134 0.55036 0.17134  0.09806  -0.01011 15  LEU A CB  
114  C CG  . LEU A 15  ? 0.80669 0.91976 0.67069 0.17164  0.11298  -0.00541 15  LEU A CG  
115  C CD1 . LEU A 15  ? 0.81990 0.90652 0.69496 0.16484  0.12694  0.00238  15  LEU A CD1 
116  C CD2 . LEU A 15  ? 0.79826 0.92717 0.63853 0.18591  0.12032  0.00666  15  LEU A CD2 
117  N N   . LEU A 16  ? 0.57795 0.70056 0.46391 0.15765  0.06772  -0.03330 16  LEU A N   
118  C CA  . LEU A 16  ? 0.56043 0.69555 0.44766 0.15335  0.05535  -0.04546 16  LEU A CA  
119  C C   . LEU A 16  ? 0.54016 0.66270 0.43844 0.14190  0.04997  -0.06098 16  LEU A C   
120  O O   . LEU A 16  ? 0.51370 0.64664 0.40970 0.13784  0.04386  -0.07508 16  LEU A O   
121  C CB  . LEU A 16  ? 0.54785 0.67976 0.43833 0.15411  0.05246  -0.03860 16  LEU A CB  
122  C CG  . LEU A 16  ? 0.54166 0.69179 0.43271 0.14990  0.04153  -0.05022 16  LEU A CG  
123  C CD1 . LEU A 16  ? 0.55598 0.74056 0.43444 0.15630  0.03810  -0.05653 16  LEU A CD1 
124  C CD2 . LEU A 16  ? 0.55813 0.70815 0.45217 0.15285  0.04031  -0.04181 16  LEU A CD2 
125  N N   . ARG A 17  ? 0.55030 0.65096 0.46001 0.13718  0.05317  -0.05901 17  ARG A N   
126  C CA  . ARG A 17  ? 0.54187 0.63027 0.46044 0.13021  0.04879  -0.07107 17  ARG A CA  
127  C C   . ARG A 17  ? 0.53391 0.63053 0.44854 0.13214  0.05024  -0.08104 17  ARG A C   
128  O O   . ARG A 17  ? 0.52045 0.61454 0.43475 0.12841  0.04565  -0.09403 17  ARG A O   
129  C CB  . ARG A 17  ? 0.51057 0.58195 0.44148 0.12724  0.05197  -0.06668 17  ARG A CB  
130  C CG  . ARG A 17  ? 0.52851 0.59054 0.46722 0.12471  0.04853  -0.07669 17  ARG A CG  
131  C CD  . ARG A 17  ? 0.49522 0.54750 0.44626 0.12213  0.04969  -0.07342 17  ARG A CD  
132  N NE  . ARG A 17  ? 0.49105 0.53798 0.44835 0.12346  0.04602  -0.08146 17  ARG A NE  
133  C CZ  . ARG A 17  ? 0.55364 0.60790 0.51548 0.12765  0.04948  -0.08622 17  ARG A CZ  
134  N NH1 . ARG A 17  ? 0.52220 0.58858 0.48267 0.12912  0.05729  -0.08428 17  ARG A NH1 
135  N NH2 . ARG A 17  ? 0.56194 0.61145 0.52897 0.13162  0.04577  -0.09247 17  ARG A NH2 
136  N N   . LEU A 18  ? 0.54035 0.64504 0.45146 0.13758  0.05827  -0.07551 18  LEU A N   
137  C CA  . LEU A 18  ? 0.56168 0.67572 0.46899 0.13980  0.06059  -0.08532 18  LEU A CA  
138  C C   . LEU A 18  ? 0.52251 0.65486 0.41744 0.14052  0.05603  -0.09501 18  LEU A C   
139  O O   . LEU A 18  ? 0.52068 0.65454 0.41478 0.13833  0.05475  -0.10970 18  LEU A O   
140  C CB  . LEU A 18  ? 0.57283 0.69361 0.47742 0.14483  0.07164  -0.07666 18  LEU A CB  
141  C CG  . LEU A 18  ? 0.59975 0.70860 0.51872 0.14195  0.07841  -0.07281 18  LEU A CG  
142  C CD1 . LEU A 18  ? 0.58935 0.70718 0.50404 0.14525  0.09128  -0.06741 18  LEU A CD1 
143  C CD2 . LEU A 18  ? 0.57677 0.67831 0.50851 0.13929  0.07283  -0.08521 18  LEU A CD2 
144  N N   . ASN A 19  ? 0.53888 0.68694 0.42435 0.14396  0.05406  -0.08805 19  ASN A N   
145  C CA  . ASN A 19  ? 0.52512 0.69852 0.39967 0.14420  0.04904  -0.09911 19  ASN A CA  
146  C C   . ASN A 19  ? 0.52678 0.69300 0.40780 0.13321  0.04193  -0.11557 19  ASN A C   
147  O O   . ASN A 19  ? 0.51628 0.69435 0.39286 0.12866  0.04036  -0.13274 19  ASN A O   
148  C CB  . ASN A 19  ? 0.51685 0.71274 0.38036 0.15298  0.04810  -0.08677 19  ASN A CB  
149  C CG  . ASN A 19  ? 0.54292 0.75936 0.39055 0.16468  0.05469  -0.07852 19  ASN A CG  
150  O OD1 . ASN A 19  ? 0.52891 0.74836 0.37336 0.16429  0.05880  -0.08606 19  ASN A OD1 
151  N ND2 . ASN A 19  ? 0.56003 0.79077 0.39632 0.17646  0.05652  -0.06248 19  ASN A ND2 
152  N N   . MET A 20  ? 0.49474 0.64064 0.38553 0.12801  0.03902  -0.11136 20  MET A N   
153  C CA  . MET A 20  ? 0.51187 0.64620 0.40752 0.11706  0.03474  -0.12555 20  MET A CA  
154  C C   . MET A 20  ? 0.52498 0.63691 0.42439 0.11389  0.03785  -0.13644 20  MET A C   
155  O O   . MET A 20  ? 0.55583 0.66323 0.45353 0.10616  0.03799  -0.15299 20  MET A O   
156  C CB  . MET A 20  ? 0.52835 0.64665 0.43176 0.11325  0.03177  -0.11698 20  MET A CB  
157  C CG  . MET A 20  ? 0.51987 0.66052 0.42016 0.11601  0.02853  -0.10967 20  MET A CG  
158  S SD  . MET A 20  ? 0.52636 0.64891 0.43593 0.11037  0.02576  -0.10247 20  MET A SD  
159  C CE  . MET A 20  ? 0.56244 0.68112 0.47395 0.09518  0.02280  -0.12260 20  MET A CE  
160  N N   . ILE A 21  ? 0.53449 0.63283 0.43930 0.11995  0.04145  -0.12818 21  ILE A N   
161  C CA  . ILE A 21  ? 0.55925 0.64028 0.46756 0.12087  0.04464  -0.13737 21  ILE A CA  
162  C C   . ILE A 21  ? 0.55248 0.64852 0.45271 0.12131  0.04799  -0.15172 21  ILE A C   
163  O O   . ILE A 21  ? 0.55662 0.63906 0.45602 0.11749  0.05020  -0.16664 21  ILE A O   
164  C CB  . ILE A 21  ? 0.55383 0.62772 0.47091 0.12797  0.04760  -0.12677 21  ILE A CB  
165  C CG1 . ILE A 21  ? 0.55528 0.61397 0.48060 0.12618  0.04422  -0.11639 21  ILE A CG1 
166  C CG2 . ILE A 21  ? 0.56267 0.62595 0.48305 0.13239  0.05108  -0.13634 21  ILE A CG2 
167  C CD1 . ILE A 21  ? 0.56333 0.62100 0.49887 0.13108  0.04706  -0.10841 21  ILE A CD1 
168  N N   . ALA A 22  ? 0.54824 0.67111 0.44110 0.12636  0.04967  -0.14743 22  ALA A N   
169  C CA  . ALA A 22  ? 0.56654 0.70864 0.44991 0.12669  0.05249  -0.16178 22  ALA A CA  
170  C C   . ALA A 22  ? 0.56886 0.71956 0.44734 0.11663  0.04907  -0.17911 22  ALA A C   
171  O O   . ALA A 22  ? 0.59524 0.74280 0.47124 0.11159  0.05248  -0.19809 22  ALA A O   
172  C CB  . ALA A 22  ? 0.53555 0.70640 0.40886 0.13502  0.05503  -0.15141 22  ALA A CB  
173  N N   . GLY A 23  ? 0.56854 0.73019 0.44660 0.11284  0.04339  -0.17433 23  GLY A N   
174  C CA  . GLY A 23  ? 0.56443 0.73794 0.44035 0.10114  0.04068  -0.19256 23  GLY A CA  
175  C C   . GLY A 23  ? 0.62386 0.76116 0.50657 0.09016  0.04412  -0.20509 23  GLY A C   
176  O O   . GLY A 23  ? 0.63168 0.77014 0.51198 0.07925  0.04740  -0.22672 23  GLY A O   
177  N N   . PHE A 24  ? 0.58476 0.68917 0.47505 0.09300  0.04453  -0.19198 24  PHE A N   
178  C CA  . PHE A 24  ? 0.63794 0.70399 0.53181 0.08624  0.04907  -0.20004 24  PHE A CA  
179  C C   . PHE A 24  ? 0.66698 0.71705 0.55845 0.08911  0.05669  -0.21265 24  PHE A C   
180  O O   . PHE A 24  ? 0.71975 0.74285 0.60994 0.08149  0.06330  -0.22656 24  PHE A O   
181  C CB  . PHE A 24  ? 0.61095 0.65112 0.51165 0.09170  0.04699  -0.18178 24  PHE A CB  
182  C CG  . PHE A 24  ? 0.64584 0.68489 0.54899 0.08398  0.04279  -0.17617 24  PHE A CG  
183  C CD1 . PHE A 24  ? 0.67155 0.70654 0.57288 0.06988  0.04502  -0.19075 24  PHE A CD1 
184  C CD2 . PHE A 24  ? 0.61576 0.65806 0.52363 0.08973  0.03795  -0.15776 24  PHE A CD2 
185  C CE1 . PHE A 24  ? 0.72073 0.75670 0.62512 0.06249  0.04186  -0.18620 24  PHE A CE1 
186  C CE2 . PHE A 24  ? 0.61919 0.66093 0.52944 0.08317  0.03467  -0.15317 24  PHE A CE2 
187  C CZ  . PHE A 24  ? 0.66153 0.70108 0.57013 0.06997  0.03630  -0.16698 24  PHE A CZ  
188  N N   . GLY A 25  ? 0.65279 0.71725 0.54329 0.10002  0.05750  -0.20820 25  GLY A N   
189  C CA  . GLY A 25  ? 0.70181 0.75478 0.59058 0.10418  0.06503  -0.22054 25  GLY A CA  
190  C C   . GLY A 25  ? 0.74276 0.80190 0.62441 0.09314  0.07046  -0.24575 25  GLY A C   
191  O O   . GLY A 25  ? 0.74983 0.79057 0.63004 0.09491  0.07877  -0.25872 25  GLY A O   
192  N N   . GLU A 26  ? 0.74653 0.83237 0.62431 0.08192  0.06654  -0.25429 26  GLU A N   
193  C CA  . GLU A 26  ? 0.75925 0.85794 0.63141 0.06863  0.07149  -0.28152 26  GLU A CA  
194  C C   . GLU A 26  ? 0.85298 0.91999 0.72783 0.05261  0.07783  -0.29575 26  GLU A C   
195  O O   . GLU A 26  ? 0.78745 0.86599 0.65937 0.03738  0.08284  -0.32082 26  GLU A O   
196  C CB  . GLU A 26  ? 0.69850 0.85179 0.56485 0.06592  0.06377  -0.28514 26  GLU A CB  
197  C CG  . GLU A 26  ? 0.65072 0.83276 0.51166 0.08228  0.05915  -0.26738 26  GLU A CG  
198  C CD  . GLU A 26  ? 0.72975 0.91586 0.58482 0.08831  0.06588  -0.27713 26  GLU A CD  
199  O OE1 . GLU A 26  ? 0.74838 0.92101 0.60263 0.07958  0.07346  -0.30039 26  GLU A OE1 
200  O OE2 . GLU A 26  ? 0.73035 0.93205 0.58139 0.10137  0.06505  -0.26199 26  GLU A OE2 
201  N N   . TYR A 27  ? 0.76959 0.79762 0.64932 0.05511  0.07884  -0.28118 27  TYR A N   
202  C CA  . TYR A 27  ? 0.84045 0.83226 0.72083 0.04104  0.08695  -0.29107 27  TYR A CA  
203  C C   . TYR A 27  ? 0.88774 0.82632 0.76799 0.05192  0.09425  -0.27997 27  TYR A C   
204  O O   . TYR A 27  ? 0.86757 0.80361 0.74980 0.06968  0.09083  -0.26449 27  TYR A O   
205  C CB  . TYR A 27  ? 0.85355 0.85712 0.73805 0.03235  0.07988  -0.28262 27  TYR A CB  
206  C CG  . TYR A 27  ? 0.80993 0.86982 0.69491 0.02519  0.07147  -0.29079 27  TYR A CG  
207  C CD1 . TYR A 27  ? 0.75185 0.84744 0.63696 0.03869  0.06011  -0.27257 27  TYR A CD1 
208  C CD2 . TYR A 27  ? 0.82817 0.90618 0.71322 0.00537  0.07580  -0.31688 27  TYR A CD2 
209  C CE1 . TYR A 27  ? 0.72756 0.87508 0.61108 0.03599  0.05264  -0.27781 27  TYR A CE1 
210  C CE2 . TYR A 27  ? 0.79640 0.93227 0.68195 0.00113  0.06702  -0.32453 27  TYR A CE2 
211  C CZ  . TYR A 27  ? 0.75396 0.92418 0.63788 0.01815  0.05509  -0.30369 27  TYR A CZ  
212  O OH  . TYR A 27  ? 0.74654 0.97468 0.62897 0.01761  0.04660  -0.30923 27  TYR A OH  
213  N N   . ASP A 28  ? 0.93716 0.83407 0.81473 0.04148  0.10514  -0.28790 28  ASP A N   
214  C CA  . ASP A 28  ? 0.97043 0.81539 0.84522 0.05370  0.11244  -0.27503 28  ASP A CA  
215  C C   . ASP A 28  ? 0.96239 0.80683 0.84091 0.06306  0.10191  -0.24862 28  ASP A C   
216  O O   . ASP A 28  ? 0.98538 0.80106 0.86115 0.05747  0.10570  -0.24256 28  ASP A O   
217  C CB  . ASP A 28  ? 1.04952 0.84629 0.91753 0.03975  0.12976  -0.29016 28  ASP A CB  
218  C CG  . ASP A 28  ? 1.12057 0.86117 0.98210 0.05643  0.13960  -0.27704 28  ASP A CG  
219  O OD1 . ASP A 28  ? 1.11995 0.86455 0.98401 0.07850  0.13154  -0.25800 28  ASP A OD1 
220  O OD2 . ASP A 28  ? 1.17249 0.86553 1.02605 0.04776  0.15628  -0.28602 28  ASP A OD2 
221  N N   . MET A 29  ? 0.92473 0.80059 0.80903 0.07630  0.09000  -0.23376 29  MET A N   
222  C CA  . MET A 29  ? 0.89709 0.77778 0.78612 0.08434  0.08011  -0.21101 29  MET A CA  
223  C C   . MET A 29  ? 0.87208 0.75432 0.76528 0.10452  0.07672  -0.19777 29  MET A C   
224  O O   . MET A 29  ? 0.86773 0.77191 0.76315 0.11037  0.07627  -0.20277 29  MET A O   
225  C CB  . MET A 29  ? 0.83700 0.76012 0.73059 0.07702  0.06968  -0.20709 29  MET A CB  
226  C CG  . MET A 29  ? 0.87119 0.80246 0.76309 0.05749  0.07166  -0.22110 29  MET A CG  
227  S SD  . MET A 29  ? 0.93853 0.83440 0.82912 0.04862  0.07526  -0.21377 29  MET A SD  
228  C CE  . MET A 29  ? 0.87645 0.79285 0.77360 0.05959  0.06179  -0.18849 29  MET A CE  
229  N N   . GLU A 30  ? 0.85825 0.72026 0.75249 0.11480  0.07462  -0.18184 30  GLU A N   
230  C CA  . GLU A 30  ? 0.84382 0.70787 0.74325 0.13404  0.07189  -0.17086 30  GLU A CA  
231  C C   . GLU A 30  ? 0.77967 0.66359 0.68659 0.13725  0.06136  -0.15387 30  GLU A C   
232  O O   . GLU A 30  ? 0.76930 0.64029 0.67367 0.13278  0.05906  -0.14587 30  GLU A O   
233  C CB  . GLU A 30  ? 0.88674 0.70885 0.77937 0.14636  0.08025  -0.16895 30  GLU A CB  
234  C CG  . GLU A 30  ? 0.88074 0.70687 0.77894 0.16806  0.07608  -0.15595 30  GLU A CG  
235  C CD  . GLU A 30  ? 0.94523 0.72888 0.83358 0.18233  0.08363  -0.15003 30  GLU A CD  
236  O OE1 . GLU A 30  ? 0.95396 0.70007 0.83070 0.17437  0.09475  -0.15733 30  GLU A OE1 
237  O OE2 . GLU A 30  ? 0.99023 0.77858 0.88194 0.20168  0.07928  -0.13824 30  GLU A OE2 
238  N N   . TYR A 31  ? 0.73607 0.65069 0.65199 0.14374  0.05645  -0.14939 31  TYR A N   
239  C CA  . TYR A 31  ? 0.70746 0.63973 0.63149 0.14584  0.04868  -0.13544 31  TYR A CA  
240  C C   . TYR A 31  ? 0.71804 0.63720 0.64455 0.15980  0.04709  -0.12677 31  TYR A C   
241  O O   . TYR A 31  ? 0.70359 0.62460 0.63370 0.17332  0.04930  -0.12867 31  TYR A O   
242  C CB  . TYR A 31  ? 0.69200 0.65812 0.62437 0.14704  0.04691  -0.13404 31  TYR A CB  
243  C CG  . TYR A 31  ? 0.65080 0.63323 0.59067 0.14431  0.04149  -0.12210 31  TYR A CG  
244  C CD1 . TYR A 31  ? 0.63959 0.62662 0.58851 0.15220  0.03870  -0.11492 31  TYR A CD1 
245  C CD2 . TYR A 31  ? 0.61850 0.61295 0.55645 0.13428  0.03978  -0.11901 31  TYR A CD2 
246  C CE1 . TYR A 31  ? 0.62033 0.62105 0.57643 0.14766  0.03541  -0.10659 31  TYR A CE1 
247  C CE2 . TYR A 31  ? 0.60397 0.60894 0.54821 0.13196  0.03697  -0.10869 31  TYR A CE2 
248  C CZ  . TYR A 31  ? 0.60045 0.60725 0.55389 0.13742  0.03534  -0.10331 31  TYR A CZ  
249  O OH  . TYR A 31  ? 0.53844 0.55479 0.49845 0.13315  0.03416  -0.09555 31  TYR A OH  
250  N N   . ASP A 32  ? 0.70060 0.60943 0.62484 0.15759  0.04316  -0.11750 32  ASP A N   
251  C CA  . ASP A 32  ? 0.71229 0.61312 0.63689 0.17163  0.04043  -0.10825 32  ASP A CA  
252  C C   . ASP A 32  ? 0.70568 0.61698 0.63337 0.16513  0.03358  -0.09884 32  ASP A C   
253  O O   . ASP A 32  ? 0.70296 0.59862 0.62308 0.15463  0.03412  -0.09698 32  ASP A O   
254  C CB  . ASP A 32  ? 0.78411 0.64469 0.69474 0.17889  0.04725  -0.10811 32  ASP A CB  
255  C CG  . ASP A 32  ? 0.81224 0.66554 0.71996 0.19720  0.04434  -0.09653 32  ASP A CG  
256  O OD1 . ASP A 32  ? 0.77036 0.65146 0.68730 0.20079  0.03584  -0.08990 32  ASP A OD1 
257  O OD2 . ASP A 32  ? 0.90091 0.72053 0.79622 0.20861  0.05144  -0.09439 32  ASP A OD2 
258  N N   . ASP A 33  ? 0.68869 0.62730 0.62813 0.17023  0.02820  -0.09455 33  ASP A N   
259  C CA  . ASP A 33  ? 0.69612 0.64567 0.63934 0.16423  0.02264  -0.08746 33  ASP A CA  
260  C C   . ASP A 33  ? 0.71087 0.65670 0.65087 0.17673  0.01847  -0.08040 33  ASP A C   
261  O O   . ASP A 33  ? 0.70497 0.66665 0.65005 0.17380  0.01340  -0.07629 33  ASP A O   
262  C CB  . ASP A 33  ? 0.66870 0.65039 0.62665 0.15848  0.02130  -0.08876 33  ASP A CB  
263  C CG  . ASP A 33  ? 0.68860 0.69374 0.65849 0.16967  0.02077  -0.09176 33  ASP A CG  
264  O OD1 . ASP A 33  ? 0.70342 0.70327 0.67068 0.18456  0.01974  -0.09177 33  ASP A OD1 
265  O OD2 . ASP A 33  ? 0.68586 0.71512 0.66788 0.16385  0.02245  -0.09413 33  ASP A OD2 
266  N N   . VAL A 34  ? 0.71713 0.64274 0.64787 0.19161  0.02116  -0.07897 34  VAL A N   
267  C CA  . VAL A 34  ? 0.75128 0.67056 0.67430 0.20676  0.01782  -0.07002 34  VAL A CA  
268  C C   . VAL A 34  ? 0.78379 0.66407 0.68815 0.20207  0.02232  -0.06383 34  VAL A C   
269  O O   . VAL A 34  ? 0.78793 0.66819 0.68700 0.19959  0.01857  -0.05653 34  VAL A O   
270  C CB  . VAL A 34  ? 0.75789 0.67811 0.68052 0.22981  0.01912  -0.06986 34  VAL A CB  
271  C CG1 . VAL A 34  ? 0.79931 0.71234 0.71025 0.24856  0.01585  -0.05845 34  VAL A CG1 
272  C CG2 . VAL A 34  ? 0.73807 0.70122 0.68100 0.23292  0.01530  -0.07715 34  VAL A CG2 
273  N N   . GLU A 35  ? 0.78668 0.63404 0.68112 0.19929  0.03158  -0.06806 35  GLU A N   
274  C CA  . GLU A 35  ? 0.83834 0.64649 0.71592 0.19136  0.03903  -0.06479 35  GLU A CA  
275  C C   . GLU A 35  ? 0.80917 0.60985 0.68843 0.16984  0.04455  -0.07626 35  GLU A C   
276  O O   . GLU A 35  ? 0.83809 0.60766 0.70799 0.16639  0.05502  -0.08266 35  GLU A O   
277  C CB  . GLU A 35  ? 0.89328 0.66268 0.75422 0.20917  0.04816  -0.05939 35  GLU A CB  
278  C CG  . GLU A 35  ? 0.94412 0.72387 0.80132 0.23450  0.04235  -0.04712 35  GLU A CG  
279  C CD  . GLU A 35  ? 1.03251 0.76970 0.87032 0.25535  0.05302  -0.03922 35  GLU A CD  
280  O OE1 . GLU A 35  ? 1.05618 0.74773 0.87720 0.24753  0.06520  -0.03730 35  GLU A OE1 
281  O OE2 . GLU A 35  ? 1.06658 0.81586 0.90602 0.27987  0.05033  -0.03515 35  GLU A OE2 
282  N N   . PRO A 36  ? 0.77117 0.60039 0.66180 0.15540  0.03851  -0.07966 36  PRO A N   
283  C CA  . PRO A 36  ? 0.75412 0.58244 0.64573 0.13704  0.04255  -0.09011 36  PRO A CA  
284  C C   . PRO A 36  ? 0.76286 0.56473 0.64336 0.12458  0.04848  -0.08970 36  PRO A C   
285  O O   . PRO A 36  ? 0.77071 0.56214 0.64448 0.12710  0.04732  -0.07946 36  PRO A O   
286  C CB  . PRO A 36  ? 0.70552 0.57150 0.61074 0.12989  0.03454  -0.08994 36  PRO A CB  
287  C CG  . PRO A 36  ? 0.71264 0.58871 0.62079 0.13692  0.02809  -0.07929 36  PRO A CG  
288  C CD  . PRO A 36  ? 0.74184 0.60500 0.64424 0.15522  0.02885  -0.07453 36  PRO A CD  
289  N N   . GLU A 37  ? 0.76331 0.55650 0.64187 0.11034  0.05553  -0.10217 37  GLU A N   
290  C CA  . GLU A 37  ? 0.76412 0.54010 0.63588 0.09397  0.06183  -0.10544 37  GLU A CA  
291  C C   . GLU A 37  ? 0.72636 0.53553 0.60837 0.07890  0.05599  -0.11095 37  GLU A C   
292  O O   . GLU A 37  ? 0.71979 0.52453 0.59940 0.06650  0.05841  -0.11128 37  GLU A O   
293  C CB  . GLU A 37  ? 0.81738 0.56063 0.68011 0.08607  0.07591  -0.11824 37  GLU A CB  
294  C CG  . GLU A 37  ? 0.86668 0.56879 0.71623 0.10212  0.08495  -0.11174 37  GLU A CG  
295  C CD  . GLU A 37  ? 0.93801 0.60414 0.77889 0.09276  0.10154  -0.12615 37  GLU A CD  
296  O OE1 . GLU A 37  ? 0.94765 0.62755 0.79461 0.07291  0.10443  -0.14335 37  GLU A OE1 
297  O OE2 . GLU A 37  ? 0.98662 0.61154 0.81439 0.10572  0.11229  -0.12080 37  GLU A OE2 
298  N N   . ILE A 38  ? 0.70094 0.54299 0.59345 0.08074  0.04940  -0.11485 38  ILE A N   
299  C CA  . ILE A 38  ? 0.65895 0.53462 0.56025 0.07206  0.04338  -0.11671 38  ILE A CA  
300  C C   . ILE A 38  ? 0.61921 0.51841 0.52898 0.08308  0.03524  -0.10660 38  ILE A C   
301  O O   . ILE A 38  ? 0.62849 0.53233 0.54078 0.09324  0.03445  -0.10636 38  ILE A O   
302  C CB  . ILE A 38  ? 0.70153 0.59546 0.60502 0.06280  0.04562  -0.13230 38  ILE A CB  
303  C CG1 . ILE A 38  ? 0.77091 0.64226 0.66764 0.04828  0.05567  -0.14573 38  ILE A CG1 
304  C CG2 . ILE A 38  ? 0.66356 0.59509 0.57474 0.05888  0.03888  -0.13145 38  ILE A CG2 
305  C CD1 . ILE A 38  ? 0.92508 0.80862 0.82226 0.04052  0.05995  -0.16461 38  ILE A CD1 
306  N N   . VAL A 39  ? 0.58622 0.49958 0.50076 0.08036  0.03066  -0.09931 39  VAL A N   
307  C CA  . VAL A 39  ? 0.56021 0.49373 0.48317 0.08770  0.02553  -0.09114 39  VAL A CA  
308  C C   . VAL A 39  ? 0.53563 0.49396 0.46359 0.08247  0.02398  -0.09181 39  VAL A C   
309  O O   . VAL A 39  ? 0.51554 0.47686 0.44355 0.07516  0.02358  -0.09128 39  VAL A O   
310  C CB  . VAL A 39  ? 0.55640 0.48287 0.47996 0.09129  0.02281  -0.08156 39  VAL A CB  
311  C CG1 . VAL A 39  ? 0.53289 0.48095 0.46637 0.09352  0.01982  -0.07619 39  VAL A CG1 
312  C CG2 . VAL A 39  ? 0.57408 0.48411 0.49304 0.10207  0.02316  -0.07911 39  VAL A CG2 
313  N N   . ILE A 40  ? 0.54216 0.51875 0.47342 0.08743  0.02381  -0.09250 40  ILE A N   
314  C CA  . ILE A 40  ? 0.50608 0.50667 0.43967 0.08692  0.02310  -0.09064 40  ILE A CA  
315  C C   . ILE A 40  ? 0.49845 0.50474 0.43809 0.09291  0.02353  -0.07979 40  ILE A C   
316  O O   . ILE A 40  ? 0.49303 0.49793 0.43583 0.09839  0.02501  -0.07774 40  ILE A O   
317  C CB  . ILE A 40  ? 0.51811 0.53530 0.44828 0.08883  0.02423  -0.09819 40  ILE A CB  
318  C CG1 . ILE A 40  ? 0.54865 0.55912 0.47378 0.08025  0.02564  -0.11229 40  ILE A CG1 
319  C CG2 . ILE A 40  ? 0.48504 0.52894 0.41507 0.09191  0.02347  -0.09380 40  ILE A CG2 
320  C CD1 . ILE A 40  ? 0.53544 0.56109 0.45672 0.08143  0.02720  -0.12279 40  ILE A CD1 
321  N N   . SER A 41  ? 0.45180 0.46438 0.39376 0.09125  0.02345  -0.07405 41  SER A N   
322  C CA  . SER A 41  ? 0.48631 0.50146 0.43366 0.09519  0.02649  -0.06496 41  SER A CA  
323  C C   . SER A 41  ? 0.48464 0.51674 0.42970 0.10073  0.02967  -0.05994 41  SER A C   
324  O O   . SER A 41  ? 0.47288 0.51671 0.41514 0.10031  0.02776  -0.06084 41  SER A O   
325  C CB  . SER A 41  ? 0.48154 0.48795 0.43220 0.09061  0.02576  -0.06177 41  SER A CB  
326  O OG  . SER A 41  ? 0.50568 0.51309 0.46185 0.09284  0.03056  -0.05507 41  SER A OG  
327  N N   . ILE A 42  ? 0.47602 0.51078 0.42175 0.10658  0.03517  -0.05450 42  ILE A N   
328  C CA  . ILE A 42  ? 0.48648 0.53454 0.42681 0.11471  0.04008  -0.04691 42  ILE A CA  
329  C C   . ILE A 42  ? 0.49884 0.53664 0.44322 0.11694  0.04885  -0.03678 42  ILE A C   
330  O O   . ILE A 42  ? 0.49467 0.52370 0.44411 0.11502  0.05465  -0.03607 42  ILE A O   
331  C CB  . ILE A 42  ? 0.47561 0.53385 0.41009 0.11981  0.04213  -0.04861 42  ILE A CB  
332  C CG1 . ILE A 42  ? 0.47944 0.54676 0.40989 0.11636  0.03505  -0.06103 42  ILE A CG1 
333  C CG2 . ILE A 42  ? 0.50364 0.57469 0.42962 0.13037  0.04833  -0.03797 42  ILE A CG2 
334  C CD1 . ILE A 42  ? 0.47188 0.55095 0.39597 0.12099  0.03704  -0.06488 42  ILE A CD1 
335  N N   . GLY A 43  ? 0.50356 0.54320 0.44632 0.12076  0.05097  -0.03007 43  GLY A N   
336  C CA  . GLY A 43  ? 0.52754 0.55367 0.47324 0.12290  0.06154  -0.02105 43  GLY A CA  
337  C C   . GLY A 43  ? 0.56831 0.59368 0.51518 0.12440  0.06115  -0.01785 43  GLY A C   
338  O O   . GLY A 43  ? 0.62170 0.66180 0.56229 0.13375  0.05981  -0.01303 43  GLY A O   
339  N N   . GLY A 44  ? 0.46325 0.47476 0.41822 0.11593  0.06229  -0.02116 44  GLY A N   
340  C CA  . GLY A 44  ? 0.52306 0.53318 0.48006 0.11621  0.06243  -0.01964 44  GLY A CA  
341  C C   . GLY A 44  ? 0.48359 0.49050 0.44600 0.10454  0.05444  -0.02921 44  GLY A C   
342  O O   . GLY A 44  ? 0.43901 0.44640 0.40160 0.09872  0.04764  -0.03598 44  GLY A O   
343  N N   . ASP A 45  ? 0.50294 0.50566 0.46856 0.10223  0.05609  -0.02923 45  ASP A N   
344  C CA  . ASP A 45  ? 0.47825 0.47756 0.44665 0.09178  0.04966  -0.03701 45  ASP A CA  
345  C C   . ASP A 45  ? 0.48447 0.47296 0.45719 0.08455  0.05075  -0.04143 45  ASP A C   
346  O O   . ASP A 45  ? 0.48535 0.47319 0.45704 0.07878  0.04349  -0.04697 45  ASP A O   
347  C CB  . ASP A 45  ? 0.48720 0.48649 0.45781 0.09132  0.05225  -0.03632 45  ASP A CB  
348  C CG  . ASP A 45  ? 0.48521 0.50257 0.45333 0.09599  0.04783  -0.03589 45  ASP A CG  
349  O OD1 . ASP A 45  ? 0.47130 0.49922 0.43620 0.09351  0.04056  -0.04043 45  ASP A OD1 
350  O OD2 . ASP A 45  ? 0.50229 0.52464 0.47231 0.10199  0.05227  -0.03222 45  ASP A OD2 
351  N N   . GLY A 46  ? 0.48072 0.46149 0.45801 0.08501  0.06069  -0.03936 46  GLY A N   
352  C CA  . GLY A 46  ? 0.50290 0.48064 0.48632 0.07752  0.06172  -0.04599 46  GLY A CA  
353  C C   . GLY A 46  ? 0.49081 0.47564 0.47302 0.07850  0.05460  -0.04871 46  GLY A C   
354  O O   . GLY A 46  ? 0.44655 0.43476 0.43097 0.07444  0.04860  -0.05489 46  GLY A O   
355  N N   . THR A 47  ? 0.48743 0.47585 0.46526 0.08534  0.05539  -0.04404 47  THR A N   
356  C CA  . THR A 47  ? 0.48427 0.47891 0.46021 0.08712  0.04918  -0.04727 47  THR A CA  
357  C C   . THR A 47  ? 0.44486 0.43975 0.41577 0.08562  0.03852  -0.05128 47  THR A C   
358  O O   . THR A 47  ? 0.42733 0.42196 0.39835 0.08530  0.03356  -0.05563 47  THR A O   
359  C CB  . THR A 47  ? 0.48033 0.48033 0.45069 0.09469  0.05246  -0.04205 47  THR A CB  
