data_8QGC
# 
_entry.id   8QGC 
# 
_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   8QGC         pdb_00008qgc 10.2210/pdb8qgc/pdb 
WWPDB D_1292133132 ?            ?                   
# 
_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                        8QGC 
_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-phenyl-urea
;
701.692   1  ?        ? ? ? 
4 water       nat water 18.015    31 ?        ? ? ? 
# 
_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-phenyl-urea
;
UYP 
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 
UYP 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-phenyl-urea
;
? 'C31 H35 N13 O7' 701.692 
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 ?   ?   ?   A . n 
A 1 111 ILE 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 LYS 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ASP 264 264 ?   ?   ?   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        UYP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UYP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CIT 1  301 1  CIT CIT A . 
C 3 UYP 1  302 1  UYP DRG A . 
D 4 HOH 1  401 9  HOH HOH A . 
D 4 HOH 2  402 7  HOH HOH A . 
D 4 HOH 3  403 1  HOH HOH A . 
D 4 HOH 4  404 28 HOH HOH A . 
D 4 HOH 5  405 31 HOH HOH A . 
D 4 HOH 6  406 10 HOH HOH A . 
D 4 HOH 7  407 13 HOH HOH A . 
D 4 HOH 8  408 39 HOH HOH A . 
D 4 HOH 9  409 18 HOH HOH A . 
D 4 HOH 10 410 33 HOH HOH A . 
D 4 HOH 11 411 11 HOH HOH A . 
D 4 HOH 12 412 5  HOH HOH A . 
D 4 HOH 13 413 6  HOH HOH A . 
D 4 HOH 14 414 16 HOH HOH A . 
D 4 HOH 15 415 8  HOH HOH A . 
D 4 HOH 16 416 42 HOH HOH A . 
D 4 HOH 17 417 4  HOH HOH A . 
D 4 HOH 18 418 21 HOH HOH A . 
D 4 HOH 19 419 12 HOH HOH A . 
D 4 HOH 20 420 25 HOH HOH A . 
D 4 HOH 21 421 27 HOH HOH A . 
D 4 HOH 22 422 19 HOH HOH A . 
D 4 HOH 23 423 32 HOH HOH A . 
D 4 HOH 24 424 22 HOH HOH A . 
D 4 HOH 25 425 40 HOH HOH A . 
D 4 HOH 26 426 24 HOH HOH A . 
D 4 HOH 27 427 34 HOH HOH A . 
D 4 HOH 28 428 17 HOH HOH A . 
D 4 HOH 29 429 41 HOH HOH A . 
D 4 HOH 30 430 36 HOH HOH A . 
D 4 HOH 31 431 20 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A LYS 114 ? CG  ? A LYS 114 CG  
6  1 Y 1 A LYS 114 ? CD  ? A LYS 114 CD  
7  1 Y 1 A LYS 114 ? CE  ? A LYS 114 CE  
8  1 Y 1 A LYS 114 ? NZ  ? A LYS 114 NZ  
9  1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
10 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
11 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
12 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
13 1 Y 1 A ARG 247 ? CG  ? A ARG 247 CG  
14 1 Y 1 A ARG 247 ? CD  ? A ARG 247 CD  
15 1 Y 1 A ARG 247 ? NE  ? A ARG 247 NE  
16 1 Y 1 A ARG 247 ? CZ  ? A ARG 247 CZ  
17 1 Y 1 A ARG 247 ? NH1 ? A ARG 247 NH1 
18 1 Y 1 A ARG 247 ? NH2 ? A ARG 247 NH2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           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                     8QGC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.107 
_cell.length_a_esd                 ? 
_cell.length_b                     74.728 
_cell.length_b_esd                 ? 
_cell.length_c                     118.239 
_cell.length_c_esd                 ? 
_cell.volume                       557598.513 
_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                         8QGC 
_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                   8QGC 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.21 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-11-07 
_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   0.97625 
_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 ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          45.50 
_reflns.entry_id                                       8QGC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.29 
_reflns.d_resolution_low                               48.21 
_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                                     12864 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_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                                0.076 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       59712 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.29 
_reflns_shell.d_res_low                                     2.37 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           5744 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1238 
_reflns_shell.percent_possible_obs                          99.2 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.883 
_reflns_shell.pdbx_Rpim_I_all                               0.398 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.768 
_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                                  0.784 
_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                               64.71 
_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                                 8QGC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.29 
_refine.ls_d_res_low                             48.21 
_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                     12851 
_refine.ls_number_reflns_R_free                  623 
_refine.ls_number_reflns_R_work                  12228 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.13 
_refine.ls_percent_reflns_R_free                 4.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2268 
_refine.ls_R_factor_R_free                       0.2421 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2260 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      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                 31.8796 
_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                            0.3026 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.29 
_refine_hist.d_res_low                        48.21 
_refine_hist.number_atoms_solvent             31 
_refine_hist.number_atoms_total               2155 
_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        2060 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0104  ? 2196 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4331  ? 2980 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0927  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0071  ? 376  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.9683 ? 798  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.29 2.52  . . 156 3013 99.37 . . . . 0.3201 . . . . . . . . . . . 0.3616 
'X-RAY DIFFRACTION' 2.52 2.89  . . 150 3025 99.37 . . . . 0.2922 . . . . . . . . . . . 0.3044 
'X-RAY DIFFRACTION' 2.89 3.63  . . 151 3045 99.29 . . . . 0.2371 . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 3.64 48.21 . . 166 3145 98.51 . . . . 0.1909 . . . . . . . . . . . 0.1981 
# 
_struct.entry_id                     8QGC 
_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        8QGC 
_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              8QGC 
_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 8QGC LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGC GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGC HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGC HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGC HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGC HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGC HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGC HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D 
1 2 A,B,C,D 
1 3 A,B,C,D 
1 4 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 63.1070000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 63.1070000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLU A 26  ? ASP A 10  GLU A 26  1 ? 17 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 58  ? GLU A 61  ? ARG A 58  GLU A 61  5 ? 4  
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 ? 6 ? 
AA2 ? 7 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 3   ? SER A 7   ? TYR A 3   SER A 7   
AA1 2 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 3 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA1 4 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA1 5 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA1 6 ALA A 116 ? ALA A 120 ? ALA A 116 ALA A 120 
AA2 1 TYR A 3   ? SER A 7   ? TYR A 3   SER A 7   
AA2 2 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA2 3 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 4 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 5 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 6 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 7 ILE A 142 ? GLY A 149 ? ILE A 142 GLY A 149 
AA3 1 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 2 ALA A 178 ? MET A 184 ? ALA A 178 MET A 184 
AA3 3 GLY A 151 ? SER A 155 ? GLY A 151 SER A 155 
AA3 4 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 5 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 6 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N MET A 4   ? N MET A 4   O ILE A 40  ? O ILE A 40  
AA1 2 3 N GLY A 43  ? N GLY A 43  O ILE A 67  ? O ILE A 67  
AA1 3 4 N PHE A 64  ? N PHE A 64  O ALA A 246 ? O ALA A 246 
AA1 4 5 O PHE A 245 ? O PHE A 245 N VAL A 98  ? N VAL A 98  
AA1 5 6 N VAL A 107 ? N VAL A 107 O ALA A 116 ? O ALA A 116 
AA2 1 2 N MET A 4   ? N MET A 4   O ILE A 40  ? O ILE A 40  
AA2 2 3 N GLY A 43  ? N GLY A 43  O ILE A 67  ? O ILE A 67  
AA2 3 4 N PHE A 64  ? N PHE A 64  O ALA A 246 ? O ALA A 246 
AA2 4 5 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA2 5 6 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 6 7 N VAL A 137 ? N VAL A 137 O PHE A 144 ? O PHE A 144 
AA3 1 2 O PHE A 201 ? O PHE A 201 N MET A 179 ? N MET A 179 
AA3 2 3 O GLN A 180 ? O GLN A 180 N SER A 155 ? N SER A 155 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N THR A 125 ? N THR A 125 O SER A 220 ? O SER A 220 
AA3 5 6 N PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QGC 
_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 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PHE 
_pdbx_validate_rmsd_bond.auth_seq_id_1             253 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PHE 
_pdbx_validate_rmsd_bond.auth_seq_id_2             253 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.394 
_pdbx_validate_rmsd_bond.bond_target_value         1.509 
_pdbx_validate_rmsd_bond.bond_deviation            -0.115 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.017 
_pdbx_validate_rmsd_bond.linker_flag               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 ASP A 28  ? ? -118.44 75.07   
2 1 ASP A 77  ? ? -108.00 57.24   
3 1 GLU A 94  ? ? 49.94   24.57   
4 1 ASN A 122 ? ? -100.28 -60.17  
5 1 ALA A 162 ? ? -102.81 -129.40 
6 1 HIS A 204 ? ? 78.13   -11.98  
7 1 VAL A 212 ? ? -97.89  -61.09  
8 1 ASN A 213 ? ? -119.88 -79.21  
# 
_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     416 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 8.91708553865 21.9237542697 28.3854240236  0.727709029808 ? 0.0575876028935   ? 0.0427894611506   
? 0.9188714457   ? -0.114441387968  ? 0.567914252296 ? 4.37012715623 ? -0.810763671494 ? -1.02391263216  ? 2.40693833699  ? 
2.03013878373    ? 5.60266676327 ? -0.16148602569    ? -0.889776138479 ? -0.128957178736 ? -0.0730548829557 ? 0.0888746835747  ? 
0.67799014613   ? -0.320130220065 ? -0.338175739812  ? 0.0869280055011   ? 
2 'X-RAY DIFFRACTION' ? refined 7.00162258504 32.9274074258 25.1310220681  0.969758080135 ? 0.21367893135     ? 0.134504833648    
? 1.34893237589  ? -0.277123685483  ? 0.851053672233 ? 3.36371389203 ? -1.19477220255  ? -1.27836360164  ? 2.14502977522  ? 
-1.73954741349   ? 3.29873704986 ? 0.487079034653    ? -0.997187427154 ? 1.20986280195   ? 0.406082475948   ? -0.0943718478109 ? 
-0.138599423923 ? -1.52036513083  ? -0.703826220509  ? 0.0555000923023   ? 
3 'X-RAY DIFFRACTION' ? refined 12.3756680922 23.3123228774 15.7165833731  0.598866072461 ? 0.138107710774    ? 0.0310022242107   
? 0.62692512927  ? -0.0869101860576 ? 0.507310943914 ? 4.02074849529 ? 0.17755297262   ? -1.63254404674  ? 2.3951799894   ? 
1.97045268101    ? 5.45729035042 ? 0.192138968532    ? -0.19806171048  ? 0.602056372824  ? 0.0513699180876  ? -0.321085336059  ? 
0.0617751444237 ? -0.693214613018 ? -0.0582816507847 ? -0.00587704947684 ? 
4 'X-RAY DIFFRACTION' ? refined 20.5176615044 21.4912362797 26.4041179403  0.636303115865 ? 0.106164455909    ? 0.0908479144486   
? 0.995259039125 ? -0.200530067702  ? 0.730874742103 ? 4.08494515573 ? -1.53517835947  ? -1.75804333252  ? 0.985640200419 ? 
