data_8QGO
# 
_entry.id   8QGO 
# 
_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   8QGO         pdb_00008qgo 10.2210/pdb8qgo/pdb 
WWPDB D_1292133184 ?            ?                   
# 
_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                        8QGO 
_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-methyl-amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
653.650   1   ?        ? ? ? 
4 water       nat water 18.015    134 ?        ? ? ? 
# 
_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-methyl-amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
UOL 
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 
UOL 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-methyl-amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-ethyl-urea
;
? 'C27 H35 N13 O7' 653.650 
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 111 111 111 ILE ILE A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 LYS 113 113 113 LYS LYS 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        UOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UOL 
_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 UOL 1   302 1   UOL UNC A . 
D 4 HOH 1   401 159 HOH HOH A . 
D 4 HOH 2   402 153 HOH HOH A . 
D 4 HOH 3   403 113 HOH HOH A . 
D 4 HOH 4   404 64  HOH HOH A . 
D 4 HOH 5   405 157 HOH HOH A . 
D 4 HOH 6   406 68  HOH HOH A . 
D 4 HOH 7   407 11  HOH HOH A . 
D 4 HOH 8   408 97  HOH HOH A . 
D 4 HOH 9   409 92  HOH HOH A . 
D 4 HOH 10  410 31  HOH HOH A . 
D 4 HOH 11  411 4   HOH HOH A . 
D 4 HOH 12  412 141 HOH HOH A . 
D 4 HOH 13  413 26  HOH HOH A . 
D 4 HOH 14  414 7   HOH HOH A . 
D 4 HOH 15  415 42  HOH HOH A . 
D 4 HOH 16  416 36  HOH HOH A . 
D 4 HOH 17  417 55  HOH HOH A . 
D 4 HOH 18  418 15  HOH HOH A . 
D 4 HOH 19  419 13  HOH HOH A . 
D 4 HOH 20  420 9   HOH HOH A . 
D 4 HOH 21  421 104 HOH HOH A . 
D 4 HOH 22  422 101 HOH HOH A . 
D 4 HOH 23  423 16  HOH HOH A . 
D 4 HOH 24  424 74  HOH HOH A . 
D 4 HOH 25  425 164 HOH HOH A . 
D 4 HOH 26  426 12  HOH HOH A . 
D 4 HOH 27  427 21  HOH HOH A . 
D 4 HOH 28  428 52  HOH HOH A . 
D 4 HOH 29  429 34  HOH HOH A . 
D 4 HOH 30  430 2   HOH HOH A . 
D 4 HOH 31  431 114 HOH HOH A . 
D 4 HOH 32  432 23  HOH HOH A . 
D 4 HOH 33  433 1   HOH HOH A . 
D 4 HOH 34  434 56  HOH HOH A . 
D 4 HOH 35  435 75  HOH HOH A . 
D 4 HOH 36  436 33  HOH HOH A . 
D 4 HOH 37  437 20  HOH HOH A . 
D 4 HOH 38  438 156 HOH HOH A . 
D 4 HOH 39  439 60  HOH HOH A . 
D 4 HOH 40  440 62  HOH HOH A . 
D 4 HOH 41  441 5   HOH HOH A . 
D 4 HOH 42  442 102 HOH HOH A . 
D 4 HOH 43  443 10  HOH HOH A . 
D 4 HOH 44  444 71  HOH HOH A . 
D 4 HOH 45  445 82  HOH HOH A . 
D 4 HOH 46  446 18  HOH HOH A . 
D 4 HOH 47  447 148 HOH HOH A . 
D 4 HOH 48  448 3   HOH HOH A . 
D 4 HOH 49  449 132 HOH HOH A . 
D 4 HOH 50  450 43  HOH HOH A . 
D 4 HOH 51  451 87  HOH HOH A . 
D 4 HOH 52  452 27  HOH HOH A . 
D 4 HOH 53  453 83  HOH HOH A . 
D 4 HOH 54  454 29  HOH HOH A . 
D 4 HOH 55  455 95  HOH HOH A . 
D 4 HOH 56  456 105 HOH HOH A . 
D 4 HOH 57  457 49  HOH HOH A . 
D 4 HOH 58  458 138 HOH HOH A . 
D 4 HOH 59  459 37  HOH HOH A . 
D 4 HOH 60  460 96  HOH HOH A . 
D 4 HOH 61  461 150 HOH HOH A . 
D 4 HOH 62  462 78  HOH HOH A . 
D 4 HOH 63  463 59  HOH HOH A . 
D 4 HOH 64  464 8   HOH HOH A . 
D 4 HOH 65  465 69  HOH HOH A . 
D 4 HOH 66  466 19  HOH HOH A . 
D 4 HOH 67  467 135 HOH HOH A . 
D 4 HOH 68  468 152 HOH HOH A . 
D 4 HOH 69  469 39  HOH HOH A . 
D 4 HOH 70  470 17  HOH HOH A . 
D 4 HOH 71  471 168 HOH HOH A . 
D 4 HOH 72  472 51  HOH HOH A . 
D 4 HOH 73  473 81  HOH HOH A . 
D 4 HOH 74  474 6   HOH HOH A . 
D 4 HOH 75  475 47  HOH HOH A . 
D 4 HOH 76  476 35  HOH HOH A . 
D 4 HOH 77  477 85  HOH HOH A . 
D 4 HOH 78  478 46  HOH HOH A . 
D 4 HOH 79  479 149 HOH HOH A . 
D 4 HOH 80  480 120 HOH HOH A . 
D 4 HOH 81  481 24  HOH HOH A . 
D 4 HOH 82  482 45  HOH HOH A . 
D 4 HOH 83  483 76  HOH HOH A . 
D 4 HOH 84  484 126 HOH HOH A . 
D 4 HOH 85  485 41  HOH HOH A . 
D 4 HOH 86  486 154 HOH HOH A . 
D 4 HOH 87  487 123 HOH HOH A . 
D 4 HOH 88  488 107 HOH HOH A . 
D 4 HOH 89  489 44  HOH HOH A . 
D 4 HOH 90  490 28  HOH HOH A . 
D 4 HOH 91  491 40  HOH HOH A . 
D 4 HOH 92  492 98  HOH HOH A . 
D 4 HOH 93  493 38  HOH HOH A . 
D 4 HOH 94  494 111 HOH HOH A . 
D 4 HOH 95  495 48  HOH HOH A . 
D 4 HOH 96  496 166 HOH HOH A . 
D 4 HOH 97  497 25  HOH HOH A . 
D 4 HOH 98  498 88  HOH HOH A . 
D 4 HOH 99  499 115 HOH HOH A . 
D 4 HOH 100 500 91  HOH HOH A . 
D 4 HOH 101 501 118 HOH HOH A . 
D 4 HOH 102 502 119 HOH HOH A . 
D 4 HOH 103 503 93  HOH HOH A . 
D 4 HOH 104 504 169 HOH HOH A . 
D 4 HOH 105 505 162 HOH HOH A . 
D 4 HOH 106 506 84  HOH HOH A . 
D 4 HOH 107 507 63  HOH HOH A . 
D 4 HOH 108 508 73  HOH HOH A . 
D 4 HOH 109 509 22  HOH HOH A . 
D 4 HOH 110 510 161 HOH HOH A . 
D 4 HOH 111 511 67  HOH HOH A . 
D 4 HOH 112 512 122 HOH HOH A . 
D 4 HOH 113 513 54  HOH HOH A . 
D 4 HOH 114 514 163 HOH HOH A . 
D 4 HOH 115 515 14  HOH HOH A . 
D 4 HOH 116 516 151 HOH HOH A . 
D 4 HOH 117 517 145 HOH HOH A . 
D 4 HOH 118 518 129 HOH HOH A . 
D 4 HOH 119 519 142 HOH HOH A . 
D 4 HOH 120 520 160 HOH HOH A . 
D 4 HOH 121 521 66  HOH HOH A . 
D 4 HOH 122 522 58  HOH HOH A . 
D 4 HOH 123 523 99  HOH HOH A . 
D 4 HOH 124 524 89  HOH HOH A . 
D 4 HOH 125 525 158 HOH HOH A . 
D 4 HOH 126 526 167 HOH HOH A . 
D 4 HOH 127 527 139 HOH HOH A . 
D 4 HOH 128 528 53  HOH HOH A . 
D 4 HOH 129 529 165 HOH HOH A . 
D 4 HOH 130 530 30  HOH HOH A . 
D 4 HOH 131 531 124 HOH HOH A . 
D 4 HOH 132 532 90  HOH HOH A . 
D 4 HOH 133 533 155 HOH HOH A . 
D 4 HOH 134 534 112 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
6  1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
7  1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
8  1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
9  1 Y 1 A ILE 111 ? CG1 ? A ILE 111 CG1 
10 1 Y 1 A ILE 111 ? CG2 ? A ILE 111 CG2 
11 1 Y 1 A ILE 111 ? CD1 ? A ILE 111 CD1 
12 1 Y 1 A LYS 113 ? CG  ? A LYS 113 CG  
13 1 Y 1 A LYS 113 ? CD  ? A LYS 113 CD  
14 1 Y 1 A LYS 113 ? CE  ? A LYS 113 CE  
15 1 Y 1 A LYS 113 ? NZ  ? A LYS 113 NZ  
16 1 Y 1 A LYS 114 ? CG  ? A LYS 114 CG  
17 1 Y 1 A LYS 114 ? CD  ? A LYS 114 CD  
18 1 Y 1 A LYS 114 ? CE  ? A LYS 114 CE  
19 1 Y 1 A LYS 114 ? NZ  ? A LYS 114 NZ  
20 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
21 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
22 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
23 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
24 1 Y 1 A ASP 264 ? CG  ? A ASP 264 CG  
25 1 Y 1 A ASP 264 ? OD1 ? A ASP 264 OD1 
26 1 Y 1 A ASP 264 ? OD2 ? A ASP 264 OD2 
# 
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                     8QGO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.969 
_cell.length_a_esd                 ? 
_cell.length_b                     74.436 
_cell.length_b_esd                 ? 
_cell.length_c                     118.370 
_cell.length_c_esd                 ? 
_cell.volume                       554819.192 
_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                         8QGO 
_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                   8QGO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.94 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.965459 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965459 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          21.97 
_reflns.entry_id                                       8QGO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.247 
_reflns.d_resolution_low                               59.185 
_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                                     76054 
_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                           98.66 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.4 
_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                                0.034 
_reflns.pdbx_Rpim_I_all                                0.016 
_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                              0.029 
_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                                    1.247 
_reflns_shell.d_res_low                                     1.393 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13615 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2330 
_reflns_shell.percent_possible_obs                          10.7 
_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                               5.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               0.951 
_reflns_shell.pdbx_Rpim_I_all                               0.391 
_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                                  0.865 
_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                               33.30 
_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                                 8QGO 
_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                            1.53 
_refine.ls_d_res_low                             55.59 
_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                     76054 
_refine.ls_number_reflns_R_free                  3746 
_refine.ls_number_reflns_R_work                  72308 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.04 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1635 
_refine.ls_R_factor_R_free                       0.2000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1616 
_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                      8A9V 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.3721 
_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                            0.2014 
_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                       1.53 
_refine_hist.d_res_low                        55.59 
_refine_hist.number_atoms_solvent             134 
_refine_hist.number_atoms_total               2279 
_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        2085 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_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' ? 0.0066  ? 2252 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9099  ? 3068 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0614  ? 335  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0055  ? 421  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.3366 ? 853  ? 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' 1.53 1.55  . . 148 2718 96.01 . . . . 0.2873 . . . . . . . . . . . 0.3049 
'X-RAY DIFFRACTION' 1.55 1.57  . . 139 2738 95.64 . . . . 0.2565 . . . . . . . . . . . 0.3275 
'X-RAY DIFFRACTION' 1.57 1.59  . . 152 2685 94.91 . . . . 0.2504 . . . . . . . . . . . 0.2826 
'X-RAY DIFFRACTION' 1.59 1.62  . . 138 2691 95.41 . . . . 0.2441 . . . . . . . . . . . 0.3162 
'X-RAY DIFFRACTION' 1.62 1.64  . . 155 2685 94.73 . . . . 0.2163 . . . . . . . . . . . 0.3091 
'X-RAY DIFFRACTION' 1.64 1.67  . . 140 2713 94.50 . . . . 0.2147 . . . . . . . . . . . 0.2780 
'X-RAY DIFFRACTION' 1.67 1.69  . . 144 2671 94.53 . . . . 0.1834 . . . . . . . . . . . 0.2140 
'X-RAY DIFFRACTION' 1.69 1.72  . . 130 2629 92.52 . . . . 0.1876 . . . . . . . . . . . 0.2237 
'X-RAY DIFFRACTION' 1.72 1.75  . . 156 2621 91.74 . . . . 0.1756 . . . . . . . . . . . 0.2487 
'X-RAY DIFFRACTION' 1.75 1.79  . . 162 2657 94.88 . . . . 0.1615 . . . . . . . . . . . 0.2482 
'X-RAY DIFFRACTION' 1.79 1.82  . . 147 2780 97.27 . . . . 0.1486 . . . . . . . . . . . 0.1903 
'X-RAY DIFFRACTION' 1.82 1.86  . . 123 2817 97.90 . . . . 0.1461 . . . . . . . . . . . 0.1961 
'X-RAY DIFFRACTION' 1.86 1.91  . . 149 2684 95.23 . . . . 0.1940 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 1.91 1.95  . . 135 2692 94.33 . . . . 0.2076 . . . . . . . . . . . 0.2812 
'X-RAY DIFFRACTION' 1.95 2.01  . . 137 2779 97.62 . . . . 0.1561 . . . . . . . . . . . 0.1931 
'X-RAY DIFFRACTION' 2.01 2.07  . . 141 2794 96.67 . . . . 0.1277 . . . . . . . . . . . 0.1885 
'X-RAY DIFFRACTION' 2.07 2.13  . . 121 2774 96.50 . . . . 0.1345 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.13 2.21  . . 142 2683 95.44 . . . . 0.1416 . . . . . . . . . . . 0.2225 
'X-RAY DIFFRACTION' 2.21 2.30  . . 125 2490 87.63 . . . . 0.1791 . . . . . . . . . . . 0.2533 
'X-RAY DIFFRACTION' 2.30 2.40  . . 141 2771 95.92 . . . . 0.1540 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 2.40 2.53  . . 114 2693 94.90 . . . . 0.1527 . . . . . . . . . . . 0.1853 
'X-RAY DIFFRACTION' 2.53 2.69  . . 131 2637 92.95 . . . . 0.1535 . . . . . . . . . . . 0.1855 
'X-RAY DIFFRACTION' 2.69 2.89  . . 134 2549 88.72 . . . . 0.1671 . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 2.89 3.19  . . 114 2423 84.34 . . . . 0.1703 . . . . . . . . . . . 0.1851 
'X-RAY DIFFRACTION' 3.19 3.65  . . 156 2573 91.06 . . . . 0.1514 . . . . . . . . . . . 0.1788 
'X-RAY DIFFRACTION' 3.65 4.59  . . 129 2665 93.76 . . . . 0.1338 . . . . . . . . . . . 0.1517 
'X-RAY DIFFRACTION' 4.59 55.59 . . 143 2696 94.13 . . . . 0.1667 . . . . . . . . . . . 0.1915 
# 
_struct.entry_id                     8QGO 
_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        8QGO 
_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              8QGO 
_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 8QGO LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGO GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGO HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGO HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGO HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGO HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGO HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGO HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 11390 ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  40090 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 62.9690000000 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 62.9690000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 GLU A 56  ? ILE A 62  ? GLU A 56  ILE A 62  5 ? 7  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 8 ? 
AA3 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 2 GLN A 96  ? TYR A 109 ? GLN A 96  TYR A 109 
AA2 3 VAL A 231 ? ARG A 247 ? VAL A 231 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA2 7 ALA A 178 ? SER A 186 ? ALA A 178 SER A 186 
AA2 8 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA3 2 GLN A 96  ? TYR A 109 ? GLN A 96  TYR A 109 
AA3 3 VAL A 231 ? ARG A 247 ? VAL A 231 ARG A 247 
AA3 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA3 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA3 6 ILE A 142 ? SER A 155 ? ILE A 142 SER A 155 
AA3 7 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 8 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 9 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N GLN A 96  ? N GLN A 96  O ARG A 247 ? O ARG A 247 
AA2 3 4 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA2 6 7 N 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 GLN A 96  ? N GLN A 96  O ARG A 247 ? O ARG A 247 
AA3 3 4 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA3 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA3 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 6 7 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 7 8 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 8 9 N PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QGO 
_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 LYS A 114 ? ? 74.52   -157.00 
2 1 ASN A 122 ? ? -101.22 -68.34  
3 1 ALA A 162 ? ? -107.19 -129.25 
4 1 HIS A 204 ? ? 81.34   -13.10  
5 1 ASN A 213 ? ? -127.24 -81.06  
6 1 ASP A 222 ? ? 53.88   -134.61 
7 1 GLU A 263 ? ? -175.22 148.28  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     418 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_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 LEU 265 ? A LEU 265 
2 1 Y 1 A GLU 266 ? A GLU 266 
3 1 Y 1 A HIS 267 ? A HIS 267 
4 1 Y 1 A HIS 268 ? A HIS 268 
5 1 Y 1 A HIS 269 ? A HIS 269 
6 1 Y 1 A HIS 270 ? A HIS 270 
7 1 Y 1 A HIS 271 ? A HIS 271 
8 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 
UOL N4   N Y N 393 
UOL C4   C N R 394 
UOL N3   N N N 395 
UOL C2   C N N 396 
UOL O2   O N N 397 
UOL C5   C N R 398 
UOL N5   N Y N 399 
UOL C6   C N R 400 
UOL O6   O N N 401 
UOL N1   N N N 402 
UOL N    N N N 403 
UOL C    C N N 404 
UOL O    O N N 405 
UOL C1   C N N 406 
UOL C10  C N N 407 
UOL C11  C N N 408 
UOL C12  C N N 409 
UOL C13  C N R 410 
UOL C14  C N R 411 
UOL C15  C N R 412 
UOL C16  C N S 413 
UOL C17  C Y N 414 
UOL C18  C Y N 415 
UOL C19  C Y N 416 
UOL C20  C Y N 417 
UOL C21  C Y N 418 
UOL C22  C N N 419 
UOL C23  C Y N 420 
UOL C24  C Y N 421 
UOL C25  C Y N 422 
UOL C26  C Y N 423 
UOL C3   C N N 424 
UOL C7   C N S 425 
UOL C8   C Y N 426 
UOL C9   C N N 427 
UOL N10  N Y N 428 
UOL N11  N Y N 429 
UOL N12  N N N 430 
UOL N2   N Y N 431 
UOL N6   N Y N 432 
UOL N7   N Y N 433 
UOL N8   N N N 434 
UOL N9   N Y N 435 
UOL O1   O N N 436 
UOL O3   O N N 437 
UOL O4   O N N 438 
UOL O5   O N N 439 
UOL H    H N N 440 
UOL H17  H N N 441 
UOL H1   H N N 442 
UOL H2   H N N 443 
UOL H24  H N N 444 
UOL H14  H N N 445 
UOL H13  H N N 446 
UOL H9   H N N 447 
UOL H8   H N N 448 
UOL H10  H N N 449 
UOL H12  H N N 450 
UOL H11  H N N 451 
UOL H20  H N N 452 
UOL H19  H N N 453 
UOL H21  H N N 454 
UOL H22  H N N 455 
UOL H4   H N N 456 
UOL H5   H N N 457 
UOL H6   H N N 458 
UOL H7   H N N 459 
UOL H25  H N N 460 
UOL H26  H N N 461 
UOL H29  H N N 462 
UOL H30  H N N 463 
UOL H31  H N N 464 
UOL H32  H N N 465 
UOL H16  H N N 466 
UOL H15  H N N 467 
UOL H3   H N N 468 
UOL H34  H N N 469 
UOL H33  H N N 470 
UOL H27  H N N 471 
UOL H28  H N N 472 
UOL H18  H N N 473 
UOL H23  H N N 474 
VAL N    N N N 475 
VAL CA   C N S 476 
VAL C    C N N 477 
VAL O    O N N 478 
VAL CB   C N N 479 
VAL CG1  C N N 480 
VAL CG2  C N N 481 
VAL OXT  O N N 482 
VAL H    H N N 483 
VAL H2   H N N 484 
VAL HA   H N N 485 
VAL HB   H N N 486 
VAL HG11 H N N 487 
VAL HG12 H N N 488 
VAL HG13 H N N 489 
VAL HG21 H N N 490 
VAL HG22 H N N 491 
VAL HG23 H N N 492 
VAL HXT  H N N 493 
# 
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 
UOL C   C1   sing N N 378 
UOL C1  N    sing N N 379 
UOL N   C2   sing N N 380 
UOL C2  O    doub N N 381 
UOL N1  C2   sing N N 382 
UOL C3  N1   sing N N 383 
UOL C4  C3   sing N N 384 
UOL C4  O1   sing N N 385 
UOL O1  C5   sing N N 386 
UOL C5  C6   sing N N 387 
UOL C6  C7   sing N N 388 
UOL C7  C4   sing N N 389 
UOL O2  C7   sing N N 390 
UOL O3  C6   sing N N 391 
UOL N2  C5   sing N N 392 
UOL N2  C8   sing Y N 393 
UOL C9  C8   sing N N 394 
UOL C10 C9   trip N N 395 
UOL C11 C10  sing N N 396 
UOL N3  C11  sing N N 397 
UOL C12 N3   sing N N 398 
UOL C13 C12  sing N N 399 
UOL C13 O4   sing N N 400 
UOL O4  C14  sing N N 401 
UOL C14 C15  sing N N 402 
UOL C15 C16  sing N N 403 
UOL C16 C13  sing N N 404 
UOL O5  C16  sing N N 405 
UOL O6  C15  sing N N 406 
UOL N4  C14  sing N N 407 
UOL N4  C17  sing Y N 408 
UOL C17 N5   doub Y N 409 
UOL N5  C18  sing Y N 410 
UOL C18 C19  doub Y N 411 
UOL C19 N4   sing Y N 412 
UOL N6  C19  sing Y N 413 
UOL C20 N6   doub Y N 414 
UOL N7  C20  sing Y N 415 
UOL C21 N7   doub Y N 416 
UOL C18 C21  sing Y N 417 
UOL N8  C21  sing N N 418 
UOL C22 N3   sing N N 419 
UOL C8  N9   doub Y N 420 
UOL N9  C23  sing Y N 421 
UOL C23 C24  doub Y N 422 
UOL C24 N2   sing Y N 423 
UOL N10 C24  sing Y N 424 
UOL C25 N10  doub Y N 425 
UOL N11 C25  sing Y N 426 
UOL C26 N11  doub Y N 427 
UOL C23 C26  sing Y N 428 
UOL N12 C26  sing N N 429 
UOL C4  H    sing N N 430 
UOL O2  H17  sing N N 431 
UOL C5  H1   sing N N 432 
UOL C6  H2   sing N N 433 
UOL O6  H24  sing N N 434 
UOL N1  H14  sing N N 435 
UOL N   H13  sing N N 436 
UOL C   H9   sing N N 437 
UOL C   H8   sing N N 438 
UOL C   H10  sing N N 439 
UOL C1  H12  sing N N 440 
UOL C1  H11  sing N N 441 
UOL C11 H20  sing N N 442 
UOL C11 H19  sing N N 443 
UOL C12 H21  sing N N 444 
UOL C12 H22  sing N N 445 
UOL C13 H4   sing N N 446 
UOL C14 H5   sing N N 447 
UOL C15 H6   sing N N 448 
UOL C16 H7   sing N N 449 
UOL C17 H25  sing N N 450 
UOL C20 H26  sing N N 451 
UOL C22 H29  sing N N 452 
UOL C22 H30  sing N N 453 
UOL C22 H31  sing N N 454 
UOL C25 H32  sing N N 455 
UOL C3  H16  sing N N 456 
UOL C3  H15  sing N N 457 
UOL C7  H3   sing N N 458 
UOL N12 H34  sing N N 459 
UOL N12 H33  sing N N 460 
UOL N8  H27  sing N N 461 
UOL N8  H28  sing N N 462 
UOL O3  H18  sing N N 463 
UOL O5  H23  sing N N 464 
VAL N   CA   sing N N 465 
VAL N   H    sing N N 466 
VAL N   H2   sing N N 467 
VAL CA  C    sing N N 468 
VAL CA  CB   sing N N 469 
VAL CA  HA   sing N N 470 
VAL C   O    doub N N 471 
VAL C   OXT  sing N N 472 
VAL CB  CG1  sing N N 473 
VAL CB  CG2  sing N N 474 
VAL CB  HB   sing N N 475 
VAL CG1 HG11 sing N N 476 
VAL CG1 HG12 sing N N 477 
VAL CG1 HG13 sing N N 478 
VAL CG2 HG21 sing N N 479 
VAL CG2 HG22 sing N N 480 
VAL CG2 HG23 sing N N 481 
VAL OXT HXT  sing N N 482 
# 
_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                    8QGO 
_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]   0.015881 
_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]   0.013434 
_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]   0.008448 
_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.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 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   ? 12.06833 36.07569 25.54910  1.000 58.68839 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 11.14666 36.34537 24.44999  1.000 57.13320 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 10.09555 35.24171 24.34262  1.000 52.12201 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.90967  34.46451 25.27987  1.000 51.32830 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.91751 36.49839 23.13738  1.000 60.44657 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.70554 35.27033 22.71881  1.000 63.42567 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.23522 35.68332 21.84570  1.000 65.64869 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.20475 36.34940 23.19714  1.000 66.48048 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.38927  35.19211 23.21522  1.000 47.81250 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.41480  34.13208 22.99873  1.000 43.61927 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 9.13953  32.81979 22.74981  1.000 39.13499 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 10.15738 32.78067 22.05540  1.000 37.41517 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.50055  34.45906 21.81357  1.000 44.38541 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.50538  35.59473 22.06991  1.000 45.37670 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.51119  35.69585 20.91938  1.000 47.89719 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.46654  36.77308 21.14816  1.000 50.82455 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 5.06361  38.13924 21.13356  1.000 53.37369 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.63141  31.74560 23.35114  1.000 36.72635 ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.23128  30.42497 23.18740  1.000 33.83872 ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 8.12695  29.37987 23.20915  1.000 32.25761 ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 7.01133  29.63641 23.67557  1.000 33.71659 ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.25248 30.12634 24.30387  1.000 32.26979 ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.59385  29.76448 25.62713  1.000 31.64802 ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 9.13593  30.75124 26.49773  1.000 31.45562 ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.41313  28.43970 25.98812  1.000 30.34940 ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.52104  30.41644 27.70124  1.000 32.06768 ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.80240  28.09601 27.18305  1.000 30.33858 ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.35622  29.08208 28.03273  1.000 31.41406 ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.74090  28.71604 29.22169  1.000 35.17569 ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.44468  28.18403 22.71144  1.000 30.18514 ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.59041  27.03775 22.98117  1.000 30.77275 ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.45957  25.80464 23.15092  1.000 28.59216 ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.64663  25.80539 22.82229  1.000 28.95919 ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.52666  26.84872 21.89841  1.000 33.21200 ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.06646  26.50696 20.52673  1.000 33.08842 ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.38673  24.73960 20.36310  1.000 33.95988 ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.72136  24.07939 20.37381  1.000 35.49901 ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.87374  24.74773 23.70664  1.000 27.37954 ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.60004  23.50836 23.95117  1.000 26.11147 ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.78500  22.34922 23.41159  1.000 26.30698 ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.61402  22.19548 23.77467  1.000 27.17884 ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.87651  23.29090 25.45054  1.000 25.38306 ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.60170  24.49506 26.02029  1.000 26.37633 ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.70192  22.01790 25.62435  1.000 26.79026 ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.96099  24.32764 27.52037  1.000 27.86427 ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.38654  21.54678 22.52998  1.000 27.94534 ? 6   THR A N   1 
ATOM   47   C CA  A THR A 1 6   ? 7.76972  20.30887 22.08175  0.700 29.63392 ? 6   THR A CA  1 
ATOM   48   C CA  B THR A 1 6   ? 7.76355  20.31212 22.09208  0.300 29.83940 ? 6   THR A CA  1 
ATOM   49   C C   . THR A 1 6   ? 8.36050  19.14821 22.86325  1.000 30.81312 ? 6   THR A C   1 
ATOM   50   O O   . THR A 1 6   ? 9.51005  19.19737 23.30663  1.000 33.85534 ? 6   THR A O   1 
ATOM   51   C CB  A THR A 1 6   ? 7.97402  20.06720 20.57734  0.700 32.71188 ? 6   THR A CB  1 
ATOM   52   C CB  B THR A 1 6   ? 7.94773  20.08084 20.59392  0.300 31.54993 ? 6   THR A CB  1 
ATOM   53   O OG1 A THR A 1 6   ? 9.34454  19.74297 20.32775  0.700 31.06703 ? 6   THR A OG1 1 
ATOM   54   O OG1 B THR A 1 6   ? 7.67367  21.29234 19.88279  0.300 34.67179 ? 6   THR A OG1 1 
ATOM   55   C CG2 A THR A 1 6   ? 7.60608  21.29528 19.76784  0.700 36.23705 ? 6   THR A CG2 1 
ATOM   56   C CG2 B THR A 1 6   ? 6.99110  19.00766 20.13195  0.300 29.33065 ? 6   THR A CG2 1 
ATOM   57   N N   . SER A 1 7   ? 7.56575  18.10909 23.03293  1.000 31.01054 ? 7   SER A N   1 
ATOM   58   C CA  . SER A 1 7   ? 7.97907  16.94989 23.80193  1.000 30.05233 ? 7   SER A CA  1 
ATOM   59   C C   . SER A 1 7   ? 7.74301  15.68340 23.00019  1.000 30.93515 ? 7   SER A C   1 
ATOM   60   O O   . SER A 1 7   ? 6.74120  15.56460 22.28819  1.000 32.42092 ? 7   SER A O   1 
ATOM   61   C CB  . SER A 1 7   ? 7.21389  16.86083 25.12701  1.000 29.84231 ? 7   SER A CB  1 
ATOM   62   O OG  . SER A 1 7   ? 7.45962  15.61173 25.73838  1.000 32.58811 ? 7   SER A OG  1 
ATOM   63   N N   . LYS A 1 8   ? 8.66676  14.73377 23.12918  1.000 31.76083 ? 8   LYS A N   1 
ATOM   64   C CA  . LYS A 1 8   ? 8.44063  13.40839 22.56813  1.000 34.22419 ? 8   LYS A CA  1 
ATOM   65   C C   . LYS A 1 8   ? 7.17043  12.77974 23.12712  1.000 36.84271 ? 8   LYS A C   1 
ATOM   66   O O   . LYS A 1 8   ? 6.54450  11.95040 22.46466  1.000 38.82861 ? 8   LYS A O   1 
ATOM   67   C CB  . LYS A 1 8   ? 9.66070  12.52873 22.84447  1.000 35.37033 ? 8   LYS A CB  1 
ATOM   68   C CG  . LYS A 1 8   ? 9.49420  11.05315 22.55465  1.000 39.64946 ? 8   LYS A CG  1 
ATOM   69   C CD  . LYS A 1 8   ? 10.65091 10.28666 23.16775  0.800 42.91967 ? 8   LYS A CD  1 
ATOM   70   C CE  . LYS A 1 8   ? 10.53900 8.79630  22.90640  0.700 44.91958 ? 8   LYS A CE  1 
ATOM   71   N NZ  . LYS A 1 8   ? 10.54598 8.52501  21.45365  0.700 46.57046 ? 8   LYS A NZ  1 
ATOM   72   N N   . GLY A 1 9   ? 6.77017  13.15352 24.33908  1.000 38.08334 ? 9   GLY A N   1 
ATOM   73   C CA  . GLY A 1 9   ? 5.52131  12.67695 24.89400  1.000 38.93290 ? 9   GLY A CA  1 
ATOM   74   C C   . GLY A 1 9   ? 5.62496  11.49855 25.83593  1.000 40.66370 ? 9   GLY A C   1 
ATOM   75   O O   . GLY A 1 9   ? 4.58466  10.97941 26.26560  1.000 43.34492 ? 9   GLY A O   1 
ATOM   76   N N   . ASP A 1 10  ? 6.82873  11.04904 26.16592  1.000 41.85489 ? 10  ASP A N   1 
ATOM   77   C CA  . ASP A 1 10  ? 6.96285  10.11398 27.26606  1.000 44.02870 ? 10  ASP A CA  1 
ATOM   78   C C   . ASP A 1 10  ? 6.97118  10.88064 28.58609  1.000 43.27402 ? 10  ASP A C   1 
ATOM   79   O O   . ASP A 1 10  ? 7.06677  12.11064 28.61598  1.000 42.83450 ? 10  ASP A O   1 
ATOM   80   C CB  . ASP A 1 10  ? 8.23026  9.27687  27.11769  1.000 47.94993 ? 10  ASP A CB  1 
ATOM   81   C CG  . ASP A 1 10  ? 9.49615  10.10510 27.22907  1.000 50.91928 ? 10  ASP A CG  1 
ATOM   82   O OD1 . ASP A 1 10  ? 9.48959  11.27349 26.78648  1.000 51.45514 ? 10  ASP A OD1 1 
ATOM   83   O OD2 . ASP A 1 10  ? 10.49809 9.58420  27.76529  1.000 52.74397 ? 10  ASP A OD2 1 
ATOM   84   N N   . GLU A 1 11  ? 6.87233  10.13454 29.69218  1.000 43.56746 ? 11  GLU A N   1 
ATOM   85   C CA  . GLU A 1 11  ? 6.81862  10.76984 31.00727  1.000 45.12040 ? 11  GLU A CA  1 
ATOM   86   C C   . GLU A 1 11  ? 8.02356  11.67005 31.23775  1.000 43.16775 ? 11  GLU A C   1 
ATOM   87   O O   . GLU A 1 11  ? 7.88448  12.79597 31.72478  1.000 43.49651 ? 11  GLU A O   1 
ATOM   88   C CB  . GLU A 1 11  ? 6.74055  9.71369  32.11093  1.000 48.43172 ? 11  GLU A CB  1 
ATOM   89   C CG  . GLU A 1 11  ? 5.42034  8.98239  32.20998  1.000 51.09688 ? 11  GLU A CG  1 
ATOM   90   C CD  . GLU A 1 11  ? 5.33449  8.13077  33.46378  0.700 53.50671 ? 11  GLU A CD  1 
ATOM   91   O OE1 . GLU A 1 11  ? 6.23178  8.25368  34.32615  0.700 54.12018 ? 11  GLU A OE1 1 
ATOM   92   O OE2 . GLU A 1 11  ? 4.37595  7.33918  33.58744  0.700 54.48880 ? 11  GLU A OE2 1 
ATOM   93   N N   . LYS A 1 12  ? 9.21656  11.19021 30.89345  1.000 41.25886 ? 12  LYS A N   1 
ATOM   94   C CA  . LYS A 1 12  ? 10.43180 11.94402 31.17746  1.000 41.58844 ? 12  LYS A CA  1 
ATOM   95   C C   . LYS A 1 12  ? 10.46066 13.26764 30.41541  1.000 38.67258 ? 12  LYS A C   1 
ATOM   96   O O   . LYS A 1 12  ? 10.82044 14.31069 30.97469  1.000 37.90931 ? 12  LYS A O   1 
ATOM   97   C CB  . LYS A 1 12  ? 11.64238 11.08043 30.83115  1.000 43.70194 ? 12  LYS A CB  1 
ATOM   98   C CG  . LYS A 1 12  ? 12.98667 11.65736 31.21073  0.900 45.47655 ? 12  LYS A CG  1 
ATOM   99   C CD  . LYS A 1 12  ? 14.09311 10.74732 30.70401  0.800 47.52696 ? 12  LYS A CD  1 
ATOM   100  C CE  . LYS A 1 12  ? 15.44368 11.14502 31.27006  0.700 49.35868 ? 12  LYS A CE  1 
ATOM   101  N NZ  . LYS A 1 12  ? 15.79049 12.54204 30.89451  0.700 50.87311 ? 12  LYS A NZ  1 
ATOM   102  N N   . SER A 1 13  ? 10.09614 13.24571 29.12903  1.000 35.90435 ? 13  SER A N   1 
ATOM   103  C CA  . SER A 1 13  ? 10.13004 14.47116 28.33992  1.000 32.93175 ? 13  SER A CA  1 
ATOM   104  C C   . SER A 1 13  ? 9.01718  15.42713 28.74166  1.000 32.79122 ? 13  SER A C   1 
ATOM   105  O O   . SER A 1 13  ? 9.21959  16.64644 28.76874  1.000 33.60663 ? 13  SER A O   1 
ATOM   106  C CB  . SER A 1 13  ? 10.02561 14.14081 26.84947  1.000 32.30208 ? 13  SER A CB  1 
ATOM   107  O OG  . SER A 1 13  ? 11.08711 13.28773 26.44900  1.000 33.87744 ? 13  SER A OG  1 
ATOM   108  N N   . ASP A 1 14  ? 7.82862  14.89819 29.03040  1.000 32.98983 ? 14  ASP A N   1 
ATOM   109  C CA  . ASP A 1 14  ? 6.72865  15.75693 29.45777  1.000 33.80919 ? 14  ASP A CA  1 
ATOM   110  C C   . ASP A 1 14  ? 7.05596  16.45375 30.77491  1.000 34.11372 ? 14  ASP A C   1 
ATOM   111  O O   . ASP A 1 14  ? 6.78494  17.64949 30.94370  1.000 33.17255 ? 14  ASP A O   1 
ATOM   112  C CB  . ASP A 1 14  ? 5.45034  14.93266 29.60421  1.000 36.65456 ? 14  ASP A CB  1 
ATOM   113  C CG  . ASP A 1 14  ? 4.74958  14.69278 28.28802  1.000 39.93255 ? 14  ASP A CG  1 
ATOM   114  O OD1 . ASP A 1 14  ? 5.23713  15.18372 27.24619  1.000 38.41343 ? 14  ASP A OD1 1 
ATOM   115  O OD2 . ASP A 1 14  ? 3.69692  14.01194 28.30248  1.000 42.88807 ? 14  ASP A OD2 1 
ATOM   116  N N   . LEU A 1 15  ? 7.63673  15.71853 31.72511  1.000 35.34930 ? 15  LEU A N   1 
ATOM   117  C CA  . LEU A 1 15  ? 7.95769  16.32134 33.01518  1.000 34.70744 ? 15  LEU A CA  1 
ATOM   118  C C   . LEU A 1 15  ? 9.05271  17.36906 32.87277  1.000 31.97269 ? 15  LEU A C   1 
ATOM   119  O O   . LEU A 1 15  ? 8.97996  18.43852 33.49152  1.000 30.98796 ? 15  LEU A O   1 
ATOM   120  C CB  . LEU A 1 15  ? 8.36631  15.24010 34.01687  1.000 36.79750 ? 15  LEU A CB  1 
ATOM   121  C CG  . LEU A 1 15  ? 7.26808  14.25426 34.42932  0.700 38.72127 ? 15  LEU A CG  1 
ATOM   122  C CD1 . LEU A 1 15  ? 7.81642  13.10632 35.26954  0.700 38.95314 ? 15  LEU A CD1 1 
ATOM   123  C CD2 . LEU A 1 15  ? 6.17636  14.98939 35.19288  0.700 38.25389 ? 15  LEU A CD2 1 
ATOM   124  N N   . LEU A 1 16  ? 10.06305 17.09498 32.04079  1.000 30.80195 ? 16  LEU A N   1 
ATOM   125  C CA  . LEU A 1 16  ? 11.10860 18.08654 31.83223  1.000 30.63902 ? 16  LEU A CA  1 
ATOM   126  C C   . LEU A 1 16  ? 10.52016 19.34177 31.21089  1.000 30.05545 ? 16  LEU A C   1 
ATOM   127  O O   . LEU A 1 16  ? 10.84991 20.46453 31.61046  1.000 31.42531 ? 16  LEU A O   1 
ATOM   128  C CB  . LEU A 1 16  ? 12.22172 17.51204 30.94459  1.000 30.59018 ? 16  LEU A CB  1 
ATOM   129  C CG  . LEU A 1 16  ? 13.47686 18.37922 30.78184  1.000 32.02159 ? 16  LEU A CG  1 
ATOM   130  C CD1 . LEU A 1 16  ? 14.10376 18.72691 32.11784  1.000 32.99157 ? 16  LEU A CD1 1 
ATOM   131  C CD2 . LEU A 1 16  ? 14.52328 17.72014 29.86646  1.000 32.97835 ? 16  LEU A CD2 1 
ATOM   132  N N   . ARG A 1 17  ? 9.63020  19.16278 30.23618  1.000 27.82494 ? 17  ARG A N   1 
ATOM   133  C CA  . ARG A 1 17  ? 8.96046  20.30202 29.62080  1.000 26.13435 ? 17  ARG A CA  1 
ATOM   134  C C   . ARG A 1 17  ? 8.21566  21.13258 30.66387  1.000 26.17256 ? 17  ARG A C   1 
ATOM   135  O O   . ARG A 1 17  ? 8.31722  22.36515 30.68673  1.000 26.38993 ? 17  ARG A O   1 
ATOM   136  C CB  . ARG A 1 17  ? 8.00839  19.81360 28.53010  1.000 25.03642 ? 17  ARG A CB  1 
ATOM   137  C CG  . ARG A 1 17  ? 7.14237  20.90706 27.97740  1.000 25.75051 ? 17  ARG A CG  1 
ATOM   138  C CD  . ARG A 1 17  ? 6.31593  20.41725 26.79675  1.000 26.83828 ? 17  ARG A CD  1 
ATOM   139  N NE  . ARG A 1 17  ? 5.43508  21.47004 26.31812  1.000 28.31659 ? 17  ARG A NE  1 
ATOM   140  C CZ  . ARG A 1 17  ? 4.27360  21.77245 26.87695  1.000 29.47641 ? 17  ARG A CZ  1 
ATOM   141  N NH1 . ARG A 1 17  ? 3.83539  21.12417 27.94146  1.000 31.24648 ? 17  ARG A NH1 1 
ATOM   142  N NH2 . ARG A 1 17  ? 3.53881  22.75149 26.35966  1.000 31.79291 ? 17  ARG A NH2 1 
ATOM   143  N N   . LEU A 1 18  ? 7.45311  20.47770 31.53561  1.000 26.68707 ? 18  LEU A N   1 
ATOM   144  C CA  . LEU A 1 18  ? 6.70012  21.23191 32.53719  1.000 28.47115 ? 18  LEU A CA  1 
ATOM   145  C C   . LEU A 1 18  ? 7.63319  21.96208 33.49508  1.000 29.11000 ? 18  LEU A C   1 
ATOM   146  O O   . LEU A 1 18  ? 7.36712  23.10449 33.87641  1.000 30.82361 ? 18  LEU A O   1 
ATOM   147  C CB  . LEU A 1 18  ? 5.75741  20.30798 33.30419  1.000 28.59043 ? 18  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 18  ? 4.50582  19.83778 32.56962  1.000 31.36950 ? 18  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 18  ? 3.60204  19.11447 33.53727  1.000 30.81607 ? 18  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 18  ? 3.77351  20.99412 31.89800  1.000 32.16200 ? 18  LEU A CD2 1 
ATOM   151  N N   . ASN A 1 19  ? 8.75292  21.33792 33.86234  1.000 30.40469 ? 19  ASN A N   1 
ATOM   152  C CA  . ASN A 1 19  ? 9.69647  22.00477 34.75761  1.000 30.87235 ? 19  ASN A CA  1 
ATOM   153  C C   . ASN A 1 19  ? 10.38633 23.17964 34.06946  1.000 30.69435 ? 19  ASN A C   1 
ATOM   154  O O   . ASN A 1 19  ? 10.68481 24.19205 34.71310  1.000 30.18189 ? 19  ASN A O   1 
ATOM   155  C CB  . ASN A 1 19  ? 10.73030 21.00947 35.28012  1.000 32.30004 ? 19  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 19  ? 10.26427 20.29098 36.52764  1.000 33.32174 ? 19  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 19  ? 9.33517  20.74620 37.21648  1.000 31.66096 ? 19  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 19  ? 10.90131 19.16379 36.83084  1.000 34.81203 ? 19  ASN A ND2 1 
ATOM   159  N N   . MET A 1 20  ? 10.66290 23.06834 32.76526  1.000 28.64133 ? 20  MET A N   1 
ATOM   160  C CA  . MET A 1 20  ? 11.27748 24.19469 32.07734  1.000 29.17483 ? 20  MET A CA  1 
ATOM   161  C C   . MET A 1 20  ? 10.29607 25.34459 31.93090  1.000 30.07254 ? 20  MET A C   1 
ATOM   162  O O   . MET A 1 20  ? 10.67494 26.51301 32.06083  1.000 31.82136 ? 20  MET A O   1 
ATOM   163  C CB  . MET A 1 20  ? 11.80317 23.75727 30.70725  1.000 28.64793 ? 20  MET A CB  1 
ATOM   164  C CG  . MET A 1 20  ? 12.99776 22.86046 30.82633  1.000 30.56700 ? 20  MET A CG  1 
ATOM   165  S SD  . MET A 1 20  ? 13.69633 22.45179 29.22183  1.000 32.09430 ? 20  MET A SD  1 
ATOM   166  C CE  . MET A 1 20  ? 14.63551 23.94064 28.83196  1.000 32.75601 ? 20  MET A CE  1 
ATOM   167  N N   . ILE A 1 21  ? 9.03333  25.03444 31.63243  1.000 30.03594 ? 21  ILE A N   1 
ATOM   168  C CA  . ILE A 1 21  ? 8.00609  26.06710 31.60638  1.000 28.03681 ? 21  ILE A CA  1 
ATOM   169  C C   . ILE A 1 21  ? 7.94317  26.78379 32.94772  1.000 28.78829 ? 21  ILE A C   1 
ATOM   170  O O   . ILE A 1 21  ? 7.82431  28.00950 33.00518  1.000 30.16513 ? 21  ILE A O   1 
ATOM   171  C CB  . ILE A 1 21  ? 6.65042  25.45312 31.22534  1.000 28.77795 ? 21  ILE A CB  1 
ATOM   172  C CG1 . ILE A 1 21  ? 6.71215  24.97644 29.75880  1.000 28.08048 ? 21  ILE A CG1 1 
ATOM   173  C CG2 . ILE A 1 21  ? 5.53718  26.47480 31.44346  1.000 30.20788 ? 21  ILE A CG2 1 
ATOM   174  C CD1 . ILE A 1 21  ? 5.44578  24.32820 29.26161  1.000 29.36649 ? 21  ILE A CD1 1 
ATOM   175  N N   . ALA A 1 22  ? 8.05333  26.03506 34.04367  1.000 29.02860 ? 22  ALA A N   1 
ATOM   176  C CA  . ALA A 1 22  ? 8.03422  26.66985 35.35718  1.000 31.49109 ? 22  ALA A CA  1 
ATOM   177  C C   . ALA A 1 22  ? 9.23883  27.58620 35.53376  1.000 32.46309 ? 22  ALA A C   1 
ATOM   178  O O   . ALA A 1 22  ? 9.09907  28.72832 35.99165  1.000 33.09723 ? 22  ALA A O   1 
ATOM   179  C CB  . ALA A 1 22  ? 7.98404  25.60643 36.45320  1.000 33.33901 ? 22  ALA A CB  1 
ATOM   180  N N   . GLY A 1 23  ? 10.42607 27.11188 35.14611  1.000 33.79297 ? 23  GLY A N   1 
ATOM   181  C CA  . GLY A 1 23  ? 11.60784 27.95605 35.21991  1.000 33.87202 ? 23  GLY A CA  1 
ATOM   182  C C   . GLY A 1 23  ? 11.48374 29.20731 34.37238  1.000 35.01823 ? 23  GLY A C   1 
ATOM   183  O O   . GLY A 1 23  ? 11.85726 30.30239 34.80271  1.000 36.57032 ? 23  GLY A O   1 
ATOM   184  N N   . PHE A 1 24  ? 10.95656 29.06435 33.15000  1.000 33.05449 ? 24  PHE A N   1 
ATOM   185  C CA  . PHE A 1 24  ? 10.80811 30.22900 32.28197  1.000 34.76934 ? 24  PHE A CA  1 
ATOM   186  C C   . PHE A 1 24  ? 9.84063  31.23984 32.87225  1.000 35.96420 ? 24  PHE A C   1 
ATOM   187  O O   . PHE A 1 24  ? 9.98540  32.44490 32.63769  1.000 38.28714 ? 24  PHE A O   1 
ATOM   188  C CB  . PHE A 1 24  ? 10.34360 29.80223 30.88882  1.000 34.42548 ? 24  PHE A CB  1 
ATOM   189  C CG  . PHE A 1 24  ? 11.44349 29.24679 30.02670  1.000 36.18573 ? 24  PHE A CG  1 
ATOM   190  C CD1 . PHE A 1 24  ? 12.61513 29.95929 29.83245  1.000 37.87666 ? 24  PHE A CD1 1 
ATOM   191  C CD2 . PHE A 1 24  ? 11.31058 28.00617 29.42371  1.000 35.16082 ? 24  PHE A CD2 1 
ATOM   192  C CE1 . PHE A 1 24  ? 13.63644 29.44973 29.03040  1.000 37.92656 ? 24  PHE A CE1 1 
ATOM   193  C CE2 . PHE A 1 24  ? 12.32372 27.48817 28.62913  1.000 36.05806 ? 24  PHE A CE2 1 
ATOM   194  C CZ  . PHE A 1 24  ? 13.48581 28.21148 28.43432  1.000 37.33869 ? 24  PHE A CZ  1 
ATOM   195  N N   . GLY A 1 25  ? 8.85960  30.77496 33.64900  1.000 35.75112 ? 25  GLY A N   1 
ATOM   196  C CA  . GLY A 1 25  ? 7.92872  31.68428 34.29697  1.000 37.12124 ? 25  GLY A CA  1 
ATOM   197  C C   . GLY A 1 25  ? 8.57985  32.61592 35.29508  1.000 39.19096 ? 25  GLY A C   1 
ATOM   198  O O   . GLY A 1 25  ? 7.96765  33.61340 35.68891  1.000 39.47159 ? 25  GLY A O   1 
ATOM   199  N N   . GLU A 1 26  ? 9.80756  32.31757 35.70767  1.000 42.72596 ? 26  GLU A N   1 
ATOM   200  C CA  . GLU A 1 26  ? 10.54994 33.21883 36.57717  1.000 44.99311 ? 26  GLU A CA  1 
ATOM   201  C C   . GLU A 1 26  ? 11.29637 34.30012 35.80396  1.000 47.14781 ? 26  GLU A C   1 
ATOM   202  O O   . GLU A 1 26  ? 12.00708 35.10481 36.42205  1.000 49.07107 ? 26  GLU A O   1 
ATOM   203  C CB  . GLU A 1 26  ? 11.51448 32.41330 37.45175  1.000 46.47522 ? 26  GLU A CB  1 
ATOM   204  C CG  . GLU A 1 26  ? 10.80746 31.37194 38.29621  0.800 46.39271 ? 26  GLU A CG  1 
ATOM   205  C CD  . GLU A 1 26  ? 9.75403  31.99432 39.20862  0.700 48.23334 ? 26  GLU A CD  1 
ATOM   206  O OE1 . GLU A 1 26  ? 9.89779  33.18804 39.56019  0.700 48.69604 ? 26  GLU A OE1 1 
ATOM   207  O OE2 . GLU A 1 26  ? 8.78210  31.29387 39.56903  0.700 49.03463 ? 26  GLU A OE2 1 
ATOM   208  N N   . TYR A 1 27  ? 11.13118 34.35092 34.48121  1.000 47.09759 ? 27  TYR A N   1 
ATOM   209  C CA  . TYR A 1 27  ? 11.76246 35.34218 33.62317  1.000 48.62563 ? 27  TYR A CA  1 
ATOM   210  C C   . TYR A 1 27  ? 10.71582 35.96281 32.70277  1.000 52.35158 ? 27  TYR A C   1 
ATOM   211  O O   . TYR A 1 27  ? 9.54390  35.57838 32.69903  1.000 53.30522 ? 27  TYR A O   1 
ATOM   212  C CB  . TYR A 1 27  ? 12.89431 34.72587 32.78829  1.000 47.46492 ? 27  TYR A CB  1 
ATOM   213  C CG  . TYR A 1 27  ? 13.98942 34.08218 33.61042  1.000 46.77359 ? 27  TYR A CG  1 
ATOM   214  C CD1 . TYR A 1 27  ? 15.09119 34.81386 34.03894  1.000 47.57787 ? 27  TYR A CD1 1 
ATOM   215  C CD2 . TYR A 1 27  ? 13.93028 32.73782 33.94857  1.000 46.29464 ? 27  TYR A CD2 1 
ATOM   216  C CE1 . TYR A 1 27  ? 16.10152 34.22055 34.79708  1.000 47.87952 ? 27  TYR A CE1 1 
ATOM   217  C CE2 . TYR A 1 27  ? 14.93657 32.13224 34.69509  1.000 45.86840 ? 27  TYR A CE2 1 
ATOM   218  C CZ  . TYR A 1 27  ? 16.02024 32.87901 35.12071  1.000 47.64340 ? 27  TYR A CZ  1 
ATOM   219  O OH  . TYR A 1 27  ? 17.02329 32.28610 35.87221  1.000 47.84108 ? 27  TYR A OH  1 
ATOM   220  N N   . ASP A 1 28  ? 11.15249 36.94387 31.91145  1.000 55.09322 ? 28  ASP A N   1 
ATOM   221  C CA  . ASP A 1 28  ? 10.28348 37.59927 30.93149  1.000 57.57263 ? 28  ASP A CA  1 
ATOM   222  C C   . ASP A 1 28  ? 10.21070 36.71595 29.68699  1.000 57.69176 ? 28  ASP A C   1 
ATOM   223  O O   . ASP A 1 28  ? 10.69721 37.04674 28.60256  1.000 59.41633 ? 28  ASP A O   1 
ATOM   224  C CB  . ASP A 1 28  ? 10.79068 38.99727 30.59733  1.000 61.09097 ? 28  ASP A CB  1 
ATOM   225  C CG  . ASP A 1 28  ? 9.92567  39.70608 29.54765  1.000 63.76550 ? 28  ASP A CG  1 
ATOM   226  O OD1 . ASP A 1 28  ? 8.86577  39.15679 29.17008  1.000 65.18976 ? 28  ASP A OD1 1 
ATOM   227  O OD2 . ASP A 1 28  ? 10.30644 40.81062 29.08845  1.000 64.54170 ? 28  ASP A OD2 1 
ATOM   228  N N   . MET A 1 29  ? 9.60533  35.54903 29.87331  1.000 55.46873 ? 29  MET A N   1 
ATOM   229  C CA  . MET A 1 29  ? 9.48865  34.55252 28.81928  1.000 53.86566 ? 29  MET A CA  1 
ATOM   230  C C   . MET A 1 29  ? 8.02013  34.19162 28.66477  1.000 52.35535 ? 29  MET A C   1 
ATOM   231  O O   . MET A 1 29  ? 7.41968  33.61780 29.57984  1.000 53.89649 ? 29  MET A O   1 
ATOM   232  C CB  . MET A 1 29  ? 10.33471 33.31954 29.13410  1.000 55.16594 ? 29  MET A CB  1 
ATOM   233  C CG  . MET A 1 29  ? 11.83374 33.59517 29.21674  1.000 57.45212 ? 29  MET A CG  1 
ATOM   234  S SD  . MET A 1 29  ? 12.57766 34.08655 27.64010  1.000 59.49563 ? 29  MET A SD  1 
ATOM   235  C CE  . MET A 1 29  ? 12.19386 32.66578 26.61995  1.000 59.01565 ? 29  MET A CE  1 
ATOM   236  N N   . GLU A 1 30  ? 7.44831  34.52871 27.50946  1.000 48.71650 ? 30  GLU A N   1 
ATOM   237  C CA  . GLU A 1 30  ? 6.06445  34.20239 27.20236  1.000 47.86698 ? 30  GLU A CA  1 
ATOM   238  C C   . GLU A 1 30  ? 6.01279  32.90115 26.41290  1.000 45.18926 ? 30  GLU A C   1 
ATOM   239  O O   . GLU A 1 30  ? 6.68506  32.76330 25.38324  1.000 45.90110 ? 30  GLU A O   1 
ATOM   240  C CB  . GLU A 1 30  ? 5.40003  35.32741 26.40328  1.000 49.85323 ? 30  GLU A CB  1 
ATOM   241  C CG  . GLU A 1 30  ? 3.96073  35.01926 26.00160  1.000 51.68721 ? 30  GLU A CG  1 
ATOM   242  C CD  . GLU A 1 30  ? 3.24803  36.20700 25.37691  0.600 52.82499 ? 30  GLU A CD  1 
ATOM   243  O OE1 . GLU A 1 30  ? 3.90214  36.99311 24.65995  0.600 52.60070 ? 30  GLU A OE1 1 
ATOM   244  O OE2 . GLU A 1 30  ? 2.03004  36.35596 25.61517  0.600 54.29659 ? 30  GLU A OE2 1 
ATOM   245  N N   . TYR A 1 31  ? 5.23623  31.94274 26.90802  1.000 42.28232 ? 31  TYR A N   1 
ATOM   246  C CA  . TYR A 1 31  ? 4.97530  30.73607 26.13638  1.000 39.85690 ? 31  TYR A CA  1 
ATOM   247  C C   . TYR A 1 31  ? 4.04596  31.09045 24.98230  1.000 40.49130 ? 31  TYR A C   1 
ATOM   248  O O   . TYR A 1 31  ? 2.96556  31.64569 25.19873  1.000 41.82283 ? 31  TYR A O   1 
ATOM   249  C CB  . TYR A 1 31  ? 4.36010  29.64755 27.01539  1.000 36.62973 ? 31  TYR A CB  1 
ATOM   250  C CG  . TYR A 1 31  ? 4.41319  28.30746 26.34301  1.000 34.43201 ? 31  TYR A CG  1 
ATOM   251  C CD1 . TYR A 1 31  ? 3.51930  27.98115 25.32621  1.000 34.71596 ? 31  TYR A CD1 1 
ATOM   252  C CD2 . TYR A 1 31  ? 5.39032  27.38508 26.67727  1.000 32.98572 ? 31  TYR A CD2 1 
ATOM   253  C CE1 . TYR A 1 31  ? 3.58772  26.76440 24.68164  1.000 33.89508 ? 31  TYR A CE1 1 
ATOM   254  C CE2 . TYR A 1 31  ? 5.46760  26.16082 26.04028  1.000 31.61657 ? 31  TYR A CE2 1 
ATOM   255  C CZ  . TYR A 1 31  ? 4.55978  25.85584 25.03645  1.000 32.44810 ? 31  TYR A CZ  1 
ATOM   256  O OH  . TYR A 1 31  ? 4.64334  24.63241 24.39510  1.000 32.23379 ? 31  TYR A OH  1 
ATOM   257  N N   . ASP A 1 32  ? 4.47771  30.79641 23.75479  1.000 41.15945 ? 32  ASP A N   1 
ATOM   258  C CA  . ASP A 1 32  ? 3.71465  31.15045 22.55977  1.000 42.26653 ? 32  ASP A CA  1 
ATOM   259  C C   . ASP A 1 32  ? 4.09585  30.15569 21.47787  1.000 40.89942 ? 32  ASP A C   1 
ATOM   260  O O   . ASP A 1 32  ? 5.20872  30.22806 20.94062  1.000 39.52284 ? 32  ASP A O   1 
ATOM   261  C CB  . ASP A 1 32  ? 4.01754  32.57859 22.11815  1.000 44.24786 ? 32  ASP A CB  1 
ATOM   262  C CG  . ASP A 1 32  ? 3.19261  33.02076 20.90774  1.000 46.25246 ? 32  ASP A CG  1 
ATOM   263  O OD1 . ASP A 1 32  ? 2.68921  32.16467 20.13980  1.000 45.44285 ? 32  ASP A OD1 1 
ATOM   264  O OD2 . ASP A 1 32  ? 3.06047  34.24877 20.72406  1.000 48.51629 ? 32  ASP A OD2 1 
ATOM   265  N N   . ASP A 1 33  ? 3.19988  29.22275 21.16326  1.000 40.82999 ? 33  ASP A N   1 
ATOM   266  C CA  . ASP A 1 33  ? 3.50301  28.25873 20.11099  1.000 40.79277 ? 33  ASP A CA  1 
ATOM   267  C C   . ASP A 1 33  ? 2.95033  28.67134 18.75455  1.000 41.59840 ? 33  ASP A C   1 
ATOM   268  O O   . ASP A 1 33  ? 3.08167  27.90614 17.79363  1.000 42.21046 ? 33  ASP A O   1 
ATOM   269  C CB  . ASP A 1 33  ? 3.01040  26.85078 20.48727  1.000 42.03653 ? 33  ASP A CB  1 
ATOM   270  C CG  . ASP A 1 33  ? 1.49888  26.75297 20.59546  1.000 44.94510 ? 33  ASP A CG  1 
ATOM   271  O OD1 . ASP A 1 33  ? 0.78836  27.66164 20.11953  1.000 44.84087 ? 33  ASP A OD1 1 
ATOM   272  O OD2 . ASP A 1 33  ? 1.02221  25.75102 21.17507  1.000 47.69051 ? 33  ASP A OD2 1 
ATOM   273  N N   . VAL A 1 34  ? 2.35959  29.86200 18.64180  1.000 41.87653 ? 34  VAL A N   1 
ATOM   274  C CA  . VAL A 1 34  ? 1.99598  30.35447 17.31892  1.000 42.37049 ? 34  VAL A CA  1 
ATOM   275  C C   . VAL A 1 34  ? 3.17765  31.06804 16.67118  1.000 43.75029 ? 34  VAL A C   1 
ATOM   276  O O   . VAL A 1 34  ? 3.57169  30.75365 15.54287  1.000 45.20873 ? 34  VAL A O   1 
ATOM   277  C CB  . VAL A 1 34  ? 0.75242  31.25810 17.39518  1.000 43.13740 ? 34  VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 34  ? 0.47905  31.87617 16.03202  1.000 43.13178 ? 34  VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 34  ? -0.44554 30.45936 17.85630  1.000 42.02598 ? 34  VAL A CG2 1 
ATOM   280  N N   . GLU A 1 35  ? 3.76924  32.02744 17.37348  1.000 43.97969 ? 35  GLU A N   1 
ATOM   281  C CA  . GLU A 1 35  ? 4.89178  32.80603 16.85230  1.000 45.37145 ? 35  GLU A CA  1 
ATOM   282  C C   . GLU A 1 35  ? 6.04411  32.80427 17.85025  1.000 43.43787 ? 35  GLU A C   1 
ATOM   283  O O   . GLU A 1 35  ? 6.49419  33.85451 18.31201  1.000 45.17284 ? 35  GLU A O   1 
ATOM   284  C CB  . GLU A 1 35  ? 4.44192  34.22522 16.51122  1.000 48.74491 ? 35  GLU A CB  1 
ATOM   285  C CG  . GLU A 1 35  ? 3.46380  34.26894 15.34284  0.700 51.86584 ? 35  GLU A CG  1 
ATOM   286  C CD  . GLU A 1 35  ? 3.17526  35.67788 14.86151  0.600 54.20628 ? 35  GLU A CD  1 
ATOM   287  O OE1 . GLU A 1 35  ? 3.45771  36.63433 15.61105  0.600 54.71760 ? 35  GLU A OE1 1 
ATOM   288  O OE2 . GLU A 1 35  ? 2.66849  35.82580 13.72987  0.600 55.22840 ? 35  GLU A OE2 1 
ATOM   289  N N   . PRO A 1 36  ? 6.56247  31.62881 18.18583  1.000 39.95904 ? 36  PRO A N   1 
ATOM   290  C CA  . PRO A 1 36  ? 7.74247  31.56722 19.05121  1.000 39.69568 ? 36  PRO A CA  1 
ATOM   291  C C   . PRO A 1 36  ? 8.95815  32.14839 18.35402  1.000 39.65500 ? 36  PRO A C   1 
ATOM   292  O O   . PRO A 1 36  ? 9.05950  32.15204 17.12684  1.000 40.86493 ? 36  PRO A O   1 
ATOM   293  C CB  . PRO A 1 36  ? 7.92460  30.06318 19.29264  1.000 37.53357 ? 36  PRO A CB  1 
ATOM   294  C CG  . PRO A 1 36  ? 7.37907  29.44025 18.00718  1.000 37.76760 ? 36  PRO A CG  1 
ATOM   295  C CD  . PRO A 1 36  ? 6.16764  30.29579 17.69484  1.000 37.92844 ? 36  PRO A CD  1 
ATOM   296  N N   . GLU A 1 37  ? 9.89813  32.63536 19.15832  1.000 38.88564 ? 37  GLU A N   1 
ATOM   297  C CA  . GLU A 1 37  ? 11.21555 32.97493 18.65106  1.000 38.83861 ? 37  GLU A CA  1 
ATOM   298  C C   . GLU A 1 37  ? 12.26921 31.95495 19.04182  1.000 35.39975 ? 37  GLU A C   1 
ATOM   299  O O   . GLU A 1 37  ? 13.31251 31.88880 18.39133  1.000 35.45289 ? 37  GLU A O   1 
ATOM   300  C CB  . GLU A 1 37  ? 11.63048 34.36756 19.14134  1.000 42.77897 ? 37  GLU A CB  1 
ATOM   301  C CG  . GLU A 1 37  ? 10.82158 35.47921 18.48490  0.800 46.32177 ? 37  GLU A CG  1 
ATOM   302  C CD  . GLU A 1 37  ? 10.94319 36.80175 19.20704  0.700 49.04344 ? 37  GLU A CD  1 
ATOM   303  O OE1 . GLU A 1 37  ? 11.58482 36.83251 20.27525  0.700 49.97633 ? 37  GLU A OE1 1 
ATOM   304  O OE2 . GLU A 1 37  ? 10.39251 37.80969 18.70659  0.700 49.88677 ? 37  GLU A OE2 1 
ATOM   305  N N   . ILE A 1 38  ? 12.00926 31.16045 20.07761  1.000 32.74221 ? 38  ILE A N   1 
ATOM   306  C CA  . ILE A 1 38  ? 12.83271 30.02953 20.47344  1.000 31.37287 ? 38  ILE A CA  1 
ATOM   307  C C   . ILE A 1 38  ? 11.93505 28.80440 20.48988  1.000 30.44417 ? 38  ILE A C   1 
ATOM   308  O O   . ILE A 1 38  ? 10.83567 28.84044 21.05794  1.000 28.99044 ? 38  ILE A O   1 
ATOM   309  C CB  . ILE A 1 38  ? 13.47076 30.24448 21.86186  1.000 33.88282 ? 38  ILE A CB  1 
ATOM   310  C CG1 . ILE A 1 38  ? 14.33195 31.50800 21.87416  1.000 35.44554 ? 38  ILE A CG1 1 
ATOM   311  C CG2 . ILE A 1 38  ? 14.30042 29.03510 22.25644  1.000 34.47934 ? 38  ILE A CG2 1 
ATOM   312  C CD1 . ILE A 1 38  ? 15.66016 31.35923 21.16086  1.000 37.03170 ? 38  ILE A CD1 1 
ATOM   313  N N   . VAL A 1 39  ? 12.39865 27.72848 19.87126  1.000 29.19237 ? 39  VAL A N   1 
ATOM   314  C CA  . VAL A 1 39  ? 11.70246 26.45129 19.86552  1.000 28.54065 ? 39  VAL A CA  1 
ATOM   315  C C   . VAL A 1 39  ? 12.62139 25.42374 20.50279  1.000 26.40498 ? 39  VAL A C   1 
ATOM   316  O O   . VAL A 1 39  ? 13.71447 25.15764 19.98755  1.000 27.09757 ? 39  VAL A O   1 
ATOM   317  C CB  . VAL A 1 39  ? 11.30791 26.03048 18.44327  1.000 27.00485 ? 39  VAL A CB  1 
ATOM   318  C CG1 . VAL A 1 39  ? 10.77901 24.62389 18.45268  1.000 26.59841 ? 39  VAL A CG1 1 
ATOM   319  C CG2 . VAL A 1 39  ? 10.25382 26.99826 17.90736  1.000 28.28727 ? 39  VAL A CG2 1 
ATOM   320  N N   . ILE A 1 40  ? 12.19713 24.87074 21.63979  1.000 25.95288 ? 40  ILE A N   1 
ATOM   321  C CA  . ILE A 1 40  ? 12.94985 23.84471 22.33618  1.000 25.33483 ? 40  ILE A CA  1 
ATOM   322  C C   . ILE A 1 40  ? 12.29014 22.50387 22.09022  1.000 24.74407 ? 40  ILE A C   1 
ATOM   323  O O   . ILE A 1 40  ? 11.08647 22.34013 22.32451  1.000 25.87553 ? 40  ILE A O   1 
ATOM   324  C CB  . ILE A 1 40  ? 13.03223 24.13645 23.84402  1.000 26.55214 ? 40  ILE A CB  1 
ATOM   325  C CG1 . ILE A 1 40  ? 13.60603 25.53050 24.07947  1.000 27.90537 ? 40  ILE A CG1 1 
ATOM   326  C CG2 . ILE A 1 40  ? 13.86300 23.04936 24.53890  1.000 28.95575 ? 40  ILE A CG2 1 
ATOM   327  C CD1 . ILE A 1 40  ? 13.40582 26.01897 25.50983  1.000 29.58322 ? 40  ILE A CD1 1 
ATOM   328  N N   . SER A 1 41  ? 13.08151 21.54720 21.62314  1.000 24.31774 ? 41  SER A N   1 
ATOM   329  C CA  . SER A 1 41  ? 12.64182 20.19428 21.36054  1.000 24.76216 ? 41  SER A CA  1 
ATOM   330  C C   . SER A 1 41  ? 13.20065 19.27402 22.43347  1.000 25.86661 ? 41  SER A C   1 
ATOM   331  O O   . SER A 1 41  ? 14.41635 19.23108 22.63388  1.000 27.67620 ? 41  SER A O   1 
ATOM   332  C CB  . SER A 1 41  ? 13.12119 19.75575 19.96496  1.000 25.89479 ? 41  SER A CB  1 
ATOM   333  O OG  . SER A 1 41  ? 12.71792 18.44706 19.70705  1.000 32.67871 ? 41  SER A OG  1 
ATOM   334  N N   . ILE A 1 42  ? 12.32373 18.52998 23.11064  1.000 26.08388 ? 42  ILE A N   1 
ATOM   335  C CA  . ILE A 1 42  ? 12.73437 17.58777 24.15504  1.000 26.27623 ? 42  ILE A CA  1 
ATOM   336  C C   . ILE A 1 42  ? 12.39236 16.17614 23.69186  1.000 27.91622 ? 42  ILE A C   1 
ATOM   337  O O   . ILE A 1 42  ? 11.21151 15.79347 23.65132  1.000 28.65429 ? 42  ILE A O   1 
ATOM   338  C CB  . ILE A 1 42  ? 12.07866 17.88213 25.50639  1.000 25.97814 ? 42  ILE A CB  1 
ATOM   339  C CG1 . ILE A 1 42  ? 12.43371 19.30127 25.95914  1.000 25.71161 ? 42  ILE A CG1 1 
ATOM   340  C CG2 . ILE A 1 42  ? 12.56702 16.84560 26.50050  1.000 28.39400 ? 42  ILE A CG2 1 
ATOM   341  C CD1 . ILE A 1 42  ? 11.81449 19.72434 27.31897  1.000 25.91433 ? 42  ILE A CD1 1 
ATOM   342  N N   . GLY A 1 43  ? 13.42026 15.38950 23.37459  1.000 26.71091 ? 43  GLY A N   1 
ATOM   343  C CA  . GLY A 1 43  ? 13.18239 14.04842 22.88762  1.000 28.56915 ? 43  GLY A CA  1 
ATOM   344  C C   . GLY A 1 43  ? 14.40342 13.49578 22.19951  1.000 30.74875 ? 43  GLY A C   1 
ATOM   345  O O   . GLY A 1 43  ? 15.47598 13.38898 22.80598  1.000 35.43724 ? 43  GLY A O   1 
ATOM   346  N N   . GLY A 1 44  ? 14.24350 13.13021 20.93696  1.000 27.73920 ? 44  GLY A N   1 
ATOM   347  C CA  . GLY A 1 44  ? 15.34108 12.66244 20.11842  1.000 28.26391 ? 44  GLY A CA  1 
ATOM   348  C C   . GLY A 1 44  ? 15.38461 13.46725 18.84162  1.000 26.48322 ? 44  GLY A C   1 
ATOM   349  O O   . GLY A 1 44  ? 14.74601 14.51919 18.75100  1.000 25.92509 ? 44  GLY A O   1 
ATOM   350  N N   . ASP A 1 45  ? 16.12798 12.98270 17.84687  1.000 24.93116 ? 45  ASP A N   1 
ATOM   351  C CA  . ASP A 1 45  ? 16.22733 13.71670 16.59352  1.000 23.88702 ? 45  ASP A CA  1 
ATOM   352  C C   . ASP A 1 45  ? 14.91024 13.70397 15.83549  1.000 25.29368 ? 45  ASP A C   1 
ATOM   353  O O   . ASP A 1 45  ? 14.60627 14.66439 15.11176  1.000 24.98668 ? 45  ASP A O   1 
ATOM   354  C CB  . ASP A 1 45  ? 17.35107 13.13497 15.74025  1.000 22.95236 ? 45  ASP A CB  1 
ATOM   355  C CG  . ASP A 1 45  ? 18.71618 13.50822 16.24786  1.000 23.42169 ? 45  ASP A CG  1 
ATOM   356  O OD1 . ASP A 1 45  ? 18.84962 14.61723 16.82051  1.000 23.55114 ? 45  ASP A OD1 1 
ATOM   357  O OD2 . ASP A 1 45  ? 19.64660 12.68307 16.10698  1.000 25.83503 ? 45  ASP A OD2 1 
ATOM   358  N N   . GLY A 1 46  ? 14.12343 12.62903 15.97432  1.000 23.37417 ? 46  GLY A N   1 
ATOM   359  C CA  . GLY A 1 46  ? 12.79622 12.62733 15.38374  1.000 25.24118 ? 46  GLY A CA  1 
ATOM   360  C C   . GLY A 1 46  ? 11.93579 13.74528 15.93293  1.000 25.24261 ? 46  GLY A C   1 
ATOM   361  O O   . GLY A 1 46  ? 11.24552 14.43912 15.17961  1.000 25.48407 ? 46  GLY A O   1 
ATOM   362  N N   . THR A 1 47  ? 11.98745 13.95149 17.26050  1.000 24.41761 ? 47  THR A N   1 
ATOM   363  C CA  . THR A 1 47  ? 11.26661 15.05538 17.87437  1.000 24.27551 ? 47  THR A CA  1 
ATOM   364  C C   . THR A 1 47  ? 11.75214 16.38263 17.33092  1.000 23.33002 ? 47  THR A C   1 
ATOM   365  O O   . THR A 1 47  ? 10.94931 17.29008 17.07588  1.000 24.10330 ? 47  THR A O   1 
ATOM   366  C CB  . THR A 1 47  ? 11.44220 15.00757 19.39281  1.000 24.23841 ? 47  THR A CB  1 
ATOM   367  O OG1 . THR A 1 47  ? 11.17257 13.67980 19.84256  1.000 26.78031 ? 47  THR A OG1 1 
ATOM   368  C CG2 . THR A 1 47  ? 10.49966 15.98609 20.09934  1.000 25.30056 ? 47  THR A CG2 1 
ATOM   369  N N   . PHE A 1 48  ? 13.06672 16.51628 17.15745  1.000 22.45247 ? 48  PHE A N   1 
ATOM   370  C CA  . PHE A 1 48  ? 13.62015 17.75470 16.63660  1.000 22.49461 ? 48  PHE A CA  1 
ATOM   371  C C   . PHE A 1 48  ? 13.17369 17.98787 15.20508  1.000 23.01404 ? 48  PHE A C   1 
ATOM   372  O O   . PHE A 1 48  ? 12.80961 19.10622 14.83618  1.000 24.60551 ? 48  PHE A O   1 
ATOM   373  C CB  . PHE A 1 48  ? 15.14871 17.73928 16.70593  1.000 22.98744 ? 48  PHE A CB  1 