360  O OG1 . THR A 47  ? 0.50541 0.50029 0.47760 0.09698  0.06501  -0.03579 47  THR A OG1 
361  C CG2 . THR A 47  ? 0.49719 0.50297 0.46670 0.09626  0.04841  -0.04661 47  THR A CG2 
362  N N   . PHE A 48  ? 0.45065 0.44577 0.41692 0.08512  0.03611  -0.04985 48  PHE A N   
363  C CA  . PHE A 48  ? 0.48186 0.47375 0.44275 0.08153  0.02901  -0.05398 48  PHE A CA  
364  C C   . PHE A 48  ? 0.46524 0.44930 0.42659 0.07721  0.02653  -0.05592 48  PHE A C   
365  O O   . PHE A 48  ? 0.46139 0.43910 0.41762 0.07726  0.02202  -0.05815 48  PHE A O   
366  C CB  . PHE A 48  ? 0.47953 0.47728 0.43753 0.08004  0.02840  -0.05370 48  PHE A CB  
367  C CG  . PHE A 48  ? 0.50466 0.49796 0.45700 0.07410  0.02395  -0.05920 48  PHE A CG  
368  C CD1 . PHE A 48  ? 0.47275 0.45589 0.42277 0.06816  0.02301  -0.05993 48  PHE A CD1 
369  C CD2 . PHE A 48  ? 0.48657 0.48472 0.43500 0.07373  0.02226  -0.06425 48  PHE A CD2 
370  C CE1 . PHE A 48  ? 0.50428 0.47876 0.44750 0.06208  0.02177  -0.06412 48  PHE A CE1 
371  C CE2 . PHE A 48  ? 0.51664 0.50662 0.45984 0.06633  0.02114  -0.07058 48  PHE A CE2 
372  C CZ  . PHE A 48  ? 0.48345 0.45983 0.42370 0.06053  0.02156  -0.06978 48  PHE A CZ  
373  N N   . LEU A 49  ? 0.47423 0.45843 0.44054 0.07435  0.03023  -0.05508 49  LEU A N   
374  C CA  . LEU A 49  ? 0.46965 0.45146 0.43580 0.07049  0.02772  -0.05789 49  LEU A CA  
375  C C   . LEU A 49  ? 0.46906 0.45505 0.43711 0.07352  0.02446  -0.06080 49  LEU A C   
376  O O   . LEU A 49  ? 0.48110 0.46558 0.44350 0.07489  0.01905  -0.06168 49  LEU A O   
377  C CB  . LEU A 49  ? 0.48603 0.46922 0.45867 0.06617  0.03395  -0.05899 49  LEU A CB  
378  C CG  . LEU A 49  ? 0.48361 0.46378 0.45367 0.06203  0.03513  -0.05873 49  LEU A CG  
379  C CD1 . LEU A 49  ? 0.47852 0.45504 0.43902 0.06081  0.02919  -0.05775 49  LEU A CD1 
380  C CD2 . LEU A 49  ? 0.47530 0.45488 0.44954 0.06418  0.04292  -0.05531 49  LEU A CD2 
381  N N   . SER A 50  ? 0.49252 0.48492 0.46793 0.07569  0.02829  -0.06187 50  SER A N   
382  C CA  . SER A 50  ? 0.48714 0.48842 0.46654 0.07911  0.02542  -0.06585 50  SER A CA  
383  C C   . SER A 50  ? 0.48368 0.47951 0.45476 0.08623  0.01944  -0.06452 50  SER A C   
384  O O   . SER A 50  ? 0.49475 0.49420 0.46414 0.09158  0.01456  -0.06615 50  SER A O   
385  C CB  . SER A 50  ? 0.48032 0.48959 0.46998 0.07821  0.03304  -0.06792 50  SER A CB  
386  O OG  . SER A 50  ? 0.50030 0.51268 0.49843 0.07060  0.04038  -0.07150 50  SER A OG  
387  N N   . ALA A 51  ? 0.47905 0.46708 0.44460 0.08702  0.02034  -0.06218 51  ALA A N   
388  C CA  . ALA A 51  ? 0.48542 0.46456 0.44269 0.09171  0.01692  -0.06289 51  ALA A CA  
389  C C   . ALA A 51  ? 0.51182 0.47773 0.45925 0.09156  0.01344  -0.06132 51  ALA A C   
390  O O   . ALA A 51  ? 0.50248 0.46037 0.44368 0.09844  0.01115  -0.06100 51  ALA A O   
391  C CB  . ALA A 51  ? 0.48648 0.46377 0.44020 0.08999  0.01909  -0.06341 51  ALA A CB  
392  N N   . PHE A 52  ? 0.44871 0.41106 0.39357 0.08477  0.01415  -0.05963 52  PHE A N   
393  C CA  . PHE A 52  ? 0.52791 0.47714 0.46195 0.08376  0.01251  -0.05722 52  PHE A CA  
394  C C   . PHE A 52  ? 0.51363 0.46773 0.44584 0.09088  0.00860  -0.05565 52  PHE A C   
395  O O   . PHE A 52  ? 0.55300 0.49480 0.47386 0.09788  0.00698  -0.05225 52  PHE A O   
396  C CB  . PHE A 52  ? 0.49696 0.44657 0.43087 0.07496  0.01460  -0.05660 52  PHE A CB  
397  C CG  . PHE A 52  ? 0.52105 0.46106 0.44449 0.07338  0.01380  -0.05369 52  PHE A CG  
398  C CD1 . PHE A 52  ? 0.54017 0.46067 0.45082 0.07175  0.01596  -0.05172 52  PHE A CD1 
399  C CD2 . PHE A 52  ? 0.48710 0.43712 0.41263 0.07273  0.01232  -0.05354 52  PHE A CD2 
400  C CE1 . PHE A 52  ? 0.54072 0.45049 0.43922 0.07087  0.01682  -0.04740 52  PHE A CE1 
401  C CE2 . PHE A 52  ? 0.51494 0.45817 0.42875 0.07207  0.01166  -0.05041 52  PHE A CE2 
402  C CZ  . PHE A 52  ? 0.53042 0.45282 0.42990 0.07182  0.01400  -0.04620 52  PHE A CZ  
403  N N   . HIS A 53  ? 0.50098 0.47384 0.44394 0.08968  0.00789  -0.05854 53  HIS A N   
404  C CA  . HIS A 53  ? 0.52655 0.51254 0.46934 0.09561  0.00338  -0.05956 53  HIS A CA  
405  C C   . HIS A 53  ? 0.56050 0.55401 0.50567 0.10694  0.00046  -0.06056 53  HIS A C   
406  O O   . HIS A 53  ? 0.55715 0.55846 0.49708 0.11688  -0.00444 -0.05915 53  HIS A O   
407  C CB  . HIS A 53  ? 0.51234 0.51770 0.46742 0.08805  0.00511  -0.06573 53  HIS A CB  
408  C CG  . HIS A 53  ? 0.51140 0.51151 0.46229 0.07982  0.00712  -0.06513 53  HIS A CG  
409  N ND1 . HIS A 53  ? 0.51730 0.51655 0.45639 0.08166  0.00342  -0.06279 53  HIS A ND1 
410  C CD2 . HIS A 53  ? 0.49464 0.49017 0.45056 0.07116  0.01301  -0.06600 53  HIS A CD2 
411  C CE1 . HIS A 53  ? 0.51915 0.51431 0.45727 0.07286  0.00701  -0.06350 53  HIS A CE1 
412  N NE2 . HIS A 53  ? 0.49345 0.48630 0.44223 0.06693  0.01276  -0.06552 53  HIS A NE2 
413  N N   . GLN A 54  ? 0.52718 0.52044 0.47946 0.10704  0.00347  -0.06274 54  GLN A N   
414  C CA  . GLN A 54  ? 0.56979 0.56900 0.52408 0.11827  0.00157  -0.06411 54  GLN A CA  
415  C C   . GLN A 54  ? 0.59201 0.56997 0.53030 0.12896  -0.00018 -0.05837 54  GLN A C   
416  O O   . GLN A 54  ? 0.60986 0.59408 0.54613 0.14263  -0.00341 -0.05735 54  GLN A O   
417  C CB  . GLN A 54  ? 0.58428 0.58479 0.54656 0.11557  0.00630  -0.06725 54  GLN A CB  
418  C CG  . GLN A 54  ? 0.62128 0.63021 0.58765 0.12626  0.00564  -0.07015 54  GLN A CG  
419  C CD  . GLN A 54  ? 0.70970 0.72273 0.68331 0.12250  0.01118  -0.07338 54  GLN A CD  
420  O OE1 . GLN A 54  ? 0.77618 0.79283 0.75500 0.11311  0.01564  -0.07342 54  GLN A OE1 
421  N NE2 . GLN A 54  ? 0.72268 0.73429 0.69524 0.13105  0.01179  -0.07553 54  GLN A NE2 
422  N N   . TYR A 55  ? 0.60393 0.55683 0.53065 0.12327  0.00299  -0.05477 55  TYR A N   
423  C CA  . TYR A 55  ? 0.63941 0.56483 0.55018 0.13068  0.00531  -0.05008 55  TYR A CA  
424  C C   . TYR A 55  ? 0.65836 0.56644 0.55427 0.12799  0.00646  -0.04354 55  TYR A C   
425  O O   . TYR A 55  ? 0.67328 0.55226 0.55563 0.12704  0.01222  -0.04047 55  TYR A O   
426  C CB  . TYR A 55  ? 0.63892 0.54826 0.54892 0.12469  0.01093  -0.05443 55  TYR A CB  
427  C CG  . TYR A 55  ? 0.65168 0.57488 0.57238 0.12952  0.01086  -0.06002 55  TYR A CG  
428  C CD1 . TYR A 55  ? 0.67180 0.58908 0.58930 0.14356  0.01132  -0.06000 55  TYR A CD1 
429  C CD2 . TYR A 55  ? 0.62929 0.57078 0.56217 0.12130  0.01141  -0.06456 55  TYR A CD2 
430  C CE1 . TYR A 55  ? 0.66820 0.59957 0.59567 0.14772  0.01196  -0.06579 55  TYR A CE1 
431  C CE2 . TYR A 55  ? 0.64796 0.60184 0.58900 0.12548  0.01259  -0.06907 55  TYR A CE2 
432  C CZ  . TYR A 55  ? 0.66388 0.61372 0.60284 0.13788  0.01267  -0.07038 55  TYR A CZ  
433  O OH  . TYR A 55  ? 0.67026 0.63379 0.61756 0.14171  0.01451  -0.07556 55  TYR A OH  
434  N N   . GLU A 56  ? 0.64016 0.56529 0.53797 0.12593  0.00237  -0.04221 56  GLU A N   
435  C CA  . GLU A 56  ? 0.67500 0.58552 0.55835 0.12217  0.00418  -0.03628 56  GLU A CA  
436  C C   . GLU A 56  ? 0.71007 0.60144 0.57335 0.13721  0.00500  -0.02657 56  GLU A C   
437  O O   . GLU A 56  ? 0.74440 0.61852 0.59212 0.13488  0.00854  -0.02006 56  GLU A O   
438  C CB  . GLU A 56  ? 0.63511 0.56981 0.52515 0.11592  0.00025  -0.03875 56  GLU A CB  
439  C CG  . GLU A 56  ? 0.64170 0.60763 0.54053 0.12449  -0.00653 -0.04225 56  GLU A CG  
440  C CD  . GLU A 56  ? 0.69554 0.68154 0.59671 0.11768  -0.00897 -0.04567 56  GLU A CD  
441  O OE1 . GLU A 56  ? 0.75019 0.73400 0.63566 0.12335  -0.01100 -0.03981 56  GLU A OE1 
442  O OE2 . GLU A 56  ? 0.63057 0.63282 0.54797 0.10678  -0.00762 -0.05415 56  GLU A OE2 
443  N N   . GLU A 57  ? 0.73698 0.63012 0.59923 0.15351  0.00290  -0.02469 57  GLU A N   
444  C CA  . GLU A 57  ? 0.80814 0.67891 0.64940 0.17141  0.00534  -0.01361 57  GLU A CA  
445  C C   . GLU A 57  ? 0.81551 0.64438 0.64599 0.17174  0.01607  -0.01161 57  GLU A C   
446  O O   . GLU A 57  ? 0.83145 0.63265 0.64228 0.18668  0.02152  -0.00141 57  GLU A O   
447  C CB  . GLU A 57  ? 0.84316 0.74174 0.68849 0.19225  -0.00267 -0.01238 57  GLU A CB  
448  C CG  . GLU A 57  ? 0.88980 0.82743 0.73926 0.19446  -0.01199 -0.01358 57  GLU A CG  
449  C CD  . GLU A 57  ? 0.96583 0.94102 0.82443 0.21243  -0.02045 -0.01644 57  GLU A CD  
450  O OE1 . GLU A 57  ? 0.99910 0.98447 0.87366 0.21354  -0.02058 -0.02378 57  GLU A OE1 
451  O OE2 . GLU A 57  ? 1.02219 1.01973 0.87198 0.22569  -0.02692 -0.01193 57  GLU A OE2 
452  N N   . ARG A 58  ? 0.79118 0.61468 0.63299 0.15607  0.02014  -0.02134 58  ARG A N   
453  C CA  . ARG A 58  ? 0.82186 0.60890 0.65543 0.15206  0.03119  -0.02366 58  ARG A CA  
454  C C   . ARG A 58  ? 0.79738 0.57785 0.63500 0.12867  0.03653  -0.03137 58  ARG A C   
455  O O   . ARG A 58  ? 0.78415 0.55605 0.62680 0.11929  0.04193  -0.04083 58  ARG A O   
456  C CB  . ARG A 58  ? 0.84147 0.63403 0.68539 0.15927  0.03084  -0.03082 58  ARG A CB  
457  C CG  . ARG A 58  ? 0.87879 0.68689 0.72345 0.18265  0.02469  -0.02557 58  ARG A CG  
458  C CD  . ARG A 58  ? 0.96665 0.77096 0.81773 0.19042  0.02781  -0.03229 58  ARG A CD  
459  N NE  . ARG A 58  ? 0.94881 0.70659 0.78291 0.19470  0.04059  -0.03028 58  ARG A NE  
460  C CZ  . ARG A 58  ? 0.95327 0.68981 0.78774 0.17936  0.04971  -0.04035 58  ARG A CZ  
461  N NH1 . ARG A 58  ? 0.87597 0.63565 0.72587 0.16121  0.04632  -0.05168 58  ARG A NH1 
462  N NH2 . ARG A 58  ? 1.04100 0.73240 0.85933 0.18276  0.06340  -0.03939 58  ARG A NH2 
463  N N   . LEU A 59  ? 0.78295 0.57064 0.61872 0.11931  0.03504  -0.02848 59  LEU A N   
464  C CA  . LEU A 59  ? 0.76583 0.55575 0.60832 0.09852  0.03879  -0.03640 59  LEU A CA  
465  C C   . LEU A 59  ? 0.80690 0.56127 0.63798 0.08827  0.05209  -0.03984 59  LEU A C   
466  O O   . LEU A 59  ? 0.80235 0.56246 0.64260 0.07232  0.05539  -0.05112 59  LEU A O   
467  C CB  . LEU A 59  ? 0.74141 0.54518 0.58344 0.09220  0.03557  -0.03252 59  LEU A CB  
468  C CG  . LEU A 59  ? 0.70165 0.54264 0.55942 0.09494  0.02488  -0.03433 59  LEU A CG  
469  C CD1 . LEU A 59  ? 0.66034 0.51123 0.51658 0.08749  0.02382  -0.03221 59  LEU A CD1 
470  C CD2 . LEU A 59  ? 0.64510 0.50491 0.52127 0.08792  0.02286  -0.04387 59  LEU A CD2 
471  N N   . ASP A 60  ? 0.84525 0.56360 0.65613 0.09720  0.06078  -0.03081 60  ASP A N   
472  C CA  . ASP A 60  ? 0.91274 0.59202 0.71184 0.08550  0.07680  -0.03484 60  ASP A CA  
473  C C   . ASP A 60  ? 0.90927 0.57598 0.71293 0.08478  0.08245  -0.04572 60  ASP A C   
474  O O   . ASP A 60  ? 0.94967 0.58954 0.74829 0.07021  0.09623  -0.05466 60  ASP A O   
475  C CB  . ASP A 60  ? 1.00272 0.64191 0.77562 0.09631  0.08707  -0.01964 60  ASP A CB  
476  C CG  . ASP A 60  ? 1.17323 0.78888 0.93555 0.07722  0.10050  -0.02032 60  ASP A CG  
477  O OD1 . ASP A 60  ? 1.06004 0.70192 0.83055 0.06566  0.09490  -0.02245 60  ASP A OD1 
478  O OD2 . ASP A 60  ? 1.29776 0.86773 1.04370 0.07347  0.11804  -0.01922 60  ASP A OD2 
479  N N   . GLU A 61  ? 0.87240 0.55894 0.68590 0.09868  0.07317  -0.04678 61  GLU A N   
480  C CA  . GLU A 61  ? 0.86596 0.54319 0.68357 0.09952  0.07813  -0.05743 61  GLU A CA  
481  C C   . GLU A 61  ? 0.81353 0.52977 0.65189 0.08927  0.06984  -0.07100 61  GLU A C   
482  O O   . GLU A 61  ? 0.80368 0.51911 0.64646 0.09001  0.07249  -0.08089 61  GLU A O   
483  C CB  . GLU A 61  ? 0.89513 0.56368 0.70678 0.12503  0.07600  -0.04868 61  GLU A CB  
484  C CG  . GLU A 61  ? 0.95881 0.58180 0.74634 0.13947  0.08737  -0.03514 61  GLU A CG  
485  C CD  . GLU A 61  ? 0.96845 0.60372 0.74754 0.15593  0.07856  -0.01815 61  GLU A CD  
486  O OE1 . GLU A 61  ? 0.92873 0.60538 0.72151 0.15183  0.06506  -0.01893 61  GLU A OE1 
487  O OE2 . GLU A 61  ? 1.03869 0.64227 0.79657 0.17362  0.08587  -0.00420 61  GLU A OE2 
488  N N   . ILE A 62  ? 0.78207 0.53139 0.63190 0.08087  0.06086  -0.07132 62  ILE A N   
489  C CA  . ILE A 62  ? 0.73559 0.52303 0.60291 0.07665  0.05235  -0.07953 62  ILE A CA  
490  C C   . ILE A 62  ? 0.70782 0.51206 0.58196 0.05808  0.05302  -0.08757 62  ILE A C   
491  O O   . ILE A 62  ? 0.68408 0.48546 0.55491 0.05152  0.05410  -0.08290 62  ILE A O   
492  C CB  . ILE A 62  ? 0.69972 0.51498 0.57597 0.08904  0.04068  -0.07095 62  ILE A CB  
493  C CG1 . ILE A 62  ? 0.71457 0.52297 0.58780 0.10772  0.03922  -0.06617 62  ILE A CG1 
494  C CG2 . ILE A 62  ? 0.64653 0.49696 0.53847 0.08348  0.03446  -0.07689 62  ILE A CG2 
495  C CD1 . ILE A 62  ? 0.69505 0.53400 0.57914 0.11773  0.02913  -0.06115 62  ILE A CD1 
496  N N   . ALA A 63  ? 0.66781 0.49232 0.55113 0.05060  0.05236  -0.09992 63  ALA A N   
497  C CA  . ALA A 63  ? 0.64422 0.49764 0.53700 0.03769  0.04988  -0.10717 63  ALA A CA  
498  C C   . ALA A 63  ? 0.61207 0.50051 0.51633 0.04592  0.03995  -0.10424 63  ALA A C   
499  O O   . ALA A 63  ? 0.62318 0.51880 0.52975 0.05316  0.03819  -0.10703 63  ALA A O   
500  C CB  . ALA A 63  ? 0.68228 0.53633 0.57548 0.02249  0.05756  -0.12472 63  ALA A CB  
501  N N   . PHE A 64  ? 0.58854 0.49642 0.49912 0.04500  0.03510  -0.09845 64  PHE A N   
502  C CA  . PHE A 64  ? 0.57135 0.50643 0.49116 0.05303  0.02846  -0.09359 64  PHE A CA  
503  C C   . PHE A 64  ? 0.55638 0.52107 0.48232 0.04811  0.02728  -0.10111 64  PHE A C   
504  O O   . PHE A 64  ? 0.54859 0.52003 0.47508 0.03712  0.02975  -0.10894 64  PHE A O   
505  C CB  . PHE A 64  ? 0.53186 0.46944 0.45458 0.05618  0.02543  -0.08317 64  PHE A CB  
506  C CG  . PHE A 64  ? 0.54694 0.46712 0.46513 0.06429  0.02424  -0.07550 64  PHE A CG  
507  C CD1 . PHE A 64  ? 0.56256 0.45883 0.47025 0.06247  0.02729  -0.07258 64  PHE A CD1 
508  C CD2 . PHE A 64  ? 0.52748 0.45756 0.45156 0.07402  0.02067  -0.07127 64  PHE A CD2 
509  C CE1 . PHE A 64  ? 0.58633 0.47198 0.48869 0.07264  0.02519  -0.06497 64  PHE A CE1 
510  C CE2 . PHE A 64  ? 0.52840 0.45020 0.44985 0.08188  0.01867  -0.06604 64  PHE A CE2 
511  C CZ  . PHE A 64  ? 0.57331 0.47451 0.48353 0.08239  0.02011  -0.06256 64  PHE A CZ  
512  N N   . ILE A 65  ? 0.52657 0.51102 0.45675 0.05689  0.02400  -0.09867 65  ILE A N   
513  C CA  . ILE A 65  ? 0.53004 0.54652 0.46425 0.05751  0.02201  -0.10197 65  ILE A CA  
514  C C   . ILE A 65  ? 0.51095 0.53881 0.44884 0.06941  0.02016  -0.08998 65  ILE A C   
515  O O   . ILE A 65  ? 0.52861 0.54801 0.46623 0.07625  0.02066  -0.08527 65  ILE A O   
516  C CB  . ILE A 65  ? 0.56027 0.58979 0.49174 0.05548  0.02271  -0.11429 65  ILE A CB  
517  C CG1 . ILE A 65  ? 0.61283 0.62401 0.54030 0.04228  0.02774  -0.12774 65  ILE A CG1 
518  C CG2 . ILE A 65  ? 0.58392 0.65220 0.51808 0.05741  0.01976  -0.11768 65  ILE A CG2 
519  C CD1 . ILE A 65  ? 0.71003 0.73167 0.63498 0.03879  0.02974  -0.14232 65  ILE A CD1 
520  N N   . GLY A 66  ? 0.47655 0.52346 0.41799 0.07206  0.01940  -0.08553 66  GLY A N   
521  C CA  . GLY A 66  ? 0.49205 0.54559 0.43568 0.08315  0.02070  -0.07378 66  GLY A CA  
522  C C   . GLY A 66  ? 0.54070 0.62294 0.48194 0.09175  0.02030  -0.07266 66  GLY A C   
523  O O   . GLY A 66  ? 0.50741 0.61262 0.44902 0.08979  0.01783  -0.07888 66  GLY A O   
524  N N   . ILE A 67  ? 0.50621 0.58898 0.44466 0.10157  0.02324  -0.06481 67  ILE A N   
525  C CA  . ILE A 67  ? 0.52182 0.62926 0.45481 0.11348  0.02436  -0.05937 67  ILE A CA  
526  C C   . ILE A 67  ? 0.52223 0.62019 0.45558 0.12354  0.03130  -0.04385 67  ILE A C   
527  O O   . ILE A 67  ? 0.51630 0.59252 0.45211 0.12231  0.03636  -0.03922 67  ILE A O   
528  C CB  . ILE A 67  ? 0.49442 0.60901 0.42095 0.11645  0.02454  -0.06338 67  ILE A CB  
529  C CG1 . ILE A 67  ? 0.48841 0.61094 0.41430 0.10582  0.01971  -0.08073 67  ILE A CG1 
530  C CG2 . ILE A 67  ? 0.52841 0.66692 0.44635 0.13123  0.02695  -0.05438 67  ILE A CG2 
531  C CD1 . ILE A 67  ? 0.54863 0.67369 0.46895 0.10720  0.02065  -0.08693 67  ILE A CD1 
532  N N   . HIS A 68  ? 0.52308 0.63760 0.45442 0.13347  0.03256  -0.03665 68  HIS A N   
533  C CA  . HIS A 68  ? 0.59789 0.69902 0.52854 0.14366  0.04176  -0.02176 68  HIS A CA  
534  C C   . HIS A 68  ? 0.63692 0.74857 0.55625 0.15948  0.04755  -0.01053 68  HIS A C   
535  O O   . HIS A 68  ? 0.63775 0.77927 0.54989 0.17047  0.04386  -0.00905 68  HIS A O   
536  C CB  . HIS A 68  ? 0.63912 0.74639 0.57406 0.14699  0.04180  -0.01894 68  HIS A CB  
537  C CG  . HIS A 68  ? 0.65576 0.80009 0.58672 0.15755  0.03668  -0.01956 68  HIS A CG  
538  N ND1 . HIS A 68  ? 0.68987 0.84838 0.61190 0.17785  0.04162  -0.00591 68  HIS A ND1 
539  C CD2 . HIS A 68  ? 0.65387 0.82627 0.58858 0.15089  0.02769  -0.03275 68  HIS A CD2 
540  C CE1 . HIS A 68  ? 0.67392 0.87230 0.59474 0.18469  0.03414  -0.01082 68  HIS A CE1 
541  N NE2 . HIS A 68  ? 0.65490 0.86320 0.58447 0.16704  0.02583  -0.02837 68  HIS A NE2 
542  N N   . THR A 69  ? 0.63288 0.72227 0.55025 0.16050  0.05704  -0.00316 69  THR A N   
543  C CA  . THR A 69  ? 0.67703 0.77019 0.58182 0.17537  0.06586  0.00985  69  THR A CA  
544  C C   . THR A 69  ? 0.71115 0.79023 0.61138 0.18878  0.07839  0.02662  69  THR A C   
545  O O   . THR A 69  ? 0.73027 0.81309 0.61676 0.20507  0.08675  0.04053  69  THR A O   
546  C CB  . THR A 69  ? 0.65973 0.73701 0.56439 0.16911  0.07200  0.00871  69  THR A CB  
547  O OG1 . THR A 69  ? 0.66530 0.71579 0.58235 0.15643  0.07655  0.00520  69  THR A OG1 
548  C CG2 . THR A 69  ? 0.63111 0.72590 0.53553 0.16222  0.06142  -0.00536 69  THR A CG2 
549  N N   . GLY A 70  ? 0.74272 0.80470 0.65269 0.18318  0.08090  0.02592  70  GLY A N   
550  C CA  . GLY A 70  ? 0.76601 0.81666 0.67261 0.19654  0.09178  0.03948  70  GLY A CA  
551  C C   . GLY A 70  ? 0.79196 0.86886 0.70073 0.20356  0.08215  0.03706  70  GLY A C   
552  O O   . GLY A 70  ? 0.75536 0.86685 0.66207 0.20537  0.06958  0.02980  70  GLY A O   
553  N N   . HIS A 71  ? 0.84987 0.91195 0.76377 0.20657  0.08886  0.04144  71  HIS A N   
554  C CA  A HIS A 71  ? 0.85635 0.94352 0.77490 0.21208  0.08079  0.03797  71  HIS A CA  
555  C CA  B HIS A 71  ? 0.85608 0.94409 0.77438 0.21233  0.08058  0.03800  71  HIS A CA  
556  C C   . HIS A 71  ? 0.84023 0.94280 0.76987 0.19194  0.06601  0.01881  71  HIS A C   
557  O O   . HIS A 71  ? 0.82293 0.90930 0.75728 0.17474  0.06350  0.00982  71  HIS A O   
558  C CB  A HIS A 71  ? 0.85368 0.91697 0.77673 0.21697  0.09241  0.04467  71  HIS A CB  
559  C CB  B HIS A 71  ? 0.85350 0.91912 0.77564 0.21877  0.09225  0.04552  71  HIS A CB  
560  C CG  A HIS A 71  ? 0.85833 0.89179 0.79292 0.19569  0.09556  0.03467  71  HIS A CG  
561  C CG  B HIS A 71  ? 0.88515 0.92800 0.79512 0.23857  0.11022  0.06509  71  HIS A CG  
562  N ND1 A HIS A 71  ? 0.81719 0.85920 0.76262 0.18006  0.08500  0.02038  71  HIS A ND1 
563  N ND1 B HIS A 71  ? 0.90574 0.96985 0.80207 0.26505  0.11222  0.07994  71  HIS A ND1 
564  C CD2 A HIS A 71  ? 0.86385 0.86174 0.80035 0.18734  0.10844  0.03619  71  HIS A CD2 
565  C CD2 B HIS A 71  ? 0.91760 0.91762 0.82611 0.23580  0.12844  0.07216  71  HIS A CD2 
566  C CE1 A HIS A 71  ? 0.79340 0.80800 0.74560 0.16493  0.09009  0.01455  71  HIS A CE1 
567  C CE1 B HIS A 71  ? 0.93025 0.96120 0.81544 0.27906  0.13183  0.09747  71  HIS A CE1 
568  N NE2 A HIS A 71  ? 0.82947 0.81893 0.77767 0.16826  0.10392  0.02266  71  HIS A NE2 
569  N NE2 B HIS A 71  ? 0.94082 0.93155 0.83393 0.26023  0.14271  0.09217  71  HIS A NE2 
570  N N   . LEU A 72  ? 0.75752 0.89193 0.69110 0.19485  0.05727  0.01274  72  LEU A N   
571  C CA  . LEU A 72  ? 0.71553 0.86272 0.65845 0.17554  0.04597  -0.00503 72  LEU A CA  
572  C C   . LEU A 72  ? 0.71335 0.82760 0.66453 0.15887  0.04900  -0.01000 72  LEU A C   
573  O O   . LEU A 72  ? 0.69502 0.79205 0.64936 0.16255  0.05711  -0.00400 72  LEU A O   
574  C CB  . LEU A 72  ? 0.69767 0.88417 0.64540 0.18071  0.03922  -0.01094 72  LEU A CB  
575  C CG  . LEU A 72  ? 0.67578 0.87265 0.63367 0.15968  0.03113  -0.02908 72  LEU A CG  
576  C CD1 . LEU A 72  ? 0.65103 0.85358 0.60674 0.14560  0.02418  -0.04166 72  LEU A CD1 
577  C CD2 . LEU A 72  ? 0.61116 0.84879 0.57571 0.16554  0.02701  -0.03457 72  LEU A CD2 
578  N N   . GLY A 73  ? 0.65901 0.76457 0.61263 0.14168  0.04314  -0.02092 73  GLY A N   
579  C CA  . GLY A 73  ? 0.60056 0.68121 0.56022 0.12686  0.04403  -0.02631 73  GLY A CA  
580  C C   . GLY A 73  ? 0.61328 0.70629 0.57749 0.11444  0.03678  -0.03820 73  GLY A C   
581  O O   . GLY A 73  ? 0.58579 0.70397 0.54936 0.11289  0.03067  -0.04554 73  GLY A O   
582  N N   . PHE A 74  ? 0.48505 0.56153 0.45345 0.10466  0.03840  -0.04114 74  PHE A N   
583  C CA  . PHE A 74  ? 0.50878 0.59354 0.47994 0.09205  0.03381  -0.05145 74  PHE A CA  
584  C C   . PHE A 74  ? 0.49222 0.56665 0.45939 0.07958  0.02923  -0.05928 74  PHE A C   
585  O O   . PHE A 74  ? 0.51693 0.60060 0.48446 0.06943  0.02658  -0.06874 74  PHE A O   
586  C CB  . PHE A 74  ? 0.45843 0.52957 0.43319 0.08664  0.03785  -0.05134 74  PHE A CB  
587  C CG  . PHE A 74  ? 0.46637 0.55881 0.44678 0.09191  0.03979  -0.05189 74  PHE A CG  
588  C CD1 . PHE A 74  ? 0.46332 0.55970 0.44559 0.10800  0.04576  -0.04276 74  PHE A CD1 
589  C CD2 . PHE A 74  ? 0.46668 0.57550 0.45048 0.08143  0.03693  -0.06159 74  PHE A CD2 
590  C CE1 . PHE A 74  ? 0.46847 0.58657 0.45634 0.11554  0.04764  -0.04296 74  PHE A CE1 
591  C CE2 . PHE A 74  ? 0.45652 0.58978 0.44728 0.08661  0.03869  -0.06327 74  PHE A CE2 
592  C CZ  . PHE A 74  ? 0.52959 0.66887 0.52264 0.10483  0.04339  -0.05379 74  PHE A CZ  
593  N N   . TYR A 75  ? 0.43616 0.49101 0.39981 0.08007  0.02960  -0.05601 75  TYR A N   
594  C CA  . TYR A 75  ? 0.46690 0.51145 0.42601 0.07218  0.02606  -0.06216 75  TYR A CA  
595  C C   . TYR A 75  ? 0.53494 0.59137 0.49122 0.07791  0.02413  -0.06350 75  TYR A C   
596  O O   . TYR A 75  ? 0.51570 0.57757 0.46941 0.07145  0.02147  -0.07259 75  TYR A O   
597  C CB  . TYR A 75  ? 0.48427 0.50414 0.44173 0.06978  0.02691  -0.05921 75  TYR A CB  
598  C CG  . TYR A 75  ? 0.45972 0.46989 0.41788 0.06369  0.02839  -0.05906 75  TYR A CG  
599  C CD1 . TYR A 75  ? 0.44457 0.45339 0.39973 0.05431  0.02763  -0.06437 75  TYR A CD1 
600  C CD2 . TYR A 75  ? 0.47022 0.47284 0.43167 0.06617  0.03188  -0.05470 75  TYR A CD2 
601  C CE1 . TYR A 75  ? 0.44813 0.44899 0.40223 0.04898  0.02957  -0.06385 75  TYR A CE1 
602  C CE2 . TYR A 75  ? 0.42627 0.42249 0.38751 0.06040  0.03325  -0.05586 75  TYR A CE2 
603  C CZ  . TYR A 75  ? 0.42783 0.42362 0.38474 0.05257  0.03170  -0.05968 75  TYR A CZ  
604  O OH  . TYR A 75  ? 0.41804 0.40830 0.37311 0.04716  0.03364  -0.06040 75  TYR A OH  
605  N N   . ALA A 76  ? 0.52334 0.58261 0.47929 0.08933  0.02690  -0.05508 76  ALA A N   
606  C CA  . ALA A 76  ? 0.56983 0.64366 0.52147 0.09676  0.02594  -0.05482 76  ALA A CA  