1.3284647553     ? 5.45024898635 ? 0.0830239398598   ? -1.47156046057  ? 1.53559499243   ? 0.416128770995   ? 1.21017996191    ? 
-0.958166034279 ? -0.902983018315 ? 1.04833863759    ? -0.0744877013089  ? 
5 'X-RAY DIFFRACTION' ? refined 17.5888498522 15.0260031867 -2.23800367688 0.28198042254  ? 0.0544073758215   ? 0.029434438253    
? 0.395033121462 ? 0.0147967208706  ? 0.352219146775 ? 1.60109531333 ? -1.1589946416   ? -0.245765070232 ? 2.45073250196  ? 
0.510045500707   ? 4.32716589803 ? 0.181584678748    ? 0.0851612867906 ? 0.129717604731  ? -0.140270072675  ? -0.161487494068  ? 
0.151415481471  ? -0.432172976358 ? -0.407129886483  ? 0.0374846193069   ? 
6 'X-RAY DIFFRACTION' ? refined 18.326581716  11.94877038   -6.16373369113 0.371429525125 ? 0.0856910625453   ? -0.00888820101884 
? 0.463985001936 ? 0.0148188483746  ? 0.405853478992 ? 2.22778566679 ? -0.274230066744 ? -0.361153570497 ? 1.55631304225  ? 
-0.57679600604   ? 3.93993813369 ? 0.0412121848436   ? 0.155801781481  ? 0.203323404222  ? -0.186362406097  ? -0.107873746748  ? 
0.48264937469   ? -0.165626259784 ? -0.526180244523  ? 0.0546864588221   ? 
7 'X-RAY DIFFRACTION' ? refined 27.170091136  19.8620334318 15.929494779   0.537378556491 ? -0.00883667731307 ? 0.0796281605762   
? 0.464350921085 ? -0.0784801792177 ? 0.440138692128 ? 3.22310381529 ? -1.40359287597  ? 0.556856588888  ? 2.36923928943  ? 
-0.0371913668249 ? 3.63691086505 ? -0.00541049165036 ? -0.305782065887 ? 0.471067727468  ? 0.4839807902     ? -0.173578182704  ? 
-0.13523920397  ? -0.603047283346 ? 0.083649942019   ? 0.00669779791012  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 1   ? A 25  A 25  ? ? 
;chain 'A' and (resid    1  through   25 )
;
2 'X-RAY DIFFRACTION' 2 A 26  A 26  ? A 37  A 37  ? ? 
;chain 'A' and (resid   26  through   37 )
;
3 'X-RAY DIFFRACTION' 3 A 38  A 38  ? A 68  A 68  ? ? 
;chain 'A' and (resid   38  through   68 )
;
4 'X-RAY DIFFRACTION' 4 A 69  A 69  ? A 92  A 92  ? ? 
;chain 'A' and (resid   69  through   92 )
;
5 'X-RAY DIFFRACTION' 5 A 93  A 93  ? A 163 A 167 ? ? 
;chain 'A' and (resid   93  through  167 )
;
6 'X-RAY DIFFRACTION' 6 A 164 A 168 ? A 234 A 238 ? ? 
;chain 'A' and (resid  168  through  238 )
;
7 'X-RAY DIFFRACTION' 7 A 235 A 239 ? A 259 A 263 ? ? 
;chain 'A' and (resid  239  through  263 )
;
# 
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 GLY 110 ? A GLY 110 
2  1 Y 1 A ILE 111 ? A ILE 111 
3  1 Y 1 A GLY 112 ? A GLY 112 
4  1 Y 1 A LYS 113 ? A LYS 113 
5  1 Y 1 A ASP 264 ? A ASP 264 
6  1 Y 1 A LEU 265 ? A LEU 265 
7  1 Y 1 A GLU 266 ? A GLU 266 
8  1 Y 1 A HIS 267 ? A HIS 267 
9  1 Y 1 A HIS 268 ? A HIS 268 
10 1 Y 1 A HIS 269 ? A HIS 269 
11 1 Y 1 A HIS 270 ? A HIS 270 
12 1 Y 1 A HIS 271 ? A HIS 271 
13 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 
UYP C4   C Y N 393 
UYP C5   C Y N 394 
UYP C6   C Y N 395 
UYP C8   C Y N 396 
UYP N1   N Y N 397 
UYP N3   N Y N 398 
UYP C2   C Y N 399 
UYP CAA  C N N 400 
UYP CAC  C N N 401 
UYP CAD  C N N 402 
UYP CAE  C N N 403 
UYP CAP  C N R 404 
UYP CAR  C N R 405 
UYP CAS  C N N 406 
UYP CAU  C N N 407 
UYP CAX  C Y N 408 
UYP CAY  C Y N 409 
UYP CAZ  C Y N 410 
UYP CBA  C Y N 411 
UYP CBB  C Y N 412 
UYP CBC  C Y N 413 
UYP CBD  C N S 414 
UYP CBF  C N R 415 
UYP CBH  C N N 416 
UYP CBI  C N R 417 
UYP CBK  C N R 418 
UYP CBL  C N R 419 
UYP CBN  C N S 420 
UYP CBQ  C Y N 421 
UYP CBS  C Y N 422 
UYP CBT  C Y N 423 
UYP CBV  C Y N 424 
UYP CBX  C Y N 425 
UYP N6   N N N 426 
UYP N7   N Y N 427 
UYP N9   N Y N 428 
UYP NAB  N N N 429 
UYP NAT  N N N 430 
UYP NAW  N N N 431 
UYP NBP  N Y N 432 
UYP NBR  N Y N 433 
UYP NBU  N Y N 434 
UYP NBW  N Y N 435 
UYP NBY  N N N 436 
UYP OAQ  O N N 437 
UYP OAV  O N N 438 
UYP OBE  O N N 439 
UYP OBG  O N N 440 
UYP OBJ  O N N 441 
UYP OBM  O N N 442 
UYP OBO  O N N 443 
UYP H1   H N N 444 
UYP H2   H N N 445 
UYP H3   H N N 446 
UYP H4   H N N 447 
UYP H5   H N N 448 
UYP H6   H N N 449 
UYP H7   H N N 450 
UYP H8   H N N 451 
UYP H9   H N N 452 
UYP H10  H N N 453 
UYP H11  H N N 454 
UYP H12  H N N 455 
UYP H13  H N N 456 
UYP H14  H N N 457 
UYP H15  H N N 458 
UYP H16  H N N 459 
UYP H17  H N N 460 
UYP H18  H N N 461 
UYP H19  H N N 462 
UYP H20  H N N 463 
UYP H21  H N N 464 
UYP H22  H N N 465 
UYP H23  H N N 466 
UYP H24  H N N 467 
UYP H25  H N N 468 
UYP H26  H N N 469 
UYP H27  H N N 470 
UYP H29  H N N 471 
UYP H30  H N N 472 
UYP H31  H N N 473 
UYP H32  H N N 474 
UYP H33  H N N 475 
UYP H34  H N N 476 
UYP H35  H N N 477 
UYP H36  H N N 478 
VAL N    N N N 479 
VAL CA   C N S 480 
VAL C    C N N 481 
VAL O    O N N 482 
VAL CB   C N N 483 
VAL CG1  C N N 484 
VAL CG2  C N N 485 
VAL OXT  O N N 486 
VAL H    H N N 487 
VAL H2   H N N 488 
VAL HA   H N N 489 
VAL HB   H N N 490 
VAL HG11 H N N 491 
VAL HG12 H N N 492 
VAL HG13 H N N 493 
VAL HG21 H N N 494 
VAL HG22 H N N 495 
VAL HG23 H N N 496 
VAL HXT  H N N 497 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
UYP NBY CBX  sing N N 378 
UYP NBR CBQ  doub Y N 379 
UYP NBR CBS  sing Y N 380 
UYP CBQ NBP  sing Y N 381 
UYP CBX CBS  doub Y N 382 
UYP CBX NBW  sing Y N 383 
UYP CBS CBT  sing Y N 384 
UYP CBL OBM  sing N N 385 
UYP CBL CBN  sing N N 386 
UYP CBL CBK  sing N N 387 
UYP OBO CBN  sing N N 388 
UYP NBP CBT  sing Y N 389 
UYP NBP CBK  sing N N 390 
UYP NBW CBV  doub Y N 391 
UYP CBT NBU  doub Y N 392 
UYP CBN CBI  sing N N 393 
UYP CBK OBJ  sing N N 394 
UYP CBV NBU  sing Y N 395 
UYP CAZ CBA  doub Y N 396 
UYP CAZ CAY  sing Y N 397 
UYP CBA CBB  sing Y N 398 
UYP OBJ CBI  sing N N 399 
UYP CAY CAX  doub Y N 400 
UYP CBI CBH  sing N N 401 
UYP CBB CBC  doub Y N 402 
UYP CBH NAB  sing N N 403 
UYP CAX CBC  sing Y N 404 
UYP CAX NAW  sing N N 405 
UYP N6  C6   sing N N 406 
UYP NAW CAU  sing N N 407 
UYP C6  N1   doub Y N 408 
UYP C6  C5   sing Y N 409 
UYP N1  C2   sing Y N 410 
UYP N7  C5   sing Y N 411 
UYP N7  C8   doub Y N 412 
UYP NAB CAA  sing N N 413 
UYP NAB CAC  sing N N 414 
UYP C5  C4   doub Y N 415 
UYP CAU NAT  sing N N 416 
UYP CAU OAV  doub N N 417 
UYP C2  N3   doub Y N 418 
UYP C8  CAE  sing N N 419 
UYP C8  N9   sing Y N 420 
UYP CAE CAD  trip N N 421 
UYP CAD CAC  sing N N 422 
UYP C4  N3   sing Y N 423 
UYP C4  N9   sing Y N 424 
UYP NAT CAS  sing N N 425 
UYP N9  CAP  sing N N 426 
UYP OAQ CAP  sing N N 427 
UYP OAQ CAR  sing N N 428 
UYP CAP CBF  sing N N 429 
UYP CAS CAR  sing N N 430 
UYP CAR CBD  sing N N 431 
UYP CBF CBD  sing N N 432 
UYP CBF OBG  sing N N 433 
UYP CBD OBE  sing N N 434 
UYP C2  H1   sing N N 435 
UYP CAA H2   sing N N 436 
UYP CAA H3   sing N N 437 
UYP CAA H4   sing N N 438 
UYP CAC H5   sing N N 439 
UYP CAC H6   sing N N 440 
UYP CAP H7   sing N N 441 
UYP CAR H8   sing N N 442 
UYP CAS H9   sing N N 443 
UYP CAS H10  sing N N 444 
UYP CAY H11  sing N N 445 
UYP CAZ H12  sing N N 446 
UYP CBA H13  sing N N 447 
UYP CBB H14  sing N N 448 
UYP CBC H15  sing N N 449 
UYP CBD H16  sing N N 450 
UYP CBF H17  sing N N 451 
UYP CBH H18  sing N N 452 
UYP CBH H19  sing N N 453 
UYP CBI H20  sing N N 454 
UYP CBK H21  sing N N 455 
UYP CBL H22  sing N N 456 
UYP CBN H23  sing N N 457 
UYP CBQ H24  sing N N 458 
UYP CBV H25  sing N N 459 
UYP N6  H26  sing N N 460 
UYP N6  H27  sing N N 461 
UYP NAT H29  sing N N 462 
UYP NAW H30  sing N N 463 
UYP NBY H31  sing N N 464 
UYP NBY H32  sing N N 465 
UYP OBE H33  sing N N 466 
UYP OBG H34  sing N N 467 
UYP OBM H35  sing N N 468 
UYP OBO H36  sing N N 469 
VAL N   CA   sing N N 470 
VAL N   H    sing N N 471 
VAL N   H2   sing N N 472 
VAL CA  C    sing N N 473 
VAL CA  CB   sing N N 474 
VAL CA  HA   sing N N 475 
VAL C   O    doub N N 476 
VAL C   OXT  sing N N 477 
VAL CB  CG1  sing N N 478 
VAL CB  CG2  sing N N 479 
VAL CB  HB   sing N N 480 
VAL CG1 HG11 sing N N 481 
VAL CG1 HG12 sing N N 482 
VAL CG1 HG13 sing N N 483 
VAL CG2 HG21 sing N N 484 
VAL CG2 HG22 sing N N 485 
VAL CG2 HG23 sing N N 486 
VAL OXT HXT  sing N N 487 
# 
_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                    8QGC 
_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]   0.015846 
_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]   0.013382 
_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]   0.008457 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 11.30512 36.58898 25.97683  1.000 110.49156 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.93399 36.61692 24.56806  1.000 110.23968 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 10.10419 35.39020 24.22173  1.000 105.71348 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 10.26371 34.33888 24.83813  1.000 102.98607 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 12.18074 36.70062 23.68536  1.000 111.22012 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 13.28439 35.71710 24.03032  0.770 109.48200 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.81271 36.14816 23.18029  0.730 111.53422 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.67568 37.04564 24.46709  0.910 114.04987 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.21321  35.52836 23.24129  1.000 102.77200 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.29243  34.44642 22.92421  1.000 97.65451  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 9.04354  33.14970 22.67590  1.000 91.80889  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 10.17491 33.14438 22.18140  1.000 91.72161  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.43472  34.81276 21.72323  1.000 98.74279  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.45341  35.87975 22.07960  1.000 102.04709 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.61788  36.26093 20.91127  0.870 103.75502 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.64662  37.32856 21.31901  1.000 106.12153 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.84221  37.71297 20.14617  0.970 107.82966 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.41164  32.04527 23.06133  1.000 87.24603  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.08680  30.75985 23.06916  1.000 81.09146  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 8.03604  29.66290 23.07531  1.000 77.90020  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.88770  29.88118 23.47017  1.000 78.93602  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.03302 30.63668 24.27567  1.000 79.32875  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.39079  30.18057 25.57939  1.000 78.40269  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.81041  31.09065 26.45847  1.000 80.47537  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.39426  28.83854 25.94169  1.000 76.18315  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.23410  30.67052 27.65225  1.000 80.64099  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.81355  28.41020 27.12285  1.000 76.79067  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.24093  29.33071 27.97913  1.000 78.87674  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.67081  28.91329 29.16276  1.000 79.67747  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.44099  28.48302 22.60786  1.000 74.10044  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.60376  27.29446 22.71163  1.000 72.27693  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.49050  26.05984 22.78729  1.000 69.65683  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.66018  26.08583 22.39210  1.000 69.23617  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.61562  27.17178 21.54320  1.000 73.41061  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.13286  26.38212 20.34397  1.000 71.86677  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 6.96758  24.58135 20.47145  1.000 70.21463  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.24377  24.41606 20.92752  1.000 72.30392  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.89355  24.96826 23.27622  1.000 68.71588  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.60160  23.75414 23.65844  1.000 67.89067  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.76389  22.54165 23.29576  1.000 68.95148  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.57671  22.46123 23.64272  1.000 71.15082  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.89655  23.72948 25.16506  1.000 67.71918  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.65447  24.98432 25.63964  1.000 67.82632  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.70534  22.49771 25.53377  1.000 66.88280  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.92132  24.98072 27.12232  1.000 68.05365  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.39736  21.58398 22.61456  1.000 68.40213  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.76190  20.41319 22.03093  1.000 68.96487  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.22569  19.16596 22.76380  1.000 67.91491  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.37392  19.12918 23.24519  1.000 66.32239  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 8.13225  20.28641 20.54593  1.000 69.63165  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 7.80070  21.49989 19.86919  1.000 71.37894  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.45920  19.09876 19.87740  1.000 70.60192  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.36266  