ATOM   374  C CG  . PHE A 1 48  ? 15.74908 19.07260 16.41046  1.000 23.23645 ? 48  PHE A CG  1 
ATOM   375  C CD1 . PHE A 1 48  ? 16.01478 19.44822 15.08908  1.000 24.11855 ? 48  PHE A CD1 1 
ATOM   376  C CD2 . PHE A 1 48  ? 15.99378 19.97358 17.43389  1.000 25.45475 ? 48  PHE A CD2 1 
ATOM   377  C CE1 . PHE A 1 48  ? 16.52692 20.68343 14.80747  1.000 25.87409 ? 48  PHE A CE1 1 
ATOM   378  C CE2 . PHE A 1 48  ? 16.51536 21.21751 17.15694  1.000 27.23397 ? 48  PHE A CE2 1 
ATOM   379  C CZ  . PHE A 1 48  ? 16.77575 21.57971 15.83836  1.000 27.38959 ? 48  PHE A CZ  1 
ATOM   380  N N   . LEU A 1 49  ? 13.22801 16.94617 14.37998  1.000 21.56371 ? 49  LEU A N   1 
ATOM   381  C CA  . LEU A 1 49  ? 12.79821 17.09728 12.99812  1.000 22.60540 ? 49  LEU A CA  1 
ATOM   382  C C   . LEU A 1 49  ? 11.34240 17.51796 12.94147  1.000 23.65877 ? 49  LEU A C   1 
ATOM   383  O O   . LEU A 1 49  ? 10.94913 18.32429 12.08899  1.000 24.79921 ? 49  LEU A O   1 
ATOM   384  C CB  . LEU A 1 49  ? 13.00236 15.78980 12.24766  1.000 23.83198 ? 49  LEU A CB  1 
ATOM   385  C CG  . LEU A 1 49  ? 14.42234 15.42949 11.83576  1.000 25.31226 ? 49  LEU A CG  1 
ATOM   386  C CD1 . LEU A 1 49  ? 14.42994 14.01204 11.29225  1.000 27.74252 ? 49  LEU A CD1 1 
ATOM   387  C CD2 . LEU A 1 49  ? 14.91560 16.39549 10.75954  1.000 25.23979 ? 49  LEU A CD2 1 
ATOM   388  N N   . SER A 1 50  ? 10.52211 16.99213 13.85807  1.000 24.40400 ? 50  SER A N   1 
ATOM   389  C CA  A SER A 1 50  ? 9.11221  17.35982 13.84058  0.700 24.18407 ? 50  SER A CA  1 
ATOM   390  C CA  B SER A 1 50  ? 9.10743  17.35143 13.86741  0.300 24.41745 ? 50  SER A CA  1 
ATOM   391  C C   . SER A 1 50  ? 8.91833  18.81019 14.25162  1.000 24.97436 ? 50  SER A C   1 
ATOM   392  O O   . SER A 1 50  ? 8.06144  19.50639 13.69001  1.000 27.50232 ? 50  SER A O   1 
ATOM   393  C CB  A SER A 1 50  ? 8.30690  16.41368 14.72680  0.700 26.78539 ? 50  SER A CB  1 
ATOM   394  C CB  B SER A 1 50  ? 8.33768  16.44359 14.82379  0.300 25.46079 ? 50  SER A CB  1 
ATOM   395  O OG  A SER A 1 50  ? 8.09446  15.18973 14.04041  0.700 27.62024 ? 50  SER A OG  1 
ATOM   396  O OG  B SER A 1 50  ? 6.97815  16.82161 14.86908  0.300 26.13903 ? 50  SER A OG  1 
ATOM   397  N N   . ALA A 1 51  ? 9.70752  19.28638 15.21501  1.000 24.79224 ? 51  ALA A N   1 
ATOM   398  C CA  . ALA A 1 51  ? 9.64851  20.69149 15.58961  1.000 23.53500 ? 51  ALA A CA  1 
ATOM   399  C C   . ALA A 1 51  ? 10.04598 21.57681 14.41894  1.000 23.73076 ? 51  ALA A C   1 
ATOM   400  O O   . ALA A 1 51  ? 9.40872  22.59996 14.15995  1.000 25.94893 ? 51  ALA A O   1 
ATOM   401  C CB  . ALA A 1 51  ? 10.55630 20.94149 16.79899  1.000 24.78136 ? 51  ALA A CB  1 
ATOM   402  N N   . PHE A 1 52  ? 11.11137 21.20202 13.70885  1.000 22.34210 ? 52  PHE A N   1 
ATOM   403  C CA  . PHE A 1 52  ? 11.51357 21.95032 12.52179  1.000 24.09159 ? 52  PHE A CA  1 
ATOM   404  C C   . PHE A 1 52  ? 10.36541 22.05473 11.52643  1.000 25.15572 ? 52  PHE A C   1 
ATOM   405  O O   . PHE A 1 52  ? 10.07049 23.13660 11.00238  1.000 27.77440 ? 52  PHE A O   1 
ATOM   406  C CB  . PHE A 1 52  ? 12.73664 21.28221 11.89497  1.000 23.44561 ? 52  PHE A CB  1 
ATOM   407  C CG  . PHE A 1 52  ? 13.04443 21.75241 10.50062  1.000 24.06894 ? 52  PHE A CG  1 
ATOM   408  C CD1 . PHE A 1 52  ? 13.58654 23.01244 10.27801  1.000 26.18291 ? 52  PHE A CD1 1 
ATOM   409  C CD2 . PHE A 1 52  ? 12.79751 20.93179 9.42389   1.000 24.61812 ? 52  PHE A CD2 1 
ATOM   410  C CE1 . PHE A 1 52  ? 13.88081 23.43719 8.97842   1.000 26.69033 ? 52  PHE A CE1 1 
ATOM   411  C CE2 . PHE A 1 52  ? 13.08078 21.34715 8.13157   1.000 25.07464 ? 52  PHE A CE2 1 
ATOM   412  C CZ  . PHE A 1 52  ? 13.61934 22.59743 7.90925   1.000 26.69386 ? 52  PHE A CZ  1 
ATOM   413  N N   . HIS A 1 53  ? 9.68405  20.94361 11.26646  1.000 24.58224 ? 53  HIS A N   1 
ATOM   414  C CA  . HIS A 1 53  ? 8.63413  20.98816 10.25709  1.000 25.63998 ? 53  HIS A CA  1 
ATOM   415  C C   . HIS A 1 53  ? 7.40415  21.71731 10.76009  1.000 27.89234 ? 53  HIS A C   1 
ATOM   416  O O   . HIS A 1 53  ? 6.66550  22.30129 9.96522   1.000 30.65057 ? 53  HIS A O   1 
ATOM   417  C CB  . HIS A 1 53  ? 8.31191  19.57792 9.78969   1.000 25.13239 ? 53  HIS A CB  1 
ATOM   418  C CG  . HIS A 1 53  ? 9.34651  19.04701 8.85990   1.000 26.11098 ? 53  HIS A CG  1 
ATOM   419  N ND1 . HIS A 1 53  ? 9.43570  19.46268 7.54712   1.000 27.33169 ? 53  HIS A ND1 1 
ATOM   420  C CD2 . HIS A 1 53  ? 10.39499 18.21935 9.06908   1.000 24.97970 ? 53  HIS A CD2 1 
ATOM   421  C CE1 . HIS A 1 53  ? 10.47619 18.88115 6.97882   1.000 26.84724 ? 53  HIS A CE1 1 
ATOM   422  N NE2 . HIS A 1 53  ? 11.07239 18.11791 7.87730   1.000 25.72219 ? 53  HIS A NE2 1 
ATOM   423  N N   . GLN A 1 54  ? 7.18432  21.72596 12.07552  1.000 28.28681 ? 54  GLN A N   1 
ATOM   424  C CA  . GLN A 1 54  ? 6.07040  22.49032 12.61755  1.000 29.96238 ? 54  GLN A CA  1 
ATOM   425  C C   . GLN A 1 54  ? 6.24897  23.97861 12.35840  1.000 31.07089 ? 54  GLN A C   1 
ATOM   426  O O   . GLN A 1 54  ? 5.25943  24.70634 12.19350  1.000 33.44961 ? 54  GLN A O   1 
ATOM   427  C CB  . GLN A 1 54  ? 5.93580  22.20179 14.11785  1.000 32.02863 ? 54  GLN A CB  1 
ATOM   428  C CG  . GLN A 1 54  ? 4.78472  22.88794 14.79904  1.000 35.75765 ? 54  GLN A CG  1 
ATOM   429  C CD  . GLN A 1 54  ? 4.63506  22.48568 16.27546  1.000 37.99187 ? 54  GLN A CD  1 
ATOM   430  O OE1 . GLN A 1 54  ? 5.21334  21.49528 16.73551  1.000 36.39481 ? 54  GLN A OE1 1 
ATOM   431  N NE2 . GLN A 1 54  ? 3.84942  23.25688 17.01501  1.000 40.85156 ? 54  GLN A NE2 1 
ATOM   432  N N   . TYR A 1 55  ? 7.49424  24.45643 12.29672  1.000 32.32358 ? 55  TYR A N   1 
ATOM   433  C CA  . TYR A 1 55  ? 7.73942  25.88571 12.13416  1.000 32.39002 ? 55  TYR A CA  1 
ATOM   434  C C   . TYR A 1 55  ? 8.51370  26.21310 10.86212  1.000 33.05360 ? 55  TYR A C   1 
ATOM   435  O O   . TYR A 1 55  ? 9.17053  27.26040 10.79459  1.000 33.22589 ? 55  TYR A O   1 
ATOM   436  C CB  . TYR A 1 55  ? 8.44483  26.43598 13.37280  1.000 33.38215 ? 55  TYR A CB  1 
ATOM   437  C CG  . TYR A 1 55  ? 7.54264  26.34282 14.58724  1.000 35.05054 ? 55  TYR A CG  1 
ATOM   438  C CD1 . TYR A 1 55  ? 6.48515  27.22478 14.75166  1.000 35.27752 ? 55  TYR A CD1 1 
ATOM   439  C CD2 . TYR A 1 55  ? 7.70683  25.33788 15.52396  1.000 35.66888 ? 55  TYR A CD2 1 
ATOM   440  C CE1 . TYR A 1 55  ? 5.63193  27.13414 15.84447  1.000 35.77382 ? 55  TYR A CE1 1 
ATOM   441  C CE2 . TYR A 1 55  ? 6.86199  25.23549 16.62657  1.000 36.19931 ? 55  TYR A CE2 1 
ATOM   442  C CZ  . TYR A 1 55  ? 5.82390  26.13655 16.77915  1.000 36.05771 ? 55  TYR A CZ  1 
ATOM   443  O OH  . TYR A 1 55  ? 4.97163  26.03849 17.86397  1.000 37.57280 ? 55  TYR A OH  1 
ATOM   444  N N   . GLU A 1 56  ? 8.40707  25.36464 9.83349   1.000 33.02837 ? 56  GLU A N   1 
ATOM   445  C CA  . GLU A 1 56  ? 9.19222  25.56590 8.61773   1.000 34.85927 ? 56  GLU A CA  1 
ATOM   446  C C   . GLU A 1 56  ? 8.83143  26.85481 7.88879   1.000 35.79960 ? 56  GLU A C   1 
ATOM   447  O O   . GLU A 1 56  ? 9.59648  27.29863 7.02169   1.000 37.43147 ? 56  GLU A O   1 
ATOM   448  C CB  . GLU A 1 56  ? 9.04124  24.36176 7.67304   1.000 35.57087 ? 56  GLU A CB  1 
ATOM   449  C CG  . GLU A 1 56  ? 7.60903  23.99916 7.31749   0.800 36.96137 ? 56  GLU A CG  1 
ATOM   450  C CD  . GLU A 1 56  ? 7.49533  22.67547 6.58056   0.700 38.84364 ? 56  GLU A CD  1 
ATOM   451  O OE1 . GLU A 1 56  ? 8.52598  21.99693 6.39321   0.700 36.97520 ? 56  GLU A OE1 1 
ATOM   452  O OE2 . GLU A 1 56  ? 6.36396  22.31373 6.18884   0.700 42.67828 ? 56  GLU A OE2 1 
ATOM   453  N N   . GLU A 1 57  ? 7.70430  27.47399 8.21849   1.000 37.33409 ? 57  GLU A N   1 
ATOM   454  C CA  . GLU A 1 57  ? 7.31623  28.71899 7.56971   1.000 40.19002 ? 57  GLU A CA  1 
ATOM   455  C C   . GLU A 1 57  ? 7.80067  29.95480 8.31785   1.000 39.67852 ? 57  GLU A C   1 
ATOM   456  O O   . GLU A 1 57  ? 7.60321  31.07150 7.82997   1.000 40.95026 ? 57  GLU A O   1 
ATOM   457  C CB  . GLU A 1 57  ? 5.79550  28.77221 7.39583   1.000 44.21300 ? 57  GLU A CB  1 
ATOM   458  C CG  . GLU A 1 57  ? 5.26765  27.75775 6.39254   0.800 47.49497 ? 57  GLU A CG  1 
ATOM   459  C CD  . GLU A 1 57  ? 5.93735  27.87046 5.03171   0.600 50.76176 ? 57  GLU A CD  1 
ATOM   460  O OE1 . GLU A 1 57  ? 6.13563  29.00532 4.54185   0.600 51.91455 ? 57  GLU A OE1 1 
ATOM   461  O OE2 . GLU A 1 57  ? 6.27371  26.81709 4.45251   0.600 52.40630 ? 57  GLU A OE2 1 
ATOM   462  N N   . ARG A 1 58  ? 8.44010  29.78762 9.47707   1.000 37.52170 ? 58  ARG A N   1 
ATOM   463  C CA  . ARG A 1 58  ? 8.98375  30.91415 10.23003  1.000 37.46198 ? 58  ARG A CA  1 
ATOM   464  C C   . ARG A 1 58  ? 10.44552 30.67528 10.58216  1.000 36.17443 ? 58  ARG A C   1 
ATOM   465  O O   . ARG A 1 58  ? 10.92802 31.12809 11.62761  1.000 36.61901 ? 58  ARG A O   1 
ATOM   466  C CB  . ARG A 1 58  ? 8.15966  31.18953 11.48951  1.000 39.75517 ? 58  ARG A CB  1 
ATOM   467  C CG  . ARG A 1 58  ? 6.86610  31.94361 11.18587  0.800 42.01246 ? 58  ARG A CG  1 
ATOM   468  C CD  . ARG A 1 58  ? 6.10927  32.37449 12.43546  0.700 44.59990 ? 58  ARG A CD  1 
ATOM   469  N NE  . ARG A 1 58  ? 6.87762  33.30378 13.25470  0.700 46.46671 ? 58  ARG A NE  1 
ATOM   470  C CZ  . ARG A 1 58  ? 7.52240  32.95782 14.36219  0.700 47.46992 ? 58  ARG A CZ  1 
ATOM   471  N NH1 . ARG A 1 58  ? 7.48922  31.71834 14.81912  0.700 48.84017 ? 58  ARG A NH1 1 
ATOM   472  N NH2 . ARG A 1 58  ? 8.22161  33.87657 15.02274  0.700 46.91974 ? 58  ARG A NH2 1 
ATOM   473  N N   . LEU A 1 59  ? 11.16841 29.97211 9.71004   1.000 35.26659 ? 59  LEU A N   1 
ATOM   474  C CA  . LEU A 1 59  ? 12.52960 29.57624 10.04387  1.000 34.92777 ? 59  LEU A CA  1 
ATOM   475  C C   . LEU A 1 59  ? 13.44627 30.77208 10.24740  1.000 37.08589 ? 59  LEU A C   1 
ATOM   476  O O   . LEU A 1 59  ? 14.41886 30.67300 11.00142  1.000 39.36630 ? 59  LEU A O   1 
ATOM   477  C CB  . LEU A 1 59  ? 13.09391 28.66752 8.96020   1.000 32.92152 ? 59  LEU A CB  1 
ATOM   478  C CG  . LEU A 1 59  ? 12.47605 27.28043 8.86705   1.000 31.70985 ? 59  LEU A CG  1 
ATOM   479  C CD1 . LEU A 1 59  ? 13.06124 26.58862 7.65327   1.000 30.70960 ? 59  LEU A CD1 1 
ATOM   480  C CD2 . LEU A 1 59  ? 12.76021 26.48815 10.12756  1.000 30.76660 ? 59  LEU A CD2 1 
ATOM   481  N N   . ASP A 1 60  ? 13.18373 31.90014 9.58538   1.000 37.58824 ? 60  ASP A N   1 
ATOM   482  C CA  . ASP A 1 60  ? 14.06503 33.04844 9.77052   1.000 41.26072 ? 60  ASP A CA  1 
ATOM   483  C C   . ASP A 1 60  ? 13.74568 33.84196 11.03466  1.000 41.24864 ? 60  ASP A C   1 
ATOM   484  O O   . ASP A 1 60  ? 14.49479 34.76261 11.37106  1.000 41.84072 ? 60  ASP A O   1 
ATOM   485  C CB  . ASP A 1 60  ? 14.05920 33.97455 8.52736   1.000 45.80255 ? 60  ASP A CB  1 
ATOM   486  C CG  . ASP A 1 60  ? 12.66357 34.34793 8.05137   0.600 48.51749 ? 60  ASP A CG  1 
ATOM   487  O OD1 . ASP A 1 60  ? 11.67232 33.77742 8.54788   0.600 49.22385 ? 60  ASP A OD1 1 
ATOM   488  O OD2 . ASP A 1 60  ? 12.56406 35.22121 7.15681   0.600 51.33764 ? 60  ASP A OD2 1 
ATOM   489  N N   . GLU A 1 61  ? 12.68720 33.48499 11.76493  1.000 39.42651 ? 61  GLU A N   1 
ATOM   490  C CA  . GLU A 1 61  ? 12.34463 34.14860 13.01474  1.000 40.79261 ? 61  GLU A CA  1 
ATOM   491  C C   . GLU A 1 61  ? 12.61308 33.29681 14.24985  1.000 37.62936 ? 61  GLU A C   1 
ATOM   492  O O   . GLU A 1 61  ? 12.38236 33.77170 15.36809  1.000 37.85110 ? 61  GLU A O   1 
ATOM   493  C CB  . GLU A 1 61  ? 10.86858 34.56508 13.01225  1.000 44.98064 ? 61  GLU A CB  1 
ATOM   494  C CG  . GLU A 1 61  ? 10.50553 35.62776 12.00031  0.700 48.90573 ? 61  GLU A CG  1 
ATOM   495  C CD  . GLU A 1 61  ? 9.97571  35.03408 10.71451  0.600 52.90803 ? 61  GLU A CD  1 
ATOM   496  O OE1 . GLU A 1 61  ? 10.05781 33.79853 10.55800  0.600 54.62973 ? 61  GLU A OE1 1 
ATOM   497  O OE2 . GLU A 1 61  ? 9.46768  35.79587 9.86673   0.600 54.32444 ? 61  GLU A OE2 1 
ATOM   498  N N   . ILE A 1 62  ? 13.10374 32.06889 14.09031  1.000 33.31890 ? 62  ILE A N   1 
ATOM   499  C CA  . ILE A 1 62  ? 13.18670 31.10066 15.17960  1.000 31.73652 ? 62  ILE A CA  1 
ATOM   500  C C   . ILE A 1 62  ? 14.61402 30.60146 15.33603  1.000 31.92189 ? 62  ILE A C   1 
ATOM   501  O O   . ILE A 1 62  ? 15.29684 30.33022 14.34246  1.000 32.70335 ? 62  ILE A O   1 
ATOM   502  C CB  . ILE A 1 62  ? 12.25208 29.89966 14.93247  1.000 31.42898 ? 62  ILE A CB  1 
ATOM   503  C CG1 . ILE A 1 62  ? 10.78528 30.34430 14.95799  1.000 31.78550 ? 62  ILE A CG1 1 
ATOM   504  C CG2 . ILE A 1 62  ? 12.53412 28.78796 15.96054  1.000 31.23220 ? 62  ILE A CG2 1 
ATOM   505  C CD1 . ILE A 1 62  ? 9.81554  29.27405 14.47283  1.000 32.91014 ? 62  ILE A CD1 1 
ATOM   506  N N   . ALA A 1 63  ? 15.05325 30.44189 16.58390  1.000 30.91116 ? 63  ALA A N   1 
ATOM   507  C CA  . ALA A 1 63  ? 16.25938 29.68725 16.89295  1.000 30.68342 ? 63  ALA A CA  1 
ATOM   508  C C   . ALA A 1 63  ? 15.85852 28.41652 17.62794  1.000 28.46219 ? 63  ALA A C   1 
ATOM   509  O O   . ALA A 1 63  ? 15.07306 28.46890 18.58533  1.000 29.00080 ? 63  ALA A O   1 
ATOM   510  C CB  . ALA A 1 63  ? 17.23903 30.50961 17.73167  1.000 31.56951 ? 63  ALA A CB  1 
ATOM   511  N N   . PHE A 1 64  ? 16.40063 27.28727 17.18727  1.000 25.24745 ? 64  PHE A N   1 
ATOM   512  C CA  . PHE A 1 64  ? 16.04230 25.97332 17.69766  1.000 24.98765 ? 64  PHE A CA  1 
ATOM   513  C C   . PHE A 1 64  ? 17.06610 25.49457 18.72299  1.000 25.71052 ? 64  PHE A C   1 
ATOM   514  O O   . PHE A 1 64  ? 18.26226 25.78669 18.61962  1.000 27.40498 ? 64  PHE A O   1 
ATOM   515  C CB  . PHE A 1 64  ? 15.94443 24.94789 16.56358  1.000 26.45415 ? 64  PHE A CB  1 
ATOM   516  C CG  . PHE A 1 64  ? 14.75269 25.12923 15.66026  1.000 25.72422 ? 64  PHE A CG  1 
ATOM   517  C CD1 . PHE A 1 64  ? 14.82907 25.94108 14.53921  1.000 26.92415 ? 64  PHE A CD1 1 
ATOM   518  C CD2 . PHE A 1 64  ? 13.57353 24.44264 15.90087  1.000 27.40000 ? 64  PHE A CD2 1 
ATOM   519  C CE1 . PHE A 1 64  ? 13.74130 26.09355 13.68939  1.000 27.57153 ? 64  PHE A CE1 1 
ATOM   520  C CE2 . PHE A 1 64  ? 12.47909 24.59204 15.06576  1.000 27.69762 ? 64  PHE A CE2 1 
ATOM   521  C CZ  . PHE A 1 64  ? 12.56677 25.41935 13.94517  1.000 27.57241 ? 64  PHE A CZ  1 
ATOM   522  N N   . ILE A 1 65  ? 16.57991 24.74576 19.71536  1.000 24.46671 ? 65  ILE A N   1 
ATOM   523  C CA  . ILE A 1 65  ? 17.43033 24.07177 20.69282  1.000 25.12834 ? 65  ILE A CA  1 
ATOM   524  C C   . ILE A 1 65  ? 16.86845 22.67679 20.91697  1.000 24.82215 ? 65  ILE A C   1 
ATOM   525  O O   . ILE A 1 65  ? 15.65663 22.51248 21.08456  1.000 26.49131 ? 65  ILE A O   1 
ATOM   526  C CB  . ILE A 1 65  ? 17.48671 24.82770 22.04248  1.000 29.14703 ? 65  ILE A CB  1 
ATOM   527  C CG1 . ILE A 1 65  ? 17.99477 26.25653 21.87615  1.000 31.41472 ? 65  ILE A CG1 1 
ATOM   528  C CG2 . ILE A 1 65  ? 18.38950 24.08058 23.03346  1.000 30.43975 ? 65  ILE A CG2 1 
ATOM   529  C CD1 . ILE A 1 65  ? 17.75528 27.13095 23.06711  1.000 34.02138 ? 65  ILE A CD1 1 
ATOM   530  N N   . GLY A 1 66  ? 17.73924 21.68225 20.97155  1.000 23.80858 ? 66  GLY A N   1 
ATOM   531  C CA  . GLY A 1 66  ? 17.33186 20.30160 21.21230  1.000 26.16175 ? 66  GLY A CA  1 
ATOM   532  C C   . GLY A 1 66  ? 17.89957 19.75936 22.50840  1.000 26.43190 ? 66  GLY A C   1 
ATOM   533  O O   . GLY A 1 66  ? 19.08411 19.93038 22.79252  1.000 28.45248 ? 66  GLY A O   1 
ATOM   534  N N   . ILE A 1 67  ? 17.04616 19.09686 23.28635  1.000 24.88487 ? 67  ILE A N   1 
ATOM   535  C CA  . ILE A 1 67  ? 17.44833 18.35712 24.47934  1.000 25.96023 ? 67  ILE A CA  1 
ATOM   536  C C   . ILE A 1 67  ? 17.18257 16.88750 24.20424  1.000 28.22240 ? 67  ILE A C   1 
ATOM   537  O O   . ILE A 1 67  ? 16.08502 16.53449 23.75846  1.000 30.83042 ? 67  ILE A O   1 
ATOM   538  C CB  . ILE A 1 67  ? 16.66441 18.82598 25.72059  1.000 27.14635 ? 67  ILE A CB  1 
ATOM   539  C CG1 . ILE A 1 67  ? 16.86004 20.32431 25.92270  1.000 29.23968 ? 67  ILE A CG1 1 
ATOM   540  C CG2 . ILE A 1 67  ? 17.08974 18.01298 26.93132  1.000 29.77887 ? 67  ILE A CG2 1 
ATOM   541  C CD1 . ILE A 1 67  ? 16.03576 20.89561 27.02434  1.000 30.31842 ? 67  ILE A CD1 1 
ATOM   542  N N   . HIS A 1 68  ? 18.16485 16.02576 24.46064  1.000 29.90219 ? 68  HIS A N   1 
ATOM   543  C CA  . HIS A 1 68  ? 17.97665 14.60219 24.20181  1.000 33.40433 ? 68  HIS A CA  1 
ATOM   544  C C   . HIS A 1 68  ? 17.72195 13.87098 25.51418  1.000 36.02996 ? 68  HIS A C   1 
ATOM   545  O O   . HIS A 1 68  ? 18.57336 13.86515 26.41287  1.000 37.38864 ? 68  HIS A O   1 
ATOM   546  C CB  . HIS A 1 68  ? 19.15673 14.00019 23.43071  1.000 35.35440 ? 68  HIS A CB  1 
ATOM   547  C CG  . HIS A 1 68  ? 20.46853 14.09714 24.13928  0.700 35.51728 ? 68  HIS A CG  1 
ATOM   548  N ND1 . HIS A 1 68  ? 20.89989 13.14716 25.04030  0.700 38.07268 ? 68  HIS A ND1 1 
ATOM   549  C CD2 . HIS A 1 68  ? 21.44593 15.03039 24.07761  0.700 35.24789 ? 68  HIS A CD2 1 
ATOM   550  C CE1 . HIS A 1 68  ? 22.08801 13.49077 25.50380  0.700 36.93102 ? 68  HIS A CE1 1 
ATOM   551  N NE2 . HIS A 1 68  ? 22.44304 14.62925 24.93436  0.700 36.44987 ? 68  HIS A NE2 1 
ATOM   552  N N   . THR A 1 69  ? 16.54714 13.25759 25.62444  1.000 38.93212 ? 69  THR A N   1 
ATOM   553  C CA  . THR A 1 69  ? 16.22613 12.51511 26.83453  1.000 43.69419 ? 69  THR A CA  1 
ATOM   554  C C   . THR A 1 69  ? 16.65026 11.05737 26.75217  1.000 46.82314 ? 69  THR A C   1 
ATOM   555  O O   . THR A 1 69  ? 16.73424 10.38864 27.79035  1.000 46.51337 ? 69  THR A O   1 
ATOM   556  C CB  . THR A 1 69  ? 14.72732 12.61790 27.16235  1.000 44.70802 ? 69  THR A CB  1 
ATOM   557  O OG1 . THR A 1 69  ? 13.94462 12.47266 25.97618  1.000 46.29351 ? 69  THR A OG1 1 
ATOM   558  C CG2 . THR A 1 69  ? 14.40910 13.96807 27.80965  1.000 45.98267 ? 69  THR A CG2 1 
ATOM   559  N N   . GLY A 1 70  ? 16.94216 10.56390 25.55932  1.000 49.33712 ? 70  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70  ? 17.60695 9.29648  25.36843  1.000 50.13429 ? 70  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70  ? 19.06083 9.48205  24.99358  1.000 51.22319 ? 70  GLY A C   1 
ATOM   562  O O   . GLY A 1 70  ? 19.72291 10.43464 25.42209  1.000 50.01764 ? 70  GLY A O   1 
ATOM   563  N N   . HIS A 1 71  ? 19.56775 8.56650  24.17302  1.000 53.02142 ? 71  HIS A N   1 
ATOM   564  C CA  . HIS A 1 71  ? 20.93406 8.68710  23.68026  1.000 55.10541 ? 71  HIS A CA  1 
ATOM   565  C C   . HIS A 1 71  ? 21.14038 10.03878 23.00551  1.000 54.65266 ? 71  HIS A C   1 
ATOM   566  O O   . HIS A 1 71  ? 20.19598 10.66483 22.51238  1.000 54.41983 ? 71  HIS A O   1 
ATOM   567  C CB  . HIS A 1 71  ? 21.24517 7.56472  22.69580  1.000 56.45118 ? 71  HIS A CB  1 
ATOM   568  C CG  . HIS A 1 71  ? 20.40076 7.59673  21.45890  0.600 57.24443 ? 71  HIS A CG  1 
ATOM   569  N ND1 . HIS A 1 71  ? 20.66285 8.43502  20.39495  0.600 57.64987 ? 71  HIS A ND1 1 
ATOM   570  C CD2 . HIS A 1 71  ? 19.30499 6.88044  21.11086  0.600 57.38435 ? 71  HIS A CD2 1 
ATOM   571  C CE1 . HIS A 1 71  ? 19.76558 8.23242  19.44492  0.600 57.70570 ? 71  HIS A CE1 1 
ATOM   572  N NE2 . HIS A 1 71  ? 18.93056 7.29366  19.85398  0.600 57.58177 ? 71  HIS A NE2 1 
ATOM   573  N N   . LEU A 1 72  ? 22.39538 10.48897 22.98783  1.000 53.19273 ? 72  LEU A N   1 
ATOM   574  C CA  . LEU A 1 72  ? 22.73442 11.75887 22.36187  1.000 51.37703 ? 72  LEU A CA  1 
ATOM   575  C C   . LEU A 1 72  ? 22.14849 11.81773 20.95746  1.000 50.25180 ? 72  LEU A C   1 
ATOM   576  O O   . LEU A 1 72  ? 22.54508 11.04924 20.07865  1.000 52.46618 ? 72  LEU A O   1 
ATOM   577  C CB  . LEU A 1 72  ? 24.25442 11.95367 22.32932  1.000 51.04433 ? 72  LEU A CB  1 
ATOM   578  C CG  . LEU A 1 72  ? 24.83248 13.12635 21.52547  1.000 51.88157 ? 72  LEU A CG  1 
ATOM   579  C CD1 . LEU A 1 72  ? 24.44030 14.49733 22.08992  1.000 52.61955 ? 72  LEU A CD1 1 
ATOM   580  C CD2 . LEU A 1 72  ? 26.35168 13.00924 21.41700  1.000 52.10769 ? 72  LEU A CD2 1 
ATOM   581  N N   . GLY A 1 73  ? 21.16288 12.68955 20.76667  1.000 47.14644 ? 73  GLY A N   1 
ATOM   582  C CA  . GLY A 1 73  ? 20.67069 12.96794 19.44588  1.000 42.04685 ? 73  GLY A CA  1 
ATOM   583  C C   . GLY A 1 73  ? 21.56588 13.96733 18.74942  1.000 38.82067 ? 73  GLY A C   1 
ATOM   584  O O   . GLY A 1 73  ? 22.21423 14.80853 19.37037  1.000 41.88560 ? 73  GLY A O   1 
ATOM   585  N N   . PHE A 1 74  ? 21.61327 13.86090 17.42917  1.000 34.96695 ? 74  PHE A N   1 
ATOM   586  C CA  . PHE A 1 74  ? 22.57694 14.66020 16.70055  1.000 30.31723 ? 74  PHE A CA  1 
ATOM   587  C C   . PHE A 1 74  ? 22.21826 16.14081 16.72975  1.000 30.76346 ? 74  PHE A C   1 
ATOM   588  O O   . PHE A 1 74  ? 23.10805 16.99554 16.78526  1.000 33.99434 ? 74  PHE A O   1 
ATOM   589  C CB  . PHE A 1 74  ? 22.69365 14.14673 15.26856  1.000 31.58788 ? 74  PHE A CB  1 
ATOM   590  C CG  . PHE A 1 74  ? 23.90918 14.60441 14.61454  1.000 32.74243 ? 74  PHE A CG  1 
ATOM   591  C CD1 . PHE A 1 74  ? 25.10725 13.99775 14.90125  1.000 34.27838 ? 74  PHE A CD1 1 
ATOM   592  C CD2 . PHE A 1 74  ? 23.87272 15.65682 13.71224  1.000 35.45434 ? 74  PHE A CD2 1 
ATOM   593  C CE1 . PHE A 1 74  ? 26.27981 14.42444 14.33150  1.000 34.38467 ? 74  PHE A CE1 1 
ATOM   594  C CE2 . PHE A 1 74  ? 25.04307 16.08433 13.09907  1.000 38.12016 ? 74  PHE A CE2 1 
ATOM   595  C CZ  . PHE A 1 74  ? 26.25259 15.46612 13.41901  1.000 38.16824 ? 74  PHE A CZ  1 
ATOM   596  N N   . TYR A 1 75  ? 20.93096 16.47270 16.69392  1.000 26.10058 ? 75  TYR A N   1 
ATOM   597  C CA  . TYR A 1 75  ? 20.51151 17.86094 16.75601  1.000 26.50436 ? 75  TYR A CA  1 
ATOM   598  C C   . TYR A 1 75  ? 20.36436 18.34298 18.19351  1.000 32.76990 ? 75  TYR A C   1 
ATOM   599  O O   . TYR A 1 75  ? 19.98373 19.49253 18.41733  1.000 37.14417 ? 75  TYR A O   1 
ATOM   600  C CB  . TYR A 1 75  ? 19.21324 18.04730 15.96974  1.000 25.23872 ? 75  TYR A CB  1 
ATOM   601  C CG  . TYR A 1 75  ? 19.42656 17.85148 14.48600  1.000 22.51609 ? 75  TYR A CG  1 
ATOM   602  C CD1 . TYR A 1 75  ? 20.23168 18.72344 13.77652  1.000 21.67157 ? 75  TYR A CD1 1 
ATOM   603  C CD2 . TYR A 1 75  ? 18.84311 16.78695 13.80250  1.000 21.41663 ? 75  TYR A CD2 1 
ATOM   604  C CE1 . TYR A 1 75  ? 20.43524 18.56013 12.40212  1.000 21.79052 ? 75  TYR A CE1 1 
ATOM   605  C CE2 . TYR A 1 75  ? 19.06318 16.60239 12.42134  1.000 21.46035 ? 75  TYR A CE2 1 
ATOM   606  C CZ  . TYR A 1 75  ? 19.86128 17.48785 11.75663  1.000 20.73720 ? 75  TYR A CZ  1 
ATOM   607  O OH  . TYR A 1 75  ? 20.07254 17.32708 10.38913  1.000 20.52003 ? 75  TYR A OH  1 
ATOM   608  N N   . ALA A 1 76  ? 20.71117 17.50692 19.16092  1.000 34.80809 ? 76  ALA A N   1 
ATOM   609  C CA  . ALA A 1 76  ? 20.64948 17.86186 20.57884  1.000 35.48625 ? 76  ALA A CA  1 
ATOM   610  C C   . ALA A 1 76  ? 21.96060 18.48361 21.07021  1.000 36.75264 ? 76  ALA A C   1 
ATOM   611  O O   . ALA A 1 76  ? 23.04687 17.95707 20.80174  1.000 35.28425 ? 76  ALA A O   1 
ATOM   612  C CB  . ALA A 1 76  ? 20.32848 16.60635 21.37721  1.000 34.76897 ? 76  ALA A CB  1 
ATOM   613  N N   . ASP A 1 77  ? 21.85888 19.60182 21.80548  1.000 39.65582 ? 77  ASP A N   1 
ATOM   614  C CA  . ASP A 1 77  ? 23.01182 20.20707 22.47857  1.000 40.82501 ? 77  ASP A CA  1 
ATOM   615  C C   . ASP A 1 77  ? 23.03287 20.00884 23.98402  1.000 41.91988 ? 77  ASP A C   1 
ATOM   616  O O   . ASP A 1 77  ? 24.04843 20.33405 24.61673  1.000 42.89395 ? 77  ASP A O   1 
ATOM   617  C CB  . ASP A 1 77  ? 23.07093 21.71634 22.22031  1.000 42.71759 ? 77  ASP A CB  1 
ATOM   618  C CG  . ASP A 1 77  ? 23.27021 22.04001 20.77375  0.800 44.60801 ? 77  ASP A CG  1 
ATOM   619  O OD1 . ASP A 1 77  ? 23.85690 21.18686 20.07066  0.800 45.04482 ? 77  ASP A OD1 1 
ATOM   620  O OD2 . ASP A 1 77  ? 22.83787 23.13794 20.35056  0.800 45.61379 ? 77  ASP A OD2 1 
ATOM   621  N N   . TRP A 1 78  ? 21.95117 19.50964 24.57413  1.000 38.74112 ? 78  TRP A N   1 
ATOM   622  C CA  . TRP A 1 78  ? 21.80072 19.49930 26.01413  1.000 38.66004 ? 78  TRP A CA  1 
ATOM   623  C C   . TRP A 1 78  ? 21.30789 18.13970 26.46759  1.000 36.16658 ? 78  TRP A C   1 
ATOM   624  O O   . TRP A 1 78  ? 20.48250 17.51425 25.80028  1.000 33.75380 ? 78  TRP A O   1 
ATOM   625  C CB  . TRP A 1 78  ? 20.82563 20.59661 26.46665  1.000 38.38310 ? 78  TRP A CB  1 
ATOM   626  C CG  . TRP A 1 78  ? 21.29176 21.94538 26.05480  0.700 39.22126 ? 78  TRP A CG  1 
ATOM   627  C CD1 . TRP A 1 78  ? 21.01972 22.58207 24.87988  0.700 38.70868 ? 78  TRP A CD1 1 
ATOM   628  C CD2 . TRP A 1 78  ? 22.15536 22.81513 26.79311  0.700 40.24790 ? 78  TRP A CD2 1 
ATOM   629  N NE1 . TRP A 1 78  ? 21.64704 23.80466 24.84642  0.700 38.36944 ? 78  TRP A NE1 1 
ATOM   630  C CE2 . TRP A 1 78  ? 22.35352 23.97067 26.00831  0.700 40.56282 ? 78  TRP A CE2 1 
ATOM   631  C CE3 . TRP A 1 78  ? 22.77095 22.73685 28.04896  0.700 41.07148 ? 78  TRP A CE3 1 
ATOM   632  C CZ2 . TRP A 1 78  ? 23.14302 25.03746 26.43494  0.700 42.42155 ? 78  TRP A CZ2 1 
ATOM   633  C CZ3 . TRP A 1 78  ? 23.55503 23.79475 28.46736  0.700 42.15386 ? 78  TRP A CZ3 1 
ATOM   634  C CH2 . TRP A 1 78  ? 23.73339 24.93108 27.66476  0.700 42.68556 ? 78  TRP A CH2 1 
ATOM   635  N N   . ARG A 1 79  ? 21.82150 17.69782 27.59536  1.000 37.51921 ? 79  ARG A N   1 
ATOM   636  C CA  . ARG A 1 79  ? 21.24739 16.61010 28.36128  1.000 38.86769 ? 79  ARG A CA  1 
ATOM   637  C C   . ARG A 1 79  ? 20.18738 17.16335 29.30019  1.000 39.03644 ? 79  ARG A C   1 
ATOM   638  O O   . ARG A 1 79  ? 20.18872 18.35325 29.62204  1.000 40.40725 ? 79  ARG A O   1 
ATOM   639  C CB  . ARG A 1 79  ? 22.33402 15.90397 29.16997  1.000 40.84336 ? 79  ARG A CB  1 
ATOM   640  C CG  . ARG A 1 79  ? 23.51532 15.41805 28.34962  1.000 43.45047 ? 79  ARG A CG  1 
ATOM   641  C CD  . ARG A 1 79  ? 24.76097 15.22423 29.21719  1.000 46.03292 ? 79  ARG A CD  1 
ATOM   642  N NE  . ARG A 1 79  ? 24.46930 14.53627 30.46972  0.800 48.27538 ? 79  ARG A NE  1 
ATOM   643  C CZ  . ARG A 1 79  ? 24.71344 15.03220 31.67584  0.700 50.52208 ? 79  ARG A CZ  1 
ATOM   644  N NH1 . ARG A 1 79  ? 25.28504 16.21597 31.83598  0.700 50.96927 ? 79  ARG A NH1 1 
ATOM   645  N NH2 . ARG A 1 79  ? 24.38100 14.32001 32.74894  0.700 51.26044 ? 79  ARG A NH2 1 
ATOM   646  N N   . PRO A 1 80  ? 19.24884 16.32723 29.73284  1.000 39.89204 ? 80  PRO A N   1 
ATOM   647  C CA  . PRO A 1 80  ? 18.18830 16.82050 30.62805  1.000 41.21424 ? 80  PRO A CA  1 
ATOM   648  C C   . PRO A 1 80  ? 18.71058 17.40294 31.92986  1.000 43.46262 ? 80  PRO A C   1 
ATOM   649  O O   . PRO A 1 80  ? 18.07063 18.29345 32.50052  1.000 43.91231 ? 80  PRO A O   1 
ATOM   650  C CB  . PRO A 1 80  ? 17.33448 15.57016 30.87630  1.000 41.81007 ? 80  PRO A CB  1 
ATOM   651  C CG  . PRO A 1 80  ? 17.59712 14.68744 29.70508  1.000 41.24191 ? 80  PRO A CG  1 
ATOM   652  C CD  . PRO A 1 80  ? 19.02447 14.93933 29.29888  1.000 40.33005 ? 80  PRO A CD  1 
ATOM   653  N N   . ALA A 1 81  ? 19.85255 16.92347 32.42035  1.000 43.96060 ? 81  ALA A N   1 
ATOM   654  C CA  . ALA A 1 81  ? 20.40119 17.43576 33.66940  1.000 45.11292 ? 81  ALA A CA  1 
ATOM   655  C C   . ALA A 1 81  ? 20.77019 18.90943 33.57335  1.000 45.49971 ? 81  ALA A C   1 
ATOM   656  O O   . ALA A 1 81  ? 20.89880 19.57240 34.61020  1.000 46.01510 ? 81  ALA A O   1 
ATOM   657  C CB  . ALA A 1 81  ? 21.62453 16.61127 34.07879  1.000 46.52195 ? 81  ALA A CB  1 
ATOM   658  N N   . GLU A 1 82  ? 20.93031 19.43603 32.35926  1.000 44.38459 ? 82  GLU A N   1 
ATOM   659  C CA  . GLU A 1 82  ? 21.33306 20.81784 32.13190  1.000 45.27166 ? 82  GLU A CA  1 
ATOM   660  C C   . GLU A 1 82  ? 20.16640 21.74180 31.80846  1.000 43.69841 ? 82  GLU A C   1 
ATOM   661  O O   . GLU A 1 82  ? 20.39389 22.89435 31.42194  1.000 42.90491 ? 82  GLU A O   1 
ATOM   662  C CB  . GLU A 1 82  ? 22.34519 20.88558 30.99442  1.000 48.01916 ? 82  GLU A CB  1 
ATOM   663  C CG  . GLU A 1 82  ? 23.56592 20.01490 31.18836  1.000 51.04193 ? 82  GLU A CG  1 
ATOM   664  C CD  . GLU A 1 82  ? 24.37905 19.89255 29.91914  1.000 51.98344 ? 82  GLU A CD  1 
ATOM   665  O OE1 . GLU A 1 82  ? 23.85275 19.34331 28.92238  1.000 50.87730 ? 82  GLU A OE1 1 
ATOM   666  O OE2 . GLU A 1 82  ? 25.53590 20.36088 29.91474  1.000 53.01714 ? 82  GLU A OE2 1 
ATOM   667  N N   . ALA A 1 83  ? 18.92619 21.26738 31.94271  1.000 42.45858 ? 83  ALA A N   1 
ATOM   668  C CA  . ALA A 1 83  ? 17.78764 22.08805 31.54503  1.000 43.19534 ? 83  ALA A CA  1 
ATOM   669  C C   . ALA A 1 83  ? 17.74773 23.39785 32.32214  1.000 43.67644 ? 83  ALA A C   1 
ATOM   670  O O   . ALA A 1 83  ? 17.48232 24.46291 31.75200  1.000 42.83549 ? 83  ALA A O   1 
ATOM   671  C CB  . ALA A 1 83  ? 16.49017 21.30633 31.73847  1.000 44.96106 ? 83  ALA A CB  1 
ATOM   672  N N   . ASP A 1 84  ? 18.01024 23.34361 33.62851  1.000 44.81134 ? 84  ASP A N   1 
ATOM   673  C CA  . ASP A 1 84  ? 17.94159 24.56051 34.42897  1.000 45.66770 ? 84  ASP A CA  1 
ATOM   674  C C   . ASP A 1 84  ? 18.99939 25.56318 33.99312  1.000 44.48755 ? 84  ASP A C   1 
ATOM   675  O O   . ASP A 1 84  ? 18.72900 26.76836 33.92624  1.000 45.20211 ? 84  ASP A O   1 
ATOM   676  C CB  . ASP A 1 84  ? 18.08164 24.21803 35.91130  1.000 47.54514 ? 84  ASP A CB  1 
ATOM   677  C CG  . ASP A 1 84  ? 16.91712 23.39533 36.42212  0.700 50.33761 ? 84  ASP A CG  1 
ATOM   678  O OD1 . ASP A 1 84  ? 15.80371 23.56019 35.87833  0.700 51.63620 ? 84  ASP A OD1 1 
ATOM   679  O OD2 . ASP A 1 84  ? 17.10607 22.58962 37.35866  0.700 51.40439 ? 84  ASP A OD2 1 
ATOM   680  N N   . LYS A 1 85  ? 20.20610 25.08173 33.67406  1.000 42.76497 ? 85  LYS A N   1 
ATOM   681  C CA  . LYS A 1 85  ? 21.24026 25.96816 33.15384  1.000 43.13530 ? 85  LYS A CA  1 
ATOM   682  C C   . LYS A 1 85  ? 20.81064 26.58359 31.82848  1.000 42.13942 ? 85  LYS A C   1 
ATOM   683  O O   . LYS A 1 85  ? 21.06665 27.76713 31.57067  1.000 42.29978 ? 85  LYS A O   1 
ATOM   684  C CB  . LYS A 1 85  ? 22.55683 25.20097 32.98969  1.000 43.83495 ? 85  LYS A CB  1 
ATOM   685  N N   . LEU A 1 86  ? 20.14608 25.78886 30.98163  1.000 41.11768 ? 86  LEU A N   1 
ATOM   686  C CA  . LEU A 1 86  ? 19.65484 26.27076 29.69291  1.000 40.12174 ? 86  LEU A CA  1 
ATOM   687  C C   . LEU A 1 86  ? 18.59091 27.35144 29.87305  1.000 41.68004 ? 86  LEU A C   1 
ATOM   688  O O   . LEU A 1 86  ? 18.63032 28.39596 29.20866  1.000 42.64022 ? 86  LEU A O   1 
ATOM   689  C CB  . LEU A 1 86  ? 19.10772 25.08819 28.88408  1.000 39.30816 ? 86  LEU A CB  1 
ATOM   690  C CG  . LEU A 1 86  ? 18.51364 25.31922 27.49844  1.000 39.14663 ? 86  LEU A CG  1 
ATOM   691  C CD1 . LEU A 1 86  ? 19.54257 25.94435 26.58475  1.000 40.23711 ? 86  LEU A CD1 1 
ATOM   692  C CD2 . LEU A 1 86  ? 18.00996 24.00832 26.89612  1.000 38.63696 ? 86  LEU A CD2 1 
ATOM   693  N N   . VAL A 1 87  ? 17.62107 27.11349 30.76334  1.000 40.24577 ? 87  VAL A N   1 
ATOM   694  C CA  . VAL A 1 87  ? 16.61435 28.13273 31.05727  1.000 40.31995 ? 87  VAL A CA  1 
ATOM   695  C C   . VAL A 1 87  ? 17.29173 29.45117 31.39534  1.000 43.25496 ? 87  VAL A C   1 
ATOM   696  O O   . VAL A 1 87  ? 16.97313 30.50226 30.82717  1.000 44.04818 ? 87  VAL A O   1 
ATOM   697  C CB  . VAL A 1 87  ? 15.69488 27.67142 32.20242  1.000 38.61161 ? 87  VAL A CB  1 
ATOM   698  C CG1 . VAL A 1 87  ? 14.88763 28.86237 32.75852  1.000 39.71788 ? 87  VAL A CG1 1 
ATOM   699  C CG2 . VAL A 1 87  ? 14.76925 26.55769 31.72666  1.000 39.36054 ? 87  VAL A CG2 1 
ATOM   700  N N   . LYS A 1 88  ? 18.23932 29.41090 32.33578  1.000 45.72839 ? 88  LYS A N   1 
ATOM   701  C CA  . LYS A 1 88  ? 18.93988 30.62550 32.73995  1.000 47.99995 ? 88  LYS A CA  1 
ATOM   702  C C   . LYS A 1 88  ? 19.63794 31.27870 31.55219  1.000 49.05855 ? 88  LYS A C   1 
ATOM   703  O O   . LYS A 1 88  ? 19.42734 32.46318 31.26878  1.000 49.36467 ? 88  LYS A O   1 
ATOM   704  C CB  . LYS A 1 88  ? 19.93504 30.29548 33.85313  1.000 50.19488 ? 88  LYS A CB  1 
ATOM   705  C CG  . LYS A 1 88  ? 20.67733 31.48578 34.43165  1.000 51.42031 ? 88  LYS A CG  1 
ATOM   706  C CD  . LYS A 1 88  ? 21.30746 31.10804 35.76219  1.000 52.97200 ? 88  LYS A CD  1 
ATOM   707  C CE  . LYS A 1 88  ? 22.33288 32.13184 36.20247  1.000 54.54059 ? 88  LYS A CE  1 
ATOM   708  N NZ  . LYS A 1 88  ? 22.65441 31.97976 37.64693  1.000 55.33992 ? 88  LYS A NZ  1 
ATOM   709  N N   . LEU A 1 89  ? 20.45775 30.51492 30.82607  1.000 50.11430 ? 89  LEU A N   1 
ATOM   710  C CA  . LEU A 1 89  ? 21.23099 31.11317 29.74104  1.000 51.04934 ? 89  LEU A CA  1 
ATOM   711  C C   . LEU A 1 89  ? 20.32028 31.69065 28.66501  1.000 51.22489 ? 89  LEU A C   1 
ATOM   712  O O   . LEU A 1 89  ? 20.56838 32.79246 28.16106  1.000 50.93227 ? 89  LEU A O   1 
ATOM   713  C CB  . LEU A 1 89  ? 22.19860 30.08603 29.15165  1.000 52.55502 ? 89  LEU A CB  1 
ATOM   714  C CG  . LEU A 1 89  ? 23.40434 29.80442 30.05344  1.000 54.75287 ? 89  LEU A CG  1 
ATOM   715  C CD1 . LEU A 1 89  ? 24.31595 28.74701 29.45127  1.000 55.07743 ? 89  LEU A CD1 1 
ATOM   716  C CD2 . LEU A 1 89  ? 24.16657 31.09972 30.33029  1.000 55.65546 ? 89  LEU A CD2 1 
ATOM   717  N N   . LEU A 1 90  ? 19.25888 30.96239 28.30077  1.000 52.10533 ? 90  LEU A N   1 
ATOM   718  C CA  . LEU A 1 90  ? 18.29957 31.48294 27.33086  1.000 52.81036 ? 90  LEU A CA  1 
ATOM   719  C C   . LEU A 1 90  ? 17.63017 32.74777 27.84170  1.000 56.34703 ? 90  LEU A C   1 
ATOM   720  O O   . LEU A 1 90  ? 17.42686 33.70083 27.08107  1.000 57.42000 ? 90  LEU A O   1 
ATOM   721  C CB  . LEU A 1 90  ? 17.24051 30.43070 27.01561  1.000 52.35433 ? 90  LEU A CB  1 
ATOM   722  C CG  . LEU A 1 90  ? 17.45244 29.45899 25.86438  1.000 52.44240 ? 90  LEU A CG  1 
ATOM   723  C CD1 . LEU A 1 90  ? 16.35884 28.40144 25.89599  1.000 52.01101 ? 90  LEU A CD1 1 
ATOM   724  C CD2 . LEU A 1 90  ? 17.43307 30.21344 24.54208  1.000 53.10496 ? 90  LEU A CD2 1 
ATOM   725  N N   . ALA A 1 91  ? 17.25831 32.76619 29.12571  1.000 58.48205 ? 91  ALA A N   1 
ATOM   726  C CA  . ALA A 1 91  ? 16.57130 33.92771 29.67566  1.000 61.20952 ? 91  ALA A CA  1 
ATOM   727  C C   . ALA A 1 91  ? 17.40762 35.18970 29.51580  1.000 64.03675 ? 91  ALA A C   1 
ATOM   728  O O   . ALA A 1 91  ? 16.88490 36.24661 29.14076  1.000 65.23365 ? 91  ALA A O   1 
ATOM   729  C CB  . ALA A 1 91  ? 16.23181 33.68784 31.14570  1.000 61.11125 ? 91  ALA A CB  1 
ATOM   730  N N   . LYS A 1 92  ? 18.70870 35.10081 29.79541  1.000 64.87678 ? 92  LYS A N   1 
ATOM   731  C CA  . LYS A 1 92  ? 19.58529 36.26365 29.72915  1.000 66.74144 ? 92  LYS A CA  1 
ATOM   732  C C   . LYS A 1 92  ? 19.96684 36.64819 28.30407  1.000 67.50586 ? 92  LYS A C   1 
ATOM   733  O O   . LYS A 1 92  ? 20.52823 37.73156 28.10222  1.000 68.10166 ? 92  LYS A O   1 
ATOM   734  C CB  . LYS A 1 92  ? 20.84600 36.00991 30.56690  1.000 68.20803 ? 92  LYS A CB  1 
ATOM   735  C CG  . LYS A 1 92  ? 22.14811 36.46210 29.91928  1.000 69.40454 ? 92  LYS A CG  1 
ATOM   736  C CD  . LYS A 1 92  ? 23.15903 36.92050 30.96248  1.000 70.00090 ? 92  LYS A CD  1 
ATOM   737  C CE  . LYS A 1 92  ? 24.50600 37.25948 30.32863  1.000 70.20332 ? 92  LYS A CE  1 
ATOM   738  N NZ  . LYS A 1 92  ? 24.50061 38.54633 29.56846  1.000 70.42354 ? 92  LYS A NZ  1 
ATOM   739  N N   . GLY A 1 93  ? 19.66203 35.80807 27.31625  1.000 67.57597 ? 93  GLY A N   1 
ATOM   740  C CA  . GLY A 1 93  ? 20.03436 36.09377 25.94465  1.000 67.54345 ? 93  GLY A CA  1 
ATOM   741  C C   . GLY A 1 93  ? 21.49202 35.86595 25.63038  1.000 67.66950 ? 93  GLY A C   1 
ATOM   742  O O   . GLY A 1 93  ? 22.01845 36.47933 24.69637  1.000 67.82864 ? 93  GLY A O   1 
ATOM   743  N N   . GLU A 1 94  ? 22.16471 34.99872 26.38516  1.000 67.98859 ? 94  GLU A N   1 
ATOM   744  C CA  . GLU A 1 94  ? 23.60409 34.78454 26.23725  1.000 68.30732 ? 94  GLU A CA  1 
ATOM   745  C C   . GLU A 1 94  ? 23.84980 33.65637 25.23753  1.000 67.79354 ? 94  GLU A C   1 
ATOM   746  O O   . GLU A 1 94  ? 24.23208 32.53736 25.58818  1.000 68.67195 ? 94  GLU A O   1 
ATOM   747  C CB  . GLU A 1 94  ? 24.23549 34.47484 27.58918  1.000 68.46635 ? 94  GLU A CB  1 
ATOM   748  N N   . TYR A 1 95  ? 23.62079 33.96497 23.96213  1.000 65.91305 ? 95  TYR A N   1 
ATOM   749  C CA  . TYR A 1 95  ? 23.79591 32.91913 22.96647  1.000 62.81361 ? 95  TYR A CA  1 
ATOM   750  C C   . TYR A 1 95  ? 24.04267 33.50678 21.58742  1.000 61.97716 ? 95  TYR A C   1 
ATOM   751  O O   . TYR A 1 95  ? 23.48138 34.54499 21.22678  1.000 62.79802 ? 95  TYR A O   1 
ATOM   752  C CB  . TYR A 1 95  ? 22.58993 31.96998 22.93141  1.000 60.61558 ? 95  TYR A CB  1 
ATOM   753  C CG  . TYR A 1 95  ? 21.28270 32.54720 22.41754  1.000 59.29805 ? 95  TYR A CG  1 
ATOM   754  C CD1 . TYR A 1 95  ? 21.00238 32.59268 21.05629  1.000 58.99795 ? 95  TYR A CD1 1 
ATOM   755  C CD2 . TYR A 1 95  ? 20.30556 32.99311 23.29772  1.000 58.58963 ? 95  TYR A CD2 1 
ATOM   756  C CE1 . TYR A 1 95  ? 19.79520 33.09415 20.58713  1.000 58.80159 ? 95  TYR A CE1 1 
ATOM   757  C CE2 . TYR A 1 95  ? 19.09919 33.49411 22.83816  1.000 58.37622 ? 95  TYR A CE2 1 
ATOM   758  C CZ  . TYR A 1 95  ? 18.84962 33.54354 21.48462  1.000 59.19774 ? 95  TYR A CZ  1 
ATOM   759  O OH  . TYR A 1 95  ? 17.64953 34.04287 21.03241  1.000 60.63666 ? 95  TYR A OH  1 
ATOM   760  N N   . GLN A 1 96  ? 24.89419 32.81956 20.83445  1.000 59.66969 ? 96  GLN A N   1 
ATOM   761  C CA  . GLN A 1 96  ? 25.11754 33.04228 19.41833  1.000 57.03239 ? 96  GLN A CA  1 
ATOM   762  C C   . GLN A 1 96  ? 24.22036 32.11683 18.60500  1.000 50.87871 ? 96  GLN A C   1 
ATOM   763  O O   . GLN A 1 96  ? 23.75182 31.07986 19.08302  1.000 50.69132 ? 96  GLN A O   1 
ATOM   764  C CB  . GLN A 1 96  ? 26.58372 32.79177 19.06247  1.000 60.50122 ? 96  GLN A CB  1 
ATOM   765  C CG  . GLN A 1 96  ? 27.32418 34.02363 18.58474  0.700 63.82149 ? 96  GLN A CG  1 
ATOM   766  C CD  . GLN A 1 96  ? 28.73219 34.10472 19.13236  0.600 66.08971 ? 96  GLN A CD  1 
ATOM   767  O OE1 . GLN A 1 96  ? 29.47342 33.12037 19.12948  0.600 66.81621 ? 96  GLN A OE1 1 
ATOM   768  N NE2 . GLN A 1 96  ? 29.10669 35.28252 19.61826  0.600 66.95801 ? 96  GLN A NE2 1 
ATOM   769  N N   . LYS A 1 97  ? 23.98724 32.49552 17.35762  1.000 44.96740 ? 97  LYS A N   1 
ATOM   770  C CA  . LYS A 1 97  ? 23.19309 31.67384 16.45933  1.000 41.21321 ? 97  LYS A CA  1 
ATOM   771  C C   . LYS A 1 97  ? 24.08410 31.10236 15.36431  1.000 40.06274 ? 97  LYS A C   1 
ATOM   772  O O   . LYS A 1 97  ? 24.94498 31.79978 14.81760  1.000 41.77749 ? 97  LYS A O   1 
ATOM   773  C CB  . LYS A 1 97  ? 22.02972 32.46989 15.85981  1.000 41.51939 ? 97  LYS A CB  1 
ATOM   774  C CG  . LYS A 1 97  ? 20.98038 32.88597 16.89640  1.000 42.86772 ? 97  LYS A CG  1 
ATOM   775  C CD  . LYS A 1 97  ? 19.83692 33.66038 16.26768  1.000 44.69985 ? 97  LYS A CD  1 
ATOM   776  C CE  . LYS A 1 97  ? 20.07422 35.15322 16.35053  1.000 46.60839 ? 97  LYS A CE  1 
ATOM   777  N NZ  . LYS A 1 97  ? 18.88332 35.93293 15.89903  1.000 47.87697 ? 97  LYS A NZ  1 
ATOM   778  N N   . VAL A 1 98  ? 23.90031 29.81709 15.08365  1.000 36.37858 ? 98  VAL A N   1 
ATOM   779  C CA  . VAL A 1 98  ? 24.58796 29.14359 13.99165  1.000 35.71122 ? 98  VAL A CA  1 
ATOM   780  C C   . VAL A 1 98  ? 23.52889 28.65231 13.01937  1.000 31.80836 ? 98  VAL A C   1 
ATOM   781  O O   . VAL A 1 98  ? 22.41950 28.28516 13.41322  1.000 31.37955 ? 98  VAL A O   1 
ATOM   782  C CB  . VAL A 1 98  ? 25.46236 27.97089 14.48099  1.000 38.35723 ? 98  VAL A CB  1 
ATOM   783  C CG1 . VAL A 1 98  ? 26.51435 28.45691 15.47196  1.000 39.96736 ? 98  VAL A CG1 1 
ATOM   784  C CG2 . VAL A 1 98  ? 24.60009 26.89903 15.10452  1.000 40.47865 ? 98  VAL A CG2 1 
ATOM   785  N N   . SER A 1 99  ? 23.87100 28.65197 11.74030  1.000 29.90398 ? 99  SER A N   1 
ATOM   786  C CA  . SER A 1 99  ? 22.93221 28.27071 10.69581  1.000 31.62099 ? 99  SER A CA  1 
ATOM   787  C C   . SER A 1 99  ? 23.43997 27.05598 9.93031   1.000 30.18017 ? 99  SER A C   1 
ATOM   788  O O   . SER A 1 99  ? 24.62618 26.96696 9.60448   1.000 31.84743 ? 99  SER A O   1 
ATOM   789  C CB  . SER A 1 99  ? 22.69551 29.44342 9.74267   1.000 35.83870 ? 99  SER A CB  1 
ATOM   790  O OG  . SER A 1 99  ? 22.24135 30.56192 10.47728  1.000 40.37193 ? 99  SER A OG  1 
ATOM   791  N N   . TYR A 1 100 ? 22.53194 26.11297 9.64850   1.000 25.43722 ? 100 TYR A N   1 
ATOM   792  C CA  . TYR A 1 100 ? 22.83164 24.99772 8.75828   1.000 25.86455 ? 100 TYR A CA  1 
ATOM   793  C C   . TYR A 1 100 ? 22.02793 25.10770 7.46066   1.000 25.12383 ? 100 TYR A C   1 
ATOM   794  O O   . TYR A 1 100 ? 20.89860 25.61053 7.45854   1.000 24.68110 ? 100 TYR A O   1 
ATOM   795  C CB  . TYR A 1 100 ? 22.49903 23.64813 9.39985   1.000 27.05947 ? 100 TYR A CB  1 
ATOM   796  C CG  . TYR A 1 100 ? 23.38030 23.19505 10.54197  1.000 28.72498 ? 100 TYR A CG  1 
ATOM   797  C CD1 . TYR A 1 100 ? 24.46474 23.94558 10.97480  1.000 30.78258 ? 100 TYR A CD1 1 
ATOM   798  C CD2 . TYR A 1 100 ? 23.14961 21.96956 11.14340  1.000 31.58163 ? 100 TYR A CD2 1 
ATOM   799  C CE1 . TYR A 1 100 ? 25.27149 23.48864 12.02977  1.000 33.60342 ? 100 TYR A CE1 1 
ATOM   800  C CE2 . TYR A 1 100 ? 23.93406 21.51558 12.18059  1.000 33.72418 ? 100 TYR A CE2 1 
ATOM   801  C CZ  . TYR A 1 100 ? 24.99881 22.26657 12.60711  1.000 35.16018 ? 100 TYR A CZ  1 
ATOM   802  O OH  . TYR A 1 100 ? 25.76978 21.77288 13.62956  1.000 37.63059 ? 100 TYR A OH  1 
ATOM   803  N N   . PRO A 1 101 ? 22.57813 24.62301 6.34649   1.000 23.90031 ? 101 PRO A N   1 
ATOM   804  C CA  . PRO A 1 101 ? 21.84806 24.67050 5.07125   1.000 22.28521 ? 101 PRO A CA  1 
ATOM   805  C C   . PRO A 1 101 ? 20.71249 23.65977 5.03541   1.000 21.54433 ? 101 PRO A C   1 
ATOM   806  O O   . PRO A 1 101 ? 20.70845 22.66033 5.75750   1.000 23.21948 ? 101 PRO A O   1 
ATOM   807  C CB  . PRO A 1 101 ? 22.92223 24.32178 4.02911   1.000 23.36459 ? 101 PRO A CB  1 
ATOM   808  C CG  . PRO A 1 101 ? 24.26800 24.50302 4.75681   1.000 22.98370 ? 101 PRO A CG  1 
ATOM   809  C CD  . PRO A 1 101 ? 23.96718 24.15461 6.18440   1.000 24.10125 ? 101 PRO A CD  1 
ATOM   810  N N   . LEU A 1 102 ? 19.75136 23.91304 4.14141   1.000 21.69503 ? 102 LEU A N   1 
ATOM   811  C CA  . LEU A 1 102 ? 18.58960 23.05786 3.97343   1.000 20.45920 ? 102 LEU A CA  1 
ATOM   812  C C   . LEU A 1 102 ? 18.46816 22.65989 2.51233   1.000 20.95819 ? 102 LEU A C   1 
ATOM   813  O O   . LEU A 1 102 ? 19.11001 23.23475 1.62867   1.000 21.46250 ? 102 LEU A O   1 
ATOM   814  C CB  . LEU A 1 102 ? 17.28916 23.74186 4.40882   1.000 20.43462 ? 102 LEU A CB  1 
ATOM   815  C CG  . LEU A 1 102 ? 17.29577 24.21610 5.86693   1.000 21.61775 ? 102 LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 102 ? 16.07014 25.05811 6.14631   1.000 23.77420 ? 102 LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 102 ? 17.35597 23.00285 6.81312   1.000 22.52417 ? 102 LEU A CD2 1 
ATOM   818  N N   . LEU A 1 103 ? 17.62672 21.66590 2.26919   1.000 20.85213 ? 103 LEU A N   1 
ATOM   819  C CA  . LEU A 1 103 ? 17.42412 21.11438 0.92743   1.000 21.71219 ? 103 LEU A CA  1 
ATOM   820  C C   . LEU A 1 103 ? 16.01498 21.42397 0.44591   1.000 23.64188 ? 103 LEU A C   1 
ATOM   821  O O   . LEU A 1 103 ? 15.04243 21.14368 1.15216   1.000 23.60913 ? 103 LEU A O   1 
ATOM   822  C CB  . LEU A 1 103 ? 17.63170 19.60594 0.94098   1.000 21.15499 ? 103 LEU A CB  1 
ATOM   823  C CG  . LEU A 1 103 ? 17.27480 18.86145 -0.35689  1.000 19.80656 ? 103 LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 103 ? 18.22848 19.25984 -1.45568  1.000 19.08859 ? 103 LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 103 ? 17.32075 17.36165 -0.13357  1.000 20.48524 ? 103 LEU A CD2 1 
ATOM   826  N N   . LYS A 1 104 ? 15.89937 21.96412 -0.76657  1.000 23.30828 ? 104 LYS A N   1 
ATOM   827  C CA  . LYS A 1 104 ? 14.60254 22.19841 -1.38776  1.000 23.20198 ? 104 LYS A CA  1 
ATOM   828  C C   . LYS A 1 104 ? 14.32976 21.07553 -2.37977  1.000 23.72973 ? 104 LYS A C   1 
ATOM   829  O O   . LYS A 1 104 ? 15.18728 20.75960 -3.20747  1.000 25.17631 ? 104 LYS A O   1 
ATOM   830  C CB  . LYS A 1 104 ? 14.56519 23.54827 -2.10107  1.000 25.46192 ? 104 LYS A CB  1 
ATOM   831  C CG  . LYS A 1 104 ? 13.21246 23.88326 -2.73186  1.000 27.35695 ? 104 LYS A CG  1 
ATOM   832  C CD  . LYS A 1 104 ? 13.29959 25.18615 -3.51631  0.700 27.75953 ? 104 LYS A CD  1 
ATOM   833  C CE  . LYS A 1 104 ? 12.00159 25.49809 -4.22976  0.600 32.63057 ? 104 LYS A CE  1 
ATOM   834  N NZ  . LYS A 1 104 ? 12.11609 26.76455 -5.00150  0.600 35.54322 ? 104 LYS A NZ  1 
ATOM   835  N N   . THR A 1 105 ? 13.16317 20.44940 -2.25595  1.000 24.66240 ? 105 THR A N   1 
ATOM   836  C CA  . THR A 1 105 ? 12.65815 19.46125 -3.20562  1.000 25.89539 ? 105 THR A CA  1 
ATOM   837  C C   . THR A 1 105 ? 11.40444 20.00761 -3.86635  1.000 25.86709 ? 105 THR A C   1 
ATOM   838  O O   . THR A 1 105 ? 10.45697 20.38974 -3.17816  1.000 27.51715 ? 105 THR A O   1 
ATOM   839  C CB  . THR A 1 105 ? 12.32427 18.13681 -2.50871  1.000 27.92927 ? 105 THR A CB  1 
ATOM   840  O OG1 . THR A 1 105 ? 13.47412 17.66606 -1.80780  1.000 28.30380 ? 105 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 105 ? 11.86612 17.07922 -3.50721  1.000 28.85307 ? 105 THR A CG2 1 
ATOM   842  N N   . THR A 1 106 ? 11.38716 20.02309 -5.19694  1.000 24.27168 ? 106 THR A N   1 
ATOM   843  C CA  . THR A 1 106 ? 10.20568 20.40605 -5.94744  1.000 26.22803 ? 106 THR A CA  1 
ATOM   844  C C   . THR A 1 106 ? 9.70757  19.19511 -6.71442  1.000 26.56695 ? 106 THR A C   1 
ATOM   845  O O   . THR A 1 106 ? 10.49064 18.52339 -7.39504  1.000 28.07866 ? 106 THR A O   1 
ATOM   846  C CB  . THR A 1 106 ? 10.49917 21.55176 -6.91487  1.000 29.21748 ? 106 THR A CB  1 
ATOM   847  O OG1 . THR A 1 106 ? 11.08131 22.64665 -6.19361  1.000 31.25631 ? 106 THR A OG1 1 
ATOM   848  C CG2 . THR A 1 106 ? 9.20538  22.00566 -7.60384  1.000 29.12562 ? 106 THR A CG2 1 
ATOM   849  N N   . VAL A 1 107 ? 8.41794  18.91174 -6.59530  1.000 26.53465 ? 107 VAL A N   1 
ATOM   850  C CA  . VAL A 1 107 ? 7.78370  17.82455 -7.32607  1.000 28.91327 ? 107 VAL A CA  1 
ATOM   851  C C   . VAL A 1 107 ? 6.79665  18.43788 -8.30636  1.000 30.84980 ? 107 VAL A C   1 
ATOM   852  O O   . VAL A 1 107 ? 5.84861  19.12119 -7.90031  1.000 31.03278 ? 107 VAL A O   1 
ATOM   853  C CB  . VAL A 1 107 ? 7.07980  16.83940 -6.38126  1.000 29.74619 ? 107 VAL A CB  1 
ATOM   854  C CG1 . VAL A 1 107 ? 6.50967  15.68276 -7.18227  1.000 30.49917 ? 107 VAL A CG1 1 
ATOM   855  C CG2 . VAL A 1 107 ? 8.04821  16.34713 -5.30640  1.000 29.50576 ? 107 VAL A CG2 1 
ATOM   856  N N   . LYS A 1 108 ? 7.02237  18.19935 -9.59003  1.000 31.11898 ? 108 LYS A N   1 
ATOM   857  C CA  . LYS A 1 108 ? 6.15038  18.68163 -10.64870 1.000 33.24491 ? 108 LYS A CA  1 
ATOM   858  C C   . LYS A 1 108 ? 5.30126  17.52774 -11.15641 1.000 37.10558 ? 108 LYS A C   1 
ATOM   859  O O   . LYS A 1 108 ? 5.78950  16.39859 -11.26959 1.000 37.03375 ? 108 LYS A O   1 
ATOM   860  C CB  . LYS A 1 108 ? 6.97073  19.27439 -11.79339 1.000 35.90771 ? 108 LYS A CB  1 
ATOM   861  C CG  . LYS A 1 108 ? 7.75613  20.52185 -11.41561 1.000 38.57053 ? 108 LYS A CG  1 
ATOM   862  C CD  . LYS A 1 108 ? 8.61778  20.98263 -12.58603 0.700 39.83582 ? 108 LYS A CD  1 
ATOM   863  C CE  . LYS A 1 108 ? 9.13719  22.38460 -12.36677 0.700 40.65606 ? 108 LYS A CE  1 
ATOM   864  N NZ  . LYS A 1 108 ? 9.98935  22.44142 -11.15000 0.600 41.84058 ? 108 LYS A NZ  1 
ATOM   865  N N   . TYR A 1 109 ? 4.03423  17.81681 -11.46306 1.000 39.67678 ? 109 TYR A N   1 
ATOM   866  C CA  . TYR A 1 109 ? 3.05926  16.82882 -11.91676 1.000 45.71169 ? 109 TYR A CA  1 
ATOM   867  C C   . TYR A 1 109 ? 2.60990  17.10254 -13.34428 1.000 49.92207 ? 109 TYR A C   1 
ATOM   868  O O   . TYR A 1 109 ? 2.80410  18.18968 -13.89762 1.000 50.01439 ? 109 TYR A O   1 
ATOM   869  C CB  . TYR A 1 109 ? 1.82779  16.81806 -11.00640 1.000 44.50215 ? 109 TYR A CB  1 
ATOM   870  C CG  . TYR A 1 109 ? 2.18689  16.64382 -9.55029  1.000 44.04894 ? 109 TYR A CG  1 
ATOM   871  C CD1 . TYR A 1 109 ? 2.28600  15.38165 -8.99033  1.000 44.59770 ? 109 TYR A CD1 1 
ATOM   872  C CD2 . TYR A 1 109 ? 2.42582  17.74729 -8.74000  1.000 42.47748 ? 109 TYR A CD2 1 
ATOM   873  C CE1 . TYR A 1 109 ? 2.61183  15.21975 -7.66435  1.000 44.52740 ? 109 TYR A CE1 1 
ATOM   874  C CE2 . TYR A 1 109 ? 2.74731  17.59913 -7.41836  1.000 43.23972 ? 109 TYR A CE2 1 
ATOM   875  C CZ  . TYR A 1 109 ? 2.84177  16.33273 -6.88159  1.000 45.59254 ? 109 TYR A CZ  1 
ATOM   876  O OH  . TYR A 1 109 ? 3.17537  16.17171 -5.55549  1.000 46.06446 ? 109 TYR A OH  1 
ATOM   877  N N   . GLY A 1 110 ? 1.97762  16.08843 -13.93315 1.000 52.06625 ? 110 GLY A N   1 
ATOM   878  C CA  . GLY A 1 110 ? 1.32640  16.24299 -15.21430 1.000 53.80692 ? 110 GLY A CA  1 
ATOM   879  C C   . GLY A 1 110 ? -0.13886 16.59541 -15.05952 1.000 56.28109 ? 110 GLY A C   1 
ATOM   880  O O   . GLY A 1 110 ? -0.66732 16.72329 -13.95684 1.000 57.56687 ? 110 GLY A O   1 
ATOM   881  N N   . ILE A 1 111 ? -0.80396 16.74355 -16.20591 1.000 56.07628 ? 111 ILE A N   1 
ATOM   882  C CA  . ILE A 1 111 ? -2.20627 17.14263 -16.26180 1.000 54.86804 ? 111 ILE A CA  1 
ATOM   883  C C   . ILE A 1 111 ? -2.41371 18.37496 -15.39245 1.000 54.32803 ? 111 ILE A C   1 
ATOM   884  O O   . ILE A 1 111 ? -3.37479 18.44501 -14.61541 1.000 54.71213 ? 111 ILE A O   1 
ATOM   885  C CB  . ILE A 1 111 ? -3.13982 15.99473 -15.83328 1.000 54.37450 ? 111 ILE A CB  1 
ATOM   886  N N   . GLY A 1 112 ? -1.50832 19.34775 -15.51705 1.000 52.21372 ? 112 GLY A N   1 
ATOM   887  C CA  . GLY A 1 112 ? -1.61331 20.61430 -14.81749 1.000 51.60670 ? 112 GLY A CA  1 
ATOM   888  C C   . GLY A 1 112 ? -1.96617 20.50619 -13.34755 1.000 53.46254 ? 112 GLY A C   1 
ATOM   889  O O   . GLY A 1 112 ? -2.80477 21.26640 -12.85059 1.000 54.24708 ? 112 GLY A O   1 
ATOM   890  N N   . LYS A 1 113 ? -1.33523 19.56780 -12.63752 1.000 54.43473 ? 113 LYS A N   1 
ATOM   891  C CA  . LYS A 1 113 ? -1.49058 19.45105 -11.19389 1.000 53.75281 ? 113 LYS A CA  1 
ATOM   892  C C   . LYS A 1 113 ? -0.40738 20.20998 -10.43212 1.000 55.08576 ? 113 LYS A C   1 
ATOM   893  O O   . LYS A 1 113 ? -0.17714 19.92867 -9.25087  1.000 56.89606 ? 113 LYS A O   1 
ATOM   894  C CB  . LYS A 1 113 ? -1.51014 17.97886 -10.77362 1.000 51.64950 ? 113 LYS A CB  1 
ATOM   895  N N   . LYS A 1 114 ? 0.27846  21.14224 -11.09413 1.000 54.41511 ? 114 LYS A N   1 
ATOM   896  C CA  . LYS A 1 114 ? 1.08132  22.14463 -10.40533 1.000 52.23918 ? 114 LYS A CA  1 
ATOM   897  C C   . LYS A 1 114 ? 2.38508  21.58753 -9.84163  1.000 50.96749 ? 114 LYS A C   1 
ATOM   898  O O   . LYS A 1 114 ? 2.90949  20.57163 -10.32337 1.000 51.48713 ? 114 LYS A O   1 
ATOM   899  C CB  . LYS A 1 114 ? 0.25247  22.78290 -9.27999  1.000 50.83903 ? 114 LYS A CB  1 
ATOM   900  N N   . GLU A 1 115 ? 2.92194  22.27274 -8.83109  1.000 47.16032 ? 115 GLU A N   1 
ATOM   901  C CA  . GLU A 1 115 ? 4.13791  21.87801 -8.13361  1.000 44.40713 ? 115 GLU A CA  1 
ATOM   902  C C   . GLU A 1 115 ? 3.87141  21.79668 -6.63832  1.000 40.99643 ? 115 GLU A C   1 
ATOM   903  O O   . GLU A 1 115 ? 3.08053  22.56816 -6.08709  1.000 42.98507 ? 115 GLU A O   1 
ATOM   904  C CB  . GLU A 1 115 ? 5.27831  22.87634 -8.32010  1.000 46.28207 ? 115 GLU A CB  1 
ATOM   905  C CG  . GLU A 1 115 ? 5.87417  23.02404 -9.68879  0.800 49.74585 ? 115 GLU A CG  1 
ATOM   906  C CD  . GLU A 1 115 ? 6.95498  24.08202 -9.66084  0.700 52.44479 ? 115 GLU A CD  1 
ATOM   907  O OE1 . GLU A 1 115 ? 7.00677  24.82808 -8.65352  0.700 54.18963 ? 115 GLU A OE1 1 
ATOM   908  O OE2 . GLU A 1 115 ? 7.75476  24.15892 -10.61112 0.700 52.97667 ? 115 GLU A OE2 1 
ATOM   909  N N   . ALA A 1 116 ? 4.56618  20.88175 -5.98153  1.000 36.23103 ? 116 ALA A N   1 
ATOM   910  C CA  . ALA A 1 116 ? 4.66909  20.86471 -4.53156  1.000 34.80791 ? 116 ALA A CA  1 
ATOM   911  C C   . ALA A 1 116 ? 6.13273  21.05096 -4.16461  1.000 33.70540 ? 116 ALA A C   1 
ATOM   912  O O   . ALA A 1 116 ? 7.01536  20.47720 -4.81020  1.000 33.09593 ? 116 ALA A O   1 
ATOM   913  C CB  . ALA A 1 116 ? 4.14771  19.55249 -3.95134  1.000 37.59092 ? 116 ALA A CB  1 
ATOM   914  N N   . THR A 1 117 ? 6.39689  21.85556 -3.14097  1.000 33.50385 ? 117 THR A N   1 
ATOM   915  C CA  . THR A 1 117 ? 7.75869  22.05976 -2.66617  1.000 32.67241 ? 117 THR A CA  1 
ATOM   916  C C   . THR A 1 117 ? 7.88234  21.63946 -1.20858  1.000 31.86513 ? 117 THR A C   1 
ATOM   917  O O   . THR A 1 117 ? 6.97102  21.83868 -0.40082  1.000 33.10807 ? 117 THR A O   1 
ATOM   918  C CB  . THR A 1 117 ? 8.21201  23.51920 -2.81516  1.000 35.67590 ? 117 THR A CB  1 
ATOM   919  O OG1 . THR A 1 117 ? 7.34460  24.37822 -2.07188  1.000 39.71413 ? 117 THR A OG1 1 
ATOM   920  C CG2 . THR A 1 117 ? 8.18288  23.93635 -4.26633  1.000 34.13748 ? 117 THR A CG2 1 
ATOM   921  N N   . TYR A 1 118 ? 9.03818  21.07500 -0.87859  1.000 28.90985 ? 118 TYR A N   1 
ATOM   922  C CA  . TYR A 1 118 ? 9.30966  20.59556 0.46740   1.000 28.70831 ? 118 TYR A CA  1 
ATOM   923  C C   . TYR A 1 118 ? 10.69600 21.03986 0.89182   1.000 28.19790 ? 118 TYR A C   1 
ATOM   924  O O   . TYR A 1 118 ? 11.60704 21.15661 0.07618   1.000 29.78140 ? 118 TYR A O   1 
ATOM   925  C CB  . TYR A 1 118 ? 9.23563  19.07289 0.55408   1.000 30.01163 ? 118 TYR A CB  1 
ATOM   926  C CG  . TYR A 1 118 ? 7.96707  18.52657 0.01097   1.000 29.92474 ? 118 TYR A CG  1 
ATOM   927  C CD1 . TYR A 1 118 ? 7.84998  18.18997 -1.33830  1.000 31.07326 ? 118 TYR A CD1 1 
ATOM   928  C CD2 . TYR A 1 118 ? 6.85423  18.38210 0.82840   1.000 30.41307 ? 118 TYR A CD2 1 
ATOM   929  C CE1 . TYR A 1 118 ? 6.66133  17.70055 -1.84360  1.000 33.68269 ? 118 TYR A CE1 1 
ATOM   930  C CE2 . TYR A 1 118 ? 5.66372  17.89680 0.32598   1.000 32.49793 ? 118 TYR A CE2 1 
ATOM   931  C CZ  . TYR A 1 118 ? 5.57288  17.55763 -1.00561  1.000 34.15527 ? 118 TYR A CZ  1 
ATOM   932  O OH  . TYR A 1 118 ? 4.38234  17.07236 -1.48408  1.000 37.45644 ? 118 TYR A OH  1 
ATOM   933  N N   . LEU A 1 119 ? 10.85479 21.25737 2.18517   1.000 26.31412 ? 119 LEU A N   1 
ATOM   934  C CA  . LEU A 1 119 ? 12.13463 21.62187 2.77111   1.000 25.82813 ? 119 LEU A CA  1 
ATOM   935  C C   . LEU A 1 119 ? 12.59698 20.47869 3.65650   1.000 23.27703 ? 119 LEU A C   1 
ATOM   936  O O   . LEU A 1 119 ? 11.79585 19.91721 4.40287   1.000 25.47636 ? 119 LEU A O   1 
ATOM   937  C CB  . LEU A 1 119 ? 11.98683 22.90082 3.58466   1.000 29.77740 ? 119 LEU A CB  1 
ATOM   938  C CG  . LEU A 1 119 ? 13.16434 23.81971 3.82982   1.000 33.83832 ? 119 LEU A CG  1 
ATOM   939  C CD1 . LEU A 1 119 ? 13.77959 24.29523 2.50660   1.000 34.35258 ? 119 LEU A CD1 1 
ATOM   940  C CD2 . LEU A 1 119 ? 12.66496 24.99347 4.66048   1.000 36.29944 ? 119 LEU A CD2 1 
ATOM   941  N N   . ALA A 1 120 ? 13.87113 20.11482 3.55844   1.000 20.45942 ? 120 ALA A N   1 
ATOM   942  C CA  . ALA A 1 120 ? 14.41399 19.01843 4.35168   1.000 19.43339 ? 120 ALA A CA  1 
ATOM   943  C C   . ALA A 1 120 ? 15.60727 19.48485 5.17308   1.000 18.01908 ? 120 ALA A C   1 
ATOM   944  O O   . ALA A 1 120 ? 16.45153 20.24948 4.68673   1.000 19.32840 ? 120 ALA A O   1 
ATOM   945  C CB  . ALA A 1 120 ? 14.85296 17.83747 3.48787   1.000 21.89902 ? 120 ALA A CB  1 
ATOM   946  N N   . LEU A 1 121 ? 15.64034 19.04344 6.44049   1.000 19.57304 ? 121 LEU A N   1 
ATOM   947  C CA  . LEU A 1 121 ? 16.78790 19.22597 7.31852   1.000 18.77000 ? 121 LEU A CA  1 
ATOM   948  C C   . LEU A 1 121 ? 17.75711 18.04988 7.26294   1.000 18.29538 ? 121 LEU A C   1 
ATOM   949  O O   . LEU A 1 121 ? 18.98023 18.23983 7.40882   1.000 19.83714 ? 121 LEU A O   1 
ATOM   950  C CB  . LEU A 1 121 ? 16.29029 19.43403 8.75640   1.000 19.82311 ? 121 LEU A CB  1 
ATOM   951  C CG  . LEU A 1 121 ? 17.34627 19.50341 9.86785   1.000 21.44655 ? 121 LEU A CG  1 
ATOM   952  C CD1 . LEU A 1 121 ? 18.38749 20.57128 9.59536   1.000 21.98842 ? 121 LEU A CD1 1 
ATOM   953  C CD2 . LEU A 1 121 ? 16.67179 19.74832 11.24265  1.000 22.17800 ? 121 LEU A CD2 1 
ATOM   954  N N   . ASN A 1 122 ? 17.25046 16.83439 7.04541   1.000 18.10069 ? 122 ASN A N   1 
ATOM   955  C CA  . ASN A 1 122 ? 18.11844 15.67263 6.89851   1.000 17.20514 ? 122 ASN A CA  1 
ATOM   956  C C   . ASN A 1 122 ? 18.26326 15.32218 5.41899   1.000 17.06172 ? 122 ASN A C   1 
ATOM   957  O O   . ASN A 1 122 ? 19.34885 15.45201 4.83692   1.000 17.97017 ? 122 ASN A O   1 
ATOM   958  C CB  . ASN A 1 122 ? 17.55063 14.47534 7.64639   1.000 16.92053 ? 122 ASN A CB  1 
ATOM   959  C CG  . ASN A 1 122 ? 18.13578 14.29076 9.03654   1.000 18.97301 ? 122 ASN A CG  1 
ATOM   960  O OD1 . ASN A 1 122 ? 19.00093 15.05133 9.50267   1.000 20.56828 ? 122 ASN A OD1 1 
ATOM   961  N ND2 . ASN A 1 122 ? 17.67341 13.25513 9.69463   1.000 19.06629 ? 122 ASN A ND2 1 
ATOM   962  N N   . GLU A 1 123 ? 17.18609 14.85515 4.79968   1.000 16.70445 ? 123 GLU A N   1 
ATOM   963  C CA  . GLU A 1 123 ? 17.31557 14.41530 3.40961   1.000 17.41838 ? 123 GLU A CA  1 
ATOM   964  C C   . GLU A 1 123 ? 15.94337 14.27469 2.78255   1.000 17.45640 ? 123 GLU A C   1 
ATOM   965  O O   . GLU A 1 123 ? 14.91274 14.27961 3.45538   1.000 19.55340 ? 123 GLU A O   1 
ATOM   966  C CB  . GLU A 1 123 ? 18.06128 13.08106 3.30567   1.000 18.87424 ? 123 GLU A CB  1 
ATOM   967  C CG  . GLU A 1 123 ? 17.22254 11.88066 3.73148   1.000 19.56324 ? 123 GLU A CG  1 
ATOM   968  C CD  . GLU A 1 123 ? 17.09693 11.79922 5.23595   1.000 19.18457 ? 123 GLU A CD  1 
ATOM   969  O OE1 . GLU A 1 123 ? 18.15818 11.76342 5.89756   1.000 19.17730 ? 123 GLU A OE1 1 
ATOM   970  O OE2 . GLU A 1 123 ? 15.94523 11.79578 5.73913   1.000 20.93101 ? 123 GLU A OE2 1 