607  C C   . ALA A 76  ? 0.55587 0.66111 0.50719 0.10416  0.02437  -0.05507 76  ALA A C   
608  O O   . ALA A 76  ? 0.54023 0.65377 0.49029 0.11759  0.02818  -0.04465 76  ALA A O   
609  C CB  . ALA A 76  ? 0.55753 0.61999 0.50765 0.10549  0.03152  -0.04494 76  ALA A CB  
610  N N   . ASP A 77  ? 0.54893 0.67258 0.50126 0.09564  0.01960  -0.06754 77  ASP A N   
611  C CA  . ASP A 77  ? 0.62260 0.78309 0.57729 0.10045  0.01698  -0.07129 77  ASP A CA  
612  C C   . ASP A 77  ? 0.62649 0.81799 0.57663 0.10374  0.01287  -0.07919 77  ASP A C   
613  O O   . ASP A 77  ? 0.69774 0.92636 0.65089 0.10391  0.00920  -0.08789 77  ASP A O   
614  C CB  . ASP A 77  ? 0.59135 0.75604 0.55294 0.08618  0.01602  -0.08206 77  ASP A CB  
615  C CG  . ASP A 77  ? 0.61588 0.76005 0.57595 0.06835  0.01606  -0.09387 77  ASP A CG  
616  O OD1 . ASP A 77  ? 0.68234 0.80862 0.63693 0.06843  0.01616  -0.09334 77  ASP A OD1 
617  O OD2 . ASP A 77  ? 0.63604 0.78095 0.59990 0.05485  0.01723  -0.10337 77  ASP A OD2 
618  N N   . TRP A 78  ? 0.62268 0.80332 0.56611 0.10632  0.01350  -0.07751 78  TRP A N   
619  C CA  . TRP A 78  ? 0.62966 0.83902 0.56698 0.11040  0.01029  -0.08466 78  TRP A CA  
620  C C   . TRP A 78  ? 0.60875 0.82371 0.53722 0.13010  0.01314  -0.06861 78  TRP A C   
621  O O   . TRP A 78  ? 0.57938 0.76386 0.50630 0.13444  0.01897  -0.05613 78  TRP A O   
622  C CB  . TRP A 78  ? 0.65677 0.84875 0.59203 0.09734  0.01027  -0.09707 78  TRP A CB  
623  C CG  . TRP A 78  ? 0.70814 0.90394 0.64820 0.07886  0.00906  -0.11622 78  TRP A CG  
624  C CD1 . TRP A 78  ? 0.71339 0.88433 0.65853 0.06560  0.01146  -0.11977 78  TRP A CD1 
625  C CD2 . TRP A 78  ? 0.72764 0.95271 0.66696 0.07049  0.00697  -0.13530 78  TRP A CD2 
626  N NE1 . TRP A 78  ? 0.80344 0.98291 0.75082 0.04914  0.01245  -0.13898 78  TRP A NE1 
627  C CE2 . TRP A 78  ? 0.74869 0.96194 0.69362 0.05084  0.00976  -0.15015 78  TRP A CE2 
628  C CE3 . TRP A 78  ? 0.71732 0.97839 0.65107 0.07725  0.00381  -0.14201 78  TRP A CE3 
629  C CZ2 . TRP A 78  ? 0.75774 0.99229 0.70449 0.03591  0.01066  -0.17298 78  TRP A CZ2 
630  C CZ3 . TRP A 78  ? 0.71752 1.00399 0.65313 0.06313  0.00292  -0.16542 78  TRP A CZ3 
631  C CH2 . TRP A 78  ? 0.72654 0.99886 0.66941 0.04175  0.00688  -0.18144 78  TRP A CH2 
632  N N   . ARG A 79  ? 0.63707 0.89341 0.55900 0.14213  0.00977  -0.06944 79  ARG A N   
633  C CA  . ARG A 79  ? 0.63168 0.89221 0.54171 0.16218  0.01403  -0.05265 79  ARG A CA  
634  C C   . ARG A 79  ? 0.62638 0.88079 0.52863 0.15954  0.01507  -0.05674 79  ARG A C   
635  O O   . ARG A 79  ? 0.63155 0.89370 0.53607 0.14577  0.01063  -0.07489 79  ARG A O   
636  C CB  . ARG A 79  ? 0.66021 0.96907 0.56385 0.18013  0.01020  -0.04902 79  ARG A CB  
637  C CG  . ARG A 79  ? 0.69074 1.00629 0.60015 0.18991  0.01129  -0.03998 79  ARG A CG  
638  C CD  . ARG A 79  ? 0.67423 1.03421 0.57379 0.21550  0.00945  -0.02985 79  ARG A CD  
639  N NE  . ARG A 79  ? 0.68661 1.10173 0.58511 0.21345  -0.00072 -0.04755 79  ARG A NE  
640  C CZ  . ARG A 79  ? 0.70165 1.14440 0.58601 0.22483  -0.00294 -0.04652 79  ARG A CZ  
641  N NH1 . ARG A 79  ? 0.72189 1.14127 0.59097 0.23986  0.00498  -0.02705 79  ARG A NH1 
642  N NH2 . ARG A 79  ? 0.68261 1.17896 0.56801 0.22008  -0.01242 -0.06655 79  ARG A NH2 
643  N N   . PRO A 80  ? 0.62399 0.86306 0.51699 0.17211  0.02252  -0.04062 80  PRO A N   
644  C CA  . PRO A 80  ? 0.65453 0.88988 0.54020 0.17037  0.02440  -0.04435 80  PRO A CA  
645  C C   . PRO A 80  ? 0.68543 0.96400 0.56230 0.17351  0.01802  -0.05635 80  PRO A C   
646  O O   . PRO A 80  ? 0.67764 0.95515 0.55244 0.16521  0.01739  -0.06835 80  PRO A O   
647  C CB  . PRO A 80  ? 0.61700 0.83281 0.49372 0.18497  0.03556  -0.02291 80  PRO A CB  
648  C CG  . PRO A 80  ? 0.64053 0.83100 0.52546 0.18547  0.04049  -0.01246 80  PRO A CG  
649  C CD  . PRO A 80  ? 0.61300 0.82958 0.50349 0.18509  0.03194  -0.01969 80  PRO A CD  
650  N N   . ALA A 81  ? 0.69213 1.01131 0.56389 0.18592  0.01339  -0.05442 81  ALA A N   
651  C CA  . ALA A 81  ? 0.73251 1.10064 0.59598 0.18898  0.00655  -0.06786 81  ALA A CA  
652  C C   . ALA A 81  ? 0.70394 1.08238 0.57830 0.16572  0.00027  -0.09619 81  ALA A C   
653  O O   . ALA A 81  ? 0.78028 1.18874 0.64885 0.16214  -0.00318 -0.11209 81  ALA A O   
654  C CB  . ALA A 81  ? 0.72804 1.14228 0.58516 0.20868  0.00216  -0.06000 81  ALA A CB  
655  N N   . GLU A 82  ? 0.69968 1.05272 0.58850 0.14965  0.00014  -0.10309 82  GLU A N   
656  C CA  . GLU A 82  ? 0.71040 1.06432 0.60859 0.12672  -0.00248 -0.12844 82  GLU A CA  
657  C C   . GLU A 82  ? 0.68169 0.99108 0.58095 0.11430  0.00258  -0.13374 82  GLU A C   
658  O O   . GLU A 82  ? 0.66462 0.96167 0.57064 0.09569  0.00329  -0.15201 82  GLU A O   
659  C CB  . GLU A 82  ? 0.72789 1.07865 0.63928 0.11640  -0.00396 -0.13272 82  GLU A CB  
660  C CG  . GLU A 82  ? 0.74937 1.15538 0.66316 0.12392  -0.01010 -0.13721 82  GLU A CG  
661  C CD  . GLU A 82  ? 0.73893 1.13794 0.66131 0.12847  -0.00959 -0.12542 82  GLU A CD  
662  O OE1 . GLU A 82  ? 0.73230 1.08330 0.65842 0.12413  -0.00452 -0.11483 82  GLU A OE1 
663  O OE2 . GLU A 82  ? 0.85778 1.30236 0.78325 0.13714  -0.01432 -0.12745 82  GLU A OE2 
664  N N   . ALA A 83  ? 0.67790 0.96343 0.57048 0.12466  0.00724  -0.11835 83  ALA A N   
665  C CA  . ALA A 83  ? 0.68770 0.93344 0.58274 0.11563  0.01180  -0.12195 83  ALA A CA  
666  C C   . ALA A 83  ? 0.68615 0.94225 0.57833 0.10518  0.01162  -0.14417 83  ALA A C   
667  O O   . ALA A 83  ? 0.67657 0.90436 0.57420 0.09153  0.01432  -0.15602 83  ALA A O   
668  C CB  . ALA A 83  ? 0.68498 0.91178 0.57456 0.12855  0.01742  -0.10308 83  ALA A CB  
669  N N   . ASP A 84  ? 0.69274 0.98889 0.57518 0.11221  0.00933  -0.15012 84  ASP A N   
670  C CA  . ASP A 84  ? 0.69911 1.00846 0.57873 0.10122  0.00986  -0.17411 84  ASP A CA  
671  C C   . ASP A 84  ? 0.68775 1.00304 0.57666 0.08141  0.00864  -0.19692 84  ASP A C   
672  O O   . ASP A 84  ? 0.68907 0.98185 0.58075 0.06638  0.01361  -0.21466 84  ASP A O   
673  C CB  . ASP A 84  ? 0.70761 1.06555 0.57382 0.11320  0.00695  -0.17643 84  ASP A CB  
674  C CG  . ASP A 84  ? 0.75466 1.10248 0.60982 0.13047  0.01137  -0.15578 84  ASP A CG  
675  O OD1 . ASP A 84  ? 0.73206 1.03685 0.59184 0.12944  0.01699  -0.14631 84  ASP A OD1 
676  O OD2 . ASP A 84  ? 0.82504 1.20963 0.66648 0.14518  0.00982  -0.14933 84  ASP A OD2 
677  N N   . LYS A 85  ? 0.67463 1.01868 0.56851 0.08113  0.00357  -0.19686 85  LYS A N   
678  C CA  . LYS A 85  ? 0.67981 1.02877 0.58408 0.06040  0.00413  -0.21832 85  LYS A CA  
679  C C   . LYS A 85  ? 0.70509 0.99590 0.61645 0.04835  0.01060  -0.21557 85  LYS A C   
680  O O   . LYS A 85  ? 0.72597 0.99983 0.64153 0.02911  0.01635  -0.23519 85  LYS A O   
681  C CB  . LYS A 85  ? 0.67136 1.06350 0.58102 0.06463  -0.00241 -0.21635 85  LYS A CB  
682  N N   . LEU A 86  ? 0.69161 0.95114 0.60333 0.05969  0.01078  -0.19153 86  LEU A N   
683  C CA  . LEU A 86  ? 0.71094 0.91914 0.62751 0.05157  0.01584  -0.18665 86  LEU A CA  
684  C C   . LEU A 86  ? 0.71688 0.89139 0.62968 0.04641  0.02216  -0.19505 86  LEU A C   
685  O O   . LEU A 86  ? 0.74161 0.88409 0.65654 0.03310  0.02828  -0.20466 86  LEU A O   
686  C CB  . LEU A 86  ? 0.69632 0.88585 0.61391 0.06553  0.01434  -0.16108 86  LEU A CB  
687  C CG  . LEU A 86  ? 0.71771 0.86808 0.64089 0.05889  0.01704  -0.15419 86  LEU A CG  
688  C CD1 . LEU A 86  ? 0.76166 0.92112 0.69055 0.04384  0.01761  -0.16682 86  LEU A CD1 
689  C CD2 . LEU A 86  ? 0.67987 0.82351 0.60467 0.07208  0.01533  -0.13223 86  LEU A CD2 
690  N N   . VAL A 87  ? 0.70521 0.88518 0.61156 0.05798  0.02195  -0.19064 87  VAL A N   
691  C CA  . VAL A 87  ? 0.71120 0.86417 0.61420 0.05542  0.02808  -0.19948 87  VAL A CA  
692  C C   . VAL A 87  ? 0.74570 0.89930 0.64869 0.03740  0.03348  -0.22642 87  VAL A C   
693  O O   . VAL A 87  ? 0.77291 0.88622 0.67638 0.02873  0.04134  -0.23365 87  VAL A O   
694  C CB  . VAL A 87  ? 0.67823 0.84922 0.57411 0.06932  0.02721  -0.19409 87  VAL A CB  
695  C CG1 . VAL A 87  ? 0.65203 0.80496 0.54456 0.06564  0.03379  -0.20882 87  VAL A CG1 
696  C CG2 . VAL A 87  ? 0.65116 0.80964 0.54802 0.08405  0.02601  -0.16905 87  VAL A CG2 
697  N N   . LYS A 88  ? 0.75169 0.95183 0.65375 0.03178  0.03020  -0.24198 88  LYS A N   
698  C CA  . LYS A 88  ? 0.77654 0.98397 0.67947 0.01224  0.03634  -0.27170 88  LYS A CA  
699  C C   . LYS A 88  ? 0.79913 0.97654 0.70898 -0.00566 0.04306  -0.27925 88  LYS A C   
700  O O   . LYS A 88  ? 0.82700 0.96884 0.73587 -0.01926 0.05424  -0.29442 88  LYS A O   
701  C CB  . LYS A 88  ? 0.78365 1.05660 0.68545 0.01070  0.02966  -0.28632 88  LYS A CB  
702  C CG  . LYS A 88  ? 0.81103 1.10162 0.71385 -0.01023 0.03600  -0.32114 88  LYS A CG  
703  C CD  . LYS A 88  ? 0.81410 1.17790 0.71413 -0.00737 0.02740  -0.33421 88  LYS A CD  
704  C CE  . LYS A 88  ? 0.86986 1.25562 0.77165 -0.02997 0.03411  -0.37232 88  LYS A CE  
705  N NZ  . LYS A 88  ? 0.80012 1.25445 0.70339 -0.02411 0.02440  -0.37645 88  LYS A NZ  
706  N N   . LEU A 89  ? 0.80261 0.99153 0.71853 -0.00536 0.03786  -0.26824 89  LEU A N   
707  C CA  . LEU A 89  ? 0.82415 0.98789 0.74594 -0.02299 0.04494  -0.27519 89  LEU A CA  
708  C C   . LEU A 89  ? 0.87234 0.97164 0.79037 -0.02050 0.05234  -0.26117 89  LEU A C   
709  O O   . LEU A 89  ? 0.91495 0.97832 0.83212 -0.03594 0.06387  -0.27204 89  LEU A O   
710  C CB  . LEU A 89  ? 0.84087 1.03592 0.77018 -0.02145 0.03741  -0.26642 89  LEU A CB  
711  C CG  . LEU A 89  ? 0.81713 1.08035 0.75110 -0.02431 0.03049  -0.28217 89  LEU A CG  
712  C CD1 . LEU A 89  ? 0.77081 1.05962 0.71353 -0.02331 0.02510  -0.27444 89  LEU A CD1 
713  C CD2 . LEU A 89  ? 0.77486 1.05172 0.71145 -0.04798 0.03865  -0.31634 89  LEU A CD2 
714  N N   . LEU A 90  ? 0.85342 0.93823 0.76861 -0.00096 0.04678  -0.23736 90  LEU A N   
715  C CA  . LEU A 90  ? 0.89737 0.92862 0.80885 0.00438  0.05217  -0.22407 90  LEU A CA  
716  C C   . LEU A 90  ? 0.94873 0.94786 0.85411 0.00049  0.06269  -0.23742 90  LEU A C   
717  O O   . LEU A 90  ? 1.00158 0.95516 0.90293 -0.00509 0.07272  -0.23801 90  LEU A O   
718  C CB  . LEU A 90  ? 0.84516 0.87630 0.75661 0.02484  0.04426  -0.20025 90  LEU A CB  
719  C CG  . LEU A 90  ? 0.85963 0.88793 0.77512 0.02963  0.03917  -0.18165 90  LEU A CG  
720  C CD1 . LEU A 90  ? 0.80353 0.83180 0.71947 0.04741  0.03387  -0.16264 90  LEU A CD1 
721  C CD2 . LEU A 90  ? 0.90553 0.89217 0.81882 0.02160  0.04604  -0.17984 90  LEU A CD2 
722  N N   . ALA A 91  ? 0.92310 0.94414 0.82638 0.00489  0.06147  -0.24728 91  ALA A N   
723  C CA  . ALA A 91  ? 0.99425 0.98597 0.89194 0.00316  0.07190  -0.26040 91  ALA A CA  
724  C C   . ALA A 91  ? 1.08589 1.05482 0.98233 -0.01895 0.08555  -0.28321 91  ALA A C   
725  O O   . ALA A 91  ? 1.13966 1.05709 1.03050 -0.02045 0.09785  -0.28424 91  ALA A O   
726  C CB  . ALA A 91  ? 0.99345 1.02082 0.88910 0.00929  0.06823  -0.26989 91  ALA A CB  
727  N N   . LYS A 92  ? 1.03487 1.04226 0.93633 -0.03601 0.08460  -0.30197 92  LYS A N   
728  C CA  . LYS A 92  ? 1.08543 1.07476 0.98776 -0.06093 0.09903  -0.32595 92  LYS A CA  
729  C C   . LYS A 92  ? 1.10403 1.04331 1.00422 -0.06514 0.10733  -0.31290 92  LYS A C   
730  O O   . LYS A 92  ? 1.16202 1.05168 1.05619 -0.07595 0.12436  -0.32213 92  LYS A O   
731  C CB  . LYS A 92  ? 1.07554 1.12509 0.98643 -0.07725 0.09395  -0.34625 92  LYS A CB  
732  C CG  . LYS A 92  ? 1.15310 1.18971 1.06853 -0.10517 0.10787  -0.36788 92  LYS A CG  
733  C CD  . LYS A 92  ? 1.17801 1.28434 1.10416 -0.11968 0.10104  -0.38880 92  LYS A CD  
734  C CE  . LYS A 92  ? 1.25316 1.34989 1.18666 -0.15060 0.11681  -0.41324 92  LYS A CE  
735  N NZ  . LYS A 92  ? 1.32253 1.49431 1.27209 -0.16297 0.10888  -0.42952 92  LYS A NZ  
736  N N   . GLY A 93  ? 1.28439 0.93490 0.91941 0.07355  0.13294  -0.35185 93  GLY A N   
737  C CA  . GLY A 93  ? 1.29462 0.93090 0.96027 0.07156  0.13006  -0.33945 93  GLY A CA  
738  C C   . GLY A 93  ? 1.32265 0.94181 0.98695 0.04916  0.11261  -0.34241 93  GLY A C   
739  O O   . GLY A 93  ? 1.30308 0.93667 0.94949 0.03321  0.10119  -0.34590 93  GLY A O   
740  N N   . GLU A 94  ? 1.36486 0.95507 1.04890 0.04785  0.11020  -0.34010 94  GLU A N   
741  C CA  . GLU A 94  ? 1.40779 0.98218 1.09645 0.02612  0.09500  -0.34079 94  GLU A CA  
742  C C   . GLU A 94  ? 1.40344 1.00625 1.09997 0.01186  0.08636  -0.32735 94  GLU A C   
743  O O   . GLU A 94  ? 1.41930 1.02321 1.11317 -0.00872 0.07185  -0.33026 94  GLU A O   
744  C CB  . GLU A 94  ? 1.35883 0.91737 1.02220 0.01294  0.08474  -0.36156 94  GLU A CB  
745  N N   . TYR A 95  ? 1.41114 1.03880 1.11873 0.02262  0.09502  -0.31274 95  TYR A N   
746  C CA  . TYR A 95  ? 1.31755 0.97723 1.03782 0.01226  0.08542  -0.29595 95  TYR A CA  
747  C C   . TYR A 95  ? 1.27602 0.92944 1.02889 0.00928  0.08060  -0.27921 95  TYR A C   
748  O O   . TYR A 95  ? 1.34720 0.97672 1.11393 0.02101  0.08977  -0.27655 95  TYR A O   
749  C CB  . TYR A 95  ? 1.26168 0.95846 0.98532 0.02549  0.09260  -0.28169 95  TYR A CB  
750  C CG  . TYR A 95  ? 1.26427 0.95709 1.00185 0.04757  0.10981  -0.27669 95  TYR A CG  
751  C CD1 . TYR A 95  ? 1.22704 0.92201 0.99730 0.05511  0.11099  -0.25878 95  TYR A CD1 
752  C CD2 . TYR A 95  ? 1.27576 0.96547 0.99387 0.06134  0.12478  -0.28972 95  TYR A CD2 
753  C CE1 . TYR A 95  ? 1.20583 0.90118 0.99051 0.07572  0.12530  -0.25387 95  TYR A CE1 
754  C CE2 . TYR A 95  ? 1.26752 0.95807 1.00126 0.08228  0.14051  -0.28494 95  TYR A CE2 
755  C CZ  . TYR A 95  ? 1.21498 0.90914 0.98281 0.08939  0.14005  -0.26687 95  TYR A CZ  
756  O OH  . TYR A 95  ? 1.19110 0.88967 0.97604 0.11069  0.15440  -0.26186 95  TYR A OH  
757  N N   . GLN A 96  ? 1.19692 0.87240 0.96118 -0.00570 0.06627  -0.26757 96  GLN A N   
758  C CA  . GLN A 96  ? 1.12154 0.79706 0.91564 -0.00854 0.06198  -0.24984 96  GLN A CA  
759  C C   . GLN A 96  ? 1.02338 0.72785 0.83762 0.00552  0.06646  -0.22822 96  GLN A C   
760  O O   . GLN A 96  ? 0.98507 0.71749 0.79235 0.01103  0.06828  -0.22405 96  GLN A O   
761  C CB  . GLN A 96  ? 1.13053 0.81909 0.93004 -0.02991 0.04574  -0.24680 96  GLN A CB  
762  C CG  . GLN A 96  ? 1.17886 0.83774 0.96674 -0.04729 0.03990  -0.26578 96  GLN A CG  
763  C CD  . GLN A 96  ? 1.19365 0.87257 0.99132 -0.06819 0.02390  -0.26140 96  GLN A CD  
764  O OE1 . GLN A 96  ? 1.15957 0.87612 0.96488 -0.06884 0.01644  -0.24795 96  GLN A OE1 
765  N NE2 . GLN A 96  ? 1.24003 0.89382 1.03852 -0.08533 0.01897  -0.27256 96  GLN A NE2 
766  N N   . LYS A 97  ? 0.94518 0.64197 0.78357 0.01059  0.06818  -0.21436 97  LYS A N   
767  C CA  . LYS A 97  ? 0.85803 0.58089 0.71739 0.02181  0.07059  -0.19405 97  LYS A CA  
768  C C   . LYS A 97  ? 0.81502 0.55356 0.69184 0.01017  0.05912  -0.17860 97  LYS A C   
769  O O   . LYS A 97  ? 0.82952 0.54995 0.71109 -0.00132 0.05364  -0.17995 97  LYS A O   
770  C CB  . LYS A 97  ? 0.84111 0.54639 0.71406 0.03968  0.08174  -0.18933 97  LYS A CB  
771  C CG  . LYS A 97  ? 0.90367 0.59316 0.76179 0.05401  0.09488  -0.20457 97  LYS A CG  
772  C CD  . LYS A 97  ? 0.88731 0.55963 0.76111 0.07312  0.10498  -0.19905 97  LYS A CD  
773  C CE  . LYS A 97  ? 0.93643 0.56794 0.79375 0.08060  0.11460  -0.21848 97  LYS A CE  
774  N NZ  . LYS A 97  ? 1.03053 0.64659 0.90282 0.10266  0.12514  -0.21276 97  LYS A NZ  
775  N N   . VAL A 98  ? 0.75480 0.52639 0.64066 0.01277  0.05625  -0.16435 98  VAL A N   
776  C CA  . VAL A 98  ? 0.71755 0.50556 0.62144 0.00607  0.04769  -0.14823 98  VAL A CA  
777  C C   . VAL A 98  ? 0.68578 0.48608 0.60746 0.01978  0.05305  -0.13280 98  VAL A C   
778  O O   . VAL A 98  ? 0.65104 0.46221 0.57092 0.03125  0.06059  -0.13259 98  VAL A O   
779  C CB  . VAL A 98  ? 0.74813 0.56372 0.64594 -0.00437 0.03764  -0.14548 98  VAL A CB  
780  C CG1 . VAL A 98  ? 0.78543 0.59232 0.66612 -0.01820 0.03073  -0.16123 98  VAL A CG1 
781  C CG2 . VAL A 98  ? 0.74269 0.58093 0.63297 0.00427  0.04179  -0.14163 98  VAL A CG2 
782  N N   . SER A 99  ? 0.64501 0.44460 0.58373 0.01811  0.04931  -0.12023 99  SER A N   
783  C CA  . SER A 99  ? 0.63960 0.44913 0.59497 0.03016  0.05277  -0.10612 99  SER A CA  
784  C C   . SER A 99  ? 0.60285 0.43708 0.56855 0.02450  0.04506  -0.09230 99  SER A C   
785  O O   . SER A 99  ? 0.57965 0.41415 0.54669 0.01278  0.03783  -0.09024 99  SER A O   
786  C CB  . SER A 99  ? 0.67069 0.45389 0.63487 0.03633  0.05640  -0.10283 99  SER A CB  
787  O OG  . SER A 99  ? 0.71157 0.46781 0.66548 0.04245  0.06403  -0.11631 99  SER A OG  
788  N N   . TYR A 100 ? 0.56496 0.42032 0.53838 0.03270  0.04703  -0.08345 100 TYR A N   
789  C CA  . TYR A 100 ? 0.53478 0.41092 0.51773 0.02964  0.04106  -0.07070 100 TYR A CA  
790  C C   . TYR A 100 ? 0.52914 0.40692 0.52755 0.03866  0.04249  -0.05962 100 TYR A C   
791  O O   . TYR A 100 ? 0.49933 0.37362 0.50244 0.05010  0.04884  -0.06042 100 TYR A O   
792  C CB  . TYR A 100 ? 0.52446 0.42333 0.50257 0.02978  0.04128  -0.06917 100 TYR A CB  
793  C CG  . TYR A 100 ? 0.52774 0.43132 0.49072 0.02021  0.03651  -0.07523 100 TYR A CG  
794  C CD1 . TYR A 100 ? 0.56167 0.45258 0.51761 0.01124  0.03168  -0.08320 100 TYR A CD1 
795  C CD2 . TYR A 100 ? 0.53786 0.45916 0.49378 0.01976  0.03635  -0.07229 100 TYR A CD2 
796  C CE1 . TYR A 100 ? 0.59073 0.48950 0.53336 0.00296  0.02575  -0.08858 100 TYR A CE1 
797  C CE2 . TYR A 100 ? 0.54938 0.47580 0.49026 0.01256  0.03115  -0.07640 100 TYR A CE2 
798  C CZ  . TYR A 100 ? 0.58942 0.50608 0.52400 0.00461  0.02529  -0.08469 100 TYR A CZ  
799  O OH  . TYR A 100 ? 0.63466 0.55972 0.55486 -0.00211 0.01863  -0.08863 100 TYR A OH  
800  N N   . PRO A 101 ? 0.49725 0.38161 0.50335 0.03460  0.03670  -0.04937 101 PRO A N   
801  C CA  . PRO A 101 ? 0.48277 0.36992 0.50097 0.04289  0.03686  -0.03879 101 PRO A CA  
802  C C   . PRO A 101 ? 0.47343 0.38334 0.49840 0.04926  0.03789  -0.03447 101 PRO A C   
803  O O   . PRO A 101 ? 0.43711 0.36129 0.45777 0.04506  0.03759  -0.03652 101 PRO A O   
804  C CB  . PRO A 101 ? 0.47220 0.36113 0.49303 0.03498  0.03069  -0.03067 101 PRO A CB  
805  C CG  . PRO A 101 ? 0.51635 0.40015 0.52917 0.02297  0.02799  -0.03776 101 PRO A CG  
806  C CD  . PRO A 101 ? 0.47579 0.36576 0.47960 0.02295  0.02980  -0.04722 101 PRO A CD  
807  N N   . LEU A 102 ? 0.41171 0.32508 0.44754 0.05914  0.03885  -0.02782 102 LEU A N   
808  C CA  . LEU A 102 ? 0.41685 0.35342 0.46246 0.06459  0.03938  -0.02367 102 LEU A CA  
809  C C   . LEU A 102 ? 0.41641 0.36135 0.47044 0.06632  0.03325  -0.01291 102 LEU A C   
810  O O   . LEU A 102 ? 0.37564 0.30693 0.42818 0.06673  0.03054  -0.00805 102 LEU A O   
811  C CB  . LEU A 102 ? 0.43321 0.37217 0.48572 0.07698  0.04678  -0.02758 102 LEU A CB  
812  C CG  . LEU A 102 ? 0.45342 0.38275 0.49559 0.07743  0.05438  -0.03959 102 LEU A CG  
813  C CD1 . LEU A 102 ? 0.47235 0.40138 0.52260 0.09245  0.06246  -0.04289 102 LEU A CD1 
814  C CD2 . LEU A 102 ? 0.43107 0.37690 0.46650 0.06922  0.05550  -0.04266 102 LEU A CD2 
815  N N   . LEU A 103 ? 0.37566 0.34300 0.43759 0.06662  0.03136  -0.00941 103 LEU A N   
816  C CA  . LEU A 103 ? 0.41468 0.39297 0.48277 0.06707  0.02470  -0.00086 103 LEU A CA  
817  C C   . LEU A 103 ? 0.42321 0.41651 0.50563 0.07827  0.02485  0.00260  103 LEU A C   
818  O O   . LEU A 103 ? 0.39153 0.40011 0.48240 0.08109  0.02931  -0.00100 103 LEU A O   
819  C CB  . LEU A 103 ? 0.39583 0.38763 0.46170 0.05724  0.02116  -0.00019 103 LEU A CB  
820  C CG  . LEU A 103 ? 0.40339 0.40842 0.47468 0.05682  0.01441  0.00623  103 LEU A CG  
821  C CD1 . LEU A 103 ? 0.38840 0.38114 0.45244 0.05652  0.00997  0.01142  103 LEU A CD1 
822  C CD2 . LEU A 103 ? 0.39657 0.41302 0.46656 0.04761  0.01277  0.00504  103 LEU A CD2 
823  N N   . LYS A 104 ? 0.41279 0.40368 0.49812 0.08485  0.02004  0.01017  104 LYS A N   
824  C CA  . LYS A 104 ? 0.40721 0.41546 0.50677 0.09641  0.01787  0.01496  104 LYS A CA  
825  C C   . LYS A 104 ? 0.43290 0.46212 0.53636 0.09146  0.00921  0.01990  104 LYS A C   
826  O O   . LYS A 104 ? 0.40495 0.42641 0.49809 0.08597  0.00400  0.02385  104 LYS A O   
827  C CB  . LYS A 104 ? 0.45310 0.44378 0.55184 0.10896  0.01787  0.02094  104 LYS A CB  
828  C CG  . LYS A 104 ? 0.47133 0.48058 0.58463 0.12337  0.01414  0.02767  104 LYS A CG  
829  C CD  . LYS A 104 ? 0.51548 0.50250 0.62352 0.13511  0.01312  0.03624  104 LYS A CD  
830  C CE  . LYS A 104 ? 0.56328 0.57012 0.68422 0.15048  0.00712  0.04512  104 LYS A CE  
831  N NZ  . LYS A 104 ? 0.63511 0.64648 0.77042 0.16651  0.01344  0.04261  104 LYS A NZ  
832  N N   . THR A 105 ? 0.41457 0.47074 0.53284 0.09272  0.00816  0.01896  105 THR A N   
833  C CA  . THR A 105 ? 0.40851 0.48643 0.53222 0.08738  -0.00053 0.02200  105 THR A CA  
834  C C   . THR A 105 ? 0.41812 0.51784 0.55823 0.09997  -0.00527 0.02718  105 THR A C   
835  O O   . THR A 105 ? 0.39749 0.51117 0.55304 0.10813  -0.00004 0.02528  105 THR A O   
836  C CB  . THR A 105 ? 0.40866 0.50203 0.53719 0.07495  0.00148  0.01640  105 THR A CB  
837  O OG1 . THR A 105 ? 0.42384 0.49750 0.53709 0.06542  0.00575  0.01243  105 THR A OG1 
838  C CG2 . THR A 105 ? 0.39950 0.51113 0.53182 0.06741  -0.00788 0.01812  105 THR A CG2 
839  N N   . THR A 106 ? 0.39483 0.49889 0.53133 0.10239  -0.01505 0.03379  106 THR A N   
840  C CA  . THR A 106 ? 0.40654 0.53493 0.55789 0.11420  -0.02219 0.03966  106 THR A CA  
841  C C   . THR A 106 ? 0.41525 0.57009 0.57145 0.10408  -0.03242 0.03870  106 THR A C   
842  O O   . THR A 106 ? 0.41597 0.56114 0.55599 0.09462  -0.03768 0.03863  106 THR A O   
843  C CB  . THR A 106 ? 0.44597 0.55758 0.58742 0.12730  -0.02604 0.04940  106 THR A CB  
844  O OG1 . THR A 106 ? 0.45186 0.53400 0.58712 0.13404  -0.01621 0.04914  106 THR A OG1 
845  C CG2 . THR A 106 ? 0.44890 0.58705 0.60661 0.14241  -0.03366 0.05641  106 THR A CG2 
846  N N   . VAL A 107 ? 0.39970 0.58814 0.57846 0.10571  -0.03484 0.03728  107 VAL A N   
847  C CA  . VAL A 107 ? 0.42292 0.63928 0.60935 0.09502  -0.04518 0.03533  107 VAL A CA  
848  C C   . VAL A 107 ? 0.44488 0.68810 0.64426 0.10850  -0.05614 0.04241  107 VAL A C   
849  O O   . VAL A 107 ? 0.45369 0.71672 0.67417 0.12163  -0.05355 0.04486  107 VAL A O   
850  C CB  . VAL A 107 ? 0.41207 0.64927 0.61575 0.08256  -0.03975 0.02796  107 VAL A CB  
851  C CG1 . VAL A 107 ? 0.43208 0.69204 0.64076 0.06783  -0.05047 0.02472  107 VAL A CG1 
852  C CG2 . VAL A 107 ? 0.41665 0.62635 0.60667 0.07290  -0.02820 0.02270  107 VAL A CG2 