18.13251 22.84112  1.000 67.93425  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 7.85577  17.02628 23.62759  1.000 67.91890  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.71020  15.71869 22.88403  1.000 68.86432  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.74117  15.52344 22.15103  1.000 70.26531  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.19020  17.03671 24.99723  1.000 69.36517  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.39321  15.82732 25.68174  1.000 71.25687  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.70419  14.83868 23.07372  1.000 69.07664  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.58549  13.46258 22.61366  1.000 68.95691  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.32979  12.82000 23.17840  1.000 71.32530  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.73353  11.94675 22.54021  1.000 72.24198  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.83523  12.66773 23.01412  1.000 67.63769  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.82350  11.16884 22.65274  1.000 68.75068  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.67470 10.34592 23.63467  1.000 69.84605  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 11.29584 9.11653  22.98103  0.790 71.46226  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 12.13244 9.52106  21.82161  0.720 70.30437  ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.89572  13.25665 24.35700  1.000 72.90951  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.63210  12.81932 24.90055  1.000 77.09558  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.69695  11.59770 25.78545  1.000 81.15794  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.64598  11.13626 26.25032  1.000 84.35893  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.88267  11.03835 26.00839  1.000 82.02553  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.04171  10.09653 27.09885  1.000 85.64907  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.13164  10.86442 28.41505  1.000 86.33228  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.18662  12.09614 28.44666  1.000 84.27454  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.27189  9.20863  26.88748  1.000 85.35986  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.58103  9.98273  26.93960  1.000 82.51236  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.55102  11.22986 26.91018  0.880 80.49275  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.64818 9.33680  27.00956  0.870 82.74330  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.16163  10.11587 29.51208  1.000 90.65084  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.08070  10.72444 30.83448  1.000 91.19476  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.26020  11.65111 31.11087  1.000 87.35347  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.07959  12.77472 31.59550  1.000 86.18970  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.01896  9.62214  31.87341  1.000 96.02812  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 6.64258  10.07138 33.23243  1.000 98.86258  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 6.19529  8.89914  34.03671  0.670 104.62295 ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.21635  7.78440  33.47399  1.000 106.62080 ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 5.82174  9.08015  35.20953  0.960 108.06702 ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.48012  11.18207 30.82125  1.000 84.45570  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.69684 11.93154 31.14268  1.000 80.96393  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.67964 13.31989 30.51265  1.000 76.48063  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 11.05021 14.30920 31.15952  1.000 76.45131  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.92338 11.13436 30.67019  1.000 81.62253  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.32923 11.70097 31.01250  0.890 81.41391  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.43272 10.82289 30.37098  1.000 81.91729  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.89912 11.28802 30.57173  0.840 81.02421  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 16.17694 12.41992 31.50487  0.900 80.60831  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.22464 13.41021 29.25816  1.000 73.26604  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.27270 14.64582 28.47972  1.000 69.61241  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.13171  15.59900 28.79965  1.000 69.11915  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.30644  16.81867 28.69267  1.000 67.93196  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.22906 14.33451 26.98358  1.000 68.53191  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.31354 13.51985 26.58434  1.000 68.39705  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.94815  15.07959 29.12506  1.000 70.35149  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.85900  15.97364 29.49652  1.000 71.04598  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.17706  16.70151 30.79417  1.000 71.83754  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.89344  17.89751 30.92968  1.000 71.19943  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.55199  15.19577 29.61613  1.000 72.27716  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.89003  14.97448 28.27860  1.000 71.74365  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.36004  15.56346 27.28416  1.000 69.14057  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.90318  14.21530 28.22502  0.840 73.67967  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.77889  15.98818 31.74976  1.000 73.31838  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.17791  16.59017 33.01806  1.000 74.62839  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.17542  17.71049 32.80571  1.000 71.27574  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.02203  18.82122 33.33026  1.000 71.15381  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.80987  15.53039 33.91062  1.000 77.92925  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.97465  14.92901 35.01769  1.000 82.39459  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 8.86941  14.79628 36.22815  1.000 83.59465  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 6.76474  15.79622 35.30645  1.000 83.52014  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.25361 17.39781 32.09152  1.000 68.94842  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.27621 18.38835 31.81319  1.000 66.92556  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.68673 19.60060 31.10729  1.000 65.15347  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 11.15407 20.73108 31.30135  1.000 65.36369  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.37719 17.73692 30.98608  1.000 66.58330  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.49951 18.62952 30.49421  1.000 66.25014  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 13.93621 19.58416 31.58326  1.000 67.82728  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.64838 17.75632 30.08111  1.000 65.96672  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.63245  19.38991 30.32118  1.000 63.96584  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.00049  20.50701 29.63816  1.000 62.96357  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.28338  21.42939 30.61759  1.000 64.15782  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.40424  22.65821 30.52320  1.000 60.72935  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.03467  19.98882 28.58346  1.000 62.22392  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.19226  21.08777 28.01216  1.000 62.29517  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.46855  20.65312 26.76885  1.000 62.20694  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.54505  21.69762 26.34853  1.000 62.93911  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.30159  21.81683 26.79487  1.000 64.63822  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.78973  20.94376 27.65173  1.000 65.59853  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.55580  22.83689 26.37607  1.000 65.57437  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.53039  20.85481 31.56044  1.000 65.44139  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.80592  21.68542 32.51505  1.000 66.46796  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.77163  22.44813 33.42296  1.000 65.65037  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.55140  23.63086 33.71433  1.000 65.30619  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.82480  20.82125 33.31482  1.000 66.67751  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.70958  20.13701 32.50192  1.000 67.35164  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.90322  19.15831 33.35198  1.000 69.98928  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.77625  21.14909 31.83615  1.000 67.77519  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.86605  21.80692 33.85098  1.000 64.82559  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.84059  22.50382 34.69030  1.000 65.13539  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.52705 23.65098 33.94700  1.000 64.13091  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.87921 24.66021 34.56876  1.000 64.86247  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.87999 21.51840 35.23699  1.000 65.21222  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.36276 20.70842 36.42410  1.000 67.87483  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.54839  21.18800 37.21490  1.000 70.21188  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 10.85053 19.47829 36.55834  1.000 67.97217  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.72137 23.53102 32.62769  1.000 62.68117  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.31636 24.63559 31.87536  1.000 62.28983  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.35037 25.81586 31.78287  1.000 63.85717  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.73982 26.96648 32.01743  1.000 65.12503  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.76226 24.16674 30.47965  1.000 60.87732  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.11619 23.43035 30.46417  1.000 60.18240  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.91691 23.21418 28.84565  0.800 58.37701  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.46574 24.87732 28.46411  0.500 58.83852  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.07880  25.54394 31.46738  1.000 64.48659  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.06309  26.59669 31.40981  1.000 66.53394  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 7.95908  27.33003 32.74197  1.000 65.92043  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.81537  28.55855 32.77775  1.000 67.29538  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.70460  26.00503 30.98788  1.000 67.51592  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.74139  25.57225 29.52633  1.000 62.97078  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.57737  27.00778 31.20699  1.000 66.78405  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.59529  24.67755 29.13950  1.000 63.55192  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.01362  26.59677 33.85714  1.000 76.97706  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 7.96705  27.25359 35.15946  1.000 78.42751  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.16439  28.17562 35.34062  1.000 78.24141  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.01468  29.33190 35.75021  1.000 79.05981  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.90478  26.21360 36.27674  1.000 69.53385  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.36304 27.67868 35.02763  1.000 75.24743  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.54408 28.52091 35.09280  1.000 76.31926  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.44731 29.72660 34.18175  1.000 75.21773  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.89269 30.81584 34.53585  1.000 77.23123  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.86121 29.54922 32.99686  1.000 72.70378  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.61167 30.69238 32.12647  1.000 73.31244  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.63880  31.67300 32.75865  1.000 76.08937  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.75087  32.88706 32.54507  1.000 78.51426  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.07427 30.21911 30.78337  1.000 71.79973  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.14009 29.79086 29.83292  1.000 70.36780  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.17787 30.64488 29.51124  1.000 71.17897  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.12274 28.52576 29.27956  1.000 68.47986  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.16748 30.24957 28.63841  1.000 69.59511  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.10278 28.12758 28.39693  1.000 66.80781  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.12830 28.99028 28.07870  1.000 67.17790  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.67386  31.16477 