ATOM   971  N N   . SER A 1 124 ? 15.95572 14.13577 1.46276   1.000 18.72949 ? 124 SER A N   1 
ATOM   972  C CA  . SER A 1 124 ? 14.79597 13.74023 0.68627   1.000 18.83381 ? 124 SER A CA  1 
ATOM   973  C C   . SER A 1 124 ? 15.19466 12.50560 -0.09722  1.000 18.28853 ? 124 SER A C   1 
ATOM   974  O O   . SER A 1 124 ? 16.26597 12.48440 -0.71374  1.000 21.57571 ? 124 SER A O   1 
ATOM   975  C CB  . SER A 1 124 ? 14.34019 14.86798 -0.25241  1.000 21.85569 ? 124 SER A CB  1 
ATOM   976  O OG  . SER A 1 124 ? 13.27902 14.42401 -1.07908  1.000 25.96516 ? 124 SER A OG  1 
ATOM   977  N N   . THR A 1 125 ? 14.36890 11.46874 -0.05200  1.000 18.43057 ? 125 THR A N   1 
ATOM   978  C CA  . THR A 1 125 ? 14.67461 10.26484 -0.81594  1.000 18.92997 ? 125 THR A CA  1 
ATOM   979  C C   . THR A 1 125 ? 13.54287 9.96866  -1.77829  1.000 21.31388 ? 125 THR A C   1 
ATOM   980  O O   . THR A 1 125 ? 12.41306 10.43641 -1.61547  1.000 22.03584 ? 125 THR A O   1 
ATOM   981  C CB  . THR A 1 125 ? 14.90444 9.03921  0.07808   1.000 20.41658 ? 125 THR A CB  1 
ATOM   982  O OG1 . THR A 1 125 ? 13.65292 8.58156  0.59820   1.000 23.14974 ? 125 THR A OG1 1 
ATOM   983  C CG2 . THR A 1 125 ? 15.81308 9.39660  1.24404   1.000 22.36415 ? 125 THR A CG2 1 
ATOM   984  N N   . VAL A 1 126 ? 13.86381 9.19041  -2.80379  1.000 20.95253 ? 126 VAL A N   1 
ATOM   985  C CA  A VAL A 1 126 ? 12.86987 8.78832  -3.78144  0.700 22.66202 ? 126 VAL A CA  1 
ATOM   986  C CA  B VAL A 1 126 ? 12.90023 8.79903  -3.82674  0.300 20.87388 ? 126 VAL A CA  1 
ATOM   987  C C   . VAL A 1 126 ? 13.03688 7.30619  -4.07342  1.000 20.68787 ? 126 VAL A C   1 
ATOM   988  O O   . VAL A 1 126 ? 14.15763 6.80724  -4.24971  1.000 20.44734 ? 126 VAL A O   1 
ATOM   989  C CB  A VAL A 1 126 ? 12.96960 9.63476  -5.06475  0.700 24.38630 ? 126 VAL A CB  1 
ATOM   990  C CB  B VAL A 1 126 ? 13.10632 9.56608  -5.14779  0.300 20.03609 ? 126 VAL A CB  1 
ATOM   991  C CG1 A VAL A 1 126 ? 14.36217 9.54899  -5.64227  0.700 25.80162 ? 126 VAL A CG1 1 
ATOM   992  C CG1 B VAL A 1 126 ? 11.97335 9.24801  -6.12477  0.300 20.58586 ? 126 VAL A CG1 1 
ATOM   993  C CG2 A VAL A 1 126 ? 11.90188 9.21245  -6.07203  0.700 25.23165 ? 126 VAL A CG2 1 
ATOM   994  C CG2 B VAL A 1 126 ? 13.18799 11.05500 -4.90244  0.300 19.18246 ? 126 VAL A CG2 1 
ATOM   995  N N   . LYS A 1 127 ? 11.90630 6.61194  -4.11305  1.000 20.30751 ? 127 LYS A N   1 
ATOM   996  C CA  . LYS A 1 127 ? 11.79809 5.20073  -4.44800  1.000 23.42803 ? 127 LYS A CA  1 
ATOM   997  C C   . LYS A 1 127 ? 10.58126 5.04267  -5.35666  1.000 24.91011 ? 127 LYS A C   1 
ATOM   998  O O   . LYS A 1 127 ? 9.77182  5.96049  -5.50473  1.000 24.44415 ? 127 LYS A O   1 
ATOM   999  C CB  . LYS A 1 127 ? 11.67936 4.33895  -3.17419  1.000 26.46661 ? 127 LYS A CB  1 
ATOM   1000 C CG  . LYS A 1 127 ? 12.84952 4.55036  -2.19975  0.900 27.47175 ? 127 LYS A CG  1 
ATOM   1001 C CD  . LYS A 1 127 ? 12.67413 3.81295  -0.86048  0.800 29.61354 ? 127 LYS A CD  1 
ATOM   1002 C CE  . LYS A 1 127 ? 13.84305 4.15187  0.08981   0.700 34.02628 ? 127 LYS A CE  1 
ATOM   1003 N NZ  . LYS A 1 127 ? 13.64256 3.83891  1.53916   0.700 36.01981 ? 127 LYS A NZ  1 
ATOM   1004 N N   . SER A 1 128 ? 10.45397 3.87989  -5.98422  1.000 26.87276 ? 128 SER A N   1 
ATOM   1005 C CA  . SER A 1 128 ? 9.26699  3.60662  -6.78044  1.000 31.75677 ? 128 SER A CA  1 
ATOM   1006 C C   . SER A 1 128 ? 8.07406  3.31124  -5.87622  1.000 34.68984 ? 128 SER A C   1 
ATOM   1007 O O   . SER A 1 128 ? 8.22082  2.97591  -4.69971  1.000 37.82093 ? 128 SER A O   1 
ATOM   1008 C CB  . SER A 1 128 ? 9.50819  2.42515  -7.71272  1.000 36.44168 ? 128 SER A CB  1 
ATOM   1009 O OG  . SER A 1 128 ? 9.42461  1.22451  -6.96673  1.000 38.89342 ? 128 SER A OG  1 
ATOM   1010 N N   . SER A 1 129 ? 6.87385  3.43530  -6.44271  1.000 36.21347 ? 129 SER A N   1 
ATOM   1011 C CA  . SER A 1 129 ? 5.67070  3.16407  -5.67268  1.000 41.55451 ? 129 SER A CA  1 
ATOM   1012 C C   . SER A 1 129 ? 5.37525  1.67440  -5.73911  1.000 46.33213 ? 129 SER A C   1 
ATOM   1013 O O   . SER A 1 129 ? 4.22607  1.24579  -5.60801  1.000 47.44900 ? 129 SER A O   1 
ATOM   1014 C CB  . SER A 1 129 ? 4.49593  3.96053  -6.21687  1.000 44.75240 ? 129 SER A CB  1 
ATOM   1015 O OG  . SER A 1 129 ? 4.12475  3.45329  -7.48504  1.000 48.99010 ? 129 SER A OG  1 
ATOM   1016 N N   . GLY A 1 130 ? 6.41713  0.87894  -5.93916  1.000 50.04523 ? 130 GLY A N   1 
ATOM   1017 C CA  . GLY A 1 130 ? 6.22765  -0.51059 -6.29162  1.000 52.81337 ? 130 GLY A CA  1 
ATOM   1018 C C   . GLY A 1 130 ? 6.55834  -0.68492 -7.75680  1.000 53.86848 ? 130 GLY A C   1 
ATOM   1019 O O   . GLY A 1 130 ? 6.17350  0.14356  -8.59030  1.000 57.44630 ? 130 GLY A O   1 
ATOM   1020 N N   . GLY A 1 131 ? 7.27454  -1.75099 -8.08486  1.000 50.18746 ? 131 GLY A N   1 
ATOM   1021 C CA  . GLY A 1 131 ? 7.80620  -1.91520 -9.41516  1.000 45.68629 ? 131 GLY A CA  1 
ATOM   1022 C C   . GLY A 1 131 ? 9.14499  -1.21779 -9.52917  1.000 41.59452 ? 131 GLY A C   1 
ATOM   1023 O O   . GLY A 1 131 ? 9.53399  -0.44909 -8.64355  1.000 41.36713 ? 131 GLY A O   1 
ATOM   1024 N N   . PRO A 1 132 ? 9.88059  -1.46906 -10.61631 1.000 38.52452 ? 132 PRO A N   1 
ATOM   1025 C CA  . PRO A 1 132 ? 11.27223 -1.00856 -10.67386 1.000 36.07028 ? 132 PRO A CA  1 
ATOM   1026 C C   . PRO A 1 132 ? 11.37263 0.51100  -10.68633 1.000 34.33486 ? 132 PRO A C   1 
ATOM   1027 O O   . PRO A 1 132 ? 10.55528 1.20966  -11.29507 1.000 36.21669 ? 132 PRO A O   1 
ATOM   1028 C CB  . PRO A 1 132 ? 11.80632 -1.61782 -11.97818 1.000 36.39486 ? 132 PRO A CB  1 
ATOM   1029 C CG  . PRO A 1 132 ? 10.60007 -1.93380 -12.78436 1.000 38.09800 ? 132 PRO A CG  1 
ATOM   1030 C CD  . PRO A 1 132 ? 9.48935  -2.22808 -11.81831 1.000 39.43208 ? 132 PRO A CD  1 
ATOM   1031 N N   . PHE A 1 133 ? 12.41015 1.01050  -10.02341 1.000 30.00783 ? 133 PHE A N   1 
ATOM   1032 C CA  . PHE A 1 133 ? 12.71615 2.43423  -9.98110  1.000 26.78496 ? 133 PHE A CA  1 
ATOM   1033 C C   . PHE A 1 133 ? 13.72916 2.74413  -11.07264 1.000 24.65836 ? 133 PHE A C   1 
ATOM   1034 O O   . PHE A 1 133 ? 14.84286 2.21959  -11.04546 1.000 24.89366 ? 133 PHE A O   1 
ATOM   1035 C CB  . PHE A 1 133 ? 13.27465 2.80457  -8.60931  1.000 24.58921 ? 133 PHE A CB  1 
ATOM   1036 C CG  . PHE A 1 133 ? 13.69579 4.24442  -8.47397  1.000 23.37376 ? 133 PHE A CG  1 
ATOM   1037 C CD1 . PHE A 1 133 ? 12.75350 5.25354  -8.36874  1.000 24.37082 ? 133 PHE A CD1 1 
ATOM   1038 C CD2 . PHE A 1 133 ? 15.03979 4.58460  -8.42625  1.000 24.84129 ? 133 PHE A CD2 1 
ATOM   1039 C CE1 . PHE A 1 133 ? 13.14590 6.57884  -8.22329  1.000 26.03101 ? 133 PHE A CE1 1 
ATOM   1040 C CE2 . PHE A 1 133 ? 15.43871 5.90828  -8.27758  1.000 24.93217 ? 133 PHE A CE2 1 
ATOM   1041 C CZ  . PHE A 1 133 ? 14.49040 6.90575  -8.17716  1.000 24.97304 ? 133 PHE A CZ  1 
ATOM   1042 N N   . VAL A 1 134 ? 13.34329 3.59505  -12.02308 1.000 23.87961 ? 134 VAL A N   1 
ATOM   1043 C CA  . VAL A 1 134 ? 14.20679 4.00063  -13.12828 1.000 24.02197 ? 134 VAL A CA  1 
ATOM   1044 C C   . VAL A 1 134 ? 13.98657 5.48572  -13.35840 1.000 23.61709 ? 134 VAL A C   1 
ATOM   1045 O O   . VAL A 1 134 ? 12.86364 5.90637  -13.65103 1.000 27.79144 ? 134 VAL A O   1 
ATOM   1046 C CB  . VAL A 1 134 ? 13.91254 3.22200  -14.42310 1.000 27.22680 ? 134 VAL A CB  1 
ATOM   1047 C CG1 . VAL A 1 134 ? 14.93762 3.57333  -15.50107 1.000 27.17057 ? 134 VAL A CG1 1 
ATOM   1048 C CG2 . VAL A 1 134 ? 13.87685 1.73549  -14.16102 1.000 28.42499 ? 134 VAL A CG2 1 
ATOM   1049 N N   . VAL A 1 135 ? 15.04330 6.28600  -13.22015 1.000 22.87006 ? 135 VAL A N   1 
ATOM   1050 C CA  . VAL A 1 135 ? 14.93899 7.71078  -13.50593 1.000 21.88942 ? 135 VAL A CA  1 
ATOM   1051 C C   . VAL A 1 135 ? 16.15910 8.15516  -14.28606 1.000 22.50070 ? 135 VAL A C   1 
ATOM   1052 O O   . VAL A 1 135 ? 17.25756 7.60909  -14.12863 1.000 23.72040 ? 135 VAL A O   1 
ATOM   1053 C CB  . VAL A 1 135 ? 14.80361 8.56291  -12.23401 1.000 22.86225 ? 135 VAL A CB  1 
ATOM   1054 C CG1 . VAL A 1 135 ? 13.48196 8.28094  -11.55477 1.000 25.98846 ? 135 VAL A CG1 1 
ATOM   1055 C CG2 . VAL A 1 135 ? 15.99362 8.31271  -11.32553 1.000 25.03269 ? 135 VAL A CG2 1 
ATOM   1056 N N   . ASP A 1 136 ? 15.95788 9.15155  -15.14564 1.000 21.39404 ? 136 ASP A N   1 
ATOM   1057 C CA  . ASP A 1 136 ? 17.08541 9.87377  -15.71247 1.000 22.30891 ? 136 ASP A CA  1 
ATOM   1058 C C   . ASP A 1 136 ? 17.51735 10.96816 -14.74851 1.000 21.23125 ? 136 ASP A C   1 
ATOM   1059 O O   . ASP A 1 136 ? 16.68143 11.71616 -14.22683 1.000 22.91424 ? 136 ASP A O   1 
ATOM   1060 C CB  . ASP A 1 136 ? 16.71606 10.47364 -17.06730 1.000 24.79502 ? 136 ASP A CB  1 
ATOM   1061 C CG  . ASP A 1 136 ? 16.73554 9.44854  -18.16348 1.000 28.83094 ? 136 ASP A CG  1 
ATOM   1062 O OD1 . ASP A 1 136 ? 17.56161 8.51184  -18.06539 1.000 31.81807 ? 136 ASP A OD1 1 
ATOM   1063 O OD2 . ASP A 1 136 ? 15.93326 9.58033  -19.11488 1.000 30.86339 ? 136 ASP A OD2 1 
ATOM   1064 N N   . VAL A 1 137 ? 18.81722 11.04925 -14.49903 1.000 19.52406 ? 137 VAL A N   1 
ATOM   1065 C CA  . VAL A 1 137 ? 19.37970 12.04854 -13.59735 1.000 20.36757 ? 137 VAL A CA  1 
ATOM   1066 C C   . VAL A 1 137 ? 19.96744 13.15859 -14.45253 1.000 20.57513 ? 137 VAL A C   1 
ATOM   1067 O O   . VAL A 1 137 ? 20.87675 12.91556 -15.25580 1.000 22.22991 ? 137 VAL A O   1 
ATOM   1068 C CB  . VAL A 1 137 ? 20.45049 11.43525 -12.68621 1.000 20.21933 ? 137 VAL A CB  1 
ATOM   1069 C CG1 . VAL A 1 137 ? 21.02137 12.49972 -11.74958 1.000 23.15039 ? 137 VAL A CG1 1 
ATOM   1070 C CG2 . VAL A 1 137 ? 19.88141 10.23881 -11.92906 1.000 23.47190 ? 137 VAL A CG2 1 
ATOM   1071 N N   . VAL A 1 138 ? 19.42872 14.36469 -14.31097 1.000 21.02621 ? 138 VAL A N   1 
ATOM   1072 C CA  . VAL A 1 138 ? 19.79551 15.51326 -15.13101 1.000 22.08053 ? 138 VAL A CA  1 
ATOM   1073 C C   . VAL A 1 138 ? 20.37316 16.57663 -14.20557 1.000 22.32243 ? 138 VAL A C   1 
ATOM   1074 O O   . VAL A 1 138 ? 19.70713 17.02129 -13.25712 1.000 25.78414 ? 138 VAL A O   1 
ATOM   1075 C CB  . VAL A 1 138 ? 18.59159 16.04826 -15.91536 1.000 23.76949 ? 138 VAL A CB  1 
ATOM   1076 C CG1 . VAL A 1 138 ? 19.00056 17.21850 -16.77908 1.000 26.11471 ? 138 VAL A CG1 1 
ATOM   1077 C CG2 . VAL A 1 138 ? 17.97589 14.92673 -16.75685 1.000 24.75590 ? 138 VAL A CG2 1 
ATOM   1078 N N   . ILE A 1 139 ? 21.61584 16.96792 -14.46098 1.000 20.38284 ? 139 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 139 ? 22.32763 17.92692 -13.61904 1.000 20.92275 ? 139 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 139 ? 22.47867 19.20373 -14.41885 1.000 23.24652 ? 139 ILE A C   1 
ATOM   1081 O O   . ILE A 1 139 ? 23.14112 19.20498 -15.45975 1.000 23.91995 ? 139 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 139 ? 23.69860 17.39988 -13.17454 1.000 21.03282 ? 139 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 139 ? 23.55316 16.06317 -12.43420 1.000 21.71258 ? 139 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 139 ? 24.37045 18.41207 -12.25408 1.000 24.47985 ? 139 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 139 ? 24.87141 15.41057 -12.13381 1.000 23.80612 ? 139 ILE A CD1 1 
ATOM   1086 N N   . ASN A 1 140 ? 21.88108 20.29203 -13.94213 1.000 24.34345 ? 140 ASN A N   1 
ATOM   1087 C CA  . ASN A 1 140 ? 21.91363 21.56001 -14.67555 1.000 24.85942 ? 140 ASN A CA  1 
ATOM   1088 C C   . ASN A 1 140 ? 21.62225 21.33408 -16.15329 1.000 28.27451 ? 140 ASN A C   1 
ATOM   1089 O O   . ASN A 1 140 ? 22.34001 21.81180 -17.03315 1.000 31.35329 ? 140 ASN A O   1 
ATOM   1090 C CB  . ASN A 1 140 ? 23.25562 22.26877 -14.50374 1.000 24.73374 ? 140 ASN A CB  1 
ATOM   1091 C CG  . ASN A 1 140 ? 23.59773 22.47480 -13.07178 1.000 25.88253 ? 140 ASN A CG  1 
ATOM   1092 O OD1 . ASN A 1 140 ? 22.72315 22.78947 -12.27988 1.000 27.28442 ? 140 ASN A OD1 1 
ATOM   1093 N ND2 . ASN A 1 140 ? 24.87078 22.29468 -12.71946 1.000 27.66336 ? 140 ASN A ND2 1 
ATOM   1094 N N   . ASP A 1 141 ? 20.57330 20.56438 -16.42170 1.000 29.07762 ? 141 ASP A N   1 
ATOM   1095 C CA  . ASP A 1 141 ? 20.08901 20.27793 -17.77590 1.000 29.97721 ? 141 ASP A CA  1 
ATOM   1096 C C   . ASP A 1 141 ? 20.97868 19.32336 -18.56549 1.000 31.13428 ? 141 ASP A C   1 
ATOM   1097 O O   . ASP A 1 141 ? 20.66821 19.05204 -19.73863 1.000 35.89294 ? 141 ASP A O   1 
ATOM   1098 C CB  . ASP A 1 141 ? 19.90093 21.55548 -18.60542 1.000 35.30443 ? 141 ASP A CB  1 
ATOM   1099 C CG  . ASP A 1 141 ? 18.89893 22.50575 -17.99318 0.700 38.83516 ? 141 ASP A CG  1 
ATOM   1100 O OD1 . ASP A 1 141 ? 18.01133 22.04126 -17.25192 0.700 39.20767 ? 141 ASP A OD1 1 
ATOM   1101 O OD2 . ASP A 1 141 ? 18.99002 23.72185 -18.26573 0.700 41.99559 ? 141 ASP A OD2 1 
ATOM   1102 N N   . ILE A 1 142 ? 22.07138 18.83332 -17.98921 1.000 28.53016 ? 142 ILE A N   1 
ATOM   1103 C CA  . ILE A 1 142 ? 22.97379 17.85936 -18.60295 1.000 27.35650 ? 142 ILE A CA  1 
ATOM   1104 C C   . ILE A 1 142 ? 22.48422 16.46688 -18.22325 1.000 24.42291 ? 142 ILE A C   1 
ATOM   1105 O O   . ILE A 1 142 ? 22.42036 16.15283 -17.03404 1.000 23.89697 ? 142 ILE A O   1 
ATOM   1106 C CB  . ILE A 1 142 ? 24.40610 18.05403 -18.07376 1.000 30.30670 ? 142 ILE A CB  1 
ATOM   1107 C CG1 . ILE A 1 142 ? 25.00654 19.39598 -18.49265 0.600 32.29981 ? 142 ILE A CG1 1 
ATOM   1108 C CG2 . ILE A 1 142 ? 25.29758 16.85479 -18.42487 0.600 28.52691 ? 142 ILE A CG2 1 
ATOM   1109 C CD1 . ILE A 1 142 ? 26.18225 19.79397 -17.61252 0.600 33.42219 ? 142 ILE A CD1 1 
ATOM   1110 N N   . HIS A 1 143 ? 22.13555 15.62955 -19.20006 1.000 23.82577 ? 143 HIS A N   1 
ATOM   1111 C CA  A HIS A 1 143 ? 21.76851 14.24885 -18.89971 0.700 23.10977 ? 143 HIS A CA  1 
ATOM   1112 C CA  B HIS A 1 143 ? 21.76965 14.24368 -18.89650 0.300 23.42995 ? 143 HIS A CA  1 
ATOM   1113 C C   . HIS A 1 143 ? 22.99784 13.51480 -18.38032 1.000 23.25561 ? 143 HIS A C   1 
ATOM   1114 O O   . HIS A 1 143 ? 23.97477 13.32348 -19.11033 1.000 25.18231 ? 143 HIS A O   1 
ATOM   1115 C CB  A HIS A 1 143 ? 21.17059 13.58913 -20.14608 0.700 26.26994 ? 143 HIS A CB  1 
ATOM   1116 C CB  B HIS A 1 143 ? 21.20349 13.49439 -20.10208 0.300 24.48630 ? 143 HIS A CB  1 
ATOM   1117 C CG  A HIS A 1 143 ? 19.78250 14.05672 -20.43966 0.700 30.08896 ? 143 HIS A CG  1 
ATOM   1118 C CG  B HIS A 1 143 ? 20.96687 12.04020 -19.81432 0.300 25.75533 ? 143 HIS A CG  1 
ATOM   1119 N ND1 A HIS A 1 143 ? 18.78392 13.21911 -20.89009 0.700 33.14747 ? 143 HIS A ND1 1 
ATOM   1120 N ND1 B HIS A 1 143 ? 21.99111 11.11730 -19.74621 0.300 26.39549 ? 143 HIS A ND1 1 
ATOM   1121 C CD2 A HIS A 1 143 ? 19.22160 15.28525 -20.33273 0.700 30.79067 ? 143 HIS A CD2 1 
ATOM   1122 C CD2 B HIS A 1 143 ? 19.83487 11.36425 -19.49898 0.300 26.65952 ? 143 HIS A CD2 1 
ATOM   1123 C CE1 A HIS A 1 143 ? 17.66952 13.91146 -21.04741 0.700 31.22651 ? 143 HIS A CE1 1 
ATOM   1124 C CE1 B HIS A 1 143 ? 21.49656 9.93118  -19.43930 0.300 25.83239 ? 143 HIS A CE1 1 
ATOM   1125 N NE2 A HIS A 1 143 ? 17.90807 15.16686 -20.71303 0.700 28.62456 ? 143 HIS A NE2 1 
ATOM   1126 N NE2 B HIS A 1 143 ? 20.19113 10.05407 -19.27872 0.300 26.60632 ? 143 HIS A NE2 1 
ATOM   1127 N N   . PHE A 1 144 ? 22.95954 13.10971 -17.11209 1.000 20.69850 ? 144 PHE A N   1 
ATOM   1128 C CA  . PHE A 1 144 ? 24.14530 12.55325 -16.47424 1.000 20.84208 ? 144 PHE A CA  1 
ATOM   1129 C C   . PHE A 1 144 ? 24.14697 11.03200 -16.41235 1.000 20.87099 ? 144 PHE A C   1 
ATOM   1130 O O   . PHE A 1 144 ? 25.16800 10.40260 -16.71686 1.000 21.28000 ? 144 PHE A O   1 
ATOM   1131 C CB  . PHE A 1 144 ? 24.28408 13.13639 -15.06265 1.000 19.35284 ? 144 PHE A CB  1 
ATOM   1132 C CG  . PHE A 1 144 ? 25.45049 12.59594 -14.31555 1.000 20.02957 ? 144 PHE A CG  1 
ATOM   1133 C CD1 . PHE A 1 144 ? 26.72784 13.06994 -14.57273 1.000 19.88954 ? 144 PHE A CD1 1 
ATOM   1134 C CD2 . PHE A 1 144 ? 25.28161 11.60494 -13.35616 1.000 20.28343 ? 144 PHE A CD2 1 
ATOM   1135 C CE1 . PHE A 1 144 ? 27.81944 12.56116 -13.90431 1.000 22.02733 ? 144 PHE A CE1 1 
ATOM   1136 C CE2 . PHE A 1 144 ? 26.38828 11.09249 -12.65780 1.000 20.11469 ? 144 PHE A CE2 1 
ATOM   1137 C CZ  . PHE A 1 144 ? 27.64840 11.56984 -12.93205 1.000 21.86605 ? 144 PHE A CZ  1 
ATOM   1138 N N   . GLU A 1 145 ? 23.02812 10.41522 -16.03237 1.000 21.09907 ? 145 GLU A N   1 
ATOM   1139 C CA  . GLU A 1 145 ? 22.98075 8.95873  -16.00092 1.000 19.43742 ? 145 GLU A CA  1 
ATOM   1140 C C   . GLU A 1 145 ? 21.52480 8.54508  -15.98907 1.000 20.25915 ? 145 GLU A C   1 
ATOM   1141 O O   . GLU A 1 145 ? 20.65142 9.33791  -15.63735 1.000 22.67594 ? 145 GLU A O   1 
ATOM   1142 C CB  . GLU A 1 145 ? 23.68986 8.39233  -14.76040 1.000 21.64109 ? 145 GLU A CB  1 
ATOM   1143 C CG  . GLU A 1 145 ? 22.89244 8.70543  -13.47448 1.000 21.67436 ? 145 GLU A CG  1 
ATOM   1144 C CD  . GLU A 1 145 ? 23.61992 8.31164  -12.21299 1.000 22.88887 ? 145 GLU A CD  1 
ATOM   1145 O OE1 . GLU A 1 145 ? 24.74751 7.80575  -12.29991 1.000 22.78007 ? 145 GLU A OE1 1 
ATOM   1146 O OE2 . GLU A 1 145 ? 23.06640 8.54413  -11.11379 1.000 25.59805 ? 145 GLU A OE2 1 
ATOM   1147 N N   . ARG A 1 146 ? 21.27511 7.28861  -16.34092 1.000 20.30471 ? 146 ARG A N   1 
ATOM   1148 C CA  . ARG A 1 146 ? 19.98182 6.66246  -16.10050 1.000 19.75948 ? 146 ARG A CA  1 
ATOM   1149 C C   . ARG A 1 146 ? 20.15927 5.72636  -14.91947 1.000 20.28192 ? 146 ARG A C   1 
ATOM   1150 O O   . ARG A 1 146 ? 20.93378 4.76728  -14.99284 1.000 24.27655 ? 146 ARG A O   1 
ATOM   1151 C CB  . ARG A 1 146 ? 19.45377 5.90295  -17.32113 1.000 22.56702 ? 146 ARG A CB  1 
ATOM   1152 C CG  . ARG A 1 146 ? 18.12823 5.18510  -17.04711 1.000 23.72852 ? 146 ARG A CG  1 
ATOM   1153 C CD  . ARG A 1 146 ? 17.44504 4.76748  -18.32395 1.000 25.57864 ? 146 ARG A CD  1 
ATOM   1154 N NE  . ARG A 1 146 ? 16.94567 5.93810  -19.01692 1.000 27.33864 ? 146 ARG A NE  1 
ATOM   1155 C CZ  . ARG A 1 146 ? 16.27777 5.86654  -20.15822 1.000 31.32258 ? 146 ARG A CZ  1 
ATOM   1156 N NH1 . ARG A 1 146 ? 16.03645 4.70122  -20.73438 1.000 34.45481 ? 146 ARG A NH1 1 
ATOM   1157 N NH2 . ARG A 1 146 ? 15.83522 6.98492  -20.72634 1.000 33.28622 ? 146 ARG A NH2 1 
ATOM   1158 N N   . PHE A 1 147 ? 19.44875 6.00513  -13.83993 1.000 19.95632 ? 147 PHE A N   1 
ATOM   1159 C CA  . PHE A 1 147 ? 19.59774 5.24716  -12.60615 1.000 20.08041 ? 147 PHE A CA  1 
ATOM   1160 C C   . PHE A 1 147 ? 18.53367 4.16675  -12.54493 1.000 19.79611 ? 147 PHE A C   1 
ATOM   1161 O O   . PHE A 1 147 ? 17.34522 4.45695  -12.66570 1.000 20.80198 ? 147 PHE A O   1 
ATOM   1162 C CB  . PHE A 1 147 ? 19.46936 6.13910  -11.37221 1.000 18.90133 ? 147 PHE A CB  1 
ATOM   1163 C CG  . PHE A 1 147 ? 19.67127 5.38327  -10.07863 1.000 19.44866 ? 147 PHE A CG  1 
ATOM   1164 C CD1 . PHE A 1 147 ? 18.60315 4.74216  -9.45737  1.000 20.83816 ? 147 PHE A CD1 1 
ATOM   1165 C CD2 . PHE A 1 147 ? 20.93053 5.25131  -9.53635  1.000 19.93993 ? 147 PHE A CD2 1 
ATOM   1166 C CE1 . PHE A 1 147 ? 18.78712 4.01928  -8.28200  1.000 19.85478 ? 147 PHE A CE1 1 
ATOM   1167 C CE2 . PHE A 1 147 ? 21.12197 4.54164  -8.35161  1.000 20.92850 ? 147 PHE A CE2 1 
ATOM   1168 C CZ  . PHE A 1 147 ? 20.05903 3.91579  -7.74867  1.000 20.09146 ? 147 PHE A CZ  1 
ATOM   1169 N N   . ARG A 1 148 ? 18.96176 2.93177  -12.33641 1.000 20.60790 ? 148 ARG A N   1 
ATOM   1170 C CA  . ARG A 1 148 ? 18.06388 1.82461  -12.07675 1.000 21.72150 ? 148 ARG A CA  1 
ATOM   1171 C C   . ARG A 1 148 ? 18.51478 1.15823  -10.78607 1.000 21.30153 ? 148 ARG A C   1 
ATOM   1172 O O   . ARG A 1 148 ? 19.69033 0.81660  -10.64491 1.000 23.63776 ? 148 ARG A O   1 
ATOM   1173 C CB  . ARG A 1 148 ? 18.06403 0.82659  -13.23419 1.000 26.19762 ? 148 ARG A CB  1 
ATOM   1174 C CG  . ARG A 1 148 ? 16.98509 -0.23631 -13.11302 0.900 31.93599 ? 148 ARG A CG  1 
ATOM   1175 C CD  . ARG A 1 148 ? 16.90993 -1.13346 -14.33768 0.800 35.47933 ? 148 ARG A CD  1 
ATOM   1176 N NE  . ARG A 1 148 ? 15.92860 -2.19575 -14.14929 0.700 37.43008 ? 148 ARG A NE  1 
ATOM   1177 C CZ  . ARG A 1 148 ? 14.68662 -2.16366 -14.61013 0.700 39.89943 ? 148 ARG A CZ  1 
ATOM   1178 N NH1 . ARG A 1 148 ? 14.24805 -1.15770 -15.35229 0.700 40.43531 ? 148 ARG A NH1 1 
ATOM   1179 N NH2 . ARG A 1 148 ? 13.86901 -3.17701 -14.33860 0.700 42.34067 ? 148 ARG A NH2 1 
ATOM   1180 N N   . GLY A 1 149 ? 17.59174 0.97182  -9.85272  1.000 22.60678 ? 149 GLY A N   1 
ATOM   1181 C CA  . GLY A 1 149 ? 17.99256 0.45955  -8.54686  1.000 22.36596 ? 149 GLY A CA  1 
ATOM   1182 C C   . GLY A 1 149 ? 16.87477 0.62222  -7.54830  1.000 21.15458 ? 149 GLY A C   1 
ATOM   1183 O O   . GLY A 1 149 ? 15.70166 0.67568  -7.91924  1.000 23.80240 ? 149 GLY A O   1 
ATOM   1184 N N   . ASP A 1 150 ? 17.24910 0.73432  -6.27211  1.000 18.46705 ? 150 ASP A N   1 
ATOM   1185 C CA  . ASP A 1 150 ? 16.20442 0.84069  -5.25795  1.000 20.45203 ? 150 ASP A CA  1 
ATOM   1186 C C   . ASP A 1 150 ? 15.72848 2.27065  -5.04242  1.000 21.07070 ? 150 ASP A C   1 
ATOM   1187 O O   . ASP A 1 150 ? 14.57006 2.47363  -4.65720  1.000 23.02216 ? 150 ASP A O   1 
ATOM   1188 C CB  . ASP A 1 150 ? 16.68962 0.28173  -3.91619  1.000 19.26664 ? 150 ASP A CB  1 
ATOM   1189 C CG  . ASP A 1 150 ? 16.73847 -1.22325 -3.89071  1.000 22.74995 ? 150 ASP A CG  1 
ATOM   1190 O OD1 . ASP A 1 150 ? 16.32957 -1.86037 -4.88456  1.000 25.38967 ? 150 ASP A OD1 1 
ATOM   1191 O OD2 . ASP A 1 150 ? 17.19400 -1.77562 -2.86961  1.000 24.19876 ? 150 ASP A OD2 1 
ATOM   1192 N N   . GLY A 1 151 ? 16.58978 3.26118  -5.22704  1.000 18.43633 ? 151 GLY A N   1 
ATOM   1193 C CA  . GLY A 1 151 ? 16.19714 4.62893  -4.95139  1.000 18.54083 ? 151 GLY A CA  1 
ATOM   1194 C C   . GLY A 1 151 ? 17.41345 5.51952  -4.84851  1.000 16.73678 ? 151 GLY A C   1 
ATOM   1195 O O   . GLY A 1 151 ? 18.54909 5.08730  -5.04828  1.000 18.02787 ? 151 GLY A O   1 
ATOM   1196 N N   . LEU A 1 152 ? 17.14362 6.78700  -4.56181  1.000 17.65663 ? 152 LEU A N   1 
ATOM   1197 C CA  . LEU A 1 152 ? 18.16938 7.81423  -4.43140  1.000 16.79835 ? 152 LEU A CA  1 
ATOM   1198 C C   . LEU A 1 152 ? 17.90111 8.62901  -3.17284  1.000 17.42923 ? 152 LEU A C   1 
ATOM   1199 O O   . LEU A 1 152 ? 16.75494 8.78140  -2.75571  1.000 19.28180 ? 152 LEU A O   1 
ATOM   1200 C CB  . LEU A 1 152 ? 18.17998 8.73423  -5.64723  1.000 19.24929 ? 152 LEU A CB  1 
ATOM   1201 C CG  . LEU A 1 152 ? 18.68123 8.09154  -6.94480  1.000 20.15344 ? 152 LEU A CG  1 
ATOM   1202 C CD1 . LEU A 1 152 ? 18.29140 8.95420  -8.15390  1.000 21.49988 ? 152 LEU A CD1 1 
ATOM   1203 C CD2 . LEU A 1 152 ? 20.18546 7.95793  -6.87894  1.000 19.91743 ? 152 LEU A CD2 1 
ATOM   1204 N N   . CYS A 1 153 ? 18.96875 9.16301  -2.58867  1.000 16.97284 ? 153 CYS A N   1 
ATOM   1205 C CA  . CYS A 1 153 ? 18.89820 9.96414  -1.37443  1.000 16.68295 ? 153 CYS A CA  1 
ATOM   1206 C C   . CYS A 1 153 ? 19.66386 11.25633 -1.60311  1.000 17.00607 ? 153 CYS A C   1 
ATOM   1207 O O   . CYS A 1 153 ? 20.83827 11.21896 -1.99068  1.000 16.81125 ? 153 CYS A O   1 
ATOM   1208 C CB  . CYS A 1 153 ? 19.51112 9.18720  -0.21282  1.000 16.88690 ? 153 CYS A CB  1 
ATOM   1209 S SG  . CYS A 1 153 ? 19.63523 10.10854 1.36441   1.000 18.94337 ? 153 CYS A SG  1 
ATOM   1210 N N   . MET A 1 154 ? 19.01547 12.39411 -1.36415  1.000 15.78023 ? 154 MET A N   1 
ATOM   1211 C CA  . MET A 1 154 ? 19.68074 13.68753 -1.43730  1.000 16.39945 ? 154 MET A CA  1 
ATOM   1212 C C   . MET A 1 154 ? 19.70466 14.28770 -0.04113  1.000 17.28987 ? 154 MET A C   1 
ATOM   1213 O O   . MET A 1 154 ? 18.64561 14.54766 0.53150   1.000 17.23386 ? 154 MET A O   1 
ATOM   1214 C CB  . MET A 1 154 ? 18.98215 14.62707 -2.41918  1.000 15.83432 ? 154 MET A CB  1 
ATOM   1215 C CG  . MET A 1 154 ? 19.73404 15.92737 -2.61788  1.000 16.74142 ? 154 MET A CG  1 
ATOM   1216 S SD  . MET A 1 154 ? 21.30082 15.71894 -3.53445  1.000 18.50131 ? 154 MET A SD  1 
ATOM   1217 C CE  . MET A 1 154 ? 20.73046 15.99659 -5.24330  1.000 18.56754 ? 154 MET A CE  1 
ATOM   1218 N N   . SER A 1 155 ? 20.90661 14.53416 0.47108   1.000 16.46566 ? 155 SER A N   1 
ATOM   1219 C CA  . SER A 1 155 ? 21.11779 14.89467 1.87237   1.000 15.57214 ? 155 SER A CA  1 
ATOM   1220 C C   . SER A 1 155 ? 21.62389 16.32597 1.99978   1.000 17.41923 ? 155 SER A C   1 
ATOM   1221 O O   . SER A 1 155 ? 22.37183 16.81493 1.14893   1.000 18.50374 ? 155 SER A O   1 
ATOM   1222 C CB  . SER A 1 155 ? 22.10946 13.91577 2.49824   1.000 18.24370 ? 155 SER A CB  1 
ATOM   1223 O OG  . SER A 1 155 ? 22.41656 14.25157 3.84718   1.000 20.59740 ? 155 SER A OG  1 
ATOM   1224 N N   . THR A 1 156 ? 21.21779 16.99415 3.08514   1.000 17.16504 ? 156 THR A N   1 
ATOM   1225 C CA  . THR A 1 156 ? 21.85369 18.22381 3.52330   1.000 17.14162 ? 156 THR A CA  1 
ATOM   1226 C C   . THR A 1 156 ? 23.17821 17.91114 4.21169   1.000 17.90673 ? 156 THR A C   1 
ATOM   1227 O O   . THR A 1 156 ? 23.47274 16.76245 4.52525   1.000 19.87338 ? 156 THR A O   1 
ATOM   1228 C CB  . THR A 1 156 ? 20.97265 18.93709 4.54215   1.000 18.98058 ? 156 THR A CB  1 
ATOM   1229 O OG1 . THR A 1 156 ? 20.99324 18.15935 5.73936   1.000 19.75173 ? 156 THR A OG1 1 
ATOM   1230 C CG2 . THR A 1 156 ? 19.53499 19.09066 4.06712   1.000 20.55903 ? 156 THR A CG2 1 
ATOM   1231 N N   . PRO A 1 157 ? 23.99994 18.92629 4.48496   1.000 18.33475 ? 157 PRO A N   1 
ATOM   1232 C CA  . PRO A 1 157 ? 25.22292 18.66348 5.27411   1.000 18.84641 ? 157 PRO A CA  1 
ATOM   1233 C C   . PRO A 1 157 ? 24.94155 18.02246 6.62871   1.000 19.65867 ? 157 PRO A C   1 
ATOM   1234 O O   . PRO A 1 157 ? 25.55415 17.00084 6.95911   1.000 20.06263 ? 157 PRO A O   1 
ATOM   1235 C CB  . PRO A 1 157 ? 25.85390 20.06141 5.39373   1.000 19.39613 ? 157 PRO A CB  1 
ATOM   1236 C CG  . PRO A 1 157 ? 25.34944 20.78069 4.16655   1.000 21.63872 ? 157 PRO A CG  1 
ATOM   1237 C CD  . PRO A 1 157 ? 23.92003 20.33599 4.07103   1.000 19.44575 ? 157 PRO A CD  1 
ATOM   1238 N N   . SER A 1 158 ? 24.01883 18.57684 7.42107   1.000 20.03779 ? 158 SER A N   1 
ATOM   1239 C CA  . SER A 1 158 ? 23.74429 17.95166 8.70999   1.000 18.53863 ? 158 SER A CA  1 
ATOM   1240 C C   . SER A 1 158 ? 23.06430 16.59800 8.55101   1.000 17.45825 ? 158 SER A C   1 
ATOM   1241 O O   . SER A 1 158 ? 23.15154 15.75760 9.45785   1.000 19.19652 ? 158 SER A O   1 
ATOM   1242 C CB  . SER A 1 158 ? 22.92467 18.89678 9.61035   1.000 20.02269 ? 158 SER A CB  1 
ATOM   1243 O OG  . SER A 1 158 ? 21.65150 19.23207 9.09720   1.000 21.26571 ? 158 SER A OG  1 
ATOM   1244 N N   . GLY A 1 159 ? 22.39983 16.35848 7.42164   1.000 15.99695 ? 159 GLY A N   1 
ATOM   1245 C CA  . GLY A 1 159 ? 21.88219 15.03471 7.16665   1.000 17.08793 ? 159 GLY A CA  1 
ATOM   1246 C C   . GLY A 1 159 ? 22.92542 14.01869 6.77808   1.000 17.16955 ? 159 GLY A C   1 
ATOM   1247 O O   . GLY A 1 159 ? 22.59599 12.83196 6.68663   1.000 17.73411 ? 159 GLY A O   1 
ATOM   1248 N N   . THR A 1 160 ? 24.17478 14.43551 6.53435   1.000 16.29862 ? 160 THR A N   1 
ATOM   1249 C CA  . THR A 1 160 ? 25.10863 13.44858 6.00484   1.000 16.79893 ? 160 THR A CA  1 
ATOM   1250 C C   . THR A 1 160 ? 25.45855 12.39597 7.03093   1.000 15.92510 ? 160 THR A C   1 
ATOM   1251 O O   . THR A 1 160 ? 25.89301 11.31131 6.64663   1.000 17.47734 ? 160 THR A O   1 
ATOM   1252 C CB  . THR A 1 160 ? 26.40270 14.07186 5.46121   1.000 16.98215 ? 160 THR A CB  1 
ATOM   1253 O OG1 . THR A 1 160 ? 27.04609 14.87633 6.46004   1.000 17.51674 ? 160 THR A OG1 1 
ATOM   1254 C CG2 . THR A 1 160 ? 26.10665 14.91198 4.20682   1.000 17.90388 ? 160 THR A CG2 1 
ATOM   1255 N N   . THR A 1 161 ? 25.23575 12.66505 8.31804   1.000 17.43043 ? 161 THR A N   1 
ATOM   1256 C CA  . THR A 1 161 ? 25.46064 11.66736 9.35005   1.000 17.58472 ? 161 THR A CA  1 
ATOM   1257 C C   . THR A 1 161 ? 24.25848 10.75828 9.55953   1.000 17.18776 ? 161 THR A C   1 
ATOM   1258 O O   . THR A 1 161 ? 24.30536 9.89641  10.43968  1.000 19.55382 ? 161 THR A O   1 
ATOM   1259 C CB  . THR A 1 161 ? 25.82785 12.36447 10.67806  1.000 17.46909 ? 161 THR A CB  1 
ATOM   1260 O OG1 . THR A 1 161 ? 24.96758 13.49549 10.85509  1.000 19.07867 ? 161 THR A OG1 1 
ATOM   1261 C CG2 . THR A 1 161 ? 27.28367 12.84841 10.65708  1.000 20.99451 ? 161 THR A CG2 1 
ATOM   1262 N N   . ALA A 1 162 ? 23.20918 10.89667 8.75822   1.000 18.38477 ? 162 ALA A N   1 
ATOM   1263 C CA  . ALA A 1 162 ? 21.97189 10.13258 8.91652   1.000 18.49309 ? 162 ALA A CA  1 
ATOM   1264 C C   . ALA A 1 162 ? 21.88399 9.08521  7.80315   1.000 19.47920 ? 162 ALA A C   1 
ATOM   1265 O O   . ALA A 1 162 ? 22.84755 8.33406  7.62106   1.000 20.21336 ? 162 ALA A O   1 
ATOM   1266 C CB  . ALA A 1 162 ? 20.77740 11.08507 8.97127   1.000 19.64415 ? 162 ALA A CB  1 
ATOM   1267 N N   . TYR A 1 163 ? 20.77339 8.99341  7.07215   1.000 18.31673 ? 163 TYR A N   1 
ATOM   1268 C CA  . TYR A 1 163 ? 20.61931 7.98289  6.02271   1.000 16.10038 ? 163 TYR A CA  1 
ATOM   1269 C C   . TYR A 1 163 ? 21.79685 7.99532  5.04984   1.000 15.40029 ? 163 TYR A C   1 
ATOM   1270 O O   . TYR A 1 163 ? 22.32527 6.93716  4.67435   1.000 17.03411 ? 163 TYR A O   1 
ATOM   1271 C CB  . TYR A 1 163 ? 19.31134 8.27304  5.29758   1.000 15.63324 ? 163 TYR A CB  1 
ATOM   1272 C CG  . TYR A 1 163 ? 18.60419 7.13584  4.61199   1.000 16.77451 ? 163 TYR A CG  1 
ATOM   1273 C CD1 . TYR A 1 163 ? 19.18224 5.87849  4.45878   1.000 16.89796 ? 163 TYR A CD1 1 
ATOM   1274 C CD2 . TYR A 1 163 ? 17.31605 7.33398  4.11904   1.000 20.61623 ? 163 TYR A CD2 1 
ATOM   1275 C CE1 . TYR A 1 163 ? 18.47812 4.83691  3.79879   1.000 17.37292 ? 163 TYR A CE1 1 
ATOM   1276 C CE2 . TYR A 1 163 ? 16.62237 6.32788  3.47278   1.000 22.85079 ? 163 TYR A CE2 1 
ATOM   1277 C CZ  . TYR A 1 163 ? 17.19849 5.08912  3.30513   1.000 20.63583 ? 163 TYR A CZ  1 
ATOM   1278 O OH  . TYR A 1 163 ? 16.44063 4.14119  2.64771   1.000 23.48940 ? 163 TYR A OH  1 
ATOM   1279 N N   . ASN A 1 164 ? 22.22941 9.19264  4.65777   1.000 15.62034 ? 164 ASN A N   1 
ATOM   1280 C CA  . ASN A 1 164 ? 23.38604 9.36048  3.77442   1.000 15.86567 ? 164 ASN A CA  1 
ATOM   1281 C C   . ASN A 1 164 ? 24.56839 8.51593  4.23577   1.000 16.53008 ? 164 ASN A C   1 
ATOM   1282 O O   . ASN A 1 164 ? 25.24333 7.85353  3.43051   1.000 16.11933 ? 164 ASN A O   1 
ATOM   1283 C CB  . ASN A 1 164 ? 23.75103 10.84918 3.73643   1.000 14.82614 ? 164 ASN A CB  1 
ATOM   1284 C CG  . ASN A 1 164 ? 25.06318 11.12385 3.02338   1.000 16.68542 ? 164 ASN A CG  1 
ATOM   1285 O OD1 . ASN A 1 164 ? 25.09439 11.27226 1.79194   1.000 19.60887 ? 164 ASN A OD1 1 
ATOM   1286 N ND2 . ASN A 1 164 ? 26.15652 11.18727 3.78318   1.000 16.74140 ? 164 ASN A ND2 1 
ATOM   1287 N N   . LYS A 1 165 ? 24.84894 8.52734  5.54230   1.000 16.84966 ? 165 LYS A N   1 
ATOM   1288 C CA  . LYS A 1 165 ? 26.00548 7.78266  6.02666   1.000 16.45747 ? 165 LYS A CA  1 
ATOM   1289 C C   . LYS A 1 165 ? 25.84539 6.28507  5.78179   1.000 16.57209 ? 165 LYS A C   1 
ATOM   1290 O O   . LYS A 1 165 ? 26.80349 5.59816  5.39574   1.000 17.08687 ? 165 LYS A O   1 
ATOM   1291 C CB  . LYS A 1 165 ? 26.20676 8.07133  7.52117   1.000 18.26715 ? 165 LYS A CB  1 
ATOM   1292 C CG  . LYS A 1 165 ? 27.43345 7.42688  8.10378   1.000 18.34285 ? 165 LYS A CG  1 
ATOM   1293 C CD  . LYS A 1 165 ? 27.56680 7.79922  9.56754   1.000 20.08187 ? 165 LYS A CD  1 
ATOM   1294 C CE  . LYS A 1 165 ? 28.87647 7.30879  10.12090  1.000 25.54386 ? 165 LYS A CE  1 
ATOM   1295 N NZ  . LYS A 1 165 ? 28.84640 5.84686  10.37524  1.000 29.84787 ? 165 LYS A NZ  1 
ATOM   1296 N N   . SER A 1 166 ? 24.64621 5.75188  6.03761   1.000 17.26928 ? 166 SER A N   1 
ATOM   1297 C CA  . SER A 1 166 ? 24.38168 4.33205  5.85878   1.000 17.10501 ? 166 SER A CA  1 
ATOM   1298 C C   . SER A 1 166 ? 24.48010 3.90565  4.40394   1.000 17.17251 ? 166 SER A C   1 
ATOM   1299 O O   . SER A 1 166 ? 24.65767 2.71237  4.12270   1.000 18.84573 ? 166 SER A O   1 
ATOM   1300 C CB  . SER A 1 166 ? 22.99000 3.99979  6.38655   1.000 19.10544 ? 166 SER A CB  1 
ATOM   1301 O OG  . SER A 1 166 ? 22.95268 4.19754  7.78383   1.000 21.44433 ? 166 SER A OG  1 
ATOM   1302 N N   . LEU A 1 167 ? 24.31115 4.84717  3.49558   1.000 18.23436 ? 167 LEU A N   1 
ATOM   1303 C CA  . LEU A 1 167 ? 24.38892 4.60144  2.06043   1.000 17.37563 ? 167 LEU A CA  1 
ATOM   1304 C C   . LEU A 1 167 ? 25.78304 4.81212  1.50488   1.000 18.32440 ? 167 LEU A C   1 
ATOM   1305 O O   . LEU A 1 167 ? 25.96691 4.73827  0.28694   1.000 19.82571 ? 167 LEU A O   1 
ATOM   1306 C CB  . LEU A 1 167 ? 23.38361 5.50287  1.33684   1.000 16.92075 ? 167 LEU A CB  1 
ATOM   1307 C CG  . LEU A 1 167 ? 21.92002 5.17671  1.62094   1.000 17.58932 ? 167 LEU A CG  1 
ATOM   1308 C CD1 . LEU A 1 167 ? 20.99760 6.25864  1.06529   1.000 20.92202 ? 167 LEU A CD1 1 
ATOM   1309 C CD2 . LEU A 1 167 ? 21.53228 3.77463  1.13180   1.000 17.26183 ? 167 LEU A CD2 1 
ATOM   1310 N N   . GLY A 1 168 ? 26.76991 5.08057  2.35664   1.000 18.27486 ? 168 GLY A N   1 
ATOM   1311 C CA  . GLY A 1 168 ? 28.14321 5.23384  1.91347   1.000 18.64314 ? 168 GLY A CA  1 
ATOM   1312 C C   . GLY A 1 168 ? 28.54966 6.65559  1.62997   1.000 18.18020 ? 168 GLY A C   1 
ATOM   1313 O O   . GLY A 1 168 ? 29.65574 6.88123  1.11381   1.000 19.25499 ? 168 GLY A O   1 
ATOM   1314 N N   . GLY A 1 169 ? 27.70892 7.62897  1.97572   1.000 17.85731 ? 169 GLY A N   1 
ATOM   1315 C CA  . GLY A 1 169 ? 28.03242 9.00685  1.68251   1.000 17.00376 ? 169 GLY A CA  1 
ATOM   1316 C C   . GLY A 1 169 ? 29.12984 9.56281  2.57193   1.000 16.77935 ? 169 GLY A C   1 
ATOM   1317 O O   . GLY A 1 169 ? 29.44869 9.03710  3.65550   1.000 17.29243 ? 169 GLY A O   1 
ATOM   1318 N N   . ALA A 1 170 ? 29.68441 10.67910 2.11712   1.000 15.63066 ? 170 ALA A N   1 
ATOM   1319 C CA  . ALA A 1 170 ? 30.65803 11.43379 2.89224   1.000 15.62962 ? 170 ALA A CA  1 
ATOM   1320 C C   . ALA A 1 170 ? 29.95600 12.23560 3.98340   1.000 17.77673 ? 170 ALA A C   1 
ATOM   1321 O O   . ALA A 1 170 ? 28.80595 12.67030 3.83021   1.000 18.71811 ? 170 ALA A O   1 
ATOM   1322 C CB  . ALA A 1 170 ? 31.44955 12.37849 1.98223   1.000 17.90058 ? 170 ALA A CB  1 
ATOM   1323 N N   . LEU A 1 171 ? 30.64505 12.41367 5.10569   1.000 17.47438 ? 171 LEU A N   1 
ATOM   1324 C CA  . LEU A 1 171 ? 30.16349 13.34045 6.13250   1.000 16.84659 ? 171 LEU A CA  1 
ATOM   1325 C C   . LEU A 1 171 ? 30.73612 14.71159 5.82969   1.000 18.65975 ? 171 LEU A C   1 
ATOM   1326 O O   . LEU A 1 171 ? 31.95162 14.85361 5.65643   1.000 20.65447 ? 171 LEU A O   1 
ATOM   1327 C CB  . LEU A 1 171 ? 30.57397 12.89835 7.54133   1.000 17.89937 ? 171 LEU A CB  1 
ATOM   1328 C CG  . LEU A 1 171 ? 30.39183 11.41007 7.83058   1.000 18.89696 ? 171 LEU A CG  1 
ATOM   1329 C CD1 . LEU A 1 171 ? 30.73582 11.13643 9.30040   1.000 21.50121 ? 171 LEU A CD1 1 
ATOM   1330 C CD2 . LEU A 1 171 ? 28.97007 10.95044 7.53569   1.000 21.32720 ? 171 LEU A CD2 1 
ATOM   1331 N N   . MET A 1 172 ? 29.86644 15.70960 5.75002   1.000 18.90701 ? 172 MET A N   1 
ATOM   1332 C CA  A MET A 1 172 ? 30.23248 17.05169 5.31568   0.700 21.24037 ? 172 MET A CA  1 
ATOM   1333 C CA  B MET A 1 172 ? 30.24090 17.04552 5.31392   0.300 20.64359 ? 172 MET A CA  1 
ATOM   1334 C C   . MET A 1 172 ? 29.95778 18.05466 6.42140   1.000 21.21794 ? 172 MET A C   1 
ATOM   1335 O O   . MET A 1 172 ? 28.84868 18.09834 6.96081   1.000 23.54871 ? 172 MET A O   1 
ATOM   1336 C CB  A MET A 1 172 ? 29.43889 17.47509 4.07881   0.700 25.19478 ? 172 MET A CB  1 
ATOM   1337 C CB  B MET A 1 172 ? 29.48083 17.39742 4.02671   0.300 22.79848 ? 172 MET A CB  1 
ATOM   1338 C CG  A MET A 1 172 ? 29.38305 16.50207 2.96530   0.700 27.19527 ? 172 MET A CG  1 
ATOM   1339 C CG  B MET A 1 172 ? 30.02085 18.57397 3.24329   0.300 24.67862 ? 172 MET A CG  1 
ATOM   1340 S SD  A MET A 1 172 ? 28.34762 17.28822 1.70807   0.700 28.11257 ? 172 MET A SD  1 
ATOM   1341 S SD  B MET A 1 172 ? 29.55131 18.44955 1.49962   0.300 27.55995 ? 172 MET A SD  1 
ATOM   1342 C CE  A MET A 1 172 ? 29.00522 18.95172 1.76993   0.700 29.27140 ? 172 MET A CE  1 
ATOM   1343 C CE  B MET A 1 172 ? 27.93673 17.68274 1.64103   0.300 27.74326 ? 172 MET A CE  1 
ATOM   1344 N N   . HIS A 1 173 ? 30.95189 18.87394 6.73155   1.000 21.35020 ? 173 HIS A N   1 
ATOM   1345 C CA  . HIS A 1 173 ? 30.76226 19.94040 7.70640   1.000 20.66295 ? 173 HIS A CA  1 
ATOM   1346 C C   . HIS A 1 173 ? 29.62671 20.86526 7.26855   1.000 23.84965 ? 173 HIS A C   1 
ATOM   1347 O O   . HIS A 1 173 ? 29.58173 21.27843 6.10076   1.000 23.59366 ? 173 HIS A O   1 
ATOM   1348 C CB  . HIS A 1 173 ? 32.03784 20.75470 7.86887   1.000 22.31248 ? 173 HIS A CB  1 
ATOM   1349 C CG  . HIS A 1 173 ? 31.98804 21.66946 9.04915   1.000 23.86402 ? 173 HIS A CG  1 
ATOM   1350 N ND1 . HIS A 1 173 ? 31.56126 22.97970 8.96304   1.000 26.27752 ? 173 HIS A ND1 1 
ATOM   1351 C CD2 . HIS A 1 173 ? 32.24956 21.44183 10.35826  1.000 24.37386 ? 173 HIS A CD2 1 
ATOM   1352 C CE1 . HIS A 1 173 ? 31.58922 23.52501 10.16656  1.000 27.21495 ? 173 HIS A CE1 1 
ATOM   1353 N NE2 . HIS A 1 173 ? 32.00446 22.61332 11.02833  1.000 25.69810 ? 173 HIS A NE2 1 
ATOM   1354 N N   . PRO A 1 174 ? 28.71702 21.24675 8.17586   1.000 23.98776 ? 174 PRO A N   1 
ATOM   1355 C CA  . PRO A 1 174 ? 27.52838 22.00913 7.75003   1.000 25.75708 ? 174 PRO A CA  1 
ATOM   1356 C C   . PRO A 1 174 ? 27.80650 23.45178 7.36778   1.000 28.29636 ? 174 PRO A C   1 
ATOM   1357 O O   . PRO A 1 174 ? 26.88591 24.13340 6.89025   1.000 31.11915 ? 174 PRO A O   1 
ATOM   1358 C CB  . PRO A 1 174 ? 26.58586 21.93907 8.97069   1.000 29.53095 ? 174 PRO A CB  1 
ATOM   1359 C CG  . PRO A 1 174 ? 27.17436 20.91335 9.88962   1.000 31.60002 ? 174 PRO A CG  1 
ATOM   1360 C CD  . PRO A 1 174 ? 28.62429 20.76629 9.56288   1.000 26.04628 ? 174 PRO A CD  1 
ATOM   1361 N N   . SER A 1 175 ? 29.02788 23.95588 7.54289   1.000 28.29296 ? 175 SER A N   1 
ATOM   1362 C CA  . SER A 1 175 ? 29.33668 25.26289 6.97349   1.000 30.44224 ? 175 SER A CA  1 
ATOM   1363 C C   . SER A 1 175 ? 29.41743 25.21459 5.45072   1.000 31.16130 ? 175 SER A C   1 
ATOM   1364 O O   . SER A 1 175 ? 29.43587 26.27249 4.80583   1.000 34.28370 ? 175 SER A O   1 
ATOM   1365 C CB  . SER A 1 175 ? 30.64558 25.80934 7.55226   1.000 31.86101 ? 175 SER A CB  1 
ATOM   1366 O OG  . SER A 1 175 ? 31.74733 25.02008 7.15198   1.000 33.98779 ? 175 SER A OG  1 
ATOM   1367 N N   . ILE A 1 176 ? 29.44640 24.02392 4.86144   1.000 26.95323 ? 176 ILE A N   1 
ATOM   1368 C CA  . ILE A 1 176 ? 29.50891 23.88767 3.40948   1.000 25.25361 ? 176 ILE A CA  1 
ATOM   1369 C C   . ILE A 1 176 ? 28.09568 23.91054 2.84594   1.000 23.83382 ? 176 ILE A C   1 
ATOM   1370 O O   . ILE A 1 176 ? 27.26624 23.06692 3.19447   1.000 23.94693 ? 176 ILE A O   1 
ATOM   1371 C CB  . ILE A 1 176 ? 30.22844 22.60031 3.00316   1.000 24.24859 ? 176 ILE A CB  1 
ATOM   1372 C CG1 . ILE A 1 176 ? 31.65367 22.60760 3.53942   1.000 26.15519 ? 176 ILE A CG1 1 
ATOM   1373 C CG2 . ILE A 1 176 ? 30.19975 22.44955 1.47875   1.000 24.96985 ? 176 ILE A CG2 1 
ATOM   1374 C CD1 . ILE A 1 176 ? 32.31972 21.29223 3.37513   1.000 27.31044 ? 176 ILE A CD1 1 
ATOM   1375 N N   . GLU A 1 177 ? 27.81882 24.86646 1.96554   1.000 22.33739 ? 177 GLU A N   1 
ATOM   1376 C CA  . GLU A 1 177 ? 26.48059 24.97708 1.39055   1.000 23.36216 ? 177 GLU A CA  1 
ATOM   1377 C C   . GLU A 1 177 ? 26.40668 24.03214 0.20621   1.000 23.23343 ? 177 GLU A C   1 
ATOM   1378 O O   . GLU A 1 177 ? 26.82501 24.36587 -0.90910  1.000 24.40884 ? 177 GLU A O   1 
ATOM   1379 C CB  . GLU A 1 177 ? 26.17415 26.41210 0.99603   1.000 27.17851 ? 177 GLU A CB  1 
ATOM   1380 C CG  . GLU A 1 177 ? 26.02416 27.33165 2.20922   0.800 29.26193 ? 177 GLU A CG  1 
ATOM   1381 C CD  . GLU A 1 177 ? 25.66581 28.75901 1.83564   0.700 34.20012 ? 177 GLU A CD  1 
ATOM   1382 O OE1 . GLU A 1 177 ? 26.38403 29.37340 1.02577   0.700 35.08205 ? 177 GLU A OE1 1 
ATOM   1383 O OE2 . GLU A 1 177 ? 24.65653 29.27059 2.36048   0.700 37.36234 ? 177 GLU A OE2 1 
ATOM   1384 N N   . ALA A 1 178 ? 25.87057 22.84547 0.44975   1.000 20.71177 ? 178 ALA A N   1 
ATOM   1385 C CA  . ALA A 1 178 ? 25.92090 21.78101 -0.54075  1.000 18.09127 ? 178 ALA A CA  1 
ATOM   1386 C C   . ALA A 1 178 ? 24.80571 20.78963 -0.24316  1.000 19.45417 ? 178 ALA A C   1 
ATOM   1387 O O   . ALA A 1 178 ? 24.18770 20.81121 0.82892   1.000 21.01620 ? 178 ALA A O   1 
ATOM   1388 C CB  . ALA A 1 178 ? 27.28420 21.08837 -0.53956  1.000 20.66121 ? 178 ALA A CB  1 
ATOM   1389 N N   . MET A 1 179 ? 24.56659 19.90771 -1.21066  1.000 17.92420 ? 179 MET A N   1 
ATOM   1390 C CA  . MET A 1 179 ? 23.71660 18.73986 -1.04183  1.000 17.29950 ? 179 MET A CA  1 
ATOM   1391 C C   . MET A 1 179 ? 24.45827 17.54198 -1.61449  1.000 16.99274 ? 179 MET A C   1 
ATOM   1392 O O   . MET A 1 179 ? 25.28827 17.68318 -2.52604  1.000 18.34649 ? 179 MET A O   1 
ATOM   1393 C CB  . MET A 1 179 ? 22.34946 18.91779 -1.72936  1.000 17.60879 ? 179 MET A CB  1 
ATOM   1394 C CG  . MET A 1 179 ? 22.46739 19.15005 -3.24419  1.000 17.62488 ? 179 MET A CG  1 
ATOM   1395 S SD  . MET A 1 179 ? 20.86160 19.54857 -3.96558  1.000 19.78790 ? 179 MET A SD  1 
ATOM   1396 C CE  . MET A 1 179 ? 21.42104 19.72975 -5.66534  1.000 18.70936 ? 179 MET A CE  1 
ATOM   1397 N N   . GLN A 1 180 ? 24.14694 16.35747 -1.09989  1.000 16.55215 ? 180 GLN A N   1 
ATOM   1398 C CA  . GLN A 1 180 ? 24.86885 15.15692 -1.49956  1.000 16.10747 ? 180 GLN A CA  1 
ATOM   1399 C C   . GLN A 1 180 ? 23.89877 14.06957 -1.92563  1.000 15.61057 ? 180 GLN A C   1 
ATOM   1400 O O   . GLN A 1 180 ? 22.98595 13.70684 -1.17291  1.000 16.63082 ? 180 GLN A O   1 
ATOM   1401 C CB  . GLN A 1 180 ? 25.77710 14.65045 -0.36801  1.000 15.84892 ? 180 GLN A CB  1 
ATOM   1402 C CG  . GLN A 1 180 ? 26.50250 13.35195 -0.73766  1.000 15.36041 ? 180 GLN A CG  1 
ATOM   1403 C CD  . GLN A 1 180 ? 27.55760 12.96097 0.28694   1.000 17.13000 ? 180 GLN A CD  1 
ATOM   1404 O OE1 . GLN A 1 180 ? 28.28898 12.00145 0.09365   1.000 18.19329 ? 180 GLN A OE1 1 
ATOM   1405 N NE2 . GLN A 1 180 ? 27.61066 13.69720 1.40787   1.000 17.48353 ? 180 GLN A NE2 1 
ATOM   1406 N N   . LEU A 1 181 ? 24.11827 13.53651 -3.13538  1.000 15.24994 ? 181 LEU A N   1 
ATOM   1407 C CA  . LEU A 1 181 ? 23.28249 12.49806 -3.71228  1.000 16.32649 ? 181 LEU A CA  1 
ATOM   1408 C C   . LEU A 1 181 ? 23.94467 11.13315 -3.57491  1.000 16.47523 ? 181 LEU A C   1 
ATOM   1409 O O   . LEU A 1 181 ? 25.06439 10.92639 -4.07538  1.000 17.78179 ? 181 LEU A O   1 
ATOM   1410 C CB  . LEU A 1 181 ? 23.02722 12.81126 -5.18931  1.000 17.50926 ? 181 LEU A CB  1 
ATOM   1411 C CG  . LEU A 1 181 ? 22.16071 11.78654 -5.91918  1.000 17.63444 ? 181 LEU A CG  1 
ATOM   1412 C CD1 . LEU A 1 181 ? 20.68814 11.88810 -5.48160  1.000 18.84355 ? 181 LEU A CD1 1 
ATOM   1413 C CD2 . LEU A 1 181 ? 22.28132 12.00976 -7.45666  1.000 19.17252 ? 181 LEU A CD2 1 
ATOM   1414 N N   . THR A 1 182 ? 23.26030 10.19496 -2.90693  1.000 15.29686 ? 182 THR A N   1 
ATOM   1415 C CA  . THR A 1 182 ? 23.75384 8.82828  -2.79366  1.000 15.45846 ? 182 THR A CA  1 
ATOM   1416 C C   . THR A 1 182 ? 22.79360 7.84282  -3.44161  1.000 15.94885 ? 182 THR A C   1 
ATOM   1417 O O   . THR A 1 182 ? 21.56956 8.06414  -3.49553  1.000 16.93308 ? 182 THR A O   1 
ATOM   1418 C CB  . THR A 1 182 ? 23.98546 8.40431  -1.31605  1.000 17.52809 ? 182 THR A CB  1 
ATOM   1419 O OG1 . THR A 1 182 ? 22.81678 8.71707  -0.55812  1.000 17.88929 ? 182 THR A OG1 1 
ATOM   1420 C CG2 . THR A 1 182 ? 25.19583 9.12882  -0.74409  1.000 19.91603 ? 182 THR A CG2 1 
ATOM   1421 N N   . GLU A 1 183 ? 23.36539 6.73626  -3.90569  1.000 16.86096 ? 183 GLU A N   1 
ATOM   1422 C CA  . GLU A 1 183 ? 22.61449 5.65268  -4.52701  1.000 17.93060 ? 183 GLU A CA  1 
ATOM   1423 C C   . GLU A 1 183 ? 22.13893 4.63036  -3.50563  1.000 18.14103 ? 183 GLU A C   1 
ATOM   1424 O O   . GLU A 1 183 ? 22.84799 4.30436  -2.54683  1.000 20.87659 ? 183 GLU A O   1 
ATOM   1425 C CB  . GLU A 1 183 ? 23.48369 4.92396  -5.53551  1.000 20.15845 ? 183 GLU A CB  1 
ATOM   1426 C CG  . GLU A 1 183 ? 23.97802 5.78105  -6.65408  1.000 21.42360 ? 183 GLU A CG  1 
ATOM   1427 C CD  . GLU A 1 183 ? 24.75333 4.97569  -7.67206  1.000 23.35701 ? 183 GLU A CD  1 
ATOM   1428 O OE1 . GLU A 1 183 ? 24.99197 3.76605  -7.43339  1.000 25.54682 ? 183 GLU A OE1 1 
ATOM   1429 O OE2 . GLU A 1 183 ? 25.13651 5.55775  -8.69524  1.000 23.19755 ? 183 GLU A OE2 1 
ATOM   1430 N N   . MET A 1 184 ? 20.97119 4.05281  -3.77503  1.000 16.34664 ? 184 MET A N   1 
ATOM   1431 C CA  . MET A 1 184 ? 20.48164 2.86021  -3.07652  1.000 16.97846 ? 184 MET A CA  1 
ATOM   1432 C C   . MET A 1 184 ? 20.46978 1.69381  -4.05923  1.000 20.00113 ? 184 MET A C   1 
ATOM   1433 O O   . MET A 1 184 ? 19.57871 1.61368  -4.91624  1.000 21.58506 ? 184 MET A O   1 
ATOM   1434 C CB  . MET A 1 184 ? 19.07487 3.06888  -2.52785  1.000 18.70606 ? 184 MET A CB  1 
ATOM   1435 C CG  . MET A 1 184 ? 18.89680 4.29862  -1.69109  1.000 21.96601 ? 184 MET A CG  1 
ATOM   1436 S SD  . MET A 1 184 ? 17.17118 4.32529  -1.18187  1.000 31.20540 ? 184 MET A SD  1 
ATOM   1437 C CE  . MET A 1 184 ? 17.07994 5.95402  -0.44712  1.000 29.47663 ? 184 MET A CE  1 
ATOM   1438 N N   . ALA A 1 185 ? 21.42241 0.78157  -3.90149  1.000 20.04173 ? 185 ALA A N   1 
ATOM   1439 C CA  . ALA A 1 185 ? 21.51852 -0.46486 -4.65714  1.000 19.46522 ? 185 ALA A CA  1 
ATOM   1440 C C   . ALA A 1 185 ? 21.26760 -0.25918 -6.14963  1.000 20.42864 ? 185 ALA A C   1 
ATOM   1441 O O   . ALA A 1 185 ? 20.24806 -0.68395 -6.68408  1.000 24.69117 ? 185 ALA A O   1 
ATOM   1442 C CB  . ALA A 1 185 ? 20.55234 -1.51003 -4.09221  1.000 20.73068 ? 185 ALA A CB  1 
ATOM   1443 N N   . SER A 1 186 ? 22.19263 0.39309  -6.82319  1.000 22.38516 ? 186 SER A N   1 
ATOM   1444 C CA  A SER A 1 186 ? 22.08521 0.54243  -8.26422  0.700 23.46547 ? 186 SER A CA  1 
ATOM   1445 C CA  B SER A 1 186 ? 22.09790 0.54843  -8.26585  0.300 22.18985 ? 186 SER A CA  1 
ATOM   1446 C C   . SER A 1 186 ? 22.49194 -0.74993 -8.95339  1.000 23.83866 ? 186 SER A C   1 
ATOM   1447 O O   . SER A 1 186 ? 23.38526 -1.46898 -8.50125  1.000 24.51222 ? 186 SER A O   1 
ATOM   1448 C CB  A SER A 1 186 ? 22.98089 1.67536  -8.74402  0.700 24.59061 ? 186 SER A CB  1 
ATOM   1449 C CB  B SER A 1 186 ? 23.00223 1.68717  -8.74687  0.300 20.55623 ? 186 SER A CB  1 
ATOM   1450 O OG  A SER A 1 186 ? 24.31716 1.37424  -8.40975  0.700 26.10466 ? 186 SER A OG  1 
ATOM   1451 O OG  B SER A 1 186 ? 23.16738 1.65823  -10.15817 0.300 19.66538 ? 186 SER A OG  1 
ATOM   1452 N N   . ILE A 1 187 ? 21.83747 -1.04190 -10.07098 1.000 22.43651 ? 187 ILE A N   1 
ATOM   1453 C CA  A ILE A 1 187 ? 22.27495 -2.16618 -10.87296 0.700 23.82953 ? 187 ILE A CA  1 
ATOM   1454 C CA  B ILE A 1 187 ? 22.23672 -2.15400 -10.92663 0.300 24.27590 ? 187 ILE A CA  1 
ATOM   1455 C C   . ILE A 1 187 ? 23.37751 -1.68750 -11.80755 1.000 26.38830 ? 187 ILE A C   1 
ATOM   1456 O O   . ILE A 1 187 ? 23.27682 -0.62981 -12.44147 1.000 29.52742 ? 187 ILE A O   1 
ATOM   1457 C CB  A ILE A 1 187 ? 21.10733 -2.80049 -11.63366 0.700 24.40544 ? 187 ILE A CB  1 
ATOM   1458 C CB  B ILE A 1 187 ? 21.06889 -2.62428 -11.79910 0.300 24.55918 ? 187 ILE A CB  1 
ATOM   1459 C CG1 A ILE A 1 187 ? 21.53673 -4.17294 -12.17232 0.700 23.46302 ? 187 ILE A CG1 1 
ATOM   1460 C CG1 B ILE A 1 187 ? 20.03227 -3.36292 -10.97380 0.300 24.84543 ? 187 ILE A CG1 1 
ATOM   1461 C CG2 A ILE A 1 187 ? 20.63463 -1.88798 -12.73484 0.700 24.36453 ? 187 ILE A CG2 1 
ATOM   1462 C CG2 B ILE A 1 187 ? 21.58866 -3.49654 -12.93837 0.300 23.75816 ? 187 ILE A CG2 1 
ATOM   1463 C CD1 A ILE A 1 187 ? 20.39910 -5.00087 -12.77958 0.700 23.92533 ? 187 ILE A CD1 1 
ATOM   1464 C CD1 B ILE A 1 187 ? 19.47471 -4.56978 -11.68847 0.300 25.87831 ? 187 ILE A CD1 1 
ATOM   1465 N N   . ASN A 1 188 ? 24.44872 -2.46298 -11.87038 1.000 25.78839 ? 188 ASN A N   1 
ATOM   1466 C CA  . ASN A 1 188 ? 25.54231 -2.12287 -12.77254 1.000 29.40908 ? 188 ASN A CA  1 
ATOM   1467 C C   . ASN A 1 188 ? 25.98697 -3.37639 -13.50044 1.000 29.71962 ? 188 ASN A C   1 
ATOM   1468 O O   . ASN A 1 188 ? 26.38145 -4.36359 -12.87867 1.000 30.71040 ? 188 ASN A O   1 
ATOM   1469 C CB  . ASN A 1 188 ? 26.69732 -1.46029 -12.02017 1.000 31.05519 ? 188 ASN A CB  1 
ATOM   1470 C CG  . ASN A 1 188 ? 26.50824 0.05193  -11.89464 1.000 30.24856 ? 188 ASN A CG  1 
ATOM   1471 O OD1 . ASN A 1 188 ? 26.96922 0.83127  -12.75640 1.000 29.45755 ? 188 ASN A OD1 1 
ATOM   1472 N ND2 . ASN A 1 188 ? 25.81084 0.47209  -10.85087 1.000 29.49742 ? 188 ASN A ND2 1 
ATOM   1473 N N   . ASN A 1 189 ? 25.88068 -3.35139 -14.81919 1.000 29.28099 ? 189 ASN A N   1 
ATOM   1474 C CA  . ASN A 1 189 ? 26.37298 -4.46275 -15.61115 1.000 31.59768 ? 189 ASN A CA  1 
ATOM   1475 C C   . ASN A 1 189 ? 26.79477 -3.90341 -16.95691 1.000 35.52367 ? 189 ASN A C   1 
ATOM   1476 O O   . ASN A 1 189 ? 26.85442 -2.68632 -17.14964 1.000 39.80011 ? 189 ASN A O   1 
ATOM   1477 C CB  . ASN A 1 189 ? 25.31266 -5.56822 -15.70400 1.000 32.19740 ? 189 ASN A CB  1 
ATOM   1478 C CG  . ASN A 1 189 ? 24.00314 -5.07097 -16.27674 1.000 34.40308 ? 189 ASN A CG  1 
ATOM   1479 O OD1 . ASN A 1 189 ? 23.98986 -4.21270 -17.15873 1.000 35.21362 ? 189 ASN A OD1 1 
ATOM   1480 N ND2 . ASN A 1 189 ? 22.89221 -5.60377 -15.77382 1.000 36.10086 ? 189 ASN A ND2 1 
ATOM   1481 N N   . ARG A 1 190 ? 27.09117 -4.79205 -17.88951 1.000 38.72959 ? 190 ARG A N   1 
ATOM   1482 C CA  . ARG A 1 190 ? 27.45923 -4.34797 -19.22860 1.000 43.71607 ? 190 ARG A CA  1 
ATOM   1483 C C   . ARG A 1 190 ? 26.43781 -3.38550 -19.83890 1.000 45.38867 ? 190 ARG A C   1 
ATOM   1484 O O   . ARG A 1 190 ? 26.80383 -2.57329 -20.69453 1.000 49.07619 ? 190 ARG A O   1 
ATOM   1485 C CB  . ARG A 1 190 ? 27.64992 -5.58217 -20.11597 1.000 44.92715 ? 190 ARG A CB  1 
ATOM   1486 C CG  . ARG A 1 190 ? 27.77690 -5.29776 -21.57994 0.800 48.12198 ? 190 ARG A CG  1 
ATOM   1487 C CD  . ARG A 1 190 ? 28.12472 -6.58014 -22.30757 0.700 50.02047 ? 190 ARG A CD  1 
ATOM   1488 N NE  . ARG A 1 190 ? 27.18588 -7.65190 -21.99698 0.600 51.90386 ? 190 ARG A NE  1 
ATOM   1489 C CZ  . ARG A 1 190 ? 26.05630 -7.86758 -22.65627 0.600 54.39014 ? 190 ARG A CZ  1 
ATOM   1490 N NH1 . ARG A 1 190 ? 25.68260 -7.08894 -23.65975 0.600 55.42511 ? 190 ARG A NH1 1 
ATOM   1491 N NH2 . ARG A 1 190 ? 25.28457 -8.89209 -22.30360 0.600 55.19900 ? 190 ARG A NH2 1 
ATOM   1492 N N   . VAL A 1 191 ? 25.17894 -3.43899 -19.40610 1.000 44.99075 ? 191 VAL A N   1 
ATOM   1493 C CA  . VAL A 1 191 ? 24.08614 -2.71552 -20.04571 1.000 43.37902 ? 191 VAL A CA  1 
ATOM   1494 C C   . VAL A 1 191 ? 23.63386 -1.50532 -19.22896 1.000 41.73105 ? 191 VAL A C   1 
ATOM   1495 O O   . VAL A 1 191 ? 23.29314 -0.46305 -19.79428 1.000 43.14143 ? 191 VAL A O   1 
ATOM   1496 C CB  . VAL A 1 191 ? 22.91068 -3.68447 -20.30609 0.700 44.26717 ? 191 VAL A CB  1 
ATOM   1497 C CG1 . VAL A 1 191 ? 21.68465 -2.94638 -20.80169 0.700 45.70442 ? 191 VAL A CG1 1 
ATOM   1498 C CG2 . VAL A 1 191 ? 23.33544 -4.75889 -21.30162 0.700 44.09533 ? 191 VAL A CG2 1 
ATOM   1499 N N   . TYR A 1 192 ? 23.60159 -1.62782 -17.90594 1.000 37.57874 ? 192 TYR A N   1 
ATOM   1500 C CA  . TYR A 1 192 ? 23.16180 -0.56713 -17.00468 1.000 33.92596 ? 192 TYR A CA  1 
ATOM   1501 C C   . TYR A 1 192 ? 24.37638 0.00022  -16.28454 1.000 31.87282 ? 192 TYR A C   1 
ATOM   1502 O O   . TYR A 1 192 ? 25.17444 -0.76672 -15.73578 1.000 32.53775 ? 192 TYR A O   1 
ATOM   1503 C CB  . TYR A 1 192 ? 22.16871 -1.10546 -15.96571 1.000 35.40214 ? 192 TYR A CB  1 
ATOM   1504 C CG  . TYR A 1 192 ? 20.91915 -1.74322 -16.54096 0.700 36.86199 ? 192 TYR A CG  1 
ATOM   1505 C CD1 . TYR A 1 192 ? 20.12866 -1.05867 -17.44874 0.700 37.63135 ? 192 TYR A CD1 1 
ATOM   1506 C CD2 . TYR A 1 192 ? 20.52698 -3.02300 -16.16356 0.700 37.67518 ? 192 TYR A CD2 1 
ATOM   1507 C CE1 . TYR A 1 192 ? 18.98213 -1.62648 -17.96788 0.700 39.09557 ? 192 TYR A CE1 1 
ATOM   1508 C CE2 . TYR A 1 192 ? 19.37834 -3.60417 -16.68233 0.700 39.89376 ? 192 TYR A CE2 1 
ATOM   1509 C CZ  . TYR A 1 192 ? 18.61184 -2.89590 -17.58683 0.700 40.35173 ? 192 TYR A CZ  1 
ATOM   1510 O OH  . TYR A 1 192 ? 17.46721 -3.45087 -18.11962 0.700 43.06255 ? 192 TYR A OH  1 
ATOM   1511 N N   . ARG A 1 193 ? 24.49580 1.33421  -16.24790 1.000 30.35407 ? 193 ARG A N   1 
ATOM   1512 C CA  . ARG A 1 193 ? 25.67375 1.98220  -15.67245 1.000 29.38572 ? 193 ARG A CA  1 
ATOM   1513 C C   . ARG A 1 193 ? 25.31039 3.24462  -14.90016 1.000 27.17444 ? 193 ARG A C   1 
ATOM   1514 O O   . ARG A 1 193 ? 24.66678 4.14937  -15.44891 1.000 30.26332 ? 193 ARG A O   1 
ATOM   1515 C CB  . ARG A 1 193 ? 26.67369 2.34304  -16.76846 1.000 36.28437 ? 193 ARG A CB  1 
ATOM   1516 C CG  . ARG A 1 193 ? 27.97890 2.89008  -16.23642 1.000 40.51594 ? 193 ARG A CG  1 
ATOM   1517 C CD  . ARG A 1 193 ? 29.09453 1.86654  -16.41262 0.800 44.02581 ? 193 ARG A CD  1 
ATOM   1518 N NE  . ARG A 1 193 ? 30.32800 2.49659  -16.86587 0.700 46.53621 ? 193 ARG A NE  1 
ATOM   1519 C CZ  . ARG A 1 193 ? 30.67212 2.63951  -18.13832 0.600 48.68105 ? 193 ARG A CZ  1 
ATOM   1520 N NH1 . ARG A 1 193 ? 29.88950 2.21527  -19.11887 0.600 49.37891 ? 193 ARG A NH1 1 
ATOM   1521 N NH2 . ARG A 1 193 ? 31.83162 3.22053  -18.43483 0.600 49.04524 ? 193 ARG A NH2 1 
ATOM   1522 N N   . THR A 1 194 ? 25.76022 3.32797  -13.64075 1.000 20.86002 ? 194 THR A N   1 
ATOM   1523 C CA  . THR A 1 194 ? 25.66208 4.56167  -12.87633 1.000 20.04109 ? 194 THR A CA  1 
ATOM   1524 C C   . THR A 1 194 ? 27.03854 4.95244  -12.34874 1.000 18.31849 ? 194 THR A C   1 
ATOM   1525 O O   . THR A 1 194 ? 28.01698 4.20528  -12.46263 1.000 19.98599 ? 194 THR A O   1 
ATOM   1526 C CB  . THR A 1 194 ? 24.67411 4.44960  -11.70314 1.000 21.99874 ? 194 THR A CB  1 
ATOM   1527 O OG1 . THR A 1 194 ? 25.22127 3.58249  -10.71069 1.000 23.66666 ? 194 THR A OG1 1 
ATOM   1528 C CG2 . THR A 1 194 ? 23.31361 3.90399  -12.15516 1.000 25.77617 ? 194 THR A CG2 1 
ATOM   1529 N N   . ILE A 1 195 ? 27.10912 6.14889  -11.76019 1.000 18.25061 ? 195 ILE A N   1 
ATOM   1530 C CA  . ILE A 1 195 ? 28.40197 6.65197  -11.29737 1.000 18.69472 ? 195 ILE A CA  1 
ATOM   1531 C C   . ILE A 1 195 ? 28.86583 5.90442  -10.04741 1.000 19.78631 ? 195 ILE A C   1 
ATOM   1532 O O   . ILE A 1 195 ? 30.07096 5.73875  -9.83439  1.000 20.00838 ? 195 ILE A O   1 
ATOM   1533 C CB  . ILE A 1 195 ? 28.31958 8.17970  -11.07378 1.000 18.43283 ? 195 ILE A CB  1 
ATOM   1534 C CG1 . ILE A 1 195 ? 29.70619 8.79766  -10.84200 1.000 19.01559 ? 195 ILE A CG1 1 
ATOM   1535 C CG2 . ILE A 1 195 ? 27.36080 8.52315  -9.92373  1.000 18.36626 ? 195 ILE A CG2 1 
ATOM   1536 C CD1 . ILE A 1 195 ? 30.68249 8.62605  -12.03660 1.000 21.79807 ? 195 ILE A CD1 1 
ATOM   1537 N N   . GLY A 1 196 ? 27.93569 5.41812  -9.23213  1.000 18.80026 ? 196 GLY A N   1 
ATOM   1538 C CA  . GLY A 1 196 ? 28.26481 4.64876  -8.01266  1.000 20.06907 ? 196 GLY A CA  1 
ATOM   1539 C C   . GLY A 1 196 ? 28.59709 5.57322  -6.86564  1.000 20.76451 ? 196 GLY A C   1 
ATOM   1540 O O   . GLY A 1 196 ? 27.96330 5.52058  -5.79960  1.000 21.78984 ? 196 GLY A O   1 
ATOM   1541 N N   . SER A 1 197 ? 29.54928 6.46334  -7.08702  1.000 18.48596 ? 197 SER A N   1 
ATOM   1542 C CA  . SER A 1 197 ? 30.04340 7.35492  -6.06133  1.000 18.11944 ? 197 SER A CA  1 
ATOM   1543 C C   . SER A 1 197 ? 28.97536 8.34152  -5.61710  1.000 16.29961 ? 197 SER A C   1 
ATOM   1544 O O   . SER A 1 197 ? 28.14896 8.77995  -6.41672  1.000 17.74452 ? 197 SER A O   1 
ATOM   1545 C CB  . SER A 1 197 ? 31.22615 8.14243  -6.59530  1.000 17.14628 ? 197 SER A CB  1 
ATOM   1546 O OG  . SER A 1 197 ? 32.23008 7.29158  -7.04649  1.000 18.41703 ? 197 SER A OG  1 
ATOM   1547 N N   . PRO A 1 198 ? 28.97127 8.71064  -4.33923  1.000 16.78435 ? 198 PRO A N   1 
ATOM   1548 C CA  . PRO A 1 198 ? 28.19235 9.88153  -3.92497  1.000 16.73767 ? 198 PRO A CA  1 
ATOM   1549 C C   . PRO A 1 198 ? 28.63601 11.10776 -4.70703  1.000 16.64219 ? 198 PRO A C   1 
ATOM   1550 O O   . PRO A 1 198 ? 29.81225 11.25191 -5.05230  1.000 17.00515 ? 198 PRO A O   1 
ATOM   1551 C CB  . PRO A 1 198 ? 28.52338 10.02203 -2.42424  1.000 18.67106 ? 198 PRO A CB  1 
ATOM   1552 C CG  . PRO A 1 198 ? 29.02476 8.66852  -2.00055  1.000 20.47907 ? 198 PRO A CG  1 
ATOM   1553 C CD  . PRO A 1 198 ? 29.77243 8.14414  -3.25031  1.000 17.94028 ? 198 PRO A CD  1 
ATOM   1554 N N   . LEU A 1 199 ? 27.69192 12.01629 -4.94151  1.000 16.70271 ? 199 LEU A N   1 
ATOM   1555 C CA  . LEU A 1 199 ? 27.93847 13.27532 -5.63959  1.000 17.14095 ? 199 LEU A CA  1 
ATOM   1556 C C   . LEU A 1 199 ? 27.59656 14.43802 -4.72437  1.000 16.66166 ? 199 LEU A C   1 
ATOM   1557 O O   . LEU A 1 199 ? 26.50814 14.45938 -4.14434  1.000 17.67235 ? 199 LEU A O   1 
ATOM   1558 C CB  . LEU A 1 199 ? 27.08768 13.37032 -6.92264  1.000 16.46979 ? 199 LEU A CB  1 
ATOM   1559 C CG  . LEU A 1 199 ? 27.19539 12.19886 -7.89505  1.000 17.22981 ? 199 LEU A CG  1 
ATOM   1560 C CD1 . LEU A 1 199 ? 26.30200 12.42380 -9.12431  1.000 20.07632 ? 199 LEU A CD1 1 
ATOM   1561 C CD2 . LEU A 1 199 ? 28.65773 12.01042 -8.34387  1.000 19.88438 ? 199 LEU A CD2 1 
ATOM   1562 N N   . VAL A 1 200 ? 28.48678 15.42396 -4.64241  1.000 16.43066 ? 200 VAL A N   1 
ATOM   1563 C CA  . VAL A 1 200 ? 28.29507 16.60697 -3.80508  1.000 17.22474 ? 200 VAL A CA  1 
ATOM   1564 C C   . VAL A 1 200 ? 28.14826 17.82238 -4.71072  1.000 17.79422 ? 200 VAL A C   1 
ATOM   1565 O O   . VAL A 1 200 ? 29.04299 18.11701 -5.52639  1.000 19.31859 ? 200 VAL A O   1 
ATOM   1566 C CB  . VAL A 1 200 ? 29.46288 16.80016 -2.82154  1.000 17.40669 ? 200 VAL A CB  1 
ATOM   1567 C CG1 . VAL A 1 200 ? 29.27743 18.08438 -2.02803  1.000 18.62558 ? 200 VAL A CG1 1 