853  N N   . LYS A 108 ? 0.46061 0.70521 0.64674 0.10632  -0.06828 0.04574  108 LYS A N   
854  C CA  . LYS A 108 ? 0.49567 0.76655 0.69034 0.11856  -0.08106 0.05315  108 LYS A CA  
855  C C   . LYS A 108 ? 0.51350 0.82097 0.72093 0.10546  -0.09278 0.04755  108 LYS A C   
856  O O   . LYS A 108 ? 0.50130 0.80191 0.69832 0.08681  -0.09382 0.03963  108 LYS A O   
857  C CB  . LYS A 108 ? 0.49085 0.73860 0.65920 0.12626  -0.08707 0.06176  108 LYS A CB  
858  N N   . TYR A 109 ? 0.53847 0.88481 0.76909 0.11544  -0.10173 0.05154  109 TYR A N   
859  C CA  . TYR A 109 ? 0.55007 0.93640 0.79645 0.10295  -0.11440 0.04620  109 TYR A CA  
860  C C   . TYR A 109 ? 0.60763 1.01685 0.85164 0.11417  -0.13217 0.05376  109 TYR A C   
861  O O   . TYR A 109 ? 0.62786 1.01355 0.84851 0.12663  -0.13490 0.06241  109 TYR A O   
862  C CB  . TYR A 109 ? 0.54955 0.97287 0.83281 0.10124  -0.10916 0.04255  109 TYR A CB  
863  C CG  . TYR A 109 ? 0.50846 0.91179 0.79500 0.09552  -0.09036 0.03751  109 TYR A CG  
864  C CD1 . TYR A 109 ? 0.51405 0.90347 0.80465 0.11328  -0.07797 0.04189  109 TYR A CD1 
865  C CD2 . TYR A 109 ? 0.47044 0.86789 0.75466 0.07265  -0.08516 0.02835  109 TYR A CD2 
866  C CE1 . TYR A 109 ? 0.48443 0.85670 0.77558 0.10813  -0.06152 0.03667  109 TYR A CE1 
867  C CE2 . TYR A 109 ? 0.47580 0.85598 0.76088 0.06810  -0.06859 0.02479  109 TYR A CE2 
868  C CZ  . TYR A 109 ? 0.47020 0.83905 0.75832 0.08574  -0.05714 0.02867  109 TYR A CZ  
869  O OH  . TYR A 109 ? 0.49098 0.84340 0.77741 0.08122  -0.04132 0.02449  109 TYR A OH  
870  N N   . GLY A 110 ? 0.64631 1.10257 0.91442 0.10939  -0.14441 0.05098  110 GLY A N   
871  C CA  . GLY A 110 ? 0.61287 1.09850 0.88211 0.12060  -0.16301 0.05810  110 GLY A CA  
872  C C   . GLY A 110 ? 0.63710 1.17432 0.94603 0.12982  -0.16871 0.06058  110 GLY A C   
873  O O   . GLY A 110 ? 0.58294 1.13366 0.89215 0.13913  -0.18092 0.06622  110 GLY A O   
874  N N   . LYS A 114 ? 0.76703 1.19096 1.06373 0.19407  -0.11325 0.08280  114 LYS A N   
875  C CA  . LYS A 114 ? 0.71778 1.13104 1.02772 0.19556  -0.09478 0.07693  114 LYS A CA  
876  C C   . LYS A 114 ? 0.77307 1.13867 1.05591 0.17985  -0.08281 0.07018  114 LYS A C   
877  O O   . LYS A 114 ? 0.68890 1.04003 0.95018 0.16327  -0.08842 0.06725  114 LYS A O   
878  C CB  . LYS A 114 ? 0.66947 1.13046 1.01427 0.18591  -0.09326 0.06888  114 LYS A CB  
879  C CG  . LYS A 114 ? 0.69476 1.17278 1.03811 0.15830  -0.10182 0.06034  114 LYS A CG  
880  C CD  . LYS A 114 ? 0.70116 1.23033 1.08193 0.14864  -0.10133 0.05412  114 LYS A CD  
881  C CE  . LYS A 114 ? 0.77236 1.34033 1.17309 0.15660  -0.11611 0.05834  114 LYS A CE  
882  N NZ  . LYS A 114 ? 0.79579 1.36441 1.17664 0.14918  -0.13545 0.06006  114 LYS A NZ  
883  N N   . GLU A 115 ? 0.58905 0.93129 0.87290 0.18580  -0.06654 0.06732  115 GLU A N   
884  C CA  . GLU A 115 ? 0.54275 0.83926 0.80084 0.17466  -0.05586 0.06237  115 GLU A CA  
885  C C   . GLU A 115 ? 0.50472 0.79767 0.77356 0.17203  -0.03961 0.05381  115 GLU A C   
886  O O   . GLU A 115 ? 0.48257 0.78943 0.77094 0.18812  -0.03282 0.05453  115 GLU A O   
887  C CB  . GLU A 115 ? 0.56071 0.81589 0.79566 0.18826  -0.05421 0.07088  115 GLU A CB  
888  C CG  . GLU A 115 ? 0.59339 0.81668 0.79784 0.17441  -0.05679 0.07120  115 GLU A CG  
889  C CD  . GLU A 115 ? 0.66549 0.84811 0.84939 0.18617  -0.05286 0.07977  115 GLU A CD  
890  O OE1 . GLU A 115 ? 0.66612 0.82711 0.85223 0.19524  -0.04132 0.07854  115 GLU A OE1 
891  O OE2 . GLU A 115 ? 0.69868 0.87043 0.86354 0.18586  -0.06087 0.08751  115 GLU A OE2 
892  N N   . ALA A 116 ? 0.46129 0.73541 0.71614 0.15280  -0.03323 0.04594  116 ALA A N   
893  C CA  . ALA A 116 ? 0.43844 0.70253 0.69563 0.14901  -0.01777 0.03814  116 ALA A CA  
894  C C   . ALA A 116 ? 0.43495 0.65274 0.66317 0.14211  -0.01173 0.03554  116 ALA A C   
895  O O   . ALA A 116 ? 0.42349 0.62616 0.63353 0.13034  -0.01829 0.03637  116 ALA A O   
896  C CB  . ALA A 116 ? 0.43259 0.72498 0.70412 0.13100  -0.01538 0.03126  116 ALA A CB  
897  N N   . THR A 117 ? 0.43031 0.62686 0.65453 0.14956  0.00074  0.03179  117 THR A N   
898  C CA  . THR A 117 ? 0.43186 0.58764 0.63118 0.14271  0.00662  0.02829  117 THR A CA  
899  C C   . THR A 117 ? 0.44064 0.59375 0.63904 0.13462  0.01883  0.01883  117 THR A C   
900  O O   . THR A 117 ? 0.40658 0.57808 0.62114 0.14241  0.02698  0.01546  117 THR A O   
901  C CB  . THR A 117 ? 0.46621 0.59080 0.65547 0.15840  0.00920  0.03250  117 THR A CB  
902  O OG1 . THR A 117 ? 0.51505 0.64444 0.71817 0.17466  0.01838  0.02988  117 THR A OG1 
903  C CG2 . THR A 117 ? 0.48185 0.60800 0.66934 0.16697  -0.00250 0.04371  117 THR A CG2 
904  N N   . TYR A 118 ? 0.43585 0.56736 0.61491 0.11972  0.02019  0.01499  118 TYR A N   
905  C CA  . TYR A 118 ? 0.42137 0.54812 0.59462 0.11079  0.03032  0.00708  118 TYR A CA  
906  C C   . TYR A 118 ? 0.43061 0.52042 0.58034 0.10680  0.03312  0.00377  118 TYR A C   
907  O O   . TYR A 118 ? 0.43303 0.50473 0.57101 0.10429  0.02637  0.00776  118 TYR A O   
908  C CB  . TYR A 118 ? 0.41058 0.55545 0.58626 0.09351  0.02813  0.00595  118 TYR A CB  
909  C CG  . TYR A 118 ? 0.42878 0.61113 0.62796 0.09325  0.02300  0.00903  118 TYR A CG  
910  C CD1 . TYR A 118 ? 0.42733 0.61862 0.62912 0.09132  0.01008  0.01415  118 TYR A CD1 
911  C CD2 . TYR A 118 ? 0.42070 0.63136 0.63957 0.09458  0.03109  0.00652  118 TYR A CD2 
912  C CE1 . TYR A 118 ? 0.42765 0.65557 0.65153 0.09001  0.00389  0.01609  118 TYR A CE1 
913  C CE2 . TYR A 118 ? 0.42414 0.67283 0.66748 0.09307  0.02597  0.00910  118 TYR A CE2 
914  C CZ  . TYR A 118 ? 0.42880 0.68615 0.67477 0.09043  0.01165  0.01359  118 TYR A CZ  
915  O OH  . TYR A 118 ? 0.44161 0.73886 0.71231 0.08776  0.00517  0.01526  118 TYR A OH  
916  N N   . LEU A 119 ? 0.41980 0.50052 0.56275 0.10568  0.04321  -0.00374 119 LEU A N   
917  C CA  . LEU A 119 ? 0.43219 0.48174 0.55401 0.10063  0.04582  -0.00859 119 LEU A CA  
918  C C   . LEU A 119 ? 0.40586 0.45839 0.51770 0.08603  0.04814  -0.01243 119 LEU A C   
919  O O   . LEU A 119 ? 0.41285 0.48430 0.53160 0.08411  0.05450  -0.01481 119 LEU A O   
920  C CB  . LEU A 119 ? 0.47155 0.50482 0.59035 0.11254  0.05502  -0.01514 119 LEU A CB  
921  C CG  . LEU A 119 ? 0.48753 0.48476 0.58952 0.11302  0.05505  -0.01819 119 LEU A CG  
922  C CD1 . LEU A 119 ? 0.48954 0.47613 0.59216 0.11560  0.04651  -0.00898 119 LEU A CD1 
923  C CD2 . LEU A 119 ? 0.53924 0.52245 0.64048 0.12614  0.06488  -0.02580 119 LEU A CD2 
924  N N   . ALA A 120 ? 0.37683 0.41183 0.47296 0.07617  0.04335  -0.01216 120 ALA A N   
925  C CA  . ALA A 120 ? 0.37926 0.41509 0.46461 0.06378  0.04437  -0.01425 120 ALA A CA  
926  C C   . ALA A 120 ? 0.40001 0.41331 0.46704 0.06074  0.04648  -0.02014 120 ALA A C   
927  O O   . ALA A 120 ? 0.37097 0.36602 0.43234 0.06212  0.04295  -0.02031 120 ALA A O   
928  C CB  . ALA A 120 ? 0.38817 0.42791 0.47246 0.05439  0.03581  -0.00847 120 ALA A CB  
929  N N   . LEU A 121 ? 0.37246 0.38803 0.43008 0.05607  0.05226  -0.02479 121 LEU A N   
930  C CA  . LEU A 121 ? 0.38583 0.38435 0.42467 0.05109  0.05236  -0.03040 121 LEU A CA  
931  C C   . LEU A 121 ? 0.35972 0.35772 0.38954 0.04065  0.04606  -0.02622 121 LEU A C   
932  O O   . LEU A 121 ? 0.38186 0.36686 0.40099 0.03671  0.04158  -0.02810 121 LEU A O   
933  C CB  . LEU A 121 ? 0.37417 0.37477 0.40412 0.05313  0.06203  -0.03802 121 LEU A CB  
934  C CG  . LEU A 121 ? 0.41622 0.40276 0.42448 0.04747  0.06166  -0.04478 121 LEU A CG  
935  C CD1 . LEU A 121 ? 0.41900 0.38440 0.42270 0.04822  0.05715  -0.04971 121 LEU A CD1 
936  C CD2 . LEU A 121 ? 0.40525 0.39567 0.40276 0.05033  0.07212  -0.05239 121 LEU A CD2 
937  N N   . ASN A 122 ? 0.32676 0.33860 0.36144 0.03609  0.04572  -0.02066 122 ASN A N   
938  C CA  . ASN A 122 ? 0.34857 0.35750 0.37537 0.02802  0.03992  -0.01605 122 ASN A CA  
939  C C   . ASN A 122 ? 0.34858 0.35825 0.38436 0.02735  0.03262  -0.01072 122 ASN A C   
940  O O   . ASN A 122 ? 0.33545 0.33499 0.36644 0.02649  0.02712  -0.00984 122 ASN A O   
941  C CB  . ASN A 122 ? 0.34716 0.36535 0.37027 0.02230  0.04434  -0.01314 122 ASN A CB  
942  C CG  . ASN A 122 ? 0.41198 0.42412 0.41635 0.02004  0.04776  -0.01591 122 ASN A CG  
943  O OD1 . ASN A 122 ? 0.38597 0.38838 0.38065 0.02215  0.04616  -0.02143 122 ASN A OD1 
944  N ND2 . ASN A 122 ? 0.40901 0.42664 0.40739 0.01502  0.05218  -0.01186 122 ASN A ND2 
945  N N   . GLU A 123 ? 0.32193 0.34495 0.37041 0.02722  0.03253  -0.00747 123 GLU A N   
946  C CA  . GLU A 123 ? 0.35302 0.37710 0.40683 0.02589  0.02515  -0.00326 123 GLU A CA  
947  C C   . GLU A 123 ? 0.36325 0.40555 0.43320 0.02695  0.02485  -0.00147 123 GLU A C   
948  O O   . GLU A 123 ? 0.33213 0.38795 0.41052 0.02733  0.03095  -0.00275 123 GLU A O   
949  C CB  . GLU A 123 ? 0.33911 0.35667 0.38322 0.01833  0.02154  -0.00068 123 GLU A CB  
950  C CG  . GLU A 123 ? 0.32383 0.34918 0.36978 0.01117  0.02431  0.00111  123 GLU A CG  
951  C CD  . GLU A 123 ? 0.38251 0.40868 0.42163 0.00944  0.03209  0.00001  123 GLU A CD  
952  O OE1 . GLU A 123 ? 0.31711 0.33194 0.34167 0.00901  0.03201  -0.00016 123 GLU A OE1 
953  O OE2 . GLU A 123 ? 0.35272 0.39266 0.40098 0.00880  0.03829  -0.00055 123 GLU A OE2 
954  N N   . SER A 124 ? 0.34117 0.38560 0.41535 0.02733  0.01760  0.00141  124 SER A N   
955  C CA  . SER A 124 ? 0.36209 0.42516 0.45016 0.02586  0.01417  0.00309  124 SER A CA  
956  C C   . SER A 124 ? 0.36481 0.42358 0.44642 0.01743  0.00784  0.00423  124 SER A C   
957  O O   . SER A 124 ? 0.37165 0.41624 0.44206 0.01836  0.00391  0.00511  124 SER A O   
958  C CB  . SER A 124 ? 0.39012 0.46080 0.48817 0.03618  0.01035  0.00512  124 SER A CB  
959  O OG  . SER A 124 ? 0.38799 0.47953 0.49928 0.03441  0.00492  0.00669  124 SER A OG  
960  N N   . THR A 125 ? 0.34852 0.41893 0.43712 0.00886  0.00753  0.00381  125 THR A N   
961  C CA  . THR A 125 ? 0.37210 0.43579 0.45377 0.00030  0.00196  0.00345  125 THR A CA  
962  C C   . THR A 125 ? 0.38008 0.46337 0.47511 -0.00343 -0.00449 0.00261  125 THR A C   
963  O O   . THR A 125 ? 0.35379 0.45929 0.46621 -0.00182 -0.00317 0.00287  125 THR A O   
964  C CB  . THR A 125 ? 0.38037 0.43378 0.45426 -0.00950 0.00687  0.00339  125 THR A CB  
965  O OG1 . THR A 125 ? 0.38144 0.45203 0.46902 -0.01736 0.01047  0.00324  125 THR A OG1 
966  C CG2 . THR A 125 ? 0.37340 0.41433 0.43646 -0.00554 0.01330  0.00440  125 THR A CG2 
967  N N   . VAL A 126 ? 0.40035 0.47654 0.48712 -0.00805 -0.01168 0.00108  126 VAL A N   
968  C CA  . VAL A 126 ? 0.36808 0.46151 0.46416 -0.01366 -0.01968 -0.00110 126 VAL A CA  
969  C C   . VAL A 126 ? 0.38600 0.46684 0.47329 -0.02707 -0.02129 -0.00499 126 VAL A C   
970  O O   . VAL A 126 ? 0.37029 0.42738 0.43970 -0.02682 -0.02097 -0.00586 126 VAL A O   
971  C CB  . VAL A 126 ? 0.40306 0.49986 0.49487 -0.00503 -0.02835 -0.00003 126 VAL A CB  
972  C CG1 . VAL A 126 ? 0.37590 0.49507 0.47814 -0.01066 -0.03784 -0.00257 126 VAL A CG1 
973  C CG2 . VAL A 126 ? 0.41316 0.51461 0.51047 0.00881  -0.02588 0.00465  126 VAL A CG2 
974  N N   . LYS A 127 ? 0.38827 0.48491 0.48892 -0.03873 -0.02255 -0.00738 127 LYS A N   
975  C CA  . LYS A 127 ? 0.43080 0.51573 0.52504 -0.05345 -0.02482 -0.01193 127 LYS A CA  
976  C C   . LYS A 127 ? 0.45356 0.56439 0.56310 -0.06202 -0.03395 -0.01616 127 LYS A C   
977  O O   . LYS A 127 ? 0.42670 0.56644 0.55386 -0.05596 -0.03715 -0.01422 127 LYS A O   
978  C CB  . LYS A 127 ? 0.45155 0.52572 0.54598 -0.06308 -0.01478 -0.00989 127 LYS A CB  
979  C CG  . LYS A 127 ? 0.44784 0.50016 0.52749 -0.05436 -0.00684 -0.00542 127 LYS A CG  
980  C CD  . LYS A 127 ? 0.49179 0.53688 0.57098 -0.06255 0.00315  -0.00177 127 LYS A CD  
981  C CE  . LYS A 127 ? 0.57814 0.60452 0.64170 -0.05297 0.00913  0.00250  127 LYS A CE  
982  N NZ  . LYS A 127 ? 0.51694 0.53797 0.57743 -0.05864 0.01905  0.00738  127 LYS A NZ  
983  N N   . SER A 128 ? 0.48341 0.58385 0.58626 -0.07593 -0.03859 -0.02230 128 SER A N   
984  C CA  . SER A 128 ? 0.52938 0.65498 0.64599 -0.08630 -0.04878 -0.02773 128 SER A CA  
985  C C   . SER A 128 ? 0.56696 0.71515 0.70794 -0.10017 -0.04404 -0.02703 128 SER A C   
986  O O   . SER A 128 ? 0.56170 0.70042 0.70438 -0.10349 -0.03233 -0.02276 128 SER A O   
987  C CB  . SER A 128 ? 0.57627 0.68074 0.67453 -0.09661 -0.05623 -0.03648 128 SER A CB  
988  O OG  . SER A 128 ? 0.63546 0.71872 0.73023 -0.11246 -0.05014 -0.03917 128 SER A OG  
989  N N   . SER A 129 ? 0.58496 0.76540 0.74501 -0.10862 -0.05343 -0.03105 129 SER A N   
990  C CA  . SER A 129 ? 0.62873 0.83646 0.81554 -0.12354 -0.04954 -0.03085 129 SER A CA  
991  C C   . SER A 129 ? 0.71782 0.90305 0.89840 -0.14609 -0.04616 -0.03555 129 SER A C   
992  O O   . SER A 129 ? 0.84843 1.04722 1.04724 -0.15958 -0.03831 -0.03334 129 SER A O   
993  C CB  . SER A 129 ? 0.60975 0.86280 0.82106 -0.12536 -0.06194 -0.03369 129 SER A CB  
994  O OG  . SER A 129 ? 0.65195 0.90000 0.85211 -0.13524 -0.07582 -0.04262 129 SER A OG  
995  N N   . GLY A 130 ? 0.75831 0.90881 0.91342 -0.15032 -0.05108 -0.04179 130 GLY A N   
996  C CA  . GLY A 130 ? 0.81550 0.93809 0.96187 -0.17058 -0.04774 -0.04648 130 GLY A CA  
997  C C   . GLY A 130 ? 0.86951 0.95621 0.98733 -0.17167 -0.05490 -0.05523 130 GLY A C   
998  O O   . GLY A 130 ? 0.88515 0.93113 0.98340 -0.17590 -0.04813 -0.05576 130 GLY A O   
999  N N   . GLY A 131 ? 0.75992 0.86133 0.87411 -0.16669 -0.06835 -0.06187 131 GLY A N   
1000 C CA  . GLY A 131 ? 0.73059 0.80150 0.81670 -0.16631 -0.07512 -0.07119 131 GLY A CA  
1001 C C   . GLY A 131 ? 0.69175 0.73846 0.75512 -0.14446 -0.07039 -0.06643 131 GLY A C   
1002 O O   . GLY A 131 ? 0.67232 0.71431 0.73792 -0.13320 -0.06009 -0.05654 131 GLY A O   
1003 N N   . PRO A 132 ? 0.66551 0.69771 0.70638 -0.13862 -0.07776 -0.07381 132 PRO A N   
1004 C CA  . PRO A 132 ? 0.64697 0.65800 0.66720 -0.11889 -0.07281 -0.06956 132 PRO A CA  
1005 C C   . PRO A 132 ? 0.59406 0.63254 0.62456 -0.10168 -0.07345 -0.05999 132 PRO A C   
1006 O O   . PRO A 132 ? 0.57500 0.64715 0.62003 -0.10121 -0.08216 -0.05945 132 PRO A O   
1007 C CB  . PRO A 132 ? 0.66719 0.66110 0.66238 -0.11939 -0.08087 -0.08116 132 PRO A CB  
1008 C CG  . PRO A 132 ? 0.68119 0.70315 0.68748 -0.13368 -0.09412 -0.08926 132 PRO A CG  
1009 C CD  . PRO A 132 ? 0.67856 0.71452 0.71136 -0.15029 -0.09084 -0.08688 132 PRO A CD  
1010 N N   . PHE A 133 ? 0.53037 0.55353 0.55314 -0.08729 -0.06435 -0.05237 133 PHE A N   
1011 C CA  . PHE A 133 ? 0.50685 0.54774 0.53566 -0.07084 -0.06349 -0.04363 133 PHE A CA  
1012 C C   . PHE A 133 ? 0.49009 0.51947 0.49693 -0.05900 -0.06657 -0.04502 133 PHE A C   
1013 O O   . PHE A 133 ? 0.47931 0.48100 0.46848 -0.05490 -0.06077 -0.04644 133 PHE A O   
1014 C CB  . PHE A 133 ? 0.47587 0.50926 0.51087 -0.06417 -0.05174 -0.03494 133 PHE A CB  
1015 C CG  . PHE A 133 ? 0.45152 0.49782 0.49128 -0.04830 -0.05002 -0.02703 133 PHE A CG  
1016 C CD1 . PHE A 133 ? 0.43718 0.51367 0.49642 -0.04499 -0.05331 -0.02325 133 PHE A CD1 
1017 C CD2 . PHE A 133 ? 0.44603 0.47402 0.47177 -0.03681 -0.04476 -0.02341 133 PHE A CD2 
1018 C CE1 . PHE A 133 ? 0.41854 0.50209 0.48088 -0.03038 -0.05115 -0.01620 133 PHE A CE1 
1019 C CE2 . PHE A 133 ? 0.42229 0.45944 0.45229 -0.02422 -0.04288 -0.01658 133 PHE A CE2 
1020 C CZ  . PHE A 133 ? 0.40948 0.47209 0.45674 -0.02099 -0.04589 -0.01306 133 PHE A CZ  
1021 N N   . VAL A 134 ? 0.46969 0.52128 0.47762 -0.05315 -0.07543 -0.04409 134 VAL A N   
1022 C CA  . VAL A 134 ? 0.47413 0.51864 0.46112 -0.04192 -0.07805 -0.04389 134 VAL A CA  
1023 C C   . VAL A 134 ? 0.45961 0.52730 0.45615 -0.02944 -0.08072 -0.03401 134 VAL A C   
1024 O O   . VAL A 134 ? 0.46558 0.56054 0.47620 -0.03117 -0.08936 -0.03307 134 VAL A O   
1025 C CB  . VAL A 134 ? 0.51254 0.55537 0.48220 -0.04915 -0.08826 -0.05488 134 VAL A CB  
1026 C CG1 . VAL A 134 ? 0.49159 0.52583 0.43711 -0.03676 -0.08855 -0.05390 134 VAL A CG1 
1027 C CG2 . VAL A 134 ? 0.51826 0.53610 0.47971 -0.06301 -0.08603 -0.06571 134 VAL A CG2 
1028 N N   . VAL A 135 ? 0.43241 0.48959 0.42227 -0.01692 -0.07340 -0.02648 135 VAL A N   
1029 C CA  . VAL A 135 ? 0.45908 0.53162 0.45430 -0.00465 -0.07508 -0.01677 135 VAL A CA  
1030 C C   . VAL A 135 ? 0.45116 0.50893 0.42518 0.00506  -0.07174 -0.01311 135 VAL A C   
1031 O O   . VAL A 135 ? 0.46896 0.50568 0.43066 0.00479  -0.06454 -0.01596 135 VAL A O   
1032 C CB  . VAL A 135 ? 0.42235 0.50043 0.43795 0.00012  -0.06774 -0.00933 135 VAL A CB  
1033 C CG1 . VAL A 135 ? 0.43651 0.53448 0.47452 -0.00838 -0.07027 -0.01181 135 VAL A CG1 
1034 C CG2 . VAL A 135 ? 0.44645 0.50116 0.45703 0.00096  -0.05641 -0.00853 135 VAL A CG2 
1035 N N   . ASP A 136 ? 0.44155 0.51151 0.41177 0.01407  -0.07673 -0.00604 136 ASP A N   
1036 C CA  . ASP A 136 ? 0.46200 0.52055 0.41543 0.02376  -0.07186 0.00065  136 ASP A CA  
1037 C C   . ASP A 136 ? 0.43534 0.48943 0.40162 0.03085  -0.06322 0.01006  136 ASP A C   
1038 O O   . ASP A 136 ? 0.42718 0.49408 0.41047 0.03451  -0.06520 0.01520  136 ASP A O   
1039 C CB  . ASP A 136 ? 0.47706 0.54854 0.41747 0.02992  -0.08110 0.00506  136 ASP A CB  
1040 C CG  . ASP A 136 ? 0.50229 0.57175 0.42068 0.02414  -0.08767 -0.00498 136 ASP A CG  
1041 O OD1 . ASP A 136 ? 0.51614 0.56655 0.42209 0.02035  -0.08101 -0.01224 136 ASP A OD1 
1042 O OD2 . ASP A 136 ? 0.52739 0.61436 0.44048 0.02389  -0.09971 -0.00605 136 ASP A OD2 
1043 N N   . VAL A 137 ? 0.41595 0.45259 0.37460 0.03276  -0.05368 0.01158  137 VAL A N   
1044 C CA  . VAL A 137 ? 0.44216 0.47246 0.41112 0.03749  -0.04556 0.01877  137 VAL A CA  
1045 C C   . VAL A 137 ? 0.44193 0.46897 0.40015 0.04561  -0.04362 0.02841  137 VAL A C   
1046 O O   . VAL A 137 ? 0.44169 0.46155 0.38281 0.04638  -0.04070 0.02857  137 VAL A O   
1047 C CB  . VAL A 137 ? 0.42760 0.44358 0.39735 0.03361  -0.03700 0.01479  137 VAL A CB  
1048 C CG1 . VAL A 137 ? 0.41852 0.42973 0.39901 0.03699  -0.03010 0.02081  137 VAL A CG1 
1049 C CG2 . VAL A 137 ? 0.40246 0.41865 0.37933 0.02537  -0.03860 0.00653  137 VAL A CG2 
1050 N N   . VAL A 138 ? 0.42512 0.45659 0.39299 0.05199  -0.04439 0.03672  138 VAL A N   
1051 C CA  . VAL A 138 ? 0.45161 0.47842 0.40988 0.05988  -0.04291 0.04785  138 VAL A CA  
1052 C C   . VAL A 138 ? 0.47393 0.48827 0.44270 0.06194  -0.03417 0.05323  138 VAL A C   
1053 O O   . VAL A 138 ? 0.44969 0.46641 0.43475 0.06358  -0.03414 0.05271  138 VAL A O   
1054 C CB  . VAL A 138 ? 0.47724 0.51847 0.43551 0.06716  -0.05283 0.05388  138 VAL A CB  
1055 C CG1 . VAL A 138 ? 0.50386 0.53678 0.45086 0.07604  -0.05057 0.06732  138 VAL A CG1 
1056 C CG2 . VAL A 138 ? 0.48068 0.53541 0.42773 0.06339  -0.06277 0.04702  138 VAL A CG2 
1057 N N   . ILE A 139 ? 0.44078 0.44254 0.40029 0.06137  -0.02650 0.05778  139 ILE A N   
1058 C CA  . ILE A 139 ? 0.43976 0.42850 0.40777 0.06081  -0.01827 0.06173  139 ILE A CA  
1059 C C   . ILE A 139 ? 0.49915 0.47893 0.45885 0.06684  -0.01605 0.07452  139 ILE A C   
1060 O O   . ILE A 139 ? 0.45515 0.43246 0.39937 0.06669  -0.01330 0.07983  139 ILE A O   
1061 C CB  . ILE A 139 ? 0.43119 0.41415 0.39842 0.05375  -0.01083 0.05695  139 ILE A CB  
1062 C CG1 . ILE A 139 ? 0.42871 0.41784 0.40099 0.04892  -0.01310 0.04579  139 ILE A CG1 
1063 C CG2 . ILE A 139 ? 0.47659 0.44810 0.45362 0.05142  -0.00381 0.05975  139 ILE A CG2 
1064 C CD1 . ILE A 139 ? 0.42462 0.40996 0.39548 0.04435  -0.00686 0.04170  139 ILE A CD1 
1065 N N   . ASN A 140 ? 0.45677 0.43037 0.42583 0.07256  -0.01631 0.07981  140 ASN A N   
1066 C CA  . ASN A 140 ? 0.48771 0.44861 0.44912 0.07932  -0.01407 0.09325  140 ASN A CA  
1067 C C   . ASN A 140 ? 0.53391 0.50296 0.47691 0.08489  -0.01991 0.10103  140 ASN A C   
1068 O O   . ASN A 140 ? 0.50513 0.46457 0.43304 0.08562  -0.01525 0.11108  140 ASN A O   
1069 C CB  . ASN A 140 ? 0.47021 0.41300 0.42966 0.07274  -0.00336 0.09710  140 ASN A CB  
1070 C CG  . ASN A 140 ? 0.50539 0.44009 0.48107 0.06720  0.00117  0.08912  140 ASN A CG  
1071 O OD1 . ASN A 140 ? 0.46496 0.39844 0.45150 0.07200  -0.00126 0.08613  140 ASN A OD1 
1072 N ND2 . ASN A 140 ? 0.48690 0.41796 0.46416 0.05745  0.00769  0.08532  140 ASN A ND2 
1073 N N   . ASP A 141 ? 0.53040 0.51830 0.47422 0.08798  -0.03022 0.09607  141 ASP A N   
1074 C CA  . ASP A 141 ? 0.55241 0.55274 0.47942 0.09323  -0.03903 0.10074  141 ASP A CA  
1075 C C   . ASP A 141 ? 0.54762 0.55027 0.45556 0.08667  -0.03718 0.09611  141 ASP A C   
1076 O O   . ASP A 141 ? 0.60941 0.62123 0.49925 0.09020  -0.04402 0.09887  141 ASP A O   
1077 C CB  . ASP A 141 ? 0.59407 0.58592 0.51031 0.10423  -0.03986 0.11756  141 ASP A CB  
1078 C CG  . ASP A 141 ? 0.67109 0.66059 0.60483 0.11392  -0.04235 0.12248  141 ASP A CG  
1079 O OD1 . ASP A 141 ? 0.63531 0.63920 0.58769 0.11385  -0.04717 0.11309  141 ASP A OD1 
1080 O OD2 . ASP A 141 ? 0.80359 0.77600 0.73223 0.12189  -0.03867 0.13598  141 ASP A OD2 
1081 N N   . ILE A 142 ? 0.52740 0.52302 0.43821 0.07815  -0.02849 0.08884  142 ILE A N   
1082 C CA  . ILE A 142 ? 0.56193 0.55950 0.45652 0.07334  -0.02530 0.08325  142 ILE A CA  
1083 C C   . ILE A 142 ? 0.55487 0.56193 0.45522 0.06794  -0.03087 0.06812  142 ILE A C   
1084 O O   . ILE A 142 ? 0.45930 0.46477 0.37766 0.06354  -0.02899 0.06140  142 ILE A O   
1085 C CB  . ILE A 142 ? 0.61691 0.60298 0.51282 0.06827  -0.01215 0.08511  142 ILE A CB  
1086 C CG1 . ILE A 142 ? 0.70031 0.67391 0.59348 0.07114  -0.00570 0.10020  142 ILE A CG1 
1087 C CG2 . ILE A 142 ? 0.64818 0.63783 0.52746 0.06567  -0.00776 0.07981  142 ILE A CG2 
1088 C CD1 . ILE A 142 ? 0.74958 0.71289 0.65447 0.06392  0.00577  0.10080  142 ILE A CD1 
1089 N N   . HIS A 143 ? 0.51783 0.53327 0.40152 0.06771  -0.03748 0.06256  143 HIS A N   
1090 C CA  A HIS A 143 ? 0.53411 0.55436 0.42105 0.06120  -0.04188 0.04789  143 HIS A CA  
1091 C CA  B HIS A 143 ? 0.54761 0.56788 0.43459 0.06123  -0.04190 0.04795  143 HIS A CA  
1092 C C   . HIS A 143 ? 0.54439 0.55413 0.43154 0.05671  -0.03155 0.04148  143 HIS A C   
1093 O O   . HIS A 143 ? 0.50893 0.51433 0.37968 0.05811  -0.02503 0.04241  143 HIS A O   
1094 C CB  A HIS A 143 ? 0.56086 0.59014 0.42783 0.06095  -0.05142 0.04198  143 HIS A CB  
1095 C CB  B HIS A 143 ? 0.53835 0.56800 0.40535 0.06132  -0.05167 0.04263  143 HIS A CB  
1096 C CG  A HIS A 143 ? 0.55074 0.57971 0.41844 0.05291  -0.05453 0.02637  143 HIS A CG  
1097 C CG  B HIS A 143 ? 0.55534 0.60063 0.42658 0.06513  -0.06440 0.04695  143 HIS A CG  
1098 N ND1 A HIS A 143 ? 0.55226 0.56937 0.40990 0.05016  -0.04663 0.01839  143 HIS A ND1 
1099 N ND1 B HIS A 143 ? 0.57542 0.63472 0.45094 0.06010  -0.07603 0.03698  143 HIS A ND1 