33.52892  1.000 76.38689  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.76881  32.04936 34.24113  1.000 79.89845  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.47224  32.91255 35.27654  1.000 83.34599  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.99200  33.99822 35.61476  1.000 86.65772  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.61937  32.44520 35.78871  1.000 108.87896 ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.40835 33.16382 36.78898  1.000 113.68370 ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.27354 34.25271 36.18982  1.000 116.17149 ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.98124 34.94952 36.92154  1.000 119.81581 ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.29672 32.19906 37.56313  1.000 112.62379 ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.54101 31.03887 38.17240  1.000 110.67749 ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.26271  31.45532 38.89385  0.520 105.01415 ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 9.07408  32.64769 39.22848  1.000 109.26758 ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.42789  30.56664 39.14445  1.000 103.80117 ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.28183 34.34897 34.89796  1.000 115.15760 ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.60687 35.50733 34.10422  1.000 119.28021 ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.26978 35.90001 33.49083  1.000 123.37637 ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.23806  35.33379 33.86972  1.000 122.87549 ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.70714 35.14585 33.09795  1.000 113.64352 ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.83798 34.34041 33.73314  1.000 111.91483 ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.67521 32.99392 34.04524  1.000 108.43801 ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 15.05751 34.92566 34.02459  1.000 114.66378 ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.68274 32.26090 34.63698  1.000 107.91844 ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 16.07903 34.19615 34.60819  1.000 114.21548 ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 15.88512 32.86565 34.91101  1.000 110.67425 ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 16.89602 32.13726 35.49098  1.000 110.12759 ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 10.23705 36.84109 32.56119  1.000 127.00006 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 8.92903  37.01995 31.93976  1.000 129.62905 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 9.10640  36.70598 30.46314  1.000 128.02767 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 9.13215  37.59680 29.61832  1.000 128.08161 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 8.32737  38.35427 32.18335  0.800 134.57087 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 6.91368  38.45293 31.63874  0.700 134.62084 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 6.43800  37.47004 31.03664  0.700 130.54935 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 6.28272  39.51489 31.80677  0.700 138.80820 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.22221  35.41067 30.16801  1.000 125.47208 ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.22519  34.87976 28.80774  1.000 117.69217 ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.80492  34.46393 28.45971  1.000 112.18559 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.26026  33.51957 29.04359  1.000 110.52700 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.16429 33.68182 28.69539  1.000 114.71061 ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.63110 34.02352 28.74655  1.000 115.85890 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.28982 34.44885 27.12638  1.000 114.64258 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 12.87178 32.85957 26.53637  0.780 109.30268 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.21820  35.14923 27.49716  1.000 109.10656 ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.86735  34.82521 27.08188  1.000 105.35616 ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.83966  33.54781 26.24575  1.000 99.34035  ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.41234  33.50575 25.15182  1.000 97.17525  ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.30721  35.99001 26.29267  0.800 106.52146 ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 4.11714  35.61466 25.50912  0.700 104.39166 ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.64861  36.74844 24.67640  0.600 105.41572 ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 4.18376  37.86259 24.85335  0.600 107.90929 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.75099  36.52297 23.84637  0.600 103.90559 ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.17522  32.50467 26.75778  1.000 97.19586  ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.89873  31.32433 25.94352  1.000 91.66609  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.88832  31.66752 24.86442  1.000 91.71629  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.79556  32.16741 25.14551  1.000 93.21611  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.35612  30.15783 26.77458  1.000 89.12687  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.19672  28.83680 25.99926  1.000 84.32572  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.06771  28.56768 25.21481  1.000 83.69352  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.17474  27.85327 26.07403  1.000 81.40819  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 2.93947  27.34982 24.51979  1.000 81.12857  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.05299  26.65011 25.39323  1.000 78.74187  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 3.94258  26.39855 24.62045  1.000 78.88001  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 3.86247  25.18881 23.96128  1.000 76.76949  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.25374  31.35470 23.63308  1.000 89.76951  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.40718  31.52526 22.46460  1.000 91.50232  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.79232  30.37121 21.56023  1.000 90.99600  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 4.96420  30.26026 21.19543  1.000 90.43344  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.68697  32.87890 21.80038  0.800 91.89775  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.70457  33.22849 20.70202  0.700 91.90033  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.06628  32.31948 20.13501  0.600 89.54533  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.58546  34.43452 20.39667  0.600 94.18850  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 2.86981  29.46846 21.24578  1.000 90.36546  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.24621  28.41710 20.31222  1.000 88.33305  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.75890  28.71148 18.90649  1.000 88.65988  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.73405  27.81545 18.05577  1.000 87.41013  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.76683  27.04704 20.79159  1.000 86.98308  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.27252  26.86085 20.68237  1.000 87.49155  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.54071  27.83505 20.41219  0.830 89.46885  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.82742  25.71122 20.87769  0.830 86.00241  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.38059  29.95240 18.65070  1.000 91.02467  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.91605  30.38526 17.34696  1.000 93.88661  ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 2.97077  31.22905 16.64116  1.000 95.17719  ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.28641  30.99460 15.47352  1.000 95.15464  ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.57251  31.13748 17.47587  1.000 97.84979  ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.23764  31.87160 16.20102  1.000 100.04558 ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.52966 30.14598 17.83345  1.000 98.25952  ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.57516  32.18289 17.36041  1.000 96.95479  ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.68611  32.97452 16.82814  1.000 97.37374  ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.90478  32.99031 17.76872  1.000 96.82484  ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.40743  34.04979 18.10390  1.000 99.13481  ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.22628  34.40943 16.57465  1.000 101.78685 ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.36274  34.62972 15.33646  1.000 103.84538 ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 3.01080  36.09849 15.15488  0.720 108.58323 ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 2.61662  36.74621 16.15072  1.000 111.29262 ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 3.14530  36.61300 14.02589  1.000 109.60020 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.41377  31.82120 18.18527  1.000 91.42464  ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.62155  31.84146 19.03072  1.000 89.34290  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.81777  32.42987 18.29074  1.000 86.40204  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.85007  32.50743 17.06097  1.000 85.66821  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.84376  30.35726 19.37308  1.000 86.30945  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.05316  29.59170 18.37743  1.000 84.98015  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 5.89149  30.45710 18.03139  1.000 88.57940  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.80266  32.88627 19.06482  1.000 84.47250  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.09687 33.27556 18.51499  1.000 82.03973  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.16074 32.22867 18.79271  1.000 78.11166  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.22933 32.25753 18.16433  1.000 77.32455  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.54215 34.63339 19.08765  1.000 85.20778  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.58308 35.77534 18.76821  0.740 87.75064  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 10.88636 37.07685 19.50919  0.660 91.66144  ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 11.64683 37.06058 20.50070  1.000 92.38370  ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.34668 38.12510 19.09346  0.730 94.32546  ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.86465 31.31684 19.70897  1.000 64.60393  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.76738 30.30006 20.21567  1.000 61.54060  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.93507 29.03611 20.29886  1.000 58.81203  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.82676 29.06654 20.84728  1.000 56.71309  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.33046 30.72165 21.59063  1.000 62.80652  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 13.99557 32.11104 21.50264  1.000 65.56955  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 14.29853 29.69888 22.15728  1.000 61.34470  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.16099 32.17198 20.53758  0.380 65.24265  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.41456 27.95620 19.69358  1.000 56.69718  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.67349 26.70095 19.67484  1.000 54.87097  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.55618 25.64267 20.30667  1.000 54.35134  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.64328 25.35750 19.79841  1.000 52.94444  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.22240 26.30854 18.25387  1.000 52.96626  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 11.01811 24.81369 18.14330  1.000 50.42845  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 9.93211  27.04290 17.88035  1.000 54.34813  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.11606 25.09566 21.43807  1.000 55.78163  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.88741 24.09083 22.16022  1.000 55.77231  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.24284 22.73434 21.93743  1.000 54.70736  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.02260 22.58357 22.07091  1.000 54.23311  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 13.00592 24.41297 23.65892  1.000 56.89834  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.65801 25.78287 23.84298  1.000 58.73107  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.84109 23.35197 24.35305  1.000 56.35026  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.27678 26.45605 25.13283  1.000 60.89568  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.06958 21.75319 21.59821  1.000 54.37516  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.63986 20.40174 21.28592  1.000 54.07934  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.22675 19.44929 22.31703  1.000 55.26945  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.40071 19.56577 22.67919  1.000 55.63739  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.08995 20.01490 19.88204  1.000 52.99515  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.64155 18.71773 