ATOM   1568 C CG2 . VAL A 1 200 ? 29.56794 15.59556 -1.88352  1.000 18.51684 ? 200 VAL A CG2 1 
ATOM   1569 N N   . PHE A 1 201 ? 27.02559 18.53077 -4.56604  1.000 17.47892 ? 201 PHE A N   1 
ATOM   1570 C CA  . PHE A 1 201 ? 26.63563 19.65659 -5.40206  1.000 18.93900 ? 201 PHE A CA  1 
ATOM   1571 C C   . PHE A 1 201 ? 26.64715 20.95183 -4.61426  1.000 18.77518 ? 201 PHE A C   1 
ATOM   1572 O O   . PHE A 1 201 ? 26.17558 20.97686 -3.47064  1.000 20.67576 ? 201 PHE A O   1 
ATOM   1573 C CB  . PHE A 1 201 ? 25.23105 19.45266 -5.97599  1.000 18.05827 ? 201 PHE A CB  1 
ATOM   1574 C CG  . PHE A 1 201 ? 25.08680 18.21143 -6.79611  1.000 18.72884 ? 201 PHE A CG  1 
ATOM   1575 C CD1 . PHE A 1 201 ? 25.34743 18.24785 -8.15547  1.000 20.40926 ? 201 PHE A CD1 1 
ATOM   1576 C CD2 . PHE A 1 201 ? 24.67548 17.02152 -6.23539  1.000 19.82497 ? 201 PHE A CD2 1 
ATOM   1577 C CE1 . PHE A 1 201 ? 25.21675 17.10737 -8.93644  1.000 20.27942 ? 201 PHE A CE1 1 
ATOM   1578 C CE2 . PHE A 1 201 ? 24.54893 15.88094 -6.98678  1.000 18.61952 ? 201 PHE A CE2 1 
ATOM   1579 C CZ  . PHE A 1 201 ? 24.81621 15.92276 -8.37041  1.000 20.23315 ? 201 PHE A CZ  1 
ATOM   1580 N N   . PRO A 1 202 ? 27.14991 22.03180 -5.20179  1.000 20.20579 ? 202 PRO A N   1 
ATOM   1581 C CA  . PRO A 1 202 ? 27.09482 23.34754 -4.56244  1.000 22.24633 ? 202 PRO A CA  1 
ATOM   1582 C C   . PRO A 1 202 ? 25.71661 23.97760 -4.69481  1.000 23.04847 ? 202 PRO A C   1 
ATOM   1583 O O   . PRO A 1 202 ? 24.83237 23.49174 -5.39902  1.000 21.94391 ? 202 PRO A O   1 
ATOM   1584 C CB  . PRO A 1 202 ? 28.12263 24.16682 -5.35838  1.000 22.24505 ? 202 PRO A CB  1 
ATOM   1585 C CG  . PRO A 1 202 ? 28.04883 23.57902 -6.69977  1.000 21.46418 ? 202 PRO A CG  1 
ATOM   1586 C CD  . PRO A 1 202 ? 27.77028 22.10131 -6.54226  1.000 19.99317 ? 202 PRO A CD  1 
ATOM   1587 N N   . LYS A 1 203 ? 25.54755 25.06754 -3.96257  1.000 24.52479 ? 203 LYS A N   1 
ATOM   1588 C CA  . LYS A 1 203 ? 24.40133 25.93711 -4.15609  1.000 26.27108 ? 203 LYS A CA  1 
ATOM   1589 C C   . LYS A 1 203 ? 24.28410 26.32551 -5.62498  1.000 26.55007 ? 203 LYS A C   1 
ATOM   1590 O O   . LYS A 1 203 ? 25.28511 26.47605 -6.33696  1.000 27.26713 ? 203 LYS A O   1 
ATOM   1591 C CB  . LYS A 1 203 ? 24.54488 27.18807 -3.27817  1.000 31.14317 ? 203 LYS A CB  1 
ATOM   1592 C CG  . LYS A 1 203 ? 23.28503 27.56864 -2.54981  1.000 36.59226 ? 203 LYS A CG  1 
ATOM   1593 C CD  . LYS A 1 203 ? 23.53309 28.70902 -1.58365  0.700 37.72067 ? 203 LYS A CD  1 
ATOM   1594 C CE  . LYS A 1 203 ? 22.29306 28.96154 -0.76044  0.700 40.33785 ? 203 LYS A CE  1 
ATOM   1595 N NZ  . LYS A 1 203 ? 21.10881 28.99929 -1.65038  0.700 42.44403 ? 203 LYS A NZ  1 
ATOM   1596 N N   . HIS A 1 204 ? 23.04257 26.45497 -6.08573  1.000 25.81291 ? 204 HIS A N   1 
ATOM   1597 C CA  . HIS A 1 204 ? 22.65399 26.88303 -7.42227  1.000 26.28737 ? 204 HIS A CA  1 
ATOM   1598 C C   . HIS A 1 204 ? 22.71837 25.76215 -8.45623  1.000 26.70832 ? 204 HIS A C   1 
ATOM   1599 O O   . HIS A 1 204 ? 22.21245 25.95007 -9.56088  1.000 30.40332 ? 204 HIS A O   1 
ATOM   1600 C CB  . HIS A 1 204 ? 23.48113 28.07912 -7.93458  1.000 29.52560 ? 204 HIS A CB  1 
ATOM   1601 C CG  . HIS A 1 204 ? 23.47032 29.24778 -7.00102  1.000 33.62492 ? 204 HIS A CG  1 
ATOM   1602 N ND1 . HIS A 1 204 ? 22.30754 29.89136 -6.63273  1.000 37.22953 ? 204 HIS A ND1 1 
ATOM   1603 C CD2 . HIS A 1 204 ? 24.47152 29.86804 -6.33246  1.000 35.76331 ? 204 HIS A CD2 1 
ATOM   1604 C CE1 . HIS A 1 204 ? 22.59522 30.87016 -5.79375  1.000 38.06381 ? 204 HIS A CE1 1 
ATOM   1605 N NE2 . HIS A 1 204 ? 23.90125 30.87952 -5.59767  1.000 37.88464 ? 204 HIS A NE2 1 
ATOM   1606 N N   . HIS A 1 205 ? 23.33732 24.62287 -8.17298  1.000 24.34839 ? 205 HIS A N   1 
ATOM   1607 C CA  . HIS A 1 205 ? 23.17055 23.47511 -9.05549  1.000 21.95643 ? 205 HIS A CA  1 
ATOM   1608 C C   . HIS A 1 205 ? 21.80239 22.84400 -8.81215  1.000 23.70999 ? 205 HIS A C   1 
ATOM   1609 O O   . HIS A 1 205 ? 21.32494 22.75794 -7.67735  1.000 26.34012 ? 205 HIS A O   1 
ATOM   1610 C CB  . HIS A 1 205 ? 24.27450 22.43237 -8.83314  1.000 22.67377 ? 205 HIS A CB  1 
ATOM   1611 C CG  . HIS A 1 205 ? 25.59508 22.82183 -9.40985  1.000 23.88788 ? 205 HIS A CG  1 
ATOM   1612 N ND1 . HIS A 1 205 ? 26.53859 21.89929 -9.81127  1.000 25.16349 ? 205 HIS A ND1 1 
ATOM   1613 C CD2 . HIS A 1 205 ? 26.11850 24.04120 -9.68025  1.000 27.71828 ? 205 HIS A CD2 1 
ATOM   1614 C CE1 . HIS A 1 205 ? 27.59415 22.53652 -10.28880 1.000 28.16024 ? 205 HIS A CE1 1 
ATOM   1615 N NE2 . HIS A 1 205 ? 27.36591 23.83728 -10.21904 1.000 28.35074 ? 205 HIS A NE2 1 
ATOM   1616 N N   . VAL A 1 206 ? 21.17978 22.39119 -9.88673  1.000 23.49192 ? 206 VAL A N   1 
ATOM   1617 C CA  . VAL A 1 206 ? 19.87480 21.75878 -9.84561  1.000 23.81639 ? 206 VAL A CA  1 
ATOM   1618 C C   . VAL A 1 206 ? 20.02233 20.33199 -10.34340 1.000 23.60303 ? 206 VAL A C   1 
ATOM   1619 O O   . VAL A 1 206 ? 20.56454 20.08948 -11.42981 1.000 26.85570 ? 206 VAL A O   1 
ATOM   1620 C CB  . VAL A 1 206 ? 18.84618 22.52352 -10.69396 1.000 26.49535 ? 206 VAL A CB  1 
ATOM   1621 C CG1 . VAL A 1 206 ? 17.51967 21.78087 -10.70187 1.000 27.34946 ? 206 VAL A CG1 1 
ATOM   1622 C CG2 . VAL A 1 206 ? 18.68419 23.92744 -10.15559 1.000 27.96367 ? 206 VAL A CG2 1 
ATOM   1623 N N   . VAL A 1 207 ? 19.54333 19.39227 -9.55213  1.000 21.18309 ? 207 VAL A N   1 
ATOM   1624 C CA  . VAL A 1 207 ? 19.51422 17.99164 -9.92388  1.000 20.44308 ? 207 VAL A CA  1 
ATOM   1625 C C   . VAL A 1 207 ? 18.05953 17.63141 -10.13293 1.000 19.88928 ? 207 VAL A C   1 
ATOM   1626 O O   . VAL A 1 207 ? 17.23321 17.77835 -9.21605  1.000 22.32147 ? 207 VAL A O   1 
ATOM   1627 C CB  . VAL A 1 207 ? 20.16493 17.10683 -8.85100  1.000 22.43779 ? 207 VAL A CB  1 
ATOM   1628 C CG1 . VAL A 1 207 ? 20.00011 15.62895 -9.21162  1.000 24.36991 ? 207 VAL A CG1 1 
ATOM   1629 C CG2 . VAL A 1 207 ? 21.63186 17.46802 -8.71765  1.000 24.46767 ? 207 VAL A CG2 1 
ATOM   1630 N N   . SER A 1 208 ? 17.74369 17.18140 -11.34300 1.000 20.97744 ? 208 SER A N   1 
ATOM   1631 C CA  . SER A 1 208 ? 16.39144 16.83969 -11.73823 1.000 21.68330 ? 208 SER A CA  1 
ATOM   1632 C C   . SER A 1 208 ? 16.31728 15.34027 -11.99765 1.000 22.24652 ? 208 SER A C   1 
ATOM   1633 O O   . SER A 1 208 ? 17.15769 14.79078 -12.71197 1.000 23.68281 ? 208 SER A O   1 
ATOM   1634 C CB  . SER A 1 208 ? 15.99620 17.62451 -12.99904 0.900 23.96960 ? 208 SER A CB  1 
ATOM   1635 O OG  . SER A 1 208 ? 14.79080 17.12533 -13.52649 0.700 29.24505 ? 208 SER A OG  1 
ATOM   1636 N N   . LEU A 1 209 ? 15.32654 14.68269 -11.40902 1.000 21.47800 ? 209 LEU A N   1 
ATOM   1637 C CA  . LEU A 1 209 ? 15.02298 13.29202 -11.69962 1.000 23.99928 ? 209 LEU A CA  1 
ATOM   1638 C C   . LEU A 1 209 ? 13.81783 13.24773 -12.62488 1.000 25.53121 ? 209 LEU A C   1 
ATOM   1639 O O   . LEU A 1 209 ? 12.78821 13.87478 -12.34224 1.000 28.42104 ? 209 LEU A O   1 
ATOM   1640 C CB  . LEU A 1 209 ? 14.72612 12.50061 -10.42466 1.000 23.14481 ? 209 LEU A CB  1 
ATOM   1641 C CG  . LEU A 1 209 ? 15.81559 12.56451 -9.36176  1.000 23.85850 ? 209 LEU A CG  1 
ATOM   1642 C CD1 . LEU A 1 209 ? 15.45946 11.66023 -8.19090  1.000 25.69609 ? 209 LEU A CD1 1 
ATOM   1643 C CD2 . LEU A 1 209 ? 17.17405 12.19198 -9.92948  1.000 24.33458 ? 209 LEU A CD2 1 
ATOM   1644 N N   . GLN A 1 210 ? 13.94088 12.50975 -13.72454 1.000 26.21909 ? 210 GLN A N   1 
ATOM   1645 C CA  . GLN A 1 210 ? 12.88654 12.46924 -14.72151 1.000 27.55163 ? 210 GLN A CA  1 
ATOM   1646 C C   . GLN A 1 210 ? 12.45976 11.02875 -14.96112 1.000 26.75272 ? 210 GLN A C   1 
ATOM   1647 O O   . GLN A 1 210 ? 13.30699 10.17400 -15.25635 1.000 25.85565 ? 210 GLN A O   1 
ATOM   1648 C CB  . GLN A 1 210 ? 13.36610 13.13941 -16.03634 1.000 30.68169 ? 210 GLN A CB  1 
ATOM   1649 C CG  . GLN A 1 210 ? 13.58425 14.63758 -15.81616 0.800 32.61943 ? 210 GLN A CG  1 
ATOM   1650 C CD  . GLN A 1 210 ? 14.34108 15.34581 -16.92237 0.700 34.66177 ? 210 GLN A CD  1 
ATOM   1651 O OE1 . GLN A 1 210 ? 14.33660 14.92183 -18.07615 0.700 34.84888 ? 210 GLN A OE1 1 
ATOM   1652 N NE2 . GLN A 1 210 ? 14.98411 16.45784 -16.56748 0.700 36.04764 ? 210 GLN A NE2 1 
ATOM   1653 N N   . PRO A 1 211 ? 11.17521 10.71669 -14.82558 1.000 28.28912 ? 211 PRO A N   1 
ATOM   1654 C CA  . PRO A 1 211 ? 10.74105 9.33214  -14.98139 1.000 29.62332 ? 211 PRO A CA  1 
ATOM   1655 C C   . PRO A 1 211 ? 11.02720 8.84219  -16.38495 1.000 30.12862 ? 211 PRO A C   1 
ATOM   1656 O O   . PRO A 1 211 ? 11.06229 9.61727  -17.34247 1.000 29.84157 ? 211 PRO A O   1 
ATOM   1657 C CB  . PRO A 1 211 ? 9.23436  9.39540  -14.71415 1.000 30.73544 ? 211 PRO A CB  1 
ATOM   1658 C CG  . PRO A 1 211 ? 9.03891  10.66197 -13.92770 1.000 33.45900 ? 211 PRO A CG  1 
ATOM   1659 C CD  . PRO A 1 211 ? 10.05653 11.61272 -14.48325 1.000 32.14475 ? 211 PRO A CD  1 
ATOM   1660 N N   . VAL A 1 212 ? 11.20817 7.53676  -16.48995 1.000 31.54624 ? 212 VAL A N   1 
ATOM   1661 C CA  . VAL A 1 212 ? 11.47896 6.86442  -17.75170 1.000 33.17005 ? 212 VAL A CA  1 
ATOM   1662 C C   . VAL A 1 212 ? 10.27156 6.06090  -18.21915 1.000 37.17453 ? 212 VAL A C   1 
ATOM   1663 O O   . VAL A 1 212 ? 9.88262  6.13205  -19.38604 1.000 39.73945 ? 212 VAL A O   1 
ATOM   1664 C CB  . VAL A 1 212 ? 12.73166 5.97086  -17.63202 1.000 32.98030 ? 212 VAL A CB  1 
ATOM   1665 C CG1 . VAL A 1 212 ? 12.91743 5.15342  -18.89030 1.000 33.06216 ? 212 VAL A CG1 1 
ATOM   1666 C CG2 . VAL A 1 212 ? 13.95958 6.81746  -17.34866 1.000 32.81968 ? 212 VAL A CG2 1 
ATOM   1667 N N   . ASN A 1 213 ? 9.66548  5.29012  -17.31943 1.000 37.60254 ? 213 ASN A N   1 
ATOM   1668 C CA  . ASN A 1 213 ? 8.43917  4.56499  -17.63109 1.000 41.21149 ? 213 ASN A CA  1 
ATOM   1669 C C   . ASN A 1 213 ? 7.37957  4.88350  -16.58215 1.000 39.84118 ? 213 ASN A C   1 
ATOM   1670 O O   . ASN A 1 213 ? 6.50762  5.72726  -16.80030 1.000 41.61051 ? 213 ASN A O   1 
ATOM   1671 C CB  . ASN A 1 213 ? 8.69076  3.05295  -17.69253 0.800 45.59684 ? 213 ASN A CB  1 
ATOM   1672 C CG  . ASN A 1 213 ? 9.57639  2.64587  -18.85984 0.700 50.97944 ? 213 ASN A CG  1 
ATOM   1673 O OD1 . ASN A 1 213 ? 10.64796 2.06815  -18.66813 0.600 53.55750 ? 213 ASN A OD1 1 
ATOM   1674 N ND2 . ASN A 1 213 ? 9.12459  2.92958  -20.07545 0.600 52.47562 ? 213 ASN A ND2 1 
ATOM   1675 N N   . ASP A 1 214 ? 7.45673  4.21417  -15.43968 1.000 39.16141 ? 214 ASP A N   1 
ATOM   1676 C CA  . ASP A 1 214 ? 6.53355  4.46085  -14.33787 1.000 38.55196 ? 214 ASP A CA  1 
ATOM   1677 C C   . ASP A 1 214 ? 6.68741  5.88541  -13.81340 1.000 36.67177 ? 214 ASP A C   1 
ATOM   1678 O O   . ASP A 1 214 ? 7.80052  6.39905  -13.67659 1.000 35.49601 ? 214 ASP A O   1 
ATOM   1679 C CB  . ASP A 1 214 ? 6.79861  3.44298  -13.22316 1.000 40.11687 ? 214 ASP A CB  1 
ATOM   1680 C CG  . ASP A 1 214 ? 5.90151  3.63142  -12.01340 0.700 43.10511 ? 214 ASP A CG  1 
ATOM   1681 O OD1 . ASP A 1 214 ? 5.01388  4.50758  -12.03405 0.700 43.56123 ? 214 ASP A OD1 1 
ATOM   1682 O OD2 . ASP A 1 214 ? 6.09393  2.88755  -11.02717 0.700 46.07945 ? 214 ASP A OD2 1 
ATOM   1683 N N   . LYS A 1 215 ? 5.55908  6.52844  -13.51375 1.000 36.44477 ? 215 LYS A N   1 
ATOM   1684 C CA  . LYS A 1 215 ? 5.55985  7.91925  -13.07818 1.000 35.98446 ? 215 LYS A CA  1 
ATOM   1685 C C   . LYS A 1 215 ? 5.13532  8.09185  -11.62138 1.000 34.39410 ? 215 LYS A C   1 
ATOM   1686 O O   . LYS A 1 215 ? 4.95374  9.22846  -11.17307 1.000 35.42898 ? 215 LYS A O   1 
ATOM   1687 C CB  . LYS A 1 215 ? 4.66280  8.76326  -13.99313 1.000 38.42722 ? 215 LYS A CB  1 
ATOM   1688 C CG  . LYS A 1 215 ? 5.23611  9.01090  -15.38877 0.800 39.79576 ? 215 LYS A CG  1 
ATOM   1689 C CD  . LYS A 1 215 ? 4.49188  10.14458 -16.07710 0.700 44.02865 ? 215 LYS A CD  1 
ATOM   1690 C CE  . LYS A 1 215 ? 5.17005  10.55540 -17.36715 0.700 47.77726 ? 215 LYS A CE  1 
ATOM   1691 N NZ  . LYS A 1 215 ? 5.31773  9.39908  -18.28246 0.700 50.14713 ? 215 LYS A NZ  1 
ATOM   1692 N N   . ASP A 1 216 ? 4.98682  7.00853  -10.86505 1.000 33.41289 ? 216 ASP A N   1 
ATOM   1693 C CA  . ASP A 1 216 ? 4.56472  7.08786  -9.46884  1.000 33.66733 ? 216 ASP A CA  1 
ATOM   1694 C C   . ASP A 1 216 ? 5.75183  6.81607  -8.55166  1.000 32.15282 ? 216 ASP A C   1 
ATOM   1695 O O   . ASP A 1 216 ? 6.50632  5.86053  -8.76248  1.000 33.23931 ? 216 ASP A O   1 
ATOM   1696 C CB  . ASP A 1 216 ? 3.43408  6.10393  -9.16692  1.000 33.41261 ? 216 ASP A CB  1 
ATOM   1697 C CG  . ASP A 1 216 ? 2.16922  6.38024  -9.98531  1.000 37.38754 ? 216 ASP A CG  1 
ATOM   1698 O OD1 . ASP A 1 216 ? 2.10120  7.42196  -10.66756 1.000 37.85605 ? 216 ASP A OD1 1 
ATOM   1699 O OD2 . ASP A 1 216 ? 1.24016  5.54789  -9.95200  1.000 39.79878 ? 216 ASP A OD2 1 
ATOM   1700 N N   . PHE A 1 217 ? 5.90632  7.64175  -7.52315  1.000 29.92132 ? 217 PHE A N   1 
ATOM   1701 C CA  . PHE A 1 217 ? 7.08232  7.56048  -6.67809  1.000 27.47675 ? 217 PHE A CA  1 
ATOM   1702 C C   . PHE A 1 217 ? 6.70773  7.76911  -5.22422  1.000 26.67511 ? 217 PHE A C   1 
ATOM   1703 O O   . PHE A 1 217 ? 5.82002  8.56146  -4.90350  1.000 28.38727 ? 217 PHE A O   1 
ATOM   1704 C CB  . PHE A 1 217 ? 8.10476  8.61038  -7.08505  1.000 27.84514 ? 217 PHE A CB  1 
ATOM   1705 C CG  . PHE A 1 217 ? 8.60361  8.44032  -8.49187  1.000 28.20835 ? 217 PHE A CG  1 
ATOM   1706 C CD1 . PHE A 1 217 ? 9.68540  7.60460  -8.75160  1.000 27.42828 ? 217 PHE A CD1 1 
ATOM   1707 C CD2 . PHE A 1 217 ? 8.00479  9.10442  -9.54759  1.000 30.61489 ? 217 PHE A CD2 1 
ATOM   1708 C CE1 . PHE A 1 217 ? 10.15878 7.42664  -10.03498 1.000 29.05238 ? 217 PHE A CE1 1 
ATOM   1709 C CE2 . PHE A 1 217 ? 8.48464  8.93844  -10.84995 1.000 30.28916 ? 217 PHE A CE2 1 
ATOM   1710 C CZ  . PHE A 1 217 ? 9.55920  8.09492  -11.09217 1.000 29.64885 ? 217 PHE A CZ  1 
ATOM   1711 N N   . GLN A 1 218 ? 7.42848  7.07518  -4.34684  1.000 25.14845 ? 218 GLN A N   1 
ATOM   1712 C CA  . GLN A 1 218 ? 7.35981  7.34632  -2.91799  1.000 24.84241 ? 218 GLN A CA  1 
ATOM   1713 C C   . GLN A 1 218 ? 8.47834  8.32411  -2.60109  1.000 24.21614 ? 218 GLN A C   1 
ATOM   1714 O O   . GLN A 1 218 ? 9.64654  7.99405  -2.78830  1.000 24.92497 ? 218 GLN A O   1 
ATOM   1715 C CB  . GLN A 1 218 ? 7.51997  6.05741  -2.11337  1.000 28.11857 ? 218 GLN A CB  1 
ATOM   1716 C CG  . GLN A 1 218 ? 7.13734  6.17112  -0.64292  1.000 31.75837 ? 218 GLN A CG  1 
ATOM   1717 C CD  . GLN A 1 218 ? 5.62233  6.18678  -0.45804  0.800 33.94539 ? 218 GLN A CD  1 
ATOM   1718 O OE1 . GLN A 1 218 ? 4.87409  5.80729  -1.35966  0.800 37.07466 ? 218 GLN A OE1 1 
ATOM   1719 N NE2 . GLN A 1 218 ? 5.16821  6.62992  0.70228   0.800 35.77747 ? 218 GLN A NE2 1 
ATOM   1720 N N   . ILE A 1 219 ? 8.12744  9.52664  -2.15248  1.000 25.27251 ? 219 ILE A N   1 
ATOM   1721 C CA  . ILE A 1 219 ? 9.09713  10.56919 -1.84605  1.000 26.16004 ? 219 ILE A CA  1 
ATOM   1722 C C   . ILE A 1 219 ? 9.06052  10.82997 -0.34772  1.000 27.26256 ? 219 ILE A C   1 
ATOM   1723 O O   . ILE A 1 219 ? 7.99717  11.10885 0.22125   1.000 28.97543 ? 219 ILE A O   1 
ATOM   1724 C CB  . ILE A 1 219 ? 8.81516  11.85600 -2.63786  1.000 28.96474 ? 219 ILE A CB  1 
ATOM   1725 C CG1 . ILE A 1 219 ? 8.90856  11.57521 -4.15133  1.000 29.17655 ? 219 ILE A CG1 1 
ATOM   1726 C CG2 . ILE A 1 219 ? 9.77777  12.94992 -2.22147  1.000 31.14241 ? 219 ILE A CG2 1 
ATOM   1727 C CD1 . ILE A 1 219 ? 8.27540  12.63984 -5.03840  1.000 30.74508 ? 219 ILE A CD1 1 
ATOM   1728 N N   . SER A 1 220 ? 10.21820 10.73236 0.28526   1.000 26.13722 ? 220 SER A N   1 
ATOM   1729 C CA  A SER A 1 220 ? 10.37153 10.99522 1.70758   0.700 26.47339 ? 220 SER A CA  1 
ATOM   1730 C CA  B SER A 1 220 ? 10.34763 11.01066 1.70259   0.300 27.38451 ? 220 SER A CA  1 
ATOM   1731 C C   . SER A 1 220 ? 11.06827 12.33654 1.88213   1.000 27.35076 ? 220 SER A C   1 
ATOM   1732 O O   . SER A 1 220 ? 11.94648 12.69656 1.09078   1.000 32.66370 ? 220 SER A O   1 
ATOM   1733 C CB  A SER A 1 220 ? 11.20178 9.90746  2.36910   0.700 29.73132 ? 220 SER A CB  1 
ATOM   1734 C CB  B SER A 1 220 ? 11.09866 9.88947  2.41354   0.300 30.82786 ? 220 SER A CB  1 
ATOM   1735 O OG  A SER A 1 220 ? 12.58127 10.20120 2.20043   0.700 29.42145 ? 220 SER A OG  1 
ATOM   1736 O OG  B SER A 1 220 ? 10.36957 8.67957  2.34678   0.300 32.61882 ? 220 SER A OG  1 
ATOM   1737 N N   . VAL A 1 221 ? 10.64780 13.08508 2.87665   1.000 24.11284 ? 221 VAL A N   1 
ATOM   1738 C CA  . VAL A 1 221 ? 11.31123 14.31460 3.27509   1.000 23.71092 ? 221 VAL A CA  1 
ATOM   1739 C C   . VAL A 1 221 ? 11.45477 14.19785 4.77874   1.000 22.89703 ? 221 VAL A C   1 
ATOM   1740 O O   . VAL A 1 221 ? 10.44795 14.21517 5.48735   1.000 24.14137 ? 221 VAL A O   1 
ATOM   1741 C CB  . VAL A 1 221 ? 10.49923 15.56113 2.90415   1.000 26.60918 ? 221 VAL A CB  1 
ATOM   1742 C CG1 . VAL A 1 221 ? 11.16354 16.80545 3.45182   1.000 28.44739 ? 221 VAL A CG1 1 
ATOM   1743 C CG2 . VAL A 1 221 ? 10.30385 15.64325 1.37956   1.000 27.25998 ? 221 VAL A CG2 1 
ATOM   1744 N N   . ASP A 1 222 ? 12.68609 14.02040 5.26787   1.000 20.23986 ? 222 ASP A N   1 
ATOM   1745 C CA  . ASP A 1 222 ? 12.89574 13.73269 6.69308   1.000 23.18746 ? 222 ASP A CA  1 
ATOM   1746 C C   . ASP A 1 222 ? 12.01714 12.51658 7.00503   1.000 26.38841 ? 222 ASP A C   1 
ATOM   1747 O O   . ASP A 1 222 ? 12.02781 11.53691 6.25923   1.000 28.71283 ? 222 ASP A O   1 
ATOM   1748 C CB  . ASP A 1 222 ? 12.67309 15.00887 7.48035   1.000 22.45032 ? 222 ASP A CB  1 
ATOM   1749 C CG  . ASP A 1 222 ? 13.71534 16.07077 7.11097   1.000 21.68255 ? 222 ASP A CG  1 
ATOM   1750 O OD1 . ASP A 1 222 ? 14.78972 15.65781 6.61551   1.000 20.36038 ? 222 ASP A OD1 1 
ATOM   1751 O OD2 . ASP A 1 222 ? 13.48426 17.28246 7.28316   1.000 22.89410 ? 222 ASP A OD2 1 
ATOM   1752 N N   . HIS A 1 223 ? 11.24966 12.45521 8.08431   1.000 31.04762 ? 223 HIS A N   1 
ATOM   1753 C CA  A HIS A 1 223 ? 10.63667 11.12782 8.15907   0.700 36.86259 ? 223 HIS A CA  1 
ATOM   1754 C CA  B HIS A 1 223 ? 10.51825 11.22609 8.38660   0.300 36.17648 ? 223 HIS A CA  1 
ATOM   1755 C C   . HIS A 1 223 ? 9.22682  11.05191 7.58283   1.000 37.01848 ? 223 HIS A C   1 
ATOM   1756 O O   . HIS A 1 223 ? 8.54114  10.04434 7.78110   1.000 41.56238 ? 223 HIS A O   1 
ATOM   1757 C CB  A HIS A 1 223 ? 10.65965 10.51770 9.54650   0.700 43.58595 ? 223 HIS A CB  1 
ATOM   1758 C CB  B HIS A 1 223 ? 10.18428 11.15436 9.88611   0.300 40.83039 ? 223 HIS A CB  1 
ATOM   1759 C CG  A HIS A 1 223 ? 10.86995 9.03559  9.47975   0.700 47.88970 ? 223 HIS A CG  1 
ATOM   1760 C CG  B HIS A 1 223 ? 9.57658  9.84729  10.30226  0.300 45.75145 ? 223 HIS A CG  1 
ATOM   1761 N ND1 A HIS A 1 223 ? 11.51892 8.44719  8.41254   0.700 47.60362 ? 223 HIS A ND1 1 
ATOM   1762 N ND1 B HIS A 1 223 ? 10.14432 8.63302  9.98144   0.300 47.92112 ? 223 HIS A ND1 1 
ATOM   1763 C CD2 A HIS A 1 223 ? 10.49405 8.02296  10.29670  0.700 49.16531 ? 223 HIS A CD2 1 
ATOM   1764 C CD2 B HIS A 1 223 ? 8.43701  9.56146  10.97690  0.300 47.81717 ? 223 HIS A CD2 1 
ATOM   1765 C CE1 A HIS A 1 223 ? 11.55271 7.13903  8.58600   0.700 48.51568 ? 223 HIS A CE1 1 
ATOM   1766 C CE1 B HIS A 1 223 ? 9.39126  7.65638  10.45468  0.300 48.76017 ? 223 HIS A CE1 1 
ATOM   1767 N NE2 A HIS A 1 223 ? 10.93981 6.85427  9.72218   0.700 49.00222 ? 223 HIS A NE2 1 
ATOM   1768 N NE2 B HIS A 1 223 ? 8.34858  8.19249  11.06292  0.300 48.67871 ? 223 HIS A NE2 1 
ATOM   1769 N N   . LEU A 1 224 ? 8.83978  11.99926 6.73978   1.000 34.68149 ? 224 LEU A N   1 
ATOM   1770 C CA  . LEU A 1 224 ? 7.51549  11.99559 6.11542   1.000 31.66686 ? 224 LEU A CA  1 
ATOM   1771 C C   . LEU A 1 224 ? 7.59660  11.37471 4.72275   1.000 31.79191 ? 224 LEU A C   1 
ATOM   1772 O O   . LEU A 1 224 ? 8.30753  11.89161 3.85936   1.000 34.58176 ? 224 LEU A O   1 
ATOM   1773 C CB  . LEU A 1 224 ? 6.98140  13.41988 6.01371   1.000 35.53502 ? 224 LEU A CB  1 
ATOM   1774 C CG  . LEU A 1 224 ? 5.59526  13.59643 5.39132   1.000 41.94015 ? 224 LEU A CG  1 
ATOM   1775 C CD1 . LEU A 1 224 ? 4.50779  13.08173 6.33754   1.000 44.18800 ? 224 LEU A CD1 1 
ATOM   1776 C CD2 . LEU A 1 224 ? 5.36174  15.06229 5.03459   1.000 44.64934 ? 224 LEU A CD2 1 
ATOM   1777 N N   . SER A 1 225 ? 6.85722  10.29061 4.49646   1.000 32.22212 ? 225 SER A N   1 
ATOM   1778 C CA  . SER A 1 225 ? 6.86973  9.59153  3.21784   1.000 34.85577 ? 225 SER A CA  1 
ATOM   1779 C C   . SER A 1 225 ? 5.51949  9.74378  2.53495   1.000 33.59828 ? 225 SER A C   1 
ATOM   1780 O O   . SER A 1 225 ? 4.48381  9.42839  3.12942   1.000 36.46723 ? 225 SER A O   1 
ATOM   1781 C CB  . SER A 1 225 ? 7.19078  8.10972  3.40159   1.000 39.46016 ? 225 SER A CB  1 
ATOM   1782 O OG  . SER A 1 225 ? 7.44800  7.49896  2.14818   1.000 41.14535 ? 225 SER A OG  1 
ATOM   1783 N N   . ILE A 1 226 ? 5.53087  10.18813 1.27683   1.000 33.73606 ? 226 ILE A N   1 
ATOM   1784 C CA  . ILE A 1 226 ? 4.30616  10.50139 0.55300   1.000 35.92925 ? 226 ILE A CA  1 
ATOM   1785 C C   . ILE A 1 226 ? 4.35848  9.86373  -0.82815  1.000 35.08580 ? 226 ILE A C   1 
ATOM   1786 O O   . ILE A 1 226 ? 5.40339  9.87151  -1.48886  1.000 34.43307 ? 226 ILE A O   1 
ATOM   1787 C CB  . ILE A 1 226 ? 4.09835  12.02751 0.44556   1.000 39.24656 ? 226 ILE A CB  1 
ATOM   1788 C CG1 . ILE A 1 226 ? 3.81727  12.62669 1.82852   1.000 41.97921 ? 226 ILE A CG1 1 
ATOM   1789 C CG2 . ILE A 1 226 ? 2.96301  12.36354 -0.51941  1.000 38.97975 ? 226 ILE A CG2 1 
ATOM   1790 C CD1 . ILE A 1 226 ? 3.75140  14.14296 1.82485   1.000 42.94127 ? 226 ILE A CD1 1 
ATOM   1791 N N   . LEU A 1 227 ? 3.23045  9.30242  -1.25526  1.000 35.83112 ? 227 LEU A N   1 
ATOM   1792 C CA  . LEU A 1 227 ? 3.10049  8.79055  -2.61311  1.000 35.62025 ? 227 LEU A CA  1 
ATOM   1793 C C   . LEU A 1 227 ? 2.73156  9.92740  -3.55502  1.000 37.37047 ? 227 LEU A C   1 
ATOM   1794 O O   . LEU A 1 227 ? 1.73441  10.62619 -3.33865  1.000 41.11322 ? 227 LEU A O   1 
ATOM   1795 C CB  . LEU A 1 227 ? 2.03610  7.69526  -2.68015  1.000 37.08112 ? 227 LEU A CB  1 
ATOM   1796 C CG  . LEU A 1 227 ? 1.76136  7.10946  -4.06566  1.000 37.51821 ? 227 LEU A CG  1 
ATOM   1797 C CD1 . LEU A 1 227 ? 2.98954  6.38921  -4.58870  1.000 38.74099 ? 227 LEU A CD1 1 
ATOM   1798 C CD2 . LEU A 1 227 ? 0.56728  6.17977  -4.00646  1.000 39.51866 ? 227 LEU A CD2 1 
ATOM   1799 N N   . HIS A 1 228 ? 3.52814  10.11114 -4.60140  1.000 36.22972 ? 228 HIS A N   1 
ATOM   1800 C CA  . HIS A 1 228 ? 3.23309  11.08316 -5.64434  1.000 36.39060 ? 228 HIS A CA  1 
ATOM   1801 C C   . HIS A 1 228 ? 2.92585  10.34533 -6.93431  1.000 36.42798 ? 228 HIS A C   1 
ATOM   1802 O O   . HIS A 1 228 ? 3.69953  9.48494  -7.36270  1.000 34.90367 ? 228 HIS A O   1 
ATOM   1803 C CB  . HIS A 1 228 ? 4.40332  12.04824 -5.84528  1.000 37.49350 ? 228 HIS A CB  1 
ATOM   1804 C CG  . HIS A 1 228 ? 4.68827  12.90062 -4.64871  1.000 37.23918 ? 228 HIS A CG  1 
ATOM   1805 N ND1 . HIS A 1 228 ? 4.29900  14.22001 -4.56732  1.000 35.89863 ? 228 HIS A ND1 1 
ATOM   1806 C CD2 . HIS A 1 228 ? 5.31550  12.61902 -3.48061  1.000 37.97647 ? 228 HIS A CD2 1 
ATOM   1807 C CE1 . HIS A 1 228 ? 4.67889  14.71643 -3.40192  1.000 36.90348 ? 228 HIS A CE1 1 
ATOM   1808 N NE2 . HIS A 1 228 ? 5.29109  13.76320 -2.72016  1.000 37.59336 ? 228 HIS A NE2 1 
ATOM   1809 N N   . ARG A 1 229 ? 1.79389  10.67058 -7.53715  1.000 36.58393 ? 229 ARG A N   1 
ATOM   1810 C CA  . ARG A 1 229 ? 1.37750  10.04547 -8.77677  1.000 37.89705 ? 229 ARG A CA  1 
ATOM   1811 C C   . ARG A 1 229 ? 1.54692  11.02397 -9.92528  1.000 40.22353 ? 229 ARG A C   1 
ATOM   1812 O O   . ARG A 1 229 ? 1.47263  12.24160 -9.74375  1.000 40.99866 ? 229 ARG A O   1 
ATOM   1813 C CB  . ARG A 1 229 ? -0.08016 9.57221  -8.70648  1.000 38.65298 ? 229 ARG A CB  1 
ATOM   1814 C CG  . ARG A 1 229 ? -0.29139 8.40901  -7.75950  1.000 42.42430 ? 229 ARG A CG  1 
ATOM   1815 C CD  . ARG A 1 229 ? -1.76088 8.01447  -7.69651  0.800 46.62253 ? 229 ARG A CD  1 
ATOM   1816 N NE  . ARG A 1 229 ? -2.02834 7.08040  -6.60969  0.700 51.38554 ? 229 ARG A NE  1 
ATOM   1817 C CZ  . ARG A 1 229 ? -1.68686 5.79931  -6.62523  0.700 55.45811 ? 229 ARG A CZ  1 
ATOM   1818 N NH1 . ARG A 1 229 ? -1.04948 5.26689  -7.65501  0.700 57.49298 ? 229 ARG A NH1 1 
ATOM   1819 N NH2 . ARG A 1 229 ? -1.98630 5.03476  -5.57881  0.700 56.58823 ? 229 ARG A NH2 1 
ATOM   1820 N N   . ASP A 1 230 ? 1.79784  10.47103 -11.10819 1.000 41.19507 ? 230 ASP A N   1 
ATOM   1821 C CA  . ASP A 1 230 ? 1.88604  11.25583 -12.33448 1.000 42.69443 ? 230 ASP A CA  1 
ATOM   1822 C C   . ASP A 1 230 ? 2.94099  12.35130 -12.19646 1.000 40.61359 ? 230 ASP A C   1 
ATOM   1823 O O   . ASP A 1 230 ? 2.69376  13.52614 -12.47365 1.000 40.47829 ? 230 ASP A O   1 
ATOM   1824 C CB  . ASP A 1 230 ? 0.52136  11.83842 -12.70297 1.000 45.19277 ? 230 ASP A CB  1 
ATOM   1825 C CG  . ASP A 1 230 ? 0.51736  12.49745 -14.06565 1.000 49.84141 ? 230 ASP A CG  1 
ATOM   1826 O OD1 . ASP A 1 230 ? 1.13272  11.93904 -15.00585 1.000 51.45374 ? 230 ASP A OD1 1 
ATOM   1827 O OD2 . ASP A 1 230 ? -0.10964 13.57207 -14.19562 1.000 51.31328 ? 230 ASP A OD2 1 
ATOM   1828 N N   . VAL A 1 231 ? 4.12814  11.94866 -11.74734 1.000 37.68749 ? 231 VAL A N   1 
ATOM   1829 C CA  . VAL A 1 231 ? 5.25230  12.86188 -11.58828 1.000 35.28491 ? 231 VAL A CA  1 
ATOM   1830 C C   . VAL A 1 231 ? 5.93516  13.06576 -12.93096 1.000 35.81382 ? 231 VAL A C   1 
ATOM   1831 O O   . VAL A 1 231 ? 6.17280  12.11003 -13.67953 1.000 37.13636 ? 231 VAL A O   1 
ATOM   1832 C CB  . VAL A 1 231 ? 6.23704  12.32080 -10.53918 1.000 35.31432 ? 231 VAL A CB  1 
ATOM   1833 C CG1 . VAL A 1 231 ? 7.52742  13.11241 -10.57773 1.000 33.69820 ? 231 VAL A CG1 1 
ATOM   1834 C CG2 . VAL A 1 231 ? 5.60393  12.37726 -9.15240  1.000 35.78787 ? 231 VAL A CG2 1 
ATOM   1835 N N   . GLN A 1 232 ? 6.23953  14.32319 -13.24802 1.000 35.57520 ? 232 GLN A N   1 
ATOM   1836 C CA  . GLN A 1 232 ? 7.03635  14.65207 -14.42109 1.000 36.63493 ? 232 GLN A CA  1 
ATOM   1837 C C   . GLN A 1 232 ? 8.47909  14.96143 -14.07117 1.000 35.73321 ? 232 GLN A C   1 
ATOM   1838 O O   . GLN A 1 232 ? 9.35847  14.80262 -14.92370 1.000 36.88715 ? 232 GLN A O   1 
ATOM   1839 C CB  . GLN A 1 232 ? 6.43845  15.85688 -15.16372 1.000 37.14887 ? 232 GLN A CB  1 
ATOM   1840 N N   . GLU A 1 233 ? 8.73637  15.39096 -12.83973 1.000 34.32258 ? 233 GLU A N   1 
ATOM   1841 C CA  . GLU A 1 233 ? 10.06590 15.84155 -12.46238 1.000 32.38640 ? 233 GLU A CA  1 
ATOM   1842 C C   . GLU A 1 233 ? 10.14323 15.94157 -10.95379 1.000 28.53996 ? 233 GLU A C   1 
ATOM   1843 O O   . GLU A 1 233 ? 9.18763  16.38541 -10.30991 1.000 28.59801 ? 233 GLU A O   1 
ATOM   1844 C CB  . GLU A 1 233 ? 10.36815 17.20974 -13.07409 1.000 36.48830 ? 233 GLU A CB  1 
ATOM   1845 C CG  . GLU A 1 233 ? 11.78139 17.65780 -12.90320 1.000 38.47331 ? 233 GLU A CG  1 
ATOM   1846 C CD  . GLU A 1 233 ? 12.02095 19.01458 -13.51394 1.000 40.85205 ? 233 GLU A CD  1 
ATOM   1847 O OE1 . GLU A 1 233 ? 11.03227 19.70468 -13.81401 1.000 41.85509 ? 233 GLU A OE1 1 
ATOM   1848 O OE2 . GLU A 1 233 ? 13.19412 19.39107 -13.69819 1.000 42.01718 ? 233 GLU A OE2 1 
ATOM   1849 N N   . ILE A 1 234 ? 11.28327 15.53167 -10.40688 1.000 26.26457 ? 234 ILE A N   1 
ATOM   1850 C CA  . ILE A 1 234 ? 11.66892 15.85121 -9.03609  1.000 24.88839 ? 234 ILE A CA  1 
ATOM   1851 C C   . ILE A 1 234 ? 12.93979 16.66898 -9.12409  1.000 25.79671 ? 234 ILE A C   1 
ATOM   1852 O O   . ILE A 1 234 ? 13.89306 16.24556 -9.78422  1.000 28.62191 ? 234 ILE A O   1 
ATOM   1853 C CB  . ILE A 1 234 ? 11.89960 14.59380 -8.18459  1.000 25.74719 ? 234 ILE A CB  1 
ATOM   1854 C CG1 . ILE A 1 234 ? 10.63155 13.74072 -8.14342  1.000 27.51277 ? 234 ILE A CG1 1 
ATOM   1855 C CG2 . ILE A 1 234 ? 12.34600 15.00602 -6.76926  1.000 26.55577 ? 234 ILE A CG2 1 
ATOM   1856 C CD1 . ILE A 1 234 ? 10.89212 12.28512 -7.79721  1.000 29.73031 ? 234 ILE A CD1 1 
ATOM   1857 N N   . ARG A 1 235 ? 12.95050 17.84185 -8.48734  1.000 22.47542 ? 235 ARG A N   1 
ATOM   1858 C CA  . ARG A 1 235 ? 14.07383 18.77098 -8.58996  1.000 23.84209 ? 235 ARG A CA  1 
ATOM   1859 C C   . ARG A 1 235 ? 14.63896 19.05874 -7.21228  1.000 22.64262 ? 235 ARG A C   1 
ATOM   1860 O O   . ARG A 1 235 ? 13.89500 19.46539 -6.30907  1.000 25.31192 ? 235 ARG A O   1 
ATOM   1861 C CB  . ARG A 1 235 ? 13.65889 20.08629 -9.23863  1.000 27.20042 ? 235 ARG A CB  1 
ATOM   1862 C CG  . ARG A 1 235 ? 13.21632 19.93218 -10.65850 0.900 31.62246 ? 235 ARG A CG  1 
ATOM   1863 C CD  . ARG A 1 235 ? 12.59709 21.22023 -11.17199 0.800 35.95481 ? 235 ARG A CD  1 
ATOM   1864 N NE  . ARG A 1 235 ? 13.54054 22.32768 -11.21930 0.700 39.99632 ? 235 ARG A NE  1 
ATOM   1865 C CZ  . ARG A 1 235 ? 14.31821 22.59749 -12.25889 0.700 43.60498 ? 235 ARG A CZ  1 
ATOM   1866 N NH1 . ARG A 1 235 ? 14.29515 21.84946 -13.35134 0.700 44.12134 ? 235 ARG A NH1 1 
ATOM   1867 N NH2 . ARG A 1 235 ? 15.14841 23.63573 -12.19689 0.700 45.09095 ? 235 ARG A NH2 1 
ATOM   1868 N N   . TYR A 1 236 ? 15.95052 18.89678 -7.07941  1.000 21.27892 ? 236 TYR A N   1 
ATOM   1869 C CA  . TYR A 1 236 ? 16.67536 19.13187 -5.83452  1.000 20.48699 ? 236 TYR A CA  1 
ATOM   1870 C C   . TYR A 1 236 ? 17.60824 20.32282 -5.99174  1.000 21.40815 ? 236 TYR A C   1 
ATOM   1871 O O   . TYR A 1 236 ? 18.32402 20.42440 -6.98921  1.000 22.45856 ? 236 TYR A O   1 
ATOM   1872 C CB  . TYR A 1 236 ? 17.51657 17.90994 -5.44485  1.000 20.60690 ? 236 TYR A CB  1 
ATOM   1873 C CG  . TYR A 1 236 ? 16.69908 16.69327 -5.12407  1.000 23.35169 ? 236 TYR A CG  1 
ATOM   1874 C CD1 . TYR A 1 236 ? 15.82174 16.69048 -4.04187  0.900 25.01537 ? 236 TYR A CD1 1 
ATOM   1875 C CD2 . TYR A 1 236 ? 16.81928 15.53628 -5.87281  0.800 25.22893 ? 236 TYR A CD2 1 
ATOM   1876 C CE1 . TYR A 1 236 ? 15.08106 15.56927 -3.73367  0.800 25.59759 ? 236 TYR A CE1 1 
ATOM   1877 C CE2 . TYR A 1 236 ? 16.08301 14.41700 -5.56303  0.700 28.41492 ? 236 TYR A CE2 1 
ATOM   1878 C CZ  . TYR A 1 236 ? 15.21994 14.44266 -4.49898  0.700 28.87337 ? 236 TYR A CZ  1 
ATOM   1879 O OH  . TYR A 1 236 ? 14.49054 13.32292 -4.20545  0.700 35.95111 ? 236 TYR A OH  1 
ATOM   1880 N N   . GLU A 1 237 ? 17.64517 21.19304 -4.98668  1.000 21.86088 ? 237 GLU A N   1 
ATOM   1881 C CA  . GLU A 1 237 ? 18.62286 22.27025 -4.94637  1.000 22.29057 ? 237 GLU A CA  1 
ATOM   1882 C C   . GLU A 1 237 ? 18.79706 22.69725 -3.50232  1.000 22.14571 ? 237 GLU A C   1 
ATOM   1883 O O   . GLU A 1 237 ? 17.86819 22.58100 -2.70498  1.000 22.46427 ? 237 GLU A O   1 
ATOM   1884 C CB  . GLU A 1 237 ? 18.20529 23.48237 -5.78480  1.000 25.38757 ? 237 GLU A CB  1 
ATOM   1885 C CG  . GLU A 1 237 ? 16.86618 24.07227 -5.47125  0.800 28.22174 ? 237 GLU A CG  1 
ATOM   1886 C CD  . GLU A 1 237 ? 16.24180 24.73327 -6.70082  0.700 31.15798 ? 237 GLU A CD  1 
ATOM   1887 O OE1 . GLU A 1 237 ? 16.83077 25.69471 -7.23609  0.700 31.56411 ? 237 GLU A OE1 1 
ATOM   1888 O OE2 . GLU A 1 237 ? 15.17732 24.26958 -7.15877  0.700 33.19293 ? 237 GLU A OE2 1 
ATOM   1889 N N   . VAL A 1 238 ? 19.98111 23.22010 -3.18678  1.000 21.99045 ? 238 VAL A N   1 
ATOM   1890 C CA  . VAL A 1 238 ? 20.18714 23.80310 -1.86510  1.000 21.36017 ? 238 VAL A CA  1 
ATOM   1891 C C   . VAL A 1 238 ? 19.24438 24.98041 -1.68696  1.000 23.19261 ? 238 VAL A C   1 
ATOM   1892 O O   . VAL A 1 238 ? 19.14796 25.87220 -2.54408  1.000 25.45101 ? 238 VAL A O   1 
ATOM   1893 C CB  . VAL A 1 238 ? 21.65241 24.21087 -1.67114  1.000 21.42071 ? 238 VAL A CB  1 
ATOM   1894 C CG1 . VAL A 1 238 ? 21.85450 24.83637 -0.27214  1.000 22.77654 ? 238 VAL A CG1 1 
ATOM   1895 C CG2 . VAL A 1 238 ? 22.55560 23.00400 -1.84555  1.000 22.94912 ? 238 VAL A CG2 1 
ATOM   1896 N N   . SER A 1 239 ? 18.51922 24.97573 -0.57592  1.000 23.07259 ? 239 SER A N   1 
ATOM   1897 C CA  . SER A 1 239 ? 17.53598 26.00955 -0.31648  1.000 23.64403 ? 239 SER A CA  1 
ATOM   1898 C C   . SER A 1 239 ? 18.20897 27.34738 -0.01352  1.000 27.46946 ? 239 SER A C   1 
ATOM   1899 O O   . SER A 1 239 ? 19.35105 27.40893 0.45691   1.000 28.08324 ? 239 SER A O   1 
ATOM   1900 C CB  . SER A 1 239 ? 16.65735 25.58908 0.86919   1.000 23.96515 ? 239 SER A CB  1 
ATOM   1901 O OG  . SER A 1 239 ? 15.74751 26.62092 1.23666   1.000 25.76409 ? 239 SER A OG  1 
ATOM   1902 N N   . ALA A 1 240 ? 17.48924 28.43344 -0.30294  1.000 28.38550 ? 240 ALA A N   1 
ATOM   1903 C CA  . ALA A 1 240 ? 17.91529 29.73788 0.18999   1.000 29.85019 ? 240 ALA A CA  1 
ATOM   1904 C C   . ALA A 1 240 ? 17.64226 29.89212 1.67623   1.000 31.41184 ? 240 ALA A C   1 
ATOM   1905 O O   . ALA A 1 240 ? 18.23763 30.76027 2.32098   1.000 34.45370 ? 240 ALA A O   1 
ATOM   1906 C CB  . ALA A 1 240 ? 17.22544 30.85215 -0.59256  1.000 32.27793 ? 240 ALA A CB  1 
ATOM   1907 N N   . LYS A 1 241 ? 16.77168 29.06394 2.23126   1.000 31.01220 ? 241 LYS A N   1 
ATOM   1908 C CA  . LYS A 1 241 ? 16.43387 29.12954 3.64673   1.000 30.00112 ? 241 LYS A CA  1 
ATOM   1909 C C   . LYS A 1 241 ? 17.43673 28.34046 4.47427   1.000 29.81865 ? 241 LYS A C   1 
ATOM   1910 O O   . LYS A 1 241 ? 18.03591 27.36757 4.00628   1.000 28.65912 ? 241 LYS A O   1 
ATOM   1911 C CB  . LYS A 1 241 ? 15.02713 28.58696 3.87924   1.000 30.40545 ? 241 LYS A CB  1 
ATOM   1912 C CG  . LYS A 1 241 ? 13.96327 29.36918 3.14613   0.900 33.79866 ? 241 LYS A CG  1 
ATOM   1913 C CD  . LYS A 1 241 ? 12.63850 28.63516 3.18613   0.800 37.14695 ? 241 LYS A CD  1 
ATOM   1914 C CE  . LYS A 1 241 ? 11.54179 29.45560 2.52513   0.700 39.21345 ? 241 LYS A CE  1 
ATOM   1915 N NZ  . LYS A 1 241 ? 10.36458 28.62710 2.14595   0.700 42.12617 ? 241 LYS A NZ  1 
ATOM   1916 N N   . LYS A 1 242 ? 17.60628 28.75846 5.72634   1.000 29.21653 ? 242 LYS A N   1 
ATOM   1917 C CA  . LYS A 1 242 ? 18.51401 28.08565 6.63687   1.000 28.83764 ? 242 LYS A CA  1 
ATOM   1918 C C   . LYS A 1 242 ? 17.79832 27.84621 7.95018   1.000 27.67651 ? 242 LYS A C   1 
ATOM   1919 O O   . LYS A 1 242 ? 16.84898 28.55575 8.28896   1.000 28.09553 ? 242 LYS A O   1 
ATOM   1920 C CB  . LYS A 1 242 ? 19.77789 28.90129 6.90948   0.900 30.93852 ? 242 LYS A CB  1 
ATOM   1921 C CG  . LYS A 1 242 ? 20.55213 29.27859 5.67421   0.800 33.14008 ? 242 LYS A CG  1 
ATOM   1922 C CD  . LYS A 1 242 ? 21.99944 29.58845 6.01486   0.700 36.95841 ? 242 LYS A CD  1 
ATOM   1923 C CE  . LYS A 1 242 ? 22.90952 28.44607 5.59545   0.700 39.64813 ? 242 LYS A CE  1 
ATOM   1924 N NZ  . LYS A 1 242 ? 24.01515 28.22512 6.56346   0.700 40.08733 ? 242 LYS A NZ  1 
ATOM   1925 N N   . ILE A 1 243 ? 18.24943 26.83369 8.67573   1.000 25.56982 ? 243 ILE A N   1 
ATOM   1926 C CA  . ILE A 1 243 ? 17.80984 26.62346 10.05071  1.000 23.97395 ? 243 ILE A CA  1 
ATOM   1927 C C   . ILE A 1 243 ? 18.82378 27.26426 10.98326  1.000 24.84498 ? 243 ILE A C   1 
ATOM   1928 O O   . ILE A 1 243 ? 20.03761 27.18073 10.76521  1.000 25.77560 ? 243 ILE A O   1 
ATOM   1929 C CB  . ILE A 1 243 ? 17.61355 25.13107 10.37965  1.000 23.53127 ? 243 ILE A CB  1 
ATOM   1930 C CG1 . ILE A 1 243 ? 17.05849 24.98308 11.81066  1.000 24.09386 ? 243 ILE A CG1 1 
ATOM   1931 C CG2 . ILE A 1 243 ? 18.90282 24.35311 10.22356  1.000 23.78592 ? 243 ILE A CG2 1 
ATOM   1932 C CD1 . ILE A 1 243 ? 16.90003 23.53989 12.25495  1.000 24.92629 ? 243 ILE A CD1 1 
ATOM   1933 N N   . HIS A 1 244 ? 18.32558 27.91164 12.02681  1.000 25.23084 ? 244 HIS A N   1 
ATOM   1934 C CA  . HIS A 1 244 ? 19.17225 28.59652 12.99110  1.000 25.04360 ? 244 HIS A CA  1 
ATOM   1935 C C   . HIS A 1 244 ? 19.08524 27.88832 14.33433  1.000 26.02063 ? 244 HIS A C   1 
ATOM   1936 O O   . HIS A 1 244 ? 17.98625 27.57750 14.80468  1.000 26.26201 ? 244 HIS A O   1 
ATOM   1937 C CB  . HIS A 1 244 ? 18.75019 30.05706 13.14659  1.000 28.83766 ? 244 HIS A CB  1 
ATOM   1938 C CG  . HIS A 1 244 ? 18.68209 30.80708 11.85339  1.000 32.41268 ? 244 HIS A CG  1 
ATOM   1939 N ND1 . HIS A 1 244 ? 19.79836 31.32908 11.23536  1.000 34.12664 ? 244 HIS A ND1 1 
ATOM   1940 C CD2 . HIS A 1 244 ? 17.62851 31.14068 11.07187  1.000 34.83820 ? 244 HIS A CD2 1 
ATOM   1941 C CE1 . HIS A 1 244 ? 19.43689 31.94212 10.12150  1.000 34.07856 ? 244 HIS A CE1 1 
ATOM   1942 N NE2 . HIS A 1 244 ? 18.12570 31.83880 9.99677   1.000 35.03005 ? 244 HIS A NE2 1 
ATOM   1943 N N   . PHE A 1 245 ? 20.23896 27.63074 14.93454  1.000 25.78280 ? 245 PHE A N   1 
ATOM   1944 C CA  . PHE A 1 245 ? 20.33861 27.05544 16.27090  1.000 28.15979 ? 245 PHE A CA  1 
ATOM   1945 C C   . PHE A 1 245 ? 20.80204 28.12080 17.24931  1.000 29.88457 ? 245 PHE A C   1 
ATOM   1946 O O   . PHE A 1 245 ? 21.65141 28.95188 16.91771  1.000 32.24915 ? 245 PHE A O   1 
ATOM   1947 C CB  . PHE A 1 245 ? 21.32209 25.88386 16.28644  1.000 27.89673 ? 245 PHE A CB  1 
ATOM   1948 C CG  . PHE A 1 245 ? 20.90174 24.73336 15.42631  1.000 27.62306 ? 245 PHE A CG  1 
ATOM   1949 C CD1 . PHE A 1 245 ? 21.24433 24.68749 14.08226  1.000 27.81972 ? 245 PHE A CD1 1 
ATOM   1950 C CD2 . PHE A 1 245 ? 20.17166 23.68842 15.96260  1.000 29.17390 ? 245 PHE A CD2 1 
ATOM   1951 C CE1 . PHE A 1 245 ? 20.85333 23.62166 13.28751  1.000 29.48052 ? 245 PHE A CE1 1 
ATOM   1952 C CE2 . PHE A 1 245 ? 19.78521 22.62309 15.17983  1.000 30.30759 ? 245 PHE A CE2 1 
ATOM   1953 C CZ  . PHE A 1 245 ? 20.12504 22.58629 13.83407  1.000 30.87794 ? 245 PHE A CZ  1 
ATOM   1954 N N   . ALA A 1 246 ? 20.24873 28.09594 18.46011  1.000 31.45504 ? 246 ALA A N   1 
ATOM   1955 C CA  . ALA A 1 246 ? 20.83132 28.86781 19.54525  1.000 32.07359 ? 246 ALA A CA  1 
ATOM   1956 C C   . ALA A 1 246 ? 21.98709 28.07007 20.13310  1.000 34.58266 ? 246 ALA A C   1 
ATOM   1957 O O   . ALA A 1 246 ? 21.80448 26.91368 20.51997  1.000 36.01086 ? 246 ALA A O   1 
ATOM   1958 C CB  . ALA A 1 246 ? 19.78240 29.16234 20.62059  1.000 32.67216 ? 246 ALA A CB  1 
ATOM   1959 N N   . ARG A 1 247 ? 23.17565 28.67254 20.19733  1.000 36.05253 ? 247 ARG A N   1 
ATOM   1960 C CA  . ARG A 1 247 ? 24.34811 28.00783 20.75262  1.000 39.17994 ? 247 ARG A CA  1 
ATOM   1961 C C   . ARG A 1 247 ? 24.82758 28.76451 21.98306  1.000 41.03957 ? 247 ARG A C   1 
ATOM   1962 O O   . ARG A 1 247 ? 24.97245 29.99067 21.94954  1.000 41.45268 ? 247 ARG A O   1 
ATOM   1963 C CB  . ARG A 1 247 ? 25.47083 27.89661 19.71852  1.000 41.47013 ? 247 ARG A CB  1 
ATOM   1964 C CG  . ARG A 1 247 ? 25.16127 26.94873 18.55012  1.000 43.67565 ? 247 ARG A CG  1 
ATOM   1965 C CD  . ARG A 1 247 ? 25.56671 25.48732 18.82461  1.000 46.05345 ? 247 ARG A CD  1 
ATOM   1966 N NE  . ARG A 1 247 ? 25.54897 24.68501 17.60248  1.000 47.75077 ? 247 ARG A NE  1 
ATOM   1967 C CZ  . ARG A 1 247 ? 24.60749 23.80390 17.28813  1.000 47.55730 ? 247 ARG A CZ  1 
ATOM   1968 N NH1 . ARG A 1 247 ? 23.61356 23.52875 18.11622  1.000 48.77237 ? 247 ARG A NH1 1 
ATOM   1969 N NH2 . ARG A 1 247 ? 24.66283 23.18593 16.11111  1.000 44.91709 ? 247 ARG A NH2 1 
ATOM   1970 N N   . PHE A 1 248 ? 25.07127 28.03470 23.06752  1.000 42.97149 ? 248 PHE A N   1 
ATOM   1971 C CA  . PHE A 1 248 ? 25.50010 28.64266 24.31846  1.000 44.28964 ? 248 PHE A CA  1 
ATOM   1972 C C   . PHE A 1 248 ? 26.92385 28.28497 24.69459  1.000 44.77026 ? 248 PHE A C   1 
ATOM   1973 O O   . PHE A 1 248 ? 27.50530 28.94576 25.56619  1.000 45.21599 ? 248 PHE A O   1 
ATOM   1974 C CB  . PHE A 1 248 ? 24.55330 28.23334 25.44917  1.000 46.63912 ? 248 PHE A CB  1 
ATOM   1975 C CG  . PHE A 1 248 ? 23.16354 28.76084 25.27216  1.000 47.94688 ? 248 PHE A CG  1 
ATOM   1976 C CD1 . PHE A 1 248 ? 22.81622 30.00540 25.77133  1.000 47.24506 ? 248 PHE A CD1 1 
ATOM   1977 C CD2 . PHE A 1 248 ? 22.21337 28.03058 24.57332  1.000 48.08387 ? 248 PHE A CD2 1 
ATOM   1978 C CE1 . PHE A 1 248 ? 21.54019 30.50633 25.59731  1.000 46.16956 ? 248 PHE A CE1 1 
ATOM   1979 C CE2 . PHE A 1 248 ? 20.93701 28.52699 24.39818  1.000 47.83975 ? 248 PHE A CE2 1 
ATOM   1980 C CZ  . PHE A 1 248 ? 20.60306 29.76690 24.91089  1.000 45.84316 ? 248 PHE A CZ  1 
ATOM   1981 N N   . ARG A 1 249 ? 27.49620 27.27446 24.05185  1.000 42.97212 ? 249 ARG A N   1 
ATOM   1982 C CA  . ARG A 1 249 ? 28.84578 26.82630 24.32672  1.000 44.46987 ? 249 ARG A CA  1 
ATOM   1983 C C   . ARG A 1 249 ? 29.35765 26.13744 23.07479  1.000 43.32940 ? 249 ARG A C   1 
ATOM   1984 O O   . ARG A 1 249 ? 28.60605 25.87671 22.13020  1.000 44.09435 ? 249 ARG A O   1 
ATOM   1985 C CB  . ARG A 1 249 ? 28.88759 25.88484 25.53542  1.000 46.33348 ? 249 ARG A CB  1 
ATOM   1986 C CG  . ARG A 1 249 ? 27.90344 24.73517 25.41809  0.800 48.04906 ? 249 ARG A CG  1 
ATOM   1987 C CD  . ARG A 1 249 ? 27.81250 23.90306 26.67888  0.700 49.73584 ? 249 ARG A CD  1 
ATOM   1988 N NE  . ARG A 1 249 ? 26.76887 22.89594 26.53946  0.700 51.87538 ? 249 ARG A NE  1 
ATOM   1989 C CZ  . ARG A 1 249 ? 26.55770 21.89909 27.38772  0.600 53.93988 ? 249 ARG A CZ  1 
ATOM   1990 N NH1 . ARG A 1 249 ? 27.30352 21.74002 28.46921  0.600 54.46679 ? 249 ARG A NH1 1 
ATOM   1991 N NH2 . ARG A 1 249 ? 25.57697 21.03445 27.13969  0.600 54.51006 ? 249 ARG A NH2 1 
ATOM   1992 N N   . SER A 1 250 ? 30.64685 25.83512 23.07853  1.000 43.68175 ? 250 SER A N   1 
ATOM   1993 C CA  . SER A 1 250 ? 31.23848 25.13485 21.95432  1.000 43.22662 ? 250 SER A CA  1 
ATOM   1994 C C   . SER A 1 250 ? 30.84974 23.66375 21.99043  1.000 41.32990 ? 250 SER A C   1 
ATOM   1995 O O   . SER A 1 250 ? 31.04315 22.98235 23.00023  1.000 43.70045 ? 250 SER A O   1 
ATOM   1996 C CB  . SER A 1 250 ? 32.75534 25.28569 21.97599  1.000 46.07882 ? 250 SER A CB  1 
ATOM   1997 O OG  . SER A 1 250 ? 33.32072 24.70916 20.81628  1.000 46.61203 ? 250 SER A OG  1 
ATOM   1998 N N   . PHE A 1 251 ? 30.28467 23.18053 20.88842  1.000 38.16275 ? 251 PHE A N   1 
ATOM   1999 C CA  . PHE A 1 251 ? 30.09959 21.75096 20.65163  1.000 35.53031 ? 251 PHE A CA  1 
ATOM   2000 C C   . PHE A 1 251 ? 30.34878 21.56283 19.16755  1.000 33.34771 ? 251 PHE A C   1 
ATOM   2001 O O   . PHE A 1 251 ? 29.40948 21.47767 18.36560  1.000 33.84800 ? 251 PHE A O   1 
ATOM   2002 C CB  . PHE A 1 251 ? 28.69878 21.28186 21.05761  1.000 35.36332 ? 251 PHE A CB  1 
ATOM   2003 C CG  . PHE A 1 251 ? 28.54602 19.78259 21.11563  1.000 36.67563 ? 251 PHE A CG  1 
ATOM   2004 C CD1 . PHE A 1 251 ? 29.62868 18.94722 20.93569  1.000 37.13763 ? 251 PHE A CD1 1 
ATOM   2005 C CD2 . PHE A 1 251 ? 27.31317 19.21410 21.36458  1.000 37.52569 ? 251 PHE A CD2 1 
ATOM   2006 C CE1 . PHE A 1 251 ? 29.48850 17.57259 21.00119  1.000 34.67517 ? 251 PHE A CE1 1 
ATOM   2007 C CE2 . PHE A 1 251 ? 27.16325 17.84191 21.42601  1.000 38.39068 ? 251 PHE A CE2 1 
ATOM   2008 C CZ  . PHE A 1 251 ? 28.25623 17.01934 21.23716  1.000 37.02596 ? 251 PHE A CZ  1 
ATOM   2009 N N   . PRO A 1 252 ? 31.61538 21.52655 18.75757  1.000 30.88174 ? 252 PRO A N   1 
ATOM   2010 C CA  . PRO A 1 252 ? 31.92421 21.49857 17.32351  1.000 29.77741 ? 252 PRO A CA  1 
ATOM   2011 C C   . PRO A 1 252 ? 31.34595 20.27150 16.65247  1.000 29.16046 ? 252 PRO A C   1 
ATOM   2012 O O   . PRO A 1 252 ? 31.28663 19.18598 17.23373  1.000 29.85826 ? 252 PRO A O   1 
ATOM   2013 C CB  . PRO A 1 252 ? 33.45642 21.47069 17.28899  1.000 30.93252 ? 252 PRO A CB  1 
ATOM   2014 C CG  . PRO A 1 252 ? 33.88751 21.96339 18.63524  1.000 30.84456 ? 252 PRO A CG  1 
ATOM   2015 C CD  . PRO A 1 252 ? 32.83562 21.48910 19.58198  1.000 30.57785 ? 252 PRO A CD  1 
ATOM   2016 N N   . PHE A 1 253 ? 30.95510 20.45796 15.38795  1.000 28.47570 ? 253 PHE A N   1 
ATOM   2017 C CA  . PHE A 1 253 ? 30.40189 19.36960 14.58779  1.000 27.89582 ? 253 PHE A CA  1 
ATOM   2018 C C   . PHE A 1 253 ? 31.27511 18.12454 14.64693  1.000 25.69152 ? 253 PHE A C   1 
ATOM   2019 O O   . PHE A 1 253 ? 30.77248 17.00720 14.80321  1.000 24.07491 ? 253 PHE A O   1 
ATOM   2020 C CB  . PHE A 1 253 ? 30.24545 19.83800 13.13923  1.000 28.06478 ? 253 PHE A CB  1 
ATOM   2021 C CG  . PHE A 1 253 ? 29.69805 18.79150 12.20492  1.000 27.01629 ? 253 PHE A CG  1 
ATOM   2022 C CD1 . PHE A 1 253 ? 28.33528 18.51473 12.16041  1.000 27.91485 ? 253 PHE A CD1 1 
ATOM   2023 C CD2 . PHE A 1 253 ? 30.53998 18.10065 11.35681  1.000 27.74671 ? 253 PHE A CD2 1 
ATOM   2024 C CE1 . PHE A 1 253 ? 27.83197 17.55914 11.27738  1.000 27.82172 ? 253 PHE A CE1 1 
ATOM   2025 C CE2 . PHE A 1 253 ? 30.04065 17.15623 10.48108  1.000 28.10256 ? 253 PHE A CE2 1 
ATOM   2026 C CZ  . PHE A 1 253 ? 28.68940 16.88585 10.43906  1.000 27.52155 ? 253 PHE A CZ  1 
ATOM   2027 N N   . TRP A 1 254 ? 32.58959 18.28497 14.46611  1.000 24.79649 ? 254 TRP A N   1 
ATOM   2028 C CA  . TRP A 1 254 ? 33.42055 17.08986 14.41114  1.000 24.04423 ? 254 TRP A CA  1 
ATOM   2029 C C   . TRP A 1 254 ? 33.49861 16.40125 15.76643  1.000 23.55753 ? 254 TRP A C   1 
ATOM   2030 O O   . TRP A 1 254 ? 33.65211 15.17422 15.82130  1.000 21.98657 ? 254 TRP A O   1 
ATOM   2031 C CB  . TRP A 1 254 ? 34.82001 17.42168 13.88469  1.000 25.15531 ? 254 TRP A CB  1 
ATOM   2032 C CG  . TRP A 1 254 ? 34.82242 17.88594 12.43968  1.000 24.27625 ? 254 TRP A CG  1 
ATOM   2033 C CD1 . TRP A 1 254 ? 35.30073 19.07586 11.96351  1.000 24.78881 ? 254 TRP A CD1 1 
ATOM   2034 C CD2 . TRP A 1 254 ? 34.30567 17.17583 11.29470  1.000 23.17789 ? 254 TRP A CD2 1 
ATOM   2035 N NE1 . TRP A 1 254 ? 35.11470 19.15003 10.59797  1.000 24.22398 ? 254 TRP A NE1 1 
ATOM   2036 C CE2 . TRP A 1 254 ? 34.51252 18.00037 10.16259  1.000 24.62003 ? 254 TRP A CE2 1 
ATOM   2037 C CE3 . TRP A 1 254 ? 33.69298 15.93073 11.11808  1.000 24.58395 ? 254 TRP A CE3 1 
ATOM   2038 C CZ2 . TRP A 1 254 ? 34.14140 17.61191 8.86480   1.000 25.89718 ? 254 TRP A CZ2 1 
ATOM   2039 C CZ3 . TRP A 1 254 ? 33.31844 15.54475 9.82284   1.000 25.41605 ? 254 TRP A CZ3 1 
ATOM   2040 C CH2 . TRP A 1 254 ? 33.54687 16.38959 8.71879   1.000 25.88335 ? 254 TRP A CH2 1 
ATOM   2041 N N   . ARG A 1 255 ? 33.39288 17.16049 16.86579  1.000 24.75069 ? 255 ARG A N   1 
ATOM   2042 C CA  . ARG A 1 255 ? 33.27784 16.52103 18.17471  1.000 25.70356 ? 255 ARG A CA  1 
ATOM   2043 C C   . ARG A 1 255 ? 31.93517 15.80582 18.31077  1.000 27.15760 ? 255 ARG A C   1 
ATOM   2044 O O   . ARG A 1 255 ? 31.86222 14.68982 18.84089  1.000 26.54664 ? 255 ARG A O   1 
ATOM   2045 C CB  . ARG A 1 255 ? 33.46668 17.55878 19.29331  1.000 27.03959 ? 255 ARG A CB  1 
ATOM   2046 C CG  . ARG A 1 255 ? 33.27824 16.98846 20.68479  1.000 28.98618 ? 255 ARG A CG  1 
ATOM   2047 C CD  . ARG A 1 255 ? 34.16429 17.70514 21.71854  0.800 31.53546 ? 255 ARG A CD  1 
ATOM   2048 N NE  . ARG A 1 255 ? 35.48732 17.09032 21.76536  0.600 33.58319 ? 255 ARG A NE  1 
ATOM   2049 C CZ  . ARG A 1 255 ? 36.61052 17.71200 22.09492  0.600 35.45807 ? 255 ARG A CZ  1 
ATOM   2050 N NH1 . ARG A 1 255 ? 36.62380 18.99418 22.43258  0.600 35.70599 ? 255 ARG A NH1 1 
ATOM   2051 N NH2 . ARG A 1 255 ? 37.75204 17.03083 22.08299  0.600 36.33251 ? 255 ARG A NH2 1 
ATOM   2052 N N   . ARG A 1 256 ? 30.86917 16.42262 17.79752  1.000 26.25056 ? 256 ARG A N   1 
ATOM   2053 C CA  . ARG A 1 256 ? 29.56586 15.77859 17.75925  1.000 27.04909 ? 256 ARG A CA  1 
ATOM   2054 C C   . ARG A 1 256 ? 29.62654 14.45511 16.99716  1.000 25.30935 ? 256 ARG A C   1 
ATOM   2055 O O   . ARG A 1 256 ? 29.05064 13.45204 17.42638  1.000 26.30146 ? 256 ARG A O   1 
ATOM   2056 C CB  . ARG A 1 256 ? 28.57707 16.75110 17.11976  1.000 30.38569 ? 256 ARG A CB  1 
ATOM   2057 C CG  . ARG A 1 256 ? 27.09770 16.44685 17.26438  1.000 32.19951 ? 256 ARG A CG  1 
ATOM   2058 C CD  . ARG A 1 256 ? 26.28136 17.41850 16.38443  0.800 30.50502 ? 256 ARG A CD  1 
ATOM   2059 N NE  . ARG A 1 256 ? 26.41344 18.82275 16.76162  0.700 30.18627 ? 256 ARG A NE  1 
ATOM   2060 C CZ  . ARG A 1 256 ? 25.71751 19.39425 17.73992  0.600 33.78436 ? 256 ARG A CZ  1 
ATOM   2061 N NH1 . ARG A 1 256 ? 24.85289 18.70318 18.46489  0.600 34.69840 ? 256 ARG A NH1 1 
ATOM   2062 N NH2 . ARG A 1 256 ? 25.89289 20.69068 17.99939  0.600 32.81899 ? 256 ARG A NH2 1 
ATOM   2063 N N   . VAL A 1 257 ? 30.32439 14.43780 15.85680  1.000 23.95007 ? 257 VAL A N   1 
ATOM   2064 C CA  . VAL A 1 257 ? 30.48349 13.20645 15.09152  1.000 22.68469 ? 257 VAL A CA  1 
ATOM   2065 C C   . VAL A 1 257 ? 31.26750 12.17924 15.88876  1.000 24.15458 ? 257 VAL A C   1 
ATOM   2066 O O   . VAL A 1 257 ? 30.89853 10.99996 15.94600  1.000 24.00521 ? 257 VAL A O   1 
ATOM   2067 C CB  . VAL A 1 257 ? 31.16448 13.51468 13.74676  1.000 22.06695 ? 257 VAL A CB  1 
ATOM   2068 C CG1 . VAL A 1 257 ? 31.60844 12.22390 13.03193  1.000 21.25350 ? 257 VAL A CG1 1 
ATOM   2069 C CG2 . VAL A 1 257 ? 30.23198 14.33564 12.87437  1.000 21.99259 ? 257 VAL A CG2 1 
ATOM   2070 N N   . HIS A 1 258 ? 32.36830 12.61092 16.50944  1.000 24.99064 ? 258 HIS A N   1 
ATOM   2071 C CA  . HIS A 1 258 ? 33.15747 11.71021 17.34374  1.000 24.37703 ? 258 HIS A CA  1 
ATOM   2072 C C   . HIS A 1 258 ? 32.29511 11.08211 18.43186  1.000 24.93412 ? 258 HIS A C   1 
ATOM   2073 O O   . HIS A 1 258 ? 32.31162 9.86159  18.64431  1.000 25.61463 ? 258 HIS A O   1 
ATOM   2074 C CB  . HIS A 1 258 ? 34.30997 12.47990 17.97839  1.000 23.07051 ? 258 HIS A CB  1 
ATOM   2075 C CG  . HIS A 1 258 ? 35.08774 11.68454 18.98356  1.000 24.56134 ? 258 HIS A CG  1 
ATOM   2076 N ND1 . HIS A 1 258 ? 34.76301 11.64721 20.32882  1.000 27.98456 ? 258 HIS A ND1 1 
ATOM   2077 C CD2 . HIS A 1 258 ? 36.18044 10.89969 18.83816  1.000 24.15115 ? 258 HIS A CD2 1 
ATOM   2078 C CE1 . HIS A 1 258 ? 35.62996 10.87732 20.96563  1.000 26.99329 ? 258 HIS A CE1 1 
ATOM   2079 N NE2 . HIS A 1 258 ? 36.50286 10.41653 20.08484  1.000 28.77768 ? 258 HIS A NE2 1 
ATOM   2080 N N   . ASP A 1 259 ? 31.53545 11.91594 19.13830  1.000 23.85978 ? 259 ASP A N   1 
ATOM   2081 C CA  . ASP A 1 259 ? 30.76530 11.44555 20.27630  1.000 27.18303 ? 259 ASP A CA  1 
ATOM   2082 C C   . ASP A 1 259 ? 29.66701 10.48502 19.84783  1.000 28.72780 ? 259 ASP A C   1 
ATOM   2083 O O   . ASP A 1 259 ? 29.27885 9.60251  20.61558  1.000 31.60564 ? 259 ASP A O   1 
ATOM   2084 C CB  . ASP A 1 259 ? 30.17448 12.64388 21.00648  1.000 28.00870 ? 259 ASP A CB  1 
ATOM   2085 C CG  . ASP A 1 259 ? 31.21676 13.43830 21.79697  1.000 30.78811 ? 259 ASP A CG  1 
ATOM   2086 O OD1 . ASP A 1 259 ? 32.39068 13.00726 21.89060  1.000 30.45087 ? 259 ASP A OD1 1 
ATOM   2087 O OD2 . ASP A 1 259 ? 30.84092 14.51158 22.32714  1.000 32.43969 ? 259 ASP A OD2 1 
ATOM   2088 N N   . SER A 1 260 ? 29.15727 10.63059 18.62990  1.000 25.71687 ? 260 SER A N   1 
ATOM   2089 C CA  . SER A 1 260 ? 28.04344 9.80537  18.17669  1.000 26.96693 ? 260 SER A CA  1 
ATOM   2090 C C   . SER A 1 260 ? 28.47569 8.48823  17.55128  1.000 26.36971 ? 260 SER A C   1 
ATOM   2091 O O   . SER A 1 260 ? 27.71895 7.50965  17.61961  1.000 29.72467 ? 260 SER A O   1 
ATOM   2092 C CB  . SER A 1 260 ? 27.20072 10.56803 17.14802  1.000 30.17538 ? 260 SER A CB  1 
ATOM   2093 O OG  . SER A 1 260 ? 26.63800 11.72842 17.70913  1.000 32.55387 ? 260 SER A OG  1 
ATOM   2094 N N   . PHE A 1 261 ? 29.65916 8.44660  16.91816  1.000 23.95265 ? 261 PHE A N   1 
ATOM   2095 C CA  . PHE A 1 261 ? 30.08110 7.28427  16.15886  1.000 24.12928 ? 261 PHE A CA  1 
ATOM   2096 C C   . PHE A 1 261 ? 31.36115 6.63722  16.65079  1.000 26.32225 ? 261 PHE A C   1 
ATOM   2097 O O   . PHE A 1 261 ? 31.56658 5.44760  16.37125  1.000 27.62536 ? 261 PHE A O   1 
ATOM   2098 C CB  . PHE A 1 261 ? 30.26136 7.65371  14.67440  1.000 22.65592 ? 261 PHE A CB  1 
ATOM   2099 C CG  . PHE A 1 261 ? 28.97826 8.11285  14.02107  1.000 21.29207 ? 261 PHE A CG  1 
ATOM   2100 C CD1 . PHE A 1 261 ? 27.98722 7.19990  13.69186  1.000 21.81306 ? 261 PHE A CD1 1 
ATOM   2101 C CD2 . PHE A 1 261 ? 28.74637 9.45505  13.80063  1.000 23.26498 ? 261 PHE A CD2 1 
ATOM   2102 C CE1 . PHE A 1 261 ? 26.77692 7.62399  13.11133  1.000 22.89732 ? 261 PHE A CE1 1 
ATOM   2103 C CE2 . PHE A 1 261 ? 27.54719 9.89112  13.21544  1.000 23.59625 ? 261 PHE A CE2 1 
ATOM   2104 C CZ  . PHE A 1 261 ? 26.56076 8.97377  12.87635  1.000 21.72849 ? 261 PHE A CZ  1 
ATOM   2105 N N   . ILE A 1 262 ? 32.22124 7.35723  17.36596  1.000 25.10826 ? 262 ILE A N   1 
ATOM   2106 C CA  . ILE A 1 262 ? 33.51081 6.81980  17.76930  1.000 25.84159 ? 262 ILE A CA  1 
ATOM   2107 C C   . ILE A 1 262 ? 33.49780 6.39636  19.23150  1.000 30.60004 ? 262 ILE A C   1 
ATOM   2108 O O   . ILE A 1 262 ? 33.79133 5.24729  19.55358  1.000 34.13222 ? 262 ILE A O   1 
ATOM   2109 C CB  . ILE A 1 262 ? 34.63164 7.84715  17.49768  1.000 26.69746 ? 262 ILE A CB  1 
ATOM   2110 C CG1 . ILE A 1 262 ? 34.68900 8.21130  16.01188  1.000 26.68188 ? 262 ILE A CG1 1 
ATOM   2111 C CG2 . ILE A 1 262 ? 35.98877 7.30300  17.94921  1.000 28.36401 ? 262 ILE A CG2 1 
ATOM   2112 C CD1 . ILE A 1 262 ? 35.07810 7.06696  15.09778  1.000 28.86660 ? 262 ILE A CD1 1 
ATOM   2113 N N   . GLU A 1 263 ? 33.13102 7.30718  20.12830  1.000 31.87336 ? 263 GLU A N   1 
ATOM   2114 C CA  . GLU A 1 263 ? 33.10754 6.99614  21.55818  1.000 40.60516 ? 263 GLU A CA  1 
ATOM   2115 C C   . GLU A 1 263 ? 32.54059 8.17529  22.33042  1.000 45.32377 ? 263 GLU A C   1 
ATOM   2116 O O   . GLU A 1 263 ? 32.72832 9.32454  21.92526  1.000 45.87073 ? 263 GLU A O   1 
ATOM   2117 C CB  . GLU A 1 263 ? 34.51522 6.66198  22.05684  1.000 45.09280 ? 263 GLU A CB  1 
ATOM   2118 C CG  . GLU A 1 263 ? 35.58138 7.64104  21.56846  0.700 47.40690 ? 263 GLU A CG  1 
ATOM   2119 C CD  . GLU A 1 263 ? 36.93648 7.44232  22.21800  0.600 48.83592 ? 263 GLU A CD  1 
ATOM   2120 O OE1 . GLU A 1 263 ? 36.97393 6.96070  23.37045  0.600 50.16299 ? 263 GLU A OE1 1 
ATOM   2121 O OE2 . GLU A 1 263 ? 37.96330 7.77246  21.57476  0.600 48.65395 ? 263 GLU A OE2 1 
ATOM   2122 N N   . ASP A 1 264 ? 31.85617 7.91436  23.44297  1.000 51.43912 ? 264 ASP A N   1 
ATOM   2123 C CA  . ASP A 1 264 ? 31.23539 8.98503  24.23143  1.000 56.25754 ? 264 ASP A CA  1 
ATOM   2124 C C   . ASP A 1 264 ? 30.91759 8.52780  25.65237  1.000 59.37067 ? 264 ASP A C   1 
ATOM   2125 O O   . ASP A 1 264 ? 31.80278 8.10184  26.39231  1.000 61.71967 ? 264 ASP A O   1 
ATOM   2126 C CB  . ASP A 1 264 ? 29.95347 9.48486  23.55946  1.000 56.38838 ? 264 ASP A CB  1 
HETATM 2127 C C1  . CIT B 2 .   ? 31.65363 24.09933 14.41764  1.000 52.99119 ? 301 CIT A C1  1 
HETATM 2128 O O1  . CIT B 2 .   ? 31.56318 22.94878 13.94837  1.000 49.80076 ? 301 CIT A O1  1 
HETATM 2129 O O2  . CIT B 2 .   ? 32.76894 24.48010 14.85091  1.000 54.50299 ? 301 CIT A O2  1 
HETATM 2130 C C2  . CIT B 2 .   ? 30.46246 25.03041 14.47279  1.000 55.72076 ? 301 CIT A C2  1 
HETATM 2131 C C3  . CIT B 2 .   ? 29.35849 24.50298 15.39315  1.000 58.29190 ? 301 CIT A C3  1 
HETATM 2132 O O7  . CIT B 2 .   ? 29.96249 23.93807 16.58927  1.000 58.52562 ? 301 CIT A O7  1 
HETATM 2133 C C4  . CIT B 2 .   ? 28.42155 25.62549 15.83028  1.000 60.18891 ? 301 CIT A C4  1 
HETATM 2134 C C5  . CIT B 2 .   ? 29.03917 26.41692 16.97080  1.000 62.36739 ? 301 CIT A C5  1 
HETATM 2135 O O3  . CIT B 2 .   ? 29.47199 27.57939 16.77900  1.000 63.21633 ? 301 CIT A O3  1 
HETATM 2136 O O4  . CIT B 2 .   ? 29.12266 25.92942 18.12554  1.000 62.51555 ? 301 CIT A O4  1 
HETATM 2137 C C6  . CIT B 2 .   ? 28.56763 23.41626 14.67011  1.000 57.22111 ? 301 CIT A C6  1 
HETATM 2138 O O5  . CIT B 2 .   ? 28.20778 23.58789 13.48517  1.000 55.26309 ? 301 CIT A O5  1 
HETATM 2139 O O6  . CIT B 2 .   ? 28.28634 22.33066 15.23820  1.000 57.90031 ? 301 CIT A O6  1 
HETATM 2140 N N4  . UOL C 3 .   ? 17.07259 6.98500  8.33405   1.000 18.90477 ? 302 UOL A N4  1 
HETATM 2141 C C4  . UOL C 3 .   ? 18.22225 7.38558  14.30850  1.000 25.46623 ? 302 UOL A C4  1 
HETATM 2142 N N3  . UOL C 3 .   ? 14.34314 9.34920  11.99863  1.000 23.70295 ? 302 UOL A N3  1 
HETATM 2143 C C2  . UOL C 3 .   ? 16.20789 5.55508  12.39547  1.000 30.30729 ? 302 UOL A C2  1 
HETATM 2144 O O2  . UOL C 3 .   ? 19.73344 7.31571  16.24408  1.000 30.33946 ? 302 UOL A O2  1 
HETATM 2145 C C5  . UOL C 3 .   ? 19.48669 9.31722  14.15969  1.000 22.52975 ? 302 UOL A C5  1 
HETATM 2146 N N5  . UOL C 3 .   ? 16.39002 5.19642  7.15691   1.000 21.29848 ? 302 UOL A N5  1 
HETATM 2147 C C6  . UOL C 3 .   ? 18.72571 9.39321  15.47535  1.000 24.38612 ? 302 UOL A C6  1 
HETATM 2148 O O6  . UOL C 3 .   ? 17.93632 10.30046 7.97823   1.000 21.54370 ? 302 UOL A O6  1 
HETATM 2149 N N1  . UOL C 3 .   ? 16.41757 6.85216  12.68086  1.000 27.81383 ? 302 UOL A N1  1 
HETATM 2150 N N   . UOL C 3 .   ? 15.87123 5.29314  11.11045  1.000 33.07611 ? 302 UOL A N   1 
HETATM 2151 C C   . UOL C 3 .   ? 16.92709 3.11689  10.64200  1.000 37.26610 ? 302 UOL A C   1 
HETATM 2152 O O   . UOL C 3 .   ? 16.28697 4.68039  13.25268  1.000 29.49752 ? 302 UOL A O   1 
HETATM 2153 C C1  . UOL C 3 .   ? 15.65037 3.93046  10.62878  1.000 35.67108 ? 302 UOL A C1  1 
HETATM 2154 C C10 . UOL C 3 .   ? 16.08904 10.80279 12.92355  1.000 23.28558 ? 302 UOL A C10 1 
HETATM 2155 C C11 . UOL C 3 .   ? 14.65974 10.45820 12.90228  1.000 23.26680 ? 302 UOL A C11 1 
HETATM 2156 C C12 . UOL C 3 .   ? 14.22387 9.76947  10.60585  1.000 21.56305 ? 302 UOL A C12 1 
HETATM 2157 C C13 . UOL C 3 .   ? 15.58294 9.72707  9.94758   1.000 20.44400 ? 302 UOL A C13 1 
HETATM 2158 C C14 . UOL C 3 .   ? 17.06316 8.30966  8.92773   1.000 20.95904 ? 302 UOL A C14 1 
HETATM 2159 C C15 . UOL C 3 .   ? 16.80585 9.44501  7.92525   1.000 20.27636 ? 302 UOL A C15 1 
HETATM 2160 C C16 . UOL C 3 .   ? 15.54948 10.12961 8.48096   1.000 18.75444 ? 302 UOL A C16 1 
HETATM 2161 C C17 . UOL C 3 .   ? 16.07364 6.38333  7.61743   1.000 19.79226 ? 302 UOL A C17 1 
HETATM 2162 C C18 . UOL C 3 .   ? 17.69154 5.01080  7.59462   1.000 19.65625 ? 302 UOL A C18 1 
HETATM 2163 C C19 . UOL C 3 .   ? 18.12201 6.10168  8.33135   1.000 18.44465 ? 302 UOL A C19 1 
HETATM 2164 C C20 . UOL C 3 .   ? 20.11155 5.22525  8.64661   1.000 19.64784 ? 302 UOL A C20 1 
HETATM 2165 C C21 . UOL C 3 .   ? 18.62021 3.96541  7.40951   1.000 20.03677 ? 302 UOL A C21 1 