1100 C CD2 A HIS A 143 ? 0.53649 0.57447 0.41487 0.04690  -0.06392 0.01772  143 HIS A CD2 
1101 C CD2 B HIS A 143 ? 0.56532 0.61514 0.43875 0.07381  -0.06735 0.06049  143 HIS A CD2 
1102 C CE1 A HIS A 143 ? 0.55640 0.57181 0.41646 0.04320  -0.05119 0.00567  143 HIS A CE1 
1103 C CE1 B HIS A 143 ? 0.58173 0.65724 0.46307 0.06589  -0.08612 0.04411  143 HIS A CE1 
1104 N NE2 A HIS A 143 ? 0.53768 0.56580 0.41042 0.03997  -0.06156 0.00501  143 HIS A NE2 
1105 N NE2 B HIS A 143 ? 0.57339 0.64243 0.45297 0.07530  -0.08105 0.05869  143 HIS A NE2 
1106 N N   . PHE A 144 ? 0.44536 0.45240 0.35092 0.05211  -0.02983 0.03546  144 PHE A N   
1107 C CA  . PHE A 144 ? 0.47576 0.47433 0.38484 0.04920  -0.02095 0.03072  144 PHE A CA  
1108 C C   . PHE A 144 ? 0.46515 0.46049 0.36811 0.04539  -0.02283 0.01826  144 PHE A C   
1109 O O   . PHE A 144 ? 0.45965 0.44888 0.35298 0.04658  -0.01631 0.01459  144 PHE A O   
1110 C CB  . PHE A 144 ? 0.43153 0.42738 0.36211 0.04708  -0.01753 0.03263  144 PHE A CB  
1111 C CG  . PHE A 144 ? 0.41651 0.40652 0.35209 0.04470  -0.01000 0.02866  144 PHE A CG  
1112 C CD1 . PHE A 144 ? 0.41490 0.40311 0.34796 0.04615  -0.00153 0.03363  144 PHE A CD1 
1113 C CD2 . PHE A 144 ? 0.41684 0.40438 0.36009 0.04107  -0.01133 0.02077  144 PHE A CD2 
1114 C CE1 . PHE A 144 ? 0.42326 0.41011 0.36295 0.04486  0.00445  0.03023  144 PHE A CE1 
1115 C CE2 . PHE A 144 ? 0.43240 0.41551 0.37988 0.04052  -0.00533 0.01823  144 PHE A CE2 
1116 C CZ  . PHE A 144 ? 0.41997 0.40413 0.36641 0.04285  0.00203  0.02267  144 PHE A CZ  
1117 N N   . GLU A 145 ? 0.43651 0.43540 0.34527 0.04084  -0.03100 0.01172  145 GLU A N   
1118 C CA  . GLU A 145 ? 0.45689 0.44855 0.36002 0.03582  -0.03244 -0.00003 145 GLU A CA  
1119 C C   . GLU A 145 ? 0.43801 0.43784 0.34661 0.02947  -0.04301 -0.00535 145 GLU A C   
1120 O O   . GLU A 145 ? 0.44571 0.45773 0.36852 0.02963  -0.04754 0.00011  145 GLU A O   
1121 C CB  . GLU A 145 ? 0.43612 0.41798 0.35074 0.03415  -0.02541 -0.00226 145 GLU A CB  
1122 C CG  . GLU A 145 ? 0.40791 0.39426 0.34332 0.03033  -0.02722 0.00021  145 GLU A CG  
1123 C CD  . GLU A 145 ? 0.41851 0.39636 0.36306 0.02933  -0.02089 -0.00057 145 GLU A CD  
1124 O OE1 . GLU A 145 ? 0.41205 0.38120 0.34907 0.03213  -0.01555 -0.00286 145 GLU A OE1 
1125 O OE2 . GLU A 145 ? 0.36852 0.34955 0.32753 0.02656  -0.02124 0.00130  145 GLU A OE2 
1126 N N   . ARG A 146 ? 0.44525 0.43842 0.34299 0.02384  -0.04659 -0.01643 146 ARG A N   
1127 C CA  . ARG A 146 ? 0.49546 0.49459 0.40139 0.01441  -0.05530 -0.02336 146 ARG A CA  
1128 C C   . ARG A 146 ? 0.46685 0.45211 0.38245 0.00828  -0.05015 -0.02817 146 ARG A C   
1129 O O   . ARG A 146 ? 0.47944 0.44638 0.38277 0.00796  -0.04553 -0.03476 146 ARG A O   
1130 C CB  . ARG A 146 ? 0.53060 0.53033 0.41733 0.00994  -0.06383 -0.03328 146 ARG A CB  
1131 C CG  . ARG A 146 ? 0.53783 0.54517 0.43488 -0.00234 -0.07319 -0.04125 146 ARG A CG  
1132 C CD  . ARG A 146 ? 0.59156 0.60858 0.47241 -0.00658 -0.08517 -0.04910 146 ARG A CD  
1133 N NE  . ARG A 146 ? 0.55247 0.59273 0.43463 0.00066  -0.09244 -0.03971 146 ARG A NE  
1134 C CZ  . ARG A 146 ? 0.61343 0.66844 0.48301 -0.00095 -0.10465 -0.04347 146 ARG A CZ  
1135 N NH1 . ARG A 146 ? 0.63028 0.67921 0.48432 -0.01080 -0.11122 -0.05798 146 ARG A NH1 
1136 N NH2 . ARG A 146 ? 0.58336 0.65875 0.45500 0.00769  -0.11079 -0.03251 146 ARG A NH2 
1137 N N   . PHE A 147 ? 0.45804 0.45150 0.39451 0.00446  -0.05041 -0.02443 147 PHE A N   
1138 C CA  . PHE A 147 ? 0.41970 0.40099 0.36508 -0.00059 -0.04478 -0.02626 147 PHE A CA  
1139 C C   . PHE A 147 ? 0.42047 0.40038 0.36897 -0.01329 -0.05014 -0.03452 147 PHE A C   
1140 O O   . PHE A 147 ? 0.44292 0.44207 0.40393 -0.01898 -0.05699 -0.03447 147 PHE A O   
1141 C CB  . PHE A 147 ? 0.42820 0.41785 0.39232 0.00209  -0.04042 -0.01781 147 PHE A CB  
1142 C CG  . PHE A 147 ? 0.38206 0.35982 0.35251 -0.00240 -0.03458 -0.01855 147 PHE A CG  
1143 C CD1 . PHE A 147 ? 0.40683 0.37026 0.37165 0.00310  -0.02748 -0.01653 147 PHE A CD1 
1144 C CD2 . PHE A 147 ? 0.41613 0.39824 0.39779 -0.01220 -0.03626 -0.02079 147 PHE A CD2 
1145 C CE1 . PHE A 147 ? 0.43156 0.38402 0.39996 0.00010  -0.02292 -0.01608 147 PHE A CE1 
1146 C CE2 . PHE A 147 ? 0.40811 0.37775 0.39278 -0.01624 -0.03031 -0.02011 147 PHE A CE2 
1147 C CZ  . PHE A 147 ? 0.40090 0.35506 0.37783 -0.00949 -0.02409 -0.01751 147 PHE A CZ  
1148 N N   . ARG A 148 ? 0.37765 0.33494 0.31600 -0.01766 -0.04665 -0.04122 148 ARG A N   
1149 C CA  . ARG A 148 ? 0.46038 0.40989 0.40175 -0.03137 -0.04940 -0.04846 148 ARG A CA  
1150 C C   . ARG A 148 ? 0.48793 0.42001 0.43434 -0.03257 -0.04076 -0.04499 148 ARG A C   
1151 O O   . ARG A 148 ? 0.50746 0.42125 0.44336 -0.02426 -0.03432 -0.04384 148 ARG A O   
1152 C CB  . ARG A 148 ? 0.53626 0.46845 0.45700 -0.03636 -0.05333 -0.06060 148 ARG A CB  
1153 C CG  . ARG A 148 ? 0.56389 0.51215 0.47558 -0.03687 -0.06320 -0.06557 148 ARG A CG  
1154 C CD  . ARG A 148 ? 0.64201 0.56885 0.53049 -0.04229 -0.06600 -0.07948 148 ARG A CD  
1155 N NE  . ARG A 148 ? 0.67851 0.62186 0.55619 -0.04449 -0.07704 -0.08545 148 ARG A NE  
1156 C CZ  . ARG A 148 ? 0.67263 0.62552 0.53716 -0.03279 -0.07794 -0.08185 148 ARG A CZ  
1157 N NH1 . ARG A 148 ? 0.65819 0.60699 0.52097 -0.01921 -0.06823 -0.07265 148 ARG A NH1 
1158 N NH2 . ARG A 148 ? 0.67809 0.64577 0.53073 -0.03540 -0.08899 -0.08727 148 ARG A NH2 
1159 N N   . GLY A 149 ? 0.45911 0.39844 0.42148 -0.04235 -0.04047 -0.04281 149 GLY A N   
1160 C CA  . GLY A 149 ? 0.47438 0.39797 0.43981 -0.04372 -0.03234 -0.03819 149 GLY A CA  
1161 C C   . GLY A 149 ? 0.45260 0.39279 0.43762 -0.05325 -0.03144 -0.03410 149 GLY A C   
1162 O O   . GLY A 149 ? 0.46416 0.42397 0.46041 -0.06213 -0.03755 -0.03732 149 GLY A O   
1163 N N   . ASP A 150 ? 0.44663 0.38065 0.43554 -0.05091 -0.02369 -0.02693 150 ASP A N   
1164 C CA  . ASP A 150 ? 0.45453 0.40350 0.46029 -0.05917 -0.02050 -0.02260 150 ASP A CA  
1165 C C   . ASP A 150 ? 0.43136 0.40996 0.45268 -0.05240 -0.02158 -0.01844 150 ASP A C   
1166 O O   . ASP A 150 ? 0.44959 0.44946 0.48796 -0.05935 -0.02179 -0.01767 150 ASP A O   
1167 C CB  . ASP A 150 ? 0.41876 0.34968 0.41968 -0.05873 -0.01167 -0.01619 150 ASP A CB  
1168 C CG  . ASP A 150 ? 0.47354 0.37568 0.46324 -0.06855 -0.00955 -0.01877 150 ASP A CG  
1169 O OD1 . ASP A 150 ? 0.47322 0.36934 0.45948 -0.07697 -0.01490 -0.02701 150 ASP A OD1 
1170 O OD2 . ASP A 150 ? 0.46684 0.35108 0.44991 -0.06782 -0.00277 -0.01261 150 ASP A OD2 
1171 N N   . GLY A 151 ? 0.36602 0.34618 0.38260 -0.03905 -0.02163 -0.01567 151 GLY A N   
1172 C CA  . GLY A 151 ? 0.39046 0.39326 0.41990 -0.03183 -0.02206 -0.01170 151 GLY A CA  
1173 C C   . GLY A 151 ? 0.37752 0.37357 0.39998 -0.01940 -0.01884 -0.00758 151 GLY A C   
1174 O O   . GLY A 151 ? 0.38028 0.35847 0.38922 -0.01563 -0.01728 -0.00788 151 GLY A O   
1175 N N   . LEU A 152 ? 0.35400 0.36526 0.38703 -0.01317 -0.01770 -0.00400 152 LEU A N   
1176 C CA  . LEU A 152 ? 0.34228 0.34973 0.37136 -0.00296 -0.01541 -0.00056 152 LEU A CA  
1177 C C   . LEU A 152 ? 0.36746 0.38184 0.40592 -0.00047 -0.00986 0.00215  152 LEU A C   
1178 O O   . LEU A 152 ? 0.36024 0.38903 0.41116 -0.00341 -0.00871 0.00200  152 LEU A O   
1179 C CB  . LEU A 152 ? 0.35890 0.37435 0.38769 0.00358  -0.02062 0.00053  152 LEU A CB  
1180 C CG  . LEU A 152 ? 0.34980 0.35725 0.36482 0.00332  -0.02515 -0.00229 152 LEU A CG  
1181 C CD1 . LEU A 152 ? 0.36370 0.38349 0.37878 0.00804  -0.03141 -0.00066 152 LEU A CD1 
1182 C CD2 . LEU A 152 ? 0.35639 0.34811 0.35968 0.00808  -0.02086 -0.00119 152 LEU A CD2 
1183 N N   . CYS A 153 ? 0.31951 0.32485 0.35209 0.00492  -0.00634 0.00400  153 CYS A N   
1184 C CA  . CYS A 153 ? 0.36530 0.37381 0.40265 0.00746  -0.00109 0.00503  153 CYS A CA  
1185 C C   . CYS A 153 ? 0.35475 0.36030 0.39090 0.01494  -0.00106 0.00625  153 CYS A C   
1186 O O   . CYS A 153 ? 0.36752 0.36394 0.39552 0.01659  -0.00214 0.00703  153 CYS A O   
1187 C CB  . CYS A 153 ? 0.34522 0.34377 0.37446 0.00392  0.00321  0.00546  153 CYS A CB  
1188 S SG  . CYS A 153 ? 0.34767 0.34744 0.37637 0.00716  0.00914  0.00540  153 CYS A SG  
1189 N N   . MET A 154 ? 0.33202 0.34501 0.37689 0.01945  0.00070  0.00646  154 MET A N   
1190 C CA  . MET A 154 ? 0.35164 0.35833 0.39541 0.02548  0.00170  0.00748  154 MET A CA  
1191 C C   . MET A 154 ? 0.34693 0.35095 0.39107 0.02626  0.00730  0.00466  154 MET A C   
1192 O O   . MET A 154 ? 0.32216 0.33472 0.37394 0.02798  0.01068  0.00314  154 MET A O   
1193 C CB  . MET A 154 ? 0.35136 0.36419 0.40235 0.03189  -0.00092 0.01024  154 MET A CB  
1194 C CG  . MET A 154 ? 0.37883 0.38035 0.42683 0.03703  0.00044  0.01243  154 MET A CG  
1195 S SD  . MET A 154 ? 0.37445 0.36577 0.41103 0.03428  -0.00152 0.01507  154 MET A SD  
1196 C CE  . MET A 154 ? 0.38163 0.37809 0.41715 0.03915  -0.00666 0.02068  154 MET A CE  
1197 N N   . SER A 155 ? 0.35555 0.34937 0.39165 0.02514  0.00825  0.00351  155 SER A N   
1198 C CA  . SER A 155 ? 0.33503 0.32560 0.36708 0.02424  0.01240  -0.00033 155 SER A CA  
1199 C C   . SER A 155 ? 0.37761 0.35937 0.40932 0.02722  0.01367  -0.00273 155 SER A C   
1200 O O   . SER A 155 ? 0.35640 0.33220 0.38791 0.02750  0.01120  -0.00040 155 SER A O   
1201 C CB  . SER A 155 ? 0.33877 0.32582 0.36095 0.01968  0.01129  -0.00024 155 SER A CB  
1202 O OG  . SER A 155 ? 0.37272 0.35765 0.38841 0.01873  0.01417  -0.00394 155 SER A OG  
1203 N N   . THR A 156 ? 0.31772 0.29774 0.34871 0.02902  0.01828  -0.00762 156 THR A N   
1204 C CA  . THR A 156 ? 0.35327 0.32125 0.38056 0.02969  0.01987  -0.01224 156 THR A CA  
1205 C C   . THR A 156 ? 0.36236 0.32709 0.38025 0.02312  0.01716  -0.01461 156 THR A C   
1206 O O   . THR A 156 ? 0.36353 0.33491 0.37701 0.02014  0.01512  -0.01252 156 THR A O   
1207 C CB  . THR A 156 ? 0.38221 0.34900 0.40915 0.03394  0.02614  -0.01839 156 THR A CB  
1208 O OG1 . THR A 156 ? 0.34010 0.31316 0.35875 0.03018  0.02831  -0.02131 156 THR A OG1 
1209 C CG2 . THR A 156 ? 0.38081 0.35638 0.41972 0.04156  0.02888  -0.01579 156 THR A CG2 
1210 N N   . PRO A 157 ? 0.36155 0.31607 0.37650 0.02071  0.01686  -0.01899 157 PRO A N   
1211 C CA  . PRO A 157 ? 0.38507 0.34074 0.39230 0.01425  0.01338  -0.02225 157 PRO A CA  
1212 C C   . PRO A 157 ? 0.36852 0.32962 0.36542 0.01358  0.01453  -0.02611 157 PRO A C   
1213 O O   . PRO A 157 ? 0.33542 0.30391 0.32712 0.01124  0.01095  -0.02327 157 PRO A O   
1214 C CB  . PRO A 157 ? 0.40860 0.35145 0.41565 0.01082  0.01365  -0.02792 157 PRO A CB  
1215 C CG  . PRO A 157 ? 0.42225 0.35681 0.43777 0.01519  0.01597  -0.02317 157 PRO A CG  
1216 C CD  . PRO A 157 ? 0.38291 0.32412 0.40196 0.02301  0.01878  -0.02017 157 PRO A CD  
1217 N N   . SER A 158 ? 0.37700 0.33434 0.36985 0.01647  0.02003  -0.03202 158 SER A N   
1218 C CA  . SER A 158 ? 0.40622 0.36918 0.38695 0.01575  0.02224  -0.03496 158 SER A CA  
1219 C C   . SER A 158 ? 0.37616 0.34945 0.35881 0.01686  0.02366  -0.02721 158 SER A C   
1220 O O   . SER A 158 ? 0.39851 0.37630 0.37034 0.01482  0.02365  -0.02563 158 SER A O   
1221 C CB  . SER A 158 ? 0.41245 0.36945 0.38765 0.01926  0.02937  -0.04376 158 SER A CB  
1222 O OG  . SER A 158 ? 0.39181 0.35003 0.37873 0.02618  0.03523  -0.04193 158 SER A OG  
1223 N N   . GLY A 159 ? 0.38456 0.36094 0.37996 0.01949  0.02438  -0.02202 159 GLY A N   
1224 C CA  . GLY A 159 ? 0.36806 0.35246 0.36591 0.01832  0.02466  -0.01539 159 GLY A CA  
1225 C C   . GLY A 159 ? 0.35195 0.33543 0.34576 0.01525  0.01868  -0.01016 159 GLY A C   
1226 O O   . GLY A 159 ? 0.36313 0.34914 0.35539 0.01355  0.01918  -0.00528 159 GLY A O   
1227 N N   . THR A 160 ? 0.35632 0.33614 0.34900 0.01446  0.01358  -0.01107 160 THR A N   
1228 C CA  . THR A 160 ? 0.34194 0.32278 0.33355 0.01369  0.00865  -0.00591 160 THR A CA  
1229 C C   . THR A 160 ? 0.38942 0.37144 0.36923 0.01297  0.00772  -0.00316 160 THR A C   
1230 O O   . THR A 160 ? 0.36526 0.34622 0.34379 0.01395  0.00528  0.00218  160 THR A O   
1231 C CB  . THR A 160 ? 0.36585 0.34646 0.36109 0.01279  0.00423  -0.00707 160 THR A CB  
1232 O OG1 . THR A 160 ? 0.33859 0.31921 0.32822 0.01008  0.00282  -0.01288 160 THR A OG1 
1233 C CG2 . THR A 160 ? 0.39030 0.36757 0.39565 0.01381  0.00535  -0.00675 160 THR A CG2 
1234 N N   . THR A 161 ? 0.35890 0.34178 0.32853 0.01202  0.00998  -0.00647 161 THR A N   
1235 C CA  . THR A 161 ? 0.41419 0.39757 0.36985 0.01188  0.00952  -0.00242 161 THR A CA  
1236 C C   . THR A 161 ? 0.41946 0.40113 0.37256 0.01074  0.01592  0.00234  161 THR A C   
1237 O O   . THR A 161 ? 0.43439 0.41422 0.37428 0.01029  0.01703  0.00706  161 THR A O   
1238 C CB  . THR A 161 ? 0.40938 0.39513 0.35199 0.01095  0.00877  -0.00817 161 THR A CB  
1239 O OG1 . THR A 161 ? 0.38918 0.37360 0.33375 0.01048  0.01470  -0.01569 161 THR A OG1 
1240 C CG2 . THR A 161 ? 0.43275 0.42224 0.37646 0.01016  0.00059  -0.01130 161 THR A CG2 
1241 N N   . ALA A 162 ? 0.41624 0.39919 0.38169 0.00987  0.01984  0.00188  162 ALA A N   
1242 C CA  . ALA A 162 ? 0.41702 0.40176 0.38379 0.00683  0.02627  0.00543  162 ALA A CA  
1243 C C   . ALA A 162 ? 0.41270 0.39299 0.38619 0.00478  0.02375  0.01041  162 ALA A C   
1244 O O   . ALA A 162 ? 0.37881 0.35140 0.34583 0.00611  0.01917  0.01414  162 ALA A O   
1245 C CB  . ALA A 162 ? 0.42675 0.41980 0.40323 0.00755  0.03241  0.00022  162 ALA A CB  
1246 N N   . TYR A 163 ? 0.40250 0.38791 0.38849 0.00197  0.02629  0.01007  163 TYR A N   
1247 C CA  . TYR A 163 ? 0.40415 0.38475 0.39506 -0.00123 0.02348  0.01295  163 TYR A CA  
1248 C C   . TYR A 163 ? 0.36593 0.33992 0.35599 0.00304  0.01660  0.01251  163 TYR A C   
1249 O O   . TYR A 163 ? 0.35833 0.32226 0.34306 0.00261  0.01427  0.01549  163 TYR A O   
1250 C CB  . TYR A 163 ? 0.42209 0.41432 0.42889 -0.00406 0.02512  0.01068  163 TYR A CB  
1251 C CG  . TYR A 163 ? 0.42627 0.41653 0.43776 -0.01121 0.02417  0.01266  163 TYR A CG  
1252 C CD1 . TYR A 163 ? 0.43901 0.41301 0.44009 -0.01388 0.02209  0.01585  163 TYR A CD1 
1253 C CD2 . TYR A 163 ? 0.44534 0.45024 0.47222 -0.01517 0.02506  0.01083  163 TYR A CD2 
1254 C CE1 . TYR A 163 ? 0.43349 0.40257 0.43778 -0.02165 0.02124  0.01614  163 TYR A CE1 
1255 C CE2 . TYR A 163 ? 0.46128 0.46542 0.49294 -0.02362 0.02325  0.01128  163 TYR A CE2 
1256 C CZ  . TYR A 163 ? 0.45885 0.44349 0.47843 -0.02750 0.02150  0.01342  163 TYR A CZ  
1257 O OH  . TYR A 163 ? 0.46398 0.44494 0.48719 -0.03709 0.01975  0.01246  163 TYR A OH  
1258 N N   . ASN A 164 ? 0.35269 0.33142 0.34779 0.00729  0.01420  0.00886  164 ASN A N   
1259 C CA  . ASN A 164 ? 0.37287 0.34820 0.36842 0.01084  0.00911  0.00873  164 ASN A CA  
1260 C C   . ASN A 164 ? 0.38708 0.35588 0.37259 0.01295  0.00674  0.01185  164 ASN A C   
1261 O O   . ASN A 164 ? 0.35098 0.31497 0.33584 0.01535  0.00407  0.01339  164 ASN A O   
1262 C CB  . ASN A 164 ? 0.33993 0.31980 0.34062 0.01350  0.00841  0.00514  164 ASN A CB  
1263 C CG  . ASN A 164 ? 0.37652 0.35488 0.37739 0.01588  0.00448  0.00558  164 ASN A CG  
1264 O OD1 . ASN A 164 ? 0.34984 0.32832 0.35582 0.01716  0.00312  0.00620  164 ASN A OD1 
1265 N ND2 . ASN A 164 ? 0.34881 0.32776 0.34419 0.01641  0.00264  0.00546  164 ASN A ND2 
1266 N N   . LYS A 165 ? 0.32569 0.29500 0.30264 0.01309  0.00764  0.01279  165 LYS A N   
1267 C CA  . LYS A 165 ? 0.36518 0.33059 0.33270 0.01660  0.00439  0.01676  165 LYS A CA  
1268 C C   . LYS A 165 ? 0.37396 0.32721 0.33564 0.01681  0.00539  0.02219  165 LYS A C   
1269 O O   . LYS A 165 ? 0.33230 0.28017 0.29152 0.02193  0.00236  0.02483  165 LYS A O   
1270 C CB  . LYS A 165 ? 0.36714 0.33624 0.32417 0.01645  0.00462  0.01686  165 LYS A CB  
1271 C CG  . LYS A 165 ? 0.39690 0.36493 0.34403 0.02129  -0.00016 0.02183  165 LYS A CG  
1272 C CD  . LYS A 165 ? 0.41707 0.39238 0.35360 0.02116  -0.00219 0.02023  165 LYS A CD  
1273 C CE  . LYS A 165 ? 0.44371 0.42305 0.37375 0.02714  -0.00931 0.02491  165 LYS A CE  
1274 N NZ  . LYS A 165 ? 0.48635 0.45382 0.40521 0.03148  -0.00828 0.03470  165 LYS A NZ  
1275 N N   . SER A 166 ? 0.36514 0.31361 0.32512 0.01118  0.01016  0.02373  166 SER A N   
1276 C CA  . SER A 166 ? 0.39383 0.32722 0.34776 0.00923  0.01172  0.02851  166 SER A CA  
1277 C C   . SER A 166 ? 0.39390 0.32118 0.35386 0.00987  0.00931  0.02572  166 SER A C   
1278 O O   . SER A 166 ? 0.39588 0.30716 0.34910 0.01057  0.00943  0.02846  166 SER A O   
1279 C CB  . SER A 166 ? 0.42280 0.35502 0.37629 0.00059  0.01802  0.03030  166 SER A CB  
1280 O OG  . SER A 166 ? 0.46056 0.39753 0.40519 0.00058  0.02135  0.03307  166 SER A OG  
1281 N N   . LEU A 167 ? 0.39155 0.32947 0.36216 0.01011  0.00736  0.02039  167 LEU A N   
1282 C CA  . LEU A 167 ? 0.35352 0.28737 0.32753 0.01091  0.00505  0.01734  167 LEU A CA  
1283 C C   . LEU A 167 ? 0.40413 0.33920 0.37744 0.01919  0.00218  0.01700  167 LEU A C   
1284 O O   . LEU A 167 ? 0.37925 0.31295 0.35424 0.02092  0.00096  0.01414  167 LEU A O   
1285 C CB  . LEU A 167 ? 0.36264 0.30798 0.34752 0.00677  0.00458  0.01310  167 LEU A CB  
1286 C CG  . LEU A 167 ? 0.37925 0.32763 0.36871 -0.00168 0.00746  0.01295  167 LEU A CG  
1287 C CD1 . LEU A 167 ? 0.40162 0.36598 0.40380 -0.00290 0.00641  0.00962  167 LEU A CD1 
1288 C CD2 . LEU A 167 ? 0.39531 0.32962 0.38003 -0.00765 0.00743  0.01286  167 LEU A CD2 
1289 N N   . GLY A 168 ? 0.37703 0.31651 0.34793 0.02407  0.00111  0.01971  168 GLY A N   
1290 C CA  . GLY A 168 ? 0.40086 0.34566 0.37399 0.03135  -0.00127 0.01979  168 GLY A CA  
1291 C C   . GLY A 168 ? 0.40452 0.36434 0.38712 0.03061  -0.00242 0.01695  168 GLY A C   
1292 O O   . GLY A 168 ? 0.39034 0.35726 0.37710 0.03511  -0.00363 0.01707  168 GLY A O   
1293 N N   . GLY A 169 ? 0.38649 0.35098 0.37309 0.02521  -0.00143 0.01459  169 GLY A N   
1294 C CA  . GLY A 169 ? 0.35066 0.32460 0.34513 0.02423  -0.00194 0.01212  169 GLY A CA  
1295 C C   . GLY A 169 ? 0.38026 0.36217 0.37541 0.02487  -0.00419 0.01189  169 GLY A C   
1296 O O   . GLY A 169 ? 0.35583 0.33783 0.34437 0.02628  -0.00580 0.01369  169 GLY A O   
1297 N N   . ALA A 170 ? 0.32522 0.31398 0.32802 0.02326  -0.00461 0.00990  170 ALA A N   
1298 C CA  . ALA A 170 ? 0.37115 0.36888 0.37644 0.02137  -0.00741 0.00814  170 ALA A CA  
1299 C C   . ALA A 170 ? 0.34846 0.34379 0.34992 0.01695  -0.00701 0.00382  170 ALA A C   
1300 O O   . ALA A 170 ? 0.35277 0.34167 0.35450 0.01558  -0.00363 0.00207  170 ALA A O   
1301 C CB  . ALA A 170 ? 0.35197 0.35674 0.36746 0.01937  -0.00712 0.00765  170 ALA A CB  
1302 N N   . LEU A 171 ? 0.37312 0.37485 0.37077 0.01540  -0.01062 0.00173  171 LEU A N   
1303 C CA  . LEU A 171 ? 0.36047 0.36005 0.35277 0.01105  -0.01027 -0.00425 171 LEU A CA  
1304 C C   . LEU A 171 ? 0.36162 0.36219 0.36243 0.00563  -0.01077 -0.00923 171 LEU A C   
1305 O O   . LEU A 171 ? 0.40487 0.41530 0.41249 0.00327  -0.01456 -0.00904 171 LEU A O   
1306 C CB  . LEU A 171 ? 0.35668 0.36231 0.33785 0.01145  -0.01464 -0.00467 171 LEU A CB  
1307 C CG  . LEU A 171 ? 0.37590 0.37926 0.34758 0.01695  -0.01460 0.00238  171 LEU A CG  
1308 C CD1 . LEU A 171 ? 0.36686 0.37559 0.32453 0.01756  -0.01895 0.00256  171 LEU A CD1 
1309 C CD2 . LEU A 171 ? 0.37557 0.36793 0.34449 0.01702  -0.00791 0.00400  171 LEU A CD2 
1310 N N   . MET A 172 ? 0.34377 0.33420 0.34515 0.00375  -0.00657 -0.01323 172 MET A N   
1311 C CA  . MET A 172 ? 0.40459 0.39012 0.41283 -0.00145 -0.00585 -0.01724 172 MET A CA  
1312 C C   . MET A 172 ? 0.43058 0.40928 0.43132 -0.00554 -0.00566 -0.02639 172 MET A C   
1313 O O   . MET A 172 ? 0.45908 0.43254 0.45144 -0.00228 -0.00237 -0.02908 172 MET A O   
1314 C CB  . MET A 172 ? 0.39056 0.36642 0.40493 0.00116  -0.00097 -0.01401 172 MET A CB  
1315 C CG  . MET A 172 ? 0.43067 0.41073 0.44862 0.00585  -0.00047 -0.00649 172 MET A CG  
1316 S SD  . MET A 172 ? 0.49280 0.46286 0.51558 0.00888  0.00369  -0.00314 172 MET A SD  
1317 C CE  . MET A 172 ? 0.45936 0.42090 0.48665 0.00238  0.00490  -0.00566 172 MET A CE  
1318 N N   . HIS A 173 ? 0.44508 0.42398 0.44890 -0.01321 -0.00864 -0.03171 173 HIS A N   
1319 C CA  . HIS A 173 ? 0.44666 0.41532 0.44222 -0.01789 -0.00823 -0.04227 173 HIS A CA  
1320 C C   . HIS A 173 ? 0.47841 0.42797 0.47470 -0.01447 -0.00083 -0.04412 173 HIS A C   
1321 O O   . HIS A 173 ? 0.49604 0.43924 0.50201 -0.01363 0.00188  -0.03867 173 HIS A O   
1322 C CB  . HIS A 173 ? 0.45256 0.42428 0.45260 -0.02887 -0.01332 -0.04830 173 HIS A CB  
1323 C CG  . HIS A 173 ? 0.49384 0.45579 0.48201 -0.03458 -0.01449 -0.06111 173 HIS A CG  
1324 N ND1 . HIS A 173 ? 0.51128 0.45061 0.49775 -0.03720 -0.00918 -0.06825 173 HIS A ND1 
1325 C CD2 . HIS A 173 ? 0.47782 0.44816 0.45308 -0.03729 -0.02019 -0.06835 173 HIS A CD2 
1326 C CE1 . HIS A 173 ? 0.53502 0.46842 0.50808 -0.04181 -0.01119 -0.08066 173 HIS A CE1 
1327 N NE2 . HIS A 173 ? 0.52318 0.47620 0.48870 -0.04231 -0.01817 -0.08097 173 HIS A NE2 
1328 N N   . PRO A 174 ? 0.48316 0.42387 0.46892 -0.01149 0.00286  -0.05134 174 PRO A N   
1329 C CA  . PRO A 174 ? 0.48662 0.41209 0.47455 -0.00495 0.01030  -0.05199 174 PRO A CA  
1330 C C   . PRO A 174 ? 0.51572 0.42150 0.50763 -0.00886 0.01238  -0.05622 174 PRO A C   
1331 O O   . PRO A 174 ? 0.54357 0.43571 0.53833 -0.00183 0.01820  -0.05519 174 PRO A O   
1332 C CB  . PRO A 174 ? 0.51292 0.43719 0.48790 -0.00081 0.01423  -0.05954 174 PRO A CB  
1333 C CG  . PRO A 174 ? 0.51336 0.45329 0.47868 -0.00412 0.00881  -0.05935 174 PRO A CG  
1334 C CD  . PRO A 174 ? 0.49753 0.44372 0.46825 -0.01235 0.00088  -0.05829 174 PRO A CD  
1335 N N   . SER A 175 ? 0.50289 0.40663 0.49561 -0.01985 0.00790  -0.06064 175 SER A N   
1336 C CA  . SER A 175 ? 0.52396 0.40689 0.52156 -0.02525 0.01047  -0.06272 175 SER A CA  
1337 C C   . SER A 175 ? 0.53383 0.41660 0.54377 -0.02322 0.01228  -0.04986 175 SER A C   
1338 O O   . SER A 175 ? 0.54813 0.41129 0.56153 -0.02586 0.01582  -0.04855 175 SER A O   
1339 C CB  . SER A 175 ? 0.54790 0.43076 0.54432 -0.04002 0.00496  -0.07142 175 SER A CB  
1340 O OG  . SER A 175 ? 0.54443 0.45250 0.54864 -0.04520 -0.00160 -0.06552 175 SER A OG  
1341 N N   . ILE A 176 ? 0.50886 0.41110 0.52372 -0.01864 0.01026  -0.04045 176 ILE A N   
1342 C CA  . ILE A 176 ? 0.49627 0.40019 0.51991 -0.01619 0.01186  -0.02882 176 ILE A CA  
1343 C C   . ILE A 176 ? 0.48915 0.38635 0.51224 -0.00393 0.01594  -0.02373 176 ILE A C   
1344 O O   . ILE A 176 ? 0.47870 0.38709 0.49961 0.00288  0.01546  -0.02333 176 ILE A O   
1345 C CB  . ILE A 176 ? 0.47482 0.40216 0.50300 -0.01713 0.00771  -0.02265 176 ILE A CB  