19.55097  1.000 52.73001  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.41551 18.51208 22.80046  1.000 56.04355  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.78923 17.69159 23.94919  1.000 58.34773  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.50683 16.22564 23.63976  1.000 58.83356  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.34186 15.81824 23.53683  1.000 58.76115  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.06504 18.13250 25.22753  1.000 59.59836  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.48937 19.55202 25.60990  1.000 60.10537  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.38321 17.19263 26.36726  1.000 61.64201  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 12.20548 19.90591 27.05396  1.000 62.05507  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.56981 15.43201 23.51841  1.000 59.57782  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.44964 14.01631 23.23154  1.000 59.88161  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.59714 13.48395 22.39525  1.000 59.28251  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.64909 13.11860 22.92736  1.000 61.01324  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.40247 13.43383 21.07625  1.000 56.91690  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.41472 12.95502 20.15731  1.000 56.81231  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.41645 13.78831 18.88990  1.000 56.14389  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.60647 14.70302 18.73353  1.000 56.25274  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.34898 13.46050 17.98613  1.000 55.96833  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.42866 14.18487 16.71816  1.000 53.75961  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 15.10435 14.13057 15.97215  1.000 51.61714  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.72323 15.09673 15.29924  1.000 50.30319  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.53489 13.61665 15.83085  1.000 53.75565  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.92466 14.05939 16.24392  1.000 54.22692  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 19.11571 15.21256 16.69179  1.000 54.27514  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.84156 13.22973 16.08214  1.000 54.64369  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.39893 12.99711 16.06211  1.000 51.29762  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 13.06578 12.91596 15.48637  1.000 50.88714  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 12.14897 13.99816 16.02260  1.000 51.51360  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.48392 14.70482 15.25886  1.000 51.23305  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 12.08885 14.13292 17.35035  1.000 52.46179  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.31577 15.22078 17.94424  1.000 52.23306  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.73960 16.55907 17.36531  1.000 51.37425  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.89838 17.40015 17.01635  1.000 51.60385  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.49196 15.24390 19.46194  1.000 53.26658  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.30677 13.92701 19.99001  1.000 54.29269  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.48730 16.19546 20.08954  1.000 53.88216  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.05099 16.75163 17.22918  1.000 50.78699  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.56506 18.00269 16.70255  1.000 51.50729  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.12504 18.21609 15.25654  1.000 51.43734  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.71759 19.32006 14.87111  1.000 51.30940  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.08054 18.01713 16.80812  1.000 51.50950  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.65764 19.31086 16.42856  1.000 52.10830  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.91263 19.60595 15.10180  1.000 51.97340  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.90642 20.26141 17.39260  1.000 52.75459  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.43106 20.81795 14.74949  1.000 52.66919  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.42694 21.47342 17.04993  1.000 53.35475  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.68883 21.75470 15.72409  1.000 53.40600  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.27382 17.18172 14.42470  1.000 52.32990  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.78688 17.25199 13.04813  1.000 53.20955  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.34735 17.75614 13.01161  1.000 53.97525  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 11.01399 18.69309 12.27436  1.000 54.11326  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.88237 15.87558 12.38633  1.000 53.12787  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 13.91943 15.53521 11.31426  1.000 53.54203  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 15.03548 16.56295 11.18995  1.000 54.03381  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.48663 14.16585 11.63196  1.000 53.50492  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.48885 17.15642 13.84353  1.000 54.23984  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 9.09835  17.59535 13.93091  1.000 54.81520  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.99128  19.05480 14.36006  1.000 55.00616  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.11961  19.78962 13.87844  1.000 55.98035  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.32275  16.70403 14.89957  1.000 55.74353  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.01089  15.46003 14.30569  1.000 56.06074  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.85659  19.49110 15.27986  1.000 54.27426  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.83015  20.89553 15.67509  1.000 54.92518  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.17314 21.79314 14.49583  1.000 54.00549  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.51188  22.81286 14.26191  1.000 54.77378  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.78827 21.13996 16.83788  1.000 55.46122  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.18443 21.40086 13.72298  1.000 52.65573  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.57508 22.15184 12.53865  1.000 52.43076  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.43311 22.23539 11.53205  1.000 52.15627  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 10.11649 23.31818 11.02682  1.000 53.02056  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.80900 21.49685 11.92357  1.000 51.06532  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 13.10963 21.95508 10.53683  1.000 51.84451  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.72511 23.17240 10.31622  1.000 53.36068  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.78772 21.16225 9.45085   1.000 51.48255  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 14.00644 23.59420 9.04154   1.000 54.47230  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 13.06548 21.57886 8.16999   1.000 52.62381  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.67616 22.79811 7.96285   1.000 54.22841  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.79387  21.10152 11.23312  1.000 51.29518  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.72425  21.11794 10.23988  1.000 52.39533  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.48276  21.82740 10.75135  1.000 54.47737  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.75717  22.44374 9.96321   1.000 56.46104  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.39146  19.69865 9.79965   1.000 51.28834  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.41915  19.12540 8.88743   1.000 50.80367  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.65262  19.63679 7.63042   1.000 51.57842  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.31500 18.12770 9.06354   1.000 49.41173  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.63596 18.96482 7.06205   1.000 50.85543  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.05114 18.03924 7.90822   1.000 49.48867  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.22140  21.76382 12.05670  1.000 54.02919  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 6.10083  22.51551 12.60296  1.000 56.90070  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.25176  24.01117 12.36507  1.000 60.20572  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.25167  24.73567 12.37855  1.000 62.31823  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.95054  22.23968 14.10006  0.800 56.21700  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.56958  22.57285 14.64679  0.700 57.68392  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.53795  22.62796 16.15934  0.600 57.13597  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.34771  21.99122 16.83453  0.600 55.51940  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.60410  23.40011 16.70127  0.600 58.98626  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.46771  24.49021 12.11211  1.000 61.28246  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.68993  25.92520 12.01321  1.000 63.89739  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.50601  26.29794 10.77652  1.000 64.17202  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.21372  27.30762 10.77910  1.000 65.43788  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.34777  26.43811 13.29544  1.000 64.65214  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.41708  26.36741 14.49154  1.000 65.34816  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.39170  27.29096 14.64283  1.000 68.05440  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.54464  25.36800 15.45460  1.000 63.85135  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.52404  27.23343 15.72007  1.000 69.29542  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.67483  25.30452 16.54138  1.000 65.08498  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.66735  26.24268 16.66480  1.000 67.76401  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.79580  26.19788 17.73146  1.000 68.91158  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.38412  25.52954 9.69046   1.000 63.44436  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.28260  25.71925 8.55631   1.000 64.70827  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.95547  26.93828 7.70229   1.000 68.78452  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.72206  27.24197 6.78280   1.000 69.43318  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.29355  24.47573 7.66852   0.900 62.60957  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 8.01706  24.25111 6.89682   0.800 63.29344  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 8.07727  22.99939 6.05403   0.700 61.01018  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.61168  21.98043 6.54071   0.600 58.16985  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 7.60077  23.03878 4.90210   0.600 62.38304  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.85769  27.64210 7.96041   1.000 72.18044  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.59648  28.88832 7.25602   1.000 76.41707  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 8.01909  30.10949 8.05692   1.000 77.83793  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.81735  31.23709 7.59883   1.000 80.07706  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 6.11667  28.99197 6.87843   1.000 79.63184  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.64039  27.87619 5.96268   1.000 79.69531  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 4.18087  28.01530 5.57854   0.350 83.91547  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 3.43112  28.68070 6.32218   0.860 86.37004  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 3.78463  27.46476 4.52919   0.630 85.15908  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.60363  29.91940 9.23435   1.000 76.76887  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 9.14451  31.03270 9.99942   1.000 78.90015  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.61556 30.81484 10.31844  1.000 77.46886  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 11.13032 31.34099 11.30452  1.000 78.35269  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.31658  31.26962 11.26085  1.000 80.06888  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 7.03546  32.00660 10.88645  0.720 83.81099  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 6.12711  32.41488 12.03578  1.000 85.70170  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.75218  33.28715 13.01625  1.000 87.59922  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.17652  32.87339 14.19894  0.940 86.08839  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.10961  31.60101 14.54593  0.980 82.87196  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.67017  33.75454 15.05627  1.000 87.97616  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.30817 30.06585 9.45867   1.000 76.17200  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.68462 29.68503 9.75430   1.000 