HETATM 2166 C C22 . UOL C 3 .   ? 13.24584 8.56310  12.51533  1.000 26.57840 ? 302 UOL A C22 1 
HETATM 2167 C C23 . UOL C 3 .   ? 20.45172 12.29385 12.37571  1.000 20.10475 ? 302 UOL A C23 1 
HETATM 2168 C C24 . UOL C 3 .   ? 20.79612 11.15699 13.08451  1.000 20.14614 ? 302 UOL A C24 1 
HETATM 2169 C C25 . UOL C 3 .   ? 22.94312 11.52949 12.81904  1.000 22.30182 ? 302 UOL A C25 1 
HETATM 2170 C C26 . UOL C 3 .   ? 21.50583 13.05730 11.84587  1.000 19.32617 ? 302 UOL A C26 1 
HETATM 2171 C C3  . UOL C 3 .   ? 16.73578 7.28442  14.02809  1.000 26.34703 ? 302 UOL A C3  1 
HETATM 2172 C C7  . UOL C 3 .   ? 18.54832 7.89564  15.71415  1.000 27.06901 ? 302 UOL A C7  1 
HETATM 2173 C C8  . UOL C 3 .   ? 18.62222 11.34682 12.89199  1.000 21.39356 ? 302 UOL A C8  1 
HETATM 2174 C C9  . UOL C 3 .   ? 17.27138 10.97553 12.96446  1.000 22.52276 ? 302 UOL A C9  1 
HETATM 2175 N N10 . UOL C 3 .   ? 22.03116 10.71930 13.35063  1.000 20.49801 ? 302 UOL A N10 1 
HETATM 2176 N N11 . UOL C 3 .   ? 22.76173 12.63836 12.09676  1.000 21.09905 ? 302 UOL A N11 1 
HETATM 2177 N N12 . UOL C 3 .   ? 21.32888 14.14202 11.07525  1.000 19.67510 ? 302 UOL A N12 1 
HETATM 2178 N N2  . UOL C 3 .   ? 19.61105 10.54840 13.40606  1.000 21.28564 ? 302 UOL A N2  1 
HETATM 2179 N N6  . UOL C 3 .   ? 19.32069 6.26730  8.89456   1.000 18.95409 ? 302 UOL A N6  1 
HETATM 2180 N N7  . UOL C 3 .   ? 19.84704 4.11741  7.95290   1.000 20.60349 ? 302 UOL A N7  1 
HETATM 2181 N N8  . UOL C 3 .   ? 18.34908 2.82590  6.76095   1.000 22.41808 ? 302 UOL A N8  1 
HETATM 2182 N N9  . UOL C 3 .   ? 19.07375 12.42321 12.27653  1.000 21.13262 ? 302 UOL A N9  1 
HETATM 2183 O O1  . UOL C 3 .   ? 18.80023 8.34856  13.39318  1.000 23.40241 ? 302 UOL A O1  1 
HETATM 2184 O O3  . UOL C 3 .   ? 19.47859 10.07418 16.47172  1.000 27.07603 ? 302 UOL A O3  1 
HETATM 2185 O O4  . UOL C 3 .   ? 16.04402 8.36418  9.90955   1.000 21.39650 ? 302 UOL A O4  1 
HETATM 2186 O O5  . UOL C 3 .   ? 15.58162 11.54780 8.37454   1.000 20.86432 ? 302 UOL A O5  1 
HETATM 2187 H H   . UOL C 3 .   ? 18.74428 6.45385  14.09571  1.000 30.56262 ? 302 UOL A H   1 
HETATM 2188 H H17 . UOL C 3 .   ? 19.48525 6.90200  17.11200  1.000 36.41049 ? 302 UOL A H17 1 
HETATM 2189 H H1  . UOL C 3 .   ? 20.50829 8.96333  14.29015  1.000 27.03884 ? 302 UOL A H1  1 
HETATM 2190 H H2  . UOL C 3 .   ? 17.76972 9.91097  15.41270  1.000 29.26648 ? 302 UOL A H2  1 
HETATM 2191 H H24 . UOL C 3 .   ? 18.30138 10.40286 7.06047   1.000 25.85559 ? 302 UOL A H24 1 
HETATM 2192 H H14 . UOL C 3 .   ? 16.36643 7.58894  11.98461  1.000 33.37974 ? 302 UOL A H14 1 
HETATM 2193 H H13 . UOL C 3 .   ? 15.75322 6.01978  10.41167  1.000 39.69448 ? 302 UOL A H13 1 
HETATM 2194 H H9  . UOL C 3 .   ? 16.79992 2.11874  10.22552  1.000 44.72246 ? 302 UOL A H9  1 
HETATM 2195 H H8  . UOL C 3 .   ? 17.32754 2.96977  11.64396  1.000 44.72246 ? 302 UOL A H8  1 
HETATM 2196 H H10 . UOL C 3 .   ? 17.73029 3.57617  10.06767  1.000 44.72246 ? 302 UOL A H10 1 
HETATM 2197 H H12 . UOL C 3 .   ? 14.89266 3.43450  11.23360  1.000 42.80844 ? 302 UOL A H12 1 
HETATM 2198 H H11 . UOL C 3 .   ? 15.23693 3.94854  9.62147   1.000 42.80844 ? 302 UOL A H11 1 
HETATM 2199 H H20 . UOL C 3 .   ? 14.11849 11.36822 12.64768  1.000 27.92330 ? 302 UOL A H20 1 
HETATM 2200 H H19 . UOL C 3 .   ? 14.36873 10.25105 13.93103  1.000 27.92330 ? 302 UOL A H19 1 
HETATM 2201 H H21 . UOL C 3 .   ? 13.82904 10.77792 10.49155  1.000 25.87880 ? 302 UOL A H21 1 
HETATM 2202 H H22 . UOL C 3 .   ? 13.55069 9.14333  10.02216  1.000 25.87880 ? 302 UOL A H22 1 
HETATM 2203 H H4  . UOL C 3 .   ? 16.29804 10.31496 10.52112  1.000 24.53594 ? 302 UOL A H4  1 
HETATM 2204 H H5  . UOL C 3 .   ? 18.00108 8.43395  9.46698   1.000 25.15399 ? 302 UOL A H5  1 
HETATM 2205 H H6  . UOL C 3 .   ? 16.69634 9.14323  6.88464   1.000 24.33477 ? 302 UOL A H6  1 
HETATM 2206 H H7  . UOL C 3 .   ? 14.66619 9.78114  7.94778   1.000 22.50847 ? 302 UOL A H7  1 
HETATM 2207 H H25 . UOL C 3 .   ? 15.10528 6.85170  7.44761   1.000 23.75385 ? 302 UOL A H25 1 
HETATM 2208 H H26 . UOL C 3 .   ? 21.11675 5.27233  9.06287   1.000 23.58054 ? 302 UOL A H26 1 
HETATM 2209 H H29 . UOL C 3 .   ? 12.38351 9.20040  12.70547  1.000 31.89722 ? 302 UOL A H29 1 
HETATM 2210 H H30 . UOL C 3 .   ? 13.53565 8.07962  13.44709  1.000 31.89722 ? 302 UOL A H30 1 
HETATM 2211 H H31 . UOL C 3 .   ? 12.96191 7.79571  11.79671  1.000 31.89722 ? 302 UOL A H31 1 
HETATM 2212 H H32 . UOL C 3 .   ? 23.98496 11.26218 12.98946  1.000 26.76533 ? 302 UOL A H32 1 
HETATM 2213 H H16 . UOL C 3 .   ? 16.26853 6.59977  14.73439  1.000 31.61958 ? 302 UOL A H16 1 
HETATM 2214 H H15 . UOL C 3 .   ? 16.25557 8.24482  14.20964  1.000 31.61958 ? 302 UOL A H15 1 
HETATM 2215 H H3  . UOL C 3 .   ? 17.75640 7.68929  16.43262  1.000 32.48596 ? 302 UOL A H3  1 
HETATM 2216 H H34 . UOL C 3 .   ? 21.53072 14.12647 10.08064  1.000 23.61326 ? 302 UOL A H34 1 
HETATM 2217 H H33 . UOL C 3 .   ? 20.98682 15.01712 11.45918  1.000 23.61326 ? 302 UOL A H33 1 
HETATM 2218 H H27 . UOL C 3 .   ? 18.24487 1.94500  7.25429   1.000 26.90484 ? 302 UOL A H27 1 
HETATM 2219 H H28 . UOL C 3 .   ? 18.23789 2.80150  5.75235   1.000 26.90484 ? 302 UOL A H28 1 
HETATM 2220 H H18 . UOL C 3 .   ? 20.03496 9.38588  16.92198  1.000 32.49438 ? 302 UOL A H18 1 
HETATM 2221 H H23 . UOL C 3 .   ? 15.94210 11.75655 7.47313   1.000 25.04033 ? 302 UOL A H23 1 
HETATM 2222 O O   . HOH D 4 .   ? 20.44091 21.85638 35.04234  1.000 55.12984 ? 401 HOH A O   1 
HETATM 2223 O O   . HOH D 4 .   ? 27.15211 27.02881 -7.70262  1.000 49.35685 ? 402 HOH A O   1 
HETATM 2224 O O   . HOH D 4 .   ? 18.92308 26.72984 -6.75405  1.000 45.31546 ? 403 HOH A O   1 
HETATM 2225 O O   . HOH D 4 .   ? 9.84249  6.48237  1.48142   1.000 45.31223 ? 404 HOH A O   1 
HETATM 2226 O O   . HOH D 4 .   ? 24.65968 31.62536 2.91678   1.000 53.23384 ? 405 HOH A O   1 
HETATM 2227 O O   . HOH D 4 .   ? 25.98406 26.86400 7.03270   1.000 39.27211 ? 406 HOH A O   1 
HETATM 2228 O O   . HOH D 4 .   ? 7.98348  31.50517 41.86705  1.000 27.54003 ? 407 HOH A O   1 
HETATM 2229 O O   . HOH D 4 .   ? 23.93721 10.68519 18.07885  1.000 55.63967 ? 408 HOH A O   1 
HETATM 2230 O O   . HOH D 4 .   ? 13.55165 10.32004 -18.84540 1.000 52.48911 ? 409 HOH A O   1 
HETATM 2231 O O   . HOH D 4 .   ? 10.44784 5.91483  -14.39503 1.000 38.49785 ? 410 HOH A O   1 
HETATM 2232 O O   . HOH D 4 .   ? 13.71231 10.91209 4.47302   1.000 23.20762 ? 411 HOH A O   1 
HETATM 2233 O O   . HOH D 4 .   ? -0.38673 11.69894 -2.39883  1.000 57.92034 ? 412 HOH A O   1 
HETATM 2234 O O   . HOH D 4 .   ? 27.90310 26.14168 -2.40749  1.000 32.43135 ? 413 HOH A O   1 
HETATM 2235 O O   . HOH D 4 .   ? 24.13384 8.04042  -8.83715  1.000 24.93368 ? 414 HOH A O   1 
HETATM 2236 O O   . HOH D 4 .   ? 13.31794 18.75550 0.51755   1.000 32.97008 ? 415 HOH A O   1 
HETATM 2237 O O   . HOH D 4 .   ? 9.00494  12.65250 18.82974  1.000 44.29297 ? 416 HOH A O   1 
HETATM 2238 O O   . HOH D 4 .   ? 14.08273 -1.08613 -8.95731  1.000 38.39390 ? 417 HOH A O   1 
HETATM 2239 O O   . HOH D 4 .   ? 31.48450 5.36340  0.00000   0.50  32.49132 ? 418 HOH A O   1 
HETATM 2240 O O   . HOH D 4 .   ? 25.22670 3.40088  -1.89534  1.000 34.90570 ? 419 HOH A O   1 
HETATM 2241 O O   . HOH D 4 .   ? 20.19975 26.46814 2.80944   1.000 25.55621 ? 420 HOH A O   1 
HETATM 2242 O O   . HOH D 4 .   ? 2.79752  24.00144 22.62899  1.000 48.77911 ? 421 HOH A O   1 
HETATM 2243 O O   . HOH D 4 .   ? 11.81286 36.31553 15.78963  1.000 57.26759 ? 422 HOH A O   1 
HETATM 2244 O O   . HOH D 4 .   ? 15.46771 28.55826 12.18671  1.000 29.76321 ? 423 HOH A O   1 
HETATM 2245 O O   . HOH D 4 .   ? 6.42442  19.15107 16.55197  1.000 41.78433 ? 424 HOH A O   1 
HETATM 2246 O O   . HOH D 4 .   ? 16.69895 2.13674  -20.72366 1.000 59.15620 ? 425 HOH A O   1 
HETATM 2247 O O   . HOH D 4 .   ? 22.08585 23.34065 -5.20125  1.000 23.60300 ? 426 HOH A O   1 
HETATM 2248 O O   . HOH D 4 .   ? 14.60762 3.97618  5.59737   1.000 30.61858 ? 427 HOH A O   1 
HETATM 2249 O O   . HOH D 4 .   ? 32.31905 15.74252 24.17520  1.000 40.45894 ? 428 HOH A O   1 
HETATM 2250 O O   . HOH D 4 .   ? 20.51812 26.69179 -4.68611  1.000 35.03599 ? 429 HOH A O   1 
HETATM 2251 O O   . HOH D 4 .   ? 22.79650 11.32458 0.42801   1.000 17.68624 ? 430 HOH A O   1 
HETATM 2252 O O   . HOH D 4 .   ? 13.38513 5.60667  10.16468  1.000 62.98524 ? 431 HOH A O   1 
HETATM 2253 O O   . HOH D 4 .   ? 24.22669 5.32441  9.85324   1.000 38.43158 ? 432 HOH A O   1 
HETATM 2254 O O   . HOH D 4 .   ? 33.64290 6.62993  -4.86359  1.000 18.37834 ? 433 HOH A O   1 
HETATM 2255 O O   . HOH D 4 .   ? 15.75289 30.67667 7.05169   1.000 37.76499 ? 434 HOH A O   1 
HETATM 2256 O O   . HOH D 4 .   ? 8.26304  4.57595  -10.34750 1.000 47.72727 ? 435 HOH A O   1 
HETATM 2257 O O   . HOH D 4 .   ? 27.56259 5.52944  -1.73653  1.000 33.88894 ? 436 HOH A O   1 
HETATM 2258 O O   . HOH D 4 .   ? 13.79225 22.28620 -5.95317  1.000 28.54492 ? 437 HOH A O   1 
HETATM 2259 O O   . HOH D 4 .   ? 5.44253  24.01103 0.11887   1.000 46.48884 ? 438 HOH A O   1 
HETATM 2260 O O   . HOH D 4 .   ? 6.64160  30.75971 30.61945  1.000 49.58033 ? 439 HOH A O   1 
HETATM 2261 O O   . HOH D 4 .   ? 28.02897 28.49900 5.48403   1.000 49.43293 ? 440 HOH A O   1 
HETATM 2262 O O   . HOH D 4 .   ? 22.39332 21.01594 7.12106   1.000 21.84103 ? 441 HOH A O   1 
HETATM 2263 O O   . HOH D 4 .   ? 0.88269  17.10911 -4.41944  1.000 58.37073 ? 442 HOH A O   1 
HETATM 2264 O O   . HOH D 4 .   ? 12.11951 1.57995  -5.47238  1.000 27.62239 ? 443 HOH A O   1 
HETATM 2265 O O   . HOH D 4 .   ? 8.52054  17.94631 18.17220  1.000 37.65100 ? 444 HOH A O   1 
HETATM 2266 O O   . HOH D 4 .   ? 26.83547 3.38232  -4.47846  1.000 53.00893 ? 445 HOH A O   1 
HETATM 2267 O O   . HOH D 4 .   ? 23.20790 7.47615  11.19644  1.000 26.45321 ? 446 HOH A O   1 
HETATM 2268 O O   . HOH D 4 .   ? 19.96104 27.50922 -9.95161  1.000 46.13848 ? 447 HOH A O   1 
HETATM 2269 O O   . HOH D 4 .   ? 20.76197 11.58754 4.97433   1.000 17.43602 ? 448 HOH A O   1 
HETATM 2270 O O   . HOH D 4 .   ? 3.98146  32.38474 29.33823  1.000 55.27071 ? 449 HOH A O   1 
HETATM 2271 O O   . HOH D 4 .   ? 31.84775 5.14233  -11.87860 1.000 30.96979 ? 450 HOH A O   1 
HETATM 2272 O O   . HOH D 4 .   ? 9.53451  34.35755 42.05147  1.000 60.39094 ? 451 HOH A O   1 
HETATM 2273 O O   . HOH D 4 .   ? 20.39145 21.92295 19.82162  1.000 33.05759 ? 452 HOH A O   1 
HETATM 2274 O O   . HOH D 4 .   ? 24.97555 34.91913 16.41389  1.000 50.72197 ? 453 HOH A O   1 
HETATM 2275 O O   . HOH D 4 .   ? 33.59006 21.05389 13.73248  1.000 32.23012 ? 454 HOH A O   1 
HETATM 2276 O O   . HOH D 4 .   ? 13.24147 1.22873  2.43979   1.000 61.38605 ? 455 HOH A O   1 
HETATM 2277 O O   . HOH D 4 .   ? 6.78794  11.09705 19.81876  1.000 53.98295 ? 456 HOH A O   1 
HETATM 2278 O O   . HOH D 4 .   ? 26.85456 21.64994 -14.59780 1.000 39.79892 ? 457 HOH A O   1 
HETATM 2279 O O   . HOH D 4 .   ? 14.94161 16.96263 20.56490  1.000 33.86656 ? 458 HOH A O   1 
HETATM 2280 O O   . HOH D 4 .   ? 17.67282 10.61858 18.55313  1.000 34.12656 ? 459 HOH A O   1 
HETATM 2281 O O   . HOH D 4 .   ? 4.82802  24.16876 34.44479  1.000 50.76330 ? 460 HOH A O   1 
HETATM 2282 O O   . HOH D 4 .   ? 16.98907 28.24093 35.57315  1.000 49.01805 ? 461 HOH A O   1 
HETATM 2283 O O   . HOH D 4 .   ? 1.25985  9.00260  0.72974   1.000 40.68956 ? 462 HOH A O   1 
HETATM 2284 O O   . HOH D 4 .   ? 12.25973 14.44589 33.39148  1.000 41.32208 ? 463 HOH A O   1 
HETATM 2285 O O   . HOH D 4 .   ? 25.37605 9.24123  -6.59235  1.000 21.29946 ? 464 HOH A O   1 
HETATM 2286 O O   . HOH D 4 .   ? 8.79952  16.29968 6.43038   1.000 49.39768 ? 465 HOH A O   1 
HETATM 2287 O O   . HOH D 4 .   ? 20.34937 7.96047  10.90385  1.000 24.77704 ? 466 HOH A O   1 
HETATM 2288 O O   . HOH D 4 .   ? 4.08804  21.38972 22.80156  1.000 50.65028 ? 467 HOH A O   1 
HETATM 2289 O O   . HOH D 4 .   ? 17.90553 18.73607 -20.27004 1.000 43.36037 ? 468 HOH A O   1 
HETATM 2290 O O   . HOH D 4 .   ? 10.29314 3.94105  -12.00484 1.000 32.43273 ? 469 HOH A O   1 
HETATM 2291 O O   . HOH D 4 .   ? 11.27823 7.39421  -0.54438  1.000 25.66031 ? 470 HOH A O   1 
HETATM 2292 O O   . HOH D 4 .   ? 22.77017 32.26764 8.26404   1.000 70.73708 ? 471 HOH A O   1 
HETATM 2293 O O   . HOH D 4 .   ? 10.18580 13.47931 12.72016  1.000 38.50022 ? 472 HOH A O   1 
HETATM 2294 O O   . HOH D 4 .   ? 26.22580 30.03471 10.92875  1.000 42.94402 ? 473 HOH A O   1 
HETATM 2295 O O   . HOH D 4 .   ? 26.21498 6.79664  -3.82259  1.000 19.84033 ? 474 HOH A O   1 
HETATM 2296 O O   . HOH D 4 .   ? 5.76967  18.24099 12.53358  1.000 46.71212 ? 475 HOH A O   1 
HETATM 2297 O O   . HOH D 4 .   ? 21.46437 1.50335  -13.06923 1.000 32.38288 ? 476 HOH A O   1 
HETATM 2298 O O   . HOH D 4 .   ? 14.96703 -0.62718 -11.37941 1.000 56.67428 ? 477 HOH A O   1 
HETATM 2299 O O   . HOH D 4 .   ? 8.57032  20.69053 3.83411   1.000 44.54202 ? 478 HOH A O   1 
HETATM 2300 O O   . HOH D 4 .   ? 22.59576 21.10724 16.94221  1.000 46.52862 ? 479 HOH A O   1 
HETATM 2301 O O   . HOH D 4 .   ? 24.99771 15.52590 19.50644  1.000 51.07416 ? 480 HOH A O   1 
HETATM 2302 O O   . HOH D 4 .   ? 29.93064 26.60959 1.06428   1.000 37.16602 ? 481 HOH A O   1 
HETATM 2303 O O   . HOH D 4 .   ? 18.80956 19.90025 -14.22989 1.000 34.95570 ? 482 HOH A O   1 
HETATM 2304 O O   . HOH D 4 .   ? 2.89378  5.86242  -14.42138 1.000 46.82486 ? 483 HOH A O   1 
HETATM 2305 O O   . HOH D 4 .   ? 29.09601 28.91114 19.32173  1.000 58.72289 ? 484 HOH A O   1 
HETATM 2306 O O   . HOH D 4 .   ? 28.70896 2.21371  -10.46871 1.000 40.25989 ? 485 HOH A O   1 
HETATM 2307 O O   . HOH D 4 .   ? 6.17125  21.54793 2.37838   1.000 50.35488 ? 486 HOH A O   1 
HETATM 2308 O O   . HOH D 4 .   ? 27.30015 1.35800  -8.51640  1.000 50.85064 ? 487 HOH A O   1 
HETATM 2309 O O   . HOH D 4 .   ? 29.71671 3.93014  14.70175  1.000 48.50887 ? 488 HOH A O   1 
HETATM 2310 O O   . HOH D 4 .   ? 4.61735  18.57908 29.13799  1.000 37.89996 ? 489 HOH A O   1 
HETATM 2311 O O   . HOH D 4 .   ? 24.49613 1.60719  -5.49090  1.000 34.24830 ? 490 HOH A O   1 
HETATM 2312 O O   . HOH D 4 .   ? 37.45311 14.25774 21.19759  1.000 40.03104 ? 491 HOH A O   1 
HETATM 2313 O O   . HOH D 4 .   ? 8.07500  12.85551 15.83201  1.000 56.69963 ? 492 HOH A O   1 
HETATM 2314 O O   . HOH D 4 .   ? 23.14216 -7.83115 -13.86350 1.000 37.33379 ? 493 HOH A O   1 
HETATM 2315 O O   . HOH D 4 .   ? 5.36006  26.90793 9.91037   1.000 50.34513 ? 494 HOH A O   1 
HETATM 2316 O O   . HOH D 4 .   ? 23.64252 0.83854  -1.96203  1.000 50.14793 ? 495 HOH A O   1 
HETATM 2317 O O   . HOH D 4 .   ? 27.57913 27.11272 9.79416   1.000 65.41950 ? 496 HOH A O   1 
HETATM 2318 O O   . HOH D 4 .   ? 21.28203 21.07288 1.35560   1.000 25.72862 ? 497 HOH A O   1 
HETATM 2319 O O   . HOH D 4 .   ? 20.91240 14.18594 31.98859  1.000 49.12044 ? 498 HOH A O   1 
HETATM 2320 O O   . HOH D 4 .   ? 9.80217  2.57069  -14.66222 1.000 49.91389 ? 499 HOH A O   1 
HETATM 2321 O O   . HOH D 4 .   ? 1.33175  22.22833 29.09977  1.000 55.69349 ? 500 HOH A O   1 
HETATM 2322 O O   . HOH D 4 .   ? 26.61149 23.67130 21.94635  1.000 52.49143 ? 501 HOH A O   1 
HETATM 2323 O O   . HOH D 4 .   ? 6.57760  7.19642  29.22904  1.000 54.58874 ? 502 HOH A O   1 
HETATM 2324 O O   . HOH D 4 .   ? 26.54915 21.76330 23.71269  1.000 43.63455 ? 503 HOH A O   1 
HETATM 2325 O O   . HOH D 4 .   ? 13.64374 18.78281 35.61621  1.000 53.83883 ? 504 HOH A O   1 
HETATM 2326 O O   . HOH D 4 .   ? 6.87568  16.27871 19.34088  1.000 57.23174 ? 505 HOH A O   1 
HETATM 2327 O O   . HOH D 4 .   ? 11.19274 26.55243 0.08607   1.000 59.14866 ? 506 HOH A O   1 
HETATM 2328 O O   . HOH D 4 .   ? 30.12764 4.58868  7.91578   1.000 37.41144 ? 507 HOH A O   1 
HETATM 2329 O O   . HOH D 4 .   ? 2.21585  17.27440 0.66428   1.000 51.37419 ? 508 HOH A O   1 
HETATM 2330 O O   . HOH D 4 .   ? 12.79530 11.31096 18.57389  1.000 35.06165 ? 509 HOH A O   1 
HETATM 2331 O O   . HOH D 4 .   ? 18.03805 20.52788 35.15749  1.000 64.25394 ? 510 HOH A O   1 
HETATM 2332 O O   . HOH D 4 .   ? 2.18632  6.72575  1.41793   1.000 48.34993 ? 511 HOH A O   1 
HETATM 2333 O O   . HOH D 4 .   ? 18.38258 22.85136 -14.28493 1.000 53.18857 ? 512 HOH A O   1 
HETATM 2334 O O   . HOH D 4 .   ? 10.53493 6.45859  4.50123   1.000 49.63945 ? 513 HOH A O   1 
HETATM 2335 O O   . HOH D 4 .   ? 10.32861 14.71871 10.05066  1.000 44.65407 ? 514 HOH A O   1 
HETATM 2336 O O   . HOH D 4 .   ? 14.99646 9.67985  16.67593  1.000 28.62151 ? 515 HOH A O   1 
HETATM 2337 O O   . HOH D 4 .   ? 31.37940 2.90097  -9.19086  1.000 48.30140 ? 516 HOH A O   1 
HETATM 2338 O O   . HOH D 4 .   ? 8.18449  13.21754 -17.44303 1.000 55.39107 ? 517 HOH A O   1 
HETATM 2339 O O   . HOH D 4 .   ? 5.72102  26.09890 -5.99560  1.000 58.24772 ? 518 HOH A O   1 
HETATM 2340 O O   . HOH D 4 .   ? 25.38836 22.79519 -17.42533 1.000 55.08757 ? 519 HOH A O   1 
HETATM 2341 O O   . HOH D 4 .   ? 14.90973 26.80787 36.14161  1.000 64.73820 ? 520 HOH A O   1 
HETATM 2342 O O   . HOH D 4 .   ? 13.10021 5.82396  4.45240   1.000 39.07842 ? 521 HOH A O   1 
HETATM 2343 O O   . HOH D 4 .   ? 13.91523 8.33698  5.69093   1.000 32.80650 ? 522 HOH A O   1 
HETATM 2344 O O   . HOH D 4 .   ? 7.87138  18.11610 4.56047   1.000 54.63008 ? 523 HOH A O   1 
HETATM 2345 O O   . HOH D 4 .   ? 13.17059 31.13025 6.01951   1.000 49.71191 ? 524 HOH A O   1 
HETATM 2346 O O   . HOH D 4 .   ? 4.51930  19.17773 10.38550  1.000 49.71289 ? 525 HOH A O   1 
HETATM 2347 O O   . HOH D 4 .   ? 24.36454 26.37939 -12.77017 1.000 68.47469 ? 526 HOH A O   1 
HETATM 2348 O O   . HOH D 4 .   ? 4.52613  26.85225 35.46961  1.000 38.86424 ? 527 HOH A O   1 
HETATM 2349 O O   . HOH D 4 .   ? 30.12206 4.63938  -2.06825  1.000 40.63094 ? 528 HOH A O   1 
HETATM 2350 O O   . HOH D 4 .   ? 28.25284 1.64209  1.13773   1.000 59.26979 ? 529 HOH A O   1 
HETATM 2351 O O   . HOH D 4 .   ? 31.75740 4.72061  -4.09306  1.000 30.87158 ? 530 HOH A O   1 
HETATM 2352 O O   . HOH D 4 .   ? 12.86784 3.10764  7.48225   1.000 49.29046 ? 531 HOH A O   1 
HETATM 2353 O O   . HOH D 4 .   ? 14.43926 10.80716 34.52014  1.000 60.46683 ? 532 HOH A O   1 
HETATM 2354 O O   . HOH D 4 .   ? 7.74610  15.52564 8.99096   1.000 49.27953 ? 533 HOH A O   1 
HETATM 2355 O O   . HOH D 4 .   ? 3.16806  22.81105 36.31618  1.000 52.30400 ? 534 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 0.90519 0.63259 0.69211 0.01807  0.07151  -0.00510 1   MET A N   
2    C CA  . MET A 1   ? 0.87577 0.61980 0.67522 0.03550  0.08299  -0.02936 1   MET A CA  
3    C C   . MET A 1   ? 0.81254 0.55823 0.60963 0.08419  0.07572  -0.03405 1   MET A C   
4    O O   . MET A 1   ? 0.78678 0.56326 0.60020 0.09636  0.08499  -0.02847 1   MET A O   
5    C CB  . MET A 1   ? 0.91083 0.66797 0.71789 0.02483  0.12328  -0.06888 1   MET A CB  
6    C CG  . MET A 1   ? 0.94434 0.70983 0.75572 -0.00544 0.14794  -0.08059 1   MET A CG  
7    S SD  . MET A 1   ? 0.97319 0.74509 0.77607 -0.03039 0.16135  -0.09080 1   MET A SD  
8    C CE  . MET A 1   ? 0.97971 0.76134 0.78491 -0.04227 0.14972  -0.09285 1   MET A CE  
9    N N   . LYS A 2   ? 0.76697 0.50578 0.54391 0.12625  0.08237  -0.03394 2   LYS A N   
10   C CA  . LYS A 2   ? 0.70750 0.45359 0.49625 0.15410  0.08650  -0.05123 2   LYS A CA  
11   C C   . LYS A 2   ? 0.65170 0.41159 0.42366 0.16455  0.09872  -0.06696 2   LYS A C   
12   O O   . LYS A 2   ? 0.65580 0.41313 0.35267 0.12975  0.11584  -0.09172 2   LYS A O   
13   C CB  . LYS A 2   ? 0.67945 0.46034 0.54665 0.19269  0.08518  -0.05135 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.66888 0.48402 0.57121 0.22466  0.10156  -0.08545 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.69888 0.52150 0.59949 0.21623  0.09999  -0.08743 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.73124 0.56669 0.63318 0.18225  0.08715  -0.08741 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.76369 0.61198 0.65228 0.16869  0.09061  -0.09330 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.60677 0.38940 0.39927 0.15860  0.11155  -0.06761 3   TYR A N   
19   C CA  . TYR A 3   ? 0.54713 0.39008 0.34850 0.15216  0.07580  -0.06359 3   TYR A CA  
20   C C   . TYR A 3   ? 0.51217 0.40273 0.31075 0.15729  0.05855  -0.06700 3   TYR A C   
21   O O   . TYR A 3   ? 0.51645 0.43516 0.32947 0.18106  0.04384  -0.05819 3   TYR A O   
22   C CB  . TYR A 3   ? 0.51683 0.39984 0.30944 0.10473  0.08774  -0.04898 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.49705 0.39776 0.30766 0.07168  0.10026  -0.05878 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.51753 0.38616 0.29148 0.05072  0.10351  -0.07427 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.47030 0.38699 0.29585 0.05359  0.07683  -0.05974 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.51287 0.40591 0.29965 0.07618  0.08436  -0.06658 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.49336 0.39107 0.26830 0.06166  0.08317  -0.08687 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.50036 0.40111 0.29212 0.08605  0.09769  -0.07397 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.57582 0.44621 0.31449 0.05329  0.09715  -0.09149 3   TYR A OH  
30   N N   . MET A 4   ? 0.47449 0.39895 0.27346 0.16888  0.02791  -0.03925 4   MET A N   
31   C CA  . MET A 4   ? 0.47962 0.42482 0.26478 0.13797  0.02057  -0.04322 4   MET A CA  
32   C C   . MET A 4   ? 0.42240 0.41231 0.25167 0.11537  0.03903  -0.04781 4   MET A C   
33   O O   . MET A 4   ? 0.42869 0.42097 0.25065 0.08789  0.03649  -0.04417 4   MET A O   
34   C CB  . MET A 4   ? 0.50923 0.47718 0.27549 0.16211  0.00410  -0.01960 4   MET A CB  
35   C CG  . MET A 4   ? 0.48600 0.49771 0.27350 0.15696  0.02502  -0.03638 4   MET A CG  
36   S SD  . MET A 4   ? 0.47494 0.52052 0.29486 0.16552  0.02802  -0.00879 4   MET A SD  
37   C CE  . MET A 4   ? 0.49706 0.55142 0.30031 0.16657  0.05201  -0.02431 4   MET A CE  
38   N N   . ILE A 5   ? 0.39394 0.41237 0.23398 0.12801  0.03984  -0.06367 5   ILE A N   
39   C CA  . ILE A 5   ? 0.36151 0.39626 0.23434 0.10461  0.02730  -0.03926 5   ILE A CA  
40   C C   . ILE A 5   ? 0.33146 0.41229 0.25579 0.11964  0.04117  -0.06256 5   ILE A C   
41   O O   . ILE A 5   ? 0.31582 0.44928 0.26757 0.08096  0.06280  -0.06512 5   ILE A O   
42   C CB  . ILE A 5   ? 0.36684 0.37722 0.22039 0.10699  0.01621  -0.02299 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.39931 0.38468 0.21820 0.09002  0.00910  -0.04823 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.39157 0.39292 0.23342 0.12361  0.02312  0.01023  5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.44044 0.38977 0.22851 0.10019  -0.00035 -0.04496 5   ILE A CD1 
46   N N   . THR A 6   ? 0.34300 0.43649 0.28230 0.10984  0.02616  -0.07759 6   THR A N   
47   C CA  A THR A 6   ? 0.36721 0.45242 0.30632 0.07185  0.01722  -0.08722 6   THR A CA  
48   C CA  B THR A 6   ? 0.37104 0.45481 0.30791 0.07501  0.01365  -0.06694 6   THR A CA  
49   C C   . THR A 6   ? 0.37175 0.46766 0.33135 0.01352  0.01567  -0.05931 6   THR A C   
50   O O   . THR A 6   ? 0.39288 0.50330 0.39017 -0.02701 0.01621  -0.00737 6   THR A O   
51   C CB  A THR A 6   ? 0.43655 0.47222 0.33413 0.07928  0.02923  -0.07634 6   THR A CB  
52   C CB  B THR A 6   ? 0.41470 0.47047 0.31358 0.08577  0.00553  -0.04577 6   THR A CB  
53   O OG1 A THR A 6   ? 0.39077 0.45650 0.33314 0.04176  0.05052  -0.11196 6   THR A OG1 
54   O OG1 B THR A 6   ? 0.48215 0.49691 0.33831 0.08837  -0.00059 -0.04121 6   THR A OG1 
55   C CG2 A THR A 6   ? 0.50624 0.50514 0.36546 0.07220  0.01849  -0.06682 6   THR A CG2 
56   C CG2 B THR A 6   ? 0.36836 0.45237 0.29370 0.08380  0.00444  -0.04835 6   THR A CG2 
57   N N   . SER A 7   ? 0.39490 0.44630 0.33706 -0.03539 0.01355  -0.06307 7   SER A N   
58   C CA  . SER A 7   ? 0.40526 0.40466 0.33193 -0.02600 0.05942  -0.05162 7   SER A CA  
59   C C   . SER A 7   ? 0.42247 0.39313 0.35980 -0.02594 0.07067  -0.05945 7   SER A C   
60   O O   . SER A 7   ? 0.42319 0.40669 0.40197 -0.01352 0.06224  -0.05544 7   SER A O   
61   C CB  . SER A 7   ? 0.40660 0.40073 0.32655 -0.01623 0.12413  -0.05177 7   SER A CB  
62   O OG  . SER A 7   ? 0.44794 0.44670 0.34356 -0.02763 0.09252  -0.05743 7   SER A OG  
63   N N   . LYS A 8   ? 0.45133 0.39147 0.36398 -0.00499 0.10429  -0.06869 8   LYS A N   
64   C CA  . LYS A 8   ? 0.48548 0.41233 0.40255 -0.03957 0.11380  -0.06586 8   LYS A CA  
65   C C   . LYS A 8   ? 0.51369 0.46514 0.42102 -0.02258 0.11916  -0.08570 8   LYS A C   
66   O O   . LYS A 8   ? 0.54544 0.49915 0.43072 -0.06578 0.10406  -0.08964 8   LYS A O   
67   C CB  . LYS A 8   ? 0.48131 0.41030 0.45230 -0.00450 0.13957  -0.09931 8   LYS A CB  
68   C CG  . LYS A 8   ? 0.55377 0.44834 0.50438 0.02021  0.10151  -0.09136 8   LYS A CG  
69   C CD  . LYS A 8   ? 0.62477 0.46352 0.54246 0.03902  0.06514  -0.08495 8   LYS A CD  
70   C CE  . LYS A 8   ? 0.67517 0.46633 0.56524 0.02679  0.04098  -0.07665 8   LYS A CE  
71   N NZ  . LYS A 8   ? 0.71949 0.47354 0.57643 0.01847  0.02637  -0.07814 8   LYS A NZ  
72   N N   . GLY A 9   ? 0.52461 0.49967 0.42271 -0.04203 0.15507  -0.08496 9   GLY A N   
73   C CA  . GLY A 9   ? 0.52082 0.51055 0.44790 -0.04669 0.18885  -0.07521 9   GLY A CA  
74   C C   . GLY A 9   ? 0.53943 0.52609 0.47952 -0.04330 0.20162  -0.06471 9   GLY A C   
75   O O   . GLY A 9   ? 0.59327 0.54599 0.50765 -0.07909 0.15863  -0.06530 9   GLY A O   
76   N N   . ASP A 10  ? 0.55984 0.53515 0.49531 -0.02067 0.21529  -0.03378 10  ASP A N   
77   C CA  . ASP A 10  ? 0.59117 0.55839 0.52333 0.00232  0.21021  0.01029  10  ASP A CA  
78   C C   . ASP A 10  ? 0.60635 0.52820 0.50967 0.01518  0.20461  0.01935  10  ASP A C   
79   O O   . ASP A 10  ? 0.61561 0.51733 0.49458 0.03863  0.21600  0.04421  10  ASP A O   
80   C CB  . ASP A 10  ? 0.63240 0.61201 0.57747 -0.00156 0.19807  0.04078  10  ASP A CB  
81   C CG  . ASP A 10  ? 0.65723 0.65998 0.61750 -0.00900 0.18659  0.08221  10  ASP A CG  
82   O OD1 . ASP A 10  ? 0.67110 0.66499 0.61897 -0.01343 0.20566  0.10810  10  ASP A OD1 
83   O OD2 . ASP A 10  ? 0.66825 0.69529 0.64050 -0.01713 0.17336  0.09347  10  ASP A OD2 
84   N N   . GLU A 11  ? 0.62671 0.52348 0.50517 -0.01906 0.19376  0.03361  11  GLU A N   
85   C CA  . GLU A 11  ? 0.67961 0.52413 0.51064 0.00749  0.15858  0.04388  11  GLU A CA  
86   C C   . GLU A 11  ? 0.65948 0.49391 0.48679 0.04221  0.17296  0.05161  11  GLU A C   
87   O O   . GLU A 11  ? 0.70634 0.45923 0.48709 0.05044  0.16811  0.06159  11  GLU A O   
88   C CB  . GLU A 11  ? 0.72956 0.56193 0.54869 -0.00302 0.11834  0.06005  11  GLU A CB  
89   C CG  . GLU A 11  ? 0.76556 0.60373 0.57217 -0.03001 0.08815  0.07551  11  GLU A CG  
90   C CD  . GLU A 11  ? 0.79554 0.64398 0.59349 -0.05633 0.06834  0.07724  11  GLU A CD  
91   O OE1 . GLU A 11  ? 0.80743 0.65439 0.59449 -0.06833 0.05364  0.08316  11  GLU A OE1 
92   O OE2 . GLU A 11  ? 0.80324 0.66029 0.60679 -0.06188 0.06183  0.06770  11  GLU A OE2 
93   N N   . LYS A 12  ? 0.60168 0.49349 0.47248 0.04521  0.15270  0.06002  12  LYS A N   
94   C CA  . LYS A 12  ? 0.61590 0.50266 0.46161 0.05230  0.11933  0.05535  12  LYS A CA  
95   C C   . LYS A 12  ? 0.59557 0.47434 0.39947 0.06838  0.11353  0.02400  12  LYS A C   
96   O O   . LYS A 12  ? 0.58895 0.48410 0.36734 0.11078  0.10398  0.01445  12  LYS A O   
97   C CB  . LYS A 12  ? 0.61031 0.52435 0.52582 0.04710  0.08226  0.09141  12  LYS A CB  
98   C CG  . LYS A 12  ? 0.62209 0.52872 0.57709 0.03765  0.06917  0.12114  12  LYS A CG  
99   C CD  . LYS A 12  ? 0.63677 0.53964 0.62939 0.03062  0.07582  0.13357  12  LYS A CD  
100  C CE  . LYS A 12  ? 0.65439 0.55032 0.67069 0.01464  0.06712  0.14103  12  LYS A CE  
101  N NZ  . LYS A 12  ? 0.66006 0.57809 0.69479 0.01091  0.07023  0.13933  12  LYS A NZ  
102  N N   . SER A 13  ? 0.53723 0.45579 0.37118 0.06935  0.12540  0.01673  13  SER A N   
103  C CA  . SER A 13  ? 0.47714 0.41643 0.35769 0.09810  0.13593  -0.01568 13  SER A CA  
104  C C   . SER A 13  ? 0.46708 0.44295 0.33589 0.06384  0.13633  -0.02740 13  SER A C   
105  O O   . SER A 13  ? 0.47915 0.46570 0.33205 0.07497  0.11617  -0.02308 13  SER A O   
106  C CB  . SER A 13  ? 0.46557 0.38900 0.37276 0.10934  0.14097  -0.05205 13  SER A CB  
107  O OG  . SER A 13  ? 0.46031 0.40397 0.42291 0.06093  0.13518  -0.03731 13  SER A OG  
108  N N   . ASP A 14  ? 0.45259 0.46226 0.33861 0.03941  0.12316  -0.02807 14  ASP A N   
109  C CA  . ASP A 14  ? 0.47309 0.48054 0.33096 0.02600  0.15150  -0.04812 14  ASP A CA  
110  C C   . ASP A 14  ? 0.51222 0.47765 0.30630 0.02688  0.11484  -0.02331 14  ASP A C   
111  O O   . ASP A 14  ? 0.52221 0.46245 0.27575 0.05800  0.11193  -0.03183 14  ASP A O   
112  C CB  . ASP A 14  ? 0.51527 0.50094 0.37649 -0.05126 0.13431  -0.04931 14  ASP A CB  
113  C CG  . ASP A 14  ? 0.56173 0.52266 0.43287 -0.05907 0.13440  -0.06191 14  ASP A CG  
114  O OD1 . ASP A 14  ? 0.52311 0.51000 0.42642 -0.02288 0.14648  -0.07472 14  ASP A OD1 
115  O OD2 . ASP A 14  ? 0.60394 0.55537 0.47024 -0.10593 0.11533  -0.06744 14  ASP A OD2 
116  N N   . LEU A 15  ? 0.53345 0.47889 0.33078 0.02554  0.09634  -0.00129 15  LEU A N   
117  C CA  . LEU A 15  ? 0.50825 0.47924 0.33123 0.02847  0.09731  0.00866  15  LEU A CA  
118  C C   . LEU A 15  ? 0.44345 0.47476 0.29661 0.06186  0.08551  0.00042  15  LEU A C   
119  O O   . LEU A 15  ? 0.43142 0.45867 0.28732 0.05203  0.05038  -0.01628 15  LEU A O   
120  C CB  . LEU A 15  ? 0.53979 0.48965 0.36869 0.01118  0.12422  0.03475  15  LEU A CB  
121  C CG  . LEU A 15  ? 0.56372 0.50246 0.40506 0.03255  0.15673  0.02305  15  LEU A CG  
122  C CD1 . LEU A 15  ? 0.55829 0.48815 0.43359 0.05806  0.15739  0.00820  15  LEU A CD1 
123  C CD2 . LEU A 15  ? 0.54569 0.49438 0.41341 0.03037  0.19293  0.01432  15  LEU A CD2 
124  N N   . LEU A 16  ? 0.40641 0.47848 0.28544 0.11600  0.06628  0.03036  16  LEU A N   
125  C CA  . LEU A 16  ? 0.42190 0.47756 0.26469 0.11672  0.07086  0.02401  16  LEU A CA  
126  C C   . LEU A 16  ? 0.42766 0.44450 0.26981 0.11762  0.06556  0.01838  16  LEU A C   
127  O O   . LEU A 16  ? 0.46316 0.45907 0.27180 0.09003  0.07900  0.01143  16  LEU A O   
128  C CB  . LEU A 16  ? 0.40140 0.51563 0.24526 0.11630  0.06628  -0.01146 16  LEU A CB  
129  C CG  . LEU A 16  ? 0.44467 0.52441 0.24759 0.11275  0.07011  -0.03216 16  LEU A CG  
130  C CD1 . LEU A 16  ? 0.46976 0.52624 0.25753 0.10251  0.02389  -0.06369 16  LEU A CD1 
131  C CD2 . LEU A 16  ? 0.46470 0.53507 0.25325 0.15525  0.07352  -0.05373 16  LEU A CD2 
132  N N   . ARG A 17  ? 0.40606 0.40839 0.24277 0.11900  0.06453  0.00123  17  ARG A N   
133  C CA  . ARG A 17  ? 0.35824 0.37404 0.26071 0.13572  0.02676  -0.01613 17  ARG A CA  
134  C C   . ARG A 17  ? 0.36435 0.37485 0.25524 0.09692  0.04140  -0.02374 17  ARG A C   
135  O O   . ARG A 17  ? 0.37379 0.36225 0.26665 0.11385  0.02514  -0.04718 17  ARG A O   
136  C CB  . ARG A 17  ? 0.33512 0.36354 0.25260 0.10599  0.04499  -0.04219 17  ARG A CB  
137  C CG  . ARG A 17  ? 0.34734 0.37681 0.25425 0.07810  0.05525  -0.07600 17  ARG A CG  
138  C CD  . ARG A 17  ? 0.34155 0.41095 0.26723 0.06293  0.04320  -0.07202 17  ARG A CD  
139  N NE  . ARG A 17  ? 0.31763 0.45497 0.30330 0.04998  0.04232  -0.05188 17  ARG A NE  
140  C CZ  . ARG A 17  ? 0.32910 0.46723 0.32364 0.05662  0.03786  -0.03780 17  ARG A CZ  
141  N NH1 . ARG A 17  ? 0.35926 0.48777 0.34019 0.03862  0.02864  -0.06293 17  ARG A NH1 
142  N NH2 . ARG A 17  ? 0.38280 0.47456 0.35062 0.08919  0.04643  -0.01335 17  ARG A NH2 
143  N N   . LEU A 18  ? 0.34710 0.40511 0.26178 0.07579  0.08020  -0.01922 18  LEU A N   
144  C CA  . LEU A 18  ? 0.39053 0.43300 0.25825 0.05648  0.06226  -0.02964 18  LEU A CA  
145  C C   . LEU A 18  ? 0.43032 0.44265 0.23308 0.08721  0.05948  -0.02974 18  LEU A C   
146  O O   . LEU A 18  ? 0.49135 0.45559 0.22421 0.07253  0.05304  -0.03080 18  LEU A O   
147  C CB  . LEU A 18  ? 0.38163 0.44014 0.26454 0.03642  0.05172  -0.01762 18  LEU A CB  
148  C CG  . LEU A 18  ? 0.42139 0.46818 0.30233 0.01423  0.04862  -0.00452 18  LEU A CG  
149  C CD1 . LEU A 18  ? 0.42769 0.46532 0.27786 -0.02284 0.03928  0.02042  18  LEU A CD1 
150  C CD2 . LEU A 18  ? 0.40110 0.50301 0.31789 -0.00923 0.01713  0.00679  18  LEU A CD2 
151  N N   . ASN A 19  ? 0.45074 0.45862 0.24588 0.08844  0.05585  -0.00438 19  ASN A N   
152  C CA  . ASN A 19  ? 0.45385 0.45804 0.26112 0.11109  0.05127  -0.02052 19  ASN A CA  
153  C C   . ASN A 19  ? 0.42831 0.47206 0.26588 0.10516  0.04439  -0.04173 19  ASN A C   
154  O O   . ASN A 19  ? 0.40400 0.46637 0.27641 0.13525  0.00088  -0.02521 19  ASN A O   
155  C CB  . ASN A 19  ? 0.47649 0.47121 0.27955 0.14278  0.02682  -0.01554 19  ASN A CB  
156  C CG  . ASN A 19  ? 0.52108 0.45000 0.29499 0.15549  -0.00958 -0.01154 19  ASN A CG  
157  O OD1 . ASN A 19  ? 0.51079 0.43795 0.25424 0.14595  0.01182  -0.00927 19  ASN A OD1 
158  N ND2 . ASN A 19  ? 0.55672 0.44617 0.31981 0.16961  -0.02049 -0.02577 19  ASN A ND2 
159  N N   . MET A 20  ? 0.35805 0.48376 0.24643 0.10832  0.07242  -0.05605 20  MET A N   
160  C CA  . MET A 20  ? 0.38515 0.46511 0.25825 0.08802  0.07434  -0.06019 20  MET A CA  
161  C C   . MET A 20  ? 0.37860 0.49668 0.26734 0.05532  0.06182  -0.06450 20  MET A C   
162  O O   . MET A 20  ? 0.38833 0.53464 0.28610 0.04986  0.04967  -0.06484 20  MET A O   
163  C CB  . MET A 20  ? 0.37110 0.45549 0.26189 0.06969  0.08064  -0.06200 20  MET A CB  
164  C CG  . MET A 20  ? 0.42725 0.46435 0.26980 0.11186  0.08614  -0.08570 20  MET A CG  
165  S SD  . MET A 20  ? 0.43990 0.49198 0.28756 0.12016  0.04671  -0.07322 20  MET A SD  
166  C CE  . MET A 20  ? 0.46553 0.48104 0.29800 0.05397  0.06464  -0.08296 20  MET A CE  
167  N N   . ILE A 21  ? 0.40102 0.48862 0.25159 0.09263  0.06636  -0.04047 21  ILE A N   
168  C CA  . ILE A 21  ? 0.38309 0.45766 0.22453 0.13128  0.02290  -0.05168 21  ILE A CA  
169  C C   . ILE A 21  ? 0.40148 0.47057 0.22177 0.16387  0.02493  -0.04145 21  ILE A C   
170  O O   . ILE A 21  ? 0.42601 0.49154 0.22858 0.16468  0.01335  -0.03930 21  ILE A O   
171  C CB  . ILE A 21  ? 0.37356 0.47006 0.24982 0.10961  0.00534  -0.04781 21  ILE A CB  
172  C CG1 . ILE A 21  ? 0.37689 0.45499 0.23505 0.08246  -0.02905 -0.04311 21  ILE A CG1 
173  C CG2 . ILE A 21  ? 0.40664 0.46028 0.28084 0.08398  0.02564  -0.05624 21  ILE A CG2 
174  C CD1 . ILE A 21  ? 0.39545 0.45117 0.26917 0.06704  0.01507  -0.06774 21  ILE A CD1 
175  N N   . ALA A 22  ? 0.40287 0.48706 0.21303 0.17481  0.01322  -0.04264 22  ALA A N   
176  C CA  . ALA A 22  ? 0.45246 0.50233 0.24173 0.16225  0.02442  -0.04285 22  ALA A CA  
177  C C   . ALA A 22  ? 0.44014 0.53363 0.25967 0.14517  0.02837  -0.06936 22  ALA A C   
178  O O   . ALA A 22  ? 0.46252 0.53369 0.26133 0.10799  0.01157  -0.06797 22  ALA A O   
179  C CB  . ALA A 22  ? 0.50617 0.51280 0.24776 0.14427  0.02618  -0.01404 22  ALA A CB  
180  N N   . GLY A 23  ? 0.44512 0.56293 0.27592 0.12702  0.02900  -0.06689 23  GLY A N   
181  C CA  . GLY A 23  ? 0.45903 0.55984 0.26811 0.06138  0.01785  -0.09458 23  GLY A CA  
182  C C   . GLY A 23  ? 0.47975 0.55937 0.29142 0.07437  0.02570  -0.10434 23  GLY A C   
183  O O   . GLY A 23  ? 0.51220 0.57834 0.29896 0.07823  0.00695  -0.10959 23  GLY A O   
184  N N   . PHE A 24  ? 0.45136 0.52291 0.28165 0.10330  0.00791  -0.09468 24  PHE A N   
185  C CA  . PHE A 24  ? 0.49512 0.52095 0.30500 0.06886  0.02072  -0.09285 24  PHE A CA  
186  C C   . PHE A 24  ? 0.50979 0.53835 0.31834 0.10721  0.03198  -0.08943 24  PHE A C   
187  O O   . PHE A 24  ? 0.56005 0.56171 0.33297 0.08507  0.02479  -0.10989 24  PHE A O   
188  C CB  . PHE A 24  ? 0.48849 0.50938 0.31015 0.04871  0.03497  -0.08394 24  PHE A CB  
189  C CG  . PHE A 24  ? 0.50531 0.52700 0.34259 0.03283  0.07052  -0.09159 24  PHE A CG  
190  C CD1 . PHE A 24  ? 0.52350 0.55112 0.36452 0.04006  0.08839  -0.11202 24  PHE A CD1 
191  C CD2 . PHE A 24  ? 0.48578 0.50767 0.34250 0.04843  0.09767  -0.11136 24  PHE A CD2 
192  C CE1 . PHE A 24  ? 0.51075 0.55606 0.37423 0.05022  0.09886  -0.11916 24  PHE A CE1 
193  C CE2 . PHE A 24  ? 0.47758 0.52557 0.36689 0.04171  0.11256  -0.12646 24  PHE A CE2 
194  C CZ  . PHE A 24  ? 0.50420 0.54067 0.37383 0.03584  0.10837  -0.13067 24  PHE A CZ  
195  N N   . GLY A 25  ? 0.48073 0.55123 0.32642 0.11908  0.05134  -0.08541 25  GLY A N   
196  C CA  . GLY A 25  ? 0.53082 0.53856 0.34105 0.12292  0.04806  -0.11583 25  GLY A CA  
197  C C   . GLY A 25  ? 0.57130 0.55466 0.36312 0.10566  0.04796  -0.13679 25  GLY A C   
198  O O   . GLY A 25  ? 0.57024 0.55331 0.37619 0.08092  0.07946  -0.15614 25  GLY A O   
199  N N   . GLU A 26  ? 0.63684 0.60643 0.38012 0.07859  0.01834  -0.14339 26  GLU A N   
200  C CA  . GLU A 26  ? 0.68117 0.63132 0.39704 0.11043  -0.00312 -0.16648 26  GLU A CA  
201  C C   . GLU A 26  ? 0.69430 0.64350 0.45360 0.09276  0.00083  -0.19147 26  GLU A C   
202  O O   . GLU A 26  ? 0.69709 0.68761 0.47977 0.08374  -0.03129 -0.18062 26  GLU A O   
203  C CB  . GLU A 26  ? 0.71812 0.67601 0.37171 0.15541  -0.00470 -0.15509 26  GLU A CB  
204  C CG  . GLU A 26  ? 0.73185 0.70077 0.33010 0.20261  0.00293  -0.14335 26  GLU A CG  
205  C CD  . GLU A 26  ? 0.77792 0.73289 0.32184 0.22920  -0.00597 -0.13204 26  GLU A CD  
206  O OE1 . GLU A 26  ? 0.77839 0.74742 0.32441 0.25496  -0.00972 -0.06272 26  GLU A OE1 
207  O OE2 . GLU A 26  ? 0.80398 0.73824 0.32087 0.22336  -0.00188 -0.16348 26  GLU A OE2 
208  N N   . TYR A 27  ? 0.70082 0.61654 0.47213 0.09751  0.04924  -0.20891 27  TYR A N   
209  C CA  . TYR A 27  ? 0.73017 0.59717 0.52021 0.07582  0.07507  -0.20835 27  TYR A CA  
210  C C   . TYR A 27  ? 0.81254 0.59680 0.57979 0.04221  0.07432  -0.20964 27  TYR A C   
211  O O   . TYR A 27  ? 0.81152 0.60024 0.61359 0.06403  0.10479  -0.20360 27  TYR A O   
212  C CB  . TYR A 27  ? 0.69723 0.60507 0.50114 0.07408  0.12422  -0.20179 27  TYR A CB  
213  C CG  . TYR A 27  ? 0.67931 0.61169 0.48618 0.06201  0.15745  -0.18433 27  TYR A CG  
214  C CD1 . TYR A 27  ? 0.69751 0.61653 0.49371 0.06152  0.14791  -0.17106 27  TYR A CD1 
215  C CD2 . TYR A 27  ? 0.66762 0.62572 0.46565 0.02736  0.19471  -0.17093 27  TYR A CD2 
216  C CE1 . TYR A 27  ? 0.68269 0.63723 0.49928 0.04814  0.16184  -0.14020 27  TYR A CE1 
217  C CE2 . TYR A 27  ? 0.64751 0.64005 0.45524 0.02173  0.20751  -0.14410 27  TYR A CE2 
218  C CZ  . TYR A 27  ? 0.66339 0.66585 0.48099 0.03146  0.20505  -0.10198 27  TYR A CZ  
219  O OH  . TYR A 27  ? 0.63926 0.70774 0.47074 0.02474  0.27332  -0.06349 27  TYR A OH  
220  N N   . ASP A 28  ? 0.88059 0.61711 0.59559 0.02948  0.05375  -0.21425 28  ASP A N   
221  C CA  . ASP A 28  ? 0.91777 0.64886 0.62087 0.01725  0.03600  -0.18900 28  ASP A CA  
222  C C   . ASP A 28  ? 0.92546 0.65835 0.60822 0.01262  0.05633  -0.16663 28  ASP A C   
223  O O   . ASP A 28  ? 0.95826 0.67112 0.62817 -0.00400 0.04457  -0.13934 28  ASP A O   
224  C CB  . ASP A 28  ? 0.94966 0.71077 0.66075 -0.00432 0.01385  -0.15132 28  ASP A CB  
225  C CG  . ASP A 28  ? 0.96873 0.75889 0.69517 -0.03236 -0.00185 -0.12352 28  ASP A CG  
226  O OD1 . ASP A 28  ? 0.98299 0.78184 0.71208 -0.03815 0.00580  -0.09449 28  ASP A OD1 
227  O OD2 . ASP A 28  ? 0.96797 0.77470 0.70962 -0.03968 -0.01379 -0.12793 28  ASP A OD2 
228  N N   . MET A 29  ? 0.88298 0.64346 0.58112 0.02186  0.09606  -0.16472 29  MET A N   
229  C CA  . MET A 29  ? 0.85112 0.64150 0.55403 0.02578  0.11388  -0.17058 29  MET A CA  
230  C C   . MET A 29  ? 0.80734 0.62815 0.55378 0.07194  0.11567  -0.15423 29  MET A C   
231  O O   . MET A 29  ? 0.82399 0.66967 0.55416 0.06732  0.12216  -0.14721 29  MET A O   
232  C CB  . MET A 29  ? 0.87644 0.67590 0.54371 0.00066  0.13244  -0.18286 29  MET A CB  
233  C CG  . MET A 29  ? 0.92517 0.70656 0.55119 -0.02650 0.15343  -0.20573 29  MET A CG  
234  S SD  . MET A 29  ? 0.96758 0.73282 0.56016 -0.03938 0.16709  -0.22369 29  MET A SD  
235  C CE  . MET A 29  ? 0.96395 0.71068 0.56769 -0.03493 0.15529  -0.24911 29  MET A CE  
236  N N   . GLU A 30  ? 0.75439 0.56582 0.53080 0.12079  0.09481  -0.17629 30  GLU A N   
237  C CA  . GLU A 30  ? 0.73245 0.55599 0.53029 0.16527  0.08774  -0.16423 30  GLU A CA  
238  C C   . GLU A 30  ? 0.68263 0.54048 0.49388 0.18494  0.11131  -0.16307 30  GLU A C   
239  O O   . GLU A 30  ? 0.71860 0.54044 0.48499 0.18673  0.12104  -0.16001 30  GLU A O   
240  C CB  . GLU A 30  ? 0.75804 0.58314 0.55301 0.17367  0.07733  -0.14249 30  GLU A CB  
241  C CG  . GLU A 30  ? 0.77745 0.61322 0.57321 0.19334  0.07989  -0.11459 30  GLU A CG  
242  C CD  . GLU A 30  ? 0.79085 0.61966 0.59659 0.21315  0.07871  -0.08720 30  GLU A CD  
243  O OE1 . GLU A 30  ? 0.78960 0.61069 0.59829 0.24116  0.10414  -0.07704 30  GLU A OE1 
244  O OE2 . GLU A 30  ? 0.81464 0.64199 0.60639 0.18960  0.04894  -0.07836 30  GLU A OE2 
245  N N   . TYR A 31  ? 0.61586 0.52649 0.46418 0.20981  0.10728  -0.15394 31  TYR A N   
246  C CA  . TYR A 31  ? 0.55952 0.53198 0.42288 0.22766  0.09149  -0.10118 31  TYR A CA  
247  C C   . TYR A 31  ? 0.56997 0.55060 0.41791 0.27274  0.09192  -0.07816 31  TYR A C   
248  O O   . TYR A 31  ? 0.57816 0.58199 0.42892 0.25101  0.09843  -0.07696 31  TYR A O   
249  C CB  . TYR A 31  ? 0.49086 0.50895 0.39195 0.22278  0.05756  -0.06501 31  TYR A CB  
250  C CG  . TYR A 31  ? 0.46230 0.49953 0.34643 0.17912  0.03594  -0.07396 31  TYR A CG  
251  C CD1 . TYR A 31  ? 0.46593 0.50990 0.34322 0.17610  -0.00630 -0.07035 31  TYR A CD1 
252  C CD2 . TYR A 31  ? 0.42982 0.50536 0.31812 0.13516  0.03352  -0.05958 31  TYR A CD2 
253  C CE1 . TYR A 31  ? 0.45492 0.51225 0.32069 0.15091  0.00161  -0.08464 31  TYR A CE1 
254  C CE2 . TYR A 31  ? 0.41264 0.48629 0.30236 0.13852  0.02799  -0.10011 31  TYR A CE2 
255  C CZ  . TYR A 31  ? 0.43267 0.50253 0.29768 0.14686  0.00806  -0.08200 31  TYR A CZ  
256  O OH  . TYR A 31  ? 0.41767 0.52138 0.28569 0.15534  0.01560  -0.07150 31  TYR A OH  
257  N N   . ASP A 32  ? 0.60846 0.54802 0.40740 0.29112  0.08134  -0.06400 32  ASP A N   
258  C CA  . ASP A 32  ? 0.63792 0.54916 0.41886 0.28195  0.08317  -0.03659 32  ASP A CA  
259  C C   . ASP A 32  ? 0.60992 0.54656 0.39751 0.26538  0.08037  -0.03824 32  ASP A C   
260  O O   . ASP A 32  ? 0.59075 0.53126 0.37968 0.26900  0.08450  -0.03777 32  ASP A O   
261  C CB  . ASP A 32  ? 0.69323 0.55172 0.43627 0.28806  0.06489  -0.01043 32  ASP A CB  
262  C CG  . ASP A 32  ? 0.74765 0.54960 0.46013 0.28529  0.04077  0.01008  32  ASP A CG  
263  O OD1 . ASP A 32  ? 0.74845 0.53659 0.44158 0.27851  0.04531  0.01654  32  ASP A OD1 
264  O OD2 . ASP A 32  ? 0.80180 0.55868 0.48292 0.28756  0.02004  0.01360  32  ASP A OD2 
265  N N   . ASP A 33  ? 0.56661 0.58346 0.40129 0.24660  0.08117  -0.04769 33  ASP A N   
266  C CA  . ASP A 33  ? 0.52871 0.62337 0.39786 0.24608  0.08574  -0.05469 33  ASP A CA  
267  C C   . ASP A 33  ? 0.51663 0.65908 0.40484 0.26403  0.04335  -0.05332 33  ASP A C   
268  O O   . ASP A 33  ? 0.51677 0.71123 0.37581 0.24704  0.04627  -0.07922 33  ASP A O   
269  C CB  . ASP A 33  ? 0.52413 0.64495 0.42812 0.19674  0.09656  -0.04869 33  ASP A CB  
270  C CG  . ASP A 33  ? 0.56690 0.68304 0.45777 0.15435  0.10776  -0.00294 33  ASP A CG  
271  O OD1 . ASP A 33  ? 0.56097 0.69230 0.45047 0.16962  0.10773  0.02909  33  ASP A OD1 
272  O OD2 . ASP A 33  ? 0.60408 0.71440 0.49354 0.10833  0.09005  0.00781  33  ASP A OD2 
273  N N   . VAL A 34  ? 0.51037 0.65231 0.42843 0.27862  0.01794  -0.02299 34  VAL A N   
274  C CA  . VAL A 34  ? 0.52389 0.62152 0.46447 0.29882  -0.00217 0.00392  34  VAL A CA  
275  C C   . VAL A 34  ? 0.56305 0.61168 0.48758 0.31129  0.00137  -0.00648 34  VAL A C   
276  O O   . VAL A 34  ? 0.58523 0.63851 0.49399 0.29889  0.03020  -0.01217 34  VAL A O   
277  C CB  . VAL A 34  ? 0.52362 0.63447 0.48094 0.26789  -0.00900 0.02433  34  VAL A CB  
278  C CG1 . VAL A 34  ? 0.50395 0.64928 0.48558 0.23697  -0.04775 0.04069  34  VAL A CG1 
279  C CG2 . VAL A 34  ? 0.50126 0.61728 0.47825 0.27509  0.01292  0.02260  34  VAL A CG2 
280  N N   . GLU A 35  ? 0.58739 0.57456 0.50908 0.33586  -0.00998 0.00678  35  GLU A N   
281  C CA  . GLU A 35  ? 0.63899 0.56708 0.51784 0.30370  -0.01041 -0.00810 35  GLU A CA  
282  C C   . GLU A 35  ? 0.63558 0.53888 0.47598 0.27411  0.02469  -0.05083 35  GLU A C   
283  O O   . GLU A 35  ? 0.62508 0.58932 0.50196 0.26382  0.07079  -0.05956 35  GLU A O   
284  C CB  . GLU A 35  ? 0.70340 0.59133 0.55735 0.27150  -0.02548 -0.00629 35  GLU A CB  
285  C CG  . GLU A 35  ? 0.74500 0.62683 0.59884 0.24058  -0.05854 -0.00527 35  GLU A CG  
286  C CD  . GLU A 35  ? 0.77818 0.65172 0.62970 0.22671  -0.08017 -0.00227 35  GLU A CD  
287  O OE1 . GLU A 35  ? 0.78033 0.65444 0.64425 0.23146  -0.08710 -0.01309 35  GLU A OE1 
288  O OE2 . GLU A 35  ? 0.79277 0.66147 0.64418 0.21538  -0.08833 0.01351  35  GLU A OE2 
289  N N   . PRO A 36  ? 0.60807 0.49375 0.41645 0.28458  0.00129  -0.05369 36  PRO A N   
290  C CA  . PRO A 36  ? 0.63859 0.46334 0.40632 0.24526  0.01805  -0.06365 36  PRO A CA  
291  C C   . PRO A 36  ? 0.65961 0.43881 0.40829 0.19840  0.05306  -0.04316 36  PRO A C   
292  O O   . PRO A 36  ? 0.66981 0.48430 0.39857 0.20234  0.08994  -0.05458 36  PRO A O   
293  C CB  . PRO A 36  ? 0.63031 0.42455 0.37125 0.25586  0.00474  -0.07712 36  PRO A CB  
294  C CG  . PRO A 36  ? 0.61680 0.44607 0.37212 0.27326  0.00804  -0.08183 36  PRO A CG  
295  C CD  . PRO A 36  ? 0.60253 0.46019 0.37839 0.28231  0.00857  -0.08812 36  PRO A CD  
296  N N   . GLU A 37  ? 0.66394 0.38857 0.42497 0.19001  0.06882  -0.02455 37  GLU A N   
297  C CA  . GLU A 37  ? 0.66763 0.38309 0.42497 0.16358  0.05810  -0.01963 37  GLU A CA  
298  C C   . GLU A 37  ? 0.61884 0.35850 0.36770 0.12800  0.05864  -0.03278 37  GLU A C   
299  O O   . GLU A 37  ? 0.63340 0.35224 0.36140 0.06713  0.03857  -0.03992 37  GLU A O   
300  C CB  . GLU A 37  ? 0.72845 0.41865 0.47830 0.14434  0.03826  -0.00472 37  GLU A CB  
301  C CG  . GLU A 37  ? 0.77477 0.45305 0.53219 0.14310  0.02166  -0.00141 37  GLU A CG  
302  C CD  . GLU A 37  ? 0.82337 0.46557 0.57449 0.12278  -0.00301 0.01407  37  GLU A CD  
303  O OE1 . GLU A 37  ? 0.84289 0.46749 0.58849 0.12921  -0.01115 0.04094  37  GLU A OE1 
304  O OE2 . GLU A 37  ? 0.84058 0.46759 0.58729 0.10955  -0.00507 0.01654  37  GLU A OE2 
305  N N   . ILE A 38  ? 0.58110 0.35515 0.30780 0.14000  0.04961  -0.05290 38  ILE A N   
306  C CA  . ILE A 38  ? 0.54222 0.35002 0.29979 0.09754  0.04363  -0.07341 38  ILE A CA  
307  C C   . ILE A 38  ? 0.52284 0.33452 0.29938 0.11359  0.03356  -0.06348 38  ILE A C   
308  O O   . ILE A 38  ? 0.50836 0.29230 0.30085 0.10764  0.06007  -0.02638 38  ILE A O   
309  C CB  . ILE A 38  ? 0.59212 0.37629 0.31898 0.09406  0.01593  -0.09743 38  ILE A CB  
310  C CG1 . ILE A 38  ? 0.60290 0.40333 0.34053 0.10049  0.02907  -0.13405 38  ILE A CG1 
311  C CG2 . ILE A 38  ? 0.61165 0.38248 0.31593 0.10235  0.00223  -0.09210 38  ILE A CG2 
312  C CD1 . ILE A 38  ? 0.60240 0.43454 0.37010 0.13012  0.03170  -0.12018 38  ILE A CD1 
313  N N   . VAL A 39  ? 0.50066 0.31844 0.29009 0.08857  0.00886  -0.07052 39  VAL A N   
314  C CA  . VAL A 39  ? 0.49271 0.32497 0.26673 0.08599  0.00694  -0.04019 39  VAL A CA  
315  C C   . VAL A 39  ? 0.45462 0.31704 0.23161 0.12170  0.03093  -0.05232 39  VAL A C   
316  O O   . VAL A 39  ? 0.49209 0.29180 0.24569 0.11356  0.03436  -0.05797 39  VAL A O   
317  C CB  . VAL A 39  ? 0.47014 0.29232 0.26361 0.10018  -0.00151 -0.02788 39  VAL A CB  
318  C CG1 . VAL A 39  ? 0.45921 0.28147 0.26995 0.08416  0.00103  -0.05168 39  VAL A CG1 
319  C CG2 . VAL A 39  ? 0.47794 0.33594 0.26091 0.11934  -0.01077 -0.00360 39  VAL A CG2 
320  N N   . ILE A 40  ? 0.42485 0.33710 0.22414 0.10595  -0.00261 -0.04879 40  ILE A N   
321  C CA  . ILE A 40  ? 0.37539 0.35222 0.23499 0.09330  0.02716  -0.06230 40  ILE A CA  
322  C C   . ILE A 40  ? 0.36005 0.33825 0.24186 0.06379  0.04132  -0.07811 40  ILE A C   
323  O O   . ILE A 40  ? 0.37129 0.32444 0.28742 0.06009  0.06785  -0.07903 40  ILE A O   
324  C CB  . ILE A 40  ? 0.40997 0.35497 0.24392 0.15760  0.02177  -0.09270 40  ILE A CB  
325  C CG1 . ILE A 40  ? 0.43711 0.36998 0.25319 0.12248  0.03954  -0.07243 40  ILE A CG1 
326  C CG2 . ILE A 40  ? 0.47219 0.37734 0.25066 0.14161  0.00972  -0.08462 40  ILE A CG2 
327  C CD1 . ILE A 40  ? 0.49001 0.39357 0.24045 0.09692  0.08122  -0.07334 40  ILE A CD1 
328  N N   . SER A 41  ? 0.35893 0.32400 0.24104 0.07069  0.01624  -0.09214 41  SER A N   
329  C CA  . SER A 41  ? 0.38037 0.34314 0.21734 0.05170  -0.00063 -0.08494 41  SER A CA  
330  C C   . SER A 41  ? 0.36767 0.37456 0.24058 0.04787  0.00510  -0.06343 41  SER A C   
331  O O   . SER A 41  ? 0.35762 0.40222 0.29172 0.00882  -0.00132 -0.02869 41  SER A O   
332  C CB  . SER A 41  ? 0.47050 0.31999 0.19339 0.03925  0.01558  -0.11725 41  SER A CB  
333  O OG  . SER A 41  ? 0.55790 0.42824 0.25550 0.09374  0.03992  -0.07154 41  SER A OG  
334  N N   . ILE A 42  ? 0.38375 0.37900 0.22832 0.07985  0.03443  -0.03892 42  ILE A N   
335  C CA  . ILE A 42  ? 0.39197 0.36276 0.24364 0.07206  0.06420  -0.04391 42  ILE A CA  
336  C C   . ILE A 42  ? 0.43869 0.36252 0.25948 0.07580  0.07580  -0.05285 42  ILE A C   
337  O O   . ILE A 42  ? 0.45991 0.37422 0.25461 0.06676  0.12059  -0.03972 42  ILE A O   
338  C CB  . ILE A 42  ? 0.37923 0.37338 0.23445 0.07898  0.06784  -0.02326 42  ILE A CB  
339  C CG1 . ILE A 42  ? 0.37514 0.37012 0.23167 0.07560  0.06418  -0.04345 42  ILE A CG1 
340  C CG2 . ILE A 42  ? 0.45267 0.38756 0.23861 0.05660  0.09828  -0.00863 42  ILE A CG2 
341  C CD1 . ILE A 42  ? 0.37337 0.39306 0.21820 0.07650  0.04243  -0.01597 42  ILE A CD1 
342  N N   . GLY A 43  ? 0.43649 0.32148 0.25692 0.10054  0.04979  -0.07179 43  GLY A N   
343  C CA  . GLY A 43  ? 0.42235 0.36851 0.29464 0.13670  0.09377  -0.08305 43  GLY A CA  
344  C C   . GLY A 43  ? 0.43323 0.40110 0.33399 0.14969  0.05692  -0.06072 43  GLY A C   
345  O O   . GLY A 43  ? 0.48060 0.47038 0.39547 0.13464  0.06183  -0.07558 43  GLY A O   
346  N N   . GLY A 44  ? 0.39114 0.37674 0.28609 0.12401  0.09013  0.02431  44  GLY A N   
347  C CA  . GLY A 44  ? 0.37704 0.41152 0.28534 0.09689  0.10382  0.02747  44  GLY A CA  
348  C C   . GLY A 44  ? 0.34753 0.39696 0.26175 0.03866  0.09549  0.02295  44  GLY A C   
349  O O   . GLY A 44  ? 0.33100 0.39648 0.25756 0.03025  0.07206  -0.00726 44  GLY A O   
350  N N   . ASP A 45  ? 0.32601 0.40277 0.21850 0.02134  0.09454  0.03869  45  ASP A N   
351  C CA  . ASP A 45  ? 0.28752 0.40556 0.21451 0.01932  0.09170  0.01345  45  ASP A CA  
352  C C   . ASP A 45  ? 0.29675 0.40307 0.26123 0.01925  0.06465  0.00372  45  ASP A C   
353  O O   . ASP A 45  ? 0.29357 0.40342 0.25239 0.00583  0.04219  0.00908  45  ASP A O   
354  C CB  . ASP A 45  ? 0.27873 0.38141 0.21195 0.06431  0.05698  -0.02557 45  ASP A CB  
355  C CG  . ASP A 45  ? 0.29350 0.37029 0.22613 0.04292  0.07822  -0.03393 45  ASP A CG  
356  O OD1 . ASP A 45  ? 0.30212 0.34237 0.25034 0.01154  0.03123  -0.03449 45  ASP A OD1 
357  O OD2 . ASP A 45  ? 0.32564 0.39946 0.25651 0.06250  0.07063  -0.03683 45  ASP A OD2 
358  N N   . GLY A 46  ? 0.23922 0.38087 0.26803 0.02212  0.06537  -0.01369 46  GLY A N   
359  C CA  . GLY A 46  ? 0.28892 0.38703 0.28310 0.03500  0.02163  -0.02984 46  GLY A CA  
360  C C   . GLY A 46  ? 0.31181 0.38495 0.26235 0.03191  0.02803  -0.03905 46  GLY A C   
361  O O   . GLY A 46  ? 0.31429 0.38720 0.26679 0.01915  0.04120  -0.03979 46  GLY A O   
362  N N   . THR A 47  ? 0.31814 0.37026 0.23936 0.05937  0.05751  -0.04267 47  THR A N   
363  C CA  . THR A 47  ? 0.36483 0.32765 0.22988 0.04715  0.02637  -0.05191 47  THR A CA  
364  C C   . THR A 47  ? 0.33282 0.32302 0.23060 0.05298  0.03310  -0.01712 47  THR A C   
365  O O   . THR A 47  ? 0.34062 0.33643 0.23877 0.04186  0.04225  -0.01957 47  THR A O   
366  C CB  . THR A 47  ? 0.37280 0.31909 0.22906 0.03903  0.05792  -0.01443 47  THR A CB  
367  O OG1 . THR A 47  ? 0.40803 0.36002 0.24948 0.00636  0.05608  0.00913  47  THR A OG1 
368  C CG2 . THR A 47  ? 0.39425 0.30457 0.26249 0.02393  0.03120  -0.01826 47  THR A CG2 
369  N N   . PHE A 48  ? 0.30899 0.32011 0.22399 0.01674  0.04817  -0.00860 48  PHE A N   
370  C CA  . PHE A 48  ? 0.29645 0.33194 0.22630 -0.02732 0.01346  -0.00985 48  PHE A CA  
371  C C   . PHE A 48  ? 0.29523 0.33990 0.23931 -0.00216 0.02581  -0.00268 48  PHE A C   
372  O O   . PHE A 48  ? 0.32561 0.33840 0.27088 -0.01161 0.01838  -0.01152 48  PHE A O   
373  C CB  . PHE A 48  ? 0.28744 0.35762 0.22835 -0.02678 0.04435  -0.01726 48  PHE A CB  
374  C CG  . PHE A 48  ? 0.31003 0.35300 0.21984 -0.03882 0.05350  -0.04458 48  PHE A CG  
375  C CD1 . PHE A 48  ? 0.34617 0.34653 0.22369 -0.03485 0.06444  -0.02945 48  PHE A CD1 
376  C CD2 . PHE A 48  ? 0.35072 0.36832 0.24813 -0.03142 0.06937  -0.06632 48  PHE A CD2 
377  C CE1 . PHE A 48  ? 0.36768 0.39157 0.22385 -0.03036 0.04767  -0.05649 48  PHE A CE1 
378  C CE2 . PHE A 48  ? 0.40260 0.37775 0.25442 -0.04614 0.05223  -0.06783 48  PHE A CE2 
379  C CZ  . PHE A 48  ? 0.41732 0.38602 0.23734 -0.04831 0.05288  -0.10371 48  PHE A CZ  
380  N N   . LEU A 49  ? 0.26706 0.33333 0.21894 0.00764  0.01466  -0.02594 49  LEU A N   
381  C CA  . LEU A 49  ? 0.27586 0.34851 0.23453 0.04856  0.01466  -0.03373 49  LEU A CA  
382  C C   . LEU A 49  ? 0.27236 0.37169 0.25488 0.06089  0.02019  -0.03627 49  LEU A C   
383  O O   . LEU A 49  ? 0.30591 0.38082 0.25553 0.06627  -0.02035 -0.06663 49  LEU A O   
384  C CB  . LEU A 49  ? 0.31552 0.33710 0.25289 0.09610  0.01837  -0.06600 49  LEU A CB  
385  C CG  . LEU A 49  ? 0.34025 0.35948 0.26202 0.08286  0.06667  -0.02298 49  LEU A CG  
386  C CD1 . LEU A 49  ? 0.37820 0.35947 0.31642 0.10160  0.09386  -0.01284 49  LEU A CD1 
387  C CD2 . LEU A 49  ? 0.36074 0.35970 0.23855 0.05890  0.07169  0.01762  49  LEU A CD2 
388  N N   . SER A 50  ? 0.27615 0.37614 0.27494 0.02756  0.04379  -0.06438 50  SER A N   
389  C CA  A SER A 50  ? 0.25168 0.37220 0.29501 0.00344  0.04098  -0.05307 50  SER A CA  
390  C CA  B SER A 50  ? 0.26775 0.38172 0.27829 0.01072  0.04208  -0.05609 50  SER A CA  
391  C C   . SER A 50  ? 0.28149 0.38527 0.28214 0.01858  0.03853  -0.05096 50  SER A C   
392  O O   . SER A 50  ? 0.31318 0.41321 0.31857 0.02295  0.03361  -0.05187 50  SER A O   
393  C CB  A SER A 50  ? 0.32701 0.36920 0.32151 -0.01137 0.02887  -0.05833 50  SER A CB  
394  C CB  B SER A 50  ? 0.28648 0.38904 0.29187 0.00044  0.03970  -0.05777 50  SER A CB  
395  O OG  A SER A 50  ? 0.35522 0.35222 0.34200 -0.04308 0.04416  -0.04270 50  SER A OG  
396  O OG  B SER A 50  ? 0.29199 0.39598 0.30519 -0.01341 0.04519  -0.04757 50  SER A OG  
397  N N   . ALA A 51  ? 0.34189 0.34613 0.25398 0.01555  0.01514  -0.07203 51  ALA A N   
398  C CA  . ALA A 51  ? 0.33223 0.33487 0.22712 0.03107  0.02838  -0.03779 51  ALA A CA  
399  C C   . ALA A 51  ? 0.30445 0.35914 0.23807 0.06890  0.00541  -0.03070 51  ALA A C   
400  O O   . ALA A 51  ? 0.33592 0.36937 0.28065 0.09772  0.01191  -0.00148 51  ALA A O   
401  C CB  . ALA A 51  ? 0.36472 0.35934 0.21752 0.00608  0.01508  -0.05268 51  ALA A CB  
402  N N   . PHE A 52  ? 0.23689 0.39126 0.22075 0.02952  0.03850  -0.03639 52  PHE A N   
403  C CA  . PHE A 52  ? 0.27526 0.40826 0.23185 0.06460  0.01934  -0.01723 52  PHE A CA  
404  C C   . PHE A 52  ? 0.32188 0.38934 0.24458 0.08898  0.00875  -0.02545 52  PHE A C   
405  O O   . PHE A 52  ? 0.35556 0.42819 0.27155 0.07182  -0.00223 -0.03375 52  PHE A O   
406  C CB  . PHE A 52  ? 0.27733 0.37847 0.23503 0.08848  0.02017  -0.00371 52  PHE A CB  
407  C CG  . PHE A 52  ? 0.29692 0.36621 0.25139 0.09595  0.01987  0.00061  52  PHE A CG  
408  C CD1 . PHE A 52  ? 0.37134 0.35663 0.26686 0.09183  0.03978  -0.01064 52  PHE A CD1 
409  C CD2 . PHE A 52  ? 0.31739 0.36274 0.25524 0.09243  0.01529  -0.01724 52  PHE A CD2 
410  C CE1 . PHE A 52  ? 0.41081 0.33552 0.26778 0.06916  0.04404  -0.03516 52  PHE A CE1 
411  C CE2 . PHE A 52  ? 0.31224 0.35997 0.28051 0.06036  0.03339  -0.01050 52  PHE A CE2 
412  C CZ  . PHE A 52  ? 0.37106 0.35673 0.28645 0.06189  0.03246  -0.01175 52  PHE A CZ  
413  N N   . HIS A 53  ? 0.27501 0.40529 0.25372 0.07946  0.00568  -0.02390 53  HIS A N   
414  C CA  . HIS A 53  ? 0.27440 0.42515 0.27465 0.12407  0.02371  -0.04682 53  HIS A CA  
415  C C   . HIS A 53  ? 0.30611 0.46440 0.28927 0.11827  0.02100  -0.04377 53  HIS A C   
416  O O   . HIS A 53  ? 0.35839 0.48685 0.31934 0.14258  0.00949  -0.03728 53  HIS A O   
417  C CB  . HIS A 53  ? 0.26173 0.43194 0.26124 0.14615  0.04408  -0.05932 53  HIS A CB  
418  C CG  . HIS A 53  ? 0.29723 0.45125 0.24361 0.11573  0.05440  -0.03183 53  HIS A CG  
419  N ND1 . HIS A 53  ? 0.32479 0.48247 0.23121 0.13444  0.06588  -0.02888 53  HIS A ND1 
420  C CD2 . HIS A 53  ? 0.26187 0.43770 0.24955 0.10425  0.03008  -0.03874 53  HIS A CD2 
421  C CE1 . HIS A 53  ? 0.29454 0.47151 0.25403 0.12303  0.05423  -0.02246 53  HIS A CE1 
422  N NE2 . HIS A 53  ? 0.28020 0.44504 0.25209 0.09023  0.00362  -0.03453 53  HIS A NE2 
423  N N   . GLN A 54  ? 0.33226 0.45744 0.28506 0.11108  0.02474  -0.06343 54  GLN A N   
424  C CA  . GLN A 54  ? 0.32963 0.49710 0.31170 0.13910  0.03190  -0.07576 54  GLN A CA  
425  C C   . GLN A 54  ? 0.31618 0.51553 0.34884 0.17942  0.01236  -0.03964 54  GLN A C   
426  O O   . GLN A 54  ? 0.34539 0.53634 0.38920 0.20014  0.01792  -0.03912 54  GLN A O   
427  C CB  . GLN A 54  ? 0.36513 0.52648 0.32533 0.10364  0.05634  -0.09728 54  GLN A CB  
428  C CG  . GLN A 54  ? 0.40354 0.57562 0.37947 0.05881  0.07900  -0.08890 54  GLN A CG  