1346 C CG1 . ILE A 176 ? 0.45678 0.39568 0.48754 -0.02791 0.00273  -0.02775 176 ILE A CG1 
1347 C CG2 . ILE A 176 ? 0.47039 0.39892 0.50508 -0.01483 0.01007  -0.01183 176 ILE A CG2 
1348 C CD1 . ILE A 176 ? 0.44179 0.40452 0.47675 -0.02637 -0.00143 -0.02254 176 ILE A CD1 
1349 N N   . GLU A 177 ? 0.46941 0.34899 0.49491 -0.00131 0.01981  -0.01927 177 GLU A N   
1350 C CA  . GLU A 177 ? 0.49515 0.37010 0.52157 0.01128  0.02270  -0.01390 177 GLU A CA  
1351 C C   . GLU A 177 ? 0.48537 0.37609 0.51554 0.01482  0.02033  -0.00323 177 GLU A C   
1352 O O   . GLU A 177 ? 0.47075 0.35662 0.50258 0.01401  0.02110  0.00510  177 GLU A O   
1353 C CB  . GLU A 177 ? 0.53947 0.38809 0.56559 0.01431  0.02727  -0.01228 177 GLU A CB  
1354 C CG  . GLU A 177 ? 0.58039 0.40855 0.60124 0.00866  0.02983  -0.02421 177 GLU A CG  
1355 C CD  . GLU A 177 ? 0.63663 0.43473 0.65619 0.01457  0.03528  -0.02263 177 GLU A CD  
1356 O OE1 . GLU A 177 ? 0.68339 0.47545 0.70200 0.02748  0.03859  -0.02482 177 GLU A OE1 
1357 O OE2 . GLU A 177 ? 0.62755 0.40822 0.64757 0.00674  0.03675  -0.01846 177 GLU A OE2 
1358 N N   . ALA A 178 ? 0.44600 0.35451 0.47608 0.01837  0.01787  -0.00365 178 ALA A N   
1359 C CA  . ALA A 178 ? 0.42565 0.34851 0.45734 0.02024  0.01512  0.00391  178 ALA A CA  
1360 C C   . ALA A 178 ? 0.41281 0.34832 0.44488 0.02590  0.01382  0.00284  178 ALA A C   
1361 O O   . ALA A 178 ? 0.41668 0.35236 0.44804 0.02774  0.01563  -0.00318 178 ALA A O   
1362 C CB  . ALA A 178 ? 0.42466 0.35727 0.45617 0.01233  0.01277  0.00423  178 ALA A CB  
1363 N N   . MET A 179 ? 0.38976 0.33567 0.42249 0.02801  0.01119  0.00851  179 MET A N   
1364 C CA  . MET A 179 ? 0.37383 0.33234 0.40728 0.03019  0.00942  0.00774  179 MET A CA  
1365 C C   . MET A 179 ? 0.40156 0.36744 0.43158 0.02696  0.00646  0.01024  179 MET A C   
1366 O O   . MET A 179 ? 0.35287 0.31692 0.38126 0.02593  0.00603  0.01422  179 MET A O   
1367 C CB  . MET A 179 ? 0.34430 0.30723 0.38300 0.03757  0.00883  0.01111  179 MET A CB  
1368 C CG  . MET A 179 ? 0.38872 0.35041 0.42615 0.04062  0.00625  0.01877  179 MET A CG  
1369 S SD  . MET A 179 ? 0.36451 0.33445 0.40843 0.05032  0.00359  0.02326  179 MET A SD  
1370 C CE  . MET A 179 ? 0.38708 0.35347 0.42330 0.05222  0.00040  0.03249  179 MET A CE  
1371 N N   . GLN A 180 ? 0.35289 0.32603 0.38123 0.02557  0.00534  0.00804  180 GLN A N   
1372 C CA  . GLN A 180 ? 0.35852 0.33530 0.38250 0.02351  0.00317  0.00939  180 GLN A CA  
1373 C C   . GLN A 180 ? 0.37148 0.35329 0.39490 0.02417  0.00129  0.00991  180 GLN A C   
1374 O O   . GLN A 180 ? 0.34405 0.32935 0.36997 0.02332  0.00220  0.00791  180 GLN A O   
1375 C CB  . GLN A 180 ? 0.34541 0.32274 0.36587 0.02034  0.00322  0.00659  180 GLN A CB  
1376 C CG  . GLN A 180 ? 0.32443 0.30416 0.34088 0.02049  0.00145  0.00845  180 GLN A CG  
1377 C CD  . GLN A 180 ? 0.36856 0.35049 0.38220 0.01924  0.00049  0.00726  180 GLN A CD  
1378 O OE1 . GLN A 180 ? 0.32760 0.31128 0.33866 0.02113  -0.00068 0.00901  180 GLN A OE1 
1379 N NE2 . GLN A 180 ? 0.30317 0.28512 0.31647 0.01685  0.00075  0.00401  180 GLN A NE2 
1380 N N   . LEU A 181 ? 0.33251 0.31491 0.35226 0.02488  -0.00090 0.01207  181 LEU A N   
1381 C CA  . LEU A 181 ? 0.34986 0.33573 0.36802 0.02410  -0.00365 0.01141  181 LEU A CA  
1382 C C   . LEU A 181 ? 0.37004 0.35129 0.38105 0.02201  -0.00384 0.00983  181 LEU A C   
1383 O O   . LEU A 181 ? 0.34150 0.31983 0.34752 0.02398  -0.00340 0.01070  181 LEU A O   
1384 C CB  . LEU A 181 ? 0.35438 0.34287 0.37065 0.02702  -0.00654 0.01409  181 LEU A CB  
1385 C CG  . LEU A 181 ? 0.37055 0.36332 0.38360 0.02523  -0.01091 0.01216  181 LEU A CG  
1386 C CD1 . LEU A 181 ? 0.32307 0.32579 0.34610 0.02364  -0.01286 0.01100  181 LEU A CD1 
1387 C CD2 . LEU A 181 ? 0.32073 0.31459 0.32620 0.02858  -0.01378 0.01476  181 LEU A CD2 
1388 N N   . THR A 182 ? 0.32445 0.30467 0.33515 0.01842  -0.00380 0.00796  182 THR A N   
1389 C CA  . THR A 182 ? 0.33434 0.30615 0.33727 0.01706  -0.00372 0.00705  182 THR A CA  
1390 C C   . THR A 182 ? 0.38106 0.35056 0.38185 0.01269  -0.00603 0.00458  182 THR A C   
1391 O O   . THR A 182 ? 0.36359 0.34140 0.37154 0.00907  -0.00737 0.00377  182 THR A O   
1392 C CB  . THR A 182 ? 0.39446 0.36281 0.39582 0.01566  -0.00122 0.00794  182 THR A CB  
1393 O OG1 . THR A 182 ? 0.36727 0.34112 0.37423 0.01183  0.00048  0.00751  182 THR A OG1 
1394 C CG2 . THR A 182 ? 0.31971 0.29042 0.32150 0.01910  -0.00045 0.00909  182 THR A CG2 
1395 N N   . GLU A 183 ? 0.36133 0.31982 0.35280 0.01305  -0.00643 0.00288  183 GLU A N   
1396 C CA  . GLU A 183 ? 0.38707 0.33918 0.37398 0.00768  -0.00883 -0.00105 183 GLU A CA  
1397 C C   . GLU A 183 ? 0.41626 0.35860 0.40203 0.00151  -0.00659 -0.00079 183 GLU A C   
1398 O O   . GLU A 183 ? 0.38114 0.31577 0.36323 0.00426  -0.00340 0.00245  183 GLU A O   
1399 C CB  . GLU A 183 ? 0.42979 0.37130 0.40482 0.01172  -0.00946 -0.00414 183 GLU A CB  
1400 C CG  . GLU A 183 ? 0.39584 0.34577 0.36932 0.01771  -0.01018 -0.00330 183 GLU A CG  
1401 C CD  . GLU A 183 ? 0.44795 0.38843 0.40828 0.02184  -0.00955 -0.00716 183 GLU A CD  
1402 O OE1 . GLU A 183 ? 0.47107 0.39640 0.42401 0.02173  -0.00817 -0.01046 183 GLU A OE1 
1403 O OE2 . GLU A 183 ? 0.41896 0.36595 0.37526 0.02568  -0.00978 -0.00668 183 GLU A OE2 
1404 N N   . MET A 184 ? 0.37404 0.31735 0.36279 -0.00730 -0.00851 -0.00377 184 MET A N   
1405 C CA  . MET A 184 ? 0.41682 0.34744 0.40289 -0.01547 -0.00600 -0.00367 184 MET A CA  
1406 C C   . MET A 184 ? 0.43259 0.34601 0.40812 -0.01931 -0.00852 -0.00949 184 MET A C   
1407 O O   . MET A 184 ? 0.47813 0.39847 0.45619 -0.02541 -0.01333 -0.01488 184 MET A O   
1408 C CB  . MET A 184 ? 0.42801 0.37344 0.42722 -0.02489 -0.00529 -0.00315 184 MET A CB  
1409 C CG  . MET A 184 ? 0.42744 0.39055 0.43711 -0.02081 -0.00250 0.00067  184 MET A CG  
1410 S SD  . MET A 184 ? 0.49423 0.47737 0.52097 -0.03112 -0.00072 0.00047  184 MET A SD  
1411 C CE  . MET A 184 ? 0.43847 0.43731 0.47336 -0.02244 0.00368  0.00367  184 MET A CE  
1412 N N   . ALA A 185 ? 0.41096 0.30193 0.37427 -0.01537 -0.00557 -0.00873 185 ALA A N   
1413 C CA  . ALA A 185 ? 0.47826 0.34638 0.42919 -0.01840 -0.00642 -0.01480 185 ALA A CA  
1414 C C   . ALA A 185 ? 0.48682 0.36049 0.43410 -0.01920 -0.01187 -0.02308 185 ALA A C   
1415 O O   . ALA A 185 ? 0.44436 0.31812 0.39258 -0.03046 -0.01586 -0.02908 185 ALA A O   
1416 C CB  . ALA A 185 ? 0.44359 0.29885 0.39513 -0.03221 -0.00489 -0.01517 185 ALA A CB  
1417 N N   . SER A 186 ? 0.49297 0.37244 0.43578 -0.00806 -0.01215 -0.02337 186 SER A N   
1418 C CA  . SER A 186 ? 0.52119 0.40518 0.45676 -0.00760 -0.01668 -0.03039 186 SER A CA  
1419 C C   . SER A 186 ? 0.54438 0.40250 0.46225 -0.00686 -0.01577 -0.03867 186 SER A C   
1420 O O   . SER A 186 ? 0.55840 0.39713 0.46925 0.00007  -0.01046 -0.03727 186 SER A O   
1421 C CB  . SER A 186 ? 0.53092 0.43029 0.46743 0.00344  -0.01585 -0.02657 186 SER A CB  
1422 O OG  . SER A 186 ? 0.61405 0.50317 0.54471 0.01391  -0.01021 -0.02428 186 SER A OG  
1423 N N   . ILE A 187 ? 0.57678 0.43458 0.48668 -0.01326 -0.02129 -0.04771 187 ILE A N   
1424 C CA  . ILE A 187 ? 0.59871 0.43201 0.48886 -0.01166 -0.02054 -0.05780 187 ILE A CA  
1425 C C   . ILE A 187 ? 0.60369 0.44335 0.48363 0.00200  -0.01823 -0.05857 187 ILE A C   
1426 O O   . ILE A 187 ? 0.59991 0.46260 0.48314 0.00375  -0.02161 -0.05608 187 ILE A O   
1427 C CB  . ILE A 187 ? 0.62512 0.45434 0.50944 -0.02641 -0.02806 -0.06876 187 ILE A CB  
1428 C CG1 . ILE A 187 ? 0.61492 0.41149 0.47701 -0.02586 -0.02624 -0.08063 187 ILE A CG1 
1429 C CG2 . ILE A 187 ? 0.66937 0.52605 0.55503 -0.02774 -0.03594 -0.07074 187 ILE A CG2 
1430 C CD1 . ILE A 187 ? 0.77606 0.56175 0.63258 -0.04365 -0.03320 -0.09243 187 ILE A CD1 
1431 N N   . ASN A 188 ? 0.62961 0.44923 0.49772 0.01243  -0.01167 -0.06099 188 ASN A N   
1432 C CA  . ASN A 188 ? 0.65968 0.48479 0.51775 0.02543  -0.00753 -0.06229 188 ASN A CA  
1433 C C   . ASN A 188 ? 0.69653 0.49321 0.53356 0.03003  -0.00397 -0.07381 188 ASN A C   
1434 O O   . ASN A 188 ? 0.67275 0.44595 0.50751 0.03447  0.00086  -0.07403 188 ASN A O   
1435 C CB  . ASN A 188 ? 0.65787 0.49491 0.52790 0.03731  -0.00114 -0.05142 188 ASN A CB  
1436 C CG  . ASN A 188 ? 0.61972 0.48527 0.50533 0.03511  -0.00377 -0.04233 188 ASN A CG  
1437 O OD1 . ASN A 188 ? 0.60511 0.48610 0.48847 0.03957  -0.00296 -0.04060 188 ASN A OD1 
1438 N ND2 . ASN A 188 ? 0.56817 0.43931 0.46852 0.02837  -0.00620 -0.03635 188 ASN A ND2 
1439 N N   . ASN A 189 ? 0.71872 0.51627 0.53897 0.02947  -0.00639 -0.08337 189 ASN A N   
1440 C CA  . ASN A 189 ? 0.76098 0.53167 0.55820 0.03493  -0.00238 -0.09622 189 ASN A CA  
1441 C C   . ASN A 189 ? 0.80692 0.59230 0.58931 0.04276  -0.00062 -0.10004 189 ASN A C   
1442 O O   . ASN A 189 ? 0.81363 0.62610 0.60575 0.04772  0.00077  -0.08993 189 ASN A O   
1443 C CB  . ASN A 189 ? 0.76487 0.51135 0.55184 0.01963  -0.00892 -0.10836 189 ASN A CB  
1444 C CG  . ASN A 189 ? 0.78546 0.55349 0.57674 0.00414  -0.02043 -0.11046 189 ASN A CG  
1445 O OD1 . ASN A 189 ? 0.80377 0.59663 0.59252 0.00702  -0.02368 -0.10854 189 ASN A OD1 
1446 N ND2 . ASN A 189 ? 0.75720 0.51683 0.55580 -0.01217 -0.02644 -0.11350 189 ASN A ND2 
1447 N N   . ARG A 190 ? 0.89283 0.65885 0.65016 0.04344  -0.00020 -0.11475 190 ARG A N   
1448 C CA  . ARG A 190 ? 0.90714 0.68576 0.64598 0.05052  0.00192  -0.11917 190 ARG A CA  
1449 C C   . ARG A 190 ? 0.88567 0.69287 0.62752 0.04117  -0.00809 -0.11442 190 ARG A C   
1450 O O   . ARG A 190 ? 0.97658 0.80649 0.71808 0.04822  -0.00518 -0.10632 190 ARG A O   
1451 C CB  . ARG A 190 ? 0.92642 0.67630 0.63521 0.05137  0.00320  -0.13797 190 ARG A CB  
1452 C CG  . ARG A 190 ? 0.92948 0.66490 0.62568 0.07008  0.01703  -0.14217 190 ARG A CG  
1453 C CD  . ARG A 190 ? 0.94103 0.64970 0.60371 0.07063  0.01789  -0.16238 190 ARG A CD  
1454 N NE  . ARG A 190 ? 1.01623 0.73761 0.66288 0.05811  0.00680  -0.16956 190 ARG A NE  
1455 C CZ  . ARG A 190 ? 1.02055 0.72788 0.65894 0.04098  -0.00500 -0.18113 190 ARG A CZ  
1456 N NH1 . ARG A 190 ? 0.98929 0.66612 0.63250 0.03303  -0.00627 -0.18712 190 ARG A NH1 
1457 N NH2 . ARG A 190 ? 1.02347 0.74852 0.64875 0.03120  -0.01597 -0.18619 190 ARG A NH2 
1458 N N   . VAL A 191 ? 0.87153 0.67837 0.61716 0.02540  -0.01972 -0.11870 191 VAL A N   
1459 C CA  . VAL A 191 ? 0.87481 0.70809 0.62115 0.01756  -0.03061 -0.11595 191 VAL A CA  
1460 C C   . VAL A 191 ? 0.82507 0.68341 0.60039 0.01443  -0.03400 -0.10012 191 VAL A C   
1461 O O   . VAL A 191 ? 0.81932 0.70188 0.59690 0.01287  -0.04085 -0.09424 191 VAL A O   
1462 C CB  . VAL A 191 ? 0.93162 0.75595 0.66639 0.00192  -0.04261 -0.13055 191 VAL A CB  
1463 C CG1 . VAL A 191 ? 0.97907 0.77892 0.68081 0.00498  -0.04005 -0.14795 191 VAL A CG1 
1464 C CG2 . VAL A 191 ? 0.89098 0.70112 0.64408 -0.01059 -0.04507 -0.13162 191 VAL A CG2 
1465 N N   . TYR A 192 ? 0.79922 0.65169 0.59520 0.01422  -0.02944 -0.09309 192 TYR A N   
1466 C CA  . TYR A 192 ? 0.74781 0.62135 0.56976 0.01102  -0.03202 -0.07993 192 TYR A CA  
1467 C C   . TYR A 192 ? 0.71863 0.59505 0.55255 0.02245  -0.02186 -0.06875 192 TYR A C   
1468 O O   . TYR A 192 ? 0.70647 0.56472 0.54065 0.02721  -0.01493 -0.07001 192 TYR A O   
1469 C CB  . TYR A 192 ? 0.73270 0.60006 0.56908 -0.00260 -0.03719 -0.08198 192 TYR A CB  
1470 C CG  . TYR A 192 ? 0.75447 0.61917 0.58145 -0.01633 -0.04758 -0.09431 192 TYR A CG  
1471 C CD1 . TYR A 192 ? 0.76734 0.65008 0.58333 -0.01748 -0.05617 -0.09781 192 TYR A CD1 
1472 C CD2 . TYR A 192 ? 0.75573 0.59993 0.58439 -0.02882 -0.04910 -0.10217 192 TYR A CD2 
1473 C CE1 . TYR A 192 ? 0.77108 0.65423 0.57887 -0.03081 -0.06715 -0.10986 192 TYR A CE1 
1474 C CE2 . TYR A 192 ? 0.77679 0.61955 0.59829 -0.04356 -0.05908 -0.11435 192 TYR A CE2 
1475 C CZ  . TYR A 192 ? 0.78089 0.64454 0.59242 -0.04457 -0.06867 -0.11868 192 TYR A CZ  
1476 O OH  . TYR A 192 ? 0.83423 0.69925 0.63895 -0.05996 -0.08008 -0.13155 192 TYR A OH  
1477 N N   . ARG A 193 ? 0.66537 0.56431 0.50937 0.02664  -0.02145 -0.05772 193 ARG A N   
1478 C CA  . ARG A 193 ? 0.62827 0.53346 0.48278 0.03623  -0.01257 -0.04779 193 ARG A CA  
1479 C C   . ARG A 193 ? 0.59191 0.51482 0.46763 0.03315  -0.01520 -0.03670 193 ARG A C   
1480 O O   . ARG A 193 ? 0.52146 0.45921 0.39806 0.03109  -0.02053 -0.03284 193 ARG A O   
1481 C CB  . ARG A 193 ? 0.68065 0.59286 0.52133 0.04569  -0.00653 -0.04624 193 ARG A CB  
1482 C CG  . ARG A 193 ? 0.76580 0.66268 0.58164 0.05010  -0.00338 -0.05822 193 ARG A CG  
1483 C CD  . ARG A 193 ? 0.80413 0.68207 0.62075 0.05669  0.00441  -0.06261 193 ARG A CD  
1484 N NE  . ARG A 193 ? 0.78216 0.66997 0.61993 0.06203  0.01014  -0.05153 193 ARG A NE  
1485 C CZ  . ARG A 193 ? 0.82702 0.70308 0.67236 0.06723  0.01468  -0.05139 193 ARG A CZ  
1486 N NH1 . ARG A 193 ? 0.84917 0.69998 0.68265 0.06868  0.01550  -0.06105 193 ARG A NH1 
1487 N NH2 . ARG A 193 ? 0.75476 0.64378 0.61924 0.07104  0.01806  -0.04129 193 ARG A NH2 
1488 N N   . THR A 194 ? 0.49498 0.41587 0.38634 0.03388  -0.01143 -0.03159 194 THR A N   
1489 C CA  . THR A 194 ? 0.47556 0.41122 0.38521 0.03301  -0.01164 -0.02179 194 THR A CA  
1490 C C   . THR A 194 ? 0.46009 0.39850 0.37638 0.04058  -0.00379 -0.01581 194 THR A C   
1491 O O   . THR A 194 ? 0.44813 0.37825 0.35787 0.04685  0.00162  -0.01873 194 THR A O   
1492 C CB  . THR A 194 ? 0.49478 0.42898 0.41777 0.02511  -0.01530 -0.02142 194 THR A CB  
1493 O OG1 . THR A 194 ? 0.48292 0.40356 0.40799 0.02669  -0.01076 -0.02186 194 THR A OG1 
1494 C CG2 . THR A 194 ? 0.49489 0.42671 0.41304 0.01613  -0.02266 -0.02866 194 THR A CG2 
1495 N N   . ILE A 195 ? 0.40245 0.35312 0.33264 0.04004  -0.00327 -0.00780 195 ILE A N   
1496 C CA  . ILE A 195 ? 0.43304 0.38941 0.37097 0.04522  0.00316  -0.00253 195 ILE A CA  
1497 C C   . ILE A 195 ? 0.41486 0.36464 0.35982 0.04643  0.00460  -0.00330 195 ILE A C   
1498 O O   . ILE A 195 ? 0.41130 0.36361 0.35903 0.05263  0.00950  -0.00179 195 ILE A O   
1499 C CB  . ILE A 195 ? 0.38042 0.34882 0.32946 0.04314  0.00317  0.00526  195 ILE A CB  
1500 C CG1 . ILE A 195 ? 0.38076 0.35669 0.33785 0.04640  0.00959  0.00992  195 ILE A CG1 
1501 C CG2 . ILE A 195 ? 0.39057 0.35947 0.35108 0.03779  -0.00119 0.00633  195 ILE A CG2 
1502 C CD1 . ILE A 195 ? 0.42994 0.40944 0.37778 0.05202  0.01586  0.00999  195 ILE A CD1 
1503 N N   . GLY A 196 ? 0.42271 0.36522 0.37054 0.04092  0.00055  -0.00506 196 GLY A N   
1504 C CA  . GLY A 196 ? 0.41994 0.35500 0.37201 0.04204  0.00171  -0.00424 196 GLY A CA  
1505 C C   . GLY A 196 ? 0.42919 0.37556 0.39450 0.04111  0.00195  0.00167  196 GLY A C   
1506 O O   . GLY A 196 ? 0.43207 0.37672 0.40204 0.03642  -0.00004 0.00281  196 GLY A O   
1507 N N   . SER A 197 ? 0.41127 0.36954 0.38218 0.04471  0.00476  0.00501  197 SER A N   
1508 C CA  . SER A 197 ? 0.39136 0.35972 0.37395 0.04327  0.00478  0.00915  197 SER A CA  
1509 C C   . SER A 197 ? 0.37704 0.34762 0.36479 0.03659  0.00205  0.01014  197 SER A C   
1510 O O   . SER A 197 ? 0.35413 0.32445 0.33944 0.03438  0.00063  0.00961  197 SER A O   
1511 C CB  . SER A 197 ? 0.35118 0.33237 0.33968 0.04597  0.00852  0.01208  197 SER A CB  
1512 O OG  . SER A 197 ? 0.37956 0.36124 0.36403 0.05354  0.01221  0.01089  197 SER A OG  
1513 N N   . PRO A 198 ? 0.38468 0.35813 0.37901 0.03422  0.00119  0.01141  198 PRO A N   
1514 C CA  . PRO A 198 ? 0.36145 0.33810 0.36159 0.02967  0.00021  0.01202  198 PRO A CA  
1515 C C   . PRO A 198 ? 0.32915 0.31115 0.33311 0.02959  0.00185  0.01448  198 PRO A C   
1516 O O   . PRO A 198 ? 0.34103 0.32812 0.34664 0.03128  0.00426  0.01616  198 PRO A O   
1517 C CB  . PRO A 198 ? 0.35867 0.33744 0.36245 0.02817  -0.00023 0.01203  198 PRO A CB  
1518 C CG  . PRO A 198 ? 0.38225 0.35684 0.38065 0.03169  -0.00063 0.01232  198 PRO A CG  
1519 C CD  . PRO A 198 ? 0.36802 0.34177 0.36335 0.03659  0.00094  0.01225  198 PRO A CD  
1520 N N   . LEU A 199 ? 0.30753 0.28869 0.31341 0.02790  0.00101  0.01538  199 LEU A N   
1521 C CA  . LEU A 199 ? 0.35811 0.34043 0.36626 0.02787  0.00282  0.01914  199 LEU A CA  
1522 C C   . LEU A 199 ? 0.32914 0.30916 0.34422 0.02532  0.00317  0.01897  199 LEU A C   
1523 O O   . LEU A 199 ? 0.35112 0.32976 0.36787 0.02538  0.00168  0.01682  199 LEU A O   
1524 C CB  . LEU A 199 ? 0.33526 0.31676 0.33744 0.03029  0.00123  0.02133  199 LEU A CB  
1525 C CG  . LEU A 199 ? 0.34535 0.32710 0.33742 0.03261  0.00053  0.01973  199 LEU A CG  
1526 C CD1 . LEU A 199 ? 0.35823 0.34101 0.34313 0.03463  -0.00196 0.02233  199 LEU A CD1 
1527 C CD2 . LEU A 199 ? 0.35603 0.34015 0.34612 0.03438  0.00511  0.02058  199 LEU A CD2 
1528 N N   . VAL A 200 ? 0.33668 0.31622 0.35591 0.02271  0.00570  0.02075  200 VAL A N   
1529 C CA  . VAL A 200 ? 0.37531 0.34919 0.39951 0.01973  0.00649  0.01924  200 VAL A CA  
1530 C C   . VAL A 200 ? 0.38705 0.35335 0.41149 0.02024  0.00889  0.02450  200 VAL A C   
1531 O O   . VAL A 200 ? 0.39447 0.36171 0.41844 0.01837  0.01161  0.02900  200 VAL A O   
1532 C CB  . VAL A 200 ? 0.36445 0.34200 0.39299 0.01448  0.00669  0.01602  200 VAL A CB  
1533 C CG1 . VAL A 200 ? 0.39528 0.36392 0.42701 0.01026  0.00783  0.01332  200 VAL A CG1 
1534 C CG2 . VAL A 200 ? 0.36878 0.35189 0.39504 0.01545  0.00387  0.01214  200 VAL A CG2 
1535 N N   . PHE A 201 ? 0.38847 0.34736 0.41372 0.02340  0.00852  0.02462  201 PHE A N   
1536 C CA  . PHE A 201 ? 0.40475 0.35428 0.42892 0.02666  0.01011  0.03086  201 PHE A CA  
1537 C C   . PHE A 201 ? 0.43727 0.37272 0.46521 0.02460  0.01298  0.02906  201 PHE A C   
1538 O O   . PHE A 201 ? 0.42421 0.35811 0.45474 0.02481  0.01266  0.02231  201 PHE A O   
1539 C CB  . PHE A 201 ? 0.39420 0.34736 0.41699 0.03425  0.00675  0.03289  201 PHE A CB  
1540 C CG  . PHE A 201 ? 0.41645 0.38043 0.43360 0.03550  0.00346  0.03389  201 PHE A CG  
1541 C CD1 . PHE A 201 ? 0.40349 0.36757 0.41283 0.03741  0.00358  0.04038  201 PHE A CD1 
1542 C CD2 . PHE A 201 ? 0.39892 0.37120 0.41687 0.03433  0.00074  0.02817  201 PHE A CD2 
1543 C CE1 . PHE A 201 ? 0.39890 0.37131 0.40069 0.03848  0.00064  0.03956  201 PHE A CE1 
1544 C CE2 . PHE A 201 ? 0.38046 0.35909 0.39205 0.03470  -0.00216 0.02776  201 PHE A CE2 
1545 C CZ  . PHE A 201 ? 0.39248 0.37123 0.39565 0.03694  -0.00242 0.03267  201 PHE A CZ  
1546 N N   . PRO A 202 ? 0.45289 0.37636 0.47995 0.02250  0.01640  0.03480  202 PRO A N   
1547 C CA  . PRO A 202 ? 0.45925 0.36445 0.48863 0.02007  0.01950  0.03254  202 PRO A CA  
1548 C C   . PRO A 202 ? 0.47590 0.37047 0.50453 0.03056  0.01958  0.03517  202 PRO A C   
1549 O O   . PRO A 202 ? 0.43552 0.33979 0.46316 0.03880  0.01647  0.03914  202 PRO A O   
1550 C CB  . PRO A 202 ? 0.49707 0.39344 0.52571 0.01296  0.02368  0.03936  202 PRO A CB  
1551 C CG  . PRO A 202 ? 0.45689 0.36215 0.47978 0.01806  0.02327  0.04875  202 PRO A CG  
1552 C CD  . PRO A 202 ? 0.45267 0.37715 0.47509 0.02187  0.01842  0.04385  202 PRO A CD  
1553 N N   . LYS A 203 ? 0.48839 0.36318 0.51798 0.03029  0.02298  0.03225  203 LYS A N   
1554 C CA  . LYS A 203 ? 0.53297 0.39465 0.56251 0.04187  0.02420  0.03581  203 LYS A CA  
1555 C C   . LYS A 203 ? 0.51545 0.37391 0.54054 0.04790  0.02369  0.04947  203 LYS A C   
1556 O O   . LYS A 203 ? 0.54135 0.39679 0.56213 0.04097  0.02550  0.05597  203 LYS A O   
1557 C CB  . LYS A 203 ? 0.54986 0.38480 0.57889 0.03993  0.02913  0.03082  203 LYS A CB  
1558 C CG  . LYS A 203 ? 0.55972 0.39437 0.59066 0.04137  0.03002  0.01781  203 LYS A CG  
1559 C CD  . LYS A 203 ? 0.61339 0.41721 0.64171 0.04294  0.03532  0.01340  203 LYS A CD  
1560 C CE  . LYS A 203 ? 0.63065 0.41448 0.65588 0.02987  0.03775  0.01573  203 LYS A CE  
1561 N NZ  . LYS A 203 ? 0.70347 0.45154 0.72492 0.03147  0.04326  0.01288  203 LYS A NZ  
1562 N N   . HIS A 204 ? 0.52857 0.38994 0.55476 0.06118  0.02121  0.05407  204 HIS A N   
1563 C CA  . HIS A 204 ? 0.54372 0.40226 0.56457 0.07045  0.01936  0.06746  204 HIS A CA  
1564 C C   . HIS A 204 ? 0.51887 0.39929 0.53450 0.06904  0.01434  0.07220  204 HIS A C   
1565 O O   . HIS A 204 ? 0.53500 0.41590 0.54366 0.07640  0.01181  0.08312  204 HIS A O   
1566 C CB  . HIS A 204 ? 0.57071 0.40083 0.58462 0.06816  0.02500  0.07664  204 HIS A CB  
1567 C CG  . HIS A 204 ? 0.58812 0.39131 0.60494 0.06975  0.03016  0.07176  204 HIS A CG  
1568 N ND1 . HIS A 204 ? 0.61390 0.39932 0.63054 0.05630  0.03532  0.06524  204 HIS A ND1 
1569 C CD2 . HIS A 204 ? 0.61753 0.40892 0.63757 0.08343  0.03096  0.07136  204 HIS A CD2 
1570 C CE1 . HIS A 204 ? 0.62875 0.38962 0.64630 0.06097  0.03911  0.06037  204 HIS A CE1 
1571 N NE2 . HIS A 204 ? 0.63588 0.39945 0.65554 0.07830  0.03713  0.06413  204 HIS A NE2 
1572 N N   . HIS A 205 ? 0.50151 0.39859 0.51868 0.06060  0.01278  0.06443  205 HIS A N   
1573 C CA  . HIS A 205 ? 0.48956 0.40639 0.50167 0.06091  0.00774  0.06632  205 HIS A CA  
1574 C C   . HIS A 205 ? 0.49330 0.42750 0.51187 0.06771  0.00157  0.06204  205 HIS A C   
1575 O O   . HIS A 205 ? 0.44292 0.38076 0.47057 0.06702  0.00227  0.05366  205 HIS A O   
1576 C CB  . HIS A 205 ? 0.47229 0.39747 0.48323 0.05018  0.00922  0.06022  205 HIS A CB  
1577 C CG  . HIS A 205 ? 0.47242 0.38948 0.47757 0.04351  0.01455  0.06601  205 HIS A CG  
1578 N ND1 . HIS A 205 ? 0.44810 0.37654 0.44959 0.03785  0.01564  0.06475  205 HIS A ND1 
1579 C CD2 . HIS A 205 ? 0.50968 0.40852 0.51281 0.04132  0.01993  0.07324  205 HIS A CD2 
1580 C CE1 . HIS A 205 ? 0.49603 0.41698 0.49487 0.03234  0.02169  0.07102  205 HIS A CE1 
1581 N NE2 . HIS A 205 ? 0.52123 0.42345 0.52076 0.03333  0.02434  0.07647  205 HIS A NE2 
1582 N N   . VAL A 206 ? 0.42213 0.36825 0.43573 0.07366  -0.00442 0.06780  206 VAL A N   
1583 C CA  . VAL A 206 ? 0.44159 0.40738 0.46284 0.07900  -0.01119 0.06453  206 VAL A CA  
1584 C C   . VAL A 206 ? 0.45390 0.43541 0.46966 0.07235  -0.01587 0.05986  206 VAL A C   
1585 O O   . VAL A 206 ? 0.44314 0.42550 0.44596 0.07188  -0.01800 0.06459  206 VAL A O   
1586 C CB  . VAL A 206 ? 0.47297 0.44213 0.49419 0.09183  -0.01619 0.07419  206 VAL A CB  
1587 C CG1 . VAL A 206 ? 0.47583 0.47106 0.50721 0.09559  -0.02418 0.07036  206 VAL A CG1 
1588 C CG2 . VAL A 206 ? 0.49653 0.44662 0.52320 0.09994  -0.01086 0.07826  206 VAL A CG2 
1589 N N   . VAL A 207 ? 0.41679 0.40911 0.44093 0.06734  -0.01685 0.05061  207 VAL A N   
1590 C CA  . VAL A 207 ? 0.41826 0.42310 0.43821 0.06123  -0.02146 0.04527  207 VAL A CA  
1591 C C   . VAL A 207 ? 0.44795 0.47228 0.47661 0.06457  -0.02898 0.04413  207 VAL A C   
1592 O O   . VAL A 207 ? 0.39470 0.42654 0.43789 0.06659  -0.02799 0.04148  207 VAL A O   