76.21917  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.56195 30.90667 9.96050   1.000 81.97118  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.32345 30.98323 10.92910  1.000 82.45284  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.24490 28.81762 8.63690   1.000 72.81202  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.60024 27.44957 8.53945   1.000 69.64229  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.38992 26.69141 7.54012   1.000 68.27417  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.60338 26.74345 9.88516   1.000 66.98504  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.44682 31.88964 9.07840   1.000 86.47209  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 14.27643 33.08274 9.18254   1.000 92.47783  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 14.04400 33.82293 10.50866  1.000 95.43731  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.77393 34.77413 10.81182  1.000 97.36303  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 14.01748 34.00085 7.98055   1.000 95.74592  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 15.29223 34.64288 7.43516   1.000 97.66502  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 16.40329 34.16326 7.74542   1.000 95.97806  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.17508 35.64151 6.69275   1.000 101.66805 ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 13.07842 33.37169 11.34204  1.000 97.02875  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.69819 34.08333 12.56776  1.000 99.74243  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.71810 33.25369 13.85574  1.000 95.95418  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.16230 33.70835 14.86605  1.000 97.40945  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 11.29705 34.68545 12.41895  1.000 103.48326 ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 11.16356 35.66085 11.28737  1.000 109.24433 ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 9.86668  35.47869 10.54577  0.790 111.67071 ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 8.80161  35.50191 11.19736  0.610 112.24975 ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 9.91664  35.28966 9.31408   0.970 112.63276 ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.33005 32.06735 13.86398  1.000 87.62501  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.31652 31.17174 15.02350  1.000 81.13128  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.71862 30.63214 15.26755  1.000 77.91049  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.41532 30.25346 14.32149  1.000 77.92652  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.36428 29.97081 14.82411  1.000 77.66411  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.90220 30.38693 14.74543  1.000 78.41806  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.55552 28.91623 15.91879  1.000 76.33401  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 10.03594 29.23485 14.32947  1.000 76.07285  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 15.11520 30.54123 16.53742  1.000 75.82489  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.28373 29.75985 16.93331  1.000 72.33849  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.81897 28.47267 17.60848  1.000 68.49791  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.11758 28.51909 18.62457  1.000 68.92195  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.20600 30.55383 17.86085  1.000 74.32621  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.21391 27.33415 17.04211  1.000 65.07964  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 15.94009 26.01436 17.59405  1.000 62.27759  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.05946 25.59350 18.55609  1.000 62.86673  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.22143 26.01773 18.41068  1.000 63.86197  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.78707 24.98725 16.45634  1.000 59.38784  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.58448 25.22239 15.51024  1.000 58.74983  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 14.69606 26.01242 14.36613  1.000 59.54355  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.37461 24.57572 15.73002  1.000 57.71855  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.60430 26.18814 13.49833  1.000 59.69493  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.28582 24.75066 14.87032  1.000 57.90773  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.40326 25.55602 13.75474  1.000 58.89495  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.68955 24.78670 19.57371  1.000 62.97195  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.59821 24.12475 20.52243  1.000 63.62826  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 17.13210 22.68949 20.69372  1.000 61.36548  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.92942 22.46881 20.89110  1.000 60.20460  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.62877 24.77278 21.93484  1.000 66.29869  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 18.19067 26.18873 21.92884  1.000 68.91124  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.31829 23.86140 22.97413  1.000 66.73558  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.09049 27.19868 21.91029  0.920 69.66484  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 18.04530 21.73427 20.70850  1.000 61.38388  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.71464 20.34672 20.98038  1.000 60.39936  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 18.20748 19.92783 22.37895  1.000 62.44007  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.34718 20.20972 22.73744  1.000 63.74124  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.32850 19.25222 23.10048  1.000 63.33097  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.69567 18.56649 24.33781  1.000 67.05020  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.39566 17.09180 24.13615  1.000 69.71048  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.25234 16.72419 23.84421  1.000 69.26946  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.94435 19.11520 25.56294  1.000 67.61634  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 17.32596 20.56968 25.81568  1.000 68.49918  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 17.24136 18.27156 26.80677  1.000 69.61897  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.58150 21.19235 26.96019  1.000 70.18769  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.41698 16.24915 24.26392  1.000 73.34982  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.21504 14.81411 24.11998  1.000 77.19623  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.96315 14.21368 25.49366  1.000 85.57393  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.81478 14.28335 26.38685  1.000 88.74841  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.39591 14.12921 23.43001  1.000 73.97859  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.63656 14.06304 24.26118  1.000 73.80179  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.57562 15.06959 24.26585  1.000 73.81706  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.10020 13.10906 25.10390  1.000 75.72889  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.56241 14.74323 25.08020  1.000 76.41275  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.29815 13.55858 25.60223  1.000 77.98065  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.77813 13.66013 25.67088  1.000 78.01401  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.47774 12.88307 26.85107  1.000 80.07534  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.68463 11.40129 26.61363  1.000 81.04980  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 16.64957 10.61759 27.56823  1.000 79.93431  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 15.04792 13.16890 27.28466  1.000 80.40185  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.14559 12.63830 26.30671  1.000 78.00335  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.85560 14.67643 27.36071  1.000 81.82335  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 16.90483 11.00751 25.36792  0.500 78.07065  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.36839 9.67150  25.11102  0.500 75.02282  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 18.86629 9.73669  24.97100  0.500 77.77053  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.57077 10.23786 25.85656  0.500 84.84093  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.35789 9.24947  23.84511  0.500 69.17836  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 20.74515 9.43916  23.49250  0.500 68.91253  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 20.90299 10.70017 22.67474  0.500 67.05012  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 19.96633 11.13975 21.97763  0.500 63.98585  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.27785 8.23854  22.72094  0.500 66.02188  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 21.25465 6.97438  23.51256  0.500 66.42945  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 22.15634 6.71586  24.52104  0.500 69.52231  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 20.42351 5.90786  23.46501  0.500 64.94914  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 21.89012 5.53646  25.05205  0.500 70.17080  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 20.84342 5.02532  24.42908  0.500 67.61620  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.09686 11.28617 22.80820  0.500 68.32271  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 22.49102 12.43339 22.02788  0.500 70.77448  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.01721 12.25275 20.58631  0.500 71.84581  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.08648 11.17239 20.02118  0.500 72.56505  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 23.99648 12.58287 22.07031  0.500 70.43602  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 24.77069 13.61751 21.29851  0.500 70.29349  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 24.38687 15.01143 21.74231  0.500 71.25313  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.22970 13.35180 21.58595  0.500 72.75973  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 21.47431 13.31709 20.01591  1.000 70.73879  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.24386 13.40689 18.60399  1.000 69.29046  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.21034 14.44997 18.09084  1.000 71.39821  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 22.97592 15.06908 18.85430  1.000 75.71450  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.12996 14.66553 16.79686  1.000 63.74252  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.94701 15.70969 16.22780  1.000 60.66335  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.30715 17.06802 16.33746  1.000 61.00781  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.00433 18.08880 16.37657  1.000 64.02933  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.22940 15.39605 14.79235  1.000 55.69299  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.42344 14.61005 14.65097  1.000 54.39854  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.43605 13.29595 15.06034  1.000 51.57826  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.58572 15.20668 14.24554  1.000 55.71013  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.56379 12.55332 14.95114  1.000 50.96783  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.72397 14.48310 14.15342  1.000 55.52172  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 26.71796 13.14807 14.50674  1.000 53.17014  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 20.99134 17.10297 16.34455  1.000 58.88074  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.30006 18.35081 16.56937  1.000 59.83051  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 19.99187 18.55368 18.03787  1.000 61.33667  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.01008 19.69252 18.52113  1.000 63.37804  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.02801 18.36958 15.73770  1.000 56.82134  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.30078 18.11287 14.27570  1.000 54.95405  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.23867 18.86697 13.58302  1.000 56.85032  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.63888 17.10420 13.59292  1.000 51.67214  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.49492 18.63787 12.24604  1.000 56.22713  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 18.88768 16.86547 12.25759  1.000 50.84875  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.81498 17.63297 11.58761  1.000 53.32992  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.06447 17.39625 10.25391  1.000 52.64058  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.74322 17.45545 18.75360  1.000 60.76783  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.44756 17.48579 20.18371  1.000 64.06798  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 20.74804 17.31606 20.95834  1.000 67.15615  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 21.05414 16.25378 21.51032  1.000 66.38295  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.43688 16.40518 20.53928  1.000 61.66658  