429  C CD  . GLN A 54  ? 0.41327 0.62223 0.40802 0.03844  0.07255  -0.11146 54  GLN A CD  
430  O OE1 . GLN A 54  ? 0.34761 0.64006 0.39516 0.03799  0.06019  -0.10563 54  GLN A OE1 
431  N NE2 . GLN A 54  ? 0.45903 0.64163 0.45152 0.02210  0.06458  -0.12444 54  GLN A NE2 
432  N N   . TYR A 55  ? 0.37422 0.52352 0.33042 0.16873  0.01277  -0.04185 55  TYR A N   
433  C CA  . TYR A 55  ? 0.41459 0.48979 0.32630 0.13674  0.02296  -0.05205 55  TYR A CA  
434  C C   . TYR A 55  ? 0.42541 0.49198 0.33850 0.14221  0.04740  -0.02192 55  TYR A C   
435  O O   . TYR A 55  ? 0.45249 0.46772 0.34222 0.17343  0.03866  0.00830  55  TYR A O   
436  C CB  . TYR A 55  ? 0.46683 0.49083 0.31071 0.14773  0.00816  -0.09608 55  TYR A CB  
437  C CG  . TYR A 55  ? 0.50614 0.51059 0.31503 0.15242  0.00916  -0.10252 55  TYR A CG  
438  C CD1 . TYR A 55  ? 0.49517 0.52819 0.31703 0.17286  -0.00144 -0.11054 55  TYR A CD1 
439  C CD2 . TYR A 55  ? 0.53386 0.51183 0.30957 0.16210  -0.00166 -0.10162 55  TYR A CD2 
440  C CE1 . TYR A 55  ? 0.51593 0.52985 0.31346 0.15379  -0.01120 -0.11037 55  TYR A CE1 
441  C CE2 . TYR A 55  ? 0.52575 0.52094 0.32872 0.15965  0.01301  -0.11597 55  TYR A CE2 
442  C CZ  . TYR A 55  ? 0.52435 0.52481 0.32088 0.16882  -0.00047 -0.12084 55  TYR A CZ  
443  O OH  . TYR A 55  ? 0.54244 0.55654 0.32862 0.19653  -0.00705 -0.10872 55  TYR A OH  
444  N N   . GLU A 56  ? 0.40783 0.50703 0.34007 0.12814  0.06004  -0.02816 56  GLU A N   
445  C CA  . GLU A 56  ? 0.43704 0.53885 0.34860 0.11771  0.05311  -0.04085 56  GLU A CA  
446  C C   . GLU A 56  ? 0.44475 0.55807 0.35740 0.15378  -0.02276 -0.01839 56  GLU A C   
447  O O   . GLU A 56  ? 0.46255 0.58212 0.37755 0.13435  -0.06015 0.00804  56  GLU A O   
448  C CB  . GLU A 56  ? 0.45409 0.54110 0.35635 0.08932  0.03910  -0.05178 56  GLU A CB  
449  C CG  . GLU A 56  ? 0.48971 0.53338 0.38127 0.09732  0.02447  -0.09617 56  GLU A CG  
450  C CD  . GLU A 56  ? 0.50239 0.54769 0.42579 0.10993  0.00202  -0.12123 56  GLU A CD  
451  O OE1 . GLU A 56  ? 0.45870 0.52119 0.42499 0.18391  0.01454  -0.15629 56  GLU A OE1 
452  O OE2 . GLU A 56  ? 0.57289 0.58609 0.46259 0.09793  -0.02845 -0.12044 56  GLU A OE2 
453  N N   . GLU A 57  ? 0.50286 0.54291 0.37276 0.19027  -0.04584 -0.01623 57  GLU A N   
454  C CA  . GLU A 57  ? 0.53899 0.57150 0.41655 0.19931  -0.05267 -0.01131 57  GLU A CA  
455  C C   . GLU A 57  ? 0.57218 0.53422 0.40120 0.22599  -0.03318 -0.00201 57  GLU A C   
456  O O   . GLU A 57  ? 0.60522 0.54307 0.40762 0.24428  -0.05504 0.02106  57  GLU A O   
457  C CB  . GLU A 57  ? 0.57211 0.63831 0.46947 0.16519  -0.06626 -0.02580 57  GLU A CB  
458  C CG  . GLU A 57  ? 0.60359 0.67981 0.52119 0.15839  -0.08399 -0.03537 57  GLU A CG  
459  C CD  . GLU A 57  ? 0.66017 0.70426 0.56429 0.14932  -0.10697 -0.05106 57  GLU A CD  
460  O OE1 . GLU A 57  ? 0.68169 0.71193 0.57889 0.16009  -0.11916 -0.05457 57  GLU A OE1 
461  O OE2 . GLU A 57  ? 0.69109 0.71361 0.58649 0.14424  -0.10047 -0.05351 57  GLU A OE2 
462  N N   . ARG A 58  ? 0.54918 0.50238 0.37410 0.21772  -0.00639 -0.01436 58  ARG A N   
463  C CA  . ARG A 58  ? 0.55961 0.48686 0.37691 0.18984  0.03962  -0.02965 58  ARG A CA  
464  C C   . ARG A 58  ? 0.54759 0.45624 0.37064 0.18115  0.06293  -0.04291 58  ARG A C   
465  O O   . ARG A 58  ? 0.57111 0.45929 0.36095 0.14996  0.08099  -0.04231 58  ARG A O   
466  C CB  . ARG A 58  ? 0.58274 0.53561 0.39216 0.20158  0.07000  -0.04806 58  ARG A CB  
467  C CG  . ARG A 58  ? 0.60338 0.59232 0.40058 0.19317  0.09855  -0.03867 58  ARG A CG  
468  C CD  . ARG A 58  ? 0.63595 0.63425 0.42439 0.16722  0.10909  -0.04938 58  ARG A CD  
469  N NE  . ARG A 58  ? 0.66398 0.65725 0.44429 0.16455  0.10410  -0.04722 58  ARG A NE  
470  C CZ  . ARG A 58  ? 0.68149 0.66895 0.45319 0.16532  0.11668  -0.02426 58  ARG A CZ  
471  N NH1 . ARG A 58  ? 0.70259 0.68822 0.46489 0.15186  0.11922  -0.01386 58  ARG A NH1 
472  N NH2 . ARG A 58  ? 0.67659 0.65835 0.44779 0.17456  0.10966  -0.02132 58  ARG A NH2 
473  N N   . LEU A 59  ? 0.52971 0.42052 0.38975 0.19065  0.05111  -0.06492 59  LEU A N   
474  C CA  . LEU A 59  ? 0.53178 0.41717 0.37815 0.17011  -0.00379 -0.03991 59  LEU A CA  
475  C C   . LEU A 59  ? 0.57156 0.43024 0.40729 0.16939  0.00298  -0.01648 59  LEU A C   
476  O O   . LEU A 59  ? 0.61224 0.44552 0.43798 0.12814  -0.02050 -0.02843 59  LEU A O   
477  C CB  . LEU A 59  ? 0.50796 0.39208 0.35082 0.16390  0.02087  -0.04644 59  LEU A CB  
478  C CG  . LEU A 59  ? 0.47576 0.39815 0.33092 0.15070  0.00969  -0.02507 59  LEU A CG  
479  C CD1 . LEU A 59  ? 0.46705 0.38438 0.31539 0.16646  0.02531  -0.05921 59  LEU A CD1 
480  C CD2 . LEU A 59  ? 0.47195 0.38481 0.31222 0.13501  -0.00170 -0.00364 59  LEU A CD2 
481  N N   . ASP A 60  ? 0.57403 0.44197 0.41218 0.20339  0.03513  -0.01360 60  ASP A N   
482  C CA  . ASP A 60  ? 0.66857 0.47860 0.42055 0.17045  0.04407  0.02257  60  ASP A CA  
483  C C   . ASP A 60  ? 0.68101 0.46248 0.42377 0.10506  0.03712  0.00461  60  ASP A C   
484  O O   . ASP A 60  ? 0.69652 0.47530 0.41793 0.06198  0.00645  0.00127  60  ASP A O   
485  C CB  . ASP A 60  ? 0.74875 0.54956 0.44198 0.17823  0.03657  0.06094  60  ASP A CB  
486  C CG  . ASP A 60  ? 0.78679 0.61549 0.44116 0.19099  0.01900  0.11042  60  ASP A CG  
487  O OD1 . ASP A 60  ? 0.80369 0.62819 0.43839 0.21098  -0.00022 0.14196  60  ASP A OD1 
488  O OD2 . ASP A 60  ? 0.83159 0.64989 0.46911 0.16608  0.02979  0.09355  60  ASP A OD2 
489  N N   . GLU A 61  ? 0.64458 0.42988 0.42356 0.11437  0.05310  0.00747  61  GLU A N   
490  C CA  . GLU A 61  ? 0.66711 0.44288 0.43993 0.07275  0.03632  -0.01514 61  GLU A CA  
491  C C   . GLU A 61  ? 0.60894 0.40961 0.41119 0.06432  0.05348  -0.01529 61  GLU A C   
492  O O   . GLU A 61  ? 0.61517 0.40341 0.41959 0.06183  0.03038  -0.03015 61  GLU A O   
493  C CB  . GLU A 61  ? 0.74280 0.48415 0.48211 0.04467  0.01460  -0.03669 61  GLU A CB  
494  C CG  . GLU A 61  ? 0.81688 0.52393 0.51739 -0.00501 -0.00436 -0.03585 61  GLU A CG  
495  C CD  . GLU A 61  ? 0.88589 0.55588 0.56849 -0.03042 -0.01842 -0.03275 61  GLU A CD  
496  O OE1 . GLU A 61  ? 0.91789 0.57259 0.58519 -0.04611 -0.02899 -0.04566 61  GLU A OE1 
497  O OE2 . GLU A 61  ? 0.91169 0.56609 0.58629 -0.04267 -0.01578 -0.01756 61  GLU A OE2 
498  N N   . ILE A 62  ? 0.54156 0.34898 0.37543 0.06839  0.07703  -0.01620 62  ILE A N   
499  C CA  . ILE A 62  ? 0.51143 0.34178 0.35263 0.05249  0.06411  -0.00212 62  ILE A CA  
500  C C   . ILE A 62  ? 0.51598 0.35436 0.34255 0.05597  0.04767  -0.01234 62  ILE A C   
501  O O   . ILE A 62  ? 0.51189 0.37903 0.35165 0.11360  0.06355  -0.01647 62  ILE A O   
502  C CB  . ILE A 62  ? 0.52957 0.32196 0.34264 0.03422  0.03285  -0.00429 62  ILE A CB  
503  C CG1 . ILE A 62  ? 0.51750 0.33381 0.35639 0.05752  0.02532  -0.03162 62  ILE A CG1 
504  C CG2 . ILE A 62  ? 0.54365 0.29904 0.34399 0.01796  0.00511  0.00841  62  ILE A CG2 
505  C CD1 . ILE A 62  ? 0.52350 0.37531 0.35162 0.04228  0.04050  -0.04914 62  ILE A CD1 
506  N N   . ALA A 63  ? 0.50524 0.32907 0.34018 -0.00031 0.01022  -0.03935 63  ALA A N   
507  C CA  . ALA A 63  ? 0.50249 0.33888 0.32445 0.01537  0.00654  -0.04712 63  ALA A CA  
508  C C   . ALA A 63  ? 0.46002 0.30800 0.31341 0.03242  0.04705  -0.04967 63  ALA A C   
509  O O   . ALA A 63  ? 0.46734 0.29878 0.33578 0.01460  0.04645  -0.03868 63  ALA A O   
510  C CB  . ALA A 63  ? 0.49328 0.35423 0.35199 0.00956  -0.03586 -0.04520 63  ALA A CB  
511  N N   . PHE A 64  ? 0.38706 0.28878 0.28345 0.04705  0.02811  -0.06345 64  PHE A N   
512  C CA  . PHE A 64  ? 0.36224 0.32880 0.25838 0.02393  0.03173  -0.06070 64  PHE A CA  
513  C C   . PHE A 64  ? 0.36681 0.33615 0.27392 0.04582  0.02987  -0.03257 64  PHE A C   
514  O O   . PHE A 64  ? 0.40899 0.36185 0.27042 0.02487  0.04592  -0.01506 64  PHE A O   
515  C CB  . PHE A 64  ? 0.38056 0.34287 0.28170 0.00462  0.04526  -0.09005 64  PHE A CB  
516  C CG  . PHE A 64  ? 0.36615 0.34559 0.26566 0.02193  0.04353  -0.08322 64  PHE A CG  
517  C CD1 . PHE A 64  ? 0.38529 0.35231 0.28539 0.00844  0.01482  -0.06952 64  PHE A CD1 
518  C CD2 . PHE A 64  ? 0.39134 0.38281 0.26693 0.00154  0.02403  -0.08673 64  PHE A CD2 
519  C CE1 . PHE A 64  ? 0.38690 0.37115 0.28954 -0.02224 0.02233  -0.07652 64  PHE A CE1 
520  C CE2 . PHE A 64  ? 0.39104 0.39584 0.26551 0.01328  0.03825  -0.06257 64  PHE A CE2 
521  C CZ  . PHE A 64  ? 0.37231 0.39224 0.28308 -0.01228 0.01742  -0.05625 64  PHE A CZ  
522  N N   . ILE A 65  ? 0.36559 0.31801 0.24602 0.01728  0.03612  -0.02762 65  ILE A N   
523  C CA  . ILE A 65  ? 0.36852 0.33214 0.25410 0.03917  0.01245  -0.02657 65  ILE A CA  
524  C C   . ILE A 65  ? 0.33872 0.32173 0.28268 0.08438  0.01314  -0.03210 65  ILE A C   
525  O O   . ILE A 65  ? 0.33802 0.35012 0.31841 0.07472  0.05089  -0.02771 65  ILE A O   
526  C CB  . ILE A 65  ? 0.47364 0.36523 0.26859 0.05289  -0.03115 -0.04130 65  ILE A CB  
527  C CG1 . ILE A 65  ? 0.50615 0.40596 0.28150 0.04858  0.00365  -0.06009 65  ILE A CG1 
528  C CG2 . ILE A 65  ? 0.50292 0.37131 0.28235 0.08897  -0.06240 -0.01014 65  ILE A CG2 
529  C CD1 . ILE A 65  ? 0.54312 0.45316 0.29637 0.00921  -0.00281 -0.06594 65  ILE A CD1 
530  N N   . GLY A 66  ? 0.32103 0.29636 0.28723 0.08745  0.01751  -0.02208 66  GLY A N   
531  C CA  . GLY A 66  ? 0.36228 0.34410 0.28764 0.06012  0.01410  -0.01241 66  GLY A CA  
532  C C   . GLY A 66  ? 0.36571 0.37655 0.26203 0.07737  0.04230  -0.03277 66  GLY A C   
533  O O   . GLY A 66  ? 0.37488 0.42504 0.28115 0.10449  0.04033  0.00528  66  GLY A O   
534  N N   . ILE A 67  ? 0.37398 0.34314 0.22839 0.09107  0.06911  -0.01769 67  ILE A N   
535  C CA  . ILE A 67  ? 0.36152 0.38391 0.24094 0.10581  0.08283  -0.01184 67  ILE A CA  
536  C C   . ILE A 67  ? 0.39423 0.40296 0.27513 0.11865  0.09235  0.01356  67  ILE A C   
537  O O   . ILE A 67  ? 0.44344 0.40806 0.31991 0.09137  0.09549  -0.00330 67  ILE A O   
538  C CB  . ILE A 67  ? 0.36827 0.42487 0.23830 0.11443  0.03956  -0.01433 67  ILE A CB  
539  C CG1 . ILE A 67  ? 0.38059 0.45145 0.27894 0.14159  0.04493  -0.05960 67  ILE A CG1 
540  C CG2 . ILE A 67  ? 0.43692 0.45956 0.23499 0.12052  0.03853  0.03595  67  ILE A CG2 
541  C CD1 . ILE A 67  ? 0.38923 0.46585 0.29688 0.12690  0.01003  -0.10536 67  ILE A CD1 
542  N N   . HIS A 68  ? 0.39264 0.45976 0.28374 0.11287  0.10047  0.01365  68  HIS A N   
543  C CA  . HIS A 68  ? 0.44934 0.47633 0.34354 0.13878  0.08119  0.06240  68  HIS A CA  
544  C C   . HIS A 68  ? 0.44460 0.54564 0.37873 0.13321  0.04611  0.08843  68  HIS A C   
545  O O   . HIS A 68  ? 0.46682 0.55064 0.40314 0.12408  -0.00329 0.10713  68  HIS A O   
546  C CB  . HIS A 68  ? 0.50140 0.45786 0.38404 0.14939  0.06601  0.05565  68  HIS A CB  
547  C CG  . HIS A 68  ? 0.48538 0.44640 0.41771 0.17889  0.06356  0.06030  68  HIS A CG  
548  N ND1 . HIS A 68  ? 0.53574 0.44786 0.46299 0.14197  0.03849  0.07953  68  HIS A ND1 
549  C CD2 . HIS A 68  ? 0.47769 0.44377 0.41779 0.20124  0.10247  0.04428  68  HIS A CD2 
550  C CE1 . HIS A 68  ? 0.51186 0.43895 0.45239 0.15751  0.03934  0.07324  68  HIS A CE1 
551  N NE2 . HIS A 68  ? 0.50699 0.44724 0.43069 0.20148  0.07491  0.05169  68  HIS A NE2 
552  N N   . THR A 69  ? 0.47564 0.59378 0.40983 0.15849  0.04316  0.09732  69  THR A N   
553  C CA  . THR A 69  ? 0.57202 0.62969 0.45847 0.10354  0.07176  0.10914  69  THR A CA  
554  C C   . THR A 69  ? 0.64955 0.64046 0.48905 0.07364  0.08501  0.08768  69  THR A C   
555  O O   . THR A 69  ? 0.67905 0.61918 0.46907 0.09129  0.09355  0.10774  69  THR A O   
556  C CB  . THR A 69  ? 0.55142 0.66145 0.48583 0.08911  0.06208  0.10392  69  THR A CB  
557  O OG1 . THR A 69  ? 0.56323 0.70079 0.49492 0.07757  0.04419  0.11978  69  THR A OG1 
558  C CG2 . THR A 69  ? 0.57004 0.67255 0.50455 0.06619  0.06629  0.10868  69  THR A CG2 
559  N N   . GLY A 70  ? 0.68244 0.66399 0.52816 0.03620  0.05638  0.06099  70  GLY A N   
560  C CA  . GLY A 70  ? 0.67542 0.67135 0.55811 0.04617  0.04105  0.05660  70  GLY A CA  
561  C C   . GLY A 70  ? 0.67798 0.69442 0.57385 0.06767  0.03478  0.05183  70  GLY A C   
562  O O   . GLY A 70  ? 0.64019 0.68494 0.57531 0.10678  0.01679  0.05296  70  GLY A O   
563  N N   . HIS A 71  ? 0.70465 0.73064 0.57929 0.03231  0.04347  0.04804  71  HIS A N   
564  C CA  . HIS A 71  ? 0.73039 0.76284 0.60053 0.02725  0.03815  0.04488  71  HIS A CA  
565  C C   . HIS A 71  ? 0.72950 0.78227 0.56479 0.01262  0.02927  0.03743  71  HIS A C   
566  O O   . HIS A 71  ? 0.72890 0.78203 0.55678 0.00420  0.02058  0.05149  71  HIS A O   
567  C CB  . HIS A 71  ? 0.72630 0.77662 0.64197 0.04297  0.04034  0.04776  71  HIS A CB  
568  C CG  . HIS A 71  ? 0.71471 0.78179 0.67853 0.04875  0.02657  0.06467  71  HIS A CG  
569  N ND1 . HIS A 71  ? 0.70689 0.78563 0.69791 0.05480  0.02196  0.06958  71  HIS A ND1 
570  C CD2 . HIS A 71  ? 0.70226 0.78173 0.69636 0.05418  0.02268  0.07131  71  HIS A CD2 
571  C CE1 . HIS A 71  ? 0.70086 0.78424 0.70745 0.06420  0.02151  0.07508  71  HIS A CE1 
572  N NE2 . HIS A 71  ? 0.69197 0.78389 0.71199 0.06090  0.02102  0.06986  71  HIS A NE2 
573  N N   . LEU A 72  ? 0.71276 0.78556 0.52276 0.02375  0.02324  0.00772  72  LEU A N   
574  C CA  . LEU A 72  ? 0.68824 0.78120 0.48265 0.04412  -0.00445 -0.00657 72  LEU A CA  
575  C C   . LEU A 72  ? 0.66699 0.78514 0.45721 0.07468  -0.02805 -0.00177 72  LEU A C   
576  O O   . LEU A 72  ? 0.72434 0.79623 0.47290 0.05918  -0.03782 0.00665  72  LEU A O   
577  C CB  . LEU A 72  ? 0.67077 0.77198 0.49670 0.04294  -0.00317 -0.01143 72  LEU A CB  
578  C CG  . LEU A 72  ? 0.67415 0.77239 0.52472 0.06257  0.00902  -0.01149 72  LEU A CG  
579  C CD1 . LEU A 72  ? 0.68373 0.78508 0.53049 0.06284  0.01510  -0.00732 72  LEU A CD1 
580  C CD2 . LEU A 72  ? 0.67998 0.75860 0.54128 0.08065  0.00705  -0.00930 72  LEU A CD2 
581  N N   . GLY A 73  ? 0.61907 0.75908 0.41321 0.10048  -0.07826 -0.00172 73  GLY A N   
582  C CA  . GLY A 73  ? 0.53522 0.70928 0.35309 0.08764  -0.08489 -0.06474 73  GLY A CA  
583  C C   . GLY A 73  ? 0.48732 0.65556 0.33213 0.09397  -0.10744 -0.09101 73  GLY A C   
584  O O   . GLY A 73  ? 0.55686 0.66514 0.36946 0.11463  -0.09170 -0.08225 73  GLY A O   
585  N N   . PHE A 74  ? 0.41958 0.60047 0.30854 0.11678  -0.02176 -0.11096 74  PHE A N   
586  C CA  . PHE A 74  ? 0.34115 0.53946 0.27131 0.03754  0.01852  -0.15184 74  PHE A CA  
587  C C   . PHE A 74  ? 0.32542 0.52413 0.31932 -0.05466 0.04252  -0.15627 74  PHE A C   
588  O O   . PHE A 74  ? 0.30761 0.58808 0.39594 -0.06580 0.09419  -0.17247 74  PHE A O   
589  C CB  . PHE A 74  ? 0.40539 0.57301 0.22180 0.02726  0.04522  -0.14251 74  PHE A CB  
590  C CG  . PHE A 74  ? 0.44598 0.59681 0.20127 -0.03302 0.05588  -0.12011 74  PHE A CG  
591  C CD1 . PHE A 74  ? 0.49823 0.62535 0.17884 -0.00655 -0.00157 -0.09125 74  PHE A CD1 
592  C CD2 . PHE A 74  ? 0.49171 0.62808 0.22731 -0.02707 0.05213  -0.09534 74  PHE A CD2 
593  C CE1 . PHE A 74  ? 0.49300 0.63571 0.17775 -0.05101 0.03196  -0.06845 74  PHE A CE1 
594  C CE2 . PHE A 74  ? 0.50735 0.64872 0.29232 -0.01232 0.04370  -0.05145 74  PHE A CE2 
595  C CZ  . PHE A 74  ? 0.53037 0.65945 0.26041 -0.01025 0.02117  -0.06241 74  PHE A CZ  
596  N N   . TYR A 75  ? 0.31335 0.42414 0.25422 0.00560  0.02197  -0.13532 75  TYR A N   
597  C CA  . TYR A 75  ? 0.36618 0.42506 0.21581 -0.01323 0.02442  -0.10153 75  TYR A CA  
598  C C   . TYR A 75  ? 0.51296 0.47590 0.25625 0.10328  0.03016  -0.13872 75  TYR A C   
599  O O   . TYR A 75  ? 0.59068 0.50043 0.32020 0.07295  -0.04245 -0.12707 75  TYR A O   
600  C CB  . TYR A 75  ? 0.37354 0.36025 0.22517 -0.02995 0.03917  -0.07458 75  TYR A CB  
601  C CG  . TYR A 75  ? 0.34645 0.30085 0.20821 -0.00390 0.03486  -0.07031 75  TYR A CG  
602  C CD1 . TYR A 75  ? 0.30221 0.32807 0.19314 -0.02190 0.02215  -0.02970 75  TYR A CD1 
603  C CD2 . TYR A 75  ? 0.31308 0.29349 0.20717 0.02071  0.03406  -0.04695 75  TYR A CD2 
604  C CE1 . TYR A 75  ? 0.29652 0.33584 0.19558 -0.00131 0.01872  -0.06521 75  TYR A CE1 
605  C CE2 . TYR A 75  ? 0.31201 0.29916 0.20422 0.03631  0.06031  -0.01761 75  TYR A CE2 
606  C CZ  . TYR A 75  ? 0.28889 0.30575 0.19328 0.02601  0.02866  -0.02326 75  TYR A CZ  
607  O OH  . TYR A 75  ? 0.29652 0.29352 0.18962 0.03740  0.03350  -0.01170 75  TYR A OH  
608  N N   . ALA A 76  ? 0.53255 0.51592 0.27408 0.07927  0.10752  -0.09930 76  ALA A N   
609  C CA  . ALA A 76  ? 0.52050 0.55519 0.27263 0.11047  0.10604  -0.09557 76  ALA A CA  
610  C C   . ALA A 76  ? 0.53664 0.55814 0.30165 0.16048  0.04825  -0.11503 76  ALA A C   
611  O O   . ALA A 76  ? 0.49249 0.50751 0.34064 0.17853  -0.05481 -0.10606 76  ALA A O   
612  C CB  . ALA A 76  ? 0.49130 0.60766 0.22210 0.02279  0.14280  -0.04183 76  ALA A CB  
613  N N   . ASP A 77  ? 0.56220 0.60209 0.34245 0.15054  0.06039  -0.05656 77  ASP A N   
614  C CA  . ASP A 77  ? 0.57765 0.64271 0.33081 0.13792  0.09200  -0.03888 77  ASP A CA  
615  C C   . ASP A 77  ? 0.56303 0.66004 0.36969 0.11398  0.09521  -0.01710 77  ASP A C   
616  O O   . ASP A 77  ? 0.57484 0.68325 0.37169 0.10879  0.10900  -0.02698 77  ASP A O   
617  C CB  . ASP A 77  ? 0.61328 0.68123 0.32857 0.12331  0.12703  -0.01878 77  ASP A CB  
618  C CG  . ASP A 77  ? 0.65908 0.69589 0.33993 0.15031  0.12094  -0.01332 77  ASP A CG  
619  O OD1 . ASP A 77  ? 0.65513 0.68875 0.36762 0.17865  0.07814  -0.01825 77  ASP A OD1 
620  O OD2 . ASP A 77  ? 0.68129 0.69551 0.35631 0.14561  0.12951  -0.02515 77  ASP A OD2 
621  N N   . TRP A 78  ? 0.46454 0.62925 0.37820 0.10039  0.09977  -0.01758 78  TRP A N   
622  C CA  . TRP A 78  ? 0.49041 0.61151 0.36699 0.11420  0.08542  -0.04388 78  TRP A CA  
623  C C   . TRP A 78  ? 0.49356 0.56611 0.31450 0.13149  0.06781  -0.02395 78  TRP A C   
624  O O   . TRP A 78  ? 0.51011 0.51131 0.26107 0.13322  0.05727  -0.02285 78  TRP A O   
625  C CB  . TRP A 78  ? 0.49771 0.60679 0.35388 0.11420  0.10292  -0.08860 78  TRP A CB  
626  C CG  . TRP A 78  ? 0.52278 0.60631 0.36114 0.08956  0.06839  -0.09664 78  TRP A CG  
627  C CD1 . TRP A 78  ? 0.51479 0.60317 0.35279 0.08822  0.04733  -0.12112 78  TRP A CD1 
628  C CD2 . TRP A 78  ? 0.54516 0.61038 0.37369 0.07065  0.01871  -0.10724 78  TRP A CD2 
629  N NE1 . TRP A 78  ? 0.50831 0.59466 0.35489 0.09195  0.05003  -0.13677 78  TRP A NE1 
630  C CE2 . TRP A 78  ? 0.55810 0.60801 0.37509 0.06846  0.00834  -0.11718 78  TRP A CE2 
631  C CE3 . TRP A 78  ? 0.56252 0.61702 0.38099 0.05621  -0.03020 -0.09120 78  TRP A CE3 
632  C CZ2 . TRP A 78  ? 0.59799 0.62274 0.39109 0.04370  -0.02733 -0.10587 78  TRP A CZ2 
633  C CZ3 . TRP A 78  ? 0.59055 0.62871 0.38239 0.05554  -0.04430 -0.09359 78  TRP A CZ3 
634  C CH2 . TRP A 78  ? 0.60369 0.63077 0.38739 0.03923  -0.05037 -0.09628 78  TRP A CH2 
635  N N   . ARG A 79  ? 0.50314 0.59587 0.32655 0.17612  0.00390  -0.05090 79  ARG A N   
636  C CA  . ARG A 79  ? 0.48662 0.63202 0.35815 0.19528  0.02697  -0.04789 79  ARG A CA  
637  C C   . ARG A 79  ? 0.49017 0.63504 0.35800 0.23060  0.00477  -0.06793 79  ARG A C   
638  O O   . ARG A 79  ? 0.51264 0.65140 0.37125 0.24458  -0.05383 -0.06798 79  ARG A O   
639  C CB  . ARG A 79  ? 0.49876 0.64747 0.40563 0.21859  0.03031  -0.01308 79  ARG A CB  
640  C CG  . ARG A 79  ? 0.52825 0.68359 0.43908 0.19382  0.03066  0.00373  79  ARG A CG  
641  C CD  . ARG A 79  ? 0.58459 0.70448 0.45997 0.17094  0.01619  0.02625  79  ARG A CD  
642  N NE  . ARG A 79  ? 0.63224 0.72356 0.47845 0.13929  0.02579  -0.00258 79  ARG A NE  
643  C CZ  . ARG A 79  ? 0.67442 0.73760 0.50759 0.10703  0.01309  0.00885  79  ARG A CZ  
644  N NH1 . ARG A 79  ? 0.67640 0.73921 0.52099 0.10223  0.02083  0.00598  79  ARG A NH1 
645  N NH2 . ARG A 79  ? 0.69239 0.73888 0.51639 0.09594  -0.00776 0.02111  79  ARG A NH2 
646  N N   . PRO A 80  ? 0.50621 0.64783 0.36167 0.22588  0.02338  -0.03700 80  PRO A N   
647  C CA  . PRO A 80  ? 0.52838 0.67788 0.35970 0.23345  -0.00394 -0.03492 80  PRO A CA  
648  C C   . PRO A 80  ? 0.55655 0.72078 0.37405 0.24595  -0.01523 -0.06181 80  PRO A C   
649  O O   . PRO A 80  ? 0.57258 0.72658 0.36931 0.25165  -0.00838 -0.05693 80  PRO A O   
650  C CB  . PRO A 80  ? 0.53784 0.67738 0.37337 0.22339  0.01068  -0.00820 80  PRO A CB  
651  C CG  . PRO A 80  ? 0.52067 0.66221 0.38412 0.23422  0.02782  0.00022  80  PRO A CG  
652  C CD  . PRO A 80  ? 0.50811 0.65316 0.37109 0.22575  0.05054  -0.01581 80  PRO A CD  
653  N N   . ALA A 81  ? 0.53621 0.75314 0.38095 0.22983  -0.05310 -0.08512 81  ALA A N   
654  C CA  . ALA A 81  ? 0.53786 0.76621 0.41002 0.21614  -0.07512 -0.12513 81  ALA A CA  
655  C C   . ALA A 81  ? 0.51892 0.77965 0.43021 0.21063  -0.06093 -0.15246 81  ALA A C   
656  O O   . ALA A 81  ? 0.51406 0.80265 0.43165 0.23639  -0.06929 -0.16622 81  ALA A O   
657  C CB  . ALA A 81  ? 0.56630 0.78399 0.41733 0.20560  -0.07790 -0.13329 81  ALA A CB  
658  N N   . GLU A 82  ? 0.47176 0.77038 0.44427 0.19252  0.00110  -0.14383 82  GLU A N   
659  C CA  . GLU A 82  ? 0.47476 0.78358 0.46178 0.10445  0.02361  -0.13496 82  GLU A CA  
660  C C   . GLU A 82  ? 0.47147 0.75114 0.43773 0.06939  0.06394  -0.15525 82  GLU A C   
661  O O   . GLU A 82  ? 0.45079 0.72885 0.45054 0.03748  0.10962  -0.17770 82  GLU A O   
662  C CB  . GLU A 82  ? 0.50829 0.82622 0.49001 0.07138  0.02888  -0.09913 82  GLU A CB  
663  C CG  . GLU A 82  ? 0.55939 0.86616 0.51381 0.05469  0.02763  -0.08094 82  GLU A CG  
664  C CD  . GLU A 82  ? 0.55998 0.89159 0.52357 0.00925  0.01703  -0.07703 82  GLU A CD  
665  O OE1 . GLU A 82  ? 0.52623 0.88528 0.52159 0.01198  -0.00338 -0.07098 82  GLU A OE1 
666  O OE2 . GLU A 82  ? 0.56812 0.90376 0.54253 -0.02460 0.00236  -0.08143 82  GLU A OE2 
667  N N   . ALA A 83  ? 0.45733 0.74817 0.40773 0.06084  0.06671  -0.15524 83  ALA A N   
668  C CA  . ALA A 83  ? 0.49067 0.74251 0.40805 0.06812  0.06713  -0.13269 83  ALA A CA  
669  C C   . ALA A 83  ? 0.52271 0.74253 0.39426 0.08246  0.09155  -0.12374 83  ALA A C   
670  O O   . ALA A 83  ? 0.48807 0.75502 0.38446 0.08696  0.11729  -0.13135 83  ALA A O   
671  C CB  . ALA A 83  ? 0.51993 0.75219 0.43619 0.06856  0.04375  -0.11535 83  ALA A CB  
672  N N   . ASP A 84  ? 0.56609 0.74091 0.39562 0.07357  0.08393  -0.12902 84  ASP A N   
673  C CA  . ASP A 84  ? 0.58164 0.74499 0.40853 0.03669  0.08017  -0.12797 84  ASP A CA  
674  C C   . ASP A 84  ? 0.53955 0.72726 0.42351 0.00675  0.07122  -0.14919 84  ASP A C   
675  O O   . ASP A 84  ? 0.51415 0.76199 0.44133 0.00020  0.07363  -0.17283 84  ASP A O   
676  C CB  . ASP A 84  ? 0.62256 0.77414 0.40980 0.01889  0.08721  -0.10641 84  ASP A CB  
677  C CG  . ASP A 84  ? 0.68047 0.79473 0.43739 -0.00639 0.08224  -0.05869 84  ASP A CG  
678  O OD1 . ASP A 84  ? 0.70249 0.80245 0.45699 -0.02018 0.09292  -0.03547 84  ASP A OD1 
679  O OD2 . ASP A 84  ? 0.70239 0.80225 0.44849 -0.00944 0.08481  -0.03664 84  ASP A OD2 
680  N N   . LYS A 85  ? 0.50867 0.70139 0.41482 0.00052  0.09164  -0.15617 85  LYS A N   
681  C CA  . LYS A 85  ? 0.52576 0.66429 0.44889 -0.02110 0.08771  -0.16489 85  LYS A CA  
682  C C   . LYS A 85  ? 0.52535 0.62513 0.45064 -0.03229 0.08658  -0.15542 85  LYS A C   
683  O O   . LYS A 85  ? 0.52831 0.62364 0.45525 -0.02474 0.10150  -0.17473 85  LYS A O   
684  C CB  . LYS A 85  ? 0.51907 0.67457 0.47189 -0.01833 0.07734  -0.15505 85  LYS A CB  
685  N N   . LEU A 86  ? 0.51282 0.60083 0.44863 -0.01463 0.10275  -0.15724 86  LEU A N   
686  C CA  . LEU A 86  ? 0.50763 0.56967 0.44714 -0.02235 0.10300  -0.15876 86  LEU A CA  
687  C C   . LEU A 86  ? 0.52484 0.60062 0.45819 -0.00908 0.11693  -0.13541 86  LEU A C   
688  O O   . LEU A 86  ? 0.54920 0.61497 0.45596 -0.01312 0.13640  -0.12222 86  LEU A O   
689  C CB  . LEU A 86  ? 0.50490 0.55129 0.43735 -0.02741 0.07960  -0.16758 86  LEU A CB  
690  C CG  . LEU A 86  ? 0.52228 0.53825 0.42686 -0.06638 0.04535  -0.14669 86  LEU A CG  
691  C CD1 . LEU A 86  ? 0.52990 0.56613 0.43279 -0.09073 0.03142  -0.12353 86  LEU A CD1 
692  C CD2 . LEU A 86  ? 0.53949 0.52005 0.40849 -0.05411 0.06161  -0.15582 86  LEU A CD2 
693  N N   . VAL A 87  ? 0.48190 0.59447 0.45279 0.01710  0.12562  -0.14886 87  VAL A N   
694  C CA  . VAL A 87  ? 0.48308 0.58628 0.46262 0.02928  0.12450  -0.17851 87  VAL A CA  
695  C C   . VAL A 87  ? 0.53059 0.61536 0.49753 0.03631  0.13588  -0.17607 87  VAL A C   
696  O O   . VAL A 87  ? 0.55533 0.62305 0.49525 0.01843  0.11874  -0.16563 87  VAL A O   
697  C CB  . VAL A 87  ? 0.44184 0.56351 0.46171 0.05181  0.11870  -0.20861 87  VAL A CB  
698  C CG1 . VAL A 87  ? 0.49094 0.56820 0.44996 0.04574  0.11474  -0.23216 87  VAL A CG1 
699  C CG2 . VAL A 87  ? 0.46120 0.56736 0.46696 0.03963  0.09467  -0.18616 87  VAL A CG2 
700  N N   . LYS A 88  ? 0.56721 0.63421 0.53605 0.03757  0.17012  -0.19118 88  LYS A N   
701  C CA  . LYS A 88  ? 0.60553 0.64743 0.57082 0.01504  0.16471  -0.17931 88  LYS A CA  
702  C C   . LYS A 88  ? 0.62399 0.64118 0.59883 0.01457  0.18994  -0.19732 88  LYS A C   
703  O O   . LYS A 88  ? 0.64706 0.61934 0.60923 0.03232  0.20854  -0.22241 88  LYS A O   
704  C CB  . LYS A 88  ? 0.64617 0.67091 0.59010 0.01211  0.13852  -0.14899 88  LYS A CB  
705  C CG  . LYS A 88  ? 0.67335 0.68632 0.59407 0.02714  0.12297  -0.12750 88  LYS A CG  
706  C CD  . LYS A 88  ? 0.70502 0.70363 0.60404 0.04370  0.09137  -0.10265 88  LYS A CD  
707  C CE  . LYS A 88  ? 0.74120 0.72393 0.60717 0.05435  0.06918  -0.07278 88  LYS A CE  
708  N NZ  . LYS A 88  ? 0.75653 0.73927 0.60687 0.04769  0.05479  -0.04664 88  LYS A NZ  
709  N N   . LEU A 89  ? 0.64612 0.65075 0.60725 -0.00738 0.18014  -0.20181 89  LEU A N   
710  C CA  . LEU A 89  ? 0.64963 0.66616 0.62385 -0.00106 0.18976  -0.18219 89  LEU A CA  
711  C C   . LEU A 89  ? 0.65520 0.66384 0.62728 0.00164  0.22918  -0.16640 89  LEU A C   
712  O O   . LEU A 89  ? 0.66460 0.64623 0.62436 -0.00319 0.21442  -0.17537 89  LEU A O   
713  C CB  . LEU A 89  ? 0.64714 0.70521 0.64450 -0.00777 0.15836  -0.16610 89  LEU A CB  
714  C CG  . LEU A 89  ? 0.66679 0.74224 0.67133 -0.01460 0.12799  -0.14607 89  LEU A CG  
715  C CD1 . LEU A 89  ? 0.66443 0.74914 0.67911 0.00558  0.11391  -0.14142 89  LEU A CD1 
716  C CD2 . LEU A 89  ? 0.66916 0.76089 0.68461 -0.04716 0.10068  -0.13280 89  LEU A CD2 
717  N N   . LEU A 90  ? 0.65141 0.69117 0.63719 0.00599  0.29298  -0.13198 90  LEU A N   
718  C CA  . LEU A 90  ? 0.64142 0.70630 0.65883 -0.00363 0.31077  -0.08068 90  LEU A CA  
719  C C   . LEU A 90  ? 0.72110 0.72225 0.69758 0.00112  0.28519  -0.07735 90  LEU A C   
720  O O   . LEU A 90  ? 0.75649 0.72422 0.70099 0.02281  0.27074  -0.08081 90  LEU A O   
721  C CB  . LEU A 90  ? 0.61104 0.72686 0.65132 -0.07243 0.32855  -0.01157 90  LEU A CB  
722  C CG  . LEU A 90  ? 0.58783 0.75612 0.64862 -0.14491 0.31613  0.04796  90  LEU A CG  
723  C CD1 . LEU A 90  ? 0.56068 0.76752 0.64798 -0.16993 0.30777  0.07137  90  LEU A CD1 
724  C CD2 . LEU A 90  ? 0.59687 0.77893 0.64195 -0.15325 0.30859  0.05899  90  LEU A CD2 
725  N N   . ALA A 91  ? 0.75324 0.73956 0.72925 0.01988  0.28075  -0.08836 91  ALA A N   
726  C CA  . ALA A 91  ? 0.79974 0.76523 0.76071 0.03710  0.26037  -0.09790 91  ALA A CA  
727  C C   . ALA A 91  ? 0.84748 0.79367 0.79195 0.04398  0.22437  -0.10743 91  ALA A C   
728  O O   . ALA A 91  ? 0.86282 0.80472 0.81104 0.05197  0.20828  -0.09371 91  ALA A O   
729  C CB  . ALA A 91  ? 0.79024 0.76673 0.76497 0.05215  0.26962  -0.09536 91  ALA A CB  
730  N N   . LYS A 92  ? 0.86030 0.80975 0.79497 0.05371  0.20817  -0.13424 92  LYS A N   
731  C CA  . LYS A 92  ? 0.88739 0.83732 0.81116 0.02590  0.17580  -0.13937 92  LYS A CA  
732  C C   . LYS A 92  ? 0.92633 0.82788 0.81070 -0.00348 0.15950  -0.15294 92  LYS A C   
733  O O   . LYS A 92  ? 0.94125 0.83497 0.81133 0.00383  0.15405  -0.15755 92  LYS A O   
734  C CB  . LYS A 92  ? 0.89164 0.87320 0.82676 0.01807  0.15781  -0.12506 92  LYS A CB  
735  C CG  . LYS A 92  ? 0.89483 0.90309 0.83914 0.01232  0.13775  -0.11272 92  LYS A CG  
736  C CD  . LYS A 92  ? 0.89100 0.92342 0.84529 0.00958  0.12526  -0.10025 92  LYS A CD  
737  C CE  . LYS A 92  ? 0.88062 0.93781 0.84898 0.01243  0.11568  -0.09208 92  LYS A CE  
738  N NZ  . LYS A 92  ? 0.87729 0.94718 0.85131 0.01564  0.10838  -0.09019 92  LYS A NZ  
739  N N   . GLY A 93  ? 0.93948 0.81949 0.80861 -0.02967 0.15310  -0.17161 93  GLY A N   
740  C CA  . GLY A 93  ? 0.94923 0.80942 0.80769 -0.04743 0.13721  -0.20045 93  GLY A CA  
741  C C   . GLY A 93  ? 0.96763 0.80042 0.80308 -0.05253 0.13429  -0.23195 93  GLY A C   
742  O O   . GLY A 93  ? 0.99925 0.77983 0.79810 -0.06251 0.12955  -0.25020 93  GLY A O   
743  N N   . GLU A 94  ? 0.95271 0.81836 0.81219 -0.05106 0.12904  -0.22410 94  GLU A N   
744  C CA  . GLU A 94  ? 0.92942 0.84401 0.82193 -0.05808 0.10279  -0.19913 94  GLU A CA  
745  C C   . GLU A 94  ? 0.91020 0.83869 0.82696 -0.07141 0.06508  -0.17643 94  GLU A C   
746  O O   . GLU A 94  ? 0.91831 0.86086 0.83005 -0.08143 0.05635  -0.16678 94  GLU A O   
747  C CB  . GLU A 94  ? 0.92020 0.85742 0.82378 -0.06053 0.10788  -0.18796 94  GLU A CB  
748  N N   . TYR A 95  ? 0.87550 0.80635 0.82254 -0.07516 0.03732  -0.16369 95  TYR A N   
749  C CA  . TYR A 95  ? 0.82034 0.76010 0.80619 -0.08624 0.00163  -0.15903 95  TYR A CA  
750  C C   . TYR A 95  ? 0.80471 0.75356 0.79658 -0.09204 -0.01332 -0.14467 95  TYR A C   
751  O O   . TYR A 95  ? 0.82850 0.73948 0.81806 -0.09257 -0.00785 -0.13662 95  TYR A O   
752  C CB  . TYR A 95  ? 0.77794 0.71700 0.80818 -0.08385 -0.01245 -0.15660 95  TYR A CB  
753  C CG  . TYR A 95  ? 0.76110 0.67594 0.81601 -0.07982 -0.03206 -0.15082 95  TYR A CG  
754  C CD1 . TYR A 95  ? 0.75860 0.66117 0.82188 -0.06697 -0.04356 -0.14145 95  TYR A CD1 
755  C CD2 . TYR A 95  ? 0.75512 0.65083 0.82019 -0.06413 -0.04339 -0.15578 95  TYR A CD2 
756  C CE1 . TYR A 95  ? 0.75962 0.65180 0.82277 -0.03984 -0.05229 -0.14152 95  TYR A CE1 
757  C CE2 . TYR A 95  ? 0.76078 0.63523 0.82202 -0.04581 -0.05108 -0.15253 95  TYR A CE2 
758  C CZ  . TYR A 95  ? 0.76749 0.65465 0.82710 -0.03230 -0.05915 -0.13963 95  TYR A CZ  
759  O OH  . TYR A 95  ? 0.79263 0.68146 0.82982 -0.02802 -0.07452 -0.14214 95  TYR A OH  
760  N N   . GLN A 96  ? 0.75911 0.75287 0.75520 -0.10510 -0.03157 -0.13867 96  GLN A N   
761  C CA  . GLN A 96  ? 0.71971 0.73754 0.70972 -0.12172 -0.04435 -0.13347 96  GLN A CA  
762  C C   . GLN A 96  ? 0.63186 0.66744 0.63386 -0.16710 -0.05386 -0.15849 96  GLN A C   
763  O O   . GLN A 96  ? 0.63189 0.67672 0.61742 -0.19100 -0.10393 -0.16873 96  GLN A O   
764  C CB  . GLN A 96  ? 0.76654 0.78617 0.74605 -0.08733 -0.04450 -0.10078 96  GLN A CB  
765  C CG  . GLN A 96  ? 0.80873 0.82300 0.79319 -0.05145 -0.04470 -0.08631 96  GLN A CG  
766  C CD  . GLN A 96  ? 0.83555 0.84946 0.82609 -0.02358 -0.04664 -0.07265 96  GLN A CD  
767  O OE1 . GLN A 96  ? 0.84490 0.85762 0.83619 -0.01182 -0.04539 -0.06475 96  GLN A OE1 
768  N NE2 . GLN A 96  ? 0.84898 0.85762 0.83749 -0.01136 -0.04443 -0.06835 96  GLN A NE2 
769  N N   . LYS A 97  ? 0.55072 0.58558 0.57226 -0.15246 0.00450  -0.16828 97  LYS A N   
770  C CA  . LYS A 97  ? 0.51052 0.53316 0.52223 -0.10390 0.05092  -0.16852 97  LYS A CA  
771  C C   . LYS A 97  ? 0.50596 0.53311 0.48313 -0.08682 0.06542  -0.13248 97  LYS A C   
772  O O   . LYS A 97  ? 0.52213 0.54664 0.51858 -0.07823 0.06635  -0.10820 97  LYS A O   
773  C CB  . LYS A 97  ? 0.52248 0.51551 0.53955 -0.07434 0.08825  -0.13686 97  LYS A CB  
774  C CG  . LYS A 97  ? 0.53116 0.52940 0.56821 -0.05412 0.09250  -0.10500 97  LYS A CG  
775  C CD  . LYS A 97  ? 0.55136 0.55900 0.58803 -0.03778 0.10843  -0.08554 97  LYS A CD  
776  C CE  . LYS A 97  ? 0.57164 0.59764 0.60162 -0.02379 0.11177  -0.05339 97  LYS A CE  
777  N NZ  . LYS A 97  ? 0.57731 0.62850 0.61330 -0.00712 0.11267  -0.03607 97  LYS A NZ  
778  N N   . VAL A 98  ? 0.46747 0.50430 0.41046 -0.09029 0.03818  -0.13194 98  VAL A N   
779  C CA  . VAL A 98  ? 0.44940 0.49366 0.41379 -0.06769 0.00065  -0.12459 98  VAL A CA  
780  C C   . VAL A 98  ? 0.42412 0.43069 0.35376 -0.06030 0.01646  -0.11728 98  VAL A C   
781  O O   . VAL A 98  ? 0.40962 0.44856 0.33409 -0.07185 0.02727  -0.10297 98  VAL A O   
782  C CB  . VAL A 98  ? 0.45170 0.55314 0.45256 -0.02193 -0.05300 -0.07327 98  VAL A CB  
783  C CG1 . VAL A 98  ? 0.47969 0.57900 0.45988 -0.00933 -0.09321 -0.08302 98  VAL A CG1 
784  C CG2 . VAL A 98  ? 0.49248 0.58811 0.45741 -0.02423 -0.02889 -0.05676 98  VAL A CG2 
785  N N   . SER A 99  ? 0.43326 0.37872 0.32424 -0.04118 0.06711  -0.14912 99  SER A N   
786  C CA  . SER A 99  ? 0.45208 0.39443 0.35495 -0.03985 0.03638  -0.12746 99  SER A CA  
787  C C   . SER A 99  ? 0.41728 0.39344 0.33599 -0.04557 0.03580  -0.11112 99  SER A C   
788  O O   . SER A 99  ? 0.42722 0.41526 0.36757 -0.06334 0.06411  -0.13685 99  SER A O   
789  C CB  . SER A 99  ? 0.55178 0.39373 0.41619 -0.04707 0.01979  -0.16853 99  SER A CB  
790  O OG  . SER A 99  ? 0.62059 0.42922 0.48414 -0.07757 -0.00067 -0.14610 99  SER A OG  
791  N N   . TYR A 100 ? 0.33042 0.35559 0.28049 -0.04080 0.00895  -0.08668 100 TYR A N   
792  C CA  . TYR A 100 ? 0.33741 0.37357 0.27175 0.06689  0.01184  -0.07072 100 TYR A CA  
793  C C   . TYR A 100 ? 0.33287 0.34969 0.27203 0.06013  0.04504  -0.03438 100 TYR A C   
794  O O   . TYR A 100 ? 0.32632 0.33129 0.28015 0.03287  0.04315  -0.00983 100 TYR A O   
795  C CB  . TYR A 100 ? 0.38399 0.37737 0.26677 0.08604  -0.01232 -0.06596 100 TYR A CB  
796  C CG  . TYR A 100 ? 0.43122 0.40505 0.25515 0.08704  -0.02140 -0.13347 100 TYR A CG  
797  C CD1 . TYR A 100 ? 0.47213 0.42812 0.26935 0.11217  -0.03795 -0.14126 100 TYR A CD1 
798  C CD2 . TYR A 100 ? 0.49893 0.44187 0.25916 0.10069  -0.03529 -0.10489 100 TYR A CD2 
799  C CE1 . TYR A 100 ? 0.54433 0.44815 0.28430 0.10572  -0.04674 -0.12429 100 TYR A CE1 
800  C CE2 . TYR A 100 ? 0.55745 0.44471 0.27921 0.11919  -0.06087 -0.09572 100 TYR A CE2 
801  C CZ  . TYR A 100 ? 0.58622 0.46267 0.28704 0.13954  -0.07368 -0.10389 100 TYR A CZ  
802  O OH  . TYR A 100 ? 0.60553 0.49301 0.33125 0.19228  -0.12401 -0.06564 100 TYR A OH  
803  N N   . PRO A 101 ? 0.32383 0.31360 0.27067 0.04055  0.03173  -0.02759 101 PRO A N   
804  C CA  . PRO A 101 ? 0.29624 0.30357 0.24693 0.04027  0.02430  -0.00870 101 PRO A CA  
805  C C   . PRO A 101 ? 0.27139 0.29337 0.25383 0.05627  0.00577  -0.00336 101 PRO A C   
806  O O   . PRO A 101 ? 0.27507 0.35240 0.25477 -0.00020 -0.00703 0.01922  101 PRO A O   
807  C CB  . PRO A 101 ? 0.29423 0.33337 0.26014 0.02569  0.03159  -0.01180 101 PRO A CB  
808  C CG  . PRO A 101 ? 0.30392 0.31977 0.24959 0.02038  0.00083  -0.01611 101 PRO A CG  
809  C CD  . PRO A 101 ? 0.31350 0.32580 0.27643 0.02987  0.04624  -0.02491 101 PRO A CD  
810  N N   . LEU A 102 ? 0.28273 0.28988 0.25170 0.07452  0.00120  -0.01940 102 LEU A N   
811  C CA  . LEU A 102 ? 0.24674 0.31041 0.22020 0.06546  0.01895  -0.04068 102 LEU A CA  
812  C C   . LEU A 102 ? 0.25927 0.32206 0.21498 0.05442  0.00158  -0.04874 102 LEU A C   
813  O O   . LEU A 102 ? 0.28420 0.30068 0.23060 0.03055  0.00943  -0.02142 102 LEU A O   
814  C CB  . LEU A 102 ? 0.24062 0.32402 0.21178 0.07107  0.03222  -0.05810 102 LEU A CB  
815  C CG  . LEU A 102 ? 0.27178 0.34405 0.20555 0.08435  0.05164  -0.04058 102 LEU A CG  
816  C CD1 . LEU A 102 ? 0.28098 0.37273 0.24960 0.06257  0.06135  -0.04372 102 LEU A CD1 
817  C CD2 . LEU A 102 ? 0.26994 0.34848 0.23739 0.07841  0.02408  -0.00212 102 LEU A CD2 
818  N N   . LEU A 103 ? 0.27083 0.30682 0.21463 0.06206  -0.03562 -0.06113 103 LEU A N   
819  C CA  . LEU A 103 ? 0.28054 0.32588 0.21854 0.09847  -0.01872 -0.03048 103 LEU A CA  
820  C C   . LEU A 103 ? 0.31859 0.36157 0.21812 0.10984  -0.00704 0.01622  103 LEU A C   
821  O O   . LEU A 103 ? 0.29026 0.37514 0.23163 0.06789  0.02164  0.00235  103 LEU A O   
822  C CB  . LEU A 103 ? 0.30772 0.27881 0.21726 0.06912  -0.03320 -0.02194 103 LEU A CB  
823  C CG  . LEU A 103 ? 0.30077 0.24624 0.20555 0.07574  -0.00485 0.00014  103 LEU A CG  
824  C CD1 . LEU A 103 ? 0.27563 0.22839 0.22126 0.08358  0.04109  0.03571  103 LEU A CD1 
825  C CD2 . LEU A 103 ? 0.34108 0.23865 0.19861 0.05439  -0.01843 0.00399  103 LEU A CD2 
826  N N   . LYS A 104 ? 0.30660 0.36231 0.21670 0.14555  -0.01603 0.03655  104 LYS A N   
827  C CA  . LYS A 104 ? 0.29710 0.36478 0.21969 0.13116  -0.00090 0.05107  104 LYS A CA  
828  C C   . LYS A 104 ? 0.27323 0.39502 0.23337 0.08265  -0.01804 0.00798  104 LYS A C   
829  O O   . LYS A 104 ? 0.29256 0.41242 0.25160 0.05537  0.00679  -0.02820 104 LYS A O   
830  C CB  . LYS A 104 ? 0.35785 0.34868 0.26091 0.16963  -0.01741 0.04315  104 LYS A CB  
831  C CG  . LYS A 104 ? 0.39990 0.35937 0.28017 0.19125  -0.04698 0.03051  104 LYS A CG  
832  C CD  . LYS A 104 ? 0.40826 0.32509 0.32138 0.19731  -0.05589 0.03475  104 LYS A CD  
833  C CE  . LYS A 104 ? 0.48193 0.37729 0.38059 0.17179  -0.04958 0.02359  104 LYS A CE  
834  N NZ  . LYS A 104 ? 0.53139 0.40429 0.41479 0.14856  -0.04773 0.01473  104 LYS A NZ  
835  N N   . THR A 105 ? 0.26514 0.42121 0.25071 0.05778  -0.02563 -0.00602 105 THR A N   
836  C CA  . THR A 105 ? 0.26509 0.43880 0.28002 0.08977  -0.01610 0.01495  105 THR A CA  
837  C C   . THR A 105 ? 0.26379 0.43784 0.28120 0.12534  -0.00504 0.01278  105 THR A C   
838  O O   . THR A 105 ? 0.27729 0.46751 0.30073 0.15152  -0.00316 0.00229  105 THR A O   
839  C CB  . THR A 105 ? 0.30453 0.45241 0.30424 0.04570  -0.03283 0.04176  105 THR A CB  
840  O OG1 . THR A 105 ? 0.29141 0.46381 0.32020 0.06929  -0.02626 0.08531  105 THR A OG1 
841  C CG2 . THR A 105 ? 0.31633 0.47437 0.30558 0.03165  -0.05468 0.02231  105 THR A CG2 
842  N N   . THR A 106 ? 0.25048 0.40443 0.26731 0.12306  -0.00861 0.02777  106 THR A N   
843  C CA  . THR A 106 ? 0.29079 0.41324 0.29251 0.11286  -0.02335 0.02580  106 THR A CA  
844  C C   . THR A 106 ? 0.26794 0.42485 0.31663 0.10385  -0.04797 0.02561  106 THR A C   
845  O O   . THR A 106 ? 0.30705 0.42628 0.33353 0.08230  -0.03383 -0.00304 106 THR A O   
846  C CB  . THR A 106 ? 0.34889 0.43774 0.32350 0.10676  -0.05105 0.01700  106 THR A CB  
847  O OG1 . THR A 106 ? 0.39122 0.44470 0.35168 0.12381  -0.04429 0.00254  106 THR A OG1 
848  C CG2 . THR A 106 ? 0.34666 0.45277 0.30721 0.09817  -0.08452 0.00767  106 THR A CG2 
849  N N   . VAL A 107 ? 0.24141 0.43655 0.33024 0.09198  -0.05995 0.04640  107 VAL A N   
850  C CA  . VAL A 107 ? 0.26710 0.46017 0.37130 0.10020  -0.05752 0.05932  107 VAL A CA  
851  C C   . VAL A 107 ? 0.30316 0.48590 0.38310 0.09573  -0.06148 0.03686  107 VAL A C   
852  O O   . VAL A 107 ? 0.30885 0.48285 0.38741 0.10506  -0.06199 0.01002  107 VAL A O   
853  C CB  . VAL A 107 ? 0.28859 0.45764 0.38399 0.05520  -0.04155 0.06019  107 VAL A CB  
854  C CG1 . VAL A 107 ? 0.29718 0.45836 0.40329 0.01666  -0.04738 0.03264  107 VAL A CG1 
855  C CG2 . VAL A 107 ? 0.30505 0.44094 0.37509 0.04754  -0.04911 0.05784  107 VAL A CG2 
856  N N   . LYS A 108 ? 0.30181 0.49732 0.38325 0.08086  -0.07908 0.04669  108 LYS A N   
857  C CA  . LYS A 108 ? 0.31345 0.51755 0.43215 0.06367  -0.09572 0.08030  108 LYS A CA  
858  C C   . LYS A 108 ? 0.36345 0.56807 0.47833 0.07223  -0.13524 0.06907  108 LYS A C   
859  O O   . LYS A 108 ? 0.35036 0.57619 0.48057 0.08551  -0.14511 0.07201  108 LYS A O   
860  C CB  . LYS A 108 ? 0.38772 0.52207 0.45454 0.04295  -0.09756 0.07208  108 LYS A CB  
861  C CG  . LYS A 108 ? 0.46261 0.53158 0.47132 -0.00106 -0.09333 0.07411  108 LYS A CG  
862  C CD  . LYS A 108 ? 0.50647 0.52607 0.48104 -0.05296 -0.08256 0.08016  108 LYS A CD  
863  C CE  . LYS A 108 ? 0.53408 0.52801 0.48265 -0.07977 -0.08865 0.07833  108 LYS A CE  
864  N NZ  . LYS A 108 ? 0.59093 0.52787 0.47094 -0.06522 -0.07963 0.09176  108 LYS A NZ  
865  N N   . TYR A 109 ? 0.36611 0.61065 0.53078 0.06626  -0.12370 0.05066  109 TYR A N   
866  C CA  . TYR A 109 ? 0.51112 0.67051 0.55520 0.01119  -0.12002 0.04620  109 TYR A CA  
867  C C   . TYR A 109 ? 0.59922 0.70246 0.59514 0.00571  -0.14619 0.06560  109 TYR A C   
868  O O   . TYR A 109 ? 0.61597 0.69541 0.58893 0.04715  -0.17449 0.11946  109 TYR A O   
869  C CB  . TYR A 109 ? 0.46323 0.67841 0.54923 0.00227  -0.11882 0.01706  109 TYR A CB  
870  C CG  . TYR A 109 ? 0.45711 0.67935 0.53720 0.01278  -0.15901 0.00057  109 TYR A CG  
871  C CD1 . TYR A 109 ? 0.47660 0.68349 0.53441 0.03167  -0.16744 -0.01479 109 TYR A CD1 
872  C CD2 . TYR A 109 ? 0.40758 0.67389 0.53248 -0.03070 -0.17225 -0.01704 109 TYR A CD2 
873  C CE1 . TYR A 109 ? 0.48103 0.68785 0.52296 -0.00314 -0.17718 -0.04300 109 TYR A CE1 
874  C CE2 . TYR A 109 ? 0.45635 0.67136 0.51521 -0.03270 -0.17870 -0.02914 109 TYR A CE2 
875  C CZ  . TYR A 109 ? 0.51296 0.69132 0.52803 -0.02198 -0.14981 -0.04730 109 TYR A CZ  
876  O OH  . TYR A 109 ? 0.51951 0.70306 0.52767 -0.03392 -0.11871 -0.05821 109 TYR A OH  
877  N N   . GLY A 110 ? 0.63528 0.72242 0.62058 -0.01013 -0.12750 0.04497  110 GLY A N   
878  C CA  . GLY A 110 ? 0.67400 0.73375 0.63666 -0.00265 -0.09189 0.04396  110 GLY A CA  
879  C C   . GLY A 110 ? 0.72274 0.75276 0.66292 0.01640  -0.03806 0.02556  110 GLY A C   
880  O O   . GLY A 110 ? 0.75527 0.76083 0.67119 0.00735  -0.01047 0.02748  110 GLY A O   
881  N N   . ILE A 111 ? 0.70926 0.73237 0.68901 0.02263  -0.01572 -0.00039 111 ILE A N   
882  C CA  . ILE A 111 ? 0.67630 0.69561 0.71283 0.03415  0.03081  -0.02691 111 ILE A CA  
883  C C   . ILE A 111 ? 0.65679 0.67901 0.72842 0.05390  0.05009  -0.01915 111 ILE A C   
884  O O   . ILE A 111 ? 0.64700 0.69339 0.73842 0.11042  0.09492  -0.03043 111 ILE A O   
885  C CB  . ILE A 111 ? 0.65860 0.67852 0.72887 0.03684  0.05226  -0.04483 111 ILE A CB  
886  N N   . GLY A 112 ? 0.62236 0.63087 0.73066 0.02211  -0.00953 -0.01635 112 GLY A N   
887  C CA  . GLY A 112 ? 0.61427 0.61814 0.72841 0.06702  -0.04090 0.00034  112 GLY A CA  
888  C C   . GLY A 112 ? 0.66182 0.63873 0.73078 0.10991  -0.05766 -0.00872 112 GLY A C   
889  O O   . GLY A 112 ? 0.66277 0.66659 0.73178 0.15604  -0.04034 -0.03489 112 GLY A O   
890  N N   . LYS A 113 ? 0.70431 0.63723 0.72674 0.08540  -0.05352 -0.00179 113 LYS A N   
891  C CA  . LYS A 113 ? 0.67940 0.64638 0.71658 0.07141  -0.03776 -0.00027 113 LYS A CA  
892  C C   . LYS A 113 ? 0.69709 0.67865 0.71726 0.03047  -0.07660 0.03279  113 LYS A C   
893  O O   . LYS A 113 ? 0.73518 0.70079 0.72582 0.00117  -0.06956 0.04856  113 LYS A O   
894  C CB  . LYS A 113 ? 0.64860 0.60675 0.70710 0.10847  -0.03171 -0.00665 113 LYS A CB  
895  N N   . LYS A 114 ? 0.65542 0.69738 0.71473 0.07977  -0.12755 0.04220  114 LYS A N   
896  C CA  . LYS A 114 ? 0.61050 0.68864 0.68570 0.17848  -0.14405 0.04508  114 LYS A CA  
897  C C   . LYS A 114 ? 0.61004 0.67944 0.64705 0.26643  -0.14243 0.02576  114 LYS A C   
898  O O   . LYS A 114 ? 0.59619 0.70206 0.65802 0.30282  -0.15700 0.02523  114 LYS A O   
899  C CB  . LYS A 114 ? 0.56201 0.68758 0.68206 0.21524  -0.13056 0.05616  114 LYS A CB  
900  N N   . GLU A 115 ? 0.56254 0.65200 0.57734 0.30459  -0.14148 0.00321  115 GLU A N   
901  C CA  . GLU A 115 ? 0.51695 0.65067 0.51965 0.29725  -0.10486 0.00363  115 GLU A CA  
902  C C   . GLU A 115 ? 0.40835 0.66220 0.48713 0.28155  -0.07078 0.00724  115 GLU A C   
903  O O   . GLU A 115 ? 0.42959 0.68957 0.51408 0.29244  -0.05146 0.01137  115 GLU A O   
904  C CB  . GLU A 115 ? 0.58334 0.65452 0.52064 0.29010  -0.08800 0.04989  115 GLU A CB  
905  C CG  . GLU A 115 ? 0.67339 0.65386 0.56286 0.27479  -0.07695 0.06737  115 GLU A CG  
906  C CD  . GLU A 115 ? 0.76639 0.63474 0.59153 0.25278  -0.06682 0.08839  115 GLU A CD  
907  O OE1 . GLU A 115 ? 0.81139 0.62957 0.61799 0.25641  -0.06574 0.09451  115 GLU A OE1 
908  O OE2 . GLU A 115 ? 0.79859 0.62259 0.59169 0.22586  -0.05540 0.09859  115 GLU A OE2 
909  N N   . ALA A 116 ? 0.30658 0.64358 0.42645 0.21692  -0.05685 0.00920  116 ALA A N   
910  C CA  . ALA A 116 ? 0.27885 0.65053 0.39316 0.17696  -0.04935 0.02780  116 ALA A CA  
911  C C   . ALA A 116 ? 0.29520 0.62074 0.36472 0.14842  -0.02545 0.00904  116 ALA A C   
912  O O   . ALA A 116 ? 0.27920 0.62465 0.35364 0.11742  0.00563  0.01442  116 ALA A O   
913  C CB  . ALA A 116 ? 0.33473 0.67586 0.41770 0.13920  -0.03431 0.02587  116 ALA A CB  
914  N N   . THR A 117 ? 0.33293 0.60056 0.33950 0.16567  -0.01785 -0.00668 117 THR A N   
915  C CA  . THR A 117 ? 0.34011 0.58537 0.31593 0.14465  -0.01566 -0.01766 117 THR A CA  
916  C C   . THR A 117 ? 0.29495 0.59217 0.32361 0.15662  0.00312  -0.01915 117 THR A C   
917  O O   . THR A 117 ? 0.29626 0.62042 0.34128 0.14660  0.00813  -0.03166 117 THR A O   
918  C CB  . THR A 117 ? 0.45610 0.58866 0.31076 0.14303  0.00674  -0.01818 117 THR A CB  
919  O OG1 . THR A 117 ? 0.54668 0.60827 0.35401 0.12582  0.01191  -0.02518 117 THR A OG1 
920  C CG2 . THR A 117 ? 0.44736 0.58413 0.26558 0.13770  -0.01454 0.00996  117 THR A CG2 
921  N N   . TYR A 118 ? 0.24924 0.54406 0.30514 0.13788  -0.02696 0.01495  118 TYR A N   
922  C CA  . TYR A 118 ? 0.26354 0.52818 0.29907 0.09713  -0.02630 0.03749  118 TYR A CA  
923  C C   . TYR A 118 ? 0.28164 0.50771 0.28204 0.09395  -0.01220 0.01380  118 TYR A C   
924  O O   . TYR A 118 ? 0.32150 0.53364 0.27641 0.09430  0.01861  0.00120  118 TYR A O   
925  C CB  . TYR A 118 ? 0.27860 0.53140 0.33031 0.04317  -0.00661 0.02916  118 TYR A CB  
926  C CG  . TYR A 118 ? 0.24894 0.54617 0.34190 0.01684  -0.04014 0.00560  118 TYR A CG  
927  C CD1 . TYR A 118 ? 0.26934 0.56169 0.34961 -0.01010 -0.05175 -0.00630 118 TYR A CD1 
928  C CD2 . TYR A 118 ? 0.24185 0.55966 0.35405 -0.00770 -0.03351 -0.01570 118 TYR A CD2 
929  C CE1 . TYR A 118 ? 0.32201 0.58991 0.36786 -0.00138 -0.02799 -0.00842 118 TYR A CE1 
930  C CE2 . TYR A 118 ? 0.27227 0.58109 0.38141 -0.00761 -0.03679 -0.02256 118 TYR A CE2 
931  C CZ  . TYR A 118 ? 0.30630 0.59967 0.39177 -0.00812 -0.01966 0.00088  118 TYR A CZ  
932  O OH  . TYR A 118 ? 0.38180 0.60927 0.43211 -0.00341 -0.01082 0.01206  118 TYR A OH  
933  N N   . LEU A 119 ? 0.28351 0.44896 0.26735 0.07179  0.01699  -0.01053 119 LEU A N   
934  C CA  . LEU A 119 ? 0.28630 0.41197 0.28308 0.11468  0.01465  -0.03788 119 LEU A CA  
935  C C   . LEU A 119 ? 0.26809 0.36305 0.25329 0.08674  -0.01508 -0.01714 119 LEU A C   
936  O O   . LEU A 119 ? 0.31807 0.37997 0.26994 0.08615  0.00601  -0.00042 119 LEU A O   
937  C CB  . LEU A 119 ? 0.34414 0.45358 0.33369 0.09753  0.04579  -0.11174 119 LEU A CB  
938  C CG  . LEU A 119 ? 0.37436 0.52955 0.38179 0.07756  0.08340  -0.15823 119 LEU A CG  
939  C CD1 . LEU A 119 ? 0.37833 0.54036 0.38655 0.06830  0.10829  -0.16482 119 LEU A CD1 
940  C CD2 . LEU A 119 ? 0.41532 0.55067 0.41322 0.06454  0.07716  -0.15640 119 LEU A CD2 
941  N N   . ALA A 120 ? 0.22595 0.31682 0.23460 0.09180  -0.02969 -0.02830 120 ALA A N   
942  C CA  . ALA A 120 ? 0.21556 0.29830 0.22452 0.06454  -0.01710 -0.04766 120 ALA A CA  
943  C C   . ALA A 120 ? 0.20340 0.28191 0.19933 0.01569  -0.00413 -0.03802 120 ALA A C   
944  O O   . ALA A 120 ? 0.26293 0.24812 0.22334 0.00294  0.01755  -0.00612 120 ALA A O   
945  C CB  . ALA A 120 ? 0.28987 0.30005 0.24214 0.02083  -0.02185 -0.08125 120 ALA A CB  
946  N N   . LEU A 121 ? 0.24032 0.31112 0.19225 0.03082  -0.01937 -0.02658 121 LEU A N   
947  C CA  . LEU A 121 ? 0.22163 0.31560 0.17595 0.05341  0.00522  -0.03513 121 LEU A CA  
948  C C   . LEU A 121 ? 0.22512 0.26927 0.20075 0.02009  0.00786  -0.04065 121 LEU A C   
949  O O   . LEU A 121 ? 0.25169 0.27759 0.22444 0.04012  -0.00358 -0.04004 121 LEU A O   
950  C CB  . LEU A 121 ? 0.25826 0.34305 0.15187 0.02319  0.00519  -0.02734 121 LEU A CB  
951  C CG  . LEU A 121 ? 0.28230 0.33897 0.19360 -0.01979 0.01827  -0.03035 121 LEU A CG  
952  C CD1 . LEU A 121 ? 0.26792 0.32387 0.24367 -0.01701 0.00439  -0.01698 121 LEU A CD1 
953  C CD2 . LEU A 121 ? 0.30675 0.34684 0.18907 0.00054  0.04117  -0.07107 121 LEU A CD2 
954  N N   . ASN A 122 ? 0.23397 0.27254 0.18123 0.02594  0.02324  -0.04340 122 ASN A N   
955  C CA  . ASN A 122 ? 0.24397 0.22845 0.18130 0.02301  0.02569  -0.01994 122 ASN A CA  
956  C C   . ASN A 122 ? 0.24563 0.21423 0.18841 0.01338  0.01367  -0.00096 122 ASN A C   
957  O O   . ASN A 122 ? 0.24839 0.22403 0.21037 0.00674  0.00339  -0.00038 122 ASN A O   
958  C CB  . ASN A 122 ? 0.24651 0.21498 0.18141 -0.00772 0.00936  -0.02188 122 ASN A CB  
959  C CG  . ASN A 122 ? 0.25047 0.28031 0.19012 0.00992  0.03612  -0.01750 122 ASN A CG  
960  O OD1 . ASN A 122 ? 0.28482 0.29085 0.20583 0.00406  0.02160  0.00707  122 ASN A OD1 
961  N ND2 . ASN A 122 ? 0.20975 0.33230 0.18237 0.02014  0.02662  0.00429  122 ASN A ND2 
962  N N   . GLU A 123 ? 0.22407 0.23919 0.17143 0.02249  -0.00916 -0.01630 123 GLU A N   
963  C CA  . GLU A 123 ? 0.20562 0.27476 0.18144 0.01873  -0.01241 -0.04286 123 GLU A CA  
964  C C   . GLU A 123 ? 0.21370 0.26847 0.18109 0.05481  0.01238  -0.04534 123 GLU A C   
965  O O   . GLU A 123 ? 0.21528 0.32917 0.19849 0.04679  0.03209  -0.01518 123 GLU A O   
966  C CB  . GLU A 123 ? 0.23395 0.29087 0.19232 -0.00930 0.00378  -0.04093 123 GLU A CB  
967  C CG  . GLU A 123 ? 0.22545 0.33359 0.18428 -0.02101 -0.00952 0.00038  123 GLU A CG  
968  C CD  . GLU A 123 ? 0.18456 0.33899 0.20537 0.01306  -0.00472 -0.00084 123 GLU A CD  
969  O OE1 . GLU A 123 ? 0.22443 0.28773 0.21649 0.01031  -0.04082 -0.02562 123 GLU A OE1 
970  O OE2 . GLU A 123 ? 0.19124 0.36637 0.23767 -0.00477 0.02514  0.00410  123 GLU A OE2 
971  N N   . SER A 124 ? 0.21921 0.31737 0.17505 0.02365  -0.02497 -0.02760 124 SER A N   
972  C CA  . SER A 124 ? 0.19336 0.33127 0.19097 0.01360  -0.02899 -0.02286 124 SER A CA  
973  C C   . SER A 124 ? 0.19591 0.29712 0.20185 0.00119  0.00025  -0.04309 124 SER A C   
974  O O   . SER A 124 ? 0.22848 0.32425 0.26705 0.03749  0.03756  -0.04295 124 SER A O   
975  C CB  . SER A 124 ? 0.24266 0.39990 0.18786 0.01054  -0.04097 -0.02246 124 SER A CB  
976  O OG  . SER A 124 ? 0.29603 0.47715 0.21337 0.03823  -0.05167 -0.01741 124 SER A OG  
977  N N   . THR A 125 ? 0.18793 0.29956 0.21279 0.04001  -0.00368 -0.03419 125 THR A N   
978  C CA  . THR A 125 ? 0.19139 0.31502 0.21284 0.00507  -0.00001 -0.03494 125 THR A CA  
979  C C   . THR A 125 ? 0.22058 0.36541 0.22384 0.01172  0.03478  -0.03572 125 THR A C   
980  O O   . THR A 125 ? 0.19123 0.42835 0.21768 0.01723  0.01278  -0.04103 125 THR A O   
981  C CB  . THR A 125 ? 0.18795 0.33793 0.24986 -0.04285 -0.00168 0.01741  125 THR A CB  
982  O OG1 . THR A 125 ? 0.20437 0.39385 0.28137 -0.04084 -0.00984 0.02291  125 THR A OG1 
983  C CG2 . THR A 125 ? 0.24290 0.35919 0.24765 -0.01089 -0.05426 0.01211  125 THR A CG2 
984  N N   . VAL A 126 ? 0.21491 0.36360 0.21759 -0.00594 0.01672  -0.00190 126 VAL A N   
985  C CA  A VAL A 126 ? 0.23802 0.37838 0.24466 -0.00703 -0.01145 -0.02769 126 VAL A CA  
986  C CA  B VAL A 126 ? 0.20278 0.36064 0.22970 -0.00198 -0.01484 -0.02546 126 VAL A CA  
987  C C   . VAL A 126 ? 0.19902 0.33835 0.24868 0.01667  -0.01267 -0.02821 126 VAL A C   
988  O O   . VAL A 126 ? 0.21469 0.32210 0.24012 0.01310  -0.01108 -0.01490 126 VAL A O   
989  C CB  A VAL A 126 ? 0.26728 0.40327 0.25601 0.00637  -0.03502 -0.00769 126 VAL A CB  
990  C CB  B VAL A 126 ? 0.17983 0.36613 0.21533 0.00338  -0.05448 -0.02428 126 VAL A CB  
991  C CG1 A VAL A 126 ? 0.29156 0.42357 0.26522 0.02063  -0.01376 -0.00121 126 VAL A CG1 
992  C CG1 B VAL A 126 ? 0.17581 0.36990 0.23646 0.00021  -0.05551 -0.02160 126 VAL A CG1 
993  C CG2 A VAL A 126 ? 0.25136 0.42069 0.28664 -0.01531 -0.03440 -0.00800 126 VAL A CG2 
994  C CG2 B VAL A 126 ? 0.16102 0.37228 0.19554 -0.00808 -0.07165 -0.03280 126 VAL A CG2 
995  N N   . LYS A 127 ? 0.16573 0.32795 0.27791 0.00015  -0.01095 -0.01862 127 LYS A N   
996  C CA  . LYS A 127 ? 0.22467 0.35464 0.31085 0.02311  -0.03356 -0.02143 127 LYS A CA  
997  C C   . LYS A 127 ? 0.22875 0.37636 0.34136 -0.01645 -0.02140 -0.04759 127 LYS A C   
998  O O   . LYS A 127 ? 0.23009 0.37556 0.32311 -0.05011 -0.01275 -0.06582 127 LYS A O   
999  C CB  . LYS A 127 ? 0.30095 0.38886 0.31580 0.00166  -0.08933 0.04471  127 LYS A CB  
1000 C CG  . LYS A 127 ? 0.29529 0.42566 0.32285 -0.02377 -0.06185 0.09537  127 LYS A CG  
1001 C CD  . LYS A 127 ? 0.30744 0.46473 0.35301 -0.04866 -0.06585 0.12080  127 LYS A CD  
1002 C CE  . LYS A 127 ? 0.38709 0.50826 0.39749 -0.01972 -0.05250 0.10159  127 LYS A CE  
1003 N NZ  . LYS A 127 ? 0.41194 0.54136 0.41529 0.00279  -0.06536 0.08522  127 LYS A NZ  
1004 N N   . SER A 128 ? 0.23026 0.41604 0.37474 -0.04837 -0.04399 -0.06158 128 SER A N   
1005 C CA  . SER A 128 ? 0.30149 0.47730 0.42783 -0.05917 -0.03479 -0.04238 128 SER A CA  
1006 C C   . SER A 128 ? 0.31073 0.55887 0.44845 -0.06792 -0.01956 -0.01293 128 SER A C   
1007 O O   . SER A 128 ? 0.36863 0.60563 0.46276 -0.12338 0.03113  0.02507  128 SER A O   
1008 C CB  . SER A 128 ? 0.42330 0.49288 0.46844 -0.03065 -0.01920 -0.02910 128 SER A CB  
1009 O OG  . SER A 128 ? 0.45238 0.52411 0.50128 -0.01821 -0.02690 -0.01640 128 SER A OG  
1010 N N   . SER A 129 ? 0.29802 0.59951 0.47841 -0.10957 0.00645  -0.03346 129 SER A N   
1011 C CA  . SER A 129 ? 0.37035 0.67408 0.53445 -0.11205 -0.00036 -0.02728 129 SER A CA  
1012 C C   . SER A 129 ? 0.44641 0.72639 0.58761 -0.12430 0.01516  -0.03592 129 SER A C   
1013 O O   . SER A 129 ? 0.41386 0.77354 0.61545 -0.16245 0.02906  -0.02021 129 SER A O   
1014 C CB  . SER A 129 ? 0.44290 0.71096 0.54653 -0.06961 -0.01411 -0.02154 129 SER A CB  
1015 O OG  . SER A 129 ? 0.52835 0.75574 0.57731 -0.07524 -0.02593 -0.02769 129 SER A OG  
1016 N N   . GLY A 130 ? 0.56142 0.72496 0.61510 -0.12424 0.02388  -0.06343 130 GLY A N   
1017 C CA  . GLY A 130 ? 0.64134 0.72594 0.63939 -0.10362 0.03246  -0.07332 130 GLY A CA  
1018 C C   . GLY A 130 ? 0.67067 0.72267 0.65342 -0.09278 0.03247  -0.09252 130 GLY A C   
1019 O O   . GLY A 130 ? 0.73482 0.76769 0.68019 -0.11807 0.02587  -0.08327 130 GLY A O   
1020 N N   . GLY A 131 ? 0.59612 0.66847 0.64230 -0.08515 0.04287  -0.11689 131 GLY A N   
1021 C CA  . GLY A 131 ? 0.51506 0.61374 0.60707 -0.10154 0.05467  -0.15211 131 GLY A CA  
1022 C C   . GLY A 131 ? 0.45344 0.56198 0.56499 -0.12803 0.04637  -0.17958 131 GLY A C   
1023 O O   . GLY A 131 ? 0.42684 0.56309 0.58184 -0.11226 0.09246  -0.19197 131 GLY A O   
1024 N N   . PRO A 132 ? 0.44979 0.51412 0.49985 -0.15176 -0.01053 -0.15746 132 PRO A N   
1025 C CA  . PRO A 132 ? 0.41409 0.49617 0.46024 -0.08871 -0.03197 -0.11434 132 PRO A CA  
1026 C C   . PRO A 132 ? 0.41430 0.47255 0.41772 -0.05893 -0.05273 -0.08620 132 PRO A C   
1027 O O   . PRO A 132 ? 0.42526 0.49764 0.45316 -0.01754 -0.11533 -0.06244 132 PRO A O   
1028 C CB  . PRO A 132 ? 0.43639 0.49075 0.45570 -0.11483 -0.05439 -0.13643 132 PRO A CB  
1029 C CG  . PRO A 132 ? 0.45144 0.52987 0.46624 -0.11081 -0.03023 -0.13807 132 PRO A CG  
1030 C CD  . PRO A 132 ? 0.46585 0.53994 0.49245 -0.11399 -0.02864 -0.13511 132 PRO A CD  
1031 N N   . PHE A 133 ? 0.40010 0.41859 0.32147 -0.07423 -0.01996 -0.08244 133 PHE A N   
1032 C CA  . PHE A 133 ? 0.34831 0.38853 0.28087 -0.02728 0.01633  -0.02553 133 PHE A CA  
1033 C C   . PHE A 133 ? 0.29734 0.37512 0.26444 0.00163  0.00473  -0.00459 133 PHE A C   
1034 O O   . PHE A 133 ? 0.30626 0.38162 0.25796 0.00745  0.00778  -0.00550 133 PHE A O   
1035 C CB  . PHE A 133 ? 0.32356 0.35020 0.26052 -0.01692 0.01535  0.00200  133 PHE A CB  
1036 C CG  . PHE A 133 ? 0.31604 0.30944 0.26262 -0.01274 0.00430  -0.02394 133 PHE A CG  
1037 C CD1 . PHE A 133 ? 0.35819 0.30067 0.26712 0.00245  0.02022  -0.03308 133 PHE A CD1 
1038 C CD2 . PHE A 133 ? 0.35928 0.30816 0.27641 0.00879  -0.02208 -0.04024 133 PHE A CD2 
1039 C CE1 . PHE A 133 ? 0.38470 0.32896 0.27540 -0.00390 0.00078  -0.05153 133 PHE A CE1 
1040 C CE2 . PHE A 133 ? 0.36502 0.31321 0.26907 0.02789  -0.02026 -0.04019 133 PHE A CE2 
1041 C CZ  . PHE A 133 ? 0.36819 0.31393 0.26674 0.01614  -0.03131 -0.04949 133 PHE A CZ  
1042 N N   . VAL A 134 ? 0.27495 0.35779 0.27458 0.01799  -0.03302 0.00290  134 VAL A N   
1043 C CA  . VAL A 134 ? 0.29616 0.33371 0.28286 0.01172  -0.03864 0.00112  134 VAL A CA  
1044 C C   . VAL A 134 ? 0.25775 0.32897 0.31062 -0.00167 -0.05345 0.03491  134 VAL A C   
1045 O O   . VAL A 134 ? 0.32019 0.35093 0.38483 0.02484  -0.07088 0.05787  134 VAL A O   
1046 C CB  . VAL A 134 ? 0.39620 0.33663 0.30166 0.01806  -0.01581 -0.02222 134 VAL A CB  
1047 C CG1 . VAL A 134 ? 0.40241 0.32890 0.30105 0.00168  0.00173  -0.03762 134 VAL A CG1 
1048 C CG2 . VAL A 134 ? 0.47017 0.31885 0.29100 0.05724  -0.05601 -0.03234 134 VAL A CG2 
1049 N N   . VAL A 135 ? 0.26568 0.33153 0.27175 -0.00395 -0.06109 0.02069  135 VAL A N   
1050 C CA  . VAL A 135 ? 0.24637 0.32861 0.25672 0.01756  -0.03685 0.00883  135 VAL A CA  
1051 C C   . VAL A 135 ? 0.28030 0.32041 0.25421 0.01909  -0.04631 0.02162  135 VAL A C   
1052 O O   . VAL A 135 ? 0.32733 0.33395 0.23999 0.04186  -0.04628 0.02877  135 VAL A O   
1053 C CB  . VAL A 135 ? 0.21671 0.38314 0.26881 0.02613  -0.04420 -0.00829 135 VAL A CB  
1054 C CG1 . VAL A 135 ? 0.24413 0.43936 0.30395 0.06128  -0.03078 -0.03594 135 VAL A CG1 
1055 C CG2 . VAL A 135 ? 0.25984 0.41824 0.27305 0.01245  -0.07884 -0.02341 135 VAL A CG2 
1056 N N   . ASP A 136 ? 0.25837 0.31221 0.24229 0.02509  -0.04160 0.01841  136 ASP A N   
1057 C CA  . ASP A 136 ? 0.29686 0.31429 0.23649 0.00002  -0.05850 0.02737  136 ASP A CA  
1058 C C   . ASP A 136 ? 0.26233 0.31254 0.23182 0.02379  -0.05262 -0.00192 136 ASP A C   
1059 O O   . ASP A 136 ? 0.25868 0.34685 0.26511 0.03265  -0.03169 -0.00097 136 ASP A O   