1593 C CB  . VAL A 207 ? 0.41368 0.41580 0.43606 0.05251  -0.01736 0.03687  207 VAL A CB  
1594 C CG1 . VAL A 207 ? 0.40922 0.41972 0.42615 0.04675  -0.02166 0.03159  207 VAL A CG1 
1595 C CG2 . VAL A 207 ? 0.41198 0.39936 0.42863 0.04937  -0.01096 0.03801  207 VAL A CG2 
1596 N N   . SER A 208 ? 0.39326 0.42739 0.41315 0.06493  -0.03640 0.04575  208 SER A N   
1597 C CA  . SER A 208 ? 0.44723 0.50322 0.47522 0.06737  -0.04549 0.04503  208 SER A CA  
1598 C C   . SER A 208 ? 0.46124 0.52579 0.48464 0.05690  -0.05027 0.03630  208 SER A C   
1599 O O   . SER A 208 ? 0.47145 0.52723 0.47783 0.05319  -0.05043 0.03468  208 SER A O   
1600 C CB  . SER A 208 ? 0.48142 0.54228 0.50155 0.07755  -0.05206 0.05487  208 SER A CB  
1601 O OG  . SER A 208 ? 0.51546 0.60130 0.54307 0.07926  -0.06275 0.05371  208 SER A OG  
1602 N N   . LEU A 209 ? 0.42649 0.50711 0.46499 0.05195  -0.05322 0.03048  209 LEU A N   
1603 C CA  . LEU A 209 ? 0.44716 0.53521 0.48294 0.04086  -0.05835 0.02199  209 LEU A CA  
1604 C C   . LEU A 209 ? 0.46375 0.57647 0.50488 0.04210  -0.07025 0.02230  209 LEU A C   
1605 O O   . LEU A 209 ? 0.46477 0.59637 0.52424 0.04787  -0.07280 0.02573  209 LEU A O   
1606 C CB  . LEU A 209 ? 0.43810 0.52668 0.48675 0.03188  -0.05296 0.01554  209 LEU A CB  
1607 C CG  . LEU A 209 ? 0.41129 0.47939 0.45651 0.03071  -0.04238 0.01502  209 LEU A CG  
1608 C CD1 . LEU A 209 ? 0.41478 0.48523 0.47003 0.02158  -0.03831 0.00954  209 LEU A CD1 
1609 C CD2 . LEU A 209 ? 0.39383 0.44314 0.41943 0.02926  -0.04047 0.01412  209 LEU A CD2 
1610 N N   . GLN A 210 ? 0.45887 0.57256 0.48391 0.03731  -0.07768 0.01835  210 GLN A N   
1611 C CA  . GLN A 210 ? 0.49826 0.63619 0.52505 0.03826  -0.09081 0.01837  210 GLN A CA  
1612 C C   . GLN A 210 ? 0.49699 0.64062 0.52089 0.02320  -0.09705 0.00630  210 GLN A C   
1613 O O   . GLN A 210 ? 0.49417 0.61738 0.49929 0.01676  -0.09399 -0.00005 210 GLN A O   
1614 C CB  . GLN A 210 ? 0.51370 0.64777 0.51947 0.04840  -0.09546 0.02619  210 GLN A CB  
1615 C CG  . GLN A 210 ? 0.52614 0.65438 0.53648 0.06287  -0.09013 0.03905  210 GLN A CG  
1616 C CD  . GLN A 210 ? 0.57961 0.69554 0.56609 0.07133  -0.09043 0.04823  210 GLN A CD  
1617 O OE1 . GLN A 210 ? 0.59856 0.71868 0.56586 0.06936  -0.09779 0.04632  210 GLN A OE1 
1618 N NE2 . GLN A 210 ? 0.59336 0.69312 0.57987 0.08019  -0.08192 0.05810  210 GLN A NE2 
1619 N N   . PRO A 211 ? 0.50549 0.67599 0.54823 0.01711  -0.10530 0.00258  211 PRO A N   
1620 C CA  . PRO A 211 ? 0.51041 0.68433 0.55227 0.00014  -0.11063 -0.00961 211 PRO A CA  
1621 C C   . PRO A 211 ? 0.55023 0.71959 0.56597 -0.00263 -0.12021 -0.01531 211 PRO A C   
1622 O O   . PRO A 211 ? 0.52500 0.70233 0.52892 0.00802  -0.12705 -0.00907 211 PRO A O   
1623 C CB  . PRO A 211 ? 0.53226 0.74243 0.60301 -0.00416 -0.11821 -0.01022 211 PRO A CB  
1624 C CG  . PRO A 211 ? 0.55479 0.77459 0.64344 0.01096  -0.11220 0.00088  211 PRO A CG  
1625 C CD  . PRO A 211 ? 0.53235 0.73191 0.59971 0.02539  -0.10960 0.00925  211 PRO A CD  
1626 N N   . VAL A 212 ? 0.57631 0.73115 0.58148 -0.01684 -0.12028 -0.02727 212 VAL A N   
1627 C CA  . VAL A 212 ? 0.60190 0.75038 0.58079 -0.02153 -0.12890 -0.03605 212 VAL A CA  
1628 C C   . VAL A 212 ? 0.64349 0.81597 0.63122 -0.03587 -0.14302 -0.04610 212 VAL A C   
1629 O O   . VAL A 212 ? 0.66135 0.85125 0.63807 -0.03437 -0.15633 -0.04799 212 VAL A O   
1630 C CB  . VAL A 212 ? 0.58577 0.69749 0.54328 -0.02597 -0.11887 -0.04355 212 VAL A CB  
1631 C CG1 . VAL A 212 ? 0.62954 0.73330 0.55941 -0.03179 -0.12701 -0.05524 212 VAL A CG1 
1632 C CG2 . VAL A 212 ? 0.54835 0.64189 0.49713 -0.01180 -0.10679 -0.03354 212 VAL A CG2 
1633 N N   . ASN A 213 ? 0.63410 0.80883 0.64167 -0.05057 -0.14049 -0.05231 213 ASN A N   
1634 C CA  . ASN A 213 ? 0.66914 0.86947 0.69043 -0.06676 -0.15321 -0.06168 213 ASN A CA  
1635 C C   . ASN A 213 ? 0.64503 0.87454 0.70441 -0.07014 -0.15129 -0.05610 213 ASN A C   
1636 O O   . ASN A 213 ? 0.64520 0.91116 0.72291 -0.06284 -0.16007 -0.04982 213 ASN A O   
1637 C CB  . ASN A 213 ? 0.71371 0.88752 0.72062 -0.08553 -0.15232 -0.07688 213 ASN A CB  
1638 C CG  . ASN A 213 ? 0.76692 0.92180 0.73741 -0.08425 -0.15844 -0.08594 213 ASN A CG  
1639 O OD1 . ASN A 213 ? 0.79418 0.97031 0.75495 -0.07954 -0.17152 -0.08629 213 ASN A OD1 
1640 N ND2 . ASN A 213 ? 0.79482 0.90995 0.74405 -0.08728 -0.14873 -0.09302 213 ASN A ND2 
1641 N N   . ASP A 214 ? 0.64871 0.86296 0.71964 -0.08015 -0.13944 -0.05783 214 ASP A N   
1642 C CA  . ASP A 214 ? 0.63207 0.87254 0.73763 -0.08355 -0.13492 -0.05262 214 ASP A CA  
1643 C C   . ASP A 214 ? 0.58118 0.83086 0.69700 -0.06237 -0.12821 -0.03897 214 ASP A C   
1644 O O   . ASP A 214 ? 0.57015 0.79242 0.66837 -0.05002 -0.11960 -0.03359 214 ASP A O   
1645 C CB  . ASP A 214 ? 0.65773 0.87464 0.76765 -0.09814 -0.12222 -0.05627 214 ASP A CB  
1646 C CG  . ASP A 214 ? 0.71173 0.95872 0.85678 -0.10681 -0.11819 -0.05326 214 ASP A CG  
1647 O OD1 . ASP A 214 ? 0.64640 0.91237 0.80897 -0.09290 -0.11285 -0.04349 214 ASP A OD1 
1648 O OD2 . ASP A 214 ? 0.95179 1.20302 1.10683 -0.12789 -0.11977 -0.06096 214 ASP A OD2 
1649 N N   . LYS A 215 ? 0.55126 0.84007 0.69659 -0.05832 -0.13202 -0.03377 215 LYS A N   
1650 C CA  . LYS A 215 ? 0.53453 0.83279 0.69142 -0.03794 -0.12595 -0.02173 215 LYS A CA  
1651 C C   . LYS A 215 ? 0.49911 0.80605 0.68181 -0.03965 -0.11282 -0.01863 215 LYS A C   
1652 O O   . LYS A 215 ? 0.48493 0.80372 0.68106 -0.02354 -0.10782 -0.01019 215 LYS A O   
1653 C CB  . LYS A 215 ? 0.53953 0.87528 0.70808 -0.02590 -0.14000 -0.01639 215 LYS A CB  
1654 C CG  . LYS A 215 ? 0.57817 0.90765 0.71874 -0.02134 -0.15307 -0.01745 215 LYS A CG  
1655 C CD  . LYS A 215 ? 0.60397 0.97270 0.75715 -0.00796 -0.16734 -0.01022 215 LYS A CD  
1656 C CE  . LYS A 215 ? 0.65287 1.01959 0.77697 -0.00537 -0.18187 -0.01174 215 LYS A CE  
1657 N NZ  . LYS A 215 ? 0.70042 1.03062 0.79332 0.00866  -0.17456 -0.00439 215 LYS A NZ  
1658 N N   . ASP A 216 ? 0.49512 0.79513 0.68371 -0.05840 -0.10655 -0.02508 216 ASP A N   
1659 C CA  . ASP A 216 ? 0.47677 0.78312 0.68614 -0.06125 -0.09274 -0.02200 216 ASP A CA  
1660 C C   . ASP A 216 ? 0.47010 0.73341 0.65857 -0.06067 -0.07884 -0.02083 216 ASP A C   
1661 O O   . ASP A 216 ? 0.49088 0.72393 0.65736 -0.07024 -0.07908 -0.02620 216 ASP A O   
1662 C CB  . ASP A 216 ? 0.46731 0.79735 0.69905 -0.08334 -0.09408 -0.02813 216 ASP A CB  
1663 C CG  . ASP A 216 ? 0.46770 0.84768 0.72579 -0.08428 -0.10790 -0.02909 216 ASP A CG  
1664 O OD1 . ASP A 216 ? 0.44296 0.83727 0.69983 -0.06638 -0.11681 -0.02430 216 ASP A OD1 
1665 O OD2 . ASP A 216 ? 0.45352 0.85900 0.73389 -0.10310 -0.10997 -0.03408 216 ASP A OD2 
1666 N N   . PHE A 217 ? 0.48782 0.67049 0.61448 -0.02180 -0.11285 -0.03476 217 PHE A N   
1667 C CA  . PHE A 217 ? 0.47007 0.62701 0.58318 -0.02121 -0.09717 -0.03385 217 PHE A CA  
1668 C C   . PHE A 217 ? 0.46204 0.63324 0.59941 -0.02361 -0.08398 -0.02956 217 PHE A C   
1669 O O   . PHE A 217 ? 0.43715 0.63406 0.59643 -0.01654 -0.08241 -0.02530 217 PHE A O   
1670 C CB  . PHE A 217 ? 0.46521 0.60383 0.55540 -0.00550 -0.09128 -0.03020 217 PHE A CB  
1671 C CG  . PHE A 217 ? 0.50007 0.62458 0.56305 -0.00146 -0.10170 -0.03331 217 PHE A CG  
1672 C CD1 . PHE A 217 ? 0.50580 0.60309 0.54337 -0.00536 -0.09983 -0.03877 217 PHE A CD1 
1673 C CD2 . PHE A 217 ? 0.52742 0.66631 0.58924 0.00736  -0.11316 -0.03059 217 PHE A CD2 
1674 C CE1 . PHE A 217 ? 0.50557 0.59072 0.51626 -0.00076 -0.10820 -0.04221 217 PHE A CE1 
1675 C CE2 . PHE A 217 ? 0.55307 0.67934 0.58676 0.01137  -0.12243 -0.03317 217 PHE A CE2 
1676 C CZ  . PHE A 217 ? 0.55428 0.65388 0.56198 0.00718  -0.11940 -0.03937 217 PHE A CZ  
1677 N N   . GLN A 218 ? 0.45361 0.60759 0.58550 -0.03231 -0.07431 -0.03063 218 GLN A N   
1678 C CA  . GLN A 218 ? 0.43440 0.59632 0.58135 -0.03325 -0.05985 -0.02644 218 GLN A CA  
1679 C C   . GLN A 218 ? 0.41438 0.55882 0.54517 -0.01971 -0.04914 -0.02398 218 GLN A C   
1680 O O   . GLN A 218 ? 0.39465 0.51232 0.50260 -0.01940 -0.04645 -0.02569 218 GLN A O   
1681 C CB  . GLN A 218 ? 0.44985 0.60128 0.59736 -0.04942 -0.05564 -0.02761 218 GLN A CB  
1682 C CG  . GLN A 218 ? 0.47170 0.63719 0.63678 -0.05284 -0.04188 -0.02273 218 GLN A CG  
1683 C CD  . GLN A 218 ? 0.47614 0.67838 0.67364 -0.06023 -0.04406 -0.02057 218 GLN A CD  
1684 O OE1 . GLN A 218 ? 0.48463 0.69865 0.69226 -0.06880 -0.05700 -0.02314 218 GLN A OE1 
1685 N NE2 . GLN A 218 ? 0.48623 0.70810 0.70037 -0.05695 -0.03142 -0.01629 218 GLN A NE2 
1686 N N   . ILE A 219 ? 0.39990 0.55946 0.54309 -0.00832 -0.04345 -0.02033 219 ILE A N   
1687 C CA  . ILE A 219 ? 0.39668 0.54020 0.52664 0.00399  -0.03445 -0.01828 219 ILE A CA  
1688 C C   . ILE A 219 ? 0.43112 0.58012 0.57146 0.00387  -0.02074 -0.01718 219 ILE A C   
1689 O O   . ILE A 219 ? 0.41337 0.58769 0.57634 0.00445  -0.01779 -0.01603 219 ILE A O   
1690 C CB  . ILE A 219 ? 0.42837 0.57847 0.55978 0.01881  -0.03928 -0.01526 219 ILE A CB  
1691 C CG1 . ILE A 219 ? 0.40363 0.54986 0.52224 0.01902  -0.05341 -0.01599 219 ILE A CG1 
1692 C CG2 . ILE A 219 ? 0.41273 0.54294 0.53034 0.02933  -0.03009 -0.01311 219 ILE A CG2 
1693 C CD1 . ILE A 219 ? 0.45015 0.60300 0.56893 0.03352  -0.05948 -0.01139 219 ILE A CD1 
1694 N N   . SER A 220 ? 0.38535 0.51232 0.50908 0.00362  -0.01241 -0.01770 220 SER A N   
1695 C CA  . SER A 220 ? 0.41038 0.53940 0.53848 0.00447  0.00013  -0.01729 220 SER A CA  
1696 C C   . SER A 220 ? 0.42617 0.54357 0.54579 0.01735  0.00550  -0.01728 220 SER A C   
1697 O O   . SER A 220 ? 0.47498 0.57441 0.57914 0.02188  0.00199  -0.01684 220 SER A O   
1698 C CB  . SER A 220 ? 0.39079 0.50427 0.50683 -0.00594 0.00497  -0.01773 220 SER A CB  
1699 O OG  . SER A 220 ? 0.40425 0.49298 0.49918 -0.00207 0.00557  -0.01864 220 SER A OG  
1700 N N   . VAL A 221 ? 0.38329 0.51102 0.51310 0.02294  0.01437  -0.01791 221 VAL A N   
1701 C CA  . VAL A 221 ? 0.37418 0.48817 0.49570 0.03325  0.02068  -0.01928 221 VAL A CA  
1702 C C   . VAL A 221 ? 0.42754 0.54327 0.54837 0.03008  0.03171  -0.02181 221 VAL A C   
1703 O O   . VAL A 221 ? 0.36412 0.50078 0.50017 0.03144  0.03743  -0.02248 221 VAL A O   
1704 C CB  . VAL A 221 ? 0.40225 0.52571 0.53567 0.04711  0.01934  -0.01860 221 VAL A CB  
1705 C CG1 . VAL A 221 ? 0.40674 0.51330 0.53183 0.05643  0.02661  -0.02107 221 VAL A CG1 
1706 C CG2 . VAL A 221 ? 0.41099 0.53157 0.54153 0.05071  0.00770  -0.01497 221 VAL A CG2 
1707 N N   . ASP A 222 ? 0.39765 0.49347 0.50094 0.02608  0.03470  -0.02298 222 ASP A N   
1708 C CA  . ASP A 222 ? 0.41529 0.51148 0.51383 0.02190  0.04365  -0.02482 222 ASP A CA  
1709 C C   . ASP A 222 ? 0.44563 0.55999 0.55465 0.01189  0.04536  -0.02201 222 ASP A C   
1710 O O   . ASP A 222 ? 0.42252 0.53389 0.53047 0.00312  0.03882  -0.01933 222 ASP A O   
1711 C CB  . ASP A 222 ? 0.38983 0.48805 0.49038 0.03229  0.05136  -0.02923 222 ASP A CB  
1712 C CG  . ASP A 222 ? 0.37986 0.45551 0.46875 0.03937  0.04933  -0.03160 222 ASP A CG  
1713 O OD1 . ASP A 222 ? 0.38372 0.44352 0.46079 0.03463  0.04468  -0.02983 222 ASP A OD1 
1714 O OD2 . ASP A 222 ? 0.38541 0.45874 0.47731 0.04955  0.05260  -0.03511 222 ASP A OD2 
1715 N N   . HIS A 223 ? 0.43540 0.56821 0.55441 0.01259  0.05424  -0.02254 223 HIS A N   
1716 C CA  . HIS A 223 ? 0.52461 0.67476 0.65419 0.00103  0.05651  -0.01834 223 HIS A CA  
1717 C C   . HIS A 223 ? 0.58005 0.75056 0.73116 -0.00132 0.04937  -0.01627 223 HIS A C   
1718 O O   . HIS A 223 ? 0.61350 0.78987 0.77078 -0.01401 0.04569  -0.01275 223 HIS A O   
1719 C CB  . HIS A 223 ? 0.62533 0.79174 0.75869 0.00183  0.06948  -0.01864 223 HIS A CB  
1720 C CG  . HIS A 223 ? 0.64841 0.83352 0.79323 -0.01117 0.07337  -0.01277 223 HIS A CG  
1721 N ND1 . HIS A 223 ? 0.65395 0.82566 0.78864 -0.02462 0.07056  -0.00783 223 HIS A ND1 
1722 C CD2 . HIS A 223 ? 0.63196 0.84816 0.79857 -0.01313 0.07998  -0.01049 223 HIS A CD2 
1723 C CE1 . HIS A 223 ? 0.65884 0.85036 0.80766 -0.03552 0.07517  -0.00233 223 HIS A CE1 
1724 N NE2 . HIS A 223 ? 0.64187 0.86243 0.81102 -0.02928 0.08122  -0.00373 223 HIS A NE2 
1725 N N   . LEU A 224 ? 0.48086 0.66110 0.64315 0.01055  0.04641  -0.01832 224 LEU A N   
1726 C CA  . LEU A 224 ? 0.46956 0.67568 0.65547 0.01031  0.04008  -0.01648 224 LEU A CA  
1727 C C   . LEU A 224 ? 0.46756 0.66392 0.64922 0.00320  0.02605  -0.01521 224 LEU A C   
1728 O O   . LEU A 224 ? 0.44720 0.62015 0.61132 0.00784  0.02034  -0.01639 224 LEU A O   
1729 C CB  . LEU A 224 ? 0.47167 0.68837 0.66845 0.02772  0.04088  -0.01871 224 LEU A CB  
1730 C CG  . LEU A 224 ? 0.50369 0.74258 0.72169 0.03407  0.03139  -0.01707 224 LEU A CG  
1731 C CD1 . LEU A 224 ? 0.51799 0.79598 0.76504 0.03046  0.03587  -0.01543 224 LEU A CD1 
1732 C CD2 . LEU A 224 ? 0.50812 0.73870 0.72390 0.05308  0.03076  -0.01877 224 LEU A CD2 
1733 N N   . SER A 225 ? 0.45375 0.66836 0.65119 -0.00851 0.02066  -0.01307 225 SER A N   
1734 C CA  . SER A 225 ? 0.46172 0.66797 0.65484 -0.01615 0.00667  -0.01338 225 SER A CA  
1735 C C   . SER A 225 ? 0.47068 0.70851 0.69009 -0.01809 -0.00192 -0.01258 225 SER A C   
1736 O O   . SER A 225 ? 0.44193 0.70596 0.68339 -0.02666 0.00232  -0.01041 225 SER A O   
1737 C CB  . SER A 225 ? 0.47006 0.65919 0.65163 -0.03229 0.00627  -0.01257 225 SER A CB  
1738 O OG  . SER A 225 ? 0.47298 0.64881 0.64579 -0.03773 -0.00706 -0.01480 225 SER A OG  
1739 N N   . ILE A 226 ? 0.45275 0.68932 0.66982 -0.01070 -0.01421 -0.01378 226 ILE A N   
1740 C CA  . ILE A 226 ? 0.45419 0.72196 0.69558 -0.00917 -0.02435 -0.01306 226 ILE A CA  
1741 C C   . ILE A 226 ? 0.46451 0.72227 0.69516 -0.01532 -0.04110 -0.01525 226 ILE A C   
1742 O O   . ILE A 226 ? 0.44069 0.67011 0.64508 -0.01008 -0.04484 -0.01670 226 ILE A O   
1743 C CB  . ILE A 226 ? 0.49407 0.77429 0.74429 0.01118  -0.02304 -0.01179 226 ILE A CB  
1744 C CG1 . ILE A 226 ? 0.53444 0.81956 0.79046 0.01892  -0.00608 -0.01163 226 ILE A CG1 
1745 C CG2 . ILE A 226 ? 0.50343 0.81989 0.78145 0.01391  -0.03409 -0.01038 226 ILE A CG2 
1746 C CD1 . ILE A 226 ? 0.58594 0.86302 0.83702 0.03958  -0.00329 -0.01181 226 ILE A CD1 
1747 N N   . LEU A 227 ? 0.46391 0.74606 0.71490 -0.02656 -0.05114 -0.01581 227 LEU A N   
1748 C CA  . LEU A 227 ? 0.47227 0.74920 0.71444 -0.03114 -0.06891 -0.01913 227 LEU A CA  
1749 C C   . LEU A 227 ? 0.47889 0.77079 0.72565 -0.01427 -0.07823 -0.01746 227 LEU A C   
1750 O O   . LEU A 227 ? 0.49775 0.82449 0.77324 -0.00878 -0.07944 -0.01481 227 LEU A O   
1751 C CB  . LEU A 227 ? 0.45723 0.75402 0.71974 -0.05090 -0.07767 -0.02100 227 LEU A CB  
1752 C CG  . LEU A 227 ? 0.49209 0.78763 0.74749 -0.05593 -0.09810 -0.02595 227 LEU A CG  
1753 C CD1 . LEU A 227 ? 0.49426 0.74674 0.71087 -0.05580 -0.10117 -0.03063 227 LEU A CD1 
1754 C CD2 . LEU A 227 ? 0.48019 0.79769 0.75966 -0.07695 -0.10728 -0.02817 227 LEU A CD2 
1755 N N   . HIS A 228 ? 0.48035 0.74671 0.69905 -0.00538 -0.08431 -0.01827 228 HIS A N   
1756 C CA  . HIS A 228 ? 0.48611 0.76180 0.70384 0.01021  -0.09455 -0.01543 228 HIS A CA  
1757 C C   . HIS A 228 ? 0.48881 0.76803 0.69901 0.00314  -0.11386 -0.01911 228 HIS A C   
1758 O O   . HIS A 228 ? 0.49148 0.74630 0.67891 -0.00718 -0.11745 -0.02426 228 HIS A O   
1759 C CB  . HIS A 228 ? 0.49632 0.74212 0.68723 0.02511  -0.08786 -0.01242 228 HIS A CB  
1760 C CG  . HIS A 228 ? 0.49465 0.73874 0.69352 0.03463  -0.07164 -0.00948 228 HIS A CG  
1761 N ND1 . HIS A 228 ? 0.49729 0.75042 0.70531 0.05234  -0.07015 -0.00490 228 HIS A ND1 
1762 C CD2 . HIS A 228 ? 0.49003 0.72359 0.68797 0.02926  -0.05681 -0.01096 228 HIS A CD2 
1763 C CE1 . HIS A 228 ? 0.50315 0.75028 0.71503 0.05716  -0.05492 -0.00488 228 HIS A CE1 
1764 N NE2 . HIS A 228 ? 0.50081 0.73720 0.70635 0.04322  -0.04680 -0.00844 228 HIS A NE2 
1765 N N   . ARG A 229 ? 0.48468 0.79439 0.71363 0.00942  -0.12665 -0.01699 229 ARG A N   
1766 C CA  . ARG A 229 ? 0.50034 0.81836 0.72413 0.00314  -0.14705 -0.02092 229 ARG A CA  
1767 C C   . ARG A 229 ? 0.51725 0.83184 0.72344 0.02139  -0.15715 -0.01642 229 ARG A C   
1768 O O   . ARG A 229 ? 0.52329 0.84417 0.73664 0.03876  -0.15155 -0.00918 229 ARG A O   
1769 C CB  . ARG A 229 ? 0.47972 0.84073 0.74205 -0.00771 -0.15674 -0.02225 229 ARG A CB  
1770 C CG  . ARG A 229 ? 0.49306 0.85120 0.76317 -0.03183 -0.15478 -0.02818 229 ARG A CG  
1771 C CD  . ARG A 229 ? 0.48777 0.89078 0.80167 -0.04363 -0.15861 -0.02744 229 ARG A CD  
1772 N NE  . ARG A 229 ? 0.50469 0.89969 0.82316 -0.06797 -0.15637 -0.03195 229 ARG A NE  
1773 C CZ  . ARG A 229 ? 0.50578 0.92918 0.85860 -0.08161 -0.14977 -0.02957 229 ARG A CZ  
1774 N NH1 . ARG A 229 ? 0.48644 0.95113 0.87369 -0.07285 -0.14403 -0.02368 229 ARG A NH1 
1775 N NH2 . ARG A 229 ? 0.53098 0.94049 0.88332 -0.10416 -0.14817 -0.03279 229 ARG A NH2 
1776 N N   . ASP A 230 ? 0.54176 0.84418 0.72283 0.01745  -0.17191 -0.02082 230 ASP A N   
1777 C CA  . ASP A 230 ? 0.56784 0.86628 0.72741 0.03297  -0.18332 -0.01626 230 ASP A CA  
1778 C C   . ASP A 230 ? 0.57581 0.84475 0.71198 0.04832  -0.16906 -0.00902 230 ASP A C   
1779 O O   . ASP A 230 ? 0.59199 0.86547 0.72822 0.06560  -0.17041 -0.00028 230 ASP A O   
1780 C CB  . ASP A 230 ? 0.57281 0.91168 0.76098 0.04244  -0.19679 -0.01118 230 ASP A CB  
1781 C CG  . ASP A 230 ? 0.63540 0.97168 0.79976 0.05660  -0.21216 -0.00640 230 ASP A CG  
1782 O OD1 . ASP A 230 ? 0.67161 0.98733 0.80282 0.05109  -0.22056 -0.01154 230 ASP A OD1 
1783 O OD2 . ASP A 230 ? 0.66469 1.01878 0.84232 0.07397  -0.21559 0.00265  230 ASP A OD2 
1784 N N   . VAL A 231 ? 0.56964 0.80773 0.68624 0.04161  -0.15575 -0.01244 231 VAL A N   
1785 C CA  . VAL A 231 ? 0.56343 0.77349 0.65910 0.05289  -0.14181 -0.00642 231 VAL A CA  
1786 C C   . VAL A 231 ? 0.59038 0.78129 0.64973 0.05968  -0.14940 -0.00423 231 VAL A C   
1787 O O   . VAL A 231 ? 0.60726 0.78941 0.64662 0.05084  -0.15738 -0.01160 231 VAL A O   
1788 C CB  . VAL A 231 ? 0.55582 0.74404 0.64679 0.04319  -0.12529 -0.01070 231 VAL A CB  
1789 C CG1 . VAL A 231 ? 0.53920 0.69712 0.60377 0.05190  -0.11389 -0.00603 231 VAL A CG1 
1790 C CG2 . VAL A 231 ? 0.54939 0.75464 0.67249 0.04061  -0.11475 -0.01011 231 VAL A CG2 
1791 N N   . GLN A 232 ? 0.59182 0.77529 0.64153 0.07560  -0.14668 0.00600  232 GLN A N   
1792 C CA  . GLN A 232 ? 0.59346 0.75649 0.60672 0.08264  -0.15003 0.01049  232 GLN A CA  
1793 C C   . GLN A 232 ? 0.59062 0.72261 0.58387 0.08381  -0.13256 0.01343  232 GLN A C   
1794 O O   . GLN A 232 ? 0.55426 0.66821 0.51586 0.08497  -0.13244 0.01444  232 GLN A O   
1795 C CB  . GLN A 232 ? 0.63063 0.80393 0.64289 0.09931  -0.15974 0.02192  232 GLN A CB  
1796 N N   . GLU A 233 ? 0.55090 0.67781 0.56169 0.08327  -0.11796 0.01443  233 GLU A N   
1797 C CA  . GLU A 233 ? 0.54126 0.64137 0.53632 0.08456  -0.10241 0.01786  233 GLU A CA  
1798 C C   . GLU A 233 ? 0.52448 0.62405 0.54230 0.08112  -0.08910 0.01556  233 GLU A C   
1799 O O   . GLU A 233 ? 0.49437 0.61181 0.53812 0.08491  -0.08998 0.01627  233 GLU A O   
1800 C CB  . GLU A 233 ? 0.56674 0.65473 0.54657 0.09839  -0.10155 0.03048  233 GLU A CB  
1801 C CG  . GLU A 233 ? 0.62402 0.68536 0.58720 0.09826  -0.08649 0.03483  233 GLU A CG  
1802 C CD  . GLU A 233 ? 0.63740 0.68567 0.58724 0.11049  -0.08550 0.04860  233 GLU A CD  
1803 O OE1 . GLU A 233 ? 0.65339 0.71192 0.61384 0.12108  -0.09383 0.05496  233 GLU A OE1 
1804 O OE2 . GLU A 233 ? 0.67153 0.69955 0.60102 0.10960  -0.07625 0.05370  233 GLU A OE2 
1805 N N   . ILE A 234 ? 0.48953 0.56993 0.49711 0.07469  -0.07691 0.01269  234 ILE A N   
1806 C CA  . ILE A 234 ? 0.47775 0.55294 0.50011 0.07244  -0.06358 0.01137  234 ILE A CA  
1807 C C   . ILE A 234 ? 0.48696 0.53819 0.49246 0.07643  -0.05326 0.01715  234 ILE A C   
1808 O O   . ILE A 234 ? 0.49751 0.53551 0.48194 0.07274  -0.05096 0.01673  234 ILE A O   
1809 C CB  . ILE A 234 ? 0.47041 0.54735 0.49902 0.05910  -0.05953 0.00217  234 ILE A CB  
1810 C CG1 . ILE A 234 ? 0.48236 0.58224 0.52721 0.05259  -0.07035 -0.00301 234 ILE A CG1 
1811 C CG2 . ILE A 234 ? 0.46401 0.53681 0.50579 0.05754  -0.04647 0.00121  234 ILE A CG2 
1812 C CD1 . ILE A 234 ? 0.47883 0.57625 0.52496 0.03843  -0.06851 -0.01108 234 ILE A CD1 
1813 N N   . ARG A 235 ? 0.44832 0.49418 0.46350 0.08386  -0.04695 0.02224  235 ARG A N   
1814 C CA  . ARG A 235 ? 0.45075 0.47390 0.45238 0.08708  -0.03828 0.02880  235 ARG A CA  
1815 C C   . ARG A 235 ? 0.45009 0.46485 0.46208 0.08266  -0.02642 0.02457  235 ARG A C   
1816 O O   . ARG A 235 ? 0.42635 0.44927 0.45716 0.08555  -0.02445 0.02156  235 ARG A O   
1817 C CB  . ARG A 235 ? 0.45712 0.47475 0.45709 0.09997  -0.04198 0.03931  235 ARG A CB  
1818 C CG  . ARG A 235 ? 0.54435 0.56689 0.52836 0.10531  -0.05355 0.04557  235 ARG A CG  
1819 C CD  . ARG A 235 ? 0.58164 0.58860 0.55507 0.11659  -0.05379 0.05883  235 ARG A CD  
1820 N NE  . ARG A 235 ? 0.64099 0.64642 0.58950 0.11934  -0.06147 0.06589  235 ARG A NE  
1821 C CZ  . ARG A 235 ? 0.66725 0.65383 0.59523 0.12362  -0.05805 0.07789  235 ARG A CZ  
1822 N NH1 . ARG A 235 ? 0.68035 0.64649 0.61083 0.12464  -0.04767 0.08415  235 ARG A NH1 
1823 N NH2 . ARG A 235 ? 0.70110 0.68894 0.60459 0.12628  -0.06518 0.08372  235 ARG A NH2 
1824 N N   . TYR A 236 ? 0.41220 0.41188 0.41157 0.07636  -0.01861 0.02438  236 TYR A N   
1825 C CA  . TYR A 236 ? 0.43745 0.42833 0.44349 0.07142  -0.00845 0.02047  236 TYR A CA  
1826 C C   . TYR A 236 ? 0.44960 0.42034 0.44723 0.07358  -0.00229 0.02761  236 TYR A C   
1827 O O   . TYR A 236 ? 0.45192 0.41466 0.43354 0.07359  -0.00230 0.03439  236 TYR A O   
1828 C CB  . TYR A 236 ? 0.41735 0.40951 0.41873 0.06113  -0.00494 0.01381  236 TYR A CB  
1829 C CG  . TYR A 236 ? 0.43478 0.44294 0.44597 0.05652  -0.00940 0.00663  236 TYR A CG  
1830 C CD1 . TYR A 236 ? 0.42160 0.43997 0.45089 0.05636  -0.00746 0.00276  236 TYR A CD1 
1831 C CD2 . TYR A 236 ? 0.44324 0.45558 0.44518 0.05195  -0.01508 0.00360  236 TYR A CD2 
1832 C CE1 . TYR A 236 ? 0.41993 0.45354 0.45923 0.05061  -0.01066 -0.00242 236 TYR A CE1 
1833 C CE2 . TYR A 236 ? 0.46301 0.48770 0.47461 0.04595  -0.01936 -0.00254 236 TYR A CE2 
1834 C CZ  . TYR A 236 ? 0.46242 0.49833 0.49337 0.04473  -0.01691 -0.00475 236 TYR A CZ  
1835 O OH  . TYR A 236 ? 0.58638 0.63531 0.62799 0.03737  -0.02031 -0.00944 236 TYR A OH  
1836 N N   . GLU A 237 ? 0.44475 0.40706 0.45262 0.07482  0.00328  0.02585  237 GLU A N   
1837 C CA  . GLU A 237 ? 0.43899 0.38033 0.44116 0.07390  0.00948  0.03101  237 GLU A CA  
1838 C C   . GLU A 237 ? 0.44799 0.38353 0.46165 0.07163  0.01531  0.02347  237 GLU A C   