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.54306 18.38553 20.99007  1.000 71.58064  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.84842 18.28016 21.62910  1.000 74.90299  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 22.87376 19.03481 22.95587  1.000 77.22148  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 23.68827 19.94420 23.15654  1.000 80.96088  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.94753 18.76774 20.68482  1.000 77.66579  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.71069 20.17851 20.19470  1.000 80.68421  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.87508 20.89335 20.78767  1.000 81.87674  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.36428 20.57155 19.21479  1.000 82.24618  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 21.96176 18.66175 23.85313  1.000 74.89178  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.92180 19.15287 25.22258  1.000 77.84926  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.40777 18.02705 26.09147  1.000 76.17088  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.39783 17.40422 25.75647  1.000 73.35985  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 20.99463 20.35358 25.38703  0.800 78.79148  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.57485 21.64673 25.05352  0.700 82.21914  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.44822 22.30779 23.87954  0.600 81.59955  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.36063 22.48166 25.90868  0.600 87.03947  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.11520 23.50313 23.93756  0.600 85.79343  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.68519 23.63377 25.17563  0.600 89.14822  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.82296 22.36568 27.21940  0.600 89.89136  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.45471 24.66341 25.70630  0.600 94.19792  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.58951 23.38486 27.74620  0.600 94.82248  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.89680 24.52067 26.99192  0.600 96.95316  ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 22.05722 17.81059 27.18899  1.000 78.22034  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.55833 16.83461 28.13252  1.000 75.80645  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.46411 17.47809 28.98534  1.000 73.49618  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.43427 18.70302 29.13627  1.000 75.12800  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.70195 16.33709 29.00956  1.000 79.87377  ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 22.79445 14.82425 29.10439  0.990 78.84165  ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 24.07361 14.35647 29.79453  1.000 82.65121  ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.82743 15.44719 30.40088  0.870 87.03721  ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 24.87157 15.70188 31.70247  0.590 90.48386  ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 24.22257 14.95094 32.57929  1.000 90.07268  ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 25.58698 16.73338 32.13754  1.000 94.80369  ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.52082 16.69207 29.53239  1.000 70.00273  ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.50663 17.31777 30.39423  1.000 69.86916  ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 19.12571 18.07695 31.53803  1.000 73.56761  ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.69072 19.19469 31.84223  1.000 75.36982  ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.67722 16.12497 30.89710  1.000 68.14883  ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 17.88504 15.07741 29.90647  1.000 65.38759  ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.31089 15.23887 29.45300  1.000 67.00235  ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.15416 17.49526 32.16492  1.000 75.40739  ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.75306 18.10013 33.34819  1.000 80.74511  ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 21.10835 19.56098 33.12203  1.000 82.36741  ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.10069 20.35948 34.06615  1.000 85.84792  ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.99465 17.31934 33.77241  1.000 83.56868  ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.38165 19.94501 31.88209  1.000 80.06508  ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.76139 21.31961 31.61502  1.000 80.99150  ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.56945 22.24263 31.41261  1.000 78.60000  ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.76111 23.39287 31.00858  1.000 79.95405  ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.66966 21.37288 30.40166  1.000 79.96203  ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 23.78971 20.37873 30.46421  0.390 80.32079  ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.77163 20.59216 29.35608  0.870 81.28419  ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 24.47995 20.17560 28.21683  1.000 77.60258  ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 25.82648 21.20005 29.62349  0.830 86.06480  ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.35230 21.77650 31.70874  1.000 75.34364  ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 18.15743 22.54471 31.37039  1.000 74.29440  ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 18.12051 23.88236 32.10379  1.000 79.35890  ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.90477 24.93028 31.48620  1.000 81.06308  ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.89632 21.73044 31.66965  1.000 71.07838  ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.30712 23.87121 33.43031  1.000 81.92453  ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.19358 25.12390 34.18029  1.000 81.94347  ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.18291 26.16726 33.67037  1.000 85.55265  ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.84147 27.35100 33.55099  1.000 87.98390  ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.39542 24.89323 35.68034  0.800 85.18379  ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.25361 24.10897 36.32140  0.700 82.61940  ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 16.08189 24.25473 35.90195  0.700 79.88041  ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.53703 23.35230 37.27364  0.700 83.74747  ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.41584 25.74891 33.36506  1.000 86.29385  ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.37777 26.66735 32.75928  1.000 89.67110  ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.84383 27.22976 31.44957  1.000 88.92590  ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 20.93856 28.43637 31.19236  1.000 92.59614  ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.71213 25.95868 32.52172  1.000 90.17322  ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.26769 26.35893 30.61977  1.000 83.24358  ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.70940 26.74873 29.33136  1.000 80.58074  ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.71495 27.88479 29.47861  1.000 82.35693  ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.85581 28.94633 28.86118  1.000 83.90286  ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.02427 25.54014 28.70605  1.000 74.47604  ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 19.13836 25.33230 27.21546  1.000 70.67111  ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.31870 26.10063 26.68406  1.000 75.05089  ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 19.34283 23.85672 27.04542  1.000 66.81662  ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.67460 27.63904 30.28104  1.000 81.72314  ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.66310 28.65013 30.57726  1.000 84.23276  ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.32171 29.97828 30.92361  1.000 91.03694  ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.92338 31.04329 30.43952  1.000 92.63173  ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.75654 28.16677 31.72363  1.000 83.07473  ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.69290 29.19540 32.01463  1.000 85.15690  ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 15.16693 26.81775 31.38825  1.000 77.49542  ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.32957 29.92765 31.78545  1.000 95.79950  ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 19.01593 31.11982 32.25994  1.000 103.26882 ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.57734 31.93001 31.10608  1.000 106.21771 ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 19.12150 33.04831 30.84499  1.000 108.67058 ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 20.13342 30.73235 33.22593  0.710 105.98384 ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 19.79045 30.98557 34.67307  0.960 108.81624 ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 20.27148 29.85435 35.55238  1.000 108.01936 ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 19.58025 29.90086 36.89957  0.960 109.95463 ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 19.69326 28.60792 37.62621  1.000 108.04981 ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.56906 31.36809 30.41538  1.000 106.35253 ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 21.16557 32.05772 29.27780  1.000 109.52475 ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 20.11435 32.40789 28.23653  1.000 108.43681 ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.13914 33.49965 27.65176  1.000 111.63775 ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.24904 31.17989 28.66913  1.000 107.86129 ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.06741 30.55605 29.78936  1.000 109.65996 ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 23.49521 29.14782 29.42761  1.000 105.12381 ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 24.26120 31.43871 30.08493  1.000 116.50343 ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 19.16578 31.49264 28.01025  1.000 104.76939 ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.07959 31.74528 27.06941  1.000 104.97946 ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.31158 33.01633 27.40614  1.000 113.45731 ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 16.68548 33.61851 26.52456  1.000 113.21076 ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.10543 30.57335 27.05520  1.000 97.89459  ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 16.73400 30.02175 25.68947  0.540 92.73763  ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 17.25349 30.90954 24.56288  1.000 95.05467  ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 17.29101 28.62430 25.58088  1.000 88.53664  ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 17.31991 33.42650 28.67549  0.840 121.70014 ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 16.57476 34.61752 29.06715  1.000 131.30307 ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 17.38972 35.88244 28.81411  1.000 141.60825 ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.91867 36.81758 28.15618  1.000 144.22252 ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 16.16404 34.52377 30.53650  1.000 132.87410 ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 18.62329 35.91709 29.32314  1.000 147.25080 ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 19.48264 37.08558 29.16548  1.000 154.69299 ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 19.78249 37.40167 27.70318  1.000 153.49229 ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 20.15360 38.53703 27.38809  1.000 159.09574 ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.77831 36.86039 29.94621  1.000 159.70965 ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 21.73237 38.03772 29.98660  0.880 169.70065 ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 22.96761 37.68284 30.79326  0.810 174.46953 ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 23.63533 36.43140 30.24299  1.000 170.51021 ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 24.79647 35.99911 31.06896  1.000 173.42257 ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 19.61154 36.44486 26.80297  1.000 110.66189 ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.93461 36.69445 25.40776  1.000 106.56615 ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 21.42418 36.60291 25.21535  1.000 105.77133 ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 22.06061 35.66990 25.70915  1.000 105.70130 ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 21.99644 37.56752 24.49389  0.200 106.29281 ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 23.44527 37.64487 24.30319  0.200 108.22341 ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 24.03731 36.31405 23.84834  0.200 108.18062 ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 25.21649 36.03167 24.09712  0.200 110.04074 ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 24.13762 38.11930 25.57849  0.200 107.58339 ? 94  GLU A CB  1 
ATOM   741  C CG  . GLU A 1 94  ? 23.59804 39.41169 26.11654  0.200 107.68604 ? 94  GLU A CG  1 
ATOM   742  C CD  . GLU A 1 94  ? 24.64725 40.13418 26.90416  0.200 107.02406 ? 94  GLU A CD  1 
ATOM   743  O OE1 . GLU A 1 94  ? 25.83814 39.82833 26.68613  0.200 105.26197 ? 94  GLU A OE1 1 