1060 C CB  . ASP A 136 ? 0.35839 0.32615 0.25756 0.02143  -0.09530 0.03673  136 ASP A CB  
1061 C CG  . ASP A 136 ? 0.41460 0.38021 0.30063 0.03374  -0.09570 0.02692  136 ASP A CG  
1062 O OD1 . ASP A 136 ? 0.46919 0.41685 0.32290 0.01787  -0.12191 0.00773  136 ASP A OD1 
1063 O OD2 . ASP A 136 ? 0.39855 0.42902 0.34510 0.03911  -0.07566 0.01059  136 ASP A OD2 
1064 N N   . VAL A 137 ? 0.25400 0.28445 0.20338 -0.04015 -0.03132 0.02637  137 VAL A N   
1065 C CA  . VAL A 137 ? 0.24070 0.29814 0.23504 0.00143  -0.03109 0.03209  137 VAL A CA  
1066 C C   . VAL A 137 ? 0.25953 0.28710 0.23513 0.03178  -0.00611 0.04022  137 VAL A C   
1067 O O   . VAL A 137 ? 0.27188 0.33283 0.23992 0.04121  0.00118  0.02773  137 VAL A O   
1068 C CB  . VAL A 137 ? 0.22040 0.31556 0.23228 0.04120  -0.00514 0.03683  137 VAL A CB  
1069 C CG1 . VAL A 137 ? 0.26563 0.36117 0.25281 0.00237  -0.01701 -0.00211 137 VAL A CG1 
1070 C CG2 . VAL A 137 ? 0.27993 0.34096 0.27093 0.04087  -0.01077 0.05387  137 VAL A CG2 
1071 N N   . VAL A 138 ? 0.27910 0.27004 0.24976 0.01536  0.00269  0.04267  138 VAL A N   
1072 C CA  . VAL A 138 ? 0.28706 0.30518 0.24672 -0.01449 -0.03397 0.03714  138 VAL A CA  
1073 C C   . VAL A 138 ? 0.30395 0.30771 0.23649 -0.00394 0.00307  -0.00024 138 VAL A C   
1074 O O   . VAL A 138 ? 0.33555 0.37466 0.26947 -0.03134 0.07183  -0.04629 138 VAL A O   
1075 C CB  . VAL A 138 ? 0.32010 0.30288 0.28016 -0.01057 -0.03850 0.03454  138 VAL A CB  
1076 C CG1 . VAL A 138 ? 0.34352 0.31286 0.33586 0.00610  -0.04763 0.08066  138 VAL A CG1 
1077 C CG2 . VAL A 138 ? 0.34534 0.32783 0.26744 0.00015  -0.06411 -0.01874 138 VAL A CG2 
1078 N N   . ILE A 139 ? 0.29181 0.26101 0.22163 -0.02001 -0.01506 0.00700  139 ILE A N   
1079 C CA  . ILE A 139 ? 0.29044 0.26896 0.23557 -0.04635 -0.01424 0.00620  139 ILE A CA  
1080 C C   . ILE A 139 ? 0.34770 0.28438 0.25117 -0.01548 -0.00735 0.01265  139 ILE A C   
1081 O O   . ILE A 139 ? 0.36441 0.29851 0.24593 -0.02086 0.02864  0.01242  139 ILE A O   
1082 C CB  . ILE A 139 ? 0.28989 0.25048 0.25879 0.00306  -0.00622 0.02964  139 ILE A CB  
1083 C CG1 . ILE A 139 ? 0.30416 0.27131 0.24950 0.02800  -0.00147 0.01106  139 ILE A CG1 
1084 C CG2 . ILE A 139 ? 0.34147 0.29153 0.29713 -0.07031 -0.00440 0.04763  139 ILE A CG2 
1085 C CD1 . ILE A 139 ? 0.31376 0.32907 0.26169 0.02590  -0.03784 -0.00116 139 ILE A CD1 
1086 N N   . ASN A 140 ? 0.41117 0.26954 0.24423 -0.00050 0.01099  0.02717  140 ASN A N   
1087 C CA  . ASN A 140 ? 0.44229 0.28076 0.22149 -0.03356 -0.02864 0.04628  140 ASN A CA  
1088 C C   . ASN A 140 ? 0.52617 0.31024 0.23789 0.00752  -0.04922 0.03876  140 ASN A C   
1089 O O   . ASN A 140 ? 0.58243 0.34794 0.26092 -0.01171 -0.04187 0.04880  140 ASN A O   
1090 C CB  . ASN A 140 ? 0.39690 0.32375 0.21912 -0.03865 -0.02342 0.03321  140 ASN A CB  
1091 C CG  . ASN A 140 ? 0.38070 0.33993 0.26278 -0.04582 0.00193  0.04049  140 ASN A CG  
1092 O OD1 . ASN A 140 ? 0.38257 0.36675 0.28737 -0.07322 0.02122  0.01204  140 ASN A OD1 
1093 N ND2 . ASN A 140 ? 0.39643 0.36243 0.29221 -0.03150 0.01718  0.04134  140 ASN A ND2 
1094 N N   . ASP A 141 ? 0.54871 0.30413 0.25197 0.03813  -0.06299 0.03910  141 ASP A N   
1095 C CA  . ASP A 141 ? 0.57159 0.32834 0.23907 0.04786  -0.05533 0.05503  141 ASP A CA  
1096 C C   . ASP A 141 ? 0.54429 0.37962 0.25905 0.04299  -0.02614 0.04552  141 ASP A C   
1097 O O   . ASP A 141 ? 0.61974 0.44985 0.29418 0.06826  -0.03906 0.00018  141 ASP A O   
1098 C CB  . ASP A 141 ? 0.65015 0.39386 0.29740 0.06581  -0.03991 0.08482  141 ASP A CB  
1099 C CG  . ASP A 141 ? 0.70466 0.42904 0.34186 0.09081  -0.02762 0.11380  141 ASP A CG  
1100 O OD1 . ASP A 141 ? 0.70878 0.44268 0.33826 0.11229  -0.03154 0.13528  141 ASP A OD1 
1101 O OD2 . ASP A 141 ? 0.73912 0.45966 0.39685 0.09332  -0.00271 0.08686  141 ASP A OD2 
1102 N N   . ILE A 142 ? 0.48034 0.33030 0.27337 0.08230  0.02073  0.05778  142 ILE A N   
1103 C CA  . ILE A 142 ? 0.41498 0.34079 0.28365 0.03311  0.03040  0.03288  142 ILE A CA  
1104 C C   . ILE A 142 ? 0.34711 0.32703 0.25382 0.03247  -0.00018 0.02307  142 ILE A C   
1105 O O   . ILE A 142 ? 0.34706 0.35862 0.20230 0.04468  -0.00510 0.02552  142 ILE A O   
1106 C CB  . ILE A 142 ? 0.44635 0.35584 0.34933 0.00009  0.10826  0.02064  142 ILE A CB  
1107 C CG1 . ILE A 142 ? 0.46944 0.35490 0.40291 -0.02836 0.10407  -0.00253 142 ILE A CG1 
1108 C CG2 . ILE A 142 ? 0.40651 0.32759 0.34979 0.03998  0.10692  0.01160  142 ILE A CG2 
1109 C CD1 . ILE A 142 ? 0.47017 0.37502 0.42469 -0.00729 0.11649  -0.00064 142 ILE A CD1 
1110 N N   . HIS A 143 ? 0.34529 0.32483 0.23515 0.03357  -0.04144 0.01786  143 HIS A N   
1111 C CA  A HIS A 143 ? 0.32613 0.33963 0.21230 0.02992  -0.06045 0.01940  143 HIS A CA  
1112 C CA  B HIS A 143 ? 0.32905 0.34227 0.21891 0.02192  -0.01796 0.00477  143 HIS A CA  
1113 C C   . HIS A 143 ? 0.31528 0.35353 0.21480 0.04633  0.00217  0.03424  143 HIS A C   
1114 O O   . HIS A 143 ? 0.32276 0.39363 0.24043 0.07407  0.01963  0.03934  143 HIS A O   
1115 C CB  A HIS A 143 ? 0.38833 0.36205 0.24776 0.01324  -0.08392 0.00697  143 HIS A CB  
1116 C CB  B HIS A 143 ? 0.35318 0.35214 0.22505 -0.00570 0.00556  -0.03776 143 HIS A CB  
1117 C CG  A HIS A 143 ? 0.45855 0.37844 0.30625 -0.00537 -0.08832 -0.00949 143 HIS A CG  
1118 C CG  B HIS A 143 ? 0.38231 0.35943 0.23685 -0.02459 0.02782  -0.07864 143 HIS A CG  
1119 N ND1 A HIS A 143 ? 0.50503 0.38981 0.36461 -0.00188 -0.07995 -0.00277 143 HIS A ND1 
1120 N ND1 B HIS A 143 ? 0.39698 0.37176 0.23417 -0.03663 0.02337  -0.08329 143 HIS A ND1 
1121 C CD2 A HIS A 143 ? 0.47658 0.37284 0.32049 0.00316  -0.09229 0.00389  143 HIS A CD2 
1122 C CD2 B HIS A 143 ? 0.40616 0.35463 0.25216 -0.04385 0.00443  -0.09836 143 HIS A CD2 
1123 C CE1 A HIS A 143 ? 0.46126 0.37854 0.34667 0.01927  -0.11627 0.01588  143 HIS A CE1 
1124 C CE1 B HIS A 143 ? 0.39979 0.34890 0.23282 -0.02964 -0.00649 -0.09655 143 HIS A CE1 
1125 N NE2 A HIS A 143 ? 0.42271 0.34403 0.32086 0.03689  -0.14167 0.01485  143 HIS A NE2 
1126 N NE2 B HIS A 143 ? 0.41337 0.35087 0.24667 -0.05266 -0.00855 -0.09623 143 HIS A NE2 
1127 N N   . PHE A 144 ? 0.24355 0.34583 0.19707 0.04708  -0.03148 0.05600  144 PHE A N   
1128 C CA  . PHE A 144 ? 0.25761 0.33105 0.20324 0.06338  -0.02992 0.01469  144 PHE A CA  
1129 C C   . PHE A 144 ? 0.27118 0.30408 0.21774 0.02387  -0.02142 0.01764  144 PHE A C   
1130 O O   . PHE A 144 ? 0.27749 0.31636 0.21469 0.01386  -0.01095 0.00079  144 PHE A O   
1131 C CB  . PHE A 144 ? 0.22815 0.32098 0.18619 0.04122  -0.02029 -0.00399 144 PHE A CB  
1132 C CG  . PHE A 144 ? 0.22671 0.33740 0.19692 0.02518  -0.00495 -0.00222 144 PHE A CG  
1133 C CD1 . PHE A 144 ? 0.21605 0.31997 0.21969 0.05175  0.00841  -0.00374 144 PHE A CD1 
1134 C CD2 . PHE A 144 ? 0.24426 0.34481 0.18160 0.04210  0.00093  0.01675  144 PHE A CD2 
1135 C CE1 . PHE A 144 ? 0.28074 0.33983 0.21636 0.04077  0.01194  0.01593  144 PHE A CE1 
1136 C CE2 . PHE A 144 ? 0.21546 0.33460 0.21420 0.02841  0.01614  0.02900  144 PHE A CE2 
1137 C CZ  . PHE A 144 ? 0.27349 0.32721 0.23011 0.01793  0.03562  0.04098  144 PHE A CZ  
1138 N N   . GLU A 145 ? 0.32041 0.28156 0.19970 0.03738  -0.01562 0.00379  145 GLU A N   
1139 C CA  . GLU A 145 ? 0.26865 0.28021 0.18967 0.03282  -0.04964 0.02113  145 GLU A CA  
1140 C C   . GLU A 145 ? 0.27755 0.28461 0.20760 0.02089  -0.03515 -0.00154 145 GLU A C   
1141 O O   . GLU A 145 ? 0.31918 0.28785 0.25456 0.06743  -0.04585 -0.01937 145 GLU A O   
1142 C CB  . GLU A 145 ? 0.30448 0.34536 0.17242 0.03435  -0.04377 0.00866  145 GLU A CB  
1143 C CG  . GLU A 145 ? 0.30994 0.35239 0.16120 0.04688  -0.01625 0.00170  145 GLU A CG  
1144 C CD  . GLU A 145 ? 0.32583 0.34185 0.20199 0.04159  -0.00781 -0.00601 145 GLU A CD  
1145 O OE1 . GLU A 145 ? 0.32549 0.31094 0.22911 0.04057  -0.00506 0.00315  145 GLU A OE1 
1146 O OE2 . GLU A 145 ? 0.34061 0.43787 0.19412 0.05627  -0.01946 0.01992  145 GLU A OE2 
1147 N N   . ARG A 146 ? 0.29790 0.27948 0.19410 -0.01075 -0.02097 0.02717  146 ARG A N   
1148 C CA  . ARG A 146 ? 0.27583 0.28086 0.19408 -0.00819 -0.04610 0.01665  146 ARG A CA  
1149 C C   . ARG A 146 ? 0.28335 0.27735 0.20992 0.01831  -0.02049 0.04225  146 ARG A C   
1150 O O   . ARG A 146 ? 0.37029 0.32342 0.22868 0.06812  -0.00954 0.05229  146 ARG A O   
1151 C CB  . ARG A 146 ? 0.31596 0.31337 0.22811 -0.04744 -0.05537 0.02950  146 ARG A CB  
1152 C CG  . ARG A 146 ? 0.32582 0.33873 0.23702 -0.02939 -0.06897 0.02685  146 ARG A CG  
1153 C CD  . ARG A 146 ? 0.33326 0.38127 0.25735 0.01575  -0.08920 0.01934  146 ARG A CD  
1154 N NE  . ARG A 146 ? 0.35808 0.43152 0.24914 0.03136  -0.12042 0.00498  146 ARG A NE  
1155 C CZ  . ARG A 146 ? 0.45555 0.47071 0.26386 0.02553  -0.12925 -0.02668 146 ARG A CZ  
1156 N NH1 . ARG A 146 ? 0.53498 0.49834 0.27581 -0.00374 -0.14001 -0.07173 146 ARG A NH1 
1157 N NH2 . ARG A 146 ? 0.47921 0.49891 0.28660 0.01272  -0.07359 -0.00862 146 ARG A NH2 
1158 N N   . PHE A 147 ? 0.27452 0.29922 0.18450 0.02035  -0.00550 0.04146  147 PHE A N   
1159 C CA  . PHE A 147 ? 0.27905 0.30351 0.18041 0.02504  -0.00829 0.01710  147 PHE A CA  
1160 C C   . PHE A 147 ? 0.24588 0.30838 0.19790 0.00711  0.00467  -0.00004 147 PHE A C   
1161 O O   . PHE A 147 ? 0.24093 0.32320 0.22626 0.02266  -0.01114 0.01602  147 PHE A O   
1162 C CB  . PHE A 147 ? 0.23846 0.29804 0.18166 0.02400  -0.01668 0.02375  147 PHE A CB  
1163 C CG  . PHE A 147 ? 0.25763 0.29449 0.18685 0.04932  -0.01929 0.02030  147 PHE A CG  
1164 C CD1 . PHE A 147 ? 0.28780 0.29659 0.20736 0.03650  -0.02650 -0.00168 147 PHE A CD1 
1165 C CD2 . PHE A 147 ? 0.26824 0.29568 0.19370 0.06903  -0.02218 0.00756  147 PHE A CD2 
1166 C CE1 . PHE A 147 ? 0.28563 0.27653 0.19224 0.03917  -0.05256 0.01228  147 PHE A CE1 
1167 C CE2 . PHE A 147 ? 0.28718 0.30841 0.19959 0.07256  -0.00892 -0.00316 147 PHE A CE2 
1168 C CZ  . PHE A 147 ? 0.27412 0.29075 0.19851 0.05506  -0.02125 0.02378  147 PHE A CZ  
1169 N N   . ARG A 148 ? 0.26933 0.30498 0.20869 -0.00439 0.00127  0.00390  148 ARG A N   
1170 C CA  . ARG A 148 ? 0.30440 0.29405 0.22687 -0.03080 -0.01313 -0.01745 148 ARG A CA  
1171 C C   . ARG A 148 ? 0.29516 0.30541 0.20880 -0.00629 0.01527  0.01723  148 ARG A C   
1172 O O   . ARG A 148 ? 0.32750 0.33338 0.23724 0.05645  0.02630  0.01011  148 ARG A O   
1173 C CB  . ARG A 148 ? 0.41528 0.31583 0.26428 -0.06646 0.00312  -0.04229 148 ARG A CB  
1174 C CG  . ARG A 148 ? 0.50383 0.38733 0.32226 -0.04392 -0.03383 -0.04945 148 ARG A CG  
1175 C CD  . ARG A 148 ? 0.56408 0.42416 0.35981 -0.01410 -0.06284 -0.01023 148 ARG A CD  
1176 N NE  . ARG A 148 ? 0.57618 0.44404 0.40195 0.00586  -0.08259 0.04826  148 ARG A NE  
1177 C CZ  . ARG A 148 ? 0.60541 0.45872 0.45186 0.06747  -0.04956 0.12207  148 ARG A CZ  
1178 N NH1 . ARG A 148 ? 0.61800 0.45298 0.46537 0.11097  -0.05593 0.13370  148 ARG A NH1 
1179 N NH2 . ARG A 148 ? 0.63836 0.50437 0.46603 0.10419  -0.03110 0.15233  148 ARG A NH2 
1180 N N   . GLY A 149 ? 0.32557 0.33372 0.19966 -0.02694 0.01986  0.01049  149 GLY A N   
1181 C CA  . GLY A 149 ? 0.30416 0.35627 0.18937 -0.02859 0.02456  0.00450  149 GLY A CA  
1182 C C   . GLY A 149 ? 0.25889 0.34604 0.19885 -0.03561 0.01321  -0.00403 149 GLY A C   
1183 O O   . GLY A 149 ? 0.25411 0.43627 0.21400 -0.02519 -0.02980 -0.00193 149 GLY A O   
1184 N N   . ASP A 150 ? 0.23623 0.27353 0.19191 -0.01680 0.01476  -0.00766 150 ASP A N   
1185 C CA  . ASP A 150 ? 0.26941 0.28177 0.22590 -0.00740 0.00565  -0.01307 150 ASP A CA  
1186 C C   . ASP A 150 ? 0.25542 0.28227 0.26290 0.01121  0.02439  -0.02417 150 ASP A C   
1187 O O   . ASP A 150 ? 0.23830 0.31536 0.32108 0.00437  0.02841  -0.02681 150 ASP A O   
1188 C CB  . ASP A 150 ? 0.24225 0.25499 0.23480 -0.00206 0.00753  0.02691  150 ASP A CB  
1189 C CG  . ASP A 150 ? 0.28940 0.30630 0.26870 -0.00017 0.00950  0.01947  150 ASP A CG  
1190 O OD1 . ASP A 150 ? 0.33732 0.31365 0.31372 -0.01331 -0.00453 0.03287  150 ASP A OD1 
1191 O OD2 . ASP A 150 ? 0.31251 0.33585 0.27108 0.02150  0.04599  0.00745  150 ASP A OD2 
1192 N N   . GLY A 151 ? 0.22740 0.24073 0.23237 0.02393  0.00591  -0.01095 151 GLY A N   
1193 C CA  . GLY A 151 ? 0.21860 0.24251 0.24336 0.02347  -0.01724 -0.00364 151 GLY A CA  
1194 C C   . GLY A 151 ? 0.22804 0.20852 0.19937 -0.01047 -0.02174 0.00830  151 GLY A C   
1195 O O   . GLY A 151 ? 0.25600 0.23225 0.19673 0.03422  -0.01898 0.00454  151 GLY A O   
1196 N N   . LEU A 152 ? 0.22101 0.24422 0.20565 -0.04031 -0.04157 0.00309  152 LEU A N   
1197 C CA  . LEU A 152 ? 0.17874 0.26812 0.19140 -0.02601 -0.02963 -0.00088 152 LEU A CA  
1198 C C   . LEU A 152 ? 0.18436 0.27422 0.20364 0.02284  -0.00167 -0.01499 152 LEU A C   
1199 O O   . LEU A 152 ? 0.19640 0.30432 0.23190 0.02121  0.00248  -0.04172 152 LEU A O   
1200 C CB  . LEU A 152 ? 0.25131 0.29556 0.18451 0.01180  0.00112  0.00908  152 LEU A CB  
1201 C CG  . LEU A 152 ? 0.24378 0.32829 0.19366 0.03477  -0.01311 0.01958  152 LEU A CG  
1202 C CD1 . LEU A 152 ? 0.26698 0.32990 0.22002 0.03665  -0.05115 0.04630  152 LEU A CD1 
1203 C CD2 . LEU A 152 ? 0.21856 0.33144 0.20677 0.02848  -0.01679 0.01775  152 LEU A CD2 
1204 N N   . CYS A 153 ? 0.18667 0.27588 0.18234 0.00653  0.01240  -0.03832 153 CYS A N   
1205 C CA  . CYS A 153 ? 0.18740 0.26748 0.17899 -0.01180 -0.01193 0.00341  153 CYS A CA  
1206 C C   . CYS A 153 ? 0.22727 0.20797 0.21091 0.02167  -0.00467 -0.00940 153 CYS A C   
1207 O O   . CYS A 153 ? 0.20736 0.22288 0.20850 0.01567  0.01563  0.00313  153 CYS A O   
1208 C CB  . CYS A 153 ? 0.19040 0.27368 0.17755 0.04298  -0.01912 0.00339  153 CYS A CB  
1209 S SG  . CYS A 153 ? 0.22019 0.29353 0.20604 0.00756  0.00523  -0.01804 153 CYS A SG  
1210 N N   . MET A 154 ? 0.21092 0.19671 0.19195 -0.00398 -0.02773 -0.02343 154 MET A N   
1211 C CA  . MET A 154 ? 0.22661 0.22055 0.17594 -0.02047 -0.01499 -0.02514 154 MET A CA  
1212 C C   . MET A 154 ? 0.20771 0.27429 0.17493 -0.00264 0.00304  -0.00841 154 MET A C   
1213 O O   . MET A 154 ? 0.19003 0.27773 0.18705 0.03260  0.01295  0.00893  154 MET A O   
1214 C CB  . MET A 154 ? 0.20790 0.19279 0.20095 0.00236  -0.00647 -0.01078 154 MET A CB  
1215 C CG  . MET A 154 ? 0.20910 0.19764 0.22936 -0.01120 -0.00726 -0.01811 154 MET A CG  
1216 S SD  . MET A 154 ? 0.20831 0.27407 0.22059 0.02458  0.00586  0.01223  154 MET A SD  
1217 C CE  . MET A 154 ? 0.23745 0.25978 0.20826 0.05100  -0.00299 0.00815  154 MET A CE  
1218 N N   . SER A 155 ? 0.21897 0.24898 0.15767 -0.00177 0.00099  0.00538  155 SER A N   
1219 C CA  . SER A 155 ? 0.19779 0.22233 0.17155 0.00452  -0.00850 -0.00612 155 SER A CA  
1220 C C   . SER A 155 ? 0.24698 0.23876 0.17612 0.01680  0.00541  -0.01749 155 SER A C   
1221 O O   . SER A 155 ? 0.24787 0.25594 0.19925 0.01791  0.02377  -0.01976 155 SER A O   
1222 C CB  . SER A 155 ? 0.27507 0.25145 0.16665 0.04984  -0.04010 0.00417  155 SER A CB  
1223 O OG  . SER A 155 ? 0.28460 0.27673 0.22127 0.02728  0.02231  -0.00753 155 SER A OG  
1224 N N   . THR A 156 ? 0.26531 0.19969 0.18719 0.01418  -0.00558 -0.04318 156 THR A N   
1225 C CA  . THR A 156 ? 0.22545 0.21488 0.21097 0.01674  0.02293  -0.03550 156 THR A CA  
1226 C C   . THR A 156 ? 0.21711 0.24473 0.21854 0.01141  0.02955  -0.01118 156 THR A C   
1227 O O   . THR A 156 ? 0.23410 0.30313 0.21787 0.04258  0.01791  -0.00463 156 THR A O   
1228 C CB  . THR A 156 ? 0.24100 0.26680 0.21338 0.02328  0.03591  -0.03094 156 THR A CB  
1229 O OG1 . THR A 156 ? 0.25849 0.28506 0.20693 0.01488  0.01380  0.00976  156 THR A OG1 
1230 C CG2 . THR A 156 ? 0.24061 0.30775 0.23279 0.00594  0.05622  -0.00638 156 THR A CG2 
1231 N N   . PRO A 157 ? 0.24890 0.22285 0.22489 -0.01144 -0.00228 -0.01911 157 PRO A N   
1232 C CA  . PRO A 157 ? 0.25502 0.22828 0.23278 -0.05907 0.00678  -0.01592 157 PRO A CA  
1233 C C   . PRO A 157 ? 0.26549 0.25395 0.22749 -0.00101 0.02727  -0.02770 157 PRO A C   
1234 O O   . PRO A 157 ? 0.26346 0.27365 0.22518 0.01547  0.00382  -0.01241 157 PRO A O   
1235 C CB  . PRO A 157 ? 0.26890 0.22738 0.24068 -0.02365 -0.02698 -0.03087 157 PRO A CB  
1236 C CG  . PRO A 157 ? 0.30414 0.25473 0.26331 -0.03066 -0.05018 -0.01328 157 PRO A CG  
1237 C CD  . PRO A 157 ? 0.26295 0.22239 0.25351 -0.02494 0.00332  -0.00582 157 PRO A CD  
1238 N N   . SER A 158 ? 0.29318 0.26427 0.20389 -0.00933 0.01664  -0.03343 158 SER A N   
1239 C CA  . SER A 158 ? 0.28519 0.21675 0.20244 0.01620  0.04108  -0.02686 158 SER A CA  
1240 C C   . SER A 158 ? 0.21823 0.25569 0.18941 -0.02605 -0.01532 -0.00646 158 SER A C   
1241 O O   . SER A 158 ? 0.26027 0.28169 0.18742 0.02653  0.01409  -0.01811 158 SER A O   
1242 C CB  . SER A 158 ? 0.29523 0.24331 0.22222 0.04122  0.00913  -0.03953 158 SER A CB  
1243 O OG  . SER A 158 ? 0.31119 0.28028 0.21653 0.05458  0.00294  -0.02516 158 SER A OG  
1244 N N   . GLY A 159 ? 0.18924 0.22011 0.19847 -0.01853 0.01601  -0.03373 159 GLY A N   
1245 C CA  . GLY A 159 ? 0.18401 0.24683 0.21842 -0.02290 0.00233  -0.01302 159 GLY A CA  
1246 C C   . GLY A 159 ? 0.20952 0.24130 0.20154 -0.00957 0.00704  0.00614  159 GLY A C   
1247 O O   . GLY A 159 ? 0.20545 0.25865 0.20972 -0.01375 -0.01129 -0.01064 159 GLY A O   
1248 N N   . THR A 160 ? 0.17591 0.26329 0.18007 0.01832  -0.00107 -0.02858 160 THR A N   
1249 C CA  . THR A 160 ? 0.19234 0.23876 0.20718 0.05465  0.03928  -0.00302 160 THR A CA  
1250 C C   . THR A 160 ? 0.17539 0.25465 0.17505 0.00946  0.00983  0.00137  160 THR A C   
1251 O O   . THR A 160 ? 0.21888 0.24597 0.19921 0.01732  0.00796  -0.01331 160 THR A O   
1252 C CB  . THR A 160 ? 0.20460 0.22451 0.21614 -0.00075 0.01555  -0.01787 160 THR A CB  
1253 O OG1 . THR A 160 ? 0.20035 0.23604 0.22917 -0.00361 0.00299  -0.03002 160 THR A OG1 
1254 C CG2 . THR A 160 ? 0.21211 0.23534 0.23281 -0.01103 0.02091  -0.00877 160 THR A CG2 
1255 N N   . THR A 161 ? 0.21361 0.29105 0.15762 -0.02106 0.00899  -0.00118 161 THR A N   
1256 C CA  . THR A 161 ? 0.20714 0.28238 0.17862 -0.03303 0.00693  -0.00509 161 THR A CA  
1257 C C   . THR A 161 ? 0.19457 0.27809 0.18039 -0.00098 0.01210  -0.00863 161 THR A C   
1258 O O   . THR A 161 ? 0.24536 0.32149 0.17611 -0.02046 -0.00831 0.02266  161 THR A O   
1259 C CB  . THR A 161 ? 0.16127 0.29022 0.21226 -0.00883 -0.01287 -0.06338 161 THR A CB  
1260 O OG1 . THR A 161 ? 0.22712 0.27877 0.21901 0.01581  -0.00309 -0.02645 161 THR A OG1 
1261 C CG2 . THR A 161 ? 0.21553 0.32727 0.25489 -0.06729 -0.01057 -0.06118 161 THR A CG2 
1262 N N   . ALA A 162 ? 0.20579 0.28774 0.20501 -0.02537 -0.01465 -0.02546 162 ALA A N   
1263 C CA  . ALA A 162 ? 0.19683 0.28674 0.21909 -0.01182 0.01933  -0.06563 162 ALA A CA  
1264 C C   . ALA A 162 ? 0.23662 0.30050 0.20300 -0.03049 0.01378  -0.01281 162 ALA A C   
1265 O O   . ALA A 162 ? 0.21523 0.35563 0.19716 0.01897  0.00997  0.00487  162 ALA A O   
1266 C CB  . ALA A 162 ? 0.23919 0.29920 0.20800 0.03132  0.05122  -0.09161 162 ALA A CB  
1267 N N   . TYR A 163 ? 0.22987 0.27612 0.18996 -0.02721 0.01026  -0.02089 163 TYR A N   
1268 C CA  . TYR A 163 ? 0.17565 0.24708 0.18901 -0.00117 -0.00320 -0.04055 163 TYR A CA  
1269 C C   . TYR A 163 ? 0.16807 0.22634 0.19073 0.00825  0.00588  -0.01428 163 TYR A C   
1270 O O   . TYR A 163 ? 0.18079 0.24896 0.21747 0.01146  0.00040  -0.01051 163 TYR A O   
1271 C CB  . TYR A 163 ? 0.12831 0.25174 0.21394 -0.01029 -0.02742 -0.00973 163 TYR A CB  
1272 C CG  . TYR A 163 ? 0.17293 0.24750 0.21693 -0.04518 -0.01505 -0.00057 163 TYR A CG  
1273 C CD1 . TYR A 163 ? 0.18273 0.24036 0.21895 -0.03008 0.02876  -0.01949 163 TYR A CD1 
1274 C CD2 . TYR A 163 ? 0.21954 0.29120 0.27258 -0.06632 -0.03985 -0.00549 163 TYR A CD2 
1275 C CE1 . TYR A 163 ? 0.14804 0.28276 0.22929 -0.05270 0.00409  -0.01768 163 TYR A CE1 
1276 C CE2 . TYR A 163 ? 0.28745 0.28194 0.29884 -0.03510 -0.06349 0.01634  163 TYR A CE2 
1277 C CZ  . TYR A 163 ? 0.24187 0.26373 0.27847 -0.04194 -0.06271 0.00349  163 TYR A CZ  
1278 O OH  . TYR A 163 ? 0.28053 0.29789 0.31407 -0.06037 -0.08061 0.01849  163 TYR A OH  
1279 N N   . ASN A 164 ? 0.18356 0.23572 0.17422 -0.02481 0.02238  0.02422  164 ASN A N   
1280 C CA  . ASN A 164 ? 0.18590 0.21423 0.20269 -0.01777 0.01894  0.02804  164 ASN A CA  
1281 C C   . ASN A 164 ? 0.19791 0.23663 0.19353 0.01707  0.00574  -0.00040 164 ASN A C   
1282 O O   . ASN A 164 ? 0.18740 0.21066 0.21440 0.03287  -0.00773 -0.00704 164 ASN A O   
1283 C CB  . ASN A 164 ? 0.21140 0.15032 0.20161 -0.02687 0.02524  -0.00248 164 ASN A CB  
1284 C CG  . ASN A 164 ? 0.22858 0.21845 0.18695 -0.03637 0.00641  0.00265  164 ASN A CG  
1285 O OD1 . ASN A 164 ? 0.26237 0.29419 0.18849 -0.04143 0.02205  -0.00982 164 ASN A OD1 
1286 N ND2 . ASN A 164 ? 0.19577 0.23749 0.20284 -0.00894 -0.00567 -0.01400 164 ASN A ND2 
1287 N N   . LYS A 165 ? 0.19445 0.27025 0.17551 0.01297  -0.04860 0.01769  165 LYS A N   
1288 C CA  . LYS A 165 ? 0.20213 0.26613 0.15705 0.01310  -0.03856 0.02365  165 LYS A CA  
1289 C C   . LYS A 165 ? 0.21816 0.26085 0.15066 -0.02265 0.00522  -0.01154 165 LYS A C   
1290 O O   . LYS A 165 ? 0.20793 0.24847 0.19282 0.00584  0.01658  -0.00373 165 LYS A O   
1291 C CB  . LYS A 165 ? 0.21976 0.32387 0.15045 0.02943  -0.04552 0.01877  165 LYS A CB  
1292 C CG  . LYS A 165 ? 0.23523 0.31726 0.14446 0.02783  -0.06893 0.00654  165 LYS A CG  
1293 C CD  . LYS A 165 ? 0.25653 0.33951 0.16698 0.02843  -0.05452 0.01180  165 LYS A CD  
1294 C CE  . LYS A 165 ? 0.35895 0.37406 0.23754 0.09210  -0.10053 -0.01636 165 LYS A CE  
1295 N NZ  . LYS A 165 ? 0.44869 0.41177 0.27362 0.11869  -0.11539 -0.01844 165 LYS A NZ  
1296 N N   . SER A 166 ? 0.23053 0.25624 0.16938 -0.04582 -0.00173 0.00907  166 SER A N   
1297 C CA  . SER A 166 ? 0.22010 0.24916 0.18064 0.00111  0.02379  0.01612  166 SER A CA  
1298 C C   . SER A 166 ? 0.21710 0.23979 0.19559 0.02993  0.01313  0.00671  166 SER A C   
1299 O O   . SER A 166 ? 0.28043 0.20877 0.22685 -0.00500 -0.00001 0.01803  166 SER A O   
1300 C CB  . SER A 166 ? 0.23712 0.29087 0.19794 0.00716  0.06092  0.00522  166 SER A CB  
1301 O OG  . SER A 166 ? 0.31141 0.27545 0.22792 -0.02110 0.06264  0.00664  166 SER A OG  
1302 N N   . LEU A 167 ? 0.23732 0.28659 0.16891 -0.01682 0.00032  0.01155  167 LEU A N   
1303 C CA  . LEU A 167 ? 0.20043 0.29208 0.16768 0.01559  -0.00707 -0.02356 167 LEU A CA  
1304 C C   . LEU A 167 ? 0.20985 0.30487 0.18152 -0.00617 -0.01672 -0.01952 167 LEU A C   
1305 O O   . LEU A 167 ? 0.21559 0.34426 0.19344 -0.01294 0.00355  -0.02178 167 LEU A O   
1306 C CB  . LEU A 167 ? 0.18835 0.25698 0.19758 -0.01322 0.00744  -0.01082 167 LEU A CB  
1307 C CG  . LEU A 167 ? 0.21405 0.24609 0.20818 -0.00743 -0.00725 0.00131  167 LEU A CG  
1308 C CD1 . LEU A 167 ? 0.27391 0.26351 0.25752 0.01007  -0.01909 0.01001  167 LEU A CD1 
1309 C CD2 . LEU A 167 ? 0.20933 0.23223 0.21431 -0.02847 -0.00929 -0.00075 167 LEU A CD2 
1310 N N   . GLY A 168 ? 0.20928 0.30215 0.18292 -0.01469 -0.01281 -0.01892 168 GLY A N   
1311 C CA  . GLY A 168 ? 0.17988 0.32089 0.20758 -0.02050 -0.00394 -0.02619 168 GLY A CA  
1312 C C   . GLY A 168 ? 0.18874 0.30361 0.19841 -0.02324 0.01547  -0.01533 168 GLY A C   
1313 O O   . GLY A 168 ? 0.21629 0.30410 0.21121 -0.01152 0.01248  0.00468  168 GLY A O   
1314 N N   . GLY A 169 ? 0.20597 0.28630 0.18623 -0.00648 0.02206  -0.01300 169 GLY A N   
1315 C CA  . GLY A 169 ? 0.19364 0.25899 0.19343 -0.03455 -0.02624 -0.01077 169 GLY A CA  
1316 C C   . GLY A 169 ? 0.19079 0.25165 0.19509 -0.02924 0.00835  -0.02233 169 GLY A C   
1317 O O   . GLY A 169 ? 0.21643 0.25164 0.18897 -0.03232 0.00238  -0.00208 169 GLY A O   
1318 N N   . ALA A 170 ? 0.19498 0.20912 0.18979 -0.01937 -0.00551 0.01496  170 ALA A N   
1319 C CA  . ALA A 170 ? 0.17701 0.22877 0.18807 -0.03592 0.02280  -0.03940 170 ALA A CA  
1320 C C   . ALA A 170 ? 0.20250 0.27463 0.19831 0.01468  0.01673  -0.02930 170 ALA A C   
1321 O O   . ALA A 170 ? 0.21851 0.29224 0.20045 0.06281  0.00291  -0.00723 170 ALA A O   
1322 C CB  . ALA A 170 ? 0.22889 0.23475 0.21651 -0.03661 0.05020  -0.01278 170 ALA A CB  
1323 N N   . LEU A 171 ? 0.20330 0.28139 0.17926 -0.02967 0.01307  -0.03546 171 LEU A N   
1324 C CA  . LEU A 171 ? 0.19512 0.26323 0.18174 -0.01289 -0.00744 -0.03428 171 LEU A CA  
1325 C C   . LEU A 171 ? 0.22097 0.25714 0.23088 0.00928  -0.00850 -0.02783 171 LEU A C   
1326 O O   . LEU A 171 ? 0.23577 0.26413 0.28487 0.00146  0.00393  -0.00337 171 LEU A O   
1327 C CB  . LEU A 171 ? 0.23304 0.27063 0.17643 -0.01117 -0.01981 0.01288  171 LEU A CB  
1328 C CG  . LEU A 171 ? 0.22226 0.29556 0.20019 -0.01269 -0.02264 0.01053  171 LEU A CG  
1329 C CD1 . LEU A 171 ? 0.24398 0.36673 0.20623 -0.01253 -0.01570 0.01330  171 LEU A CD1 
1330 C CD2 . LEU A 171 ? 0.22185 0.36847 0.22002 0.00307  -0.01830 0.00203  171 LEU A CD2 
1331 N N   . MET A 172 ? 0.23558 0.23648 0.24632 0.01601  0.00607  -0.02611 172 MET A N   
1332 C CA  A MET A 172 ? 0.27872 0.26335 0.26497 -0.02739 -0.00208 -0.02619 172 MET A CA  
1333 C CA  B MET A 172 ? 0.27378 0.24592 0.26466 -0.00439 0.00627  -0.02068 172 MET A CA  
1334 C C   . MET A 172 ? 0.25557 0.26204 0.28858 -0.00859 0.02956  -0.04564 172 MET A C   
1335 O O   . MET A 172 ? 0.27816 0.28975 0.32683 -0.01492 0.05298  -0.07105 172 MET A O   
1336 C CB  A MET A 172 ? 0.37727 0.30500 0.27502 -0.01255 -0.02028 -0.00867 172 MET A CB  
1337 C CB  B MET A 172 ? 0.34429 0.24998 0.27197 0.01938  -0.01101 0.00624  172 MET A CB  
1338 C CG  A MET A 172 ? 0.44025 0.32120 0.27185 -0.01503 0.00574  -0.00951 172 MET A CG  
1339 C CG  B MET A 172 ? 0.40302 0.25362 0.28104 0.04310  0.00504  0.02412  172 MET A CG  
1340 S SD  A MET A 172 ? 0.50814 0.29996 0.26005 -0.04022 -0.01256 -0.02373 172 MET A SD  
1341 S SD  B MET A 172 ? 0.47787 0.26843 0.30085 0.06753  0.01895  0.02092  172 MET A SD  
1342 C CE  A MET A 172 ? 0.51961 0.30307 0.28950 0.00965  -0.07628 0.02903  172 MET A CE  
1343 C CE  B MET A 172 ? 0.49746 0.26203 0.29463 0.06270  0.02471  0.00694  172 MET A CE  
1344 N N   . HIS A 173 ? 0.28279 0.23655 0.29187 -0.05294 0.02146  -0.07259 173 HIS A N   
1345 C CA  . HIS A 173 ? 0.23643 0.25776 0.29090 -0.03120 0.00297  -0.06952 173 HIS A CA  
1346 C C   . HIS A 173 ? 0.26886 0.32374 0.31358 -0.00362 0.00159  -0.06739 173 HIS A C   
1347 O O   . HIS A 173 ? 0.27485 0.33738 0.28422 0.00905  -0.01281 -0.04708 173 HIS A O   
1348 C CB  . HIS A 173 ? 0.28836 0.25147 0.30794 -0.02387 0.01068  -0.05901 173 HIS A CB  
1349 C CG  . HIS A 173 ? 0.31455 0.25879 0.33338 0.01987  -0.00655 -0.08074 173 HIS A CG  
1350 N ND1 . HIS A 173 ? 0.37677 0.26327 0.35839 0.01082  -0.02808 -0.08269 173 HIS A ND1 
1351 C CD2 . HIS A 173 ? 0.30126 0.28441 0.34043 -0.00637 -0.00009 -0.06670 173 HIS A CD2 
1352 C CE1 . HIS A 173 ? 0.37465 0.30094 0.35846 0.02075  -0.02540 -0.05108 173 HIS A CE1 
1353 N NE2 . HIS A 173 ? 0.33776 0.28646 0.35220 0.01253  -0.01868 -0.05914 173 HIS A NE2 
1354 N N   . PRO A 174 ? 0.25565 0.31822 0.33756 0.02951  -0.00034 -0.13224 174 PRO A N   
1355 C CA  . PRO A 174 ? 0.24130 0.38406 0.35329 0.05751  -0.01217 -0.12443 174 PRO A CA  
1356 C C   . PRO A 174 ? 0.27286 0.42531 0.37697 0.05444  -0.04466 -0.13236 174 PRO A C   
1357 O O   . PRO A 174 ? 0.29665 0.45323 0.43251 0.06272  -0.03974 -0.11608 174 PRO A O   
1358 C CB  . PRO A 174 ? 0.28873 0.44534 0.38797 0.06593  -0.00737 -0.08670 174 PRO A CB  
1359 C CG  . PRO A 174 ? 0.33558 0.45087 0.41421 0.07418  0.03632  -0.05316 174 PRO A CG  
1360 C CD  . PRO A 174 ? 0.24252 0.37611 0.37101 0.00842  0.03887  -0.10003 174 PRO A CD  
1361 N N   . SER A 175 ? 0.32103 0.39071 0.36326 0.02907  -0.04165 -0.13497 175 SER A N   
1362 C CA  . SER A 175 ? 0.39004 0.38213 0.38450 0.03534  -0.08144 -0.08016 175 SER A CA  
1363 C C   . SER A 175 ? 0.42538 0.38471 0.37389 0.01374  -0.09501 -0.06314 175 SER A C   
1364 O O   . SER A 175 ? 0.49793 0.40154 0.40316 0.02364  -0.11907 -0.06546 175 SER A O   
1365 C CB  . SER A 175 ? 0.42111 0.36983 0.41964 0.02142  -0.06291 -0.05229 175 SER A CB  
1366 O OG  . SER A 175 ? 0.47193 0.38651 0.43295 -0.01034 -0.08699 -0.05096 175 SER A OG  
1367 N N   . ILE A 176 ? 0.32739 0.34928 0.34743 0.00526  -0.06674 -0.04074 176 ILE A N   
1368 C CA  . ILE A 176 ? 0.29937 0.33283 0.32732 -0.02084 -0.05683 -0.02625 176 ILE A CA  
1369 C C   . ILE A 176 ? 0.29261 0.29554 0.31743 -0.01734 -0.01777 -0.01024 176 ILE A C   
1370 O O   . ILE A 176 ? 0.30707 0.29180 0.31101 0.00817  0.01070  0.02664  176 ILE A O   
1371 C CB  . ILE A 176 ? 0.26211 0.32744 0.33178 -0.00314 -0.05411 -0.05863 176 ILE A CB  
1372 C CG1 . ILE A 176 ? 0.30081 0.32106 0.37191 0.05419  -0.09223 -0.08711 176 ILE A CG1 
1373 C CG2 . ILE A 176 ? 0.26739 0.37310 0.30825 -0.02272 -0.03321 -0.03826 176 ILE A CG2 
1374 C CD1 . ILE A 176 ? 0.35227 0.29120 0.39420 0.10671  -0.08831 -0.10472 176 ILE A CD1 
1375 N N   . GLU A 177 ? 0.29539 0.27416 0.27917 -0.00125 0.00657  -0.02031 177 GLU A N   
1376 C CA  . GLU A 177 ? 0.35688 0.23114 0.29964 -0.00824 0.00315  -0.03620 177 GLU A CA  
1377 C C   . GLU A 177 ? 0.36896 0.22639 0.28742 -0.02485 0.01788  -0.02494 177 GLU A C   
1378 O O   . GLU A 177 ? 0.38253 0.28123 0.26366 -0.02940 0.02328  -0.00421 177 GLU A O   
1379 C CB  . GLU A 177 ? 0.47711 0.20924 0.34632 -0.02324 0.01665  -0.03220 177 GLU A CB  
1380 C CG  . GLU A 177 ? 0.56713 0.19793 0.34676 0.01051  0.04391  -0.06616 177 GLU A CG  
1381 C CD  . GLU A 177 ? 0.64438 0.25720 0.39786 0.00629  0.07029  -0.06474 177 GLU A CD  
1382 O OE1 . GLU A 177 ? 0.66060 0.25682 0.41553 -0.04485 0.05722  -0.03553 177 GLU A OE1 
1383 O OE2 . GLU A 177 ? 0.69636 0.28454 0.43869 0.03000  0.09666  -0.06334 177 GLU A OE2 
1384 N N   . ALA A 178 ? 0.32459 0.16989 0.29248 0.01592  0.01736  -0.03468 178 ALA A N   
1385 C CA  . ALA A 178 ? 0.25793 0.17799 0.25147 0.06514  0.01012  -0.04036 178 ALA A CA  
1386 C C   . ALA A 178 ? 0.25624 0.25079 0.23214 0.01651  -0.01421 0.00408  178 ALA A C   
1387 O O   . ALA A 178 ? 0.27609 0.29697 0.22547 0.04191  0.03622  0.03895  178 ALA A O   
1388 C CB  . ALA A 178 ? 0.30804 0.20632 0.27068 0.03307  -0.00479 -0.02125 178 ALA A CB  
1389 N N   . MET A 179 ? 0.23127 0.21549 0.23428 0.01989  -0.01404 0.03256  179 MET A N   
1390 C CA  . MET A 179 ? 0.23417 0.21227 0.21087 0.03432  -0.01679 0.02465  179 MET A CA  
1391 C C   . MET A 179 ? 0.23059 0.20649 0.20856 0.02729  -0.02612 0.03616  179 MET A C   
1392 O O   . MET A 179 ? 0.23148 0.23710 0.22851 -0.01652 0.04252  0.04164  179 MET A O   
1393 C CB  . MET A 179 ? 0.26032 0.21101 0.19772 0.06914  -0.02131 0.02737  179 MET A CB  
1394 C CG  . MET A 179 ? 0.26053 0.22093 0.18820 0.05380  -0.01983 0.01525  179 MET A CG  
1395 S SD  . MET A 179 ? 0.25996 0.26525 0.22664 0.05348  -0.00314 0.00630  179 MET A SD  
1396 C CE  . MET A 179 ? 0.23423 0.27797 0.19867 0.02439  0.00752  0.02250  179 MET A CE  
1397 N N   . GLN A 180 ? 0.22246 0.20802 0.19842 0.04370  -0.02350 0.01296  180 GLN A N   
1398 C CA  . GLN A 180 ? 0.22302 0.18327 0.20572 0.02460  -0.00345 0.00424  180 GLN A CA  
1399 C C   . GLN A 180 ? 0.20000 0.20784 0.18529 0.01286  0.00378  0.00746  180 GLN A C   
1400 O O   . GLN A 180 ? 0.20315 0.23520 0.19354 0.00890  0.00729  0.00797  180 GLN A O   
1401 C CB  . GLN A 180 ? 0.22192 0.17671 0.20356 0.07943  -0.01894 0.00933  180 GLN A CB  
1402 C CG  . GLN A 180 ? 0.22138 0.16976 0.19249 0.07450  0.00309  0.00617  180 GLN A CG  
1403 C CD  . GLN A 180 ? 0.22181 0.22359 0.20546 0.05924  0.01580  0.01697  180 GLN A CD  
1404 O OE1 . GLN A 180 ? 0.24270 0.24059 0.20797 0.03358  -0.02232 -0.00854 180 GLN A OE1 
1405 N NE2 . GLN A 180 ? 0.23192 0.20603 0.22634 -0.01664 0.00358  -0.00732 180 GLN A NE2 
1406 N N   . LEU A 181 ? 0.19398 0.22423 0.16122 0.01634  -0.02051 -0.01095 181 LEU A N   
1407 C CA  . LEU A 181 ? 0.21482 0.24956 0.15596 0.01793  -0.03571 -0.00844 181 LEU A CA  
1408 C C   . LEU A 181 ? 0.20841 0.23378 0.18380 0.01954  0.01146  0.00156  181 LEU A C   
1409 O O   . LEU A 181 ? 0.20405 0.25010 0.22148 0.01646  0.01405  0.03674  181 LEU A O   
1410 C CB  . LEU A 181 ? 0.24191 0.26679 0.15657 -0.04253 -0.02011 -0.02811 181 LEU A CB  
1411 C CG  . LEU A 181 ? 0.21467 0.28314 0.17222 -0.05646 0.00283  -0.00113 181 LEU A CG  
1412 C CD1 . LEU A 181 ? 0.19923 0.28748 0.22926 -0.00748 0.02003  0.03397  181 LEU A CD1 
1413 C CD2 . LEU A 181 ? 0.28476 0.29322 0.15049 -0.05474 -0.01615 -0.01950 181 LEU A CD2 
1414 N N   . THR A 182 ? 0.17021 0.21306 0.19795 -0.00737 0.00191  -0.00674 182 THR A N   
1415 C CA  . THR A 182 ? 0.20627 0.22312 0.15796 0.03804  -0.02650 -0.00120 182 THR A CA  
1416 C C   . THR A 182 ? 0.17280 0.24577 0.18741 0.04689  -0.01305 0.00018  182 THR A C   
1417 O O   . THR A 182 ? 0.19231 0.25675 0.19432 0.01744  -0.00202 -0.01183 182 THR A O   
1418 C CB  . THR A 182 ? 0.17247 0.29786 0.19565 -0.00677 0.03282  0.01063  182 THR A CB  
1419 O OG1 . THR A 182 ? 0.18909 0.28840 0.20222 -0.00766 0.01384  0.01347  182 THR A OG1 
1420 C CG2 . THR A 182 ? 0.18642 0.34243 0.22786 -0.01533 -0.00722 0.00288  182 THR A CG2 
1421 N N   . GLU A 183 ? 0.20324 0.24033 0.19707 0.01997  0.00711  -0.00180 183 GLU A N   
1422 C CA  . GLU A 183 ? 0.21134 0.26027 0.20967 -0.00704 0.01540  0.00056  183 GLU A CA  
1423 C C   . GLU A 183 ? 0.20266 0.27267 0.21394 0.00494  -0.00104 0.01578  183 GLU A C   
1424 O O   . GLU A 183 ? 0.21875 0.33132 0.24315 -0.02548 -0.06376 0.04335  183 GLU A O   
1425 C CB  . GLU A 183 ? 0.25869 0.29462 0.21261 0.01734  0.00168  -0.01186 183 GLU A CB  
1426 C CG  . GLU A 183 ? 0.27795 0.31602 0.22003 0.00753  0.05301  0.00330  183 GLU A CG  
1427 C CD  . GLU A 183 ? 0.26368 0.36596 0.25783 -0.01979 0.04553  -0.00317 183 GLU A CD  
1428 O OE1 . GLU A 183 ? 0.31262 0.36134 0.29670 -0.06000 0.07239  -0.04557 183 GLU A OE1 
1429 O OE2 . GLU A 183 ? 0.26480 0.41181 0.20480 -0.01910 0.00011  -0.00449 183 GLU A OE2 
1430 N N   . MET A 184 ? 0.16618 0.23426 0.22066 0.00094  0.01414  -0.00625 184 MET A N   
1431 C CA  . MET A 184 ? 0.18397 0.24904 0.21209 -0.00144 0.01285  -0.02663 184 MET A CA  
1432 C C   . MET A 184 ? 0.25907 0.28358 0.21730 0.01183  -0.03972 -0.02173 184 MET A C   
1433 O O   . MET A 184 ? 0.25294 0.31423 0.25296 0.00015  -0.05824 -0.00203 184 MET A O   
1434 C CB  . MET A 184 ? 0.18039 0.29604 0.23431 0.02712  0.03648  0.00299  184 MET A CB  
1435 C CG  . MET A 184 ? 0.20149 0.36161 0.27151 0.06173  0.05857  -0.02201 184 MET A CG  
1436 S SD  . MET A 184 ? 0.35928 0.45063 0.37575 0.06141  0.07793  -0.01538 184 MET A SD  
1437 C CE  . MET A 184 ? 0.32986 0.39540 0.39471 0.08963  0.02660  -0.00149 184 MET A CE  
1438 N N   . ALA A 185 ? 0.26785 0.28942 0.20422 0.01258  0.00937  0.00898  185 ALA A N   
1439 C CA  . ALA A 185 ? 0.27351 0.27880 0.18728 -0.00137 0.01929  0.04244  185 ALA A CA  
1440 C C   . ALA A 185 ? 0.26983 0.30625 0.20012 -0.00102 -0.00388 0.04341  185 ALA A C   
1441 O O   . ALA A 185 ? 0.36992 0.33761 0.23062 -0.04528 -0.02800 0.03773  185 ALA A O   
1442 C CB  . ALA A 185 ? 0.29182 0.28439 0.21146 -0.00522 -0.01485 0.06940  185 ALA A CB  
1443 N N   . SER A 186 ? 0.32701 0.33614 0.18738 0.03386  0.03187  0.02302  186 SER A N   
1444 C CA  A SER A 186 ? 0.34676 0.33260 0.21222 0.03116  0.05305  -0.00689 186 SER A CA  
1445 C CA  B SER A 186 ? 0.30824 0.33963 0.19524 0.01841  0.01945  0.02455  186 SER A CA  
1446 C C   . SER A 186 ? 0.33452 0.34138 0.22986 0.02895  0.01528  0.00539  186 SER A C   
1447 O O   . SER A 186 ? 0.32292 0.36507 0.24336 0.05190  0.01948  0.02010  186 SER A O   
1448 C CB  A SER A 186 ? 0.36038 0.32964 0.24431 0.05281  0.07179  0.00251  186 SER A CB  
1449 C CB  B SER A 186 ? 0.25817 0.34437 0.17850 0.00023  -0.00222 0.06103  186 SER A CB  
1450 O OG  A SER A 186 ? 0.37636 0.31691 0.29859 0.10690  0.06412  -0.00077 186 SER A OG  
1451 O OG  B SER A 186 ? 0.20992 0.36297 0.17431 -0.00550 -0.04690 0.07989  186 SER A OG  
1452 N N   . ILE A 187 ? 0.28234 0.33583 0.23432 0.00193  0.05003  -0.01070 187 ILE A N   
1453 C CA  A ILE A 187 ? 0.30117 0.35882 0.24542 -0.02290 0.02203  -0.02396 187 ILE A CA  
1454 C CA  B ILE A 187 ? 0.29515 0.36329 0.26393 -0.02163 0.06271  -0.02249 187 ILE A CA  
1455 C C   . ILE A 187 ? 0.33936 0.38825 0.27502 -0.00313 0.06041  -0.04429 187 ILE A C   
1456 O O   . ILE A 187 ? 0.41479 0.39559 0.31152 0.02920  0.08851  -0.07673 187 ILE A O   
1457 C CB  A ILE A 187 ? 0.36163 0.32378 0.24188 -0.03273 -0.01632 -0.01979 187 ILE A CB  
1458 C CB  B ILE A 187 ? 0.29218 0.35008 0.29087 -0.04560 0.08414  -0.01376 187 ILE A CB  
1459 C CG1 A ILE A 187 ? 0.36679 0.30390 0.22079 -0.05766 -0.00446 -0.03883 187 ILE A CG1 
1460 C CG1 B ILE A 187 ? 0.30096 0.34765 0.29541 -0.02463 0.09240  -0.01813 187 ILE A CG1 
1461 C CG2 A ILE A 187 ? 0.38969 0.31208 0.22397 0.02944  -0.05697 -0.00298 187 ILE A CG2 
1462 C CG2 B ILE A 187 ? 0.25893 0.34265 0.30112 -0.07493 0.09227  -0.00336 187 ILE A CG2 
1463 C CD1 A ILE A 187 ? 0.39037 0.30471 0.21398 -0.09481 0.02579  -0.01006 187 ILE A CD1 
1464 C CD1 B ILE A 187 ? 0.32036 0.35273 0.31017 -0.00639 0.08692  -0.02489 187 ILE A CD1 
1465 N N   . ASN A 188 ? 0.28380 0.40322 0.29283 0.03161  0.02934  -0.08659 188 ASN A N   
1466 C CA  . ASN A 188 ? 0.38001 0.40972 0.32768 0.00076  0.04637  -0.11907 188 ASN A CA  
1467 C C   . ASN A 188 ? 0.38628 0.42847 0.31446 0.00585  0.08592  -0.10391 188 ASN A C   
1468 O O   . ASN A 188 ? 0.39385 0.44952 0.32348 -0.00089 0.08531  -0.08988 188 ASN A O   
1469 C CB  . ASN A 188 ? 0.38330 0.42485 0.37180 -0.00232 0.03655  -0.07709 188 ASN A CB  
1470 C CG  . ASN A 188 ? 0.37726 0.40597 0.36608 0.00927  0.03103  -0.06828 188 ASN A CG  
1471 O OD1 . ASN A 188 ? 0.39384 0.35763 0.36779 0.00308  0.00685  -0.03066 188 ASN A OD1 
1472 N ND2 . ASN A 188 ? 0.29556 0.44911 0.37610 -0.03523 -0.00188 -0.07466 188 ASN A ND2 
1473 N N   . ASN A 189 ? 0.40831 0.40635 0.29789 -0.02575 0.09633  -0.11657 189 ASN A N   
1474 C CA  . ASN A 189 ? 0.46578 0.44874 0.28605 0.03030  0.07355  -0.09856 189 ASN A CA  
1475 C C   . ASN A 189 ? 0.54680 0.47165 0.33129 0.03458  0.10621  -0.05186 189 ASN A C   
1476 O O   . ASN A 189 ? 0.58280 0.55008 0.37934 0.04629  0.11604  -0.01973 189 ASN A O   
1477 C CB  . ASN A 189 ? 0.45291 0.50131 0.26914 0.05711  0.01613  -0.09449 189 ASN A CB  
1478 C CG  . ASN A 189 ? 0.47746 0.53852 0.29118 0.04202  -0.02047 -0.11360 189 ASN A CG  
1479 O OD1 . ASN A 189 ? 0.51562 0.51090 0.31144 0.05710  -0.05026 -0.11901 189 ASN A OD1 
1480 N ND2 . ASN A 189 ? 0.47893 0.59882 0.29392 0.03447  -0.00824 -0.10352 189 ASN A ND2 
1481 N N   . ARG A 190 ? 0.64738 0.48461 0.33955 0.06314  0.11535  -0.04548 190 ARG A N   
1482 C CA  . ARG A 190 ? 0.78508 0.51496 0.36097 0.08135  0.11382  -0.04398 190 ARG A CA  
1483 C C   . ARG A 190 ? 0.83582 0.52583 0.36291 0.11022  0.08637  -0.05073 190 ARG A C   
1484 O O   . ARG A 190 ? 0.90147 0.55503 0.40817 0.09034  0.09496  -0.01493 190 ARG A O   
1485 C CB  . ARG A 190 ? 0.80115 0.51741 0.38847 0.10211  0.16331  -0.05410 190 ARG A CB  
1486 C CG  . ARG A 190 ? 0.84490 0.55799 0.42553 0.06299  0.16252  -0.05952 190 ARG A CG  
1487 C CD  . ARG A 190 ? 0.86674 0.57493 0.45888 0.06202  0.17614  -0.08545 190 ARG A CD  
1488 N NE  . ARG A 190 ? 0.88206 0.60236 0.48769 0.04703  0.18719  -0.09551 190 ARG A NE  
1489 C CZ  . ARG A 190 ? 0.91134 0.63644 0.51879 0.01448  0.18243  -0.09839 190 ARG A CZ  
1490 N NH1 . ARG A 190 ? 0.92674 0.65207 0.52709 -0.00248 0.16629  -0.09753 190 ARG A NH1 
1491 N NH2 . ARG A 190 ? 0.92016 0.64896 0.52819 0.01356  0.19823  -0.10004 190 ARG A NH2 
1492 N N   . VAL A 191 ? 0.83091 0.52838 0.35015 0.10365  0.01177  -0.05219 191 VAL A N   
1493 C CA  . VAL A 191 ? 0.79421 0.52245 0.33155 0.09105  -0.04861 -0.08474 191 VAL A CA  
1494 C C   . VAL A 191 ? 0.74693 0.52030 0.31836 0.07457  -0.07690 -0.06999 191 VAL A C   
1495 O O   . VAL A 191 ? 0.79217 0.55434 0.29267 0.07977  -0.13392 -0.05510 191 VAL A O   
1496 C CB  . VAL A 191 ? 0.79651 0.52181 0.36363 0.10784  -0.02869 -0.10184 191 VAL A CB  
1497 C CG1 . VAL A 191 ? 0.80876 0.53220 0.39559 0.09880  -0.01385 -0.08898 191 VAL A CG1 
1498 C CG2 . VAL A 191 ? 0.79109 0.52604 0.35829 0.11411  -0.00052 -0.12242 191 VAL A CG2 
1499 N N   . TYR A 192 ? 0.62612 0.48257 0.31913 0.01719  -0.09445 -0.10068 192 TYR A N   
1500 C CA  . TYR A 192 ? 0.51391 0.44015 0.33497 -0.01945 -0.05774 -0.12401 192 TYR A CA  
1501 C C   . TYR A 192 ? 0.44123 0.44010 0.32970 0.00280  -0.05784 -0.12351 192 TYR A C   
1502 O O   . TYR A 192 ? 0.43353 0.42926 0.37350 0.00092  -0.04804 -0.12178 192 TYR A O   
1503 C CB  . TYR A 192 ? 0.51289 0.45958 0.37265 -0.01393 -0.09822 -0.07370 192 TYR A CB  
1504 C CG  . TYR A 192 ? 0.50220 0.48520 0.41319 -0.04433 -0.14504 -0.05251 192 TYR A CG  
1505 C CD1 . TYR A 192 ? 0.50889 0.48933 0.43159 -0.04389 -0.19257 -0.01479 192 TYR A CD1 
1506 C CD2 . TYR A 192 ? 0.49822 0.50168 0.43159 -0.03410 -0.16299 -0.03107 192 TYR A CD2 
1507 C CE1 . TYR A 192 ? 0.50089 0.51497 0.46959 -0.05669 -0.20746 0.00702  192 TYR A CE1 
1508 C CE2 . TYR A 192 ? 0.51949 0.53719 0.45909 -0.02777 -0.17169 0.00798  192 TYR A CE2 
1509 C CZ  . TYR A 192 ? 0.50619 0.54769 0.47929 -0.04220 -0.20584 0.01440  192 TYR A CZ  
1510 O OH  . TYR A 192 ? 0.54049 0.57759 0.51809 -0.01192 -0.21545 0.04886  192 TYR A OH  
1511 N N   . ARG A 193 ? 0.40933 0.44308 0.30091 -0.02748 -0.05789 -0.10196 193 ARG A N   
1512 C CA  . ARG A 193 ? 0.34821 0.44188 0.32644 -0.01047 -0.00266 -0.10336 193 ARG A CA  
1513 C C   . ARG A 193 ? 0.36716 0.38599 0.27935 -0.00981 -0.06757 -0.06667 193 ARG A C   
1514 O O   . ARG A 193 ? 0.48067 0.40773 0.26147 0.02478  -0.08446 -0.05664 193 ARG A O   
1515 C CB  . ARG A 193 ? 0.41932 0.53615 0.42318 -0.01957 0.02385  -0.06990 193 ARG A CB  
1516 C CG  . ARG A 193 ? 0.45336 0.59219 0.49387 0.00699  0.06503  -0.05302 193 ARG A CG  
1517 C CD  . ARG A 193 ? 0.48656 0.63382 0.55240 0.01759  0.09036  -0.02852 193 ARG A CD  
1518 N NE  . ARG A 193 ? 0.51511 0.66095 0.59211 0.01823  0.09165  -0.01514 193 ARG A NE  
1519 C CZ  . ARG A 193 ? 0.55699 0.67716 0.61551 0.00266  0.07182  0.00532  193 ARG A CZ  
1520 N NH1 . ARG A 193 ? 0.56581 0.68471 0.62565 -0.00912 0.05932  0.00524  193 ARG A NH1 
1521 N NH2 . ARG A 193 ? 0.55662 0.67919 0.62768 -0.00501 0.06870  0.01151  193 ARG A NH2 
1522 N N   . THR A 194 ? 0.27687 0.29535 0.22037 -0.02658 -0.02463 -0.02237 194 THR A N   
1523 C CA  . THR A 194 ? 0.25446 0.27994 0.22707 -0.01029 -0.02860 -0.01695 194 THR A CA  
1524 C C   . THR A 194 ? 0.22762 0.26026 0.20814 0.02270  -0.03355 -0.03333 194 THR A C   
1525 O O   . THR A 194 ? 0.27206 0.26120 0.22612 0.04236  -0.03024 -0.00853 194 THR A O   
1526 C CB  . THR A 194 ? 0.24389 0.35560 0.23637 -0.02317 -0.02666 0.00036  194 THR A CB  
1527 O OG1 . THR A 194 ? 0.25844 0.38496 0.25582 -0.04288 -0.01599 -0.00546 194 THR A OG1 
1528 C CG2 . THR A 194 ? 0.28055 0.42696 0.27186 -0.05956 -0.00906 -0.01656 194 THR A CG2 
1529 N N   . ILE A 195 ? 0.23686 0.25925 0.19734 -0.01342 -0.03940 -0.00570 195 ILE A N   
1530 C CA  . ILE A 195 ? 0.23975 0.27761 0.19295 -0.02494 -0.05816 0.00059  195 ILE A CA  
1531 C C   . ILE A 195 ? 0.27266 0.28588 0.19325 0.01576  -0.02781 0.00453  195 ILE A C   
1532 O O   . ILE A 195 ? 0.25392 0.29883 0.20748 0.02468  -0.00504 0.00870  195 ILE A O   
1533 C CB  . ILE A 195 ? 0.24068 0.26138 0.19830 -0.00667 0.00250  0.00658  195 ILE A CB  
1534 C CG1 . ILE A 195 ? 0.22780 0.30475 0.18996 -0.03106 0.03096  0.00756  195 ILE A CG1 
1535 C CG2 . ILE A 195 ? 0.23253 0.26543 0.19988 -0.01331 0.01130  0.00069  195 ILE A CG2 
1536 C CD1 . ILE A 195 ? 0.27871 0.35750 0.19202 -0.00561 0.02072  -0.01356 195 ILE A CD1 
1537 N N   . GLY A 196 ? 0.27129 0.26162 0.18141 0.00624  -0.01667 0.00410  196 GLY A N   
1538 C CA  . GLY A 196 ? 0.29852 0.28481 0.17920 -0.01470 -0.02957 0.01600  196 GLY A CA  
1539 C C   . GLY A 196 ? 0.26424 0.33389 0.19083 -0.00591 -0.00448 0.01434  196 GLY A C   
1540 O O   . GLY A 196 ? 0.24458 0.35950 0.22384 -0.00666 0.03895  0.01625  196 GLY A O   
1541 N N   . SER A 197 ? 0.20639 0.29416 0.20183 0.02522  -0.01981 -0.00590 197 SER A N   
1542 C CA  . SER A 197 ? 0.20704 0.27485 0.20657 0.02710  0.00066  -0.02258 197 SER A CA  
1543 C C   . SER A 197 ? 0.18246 0.25134 0.18551 0.01671  -0.00585 -0.00142 197 SER A C   
1544 O O   . SER A 197 ? 0.21406 0.27715 0.18300 0.01981  -0.01144 -0.00096 197 SER A O   
1545 C CB  . SER A 197 ? 0.16522 0.26077 0.22549 -0.02891 0.00851  -0.01185 197 SER A CB  
1546 O OG  . SER A 197 ? 0.18613 0.29536 0.21828 0.01614  0.01988  -0.01636 197 SER A OG  
1547 N N   . PRO A 198 ? 0.22363 0.24099 0.17311 0.03155  0.00681  -0.00854 198 PRO A N   
1548 C CA  . PRO A 198 ? 0.25259 0.20749 0.17587 -0.01837 -0.00585 -0.00999 198 PRO A CA  
1549 C C   . PRO A 198 ? 0.23060 0.22292 0.17881 -0.01763 -0.00376 0.01060  198 PRO A C   
1550 O O   . PRO A 198 ? 0.22243 0.23010 0.19359 -0.00720 -0.00874 0.02059  198 PRO A O   
1551 C CB  . PRO A 198 ? 0.25233 0.27716 0.17992 0.01090  -0.02090 0.01402  198 PRO A CB  
1552 C CG  . PRO A 198 ? 0.30367 0.29358 0.18086 0.04403  0.00618  0.01156  198 PRO A CG  
1553 C CD  . PRO A 198 ? 0.24889 0.26779 0.16497 0.05286  0.00826  -0.00806 198 PRO A CD  
1554 N N   . LEU A 199 ? 0.23492 0.22552 0.17418 -0.00346 -0.00286 0.02847  199 LEU A N   
1555 C CA  . LEU A 199 ? 0.23208 0.23001 0.18918 -0.00781 -0.00609 0.00398  199 LEU A CA  
1556 C C   . LEU A 199 ? 0.19639 0.22598 0.21070 -0.05133 -0.01790 -0.00893 199 LEU A C   
1557 O O   . LEU A 199 ? 0.22806 0.21694 0.22647 -0.02436 0.02884  0.02400  199 LEU A O   
1558 C CB  . LEU A 199 ? 0.18982 0.24291 0.19305 0.00587  -0.00936 -0.00036 199 LEU A CB  
1559 C CG  . LEU A 199 ? 0.19859 0.25728 0.19879 0.01387  0.01290  -0.00913 199 LEU A CG  
1560 C CD1 . LEU A 199 ? 0.25582 0.28559 0.22140 0.02703  -0.03228 -0.00146 199 LEU A CD1 
1561 C CD2 . LEU A 199 ? 0.22180 0.30199 0.23172 0.04618  0.03442  -0.00925 199 LEU A CD2 
1562 N N   . VAL A 200 ? 0.18685 0.22463 0.21281 -0.01684 -0.02740 -0.00148 200 VAL A N   
1563 C CA  . VAL A 200 ? 0.23782 0.19923 0.21740 -0.01443 0.00587  -0.03123 200 VAL A CA  
1564 C C   . VAL A 200 ? 0.23193 0.22316 0.22100 0.01416  0.00865  0.00657  200 VAL A C   
1565 O O   . VAL A 200 ? 0.25808 0.24399 0.23195 -0.00442 0.02453  0.02161  200 VAL A O   
1566 C CB  . VAL A 200 ? 0.23114 0.19645 0.23378 -0.01430 0.01272  -0.01251 200 VAL A CB  
1567 C CG1 . VAL A 200 ? 0.26480 0.20198 0.24090 -0.03370 0.02050  -0.02049 200 VAL A CG1 
1568 C CG2 . VAL A 200 ? 0.23797 0.22187 0.24372 -0.02905 0.02747  0.03903  200 VAL A CG2 
1569 N N   . PHE A 201 ? 0.23030 0.21492 0.21890 0.01052  0.01362  0.04115  201 PHE A N   
1570 C CA  . PHE A 201 ? 0.24934 0.24261 0.22764 0.03745  -0.01189 0.01541  201 PHE A CA  
1571 C C   . PHE A 201 ? 0.26397 0.24152 0.20788 0.04044  0.02390  0.01144  201 PHE A C   
1572 O O   . PHE A 201 ? 0.32260 0.25279 0.21019 0.04296  0.03856  0.00794  201 PHE A O   
1573 C CB  . PHE A 201 ? 0.22531 0.24882 0.21200 0.04062  -0.00422 -0.01329 201 PHE A CB  
1574 C CG  . PHE A 201 ? 0.24262 0.26059 0.20840 0.04840  0.02903  -0.01225 201 PHE A CG  
1575 C CD1 . PHE A 201 ? 0.26907 0.30192 0.20447 0.00446  0.01344  0.00129  201 PHE A CD1 
1576 C CD2 . PHE A 201 ? 0.25731 0.26946 0.22648 0.06399  0.01535  0.00063  201 PHE A CD2 
1577 C CE1 . PHE A 201 ? 0.28919 0.25153 0.22981 0.01885  0.01923  0.01668  201 PHE A CE1 
1578 C CE2 . PHE A 201 ? 0.24171 0.24334 0.22241 0.04376  -0.02110 0.01483  201 PHE A CE2 
1579 C CZ  . PHE A 201 ? 0.27699 0.26379 0.22798 -0.00979 0.00663  0.05027  201 PHE A CZ  
1580 N N   . PRO A 202 ? 0.26966 0.25590 0.24217 0.00879  0.01541  0.03280  202 PRO A N   
1581 C CA  . PRO A 202 ? 0.28772 0.28062 0.27692 0.01574  0.04248  0.01939  202 PRO A CA  
1582 C C   . PRO A 202 ? 0.32933 0.26739 0.27902 0.03184  0.00150  0.01487  202 PRO A C   
1583 O O   . PRO A 202 ? 0.34466 0.24614 0.24296 0.03075  -0.00922 0.02248  202 PRO A O   
1584 C CB  . PRO A 202 ? 0.30642 0.27550 0.26329 0.01050  0.01855  0.05027  202 PRO A CB  
1585 C CG  . PRO A 202 ? 0.32112 0.24124 0.25319 0.01577  0.02005  0.06679  202 PRO A CG  
1586 C CD  . PRO A 202 ? 0.29786 0.23124 0.23055 0.00966  0.04852  0.05092  202 PRO A CD  
1587 N N   . LYS A 203 ? 0.35346 0.26538 0.31299 0.05076  -0.00595 -0.02713 203 LYS A N   
1588 C CA  . LYS A 203 ? 0.38513 0.26681 0.34624 0.08328  -0.01138 -0.06984 203 LYS A CA  
1589 C C   . LYS A 203 ? 0.36285 0.27920 0.36673 0.04074  0.02640  0.01433  203 LYS A C   
1590 O O   . LYS A 203 ? 0.38772 0.24047 0.40783 -0.00554 0.02997  0.03220  203 LYS A O   
1591 C CB  . LYS A 203 ? 0.45469 0.31267 0.41594 0.08545  -0.02184 -0.10773 203 LYS A CB  
1592 C CG  . LYS A 203 ? 0.56127 0.37449 0.45458 0.03763  -0.01641 -0.11487 203 LYS A CG  
1593 C CD  . LYS A 203 ? 0.58391 0.37001 0.47929 0.06367  -0.00850 -0.14552 203 LYS A CD  
1594 C CE  . LYS A 203 ? 0.59712 0.41434 0.52119 0.02453  -0.01800 -0.11240 203 LYS A CE  
1595 N NZ  . LYS A 203 ? 0.62370 0.44549 0.54349 0.02068  -0.00953 -0.09037 203 LYS A NZ  
1596 N N   . HIS A 204 ? 0.34061 0.27821 0.36196 0.06927  0.00995  0.04440  204 HIS A N   
1597 C CA  . HIS A 204 ? 0.37911 0.26529 0.35441 0.05837  0.02084  0.05375  204 HIS A CA  
1598 C C   . HIS A 204 ? 0.42592 0.28269 0.30619 0.05762  -0.00478 0.04118  204 HIS A C   
1599 O O   . HIS A 204 ? 0.53554 0.31331 0.30633 0.08778  -0.05305 0.03933  204 HIS A O   
1600 C CB  . HIS A 204 ? 0.44144 0.27980 0.40060 0.04883  0.04951  0.05003  204 HIS A CB  
1601 C CG  . HIS A 204 ? 0.51491 0.31741 0.44528 0.04772  0.02741  0.03447  204 HIS A CG  
1602 N ND1 . HIS A 204 ? 0.59276 0.35981 0.46199 0.05761  0.01609  0.02300  204 HIS A ND1 
1603 C CD2 . HIS A 204 ? 0.55738 0.33485 0.46662 0.05217  0.01515  0.01848  204 HIS A CD2 
1604 C CE1 . HIS A 204 ? 0.59893 0.37275 0.47457 0.03981  0.00584  0.00134  204 HIS A CE1 
1605 N NE2 . HIS A 204 ? 0.60533 0.35946 0.47466 0.04788  -0.00767 0.00218  204 HIS A NE2 
1606 N N   . HIS A 205 ? 0.39936 0.27414 0.25162 0.02831  0.00478  0.02309  205 HIS A N   
1607 C CA  . HIS A 205 ? 0.30501 0.28949 0.23974 0.04302  -0.03254 -0.00912 205 HIS A CA  
1608 C C   . HIS A 205 ? 0.32716 0.34541 0.22830 0.03437  -0.00694 0.02286  205 HIS A C   
1609 O O   . HIS A 205 ? 0.35281 0.42994 0.21806 0.02183  0.03710  0.02235  205 HIS A O   
1610 C CB  . HIS A 205 ? 0.30087 0.30572 0.25492 0.03955  -0.02503 0.02353  205 HIS A CB  
1611 C CG  . HIS A 205 ? 0.26250 0.34671 0.29842 0.03388  -0.01361 0.03217  205 HIS A CG  
1612 N ND1 . HIS A 205 ? 0.28287 0.36765 0.30558 0.00184  0.01070  0.02152  205 HIS A ND1 
1613 C CD2 . HIS A 205 ? 0.32832 0.37319 0.35165 0.03281  0.02102  0.04915  205 HIS A CD2 
1614 C CE1 . HIS A 205 ? 0.36331 0.37002 0.33662 0.01998  0.02377  0.01372  205 HIS A CE1 
1615 N NE2 . HIS A 205 ? 0.32989 0.38500 0.36231 0.05116  0.02971  0.04992  205 HIS A NE2 
1616 N N   . VAL A 206 ? 0.31960 0.32792 0.24506 0.03666  -0.03020 0.04064  206 VAL A N   
1617 C CA  . VAL A 206 ? 0.33631 0.31591 0.25269 0.04046  -0.00610 0.02989  206 VAL A CA  
1618 C C   . VAL A 206 ? 0.35218 0.30748 0.23714 0.03016  0.01751  0.00445  206 VAL A C   
1619 O O   . VAL A 206 ? 0.40907 0.35293 0.25839 0.01837  0.03673  -0.01215 206 VAL A O   
1620 C CB  . VAL A 206 ? 0.36076 0.33301 0.31294 0.04304  -0.02195 0.01965  206 VAL A CB  
1621 C CG1 . VAL A 206 ? 0.32700 0.36417 0.34798 0.00559  -0.01787 0.01930  206 VAL A CG1 
1622 C CG2 . VAL A 206 ? 0.42224 0.32668 0.31357 0.03962  -0.03611 -0.01670 206 VAL A CG2 
1623 N N   . VAL A 207 ? 0.29021 0.28112 0.23354 0.06241  0.00512  0.01230  207 VAL A N   
1624 C CA  . VAL A 207 ? 0.26139 0.29636 0.21900 0.07078  -0.01035 0.00086  207 VAL A CA  
1625 C C   . VAL A 207 ? 0.24106 0.30651 0.20813 0.06087  -0.02623 -0.00498 207 VAL A C   
1626 O O   . VAL A 207 ? 0.27851 0.34371 0.22589 0.04936  0.01457  -0.01173 207 VAL A O   
1627 C CB  . VAL A 207 ? 0.27603 0.35851 0.21799 0.08675  -0.01421 -0.00288 207 VAL A CB  
1628 C CG1 . VAL A 207 ? 0.34923 0.34826 0.22845 0.10371  0.03209  0.00583  207 VAL A CG1 
1629 C CG2 . VAL A 207 ? 0.26637 0.43512 0.22817 0.04938  -0.02479 -0.02951 207 VAL A CG2 
1630 N N   . SER A 208 ? 0.26610 0.29839 0.23256 0.06443  -0.03127 0.00382  208 SER A N   
1631 C CA  . SER A 208 ? 0.27357 0.27902 0.27127 0.00637  -0.03535 0.02528  208 SER A CA  
1632 C C   . SER A 208 ? 0.27002 0.29470 0.28055 0.02433  0.02297  0.01860  208 SER A C   
1633 O O   . SER A 208 ? 0.26096 0.32527 0.31360 0.00773  0.04048  -0.00197 208 SER A O   
1634 C CB  . SER A 208 ? 0.26431 0.31887 0.32755 0.00662  -0.09585 0.04265  208 SER A CB  
1635 O OG  . SER A 208 ? 0.36759 0.38529 0.35829 -0.00467 -0.08876 0.03580  208 SER A OG  
1636 N N   . LEU A 209 ? 0.24746 0.29358 0.27502 0.00712  0.00186  0.04323  209 LEU A N   
1637 C CA  . LEU A 209 ? 0.28239 0.33844 0.29103 0.02137  -0.01634 0.04428  209 LEU A CA  
1638 C C   . LEU A 209 ? 0.25136 0.38820 0.33050 0.06780  -0.02384 0.01773  209 LEU A C   
1639 O O   . LEU A 209 ? 0.27312 0.43184 0.37491 0.05260  0.00078  -0.00102 209 LEU A O   
1640 C CB  . LEU A 209 ? 0.25242 0.36552 0.26146 0.03692  0.00563  0.06819  209 LEU A CB  
1641 C CG  . LEU A 209 ? 0.27225 0.38553 0.24873 0.04188  0.02027  0.07052  209 LEU A CG  
1642 C CD1 . LEU A 209 ? 0.33951 0.37170 0.26512 0.03591  0.04279  0.07366  209 LEU A CD1 
1643 C CD2 . LEU A 209 ? 0.25833 0.40611 0.26016 0.06380  0.00924  0.04177  209 LEU A CD2 
1644 N N   . GLN A 210 ? 0.25642 0.40115 0.33864 0.05731  -0.06903 -0.01397 210 GLN A N   
1645 C CA  . GLN A 210 ? 0.29043 0.41755 0.33886 0.07296  -0.06797 0.02217  210 GLN A CA  
1646 C C   . GLN A 210 ? 0.27993 0.40849 0.32806 0.06638  -0.06432 0.00216  210 GLN A C   
1647 O O   . GLN A 210 ? 0.25760 0.37123 0.35357 0.06300  -0.07034 0.00340  210 GLN A O   
1648 C CB  . GLN A 210 ? 0.34587 0.44890 0.37099 0.05510  -0.09825 0.04674  210 GLN A CB  
1649 C CG  . GLN A 210 ? 0.37847 0.47034 0.39057 0.02632  -0.09602 0.05062  210 GLN A CG  
1650 C CD  . GLN A 210 ? 0.39449 0.51079 0.41170 0.02424  -0.11634 0.06566  210 GLN A CD  
1651 O OE1 . GLN A 210 ? 0.42879 0.51949 0.37581 0.01966  -0.12211 0.06340  210 GLN A OE1 
1652 N NE2 . GLN A 210 ? 0.40009 0.53636 0.43319 0.05053  -0.12574 0.07230  210 GLN A NE2 
1653 N N   . PRO A 211 ? 0.31346 0.41510 0.34630 0.07020  -0.01862 -0.03125 211 PRO A N   
1654 C CA  . PRO A 211 ? 0.34118 0.42419 0.36018 0.05009  -0.01199 -0.05569 211 PRO A CA  
1655 C C   . PRO A 211 ? 0.36246 0.43766 0.34463 0.03199  -0.03711 -0.03369 211 PRO A C   
1656 O O   . PRO A 211 ? 0.34619 0.43273 0.35493 0.04441  -0.05121 0.01024  211 PRO A O   
1657 C CB  . PRO A 211 ? 0.33327 0.43126 0.40327 0.02856  0.01599  -0.08249 211 PRO A CB  
1658 C CG  . PRO A 211 ? 0.39068 0.45510 0.42551 0.01320  0.03464  -0.07139 211 PRO A CG  
1659 C CD  . PRO A 211 ? 0.36889 0.45651 0.39596 0.03135  0.03059  -0.05252 211 PRO A CD  
1660 N N   . VAL A 212 ? 0.40387 0.45757 0.33717 0.03809  -0.06981 -0.04694 212 VAL A N   
1661 C CA  . VAL A 212 ? 0.44115 0.46701 0.35216 0.01100  -0.09582 -0.07528 212 VAL A CA  
1662 C C   . VAL A 212 ? 0.50501 0.53028 0.37717 0.01747  -0.09604 -0.06264 212 VAL A C   
1663 O O   . VAL A 212 ? 0.55999 0.57870 0.37123 0.03105  -0.12019 -0.03933 212 VAL A O   
1664 C CB  . VAL A 212 ? 0.45989 0.42916 0.36405 0.01365  -0.08283 -0.07306 212 VAL A CB  
1665 C CG1 . VAL A 212 ? 0.45861 0.41980 0.37780 -0.00247 -0.08053 -0.08621 212 VAL A CG1 
1666 C CG2 . VAL A 212 ? 0.48964 0.40991 0.34745 0.01394  -0.08316 -0.06024 212 VAL A CG2 
1667 N N   . ASN A 213 ? 0.47900 0.54891 0.40082 0.02238  -0.08894 -0.06061 213 ASN A N   
1668 C CA  . ASN A 213 ? 0.52225 0.60205 0.44154 0.01423  -0.07230 -0.05543 213 ASN A CA  
1669 C C   . ASN A 213 ? 0.47498 0.60742 0.43138 0.01954  -0.07349 -0.05005 213 ASN A C   
1670 O O   . ASN A 213 ? 0.52846 0.62318 0.42937 0.00708  -0.05265 -0.05308 213 ASN A O   
1671 C CB  . ASN A 213 ? 0.60802 0.64356 0.48089 0.01727  -0.03770 -0.06548 213 ASN A CB  
1672 C CG  . ASN A 213 ? 0.71699 0.68970 0.53029 0.02812  -0.04571 -0.06817 213 ASN A CG  
1673 O OD1 . ASN A 213 ? 0.76459 0.71405 0.55629 0.01787  -0.03083 -0.07213 213 ASN A OD1 
1674 N ND2 . ASN A 213 ? 0.75479 0.69515 0.54389 0.03002  -0.03213 -0.06721 213 ASN A ND2 
1675 N N   . ASP A 214 ? 0.43744 0.61028 0.44024 -0.00831 -0.09633 -0.02691 214 ASP A N   
1676 C CA  . ASP A 214 ? 0.42471 0.60032 0.43977 0.00802  -0.08638 -0.01613 214 ASP A CA  
1677 C C   . ASP A 214 ? 0.37774 0.60042 0.41520 0.01077  -0.07597 -0.01443 214 ASP A C   
1678 O O   . ASP A 214 ? 0.32625 0.60735 0.41508 -0.01257 -0.06601 -0.00823 214 ASP A O   
1679 C CB  . ASP A 214 ? 0.48084 0.58704 0.45638 0.04299  -0.10456 0.03375  214 ASP A CB  
1680 C CG  . ASP A 214 ? 0.51929 0.59571 0.52279 0.03361  -0.09882 0.04589  214 ASP A CG  
1681 O OD1 . ASP A 214 ? 0.52699 0.58784 0.54029 0.05585  -0.08229 0.05331  214 ASP A OD1 
1682 O OD2 . ASP A 214 ? 0.57409 0.61032 0.56639 0.00744  -0.09053 0.04121  214 ASP A OD2 
1683 N N   . LYS A 215 ? 0.41104 0.60033 0.37337 0.00964  -0.06786 -0.00518 215 LYS A N   
1684 C CA  . LYS A 215 ? 0.39752 0.60131 0.36841 0.02965  -0.06756 -0.00020 215 LYS A CA  
1685 C C   . LYS A 215 ? 0.36014 0.57675 0.36993 0.00963  -0.08319 -0.02845 215 LYS A C   
1686 O O   . LYS A 215 ? 0.38291 0.58616 0.37707 0.01800  -0.08589 -0.03016 215 LYS A O   
1687 C CB  . LYS A 215 ? 0.44410 0.64265 0.37331 0.05300  -0.02491 0.00440  215 LYS A CB  
1688 C CG  . LYS A 215 ? 0.47784 0.65913 0.37508 0.06628  0.00338  -0.00494 215 LYS A CG  
1689 C CD  . LYS A 215 ? 0.58060 0.70376 0.38853 0.04292  0.02694  -0.01890 215 LYS A CD  