1839 O O   . GLU A 237 ? 0.42739 0.37373 0.45315 0.07518  0.01449  0.01688  237 GLU A O   
1840 C CB  . GLU A 237 ? 0.47945 0.40858 0.47642 0.08361  0.00612  0.04180  237 GLU A CB  
1841 C CG  . GLU A 237 ? 0.48926 0.42400 0.49945 0.09513  0.00126  0.04079  237 GLU A CG  
1842 C CD  . GLU A 237 ? 0.65602 0.58512 0.65921 0.10632  -0.00558 0.05246  237 GLU A CD  
1843 O OE1 . GLU A 237 ? 0.57932 0.48682 0.57098 0.10701  -0.00291 0.06210  237 GLU A OE1 
1844 O OE2 . GLU A 237 ? 0.56925 0.51625 0.57866 0.11399  -0.01400 0.05261  237 GLU A OE2 
1845 N N   . VAL A 238 ? 0.42098 0.34073 0.43065 0.06526  0.02127  0.02424  238 VAL A N   
1846 C CA  . VAL A 238 ? 0.44338 0.35479 0.46116 0.06320  0.02579  0.01661  238 VAL A CA  
1847 C C   . VAL A 238 ? 0.47007 0.37090 0.49396 0.07435  0.02449  0.01740  238 VAL A C   
1848 O O   . VAL A 238 ? 0.46046 0.34662 0.47941 0.08005  0.02263  0.02667  238 VAL A O   
1849 C CB  . VAL A 238 ? 0.44702 0.34380 0.46017 0.05337  0.03088  0.01766  238 VAL A CB  
1850 C CG1 . VAL A 238 ? 0.44867 0.33552 0.46838 0.05110  0.03405  0.00844  238 VAL A CG1 
1851 C CG2 . VAL A 238 ? 0.42777 0.33719 0.43651 0.04460  0.03233  0.01677  238 VAL A CG2 
1852 N N   . SER A 239 ? 0.42248 0.33066 0.45658 0.07838  0.02584  0.00811  239 SER A N   
1853 C CA  . SER A 239 ? 0.47190 0.37187 0.51315 0.09103  0.02538  0.00719  239 SER A CA  
1854 C C   . SER A 239 ? 0.49991 0.36925 0.53644 0.09057  0.02865  0.00755  239 SER A C   
1855 O O   . SER A 239 ? 0.49040 0.34948 0.52181 0.07906  0.03205  0.00480  239 SER A O   
1856 C CB  . SER A 239 ? 0.47144 0.38862 0.52430 0.09500  0.02796  -0.00365 239 SER A CB  
1857 O OG  . SER A 239 ? 0.49810 0.40931 0.55891 0.10919  0.02835  -0.00546 239 SER A OG  
1858 N N   . ALA A 240 ? 0.52404 0.37840 0.56299 0.10325  0.02695  0.01121  240 ALA A N   
1859 C CA  . ALA A 240 ? 0.53614 0.35874 0.57222 0.10434  0.02991  0.00899  240 ALA A CA  
1860 C C   . ALA A 240 ? 0.56013 0.38231 0.60205 0.10705  0.03424  -0.00630 240 ALA A C   
1861 O O   . ALA A 240 ? 0.58405 0.38046 0.62188 0.10407  0.03684  -0.01201 240 ALA A O   
1862 C CB  . ALA A 240 ? 0.56186 0.36510 0.59717 0.11839  0.02636  0.01884  240 ALA A CB  
1863 N N   . LYS A 241 ? 0.53590 0.38583 0.58655 0.11209  0.03513  -0.01302 241 LYS A N   
1864 C CA  . LYS A 241 ? 0.56612 0.41997 0.62079 0.11528  0.04037  -0.02713 241 LYS A CA  
1865 C C   . LYS A 241 ? 0.55719 0.41866 0.60605 0.09974  0.04326  -0.03422 241 LYS A C   
1866 O O   . LYS A 241 ? 0.50988 0.38590 0.55677 0.08955  0.04138  -0.02907 241 LYS A O   
1867 C CB  . LYS A 241 ? 0.56921 0.45220 0.63716 0.12725  0.04105  -0.02971 241 LYS A CB  
1868 C CG  . LYS A 241 ? 0.59380 0.47650 0.67013 0.14388  0.03666  -0.02178 241 LYS A CG  
1869 C CD  . LYS A 241 ? 0.63115 0.55184 0.72311 0.15072  0.03547  -0.02170 241 LYS A CD  
1870 C CE  . LYS A 241 ? 0.67809 0.60263 0.78101 0.16911  0.03043  -0.01483 241 LYS A CE  
1871 N NZ  . LYS A 241 ? 0.72279 0.68811 0.84393 0.17405  0.02882  -0.01515 241 LYS A NZ  
1872 N N   . LYS A 242 ? 0.55402 0.40500 0.59920 0.09894  0.04745  -0.04648 242 LYS A N   
1873 C CA  . LYS A 242 ? 0.55493 0.41213 0.59356 0.08567  0.04942  -0.05384 242 LYS A CA  
1874 C C   . LYS A 242 ? 0.55941 0.42867 0.59843 0.09142  0.05480  -0.06638 242 LYS A C   
1875 O O   . LYS A 242 ? 0.56155 0.42383 0.60349 0.10479  0.05783  -0.07244 242 LYS A O   
1876 C CB  . LYS A 242 ? 0.61522 0.44473 0.64512 0.07514  0.04811  -0.05641 242 LYS A CB  
1877 C CG  . LYS A 242 ? 0.67313 0.48549 0.70249 0.07124  0.04461  -0.04365 242 LYS A CG  
1878 C CD  . LYS A 242 ? 0.73332 0.52829 0.75713 0.05596  0.04358  -0.04467 242 LYS A CD  
1879 C CE  . LYS A 242 ? 0.77044 0.58845 0.79365 0.04337  0.04312  -0.04377 242 LYS A CE  
1880 N NZ  . LYS A 242 ? 0.79779 0.60435 0.81938 0.02856  0.04170  -0.04143 242 LYS A NZ  
1881 N N   . ILE A 243 ? 0.52771 0.41515 0.56309 0.08213  0.05640  -0.06984 243 ILE A N   
1882 C CA  . ILE A 243 ? 0.53052 0.42839 0.56230 0.08537  0.06222  -0.08132 243 ILE A CA  
1883 C C   . ILE A 243 ? 0.56745 0.44394 0.58572 0.07866  0.06196  -0.09194 243 ILE A C   
1884 O O   . ILE A 243 ? 0.57037 0.43743 0.58384 0.06625  0.05735  -0.08924 243 ILE A O   
1885 C CB  . ILE A 243 ? 0.47872 0.40658 0.51243 0.07911  0.06403  -0.07845 243 ILE A CB  
1886 C CG1 . ILE A 243 ? 0.51699 0.45581 0.54499 0.08244  0.07121  -0.08915 243 ILE A CG1 
1887 C CG2 . ILE A 243 ? 0.47647 0.40397 0.50384 0.06439  0.05942  -0.07354 243 ILE A CG2 
1888 C CD1 . ILE A 243 ? 0.46158 0.42759 0.49048 0.07587  0.07382  -0.08546 243 ILE A CD1 
1889 N N   . HIS A 244 ? 0.56354 0.43324 0.57595 0.08708  0.06677  -0.10457 244 HIS A N   
1890 C CA  . HIS A 244 ? 0.60163 0.44925 0.59974 0.08191  0.06576  -0.11711 244 HIS A CA  
1891 C C   . HIS A 244 ? 0.58278 0.44784 0.56990 0.07994  0.07013  -0.12645 244 HIS A C   
1892 O O   . HIS A 244 ? 0.57087 0.45458 0.56027 0.09001  0.07740  -0.12912 244 HIS A O   
1893 C CB  . HIS A 244 ? 0.63672 0.45555 0.63269 0.09401  0.06726  -0.12607 244 HIS A CB  
1894 C CG  . HIS A 244 ? 0.67475 0.47510 0.68031 0.09801  0.06348  -0.11556 244 HIS A CG  
1895 N ND1 . HIS A 244 ? 0.66362 0.44277 0.66772 0.08584  0.05730  -0.10928 244 HIS A ND1 
1896 C CD2 . HIS A 244 ? 0.68302 0.48402 0.69955 0.11297  0.06496  -0.10936 244 HIS A CD2 
1897 C CE1 . HIS A 244 ? 0.70007 0.46572 0.71172 0.09298  0.05561  -0.09918 244 HIS A CE1 
1898 N NE2 . HIS A 244 ? 0.71605 0.49431 0.73508 0.10990  0.05949  -0.09912 244 HIS A NE2 
1899 N N   . PHE A 245 ? 0.59719 0.45750 0.57269 0.06707  0.06574  -0.13076 245 PHE A N   
1900 C CA  . PHE A 245 ? 0.60953 0.48265 0.57050 0.06444  0.06843  -0.13960 245 PHE A CA  
1901 C C   . PHE A 245 ? 0.65217 0.50071 0.59693 0.06436  0.06666  -0.15634 245 PHE A C   
1902 O O   . PHE A 245 ? 0.68710 0.51134 0.63139 0.05705  0.05975  -0.15872 245 PHE A O   
1903 C CB  . PHE A 245 ? 0.58656 0.47522 0.54515 0.05046  0.06338  -0.13193 245 PHE A CB  
1904 C CG  . PHE A 245 ? 0.58158 0.49230 0.55318 0.04936  0.06445  -0.11711 245 PHE A CG  
1905 C CD1 . PHE A 245 ? 0.54199 0.44832 0.52628 0.04628  0.06017  -0.10627 245 PHE A CD1 
1906 C CD2 . PHE A 245 ? 0.54869 0.48363 0.51847 0.05060  0.06963  -0.11403 245 PHE A CD2 
1907 C CE1 . PHE A 245 ? 0.54671 0.47173 0.54081 0.04518  0.06034  -0.09430 245 PHE A CE1 
1908 C CE2 . PHE A 245 ? 0.54278 0.49543 0.52415 0.04833  0.06969  -0.10137 245 PHE A CE2 
1909 C CZ  . PHE A 245 ? 0.51345 0.46079 0.50655 0.04590  0.06465  -0.09233 245 PHE A CZ  
1910 N N   . ALA A 246 ? 0.69351 0.54830 0.62440 0.07183  0.07299  -0.16812 246 ALA A N   
1911 C CA  . ALA A 246 ? 0.74918 0.58406 0.65991 0.06954  0.07011  -0.18529 246 ALA A CA  
1912 C C   . ALA A 246 ? 0.76606 0.61040 0.66678 0.05389  0.06240  -0.18399 246 ALA A C   
1913 O O   . ALA A 246 ? 0.75278 0.62346 0.65074 0.05166  0.06496  -0.17690 246 ALA A O   
1914 C CB  . ALA A 246 ? 0.83644 0.67671 0.73324 0.08367  0.08019  -0.19853 246 ALA A CB  
1915 N N   . ARG A 247 ? 0.81200 0.63544 0.70875 0.04277  0.05258  -0.18978 247 ARG A N   
1916 C CA  . ARG A 247 ? 0.87360 0.70648 0.76209 0.02859  0.04385  -0.18973 247 ARG A CA  
1917 C C   . ARG A 247 ? 0.94478 0.76328 0.80974 0.02730  0.04003  -0.20940 247 ARG A C   
1918 O O   . ARG A 247 ? 0.98304 0.77257 0.84356 0.02962  0.03848  -0.22224 247 ARG A O   
1919 C CB  . ARG A 247 ? 0.88702 0.71369 0.79140 0.01487  0.03475  -0.18015 247 ARG A CB  
1920 C CG  . ARG A 247 ? 0.96581 0.76056 0.87040 0.00778  0.02785  -0.18995 247 ARG A CG  
1921 C CD  . ARG A 247 ? 1.00020 0.79576 0.91978 -0.00828 0.01920  -0.18013 247 ARG A CD  
1922 N NE  . ARG A 247 ? 1.00482 0.82383 0.92067 -0.01815 0.01242  -0.17830 247 ARG A NE  
1923 C CZ  . ARG A 247 ? 1.03962 0.85574 0.94251 -0.02650 0.00379  -0.19097 247 ARG A CZ  
1924 N NH1 . ARG A 247 ? 1.04052 0.82995 0.93108 -0.02692 0.00100  -0.20803 247 ARG A NH1 
1925 N NH2 . ARG A 247 ? 0.95485 0.79481 0.85660 -0.03413 -0.00287 -0.18680 247 ARG A NH2 
1926 N N   . PHE A 248 ? 0.93941 0.77679 0.78772 0.02421  0.03837  -0.21187 248 PHE A N   
1927 C CA  . PHE A 248 ? 0.99018 0.81726 0.81277 0.02248  0.03355  -0.23047 248 PHE A CA  
1928 C C   . PHE A 248 ? 1.01092 0.84608 0.82762 0.00723  0.02003  -0.23036 248 PHE A C   
1929 O O   . PHE A 248 ? 1.04454 0.86614 0.84327 0.00227  0.01200  -0.24670 248 PHE A O   
1930 C CB  . PHE A 248 ? 1.06457 0.90633 0.86612 0.03503  0.04436  -0.23650 248 PHE A CB  
1931 C CG  . PHE A 248 ? 1.16225 0.99298 0.96493 0.05138  0.05667  -0.24373 248 PHE A CG  
1932 C CD1 . PHE A 248 ? 1.12263 0.92415 0.91111 0.05723  0.05614  -0.26393 248 PHE A CD1 
1933 C CD2 . PHE A 248 ? 1.11850 0.96778 0.93736 0.06116  0.06816  -0.23076 248 PHE A CD2 
1934 C CE1 . PHE A 248 ? 1.13157 0.92285 0.92194 0.07435  0.06755  -0.27077 248 PHE A CE1 
1935 C CE2 . PHE A 248 ? 1.10385 0.94609 0.92626 0.07731  0.07905  -0.23715 248 PHE A CE2 
1936 C CZ  . PHE A 248 ? 1.12391 0.93720 0.93210 0.08479  0.07907  -0.25701 248 PHE A CZ  
1937 N N   . ARG A 249 ? 0.91932 0.77610 0.75060 0.00022  0.01678  -0.21320 249 ARG A N   
1938 C CA  . ARG A 249 ? 0.88469 0.75074 0.71612 -0.01350 0.00340  -0.21141 249 ARG A CA  
1939 C C   . ARG A 249 ? 0.84761 0.72651 0.70573 -0.01964 0.00174  -0.19257 249 ARG A C   
1940 O O   . ARG A 249 ? 0.80788 0.68935 0.68043 -0.01329 0.01056  -0.18130 249 ARG A O   
1941 C CB  . ARG A 249 ? 0.87657 0.76273 0.68456 -0.01236 0.00095  -0.21302 249 ARG A CB  
1942 C CG  . ARG A 249 ? 0.89384 0.79797 0.69559 -0.00109 0.01380  -0.20306 249 ARG A CG  
1943 C CD  . ARG A 249 ? 0.88628 0.81266 0.67205 -0.00339 0.00933  -0.19652 249 ARG A CD  
1944 N NE  . ARG A 249 ? 0.90076 0.84140 0.67465 0.00631  0.02200  -0.18974 249 ARG A NE  
1945 C CZ  . ARG A 249 ? 0.88552 0.83814 0.67563 0.00968  0.03067  -0.17371 249 ARG A CZ  
1946 N NH1 . ARG A 249 ? 0.87430 0.82571 0.69139 0.00587  0.02871  -0.16334 249 ARG A NH1 
1947 N NH2 . ARG A 249 ? 0.88926 0.85555 0.66766 0.01649  0.04165  -0.16805 249 ARG A NH2 
1948 N N   . SER A 250 ? 0.81637 0.70446 0.68095 -0.03171 -0.00993 -0.18976 250 SER A N   
1949 C CA  . SER A 250 ? 0.75914 0.66125 0.64769 -0.03707 -0.01147 -0.17292 250 SER A CA  
1950 C C   . SER A 250 ? 0.72273 0.64884 0.60868 -0.03070 -0.00720 -0.15974 250 SER A C   
1951 O O   . SER A 250 ? 0.70554 0.64505 0.57546 -0.03059 -0.01185 -0.16116 250 SER A O   
1952 C CB  . SER A 250 ? 0.75679 0.66384 0.65529 -0.05146 -0.02482 -0.17441 250 SER A CB  
1953 O OG  . SER A 250 ? 0.73989 0.66299 0.66098 -0.05511 -0.02502 -0.15831 250 SER A OG  
1954 N N   . PHE A 251 ? 0.67716 0.60714 0.57752 -0.02545 0.00124  -0.14699 251 PHE A N   
1955 C CA  . PHE A 251 ? 0.65539 0.60536 0.55830 -0.02176 0.00416  -0.13283 251 PHE A CA  
1956 C C   . PHE A 251 ? 0.62008 0.57195 0.54653 -0.02392 0.00554  -0.12069 251 PHE A C   
1957 O O   . PHE A 251 ? 0.61242 0.56047 0.54655 -0.01806 0.01375  -0.11488 251 PHE A O   
1958 C CB  . PHE A 251 ? 0.68356 0.63679 0.57471 -0.01153 0.01496  -0.13142 251 PHE A CB  
1959 C CG  . PHE A 251 ? 0.70458 0.67602 0.59210 -0.00944 0.01649  -0.11900 251 PHE A CG  
1960 C CD1 . PHE A 251 ? 0.67100 0.65360 0.56328 -0.01448 0.00802  -0.11114 251 PHE A CD1 
1961 C CD2 . PHE A 251 ? 0.73860 0.71585 0.61900 -0.00237 0.02655  -0.11486 251 PHE A CD2 
1962 C CE1 . PHE A 251 ? 0.66404 0.65939 0.55207 -0.01183 0.00916  -0.09954 251 PHE A CE1 
1963 C CE2 . PHE A 251 ? 0.74086 0.73162 0.61772 -0.00171 0.02789  -0.10282 251 PHE A CE2 
1964 C CZ  . PHE A 251 ? 0.70099 0.69884 0.58069 -0.00611 0.01898  -0.09523 251 PHE A CZ  
1965 N N   . PRO A 252 ? 0.60005 0.55904 0.53848 -0.03219 -0.00248 -0.11693 252 PRO A N   
1966 C CA  . PRO A 252 ? 0.58211 0.54234 0.54162 -0.03452 -0.00050 -0.10649 252 PRO A CA  
1967 C C   . PRO A 252 ? 0.53190 0.50223 0.49512 -0.02720 0.00581  -0.09411 252 PRO A C   
1968 O O   . PRO A 252 ? 0.48276 0.46438 0.43670 -0.02342 0.00558  -0.09045 252 PRO A O   
1969 C CB  . PRO A 252 ? 0.56368 0.53625 0.53350 -0.04402 -0.01019 -0.10518 252 PRO A CB  
1970 C CG  . PRO A 252 ? 0.59946 0.56886 0.55565 -0.04906 -0.01841 -0.11852 252 PRO A CG  
1971 C CD  . PRO A 252 ? 0.61189 0.57876 0.54557 -0.04000 -0.01393 -0.12305 252 PRO A CD  
1972 N N   . PHE A 253 ? 0.55185 0.51667 0.52797 -0.02568 0.01100  -0.08745 253 PHE A N   
1973 C CA  . PHE A 253 ? 0.48947 0.46154 0.46941 -0.01949 0.01628  -0.07696 253 PHE A CA  
1974 C C   . PHE A 253 ? 0.42044 0.40862 0.40211 -0.01998 0.01229  -0.06961 253 PHE A C   
1975 O O   . PHE A 253 ? 0.40526 0.39927 0.38058 -0.01506 0.01446  -0.06462 253 PHE A O   
1976 C CB  . PHE A 253 ? 0.50755 0.47194 0.50036 -0.01900 0.02025  -0.07129 253 PHE A CB  
1977 C CG  . PHE A 253 ? 0.45121 0.42242 0.44780 -0.01361 0.02422  -0.06163 253 PHE A CG  
1978 C CD1 . PHE A 253 ? 0.47542 0.44518 0.46763 -0.00711 0.02922  -0.06092 253 PHE A CD1 
1979 C CD2 . PHE A 253 ? 0.46485 0.44447 0.46988 -0.01509 0.02295  -0.05386 253 PHE A CD2 
1980 C CE1 . PHE A 253 ? 0.48346 0.45874 0.47929 -0.00356 0.03157  -0.05297 253 PHE A CE1 
1981 C CE2 . PHE A 253 ? 0.43000 0.41343 0.43650 -0.01014 0.02596  -0.04657 253 PHE A CE2 
1982 C CZ  . PHE A 253 ? 0.43401 0.41453 0.43574 -0.00505 0.02962  -0.04630 253 PHE A CZ  
1983 N N   . TRP A 254 ? 0.44198 0.43757 0.43312 -0.02586 0.00644  -0.06864 254 TRP A N   
1984 C CA  . TRP A 254 ? 0.43572 0.44719 0.43043 -0.02437 0.00266  -0.06155 254 TRP A CA  
1985 C C   . TRP A 254 ? 0.43092 0.44949 0.41115 -0.02261 -0.00266 -0.06379 254 TRP A C   
1986 O O   . TRP A 254 ? 0.38807 0.41522 0.36595 -0.01797 -0.00404 -0.05665 254 TRP A O   
1987 C CB  . TRP A 254 ? 0.42389 0.44541 0.43501 -0.03063 -0.00171 -0.05982 254 TRP A CB  
1988 C CG  . TRP A 254 ? 0.40784 0.42441 0.43200 -0.03220 0.00416  -0.05499 254 TRP A CG  
1989 C CD1 . TRP A 254 ? 0.42164 0.43252 0.45592 -0.04032 0.00424  -0.05711 254 TRP A CD1 
1990 C CD2 . TRP A 254 ? 0.39799 0.41381 0.42470 -0.02582 0.01057  -0.04694 254 TRP A CD2 
1991 N NE1 . TRP A 254 ? 0.39259 0.39997 0.43477 -0.03887 0.01089  -0.04967 254 TRP A NE1 
1992 C CE2 . TRP A 254 ? 0.41005 0.42090 0.44717 -0.02972 0.01450  -0.04406 254 TRP A CE2 
1993 C CE3 . TRP A 254 ? 0.40697 0.42467 0.42728 -0.01779 0.01296  -0.04198 254 TRP A CE3 
1994 C CZ2 . TRP A 254 ? 0.38656 0.39581 0.42616 -0.02495 0.02049  -0.03680 254 TRP A CZ2 
1995 C CZ3 . TRP A 254 ? 0.38357 0.39872 0.40754 -0.01378 0.01828  -0.03599 254 TRP A CZ3 
1996 C CH2 . TRP A 254 ? 0.38792 0.39962 0.42061 -0.01690 0.02189  -0.03366 254 TRP A CH2 
1997 N N   . ARG A 255 ? 0.44644 0.46027 0.41532 -0.02582 -0.00591 -0.07357 255 ARG A N   
1998 C CA  . ARG A 255 ? 0.47245 0.49165 0.42294 -0.02316 -0.00966 -0.07525 255 ARG A CA  
1999 C C   . ARG A 255 ? 0.46960 0.48388 0.40850 -0.01649 -0.00122 -0.07099 255 ARG A C   
2000 O O   . ARG A 255 ? 0.49615 0.51660 0.42505 -0.01291 -0.00211 -0.06457 255 ARG A O   
2001 C CB  . ARG A 255 ? 0.49349 0.50825 0.43241 -0.02815 -0.01520 -0.08825 255 ARG A CB  
2002 C CG  . ARG A 255 ? 0.56785 0.58547 0.48256 -0.02459 -0.01701 -0.09120 255 ARG A CG  
2003 C CD  . ARG A 255 ? 0.57580 0.59541 0.48029 -0.03046 -0.02760 -0.10296 255 ARG A CD  
2004 N NE  . ARG A 255 ? 0.59566 0.63254 0.50779 -0.03335 -0.03901 -0.09826 255 ARG A NE  
2005 C CZ  . ARG A 255 ? 0.63589 0.67922 0.55152 -0.04119 -0.05051 -0.10638 255 ARG A CZ  
2006 N NH1 . ARG A 255 ? 0.65871 0.68931 0.57011 -0.04794 -0.05251 -0.12029 255 ARG A NH1 
2007 N NH2 . ARG A 255 ? 0.62017 0.68314 0.54456 -0.04217 -0.06072 -0.10068 255 ARG A NH2 
2008 N N   . ARG A 256 ? 0.44515 0.44876 0.38651 -0.01492 0.00688  -0.07364 256 ARG A N   
2009 C CA  . ARG A 256 ? 0.48403 0.48611 0.41962 -0.00960 0.01524  -0.06900 256 ARG A CA  
2010 C C   . ARG A 256 ? 0.49145 0.49842 0.43438 -0.00740 0.01609  -0.05711 256 ARG A C   
2011 O O   . ARG A 256 ? 0.46623 0.47567 0.40050 -0.00496 0.01878  -0.05119 256 ARG A O   
2012 C CB  . ARG A 256 ? 0.55143 0.54355 0.49308 -0.00766 0.02239  -0.07364 256 ARG A CB  
2013 C CG  . ARG A 256 ? 0.66382 0.65697 0.59817 -0.00269 0.03089  -0.07309 256 ARG A CG  
2014 C CD  . ARG A 256 ? 0.67681 0.66098 0.61004 0.00041  0.03582  -0.08321 256 ARG A CD  
2015 N NE  . ARG A 256 ? 0.57466 0.55102 0.52389 0.00181  0.03764  -0.08177 256 ARG A NE  
2016 C CZ  . ARG A 256 ? 0.61819 0.58287 0.57354 -0.00078 0.03421  -0.08667 256 ARG A CZ  
2017 N NH1 . ARG A 256 ? 0.67839 0.63836 0.62741 -0.00600 0.02807  -0.09431 256 ARG A NH1 
2018 N NH2 . ARG A 256 ? 0.61930 0.57665 0.58717 0.00138  0.03654  -0.08343 256 ARG A NH2 
2019 N N   . VAL A 257 ? 0.42179 0.42925 0.37987 -0.00841 0.01417  -0.05357 257 VAL A N   
2020 C CA  . VAL A 257 ? 0.43170 0.44253 0.39522 -0.00555 0.01413  -0.04404 257 VAL A CA  
2021 C C   . VAL A 257 ? 0.44057 0.45866 0.39600 -0.00404 0.00810  -0.03971 257 VAL A C   
2022 O O   . VAL A 257 ? 0.43439 0.45104 0.38416 -0.00082 0.00930  -0.03245 257 VAL A O   
2023 C CB  . VAL A 257 ? 0.41476 0.42627 0.39418 -0.00632 0.01369  -0.04209 257 VAL A CB  
2024 C CG1 . VAL A 257 ? 0.38149 0.39637 0.36452 -0.00216 0.01304  -0.03400 257 VAL A CG1 
2025 C CG2 . VAL A 257 ? 0.40129 0.40411 0.38661 -0.00654 0.01946  -0.04407 257 VAL A CG2 
2026 N N   . HIS A 258 ? 0.41589 0.44134 0.37087 -0.00650 0.00083  -0.04377 258 HIS A N   
2027 C CA  . HIS A 258 ? 0.47181 0.50575 0.41918 -0.00398 -0.00642 -0.03932 258 HIS A CA  
2028 C C   . HIS A 258 ? 0.50604 0.53621 0.43295 -0.00200 -0.00451 -0.03678 258 HIS A C   
2029 O O   . HIS A 258 ? 0.50520 0.53498 0.42562 0.00205  -0.00566 -0.02781 258 HIS A O   
2030 C CB  . HIS A 258 ? 0.45889 0.50336 0.40944 -0.00809 -0.01556 -0.04559 258 HIS A CB  
2031 C CG  . HIS A 258 ? 0.48324 0.53743 0.42266 -0.00521 -0.02441 -0.04226 258 HIS A CG  
2032 N ND1 . HIS A 258 ? 0.53421 0.58682 0.45189 -0.00545 -0.02658 -0.04521 258 HIS A ND1 
2033 C CD2 . HIS A 258 ? 0.47735 0.54356 0.42368 -0.00103 -0.03178 -0.03593 258 HIS A CD2 
2034 C CE1 . HIS A 258 ? 0.52740 0.58986 0.43798 -0.00196 -0.03562 -0.04013 258 HIS A CE1 
2035 N NE2 . HIS A 258 ? 0.55359 0.62456 0.48232 0.00116  -0.03918 -0.03446 258 HIS A NE2 
2036 N N   . ASP A 259 ? 0.50843 0.53504 0.42444 -0.00454 -0.00102 -0.04438 259 ASP A N   
2037 C CA  . ASP A 259 ? 0.57741 0.60300 0.47265 -0.00301 0.00197  -0.04216 259 ASP A CA  
2038 C C   . ASP A 259 ? 0.59921 0.61941 0.49453 -0.00112 0.01013  -0.03281 259 ASP A C   
2039 O O   . ASP A 259 ? 0.61825 0.63816 0.49906 0.00009  0.01125  -0.02534 259 ASP A O   
2040 C CB  . ASP A 259 ? 0.59288 0.61608 0.47740 -0.00496 0.00562  -0.05369 259 ASP A CB  
2041 C CG  . ASP A 259 ? 0.59631 0.62335 0.47549 -0.00801 -0.00399 -0.06357 259 ASP A CG  
2042 O OD1 . ASP A 259 ? 0.54392 0.57899 0.42761 -0.00864 -0.01374 -0.06028 259 ASP A OD1 
2043 O OD2 . ASP A 259 ? 0.60152 0.62377 0.47255 -0.00962 -0.00217 -0.07513 259 ASP A OD2 
2044 N N   . SER A 260 ? 0.52027 0.53597 0.43133 -0.00146 0.01530  -0.03258 260 SER A N   
2045 C CA  . SER A 260 ? 0.53110 0.54237 0.44384 -0.00122 0.02230  -0.02531 260 SER A CA  
2046 C C   . SER A 260 ? 0.55332 0.56026 0.47022 0.00068  0.01888  -0.01563 260 SER A C   
2047 O O   . SER A 260 ? 0.57148 0.57352 0.48250 0.00004  0.02200  -0.00774 260 SER A O   
2048 C CB  . SER A 260 ? 0.52428 0.53328 0.45088 -0.00194 0.02836  -0.02979 260 SER A CB  
2049 O OG  . SER A 260 ? 0.57624 0.58697 0.49871 -0.00208 0.03267  -0.03852 260 SER A OG  
2050 N N   . PHE A 261 ? 0.50470 0.51292 0.43204 0.00298  0.01301  -0.01613 261 PHE A N   
2051 C CA  . PHE A 261 ? 0.51035 0.51321 0.44249 0.00657  0.01063  -0.00870 261 PHE A CA  
2052 C C   . PHE A 261 ? 0.50618 0.51295 0.43431 0.01138  0.00244  -0.00434 261 PHE A C   
2053 O O   . PHE A 261 ? 0.50429 0.50364 0.43065 0.01568  0.00070  0.00317  261 PHE A O   
2054 C CB  . PHE A 261 ? 0.44812 0.44994 0.39650 0.00739  0.01205  -0.01169 261 PHE A CB  
2055 C CG  . PHE A 261 ? 0.45275 0.45051 0.40594 0.00420  0.01874  -0.01436 261 PHE A CG  
2056 C CD1 . PHE A 261 ? 0.47168 0.46184 0.42360 0.00318  0.02196  -0.00959 261 PHE A CD1 
2057 C CD2 . PHE A 261 ? 0.44588 0.44713 0.40545 0.00215  0.02113  -0.02145 261 PHE A CD2 
2058 C CE1 . PHE A 261 ? 0.46091 0.45068 0.41909 0.00044  0.02695  -0.01193 261 PHE A CE1 
2059 C CE2 . PHE A 261 ? 0.46041 0.45908 0.42506 0.00085  0.02650  -0.02327 261 PHE A CE2 
2060 C CZ  . PHE A 261 ? 0.44511 0.43985 0.40972 0.00014  0.02917  -0.01854 261 PHE A CZ  
2061 N N   . ILE A 262 ? 0.47419 0.49196 0.40109 0.01103  -0.00328 -0.00898 262 ILE A N   
2062 C CA  . ILE A 262 ? 0.52776 0.55283 0.45349 0.01633  -0.01227 -0.00469 262 ILE A CA  
2063 C C   . ILE A 262 ? 0.58246 0.60735 0.48718 0.01698  -0.01588 -0.00017 262 ILE A C   
2064 O O   . ILE A 262 ? 0.58039 0.60001 0.47703 0.02239  -0.01918 0.00951  262 ILE A O   
2065 C CB  . ILE A 262 ? 0.48978 0.53001 0.42945 0.01508  -0.01809 -0.01161 262 ILE A CB  
2066 C CG1 . ILE A 262 ? 0.48352 0.52353 0.44191 0.01402  -0.01308 -0.01463 262 ILE A CG1 
2067 C CG2 . ILE A 262 ? 0.51979 0.57144 0.46172 0.02157  -0.02787 -0.00669 262 ILE A CG2 
2068 C CD1 . ILE A 262 ? 0.45225 0.48778 0.41749 0.02127  -0.01164 -0.00813 262 ILE A CD1 
2069 N N   . GLU A 263 ? 0.59353 0.62270 0.48769 0.01206  -0.01508 -0.00698 263 GLU A N   
2070 C CA  . GLU A 263 ? 0.71441 0.74520 0.58555 0.01262  -0.01833 -0.00374 263 GLU A CA  
2071 C C   . GLU A 263 ? 0.76283 0.79768 0.62344 0.00746  -0.01607 -0.01472 263 GLU A C   
2072 O O   . GLU A 263 ? 0.73826 0.77750 0.61032 0.00405  -0.01749 -0.02545 263 GLU A O   
2073 C CB  . GLU A 263 ? 0.74962 0.79028 0.61816 0.01799  -0.03092 0.00028  263 GLU A CB  
2074 C CG  . GLU A 263 ? 0.77334 0.82841 0.66059 0.01659  -0.03816 -0.00857 263 GLU A CG  
2075 C CD  . GLU A 263 ? 0.80792 0.87801 0.68921 0.01923  -0.05164 -0.00839 263 GLU A CD  
2076 O OE1 . GLU A 263 ? 0.78221 0.85150 0.63969 0.02019  -0.05503 -0.00563 263 GLU A OE1 
2077 O OE2 . GLU A 263 ? 0.82147 0.90573 0.72208 0.02029  -0.05883 -0.01070 263 GLU A OE2 
2078 N N   . ASP A 264 ? 0.93202 0.96460 0.77003 0.00699  -0.01230 -0.01213 264 ASP A N   
2079 C CA  . ASP A 264 ? 0.98492 1.02105 0.80886 0.00388  -0.01021 -0.02341 264 ASP A CA  
2080 C C   . ASP A 264 ? 1.16617 1.20590 0.96104 0.00581  -0.01396 -0.01924 264 ASP A C   
2081 O O   . ASP A 264 ? 1.25701 1.29922 1.04522 0.00961  -0.02268 -0.00969 264 ASP A O   
2082 C CB  . ASP A 264 ? 1.04501 1.07544 0.87176 0.00142  0.00346  -0.02738 264 ASP A CB  
2083 C CG  . ASP A 264 ? 1.08901 1.12137 0.90510 -0.00018 0.00610  -0.04177 264 ASP A CG  
2084 O OD1 . ASP A 264 ? 1.08151 1.11824 0.88747 -0.00075 -0.00325 -0.04954 264 ASP A OD1 
2085 O OD2 . ASP A 264 ? 1.00780 1.03735 0.82597 -0.00052 0.01712  -0.04588 264 ASP A OD2 
# 