ATOM   744  O OE2 . GLU A 1 94  ? 24.29306 40.98950 27.73892  0.200 108.78413 ? 94  GLU A OE2 1 
ATOM   745  N N   . TYR A 1 95  ? 23.20460 35.48741 23.22071  1.000 105.79887 ? 95  TYR A N   1 
ATOM   746  C CA  . TYR A 1 95  ? 23.58096 34.23776 22.58064  1.000 104.54330 ? 95  TYR A CA  1 
ATOM   747  C C   . TYR A 1 95  ? 23.77781 34.45806 21.08271  1.000 103.77636 ? 95  TYR A C   1 
ATOM   748  O O   . TYR A 1 95  ? 23.28719 35.43379 20.51166  1.000 105.22787 ? 95  TYR A O   1 
ATOM   749  C CB  . TYR A 1 95  ? 22.51017 33.16515 22.82733  1.000 103.96219 ? 95  TYR A CB  1 
ATOM   750  C CG  . TYR A 1 95  ? 21.10475 33.51726 22.35430  1.000 105.11038 ? 95  TYR A CG  1 
ATOM   751  C CD1 . TYR A 1 95  ? 20.70989 33.26393 21.04681  1.000 103.53635 ? 95  TYR A CD1 1 
ATOM   752  C CD2 . TYR A 1 95  ? 20.16832 34.07785 23.21927  1.000 108.00055 ? 95  TYR A CD2 1 
ATOM   753  C CE1 . TYR A 1 95  ? 19.43283 33.57520 20.60581  1.000 104.07068 ? 95  TYR A CE1 1 
ATOM   754  C CE2 . TYR A 1 95  ? 18.88382 34.39360 22.78424  1.000 108.56016 ? 95  TYR A CE2 1 
ATOM   755  C CZ  . TYR A 1 95  ? 18.52482 34.13838 21.47715  1.000 106.80902 ? 95  TYR A CZ  1 
ATOM   756  O OH  . TYR A 1 95  ? 17.25945 34.44509 21.03005  1.000 107.61400 ? 95  TYR A OH  1 
ATOM   757  N N   . GLN A 1 96  ? 24.49727 33.52668 20.45119  1.000 101.88583 ? 96  GLN A N   1 
ATOM   758  C CA  . GLN A 1 96  ? 24.83210 33.56933 19.03070  1.000 100.96874 ? 96  GLN A CA  1 
ATOM   759  C C   . GLN A 1 96  ? 23.98382 32.58356 18.22714  1.000 96.45725  ? 96  GLN A C   1 
ATOM   760  O O   . GLN A 1 96  ? 23.56153 31.54214 18.73752  1.000 95.98398  ? 96  GLN A O   1 
ATOM   761  C CB  . GLN A 1 96  ? 26.31309 33.23853 18.80718  1.000 102.98255 ? 96  GLN A CB  1 
ATOM   762  C CG  . GLN A 1 96  ? 27.31131 34.33686 19.14599  1.000 108.33624 ? 96  GLN A CG  1 
ATOM   763  C CD  . GLN A 1 96  ? 28.72544 33.79696 19.31382  0.540 109.94211 ? 96  GLN A CD  1 
ATOM   764  O OE1 . GLN A 1 96  ? 28.96799 32.59929 19.15693  0.790 107.56243 ? 96  GLN A OE1 1 
ATOM   765  N NE2 . GLN A 1 96  ? 29.66208 34.67886 19.64431  0.990 113.98955 ? 96  GLN A NE2 1 
ATOM   766  N N   . LYS A 1 97  ? 23.76720 32.90935 16.94808  1.000 93.52919  ? 97  LYS A N   1 
ATOM   767  C CA  . LYS A 1 97  ? 23.00353 32.07492 16.02123  1.000 88.77950  ? 97  LYS A CA  1 
ATOM   768  C C   . LYS A 1 97  ? 23.97424 31.35496 15.07808  1.000 85.14728  ? 97  LYS A C   1 
ATOM   769  O O   . LYS A 1 97  ? 24.88651 31.98580 14.53538  1.000 86.72422  ? 97  LYS A O   1 
ATOM   770  C CB  . LYS A 1 97  ? 21.99704 32.92309 15.20997  1.000 89.16969  ? 97  LYS A CB  1 
ATOM   771  C CG  . LYS A 1 97  ? 21.05039 33.88620 16.01524  1.000 91.90290  ? 97  LYS A CG  1 
ATOM   772  C CD  . LYS A 1 97  ? 19.80716 34.46217 15.22309  1.000 91.88560  ? 97  LYS A CD  1 
ATOM   773  C CE  . LYS A 1 97  ? 20.10582 34.89393 13.77088  1.000 90.85593  ? 97  LYS A CE  1 
ATOM   774  N NZ  . LYS A 1 97  ? 18.92799 35.42633 12.98604  1.000 90.43169  ? 97  LYS A NZ  1 
ATOM   775  N N   . VAL A 1 98  ? 23.80922 30.03593 14.89777  1.000 80.60276  ? 98  VAL A N   1 
ATOM   776  C CA  . VAL A 1 98  ? 24.43835 29.34943 13.76984  1.000 75.31047  ? 98  VAL A CA  1 
ATOM   777  C C   . VAL A 1 98  ? 23.33693 28.83032 12.86018  1.000 70.41917  ? 98  VAL A C   1 
ATOM   778  O O   . VAL A 1 98  ? 22.26248 28.43024 13.33346  1.000 69.73344  ? 98  VAL A O   1 
ATOM   779  C CB  . VAL A 1 98  ? 25.43396 28.21580 14.15280  1.000 73.32184  ? 98  VAL A CB  1 
ATOM   780  C CG1 . VAL A 1 98  ? 25.63370 28.07321 15.65964  1.000 73.49785  ? 98  VAL A CG1 1 
ATOM   781  C CG2 . VAL A 1 98  ? 25.09518 26.86849 13.47137  1.000 69.71252  ? 98  VAL A CG2 1 
ATOM   782  N N   . SER A 1 99  ? 23.59815 28.89253 11.55481  1.000 67.60827  ? 99  SER A N   1 
ATOM   783  C CA  . SER A 1 99  ? 22.63937 28.52562 10.53202  1.000 65.56520  ? 99  SER A CA  1 
ATOM   784  C C   . SER A 1 99  ? 23.16213 27.32488 9.77483   1.000 62.17963  ? 99  SER A C   1 
ATOM   785  O O   . SER A 1 99  ? 24.31372 27.32501 9.33764   1.000 62.47055  ? 99  SER A O   1 
ATOM   786  C CB  . SER A 1 99  ? 22.38488 29.69103 9.59290   1.000 67.91051  ? 99  SER A CB  1 
ATOM   787  O OG  . SER A 1 99  ? 23.61233 30.06868 8.97761   1.000 70.56197  ? 99  SER A OG  1 
ATOM   788  N N   . TYR A 1 100 ? 22.33084 26.30264 9.62047   1.000 59.58045  ? 100 TYR A N   1 
ATOM   789  C CA  . TYR A 1 100 ? 22.75098 25.20663 8.76069   1.000 56.10838  ? 100 TYR A CA  1 
ATOM   790  C C   . TYR A 1 100 ? 21.97141 25.26663 7.43779   1.000 54.47920  ? 100 TYR A C   1 
ATOM   791  O O   . TYR A 1 100 ? 20.81356 25.69189 7.42325   1.000 54.22872  ? 100 TYR A O   1 
ATOM   792  C CB  . TYR A 1 100 ? 22.53691 23.83765 9.43692   1.000 53.53956  ? 100 TYR A CB  1 
ATOM   793  C CG  . TYR A 1 100 ? 23.51088 23.41534 10.56538  1.000 53.45014  ? 100 TYR A CG  1 
ATOM   794  C CD1 . TYR A 1 100 ? 24.63120 24.17217 10.90341  1.000 55.00317  ? 100 TYR A CD1 1 
ATOM   795  C CD2 . TYR A 1 100 ? 23.29573 22.23249 11.28043  1.000 52.14054  ? 100 TYR A CD2 1 
ATOM   796  C CE1 . TYR A 1 100 ? 25.50340 23.76281 11.93040  1.000 55.78104  ? 100 TYR A CE1 1 
ATOM   797  C CE2 . TYR A 1 100 ? 24.15934 21.81964 12.30150  1.000 53.01963  ? 100 TYR A CE2 1 
ATOM   798  C CZ  . TYR A 1 100 ? 25.26020 22.58648 12.62040  1.000 54.91775  ? 100 TYR A CZ  1 
ATOM   799  O OH  . TYR A 1 100 ? 26.11784 22.18504 13.62526  1.000 55.89089  ? 100 TYR A OH  1 
ATOM   800  N N   . PRO A 1 101 ? 22.57229 24.87595 6.31221   1.000 53.17113  ? 101 PRO A N   1 
ATOM   801  C CA  . PRO A 1 101 ? 21.85194 24.91995 5.03324   1.000 52.63829  ? 101 PRO A CA  1 
ATOM   802  C C   . PRO A 1 101 ? 20.74909 23.87058 4.97634   1.000 51.27715  ? 101 PRO A C   1 
ATOM   803  O O   . PRO A 1 101 ? 20.77193 22.87020 5.69984   1.000 50.70257  ? 101 PRO A O   1 
ATOM   804  C CB  . PRO A 1 101 ? 22.94389 24.63127 3.99119   1.000 52.24209  ? 101 PRO A CB  1 
ATOM   805  C CG  . PRO A 1 101 ? 24.22043 24.37261 4.76082   1.000 52.12368  ? 101 PRO A CG  1 
ATOM   806  C CD  . PRO A 1 101 ? 23.85242 24.16828 6.19296   1.000 52.26444  ? 101 PRO A CD  1 
ATOM   807  N N   . LEU A 1 102 ? 19.77960 24.10644 4.08396   1.000 51.18660  ? 102 LEU A N   1 
ATOM   808  C CA  . LEU A 1 102 ? 18.62175 23.23176 3.90639   1.000 50.15819  ? 102 LEU A CA  1 
ATOM   809  C C   . LEU A 1 102 ? 18.49214 22.81440 2.43968   1.000 49.65545  ? 102 LEU A C   1 
ATOM   810  O O   . LEU A 1 102 ? 19.15567 23.36301 1.55489   1.000 49.81627  ? 102 LEU A O   1 
ATOM   811  C CB  . LEU A 1 102 ? 17.32888 23.91535 4.37983   1.000 50.66859  ? 102 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 102 ? 17.34258 24.56005 5.76778   1.000 52.05137  ? 102 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 102 ? 16.11891 25.42514 5.95657   1.000 53.62119  ? 102 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 102 ? 17.42208 23.51129 6.86606   1.000 50.82458  ? 102 LEU A CD2 1 
ATOM   815  N N   . LEU A 1 103 ? 17.60987 21.83695 2.18576   1.000 49.49968  ? 103 LEU A N   1 
ATOM   816  C CA  . LEU A 1 103 ? 17.39006 21.25579 0.85945   1.000 48.02964  ? 103 LEU A CA  1 
ATOM   817  C C   . LEU A 1 103 ? 15.96539 21.52928 0.39531   1.000 47.73038  ? 103 LEU A C   1 
ATOM   818  O O   . LEU A 1 103 ? 15.00436 21.22180 1.10764   1.000 48.08241  ? 103 LEU A O   1 
ATOM   819  C CB  . LEU A 1 103 ? 17.65143 19.73441 0.86131   1.000 46.83552  ? 103 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 103 ? 17.30378 18.82658 -0.33874  1.000 46.27178  ? 103 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 103 ? 18.01056 19.25594 -1.61583  1.000 46.34181  ? 103 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 103 ? 17.60848 17.35061 -0.05176  1.000 44.83353  ? 103 LEU A CD2 1 
ATOM   823  N N   . LYS A 1 104 ? 15.83128 22.09537 -0.79857  1.000 47.37923  ? 104 LYS A N   1 
ATOM   824  C CA  . LYS A 1 104 ? 14.53681 22.26119 -1.44106  1.000 47.86985  ? 104 LYS A CA  1 
ATOM   825  C C   . LYS A 1 104 ? 14.32486 21.11334 -2.41826  1.000 47.35898  ? 104 LYS A C   1 
ATOM   826  O O   . LYS A 1 104 ? 15.21400 20.79553 -3.21501  1.000 46.25729  ? 104 LYS A O   1 
ATOM   827  C CB  . LYS A 1 104 ? 14.45502 23.60345 -2.16451  0.800 48.84964  ? 104 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 104 ? 13.06197 24.01358 -2.58270  0.700 50.52156  ? 104 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 104 ? 13.19086 25.13368 -3.57308  0.700 51.81580  ? 104 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 104 ? 11.86425 25.70110 -3.97772  0.600 53.17930  ? 104 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 104 ? 12.09188 27.13926 -4.24197  0.600 54.67304  ? 104 LYS A NZ  1 
ATOM   832  N N   . THR A 1 105 ? 13.17004 20.46802 -2.31849  1.000 48.68050  ? 105 THR A N   1 
ATOM   833  C CA  . THR A 1 105 ? 12.72420 19.46575 -3.27221  1.000 48.77378  ? 105 THR A CA  1 
ATOM   834  C C   . THR A 1 105 ? 11.50478 20.03234 -3.97854  1.000 51.11134  ? 105 THR A C   1 
ATOM   835  O O   . THR A 1 105 ? 10.58168 20.51828 -3.32048  1.000 52.37652  ? 105 THR A O   1 
ATOM   836  C CB  . THR A 1 105 ? 12.37098 18.14905 -2.57194  1.000 48.17694  ? 105 THR A CB  1 
ATOM   837  O OG1 . THR A 1 105 ? 13.53046 17.61447 -1.92102  1.000 46.78303  ? 105 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 105 ? 11.84048 17.12683 -3.57443  1.000 47.97889  ? 105 THR A CG2 1 
ATOM   839  N N   . THR A 1 106 ? 11.50937 20.00280 -5.30605  1.000 52.15630  ? 106 THR A N   1 
ATOM   840  C CA  . THR A 1 106 ? 10.37893 20.47416 -6.09306  1.000 54.60580  ? 106 THR A CA  1 
ATOM   841  C C   . THR A 1 106 ? 9.85249  19.31679 -6.93598  1.000 55.24607  ? 106 THR A C   1 
ATOM   842  O O   . THR A 1 106 ? 10.62843 18.65110 -7.62987  1.000 54.25311  ? 106 THR A O   1 
ATOM   843  C CB  . THR A 1 106 ? 10.78325 21.66762 -6.96713  1.000 55.71457  ? 106 THR A CB  1 
ATOM   844  O OG1 . THR A 1 106 ? 11.24920 22.73937 -6.13416  1.000 56.42651  ? 106 THR A OG1 1 
ATOM   845  C CG2 . THR A 1 106 ? 9.59808  22.15877 -7.77270  1.000 57.90355  ? 106 THR A CG2 1 
ATOM   846  N N   . VAL A 1 107 ? 8.53606  19.07854 -6.86623  1.000 57.56059  ? 107 VAL A N   1 
ATOM   847  C CA  . VAL A 1 107 ? 7.87370  17.90969 -7.46502  1.000 60.30393  ? 107 VAL A CA  1 
ATOM   848  C C   . VAL A 1 107 ? 6.81713  18.41108 -8.45394  1.000 65.60056  ? 107 VAL A C   1 
ATOM   849  O O   . VAL A 1 107 ? 5.73124  18.82778 -8.03417  1.000 67.24105  ? 107 VAL A O   1 
ATOM   850  C CB  . VAL A 1 107 ? 7.22626  17.00785 -6.39902  1.000 59.74451  ? 107 VAL A CB  1 
ATOM   851  C CG1 . VAL A 1 107 ? 6.64558  15.74231 -7.03377  1.000 60.23540  ? 107 VAL A CG1 1 
ATOM   852  C CG2 . VAL A 1 107 ? 8.18893  16.67784 -5.24658  1.000 57.75508  ? 107 VAL A CG2 1 
ATOM   853  N N   . LYS A 1 108 ? 7.09149  18.33044 -9.76588  1.000 68.95303  ? 108 LYS A N   1 
ATOM   854  C CA  . LYS A 1 108 ? 6.16018  18.77255 -10.80989 1.000 74.45792  ? 108 LYS A CA  1 
ATOM   855  C C   . LYS A 1 108 ? 5.32990  17.61058 -11.35814 1.000 78.35809  ? 108 LYS A C   1 
ATOM   856  O O   . LYS A 1 108 ? 5.85958  16.52564 -11.61679 1.000 76.53396  ? 108 LYS A O   1 
ATOM   857  C CB  . LYS A 1 108 ? 6.89647  19.43579 -11.98359 0.800 73.77891  ? 108 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 108 ? 7.52729  20.80409 -11.71348 0.700 72.83424  ? 108 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 108 ? 8.11983  21.43401 -12.98648 0.600 73.34804  ? 108 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 108 ? 8.79384  22.77202 -12.67758 0.500 73.53506  ? 108 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 108 ? 9.29770  23.49699 -13.88151 0.500 74.95297  ? 108 LYS A NZ  1 
ATOM   862  N N   . TYR A 1 109 ? 4.03794  17.85985 -11.58514 1.000 84.62774  ? 109 TYR A N   1 
ATOM   863  C CA  . TYR A 1 109 ? 3.10600  16.81663 -12.03799 1.000 88.63065  ? 109 TYR A CA  1 
ATOM   864  C C   . TYR A 1 109 ? 2.58016  17.02028 -13.47076 1.000 91.16234  ? 109 TYR A C   1 
ATOM   865  O O   . TYR A 1 109 ? 3.02762  17.90118 -14.20861 1.000 91.00156  ? 109 TYR A O   1 
ATOM   866  C CB  . TYR A 1 109 ? 1.90838  16.71800 -11.07582 1.000 92.68851  ? 109 TYR A CB  1 
ATOM   867  C CG  . TYR A 1 109 ? 2.26190  16.56432 -9.60450  1.000 92.43913  ? 109 TYR A CG  1 
ATOM   868  C CD1 . TYR A 1 109 ? 2.55145  15.31673 -9.05952  1.000 91.72895  ? 109 TYR A CD1 1 
ATOM   869  C CD2 . TYR A 1 109 ? 2.28765  17.66692 -8.75662  1.000 93.29546  ? 109 TYR A CD2 1 
ATOM   870  C CE1 . TYR A 1 109 ? 2.87110  15.17584 -7.71277  1.000 91.16735  ? 109 TYR A CE1 1 
ATOM   871  C CE2 . TYR A 1 109 ? 2.60554  17.53352 -7.40907  1.000 92.53042  ? 109 TYR A CE2 1 
ATOM   872  C CZ  . TYR A 1 109 ? 2.89559  16.28712 -6.89517  1.000 91.59531  ? 109 TYR A CZ  1 
ATOM   873  O OH  . TYR A 1 109 ? 3.20858  16.15184 -5.56189  1.000 90.86862  ? 109 TYR A OH  1 
ATOM   874  N N   . LYS A 1 114 ? -0.00976 20.07372 -10.22444 1.000 96.29856  ? 114 LYS A N   1 
ATOM   875  C CA  . LYS A 1 114 ? 0.65606  21.37043 -10.16907 1.000 95.98723  ? 114 LYS A CA  1 
ATOM   876  C C   . LYS A 1 114 ? 2.14183  21.22580 -9.83468  1.000 91.55043  ? 114 LYS A C   1 
ATOM   877  O O   . LYS A 1 114 ? 2.89243  20.58600 -10.57338 1.000 89.64926  ? 114 LYS A O   1 
ATOM   878  C CB  . LYS A 1 