1690 C CE  . LYS A 215 ? 0.67009 0.73123 0.41399 0.02713  0.03649  -0.02378 215 LYS A CE  
1691 N NZ  . LYS A 215 ? 0.72739 0.75328 0.42469 0.02243  0.02921  -0.03612 215 LYS A NZ  
1692 N N   . ASP A 216 ? 0.33669 0.56336 0.36948 -0.01531 -0.08602 -0.02884 216 ASP A N   
1693 C CA  . ASP A 216 ? 0.34208 0.56996 0.36716 -0.01747 -0.11706 -0.04066 216 ASP A CA  
1694 C C   . ASP A 216 ? 0.30620 0.55837 0.35709 -0.01025 -0.07207 -0.05859 216 ASP A C   
1695 O O   . ASP A 216 ? 0.30291 0.57385 0.38618 -0.03986 -0.10273 -0.05380 216 ASP A O   
1696 C CB  . ASP A 216 ? 0.29136 0.57662 0.40155 -0.03368 -0.12126 -0.01098 216 ASP A CB  
1697 C CG  . ASP A 216 ? 0.35027 0.60889 0.46140 -0.02266 -0.10490 -0.00310 216 ASP A CG  
1698 O OD1 . ASP A 216 ? 0.36284 0.62711 0.44841 -0.01071 -0.11200 -0.00859 216 ASP A OD1 
1699 O OD2 . ASP A 216 ? 0.37827 0.63307 0.50083 -0.02320 -0.09043 -0.00720 216 ASP A OD2 
1700 N N   . PHE A 217 ? 0.26299 0.54734 0.32654 0.02961  -0.03923 -0.06700 217 PHE A N   
1701 C CA  . PHE A 217 ? 0.23385 0.53424 0.27590 0.01243  -0.04011 -0.07500 217 PHE A CA  
1702 C C   . PHE A 217 ? 0.20074 0.52602 0.28677 0.03499  -0.00962 -0.07470 217 PHE A C   
1703 O O   . PHE A 217 ? 0.19140 0.56266 0.32452 0.04434  -0.00806 -0.07103 217 PHE A O   
1704 C CB  . PHE A 217 ? 0.21872 0.55088 0.28839 0.01051  0.00414  -0.05205 217 PHE A CB  
1705 C CG  . PHE A 217 ? 0.25215 0.53596 0.28368 -0.00091 -0.02693 -0.00031 217 PHE A CG  
1706 C CD1 . PHE A 217 ? 0.22190 0.52654 0.29370 0.00342  0.00002  -0.00714 217 PHE A CD1 
1707 C CD2 . PHE A 217 ? 0.29107 0.55724 0.31492 -0.00014 -0.03052 0.00101  217 PHE A CD2 
1708 C CE1 . PHE A 217 ? 0.28977 0.53434 0.27975 -0.01913 -0.01546 0.01391  217 PHE A CE1 
1709 C CE2 . PHE A 217 ? 0.28752 0.54644 0.31689 -0.01448 -0.01697 0.00929  217 PHE A CE2 
1710 C CZ  . PHE A 217 ? 0.28944 0.53462 0.30246 -0.00341 -0.01728 0.00608  217 PHE A CZ  
1711 N N   . GLN A 218 ? 0.19829 0.49255 0.26469 0.02411  -0.02157 -0.06742 218 GLN A N   
1712 C CA  . GLN A 218 ? 0.19457 0.50204 0.24729 0.02200  -0.05046 -0.05062 218 GLN A CA  
1713 C C   . GLN A 218 ? 0.19470 0.47913 0.24627 0.04500  -0.00634 -0.06338 218 GLN A C   
1714 O O   . GLN A 218 ? 0.17479 0.49209 0.28016 0.04440  -0.00025 -0.08012 218 GLN A O   
1715 C CB  . GLN A 218 ? 0.25785 0.53138 0.27915 0.06513  -0.04778 -0.00643 218 GLN A CB  
1716 C CG  . GLN A 218 ? 0.31022 0.57583 0.32063 0.03252  -0.04466 0.00065  218 GLN A CG  
1717 C CD  . GLN A 218 ? 0.33608 0.60287 0.35083 -0.03402 -0.03118 0.00862  218 GLN A CD  
1718 O OE1 . GLN A 218 ? 0.41893 0.61847 0.37127 -0.04807 0.00359  0.00788  218 GLN A OE1 
1719 N NE2 . GLN A 218 ? 0.36789 0.60267 0.38882 -0.05707 -0.01988 0.01644  218 GLN A NE2 
1720 N N   . ILE A 219 ? 0.21490 0.48305 0.26229 0.02712  -0.01311 -0.06005 219 ILE A N   
1721 C CA  . ILE A 219 ? 0.23082 0.49657 0.26657 0.02627  -0.03431 -0.05871 219 ILE A CA  
1722 C C   . ILE A 219 ? 0.23491 0.53074 0.27021 -0.00383 0.00166  -0.09152 219 ILE A C   
1723 O O   . ILE A 219 ? 0.23073 0.57856 0.29165 0.00652  0.00611  -0.13115 219 ILE A O   
1724 C CB  . ILE A 219 ? 0.33078 0.48006 0.28969 0.04502  -0.05181 -0.04249 219 ILE A CB  
1725 C CG1 . ILE A 219 ? 0.38084 0.45770 0.27003 0.09159  -0.06347 0.00619  219 ILE A CG1 
1726 C CG2 . ILE A 219 ? 0.35526 0.49793 0.33008 0.04273  -0.07310 -0.06148 219 ILE A CG2 
1727 C CD1 . ILE A 219 ? 0.40752 0.46003 0.30062 0.10142  -0.01699 0.02143  219 ILE A CD1 
1728 N N   . SER A 220 ? 0.24689 0.52318 0.22303 -0.02121 0.01850  -0.05304 220 SER A N   
1729 C CA  A SER A 220 ? 0.22409 0.53479 0.24698 -0.04237 0.01586  -0.04642 220 SER A CA  
1730 C CA  B SER A 220 ? 0.25234 0.54194 0.24621 -0.03479 0.01551  -0.06807 220 SER A CA  
1731 C C   . SER A 220 ? 0.24864 0.52736 0.26321 -0.02793 0.04093  -0.06865 220 SER A C   
1732 O O   . SER A 220 ? 0.31743 0.56279 0.36084 -0.02090 0.11079  -0.09866 220 SER A O   
1733 C CB  A SER A 220 ? 0.26636 0.59184 0.27145 -0.07178 0.02949  -0.01906 220 SER A CB  
1734 C CB  B SER A 220 ? 0.31009 0.59235 0.26887 -0.05041 0.00999  -0.07701 220 SER A CB  
1735 O OG  A SER A 220 ? 0.20311 0.65329 0.26148 -0.07323 0.02465  -0.02673 220 SER A OG  
1736 O OG  B SER A 220 ? 0.30315 0.65329 0.28292 -0.07506 -0.00630 -0.08963 220 SER A OG  
1737 N N   . VAL A 221 ? 0.22310 0.46143 0.23164 0.05310  0.02043  -0.04496 221 VAL A N   
1738 C CA  . VAL A 221 ? 0.22967 0.41196 0.25927 0.00940  0.00196  -0.03686 221 VAL A CA  
1739 C C   . VAL A 221 ? 0.21764 0.39643 0.25591 0.00106  0.03561  -0.02894 221 VAL A C   
1740 O O   . VAL A 221 ? 0.22834 0.41494 0.27398 -0.01380 0.06747  -0.03594 221 VAL A O   
1741 C CB  . VAL A 221 ? 0.32394 0.40460 0.28248 0.01846  -0.01647 -0.01771 221 VAL A CB  
1742 C CG1 . VAL A 221 ? 0.34844 0.40717 0.32526 0.01276  0.02223  -0.01180 221 VAL A CG1 
1743 C CG2 . VAL A 221 ? 0.34583 0.42140 0.26853 0.01840  -0.03421 -0.02446 221 VAL A CG2 
1744 N N   . ASP A 222 ? 0.20446 0.33745 0.22711 0.01599  0.03582  -0.05552 222 ASP A N   
1745 C CA  . ASP A 222 ? 0.25865 0.35470 0.26767 0.02084  0.08126  -0.02355 222 ASP A CA  
1746 C C   . ASP A 222 ? 0.26849 0.42004 0.31411 0.00401  0.07036  0.01508  222 ASP A C   
1747 O O   . ASP A 222 ? 0.35576 0.39127 0.34393 0.04474  0.01330  -0.06732 222 ASP A O   
1748 C CB  . ASP A 222 ? 0.24400 0.33140 0.27760 0.03563  0.08462  -0.02415 222 ASP A CB  
1749 C CG  . ASP A 222 ? 0.23171 0.33783 0.25430 0.06562  0.05700  -0.02691 222 ASP A CG  
1750 O OD1 . ASP A 222 ? 0.22644 0.32980 0.21737 0.03350  0.02723  -0.03774 222 ASP A OD1 
1751 O OD2 . ASP A 222 ? 0.26185 0.35906 0.24896 0.05148  0.03920  0.00144  222 ASP A OD2 
1752 N N   . HIS A 223 ? 0.30461 0.48214 0.39292 -0.05324 0.02256  0.08517  223 HIS A N   
1753 C CA  A HIS A 223 ? 0.40990 0.53791 0.45280 -0.13497 -0.00771 0.09345  223 HIS A CA  
1754 C CA  B HIS A 223 ? 0.40254 0.53317 0.43883 -0.09325 0.00942  0.08890  223 HIS A CA  
1755 C C   . HIS A 223 ? 0.38125 0.56925 0.45603 -0.08471 0.01019  0.07655  223 HIS A C   
1756 O O   . HIS A 223 ? 0.43605 0.61908 0.52406 -0.08353 0.01338  0.06445  223 HIS A O   
1757 C CB  A HIS A 223 ? 0.56118 0.59275 0.50213 -0.12497 -0.09750 0.09790  223 HIS A CB  
1758 C CB  B HIS A 223 ? 0.50743 0.56380 0.48013 -0.09126 -0.02573 0.09469  223 HIS A CB  
1759 C CG  A HIS A 223 ? 0.67595 0.62366 0.51998 -0.11565 -0.14770 0.09309  223 HIS A CG  
1760 C CG  B HIS A 223 ? 0.62329 0.59628 0.51877 -0.09822 -0.04555 0.10082  223 HIS A CG  
1761 N ND1 A HIS A 223 ? 0.68820 0.62831 0.49221 -0.12038 -0.20702 0.09501  223 HIS A ND1 
1762 N ND1 B HIS A 223 ? 0.67609 0.61029 0.53440 -0.11595 -0.05548 0.10525  223 HIS A ND1 
1763 C CD2 A HIS A 223 ? 0.71324 0.62850 0.52632 -0.12123 -0.15041 0.09782  223 HIS A CD2 
1764 C CD2 B HIS A 223 ? 0.67859 0.60745 0.53079 -0.09940 -0.05430 0.09829  223 HIS A CD2 
1765 C CE1 A HIS A 223 ? 0.70712 0.62965 0.50660 -0.10742 -0.20695 0.07380  223 HIS A CE1 
1766 C CE1 B HIS A 223 ? 0.69986 0.61430 0.53851 -0.11787 -0.06697 0.09865  223 HIS A CE1 
1767 N NE2 A HIS A 223 ? 0.71810 0.62378 0.51998 -0.11577 -0.17507 0.08695  223 HIS A NE2 
1768 N NE2 B HIS A 223 ? 0.70419 0.60954 0.53583 -0.10853 -0.06726 0.09844  223 HIS A NE2 
1769 N N   . LEU A 224 ? 0.34497 0.59791 0.37486 -0.08161 0.02804  0.03307  224 LEU A N   
1770 C CA  . LEU A 224 ? 0.26370 0.61023 0.32927 -0.00948 0.01142  -0.03661 224 LEU A CA  
1771 C C   . LEU A 224 ? 0.28955 0.58685 0.33154 -0.02463 0.04108  -0.06155 224 LEU A C   
1772 O O   . LEU A 224 ? 0.41642 0.56287 0.33465 -0.06446 0.09647  -0.07425 224 LEU A O   
1773 C CB  . LEU A 224 ? 0.33737 0.63988 0.37292 0.01806  -0.02227 -0.05785 224 LEU A CB  
1774 C CG  . LEU A 224 ? 0.46610 0.67006 0.45738 0.03183  -0.01626 -0.04183 224 LEU A CG  
1775 C CD1 . LEU A 224 ? 0.50826 0.70461 0.46608 0.02662  0.01525  -0.03905 224 LEU A CD1 
1776 C CD2 . LEU A 224 ? 0.51858 0.67739 0.50050 0.05346  -0.04308 -0.04111 224 LEU A CD2 
1777 N N   . SER A 225 ? 0.28064 0.60599 0.33767 -0.00939 0.04481  -0.04171 225 SER A N   
1778 C CA  . SER A 225 ? 0.29951 0.64184 0.38300 0.05015  0.02745  -0.05422 225 SER A CA  
1779 C C   . SER A 225 ? 0.20978 0.68471 0.38209 0.02611  0.05054  -0.07792 225 SER A C   
1780 O O   . SER A 225 ? 0.25868 0.72329 0.40362 -0.04403 0.04896  -0.08810 225 SER A O   
1781 C CB  . SER A 225 ? 0.41723 0.65270 0.42938 0.07085  0.01585  -0.06312 225 SER A CB  
1782 O OG  . SER A 225 ? 0.44907 0.64973 0.46454 0.12507  0.00480  -0.05997 225 SER A OG  
1783 N N   . ILE A 226 ? 0.20543 0.67584 0.40055 0.02512  0.00143  -0.09723 226 ILE A N   
1784 C CA  . ILE A 226 ? 0.28782 0.65955 0.41777 0.07473  -0.02432 -0.13395 226 ILE A CA  
1785 C C   . ILE A 226 ? 0.25954 0.64889 0.42467 0.04477  -0.03220 -0.14794 226 ILE A C   
1786 O O   . ILE A 226 ? 0.25072 0.64331 0.41427 0.03681  -0.01223 -0.15175 226 ILE A O   
1787 C CB  . ILE A 226 ? 0.38272 0.65349 0.45499 0.10567  -0.04023 -0.13250 226 ILE A CB  
1788 C CG1 . ILE A 226 ? 0.46301 0.63151 0.50050 0.14688  -0.03660 -0.16831 226 ILE A CG1 
1789 C CG2 . ILE A 226 ? 0.35833 0.66252 0.46021 0.12165  -0.05179 -0.08593 226 ILE A CG2 
1790 C CD1 . ILE A 226 ? 0.48099 0.62595 0.52464 0.16270  -0.04372 -0.16468 226 ILE A CD1 
1791 N N   . LEU A 227 ? 0.26271 0.65215 0.44656 0.03578  -0.05693 -0.14360 227 LEU A N   
1792 C CA  . LEU A 227 ? 0.23797 0.66620 0.44924 0.01241  -0.04555 -0.13549 227 LEU A CA  
1793 C C   . LEU A 227 ? 0.26657 0.68420 0.46914 0.07271  -0.04659 -0.12247 227 LEU A C   
1794 O O   . LEU A 227 ? 0.32982 0.74465 0.48765 0.09992  -0.05991 -0.12213 227 LEU A O   
1795 C CB  . LEU A 227 ? 0.27951 0.66878 0.46062 -0.04514 -0.01524 -0.13689 227 LEU A CB  
1796 C CG  . LEU A 227 ? 0.26117 0.66455 0.49981 -0.07605 -0.02312 -0.14264 227 LEU A CG  
1797 C CD1 . LEU A 227 ? 0.28947 0.66647 0.51605 -0.06377 -0.00149 -0.14445 227 LEU A CD1 
1798 C CD2 . LEU A 227 ? 0.30619 0.67229 0.52305 -0.09799 -0.05146 -0.14466 227 LEU A CD2 
1799 N N   . HIS A 228 ? 0.25516 0.65025 0.47116 0.06848  -0.02797 -0.09693 228 HIS A N   
1800 C CA  . HIS A 228 ? 0.29063 0.61426 0.47778 0.03334  -0.05007 -0.10331 228 HIS A CA  
1801 C C   . HIS A 228 ? 0.29406 0.60151 0.48852 0.02175  -0.06912 -0.08388 228 HIS A C   
1802 O O   . HIS A 228 ? 0.26777 0.59975 0.45866 0.02617  -0.08780 -0.07721 228 HIS A O   
1803 C CB  . HIS A 228 ? 0.33279 0.59862 0.49317 0.02844  -0.03076 -0.10673 228 HIS A CB  
1804 C CG  . HIS A 228 ? 0.34356 0.57569 0.49567 0.05145  -0.06943 -0.09771 228 HIS A CG  
1805 N ND1 . HIS A 228 ? 0.33411 0.53698 0.49290 0.06841  -0.06633 -0.08641 228 HIS A ND1 
1806 C CD2 . HIS A 228 ? 0.36428 0.56765 0.51101 0.05829  -0.07535 -0.08758 228 HIS A CD2 
1807 C CE1 . HIS A 228 ? 0.34391 0.54815 0.51010 0.09781  -0.05673 -0.08453 228 HIS A CE1 
1808 N NE2 . HIS A 228 ? 0.35257 0.56040 0.51541 0.07925  -0.05894 -0.09398 228 HIS A NE2 
1809 N N   . ARG A 229 ? 0.28011 0.59507 0.51484 0.02947  -0.09380 -0.08462 229 ARG A N   
1810 C CA  . ARG A 229 ? 0.29765 0.59706 0.54521 -0.04547 -0.11903 -0.08448 229 ARG A CA  
1811 C C   . ARG A 229 ? 0.35721 0.59634 0.57477 -0.01334 -0.14952 -0.03662 229 ARG A C   
1812 O O   . ARG A 229 ? 0.36639 0.60362 0.58775 0.02335  -0.16642 -0.02381 229 ARG A O   
1813 C CB  . ARG A 229 ? 0.28316 0.61781 0.56766 -0.05099 -0.08720 -0.08902 229 ARG A CB  
1814 C CG  . ARG A 229 ? 0.38021 0.63530 0.59642 -0.06874 -0.07696 -0.08871 229 ARG A CG  
1815 C CD  . ARG A 229 ? 0.49291 0.65961 0.61892 -0.06480 -0.08013 -0.07662 229 ARG A CD  
1816 N NE  . ARG A 229 ? 0.63829 0.68295 0.63117 -0.07023 -0.07731 -0.07258 229 ARG A NE  
1817 C CZ  . ARG A 229 ? 0.77269 0.69310 0.64136 -0.07693 -0.05713 -0.07565 229 ARG A CZ  
1818 N NH1 . ARG A 229 ? 0.83099 0.70256 0.65091 -0.07144 -0.03547 -0.06663 229 ARG A NH1 
1819 N NH2 . ARG A 229 ? 0.80679 0.70132 0.64198 -0.08878 -0.05372 -0.08707 229 ARG A NH2 
1820 N N   . ASP A 230 ? 0.37802 0.60739 0.57982 -0.02651 -0.18077 -0.00199 230 ASP A N   
1821 C CA  . ASP A 230 ? 0.40565 0.61532 0.60123 -0.00957 -0.19478 0.03151  230 ASP A CA  
1822 C C   . ASP A 230 ? 0.39843 0.55314 0.59156 -0.00307 -0.20456 0.03404  230 ASP A C   
1823 O O   . ASP A 230 ? 0.39940 0.53094 0.60765 0.02836  -0.23581 0.04806  230 ASP A O   
1824 C CB  . ASP A 230 ? 0.42636 0.66791 0.62285 0.04557  -0.21171 0.04336  230 ASP A CB  
1825 C CG  . ASP A 230 ? 0.50604 0.73805 0.64965 0.04678  -0.19856 0.01701  230 ASP A CG  
1826 O OD1 . ASP A 230 ? 0.55648 0.75443 0.64410 0.04213  -0.21683 -0.01762 230 ASP A OD1 
1827 O OD2 . ASP A 230 ? 0.50261 0.77907 0.66798 0.03944  -0.18405 0.02463  230 ASP A OD2 
1828 N N   . VAL A 231 ? 0.36850 0.50957 0.55389 0.00811  -0.18545 0.01339  231 VAL A N   
1829 C CA  . VAL A 231 ? 0.33775 0.47882 0.52409 0.02707  -0.14459 0.00595  231 VAL A CA  
1830 C C   . VAL A 231 ? 0.34359 0.49767 0.51950 0.05610  -0.12343 -0.00690 231 VAL A C   
1831 O O   . VAL A 231 ? 0.36194 0.52314 0.52594 0.06220  -0.08212 -0.01654 231 VAL A O   
1832 C CB  . VAL A 231 ? 0.34036 0.48196 0.51947 -0.00163 -0.13364 0.00623  231 VAL A CB  
1833 C CG1 . VAL A 231 ? 0.30808 0.45597 0.51633 -0.00730 -0.14788 0.01623  231 VAL A CG1 
1834 C CG2 . VAL A 231 ? 0.35126 0.48930 0.51921 0.00313  -0.12667 0.01686  231 VAL A CG2 
1835 N N   . GLN A 232 ? 0.33992 0.51763 0.49415 0.05716  -0.12932 0.00064  232 GLN A N   
1836 C CA  . GLN A 232 ? 0.40060 0.51736 0.47400 0.05961  -0.12439 0.00519  232 GLN A CA  
1837 C C   . GLN A 232 ? 0.41592 0.50061 0.44117 0.05398  -0.13132 0.00048  232 GLN A C   
1838 O O   . GLN A 232 ? 0.47590 0.48992 0.43572 0.04223  -0.12069 0.02834  232 GLN A O   
1839 C CB  . GLN A 232 ? 0.44501 0.49379 0.47269 0.09303  -0.10015 0.01550  232 GLN A CB  
1840 N N   . GLU A 233 ? 0.39827 0.49833 0.40751 0.03629  -0.12233 -0.02847 233 GLU A N   
1841 C CA  . GLU A 233 ? 0.37092 0.48940 0.37021 0.04545  -0.10417 -0.02199 233 GLU A CA  
1842 C C   . GLU A 233 ? 0.29705 0.45040 0.33694 0.05885  -0.05664 -0.02114 233 GLU A C   
1843 O O   . GLU A 233 ? 0.27389 0.44404 0.36866 0.08562  -0.04628 -0.01878 233 GLU A O   
1844 C CB  . GLU A 233 ? 0.44739 0.50636 0.43264 0.03067  -0.06263 -0.01626 233 GLU A CB  
1845 C CG  . GLU A 233 ? 0.44771 0.50702 0.50708 0.05000  -0.04662 0.00013  233 GLU A CG  
1846 C CD  . GLU A 233 ? 0.44989 0.51947 0.58283 0.08532  -0.03973 0.01242  233 GLU A CD  
1847 O OE1 . GLU A 233 ? 0.44639 0.53714 0.60677 0.10147  -0.01777 -0.01103 233 GLU A OE1 
1848 O OE2 . GLU A 233 ? 0.43857 0.53423 0.62367 0.05297  -0.01553 0.02464  233 GLU A OE2 
1849 N N   . ILE A 234 ? 0.26853 0.41259 0.31681 0.00389  -0.04775 -0.02066 234 ILE A N   
1850 C CA  . ILE A 234 ? 0.24234 0.39281 0.31049 0.02224  -0.01430 -0.02028 234 ILE A CA  
1851 C C   . ILE A 234 ? 0.27653 0.36970 0.33392 -0.00055 -0.00659 -0.02633 234 ILE A C   
1852 O O   . ILE A 234 ? 0.29597 0.39699 0.39454 0.00641  0.01730  -0.06113 234 ILE A O   
1853 C CB  . ILE A 234 ? 0.26243 0.39448 0.32137 0.02955  -0.04469 -0.00493 234 ILE A CB  
1854 C CG1 . ILE A 234 ? 0.30562 0.37496 0.36477 0.00244  -0.06093 0.01788  234 ILE A CG1 
1855 C CG2 . ILE A 234 ? 0.30277 0.42183 0.28440 0.02558  -0.04794 -0.02315 234 ILE A CG2 
1856 C CD1 . ILE A 234 ? 0.31134 0.40390 0.41438 0.02207  -0.05282 0.02316  234 ILE A CD1 
1857 N N   . ARG A 235 ? 0.26080 0.32013 0.27304 0.03552  -0.04258 -0.01244 235 ARG A N   
1858 C CA  . ARG A 235 ? 0.30215 0.35108 0.25266 0.06611  -0.07188 0.00534  235 ARG A CA  
1859 C C   . ARG A 235 ? 0.28273 0.34809 0.22950 0.06100  -0.04434 0.01485  235 ARG A C   
1860 O O   . ARG A 235 ? 0.25645 0.45281 0.25248 0.09648  -0.00098 -0.01561 235 ARG A O   
1861 C CB  . ARG A 235 ? 0.38413 0.39531 0.25405 0.10642  -0.09528 0.01424  235 ARG A CB  
1862 C CG  . ARG A 235 ? 0.42010 0.47292 0.30850 0.07137  -0.12670 0.01715  235 ARG A CG  
1863 C CD  . ARG A 235 ? 0.47671 0.51372 0.37570 0.05057  -0.12061 0.04570  235 ARG A CD  
1864 N NE  . ARG A 235 ? 0.54115 0.55813 0.42039 0.03136  -0.12480 0.05580  235 ARG A NE  
1865 C CZ  . ARG A 235 ? 0.58404 0.59925 0.47349 0.04207  -0.15772 0.06406  235 ARG A CZ  
1866 N NH1 . ARG A 235 ? 0.58031 0.61181 0.48429 0.03648  -0.19757 0.06244  235 ARG A NH1 
1867 N NH2 . ARG A 235 ? 0.59486 0.61850 0.49989 0.05601  -0.14242 0.08659  235 ARG A NH2 
1868 N N   . TYR A 236 ? 0.25961 0.32069 0.22820 0.03754  -0.04705 0.03354  236 TYR A N   
1869 C CA  . TYR A 236 ? 0.23858 0.30752 0.23232 0.05749  -0.03633 0.01376  236 TYR A CA  
1870 C C   . TYR A 236 ? 0.25100 0.32175 0.24066 0.04437  0.00581  0.00115  236 TYR A C   
1871 O O   . TYR A 236 ? 0.26790 0.34800 0.23742 0.05043  0.01572  0.01930  236 TYR A O   
1872 C CB  . TYR A 236 ? 0.23767 0.28692 0.25838 0.07486  -0.00887 0.01897  236 TYR A CB  
1873 C CG  . TYR A 236 ? 0.26714 0.29759 0.32253 0.01132  -0.07738 0.04615  236 TYR A CG  
1874 C CD1 . TYR A 236 ? 0.27088 0.33544 0.34415 -0.01770 -0.10378 0.07068  236 TYR A CD1 
1875 C CD2 . TYR A 236 ? 0.30220 0.26839 0.38799 -0.00136 -0.05035 0.04917  236 TYR A CD2 
1876 C CE1 . TYR A 236 ? 0.25933 0.32447 0.38879 -0.03359 -0.12529 0.10487  236 TYR A CE1 
1877 C CE2 . TYR A 236 ? 0.33099 0.29619 0.45245 -0.02760 -0.05808 0.06320  236 TYR A CE2 
1878 C CZ  . TYR A 236 ? 0.32869 0.29868 0.46968 -0.02924 -0.08087 0.11238  236 TYR A CZ  
1879 O OH  . TYR A 236 ? 0.42069 0.37389 0.57139 -0.00289 -0.08265 0.13228  236 TYR A OH  
1880 N N   . GLU A 237 ? 0.28251 0.32404 0.22407 0.06036  -0.00992 0.00391  237 GLU A N   
1881 C CA  . GLU A 237 ? 0.32505 0.28386 0.23803 0.09843  -0.03053 0.02879  237 GLU A CA  
1882 C C   . GLU A 237 ? 0.32760 0.27879 0.23505 0.07392  0.00097  0.00272  237 GLU A C   
1883 O O   . GLU A 237 ? 0.32872 0.28673 0.23808 0.05760  0.03743  0.01822  237 GLU A O   
1884 C CB  . GLU A 237 ? 0.37570 0.31069 0.27822 0.08791  -0.05541 0.04365  237 GLU A CB  
1885 C CG  . GLU A 237 ? 0.40541 0.33550 0.33139 0.07049  -0.04797 0.05029  237 GLU A CG  
1886 C CD  . GLU A 237 ? 0.44006 0.36091 0.38289 0.05336  -0.06632 0.09434  237 GLU A CD  
1887 O OE1 . GLU A 237 ? 0.45515 0.33669 0.40746 0.06034  -0.05282 0.11588  237 GLU A OE1 
1888 O OE2 . GLU A 237 ? 0.43866 0.40523 0.41729 0.05943  -0.06978 0.09031  237 GLU A OE2 
1889 N N   . VAL A 238 ? 0.30638 0.29355 0.23561 0.03268  -0.00390 0.00413  238 VAL A N   
1890 C CA  . VAL A 238 ? 0.31331 0.26047 0.23781 0.04196  -0.01749 -0.02030 238 VAL A CA  
1891 C C   . VAL A 238 ? 0.34555 0.29384 0.24182 0.06014  0.02438  -0.00706 238 VAL A C   
1892 O O   . VAL A 238 ? 0.39345 0.31042 0.26316 0.05515  0.01939  0.02560  238 VAL A O   
1893 C CB  . VAL A 238 ? 0.31660 0.26495 0.23234 0.01787  -0.01251 -0.02878 238 VAL A CB  
1894 C CG1 . VAL A 238 ? 0.35734 0.27413 0.23393 0.01294  -0.02775 -0.04185 238 VAL A CG1 
1895 C CG2 . VAL A 238 ? 0.32675 0.28451 0.26070 0.05305  -0.00563 0.00493  238 VAL A CG2 
1896 N N   . SER A 239 ? 0.35236 0.29612 0.22817 0.06782  0.03833  -0.00639 239 SER A N   
1897 C CA  . SER A 239 ? 0.36284 0.27806 0.25746 0.08684  0.03476  -0.01244 239 SER A CA  
1898 C C   . SER A 239 ? 0.44953 0.30813 0.28605 0.10845  0.04013  0.02093  239 SER A C   
1899 O O   . SER A 239 ? 0.45889 0.30412 0.30402 0.07080  0.07735  0.01807  239 SER A O   
1900 C CB  . SER A 239 ? 0.32919 0.31484 0.26653 0.10446  0.07049  -0.02722 239 SER A CB  
1901 O OG  . SER A 239 ? 0.37484 0.31338 0.29070 0.11402  0.01114  -0.02467 239 SER A OG  
1902 N N   . ALA A 240 ? 0.47672 0.31954 0.28226 0.15667  0.03425  0.03608  240 ALA A N   
1903 C CA  . ALA A 240 ? 0.49645 0.34024 0.29748 0.13030  0.04562  0.03859  240 ALA A CA  
1904 C C   . ALA A 240 ? 0.51580 0.36361 0.31411 0.12760  0.03522  0.02135  240 ALA A C   
1905 O O   . ALA A 240 ? 0.58661 0.37684 0.34563 0.13504  0.06263  0.00743  240 ALA A O   
1906 C CB  . ALA A 240 ? 0.54095 0.37638 0.30908 0.13413  0.04138  0.03693  240 ALA A CB  
1907 N N   . LYS A 241 ? 0.50230 0.37756 0.29846 0.10344  0.03565  0.04865  241 LYS A N   
1908 C CA  . LYS A 241 ? 0.44947 0.38503 0.30541 0.12807  0.05814  0.02500  241 LYS A CA  
1909 C C   . LYS A 241 ? 0.48043 0.36009 0.29245 0.11583  0.05465  0.03520  241 LYS A C   
1910 O O   . LYS A 241 ? 0.43576 0.34569 0.30747 0.09761  0.03903  0.06024  241 LYS A O   
1911 C CB  . LYS A 241 ? 0.40545 0.41057 0.33926 0.17578  0.02413  0.01869  241 LYS A CB  
1912 C CG  . LYS A 241 ? 0.45017 0.45625 0.37777 0.16812  -0.03642 0.06526  241 LYS A CG  
1913 C CD  . LYS A 241 ? 0.49445 0.50085 0.41611 0.14188  -0.08726 0.07273  241 LYS A CD  
1914 C CE  . LYS A 241 ? 0.50214 0.52349 0.46429 0.15066  -0.11897 0.08192  241 LYS A CE  
1915 N NZ  . LYS A 241 ? 0.52872 0.56559 0.50629 0.14750  -0.10978 0.07728  241 LYS A NZ  
1916 N N   . LYS A 242 ? 0.48934 0.32972 0.29103 0.08980  0.04694  0.00930  242 LYS A N   
1917 C CA  . LYS A 242 ? 0.45129 0.36773 0.27668 0.03015  0.04799  0.02199  242 LYS A CA  
1918 C C   . LYS A 242 ? 0.42967 0.34400 0.27791 0.05171  0.03691  -0.00533 242 LYS A C   
1919 O O   . LYS A 242 ? 0.41960 0.34536 0.30255 0.06581  0.03514  -0.01664 242 LYS A O   
1920 C CB  . LYS A 242 ? 0.44982 0.41651 0.30919 0.04907  0.05468  0.02683  242 LYS A CB  
1921 C CG  . LYS A 242 ? 0.46766 0.46298 0.32853 0.04540  0.06020  0.03787  242 LYS A CG  
1922 C CD  . LYS A 242 ? 0.53549 0.49687 0.37189 0.01674  0.04650  0.02605  242 LYS A CD  
1923 C CE  . LYS A 242 ? 0.58074 0.51851 0.40719 0.00642  0.03803  0.02592  242 LYS A CE  
1924 N NZ  . LYS A 242 ? 0.58364 0.52520 0.41429 -0.00306 0.04828  0.04525  242 LYS A NZ  
1925 N N   . ILE A 243 ? 0.39805 0.29599 0.27749 0.03403  0.02725  -0.01247 243 ILE A N   
1926 C CA  . ILE A 243 ? 0.36440 0.28810 0.25840 0.00462  0.04203  -0.03148 243 ILE A CA  
1927 C C   . ILE A 243 ? 0.37358 0.29105 0.27937 -0.00834 0.03472  -0.06096 243 ILE A C   
1928 O O   . ILE A 243 ? 0.39532 0.29780 0.28624 -0.02220 0.05664  -0.06077 243 ILE A O   
1929 C CB  . ILE A 243 ? 0.32040 0.29838 0.27530 0.02258  0.07388  0.00425  243 ILE A CB  
1930 C CG1 . ILE A 243 ? 0.38223 0.28060 0.25263 0.03429  0.06566  0.02866  243 ILE A CG1 
1931 C CG2 . ILE A 243 ? 0.26927 0.31613 0.31835 0.02735  0.00848  -0.03057 243 ILE A CG2 
1932 C CD1 . ILE A 243 ? 0.40413 0.26617 0.27679 0.03616  0.05712  -0.01558 243 ILE A CD1 
1933 N N   . HIS A 244 ? 0.40332 0.28805 0.26729 0.00555  0.00755  -0.05844 244 HIS A N   
1934 C CA  . HIS A 244 ? 0.42651 0.26286 0.26218 -0.03060 -0.00726 -0.08676 244 HIS A CA  
1935 C C   . HIS A 244 ? 0.42292 0.29363 0.27212 -0.03573 0.00889  -0.04713 244 HIS A C   
1936 O O   . HIS A 244 ? 0.38557 0.31587 0.29640 -0.04215 0.01596  -0.05254 244 HIS A O   
1937 C CB  . HIS A 244 ? 0.46712 0.31171 0.31688 -0.00236 0.00847  -0.03180 244 HIS A CB  
1938 C CG  . HIS A 244 ? 0.50978 0.35837 0.36339 -0.00468 0.01747  0.01705  244 HIS A CG  
1939 N ND1 . HIS A 244 ? 0.51097 0.39628 0.38940 0.01870  0.04042  0.02836  244 HIS A ND1 
1940 C CD2 . HIS A 244 ? 0.54730 0.39958 0.37681 -0.01802 -0.00085 0.02158  244 HIS A CD2 
1941 C CE1 . HIS A 244 ? 0.51100 0.40155 0.38228 0.02374  0.05048  0.01658  244 HIS A CE1 
1942 N NE2 . HIS A 244 ? 0.54589 0.39085 0.39424 0.00246  0.03864  0.02090  244 HIS A NE2 
1943 N N   . PHE A 245 ? 0.40468 0.33864 0.23631 -0.00856 -0.00115 -0.04372 245 PHE A N   
1944 C CA  . PHE A 245 ? 0.44485 0.35560 0.26949 -0.00173 -0.01051 -0.03869 245 PHE A CA  
1945 C C   . PHE A 245 ? 0.47496 0.39849 0.26203 -0.03775 0.00678  -0.01759 245 PHE A C   
1946 O O   . PHE A 245 ? 0.52498 0.42987 0.27047 -0.07060 0.04183  -0.00422 245 PHE A O   
1947 C CB  . PHE A 245 ? 0.42074 0.34850 0.29070 0.00372  -0.01979 -0.04433 245 PHE A CB  
1948 C CG  . PHE A 245 ? 0.39461 0.34793 0.30702 0.03258  0.00880  -0.08718 245 PHE A CG  
1949 C CD1 . PHE A 245 ? 0.39874 0.34166 0.31662 0.02126  0.01256  -0.09996 245 PHE A CD1 
1950 C CD2 . PHE A 245 ? 0.42230 0.35692 0.32926 0.04028  -0.00095 -0.09185 245 PHE A CD2 
1951 C CE1 . PHE A 245 ? 0.42896 0.35817 0.33300 0.01938  0.01769  -0.09230 245 PHE A CE1 
1952 C CE2 . PHE A 245 ? 0.43871 0.36762 0.34522 0.05104  0.02030  -0.10645 245 PHE A CE2 
1953 C CZ  . PHE A 245 ? 0.44908 0.38759 0.33656 0.02523  0.01006  -0.09532 245 PHE A CZ  
1954 N N   . ALA A 246 ? 0.49827 0.42569 0.27119 -0.03553 0.00453  -0.02975 246 ALA A N   
1955 C CA  . ALA A 246 ? 0.47511 0.44844 0.29509 -0.03853 0.01621  -0.04410 246 ALA A CA  
1956 C C   . ALA A 246 ? 0.47430 0.48823 0.35145 -0.05360 0.00451  -0.03611 246 ALA A C   
1957 O O   . ALA A 246 ? 0.45766 0.52174 0.38885 -0.05311 -0.05564 0.01017  246 ALA A O   
1958 C CB  . ALA A 246 ? 0.46809 0.48150 0.29181 0.01142  0.00280  -0.05145 246 ALA A CB  
1959 N N   . ARG A 247 ? 0.49802 0.51442 0.35739 -0.06915 0.04383  -0.06987 247 ARG A N   
1960 C CA  . ARG A 247 ? 0.54273 0.55073 0.39520 -0.06411 0.03956  -0.10898 247 ARG A CA  
1961 C C   . ARG A 247 ? 0.55901 0.56885 0.43145 -0.03284 0.02713  -0.11318 247 ARG A C   
1962 O O   . ARG A 247 ? 0.55364 0.58804 0.43333 -0.03452 0.00623  -0.11624 247 ARG A O   
1963 C CB  . ARG A 247 ? 0.59294 0.57175 0.41098 -0.05472 0.04276  -0.11806 247 ARG A CB  
1964 C CG  . ARG A 247 ? 0.64472 0.58904 0.42571 -0.04893 0.01869  -0.12093 247 ARG A CG  
1965 C CD  . ARG A 247 ? 0.69502 0.60955 0.44526 -0.04433 0.01586  -0.13098 247 ARG A CD  
1966 N NE  . ARG A 247 ? 0.69726 0.64076 0.47629 -0.02539 0.03345  -0.10459 247 ARG A NE  
1967 C CZ  . ARG A 247 ? 0.66592 0.64797 0.49306 0.01645  0.04783  -0.10896 247 ARG A CZ  
1968 N NH1 . ARG A 247 ? 0.65154 0.68160 0.51999 0.00086  0.09069  -0.08117 247 ARG A NH1 
1969 N NH2 . ARG A 247 ? 0.62825 0.60624 0.47215 0.04527  0.01144  -0.14362 247 ARG A NH2 
1970 N N   . PHE A 248 ? 0.56531 0.58279 0.48462 -0.01604 0.02312  -0.11748 248 PHE A N   
1971 C CA  . PHE A 248 ? 0.55037 0.61710 0.51533 0.04208  0.04421  -0.12392 248 PHE A CA  
1972 C C   . PHE A 248 ? 0.57334 0.61233 0.51540 0.02659  0.05354  -0.16439 248 PHE A C   
1973 O O   . PHE A 248 ? 0.56230 0.63711 0.51859 0.01525  0.09587  -0.16831 248 PHE A O   
1974 C CB  . PHE A 248 ? 0.55814 0.65473 0.55920 0.06301  0.05213  -0.07942 248 PHE A CB  
1975 C CG  . PHE A 248 ? 0.55417 0.67886 0.58873 0.08879  0.04987  -0.05399 248 PHE A CG  
1976 C CD1 . PHE A 248 ? 0.53552 0.66861 0.59097 0.11174  0.07373  -0.04794 248 PHE A CD1 
1977 C CD2 . PHE A 248 ? 0.53834 0.68534 0.60329 0.08972  0.04861  -0.05145 248 PHE A CD2 
1978 C CE1 . PHE A 248 ? 0.49736 0.66530 0.59158 0.12334  0.08130  -0.03628 248 PHE A CE1 
1979 C CE2 . PHE A 248 ? 0.52366 0.68545 0.60859 0.09916  0.05552  -0.04196 248 PHE A CE2 
1980 C CZ  . PHE A 248 ? 0.47887 0.66572 0.59725 0.13653  0.08226  -0.03868 248 PHE A CZ  
1981 N N   . ARG A 249 ? 0.55110 0.57653 0.50511 0.05831  0.05301  -0.19877 249 ARG A N   
1982 C CA  . ARG A 249 ? 0.60636 0.56806 0.51523 0.03263  0.04053  -0.21295 249 ARG A CA  
1983 C C   . ARG A 249 ? 0.59427 0.55316 0.49889 0.05764  0.02604  -0.25086 249 ARG A C   
1984 O O   . ARG A 249 ? 0.59122 0.57449 0.50967 0.06191  0.01355  -0.25560 249 ARG A O   
1985 C CB  . ARG A 249 ? 0.64221 0.57760 0.54065 0.00896  0.01524  -0.17734 249 ARG A CB  
1986 C CG  . ARG A 249 ? 0.67642 0.59057 0.55866 0.00649  0.00695  -0.14975 249 ARG A CG  
1987 C CD  . ARG A 249 ? 0.69921 0.61553 0.57499 0.00482  0.00048  -0.11414 249 ARG A CD  
1988 N NE  . ARG A 249 ? 0.72806 0.64428 0.59869 -0.00866 -0.01357 -0.09233 249 ARG A NE  
1989 C CZ  . ARG A 249 ? 0.75129 0.67388 0.62429 -0.02876 -0.02465 -0.07053 249 ARG A CZ  
1990 N NH1 . ARG A 249 ? 0.75600 0.68749 0.62599 -0.04840 -0.03889 -0.05681 249 ARG A NH1 
1991 N NH2 . ARG A 249 ? 0.75358 0.68466 0.63289 -0.02758 -0.02523 -0.07134 249 ARG A NH2 
1992 N N   . SER A 250 ? 0.62538 0.54356 0.49077 0.02686  0.01589  -0.24347 250 SER A N   
1993 C CA  . SER A 250 ? 0.61837 0.54149 0.48255 0.05038  0.02584  -0.22208 250 SER A CA  
1994 C C   . SER A 250 ? 0.58429 0.52619 0.45987 0.03123  -0.00562 -0.20994 250 SER A C   
1995 O O   . SER A 250 ? 0.62756 0.56672 0.46614 0.02424  -0.01930 -0.21077 250 SER A O   
1996 C CB  . SER A 250 ? 0.67107 0.57349 0.50622 0.06537  0.01443  -0.18521 250 SER A CB  
1997 O OG  . SER A 250 ? 0.69301 0.57969 0.49834 0.08593  0.01045  -0.18061 250 SER A OG  
1998 N N   . PHE A 251 ? 0.51983 0.47950 0.45068 0.01490  -0.01136 -0.19782 251 PHE A N   
1999 C CA  . PHE A 251 ? 0.46268 0.44680 0.44051 -0.02324 0.01957  -0.18126 251 PHE A CA  
2000 C C   . PHE A 251 ? 0.42599 0.43857 0.40250 -0.01967 -0.01445 -0.17566 251 PHE A C   
2001 O O   . PHE A 251 ? 0.40998 0.44135 0.43474 0.01704  -0.01738 -0.16475 251 PHE A O   
2002 C CB  . PHE A 251 ? 0.43811 0.43118 0.47436 -0.04673 0.05671  -0.15683 251 PHE A CB  
2003 C CG  . PHE A 251 ? 0.44555 0.44268 0.50527 -0.06243 0.05832  -0.15664 251 PHE A CG  
2004 C CD1 . PHE A 251 ? 0.45777 0.43861 0.51468 -0.08576 0.06719  -0.16276 251 PHE A CD1 
2005 C CD2 . PHE A 251 ? 0.45522 0.43551 0.53507 -0.06907 0.04803  -0.16464 251 PHE A CD2 
2006 C CE1 . PHE A 251 ? 0.39766 0.40842 0.51142 -0.13561 0.07268  -0.18647 251 PHE A CE1 
2007 C CE2 . PHE A 251 ? 0.47099 0.43510 0.55257 -0.06263 0.05220  -0.16933 251 PHE A CE2 
2008 C CZ  . PHE A 251 ? 0.45218 0.41861 0.53603 -0.08594 0.07670  -0.17799 251 PHE A CZ  
2009 N N   . PRO A 252 ? 0.38602 0.43558 0.35177 0.01754  0.00144  -0.14394 252 PRO A N   
2010 C CA  . PRO A 252 ? 0.38441 0.42097 0.32603 0.02461  0.01117  -0.11637 252 PRO A CA  
2011 C C   . PRO A 252 ? 0.38747 0.42407 0.29643 0.05999  0.00268  -0.09412 252 PRO A C   
2012 O O   . PRO A 252 ? 0.39905 0.46269 0.27274 0.06877  -0.01974 -0.07053 252 PRO A O   
2013 C CB  . PRO A 252 ? 0.39163 0.43322 0.35045 -0.03263 0.01650  -0.09929 252 PRO A CB  
2014 C CG  . PRO A 252 ? 0.39420 0.42454 0.35321 -0.00815 0.00811  -0.08867 252 PRO A CG  
2015 C CD  . PRO A 252 ? 0.36824 0.42757 0.36601 -0.00375 0.01545  -0.12049 252 PRO A CD  
2016 N N   . PHE A 253 ? 0.39171 0.39175 0.29849 0.07880  -0.03024 -0.09492 253 PHE A N   
2017 C CA  . PHE A 253 ? 0.38725 0.39271 0.27995 0.03404  -0.01669 -0.08127 253 PHE A CA  
2018 C C   . PHE A 253 ? 0.34585 0.36230 0.26801 0.04145  -0.00108 -0.04499 253 PHE A C   
2019 O O   . PHE A 253 ? 0.33881 0.32154 0.25439 0.02870  0.01211  -0.06708 253 PHE A O   
2020 C CB  . PHE A 253 ? 0.40232 0.39348 0.27053 0.00610  -0.01690 -0.05375 253 PHE A CB  
2021 C CG  . PHE A 253 ? 0.37902 0.38322 0.26426 -0.01221 -0.01912 -0.02499 253 PHE A CG  
2022 C CD1 . PHE A 253 ? 0.37084 0.40840 0.28139 -0.02746 -0.03350 -0.04982 253 PHE A CD1 
2023 C CD2 . PHE A 253 ? 0.40241 0.37843 0.27341 -0.00920 -0.01657 -0.00461 253 PHE A CD2 
2024 C CE1 . PHE A 253 ? 0.36928 0.40186 0.28596 -0.00394 0.01258  -0.04915 253 PHE A CE1 
2025 C CE2 . PHE A 253 ? 0.40766 0.38405 0.27606 -0.02727 0.01211  -0.02939 253 PHE A CE2 
2026 C CZ  . PHE A 253 ? 0.38490 0.39652 0.26428 -0.03434 0.00534  -0.04518 253 PHE A CZ  
2027 N N   . TRP A 254 ? 0.31684 0.36543 0.25989 0.06388  0.00501  -0.02818 254 TRP A N   
2028 C CA  . TRP A 254 ? 0.33681 0.33057 0.24620 0.01108  0.01502  -0.01105 254 TRP A CA  
2029 C C   . TRP A 254 ? 0.33766 0.33511 0.22231 -0.02345 0.00945  -0.04691 254 TRP A C   
2030 O O   . TRP A 254 ? 0.29446 0.31290 0.22804 -0.02919 -0.01094 -0.04289 254 TRP A O   
2031 C CB  . TRP A 254 ? 0.36425 0.33850 0.25304 0.01591  0.02541  0.01703  254 TRP A CB  
2032 C CG  . TRP A 254 ? 0.36649 0.31142 0.24448 0.02378  0.03058  -0.00854 254 TRP A CG  
2033 C CD1 . TRP A 254 ? 0.37343 0.31872 0.24972 0.04587  0.04570  -0.00799 254 TRP A CD1 
2034 C CD2 . TRP A 254 ? 0.33031 0.31096 0.23938 0.04224  0.07849  -0.03835 254 TRP A CD2 
2035 N NE1 . TRP A 254 ? 0.36895 0.29597 0.25549 0.03530  0.05329  -0.00734 254 TRP A NE1 
2036 C CE2 . TRP A 254 ? 0.35132 0.32779 0.25634 0.04550  0.04790  -0.03865 254 TRP A CE2 
2037 C CE3 . TRP A 254 ? 0.35527 0.33224 0.24657 0.08636  0.07226  -0.03003 254 TRP A CE3 
2038 C CZ2 . TRP A 254 ? 0.36372 0.35734 0.26291 0.02722  0.05318  -0.06299 254 TRP A CZ2 
2039 C CZ3 . TRP A 254 ? 0.36075 0.35747 0.24748 0.06995  0.05538  -0.04597 254 TRP A CZ3 
2040 C CH2 . TRP A 254 ? 0.36054 0.36222 0.26069 0.02976  0.05255  -0.07341 254 TRP A CH2 
2041 N N   . ARG A 255 ? 0.36243 0.37039 0.20760 -0.04429 -0.01033 -0.05700 255 ARG A N   
2042 C CA  . ARG A 255 ? 0.37886 0.38853 0.20923 -0.07430 -0.02819 -0.09324 255 ARG A CA  
2043 C C   . ARG A 255 ? 0.37502 0.41730 0.23955 -0.04761 -0.01794 -0.09170 255 ARG A C   
2044 O O   . ARG A 255 ? 0.34577 0.43075 0.23213 -0.05489 0.00232  -0.09329 255 ARG A O   
2045 C CB  . ARG A 255 ? 0.42382 0.40139 0.20217 -0.06667 -0.01880 -0.09201 255 ARG A CB  
2046 C CG  . ARG A 255 ? 0.45197 0.42798 0.22140 -0.07377 -0.02950 -0.06041 255 ARG A CG  
2047 C CD  . ARG A 255 ? 0.49124 0.45481 0.25215 -0.06752 -0.04668 -0.08055 255 ARG A CD  
2048 N NE  . ARG A 255 ? 0.49819 0.48642 0.29139 -0.09321 -0.06355 -0.08093 255 ARG A NE  
2049 C CZ  . ARG A 255 ? 0.50094 0.49871 0.34759 -0.09360 -0.07698 -0.06709 255 ARG A CZ  
2050 N NH1 . ARG A 255 ? 0.48668 0.50029 0.36969 -0.11181 -0.11449 -0.04306 255 ARG A NH1 
2051 N NH2 . ARG A 255 ? 0.50558 0.51339 0.36149 -0.12244 -0.07490 -0.09134 255 ARG A NH2 
2052 N N   . ARG A 256 ? 0.33914 0.43213 0.22614 -0.01760 -0.00042 -0.10428 256 ARG A N   
2053 C CA  . ARG A 256 ? 0.34005 0.45790 0.22980 -0.01639 0.02742  -0.10532 256 ARG A CA  
2054 C C   . ARG A 256 ? 0.29636 0.43537 0.22991 -0.03782 0.03301  -0.09605 256 ARG A C   
2055 O O   . ARG A 256 ? 0.30996 0.44372 0.24566 -0.04071 0.00669  -0.09701 256 ARG A O   
2056 C CB  . ARG A 256 ? 0.34088 0.51572 0.29791 -0.00465 -0.00246 -0.07097 256 ARG A CB  
2057 C CG  . ARG A 256 ? 0.36462 0.52975 0.32906 0.01434  0.00726  -0.04649 256 ARG A CG  
2058 C CD  . ARG A 256 ? 0.37613 0.50532 0.27760 0.03766  -0.00177 -0.03331 256 ARG A CD  
2059 N NE  . ARG A 256 ? 0.37799 0.47198 0.29697 0.13361  0.02116  -0.07508 256 ARG A NE  
2060 C CZ  . ARG A 256 ? 0.49139 0.45907 0.33319 0.13662  0.01386  -0.07346 256 ARG A CZ  
2061 N NH1 . ARG A 256 ? 0.50869 0.46359 0.34609 0.13109  -0.00334 -0.05539 256 ARG A NH1 
2062 N NH2 . ARG A 256 ? 0.47569 0.43868 0.33259 0.19437  0.00400  -0.08820 256 ARG A NH2 
2063 N N   . VAL A 257 ? 0.31365 0.40917 0.18717 -0.00223 0.02995  -0.10635 257 VAL A N   
2064 C CA  . VAL A 257 ? 0.29901 0.37102 0.19188 -0.01524 0.04319  -0.05240 257 VAL A CA  
2065 C C   . VAL A 257 ? 0.34129 0.37291 0.20357 -0.03732 0.02864  -0.04631 257 VAL A C   
2066 O O   . VAL A 257 ? 0.33242 0.36781 0.21186 -0.05146 0.00443  -0.07196 257 VAL A O   
2067 C CB  . VAL A 257 ? 0.31534 0.34241 0.18069 0.01734  0.05254  -0.03974 257 VAL A CB  
2068 C CG1 . VAL A 257 ? 0.33190 0.28377 0.19186 -0.01776 0.04019  -0.05613 257 VAL A CG1 
2069 C CG2 . VAL A 257 ? 0.30756 0.33997 0.18809 0.01725  -0.01379 -0.01694 257 VAL A CG2 
2070 N N   . HIS A 258 ? 0.35608 0.38678 0.20667 -0.00591 0.02959  -0.02657 258 HIS A N   
2071 C CA  . HIS A 258 ? 0.33052 0.38944 0.20625 -0.01289 0.01723  -0.04334 258 HIS A CA  
2072 C C   . HIS A 258 ? 0.34779 0.39170 0.20790 -0.04883 0.04274  -0.05221 258 HIS A C   
2073 O O   . HIS A 258 ? 0.32732 0.43837 0.20756 -0.04462 0.03873  -0.03884 258 HIS A O   
2074 C CB  . HIS A 258 ? 0.27386 0.38927 0.21344 -0.02553 -0.00544 -0.04369 258 HIS A CB  
2075 C CG  . HIS A 258 ? 0.31166 0.41600 0.20556 -0.03686 -0.01236 -0.03584 258 HIS A CG  
2076 N ND1 . HIS A 258 ? 0.35721 0.46764 0.23843 -0.03566 -0.00913 -0.04165 258 HIS A ND1 
2077 C CD2 . HIS A 258 ? 0.31101 0.39384 0.21279 -0.08018 -0.03505 -0.04587 258 HIS A CD2 
2078 C CE1 . HIS A 258 ? 0.36403 0.43516 0.22644 -0.05248 -0.00352 -0.03204 258 HIS A CE1 
2079 N NE2 . HIS A 258 ? 0.39706 0.43123 0.26514 -0.05715 -0.01971 -0.01127 258 HIS A NE2 
2080 N N   . ASP A 259 ? 0.31039 0.38022 0.21595 -0.07757 0.02834  -0.08255 259 ASP A N   
2081 C CA  . ASP A 259 ? 0.35894 0.42678 0.24711 -0.09387 0.02211  -0.07793 259 ASP A CA  
2082 C C   . ASP A 259 ? 0.39978 0.43646 0.25528 -0.10776 0.01857  -0.07182 259 ASP A C   
2083 O O   . ASP A 259 ? 0.47897 0.45296 0.26894 -0.12944 0.01129  -0.05507 259 ASP A O   
2084 C CB  . ASP A 259 ? 0.37624 0.43700 0.25096 -0.04810 0.03519  -0.10935 259 ASP A CB  
2085 C CG  . ASP A 259 ? 0.39532 0.46634 0.30815 -0.01109 0.05410  -0.11425 259 ASP A CG  
2086 O OD1 . ASP A 259 ? 0.39411 0.47012 0.29276 -0.00685 0.02271  -0.12218 259 ASP A OD1 
2087 O OD2 . ASP A 259 ? 0.39570 0.48917 0.34769 0.01744  0.06048  -0.10629 259 ASP A OD2 
2088 N N   . SER A 260 ? 0.32103 0.42008 0.23602 -0.09100 0.03300  -0.06743 260 SER A N   
2089 C CA  . SER A 260 ? 0.32915 0.41360 0.28187 -0.08043 0.04639  -0.08490 260 SER A CA  
2090 C C   . SER A 260 ? 0.31892 0.40197 0.28105 -0.11845 0.05394  -0.06624 260 SER A C   
2091 O O   . SER A 260 ? 0.37012 0.45699 0.30228 -0.15180 0.09391  -0.07288 260 SER A O   
2092 C CB  . SER A 260 ? 0.39235 0.43586 0.31831 -0.03807 0.01206  -0.08650 260 SER A CB  
2093 O OG  . SER A 260 ? 0.43160 0.44358 0.36172 0.01739  -0.00653 -0.07678 260 SER A OG  
2094 N N   . PHE A 261 ? 0.27866 0.38500 0.24642 -0.03615 0.03061  -0.04110 261 PHE A N   
2095 C CA  . PHE A 261 ? 0.32055 0.36870 0.22756 -0.02422 -0.00905 -0.02893 261 PHE A CA  
2096 C C   . PHE A 261 ? 0.37113 0.35917 0.26982 -0.00285 -0.05170 -0.02707 261 PHE A C   
2097 O O   . PHE A 261 ? 0.41519 0.32134 0.31311 0.00037  -0.07733 -0.04127 261 PHE A O   
2098 C CB  . PHE A 261 ? 0.30919 0.36591 0.18572 -0.02927 -0.03019 -0.01706 261 PHE A CB  
2099 C CG  . PHE A 261 ? 0.26937 0.36012 0.17951 0.00285  -0.04119 0.00283  261 PHE A CG  
2100 C CD1 . PHE A 261 ? 0.29449 0.34443 0.18988 -0.03536 -0.01950 -0.02647 261 PHE A CD1 
2101 C CD2 . PHE A 261 ? 0.30821 0.37220 0.20355 -0.02096 -0.01850 0.01272  261 PHE A CD2 
2102 C CE1 . PHE A 261 ? 0.33026 0.33132 0.20842 -0.00969 -0.00557 -0.02486 261 PHE A CE1 
2103 C CE2 . PHE A 261 ? 0.31869 0.36946 0.20840 -0.03763 -0.03122 -0.00161 261 PHE A CE2 
2104 C CZ  . PHE A 261 ? 0.29209 0.33838 0.19512 -0.02211 -0.01059 -0.01764 261 PHE A CZ  
2105 N N   . ILE A 262 ? 0.35645 0.36446 0.23309 -0.02001 -0.04030 -0.00194 262 ILE A N   
2106 C CA  . ILE A 262 ? 0.36651 0.37801 0.23734 0.01752  -0.03506 0.01583  262 ILE A CA  
2107 C C   . ILE A 262 ? 0.48574 0.42397 0.25295 0.05302  -0.03644 0.05832  262 ILE A C   
2108 O O   . ILE A 262 ? 0.56249 0.44499 0.28939 0.05692  -0.03032 0.06502  262 ILE A O   
2109 C CB  . ILE A 262 ? 0.37480 0.38188 0.25771 0.01818  -0.04873 -0.00218 262 ILE A CB  
2110 C CG1 . ILE A 262 ? 0.34846 0.39769 0.26764 0.00895  -0.04560 -0.04144 262 ILE A CG1 
2111 C CG2 . ILE A 262 ? 0.39934 0.39135 0.28702 0.02986  -0.04086 -0.01084 262 ILE A CG2 
2112 C CD1 . ILE A 262 ? 0.35908 0.44696 0.29076 0.00409  -0.03354 -0.04469 262 ILE A CD1 
2113 N N   . GLU A 263 ? 0.51117 0.48108 0.21880 0.03212  -0.00153 0.03737  263 GLU A N   
2114 C CA  . GLU A 263 ? 0.61268 0.60154 0.32858 0.04420  -0.02969 0.04256  263 GLU A CA  
2115 C C   . GLU A 263 ? 0.68215 0.67248 0.36746 0.01487  0.00129  0.00002  263 GLU A C   
2116 O O   . GLU A 263 ? 0.67797 0.71652 0.34839 -0.03232 0.02512  -0.03713 263 GLU A O   
2117 C CB  . GLU A 263 ? 0.68852 0.62191 0.40289 0.03754  -0.04785 0.05750  263 GLU A CB  
2118 C CG  . GLU A 263 ? 0.71397 0.61518 0.47209 0.00502  -0.04219 0.04854  263 GLU A CG  
2119 C CD  . GLU A 263 ? 0.72776 0.60339 0.52439 0.01177  -0.06450 0.03792  263 GLU A CD  
2120 O OE1 . GLU A 263 ? 0.73625 0.61743 0.55229 0.00798  -0.07706 0.02653  263 GLU A OE1 
2121 O OE2 . GLU A 263 ? 0.73404 0.57849 0.53609 0.02430  -0.06866 0.01198  263 GLU A OE2 
2122 N N   . ASP A 264 ? 0.78622 0.73234 0.43589 0.04248  0.01844  -0.00356 264 ASP A N   
2123 C CA  . ASP A 264 ? 0.85859 0.77525 0.50369 0.06223  -0.00078 -0.01032 264 ASP A CA  
2124 C C   . ASP A 264 ? 0.90085 0.81257 0.54239 0.04499  -0.00978 -0.01228 264 ASP A C   
2125 O O   . ASP A 264 ? 0.93249 0.84249 0.57009 0.02606  -0.01517 -0.03466 264 ASP A O   
2126 C CB  . ASP A 264 ? 0.86225 0.76536 0.51489 0.08023  0.00305  -0.00265 264 ASP A CB  
2127 C C1  . CIT B .   ? 0.58120 0.71327 0.71896 -0.03358 -0.16349 -0.10633 301 CIT A C1  
2128 O O1  . CIT B .   ? 0.51810 0.69083 0.68327 -0.05279 -0.17465 -0.12222 301 CIT A O1  
2129 O O2  . CIT B .   ? 0.63048 0.71496 0.72542 -0.01299 -0.14065 -0.08559 301 CIT A O2  
2130 C C2  . CIT B .   ? 0.64088 0.72861 0.74765 -0.00207 -0.15146 -0.12255 301 CIT A C2  
2131 C C3  . CIT B .   ? 0.70291 0.73469 0.77723 0.05080  -0.14726 -0.14305 301 CIT A C3  
2132 O O7  . CIT B .   ? 0.70747 0.73108 0.78516 0.03961  -0.15996 -0.14807 301 CIT A O7  
2133 C C4  . CIT B .   ? 0.74975 0.73773 0.79943 0.08056  -0.14023 -0.13020 301 CIT A C4  
2134 C C5  . CIT B .   ? 0.80778 0.74300 0.81890 0.06778  -0.12688 -0.12314 301 CIT A C5  
2135 O O3  . CIT B .   ? 0.83258 0.73931 0.83004 0.08334  -0.11501 -0.11410 301 CIT A O3  
2136 O O4  . CIT B .   ? 0.82058 0.73951 0.81521 0.03744  -0.12976 -0.12309 301 CIT A O4  
2137 C C6  . CIT B .   ? 0.66415 0.73872 0.77127 0.09642  -0.14181 -0.17295 301 CIT A C6  
2138 O O5  . CIT B .   ? 0.63139 0.71458 0.75377 0.11620  -0.17572 -0.16094 301 CIT A O5  
2139 O O6  . CIT B .   ? 0.65808 0.76851 0.77336 0.11186  -0.10793 -0.21585 301 CIT A O6  
2140 N N4  . UOL C .   ? 0.20860 0.27231 0.23739 -0.00269 0.00431  -0.03522 302 UOL A N4  
2141 C C4  . UOL C .   ? 0.34063 0.36573 0.26124 -0.01997 0.03743  0.04640  302 UOL A C4  
2142 N N3  . UOL C .   ? 0.25872 0.39855 0.24333 -0.03226 0.05871  -0.03107 302 UOL A N3  
2143 C C2  . UOL C .   ? 0.43499 0.40512 0.31143 -0.01570 0.04122  0.03749  302 UOL A C2  
2144 O O2  . UOL C .   ? 0.44736 0.39760 0.30781 0.03758  -0.00498 0.05423  302 UOL A O2  
2145 C C5  . UOL C .   ? 0.29119 0.33836 0.22648 -0.02963 0.02078  0.01449  302 UOL A C5  
2146 N N5  . UOL C .   ? 0.26226 0.29157 0.25542 -0.00276 0.01127  -0.03077 302 UOL A N5  
2147 C C6  . UOL C .   ? 0.32341 0.36766 0.23550 0.03660  0.00525  0.03334  302 UOL A C6  
2148 O O6  . UOL C .   ? 0.22977 0.36065 0.22814 -0.01743 0.04081  -0.02565 302 UOL A O6  
2149 N N1  . UOL C .   ? 0.37656 0.38764 0.29261 0.01757  0.02819  0.03004  302 UOL A N1  
2150 N N   . UOL C .   ? 0.49333 0.43927 0.32414 -0.07332 0.05192  0.04492  302 UOL A N   
2151 C C   . UOL C .   ? 0.56746 0.47394 0.37454 -0.09619 0.05936  0.02776  302 UOL A C   
2152 O O   . UOL C .   ? 0.43142 0.38159 0.30775 0.01056  0.04859  0.04110  302 UOL A O   
2153 C C1  . UOL C .   ? 0.55432 0.44904 0.35198 -0.09071 0.03636  0.01983  302 UOL A C1  
2154 C C10 . UOL C .   ? 0.28713 0.37125 0.22637 -0.08548 -0.00065 -0.01642 302 UOL A C10 
2155 C C11 . UOL C .   ? 0.26171 0.39543 0.22689 -0.04379 -0.00489 -0.04170 302 UOL A C11 
2156 C C12 . UOL C .   ? 0.23759 0.35275 0.22895 0.01174  0.07030  -0.03097 302 UOL A C12 
2157 C C13 . UOL C .   ? 0.24298 0.32374 0.21006 0.02510  0.05695  -0.03623 302 UOL A C13 
2158 C C14 . UOL C .   ? 0.25049 0.31052 0.23533 0.01042  0.02340  -0.03944 302 UOL A C14 
2159 C C15 . UOL C .   ? 0.22621 0.32905 0.21515 -0.00652 0.03404  -0.04419 302 UOL A C15 
2160 C C16 . UOL C .   ? 0.20540 0.30800 0.19918 -0.01419 0.06600  -0.03273 302 UOL A C16 
2161 C C17 . UOL C .   ? 0.23174 0.27519 0.24509 -0.02008 -0.02402 -0.02323 302 UOL A C17 
2162 C C18 . UOL C .   ? 0.21079 0.28275 0.25330 -0.00350 0.00242  -0.00853 302 UOL A C18 
2163 C C19 . UOL C .   ? 0.18020 0.27785 0.24276 0.00372  0.02063  -0.00493 302 UOL A C19 
2164 C C20 . UOL C .   ? 0.16548 0.30120 0.27984 0.04326  -0.00117 0.02374  302 UOL A C20 
2165 C C21 . UOL C .   ? 0.23139 0.29166 0.23826 -0.00720 0.00307  -0.00349 302 UOL A C21 
2166 C C22 . UOL C .   ? 0.32549 0.43035 0.25402 -0.07269 0.05669  0.01930  302 UOL A C22 
2167 C C23 . UOL C .   ? 0.27617 0.28499 0.20273 -0.01958 0.02597  0.00445  302 UOL A C23 
2168 C C24 . UOL C .   ? 0.25974 0.30224 0.20348 -0.01576 0.03551  -0.00372 302 UOL A C24 
2169 C C25 . UOL C .   ? 0.30397 0.33105 0.21235 0.02177  0.07778  -0.00873 302 UOL A C25 
2170 C C26 . UOL C .   ? 0.26414 0.27384 0.19633 -0.01707 0.04335  -0.01441 302 UOL A C26 
2171 C C3  . UOL C .   ? 0.31823 0.39880 0.28404 0.03070  0.03117  0.02082  302 UOL A C3  
2172 C C7  . UOL C .   ? 0.37001 0.38393 0.27456 -0.00414 0.00648  0.03120  302 UOL A C7  
2173 C C8  . UOL C .   ? 0.28216 0.32440 0.20629 -0.05944 0.02990  -0.00453 302 UOL A C8  
2174 C C9  . UOL C .   ? 0.27742 0.36374 0.21460 -0.07583 0.00811  -0.02330 302 UOL A C9  
2175 N N10 . UOL C .   ? 0.28650 0.29920 0.19314 0.02698  0.03199  -0.00070 302 UOL A N10 
2176 N N11 . UOL C .   ? 0.30169 0.30044 0.19954 0.02226  0.06323  -0.01545 302 UOL A N11 
2177 N N12 . UOL C .   ? 0.28503 0.26150 0.20104 -0.01238 0.02550  0.00131  302 UOL A N12 
2178 N N2  . UOL C .   ? 0.28479 0.31196 0.21201 -0.02195 0.02851  -0.00430 302 UOL A N2  
2179 N N6  . UOL C .   ? 0.17355 0.29140 0.25522 0.01628  0.01035  0.01173  302 UOL A N6  
2180 N N7  . UOL C .   ? 0.22322 0.29711 0.26251 0.03056  0.00300  0.01040  302 UOL A N7  
2181 N N8  . UOL C .   ? 0.32273 0.32382 0.20523 -0.04138 0.02732  -0.00768 302 UOL A N8  
2182 N N9  . UOL C .   ? 0.28657 0.31720 0.19917 -0.03762 0.03611  0.00235  302 UOL A N9  
2183 O O1  . UOL C .   ? 0.33076 0.33594 0.22248 -0.02502 0.00524  0.00518  302 UOL A O1  
2184 O O3  . UOL C .   ? 0.36263 0.42140 0.24474 0.05482  -0.00285 0.00028  302 UOL A O3  
2185 O O4  . UOL C .   ? 0.24559 0.34157 0.22581 0.03439  0.01796  -0.02651 302 UOL A O4  
2186 O O5  . UOL C .   ? 0.25067 0.33856 0.20351 -0.00702 0.00503  -0.00889 302 UOL A O5  
2222 O O   . HOH D .   ? 0.75525 0.63378 0.70565 0.11204  0.00982  -0.12663 401 HOH A O   
2223 O O   . HOH D .   ? 0.57768 0.50936 0.78830 0.06057  0.12082  0.18590  402 HOH A O   
2224 O O   . HOH D .   ? 0.59417 0.56346 0.56415 -0.00219 -0.12600 0.17160  403 HOH A O   
2225 O O   . HOH D .   ? 0.27864 0.82213 0.62089 -0.06912 0.08917  0.08010  404 HOH A O   
2226 O O   . HOH D .   ? 0.70457 0.62032 0.69776 0.06559  0.11019  -0.01532 405 HOH A O   
2227 O O   . HOH D .   ? 0.42741 0.46582 0.59892 0.04932  0.04079  -0.10517 406 HOH A O   
2228 O O   . HOH D .   ? 0.32819 0.42899 0.28921 0.03582  -0.01400 -0.02963 407 HOH A O   
2229 O O   . HOH D .   ? 0.87568 0.72800 0.51037 0.44919  -0.03679 -0.12497 408 HOH A O   
2230 O O   . HOH D .   ? 0.76813 0.52822 0.69799 0.24494  -0.30646 -0.02368 409 HOH A O   
2231 O O   . HOH D .   ? 0.37044 0.63440 0.45791 0.00902  -0.13715 0.01144  410 HOH A O   
2232 O O   . HOH D .   ? 0.23259 0.37893 0.27027 0.00178  0.01087  -0.09169 411 HOH A O   
2233 O O   . HOH D .   ? 0.47096 1.05486 0.67489 0.30218  -0.12599 0.04452  412 HOH A O   
2234 O O   . HOH D .   ? 0.47783 0.39077 0.36364 -0.02385 0.01754  -0.00410 413 HOH A O   
2235 O O   . HOH D .   ? 0.25850 0.50846 0.18041 -0.05098 -0.01447 0.02148  414 HOH A O   
2236 O O   . HOH D .   ? 0.43209 0.48220 0.33842 0.01371  0.00429  0.01093  415 HOH A O   
2237 O O   . HOH D .   ? 0.67964 0.65042 0.35288 -0.10928 0.07159  -0.03049 416 HOH A O   
2238 O O   . HOH D .   ? 0.41356 0.40649 0.63875 -0.09927 -0.16931 0.07343  417 HOH A O   
2239 O O   . HOH D .   ? 0.31265 0.32008 0.60179 0.00000  0.11767  0.00000  418 HOH A O   
2240 O O   . HOH D .   ? 0.30723 0.65506 0.36397 0.18852  -0.11545 -0.21177 419 HOH A O   
2241 O O   . HOH D .   ? 0.37772 0.30105 0.29225 0.07125  0.05840  -0.01191 420 HOH A O   
2242 O O   . HOH D .   ? 0.71793 0.69607 0.43938 0.14067  -0.12865 -0.07058 421 HOH A O   
2243 O O   . HOH D .   ? 1.02206 0.65498 0.49887 0.14433  -0.05793 -0.10921 422 HOH A O   
2244 O O   . HOH D .   ? 0.41127 0.39226 0.32734 0.09895  -0.02358 -0.07650 423 HOH A O   
2245 O O   . HOH D .   ? 0.47146 0.67466 0.44149 0.09720  0.05661  -0.05064 424 HOH A O   
2246 O O   . HOH D .   ? 0.64821 0.68934 0.91012 0.05158  -0.06333 -0.06333 425 HOH A O   
2247 O O   . HOH D .   ? 0.32642 0.31490 0.25548 -0.02230 0.02414  -0.02588 426 HOH A O   
2248 O O   . HOH D .   ? 0.33871 0.49074 0.33392 0.07708  -0.02931 -0.02015 427 HOH A O   
2249 O O   . HOH D .   ? 0.56730 0.50638 0.46357 -0.03860 0.00835  -0.16826 428 HOH A O   
2250 O O   . HOH D .   ? 0.39046 0.49435 0.44640 0.15537  0.11777  0.11156  429 HOH A O   
2251 O O   . HOH D .   ? 0.21730 0.25476 0.19993 0.00137  0.01533  0.00906  430 HOH A O   
2252 O O   . HOH D .   ? 0.59119 0.75442 1.04754 -0.05323 0.10470  -0.15178 431 HOH A O   
2253 O O   . HOH D .   ? 0.34202 0.85813 0.26008 -0.18906 0.01164  -0.01808 432 HOH A O   
2254 O O   . HOH D .   ? 0.23935 0.25659 0.20235 0.00242  0.00048  -0.00039 433 HOH A O   
2255 O O   . HOH D .   ? 0.61097 0.40733 0.41659 0.13990  0.05201  -0.02160 434 HOH A O   
2256 O O   . HOH D .   ? 0.75152 0.43373 0.62817 0.12645  0.01913  -0.22921 435 HOH A O   
2257 O O   . HOH D .   ? 0.31083 0.71812 0.25867 0.04575  0.02481  0.09391  436 HOH A O   
2258 O O   . HOH D .   ? 0.37720 0.38585 0.32152 0.07598  -0.00851 0.04640  437 HOH A O   
2259 O O   . HOH D .   ? 0.63408 0.64379 0.48849 0.19353  0.00676  -0.01295 438 HOH A O   
2260 O O   . HOH D .   ? 0.83913 0.64158 0.40311 0.00643  0.20918  -0.19454 439 HOH A O   
2261 O O   . HOH D .   ? 0.80600 0.46416 0.60807 0.18313  -0.01373 -0.14137 440 HOH A O   
2262 O O   . HOH D .   ? 0.32066 0.28417 0.22503 -0.01071 0.03054  -0.03377 441 HOH A O   
2263 O O   . HOH D .   ? 0.74670 0.66581 0.80532 0.09312  0.27753  0.04413  442 HOH A O   
2264 O O   . HOH D .   ? 0.24625 0.39912 0.40416 -0.00268 -0.02018 0.01911  443 HOH A O   
2265 O O   . HOH D .   ? 0.40989 0.65377 0.36690 0.14364  0.14334  0.05114  444 HOH A O   
2266 O O   . HOH D .   ? 0.51252 0.57233 0.92924 0.19865  0.32834  0.31242  445 HOH A O   
2267 O O   . HOH D .   ? 0.35810 0.33756 0.30944 -0.09229 -0.07814 0.04212  446 HOH A O   
2268 O O   . HOH D .   ? 0.60010 0.39513 0.75782 0.10638  -0.13986 0.06276  447 HOH A O   
2269 O O   . HOH D .   ? 0.18466 0.26077 0.21706 0.02541  -0.00121 -0.01168 448 HOH A O   
2270 O O   . HOH D .   ? 0.74437 0.69981 0.65586 0.05224  0.34214  -0.20748 449 HOH A O   
2271 O O   . HOH D .   ? 0.36634 0.46161 0.34877 -0.01601 0.02818  0.06305  450 HOH A O   
2272 O O   . HOH D .   ? 0.60754 0.56862 1.11842 0.02555  0.44048  0.11896  451 HOH A O   
2273 O O   . HOH D .   ? 0.44095 0.33275 0.48234 0.03665  0.18687  -0.02858 452 HOH A O   
2274 O O   . HOH D .   ? 0.78111 0.54411 0.60199 -0.16237 0.24027  -0.03400 453 HOH A O   
2275 O O   . HOH D .   ? 0.44967 0.39566 0.37927 0.06018  0.01754  -0.03219 454 HOH A O   
2276 O O   . HOH D .   ? 0.67389 0.84894 0.80956 -0.06940 -0.21995 -0.02143 455 HOH A O   
2277 O O   . HOH D .   ? 0.59181 0.76001 0.69928 -0.23869 -0.01327 -0.09035 456 HOH A O   
2278 O O   . HOH D .   ? 0.34348 0.78875 0.37994 0.05290  0.05785  0.01153  457 HOH A O   
2279 O O   . HOH D .   ? 0.51903 0.37422 0.39353 0.00024  -0.00526 -0.09906 458 HOH A O   
2280 O O   . HOH D .   ? 0.52789 0.37910 0.38966 0.09864  0.19262  0.06717  459 HOH A O   
2281 O O   . HOH D .   ? 0.56100 0.72818 0.63959 0.20033  0.19806  0.04721  460 HOH A O   
2282 O O   . HOH D .   ? 0.56826 0.56635 0.72785 -0.04089 0.07685  -0.05918 461 HOH A O   
2283 O O   . HOH D .   ? 0.27816 0.87362 0.39424 0.00550  0.03346  -0.05422 462 HOH A O   
2284 O O   . HOH D .   ? 0.70049 0.54824 0.32132 0.09732  0.01258  -0.01534 463 HOH A O   
2285 O O   . HOH D .   ? 0.22671 0.35795 0.22463 0.02777  -0.01398 0.02028  464 HOH A O   
2286 O O   . HOH D .   ? 0.46688 0.61689 0.79311 -0.03138 0.18964  -0.28763 465 HOH A O   
2287 O O   . HOH D .   ? 0.30973 0.39719 0.23449 -0.02377 0.00859  0.01731  466 HOH A O   
2288 O O   . HOH D .   ? 0.52806 0.90031 0.49611 0.17817  -0.01115 -0.21559 467 HOH A O   
2289 O O   . HOH D .   ? 0.53363 0.57958 0.53429 0.17795  0.08416  0.14597  468 HOH A O   
2290 O O   . HOH D .   ? 0.27278 0.50259 0.45693 0.05452  -0.04219 0.00430  469 HOH A O   
2291 O O   . HOH D .   ? 0.26878 0.41909 0.28710 -0.04147 -0.04079 0.02035  470 HOH A O   
2292 O O   . HOH D .   ? 0.88086 0.74870 1.05813 -0.03156 0.09230  0.06322  471 HOH A O   
2293 O O   . HOH D .   ? 0.54179 0.43094 0.49009 -0.07752 0.14960  -0.05100 472 HOH A O   
2294 O O   . HOH D .   ? 0.42643 0.65716 0.54809 -0.15055 0.02498  0.04862  473 HOH A O   
2295 O O   . HOH D .   ? 0.22668 0.28124 0.24593 -0.00598 -0.00224 0.01930  474 HOH A O   
2296 O O   . HOH D .   ? 0.42744 0.95873 0.38868 0.07534  0.04949  -0.04543 475 HOH A O   
2297 O O   . HOH D .   ? 0.34216 0.40631 0.48194 0.00215  0.01259  -0.05269 476 HOH A O   
2298 O O   . HOH D .   ? 0.59043 0.53684 1.02609 0.20688  0.13668  0.06825  477 HOH A O   
2299 O O   . HOH D .   ? 0.43186 0.87900 0.38153 -0.08907 0.16688  -0.12594 478 HOH A O   
2300 O O   . HOH D .   ? 0.36619 0.64539 0.75629 0.10852  0.05704  -0.06523 479 HOH A O   
2301 O O   . HOH D .   ? 0.60770 0.53726 0.79562 0.03593  -0.08637 -0.03534 480 HOH A O   
2302 O O   . HOH D .   ? 0.46555 0.42309 0.52350 -0.17580 -0.03502 0.14038  481 HOH A O   
2303 O O   . HOH D .   ? 0.38171 0.58471 0.36174 0.01248  -0.05739 0.10250  482 HOH A O   
2304 O O   . HOH D .   ? 0.34319 0.73886 0.69708 -0.00246 -0.16722 -0.06324 483 HOH A O   
2305 O O   . HOH D .   ? 0.68798 0.64011 0.90311 0.06368  0.00953  -0.17800 484 HOH A O   
2306 O O   . HOH D .   ? 0.66604 0.50921 0.35445 0.14677  -0.14403 0.03119  485 HOH A O   
2307 O O   . HOH D .   ? 0.61589 0.65707 0.64030 -0.00618 -0.00411 0.12663  486 HOH A O   
2308 O O   . HOH D .   ? 0.71675 0.44861 0.76673 -0.14992 0.17574  -0.12763 487 HOH A O   
2309 O O   . HOH D .   ? 0.53943 0.59899 0.70469 0.01539  -0.25040 -0.17741 488 HOH A O   
2310 O O   . HOH D .   ? 0.43614 0.65192 0.35197 0.05444  0.13899  -0.07332 489 HOH A O   
2311 O O   . HOH D .   ? 0.26666 0.45149 0.58312 -0.03017 0.05546  -0.13071 490 HOH A O   
2312 O O   . HOH D .   ? 0.66819 0.43958 0.41323 -0.01010 0.22658  -0.02791 491 HOH A O   
2313 O O   . HOH D .   ? 0.74185 0.86276 0.54971 -0.15176 0.17111  0.06276  492 HOH A O   
2314 O O   . HOH D .   ? 0.29305 0.62242 0.50304 -0.01268 0.00797  -0.13649 493 HOH A O   
2315 O O   . HOH D .   ? 0.47174 0.96950 0.47164 0.16785  0.01098  0.04969  494 HOH A O   
2316 O O   . HOH D .   ? 0.60553 0.57041 0.72946 0.06965  -0.37993 -0.14179 495 HOH A O   
2317 O O   . HOH D .   ? 0.81598 0.80856 0.86111 0.05055  0.09751  -0.06333 496 HOH A O   
2318 O O   . HOH D .   ? 0.30311 0.34872 0.32574 0.08418  0.06810  0.07976  497 HOH A O   
2319 O O   . HOH D .   ? 0.64124 0.73030 0.49481 0.24795  0.09450  0.16229  498 HOH A O   
2320 O O   . HOH D .   ? 0.53375 0.74564 0.61711 0.06833  -0.16629 -0.14507 499 HOH A O   
2321 O O   . HOH D .   ? 0.48004 0.94258 0.69347 0.23596  0.18240  -0.00230 500 HOH A O   
2322 O O   . HOH D .   ? 0.88938 0.55444 0.55062 0.19601  -0.19525 -0.07619 501 HOH A O   
2323 O O   . HOH D .   ? 0.69990 0.64374 0.73048 -0.16570 0.20512  0.00809  502 HOH A O   
2324 O O   . HOH D .   ? 0.54822 0.70811 0.40158 -0.03153 0.00034  -0.07493 503 HOH A O   
2325 O O   . HOH D .   ? 0.82147 0.66828 0.55588 0.16879  0.10170  -0.03209 504 HOH A O   
2326 O O   . HOH D .   ? 0.64679 0.69207 0.83569 0.00970  0.13345  -0.06333 505 HOH A O   
2327 O O   . HOH D .   ? 0.69896 1.07515 0.47327 0.14338  -0.11560 0.12757  506 HOH A O   
2328 O O   . HOH D .   ? 0.55812 0.43149 0.43185 0.09204  0.00807  0.06852  507 HOH A O   
2329 O O   . HOH D .   ? 0.43853 0.70001 0.81344 -0.11034 0.03378  0.01167  508 HOH A O   
2330 O O   . HOH D .   ? 0.48182 0.50537 0.34500 0.03127  0.03522  0.03973  509 HOH A O   
2331 O O   . HOH D .   ? 0.86505 0.78567 0.79064 0.14415  0.07641  0.01933  510 HOH A O   
2332 O O   . HOH D .   ? 0.62103 0.70414 0.51191 0.03023  0.18276  0.02380  511 HOH A O   
2333 O O   . HOH D .   ? 0.79018 0.87871 0.35203 0.25933  -0.00111 0.13985  512 HOH A O   
2334 O O   . HOH D .   ? 0.42917 0.65983 0.79707 -0.10642 -0.22861 0.00659  513 HOH A O   
2335 O O   . HOH D .   ? 0.59123 0.74461 0.36081 -0.00634 0.15942  -0.06333 514 HOH A O   
2336 O O   . HOH D .   ? 0.43479 0.34952 0.30318 0.08307  0.08667  -0.00686 515 HOH A O   
2337 O O   . HOH D .   ? 0.39979 0.68480 0.75064 0.08238  0.07512  0.05680  516 HOH A O   
2338 O O   . HOH D .   ? 0.67130 0.95979 0.47352 0.29000  0.04734  0.18591  517 HOH A O   
2339 O O   . HOH D .   ? 0.79266 0.66046 0.76003 -0.04494 -0.19942 0.12100  518 HOH A O   
2340 O O   . HOH D .   ? 0.93551 0.52380 0.63377 0.15844  0.29646  0.09901  519 HOH A O   
2341 O O   . HOH D .   ? 0.61392 0.77199 1.07384 0.29139  -0.06122 -0.06333 520 HOH A O   
2342 O O   . HOH D .   ? 0.51814 0.41067 0.55599 -0.09309 -0.09193 0.01868  521 HOH A O   
2343 O O   . HOH D .   ? 0.38565 0.47432 0.38652 0.14509  -0.02295 0.00806  522 HOH A O   
2344 O O   . HOH D .   ? 0.66248 0.90985 0.50337 0.21416  -0.14662 0.11437  523 HOH A O   
2345 O O   . HOH D .   ? 0.59445 0.74448 0.54989 0.23079  0.17651  0.17880  524 HOH A O   
2346 O O   . HOH D .   ? 0.50179 0.61647 0.77060 0.07617  -0.12663 0.00781  525 HOH A O   
2347 O O   . HOH D .   ? 0.85981 0.73277 1.00915 -0.01368 -0.06333 -0.06333 526 HOH A O   
2348 O O   . HOH D .   ? 0.38219 0.62116 0.47332 0.01470  0.08874  0.02027  527 HOH A O   
2349 O O   . HOH D .   ? 0.39569 0.65996 0.48813 -0.02560 -0.05623 0.22183  528 HOH A O   
2350 O O   . HOH D .   ? 0.78071 0.56995 0.90132 0.03425  0.01800  0.17002  529 HOH A O   
2351 O O   . HOH D .   ? 0.29973 0.38080 0.49245 0.00494  -0.05103 0.09047  530 HOH A O   
2352 O O   . HOH D .   ? 0.40452 0.77215 0.69615 -0.12831 0.05534  0.03136  531 HOH A O   
2353 O O   . HOH D .   ? 0.89454 0.62549 0.77743 0.14326  0.16855  0.22983  532 HOH A O   
2354 O O   . HOH D .   ? 0.69222 0.59728 0.58289 -0.05243 0.14242  -0.12373 533 HOH A O   
2355 O O   . HOH D .   ? 0.67435 0.80173 0.51123 0.20616  0.29657  0.04239  534 HOH A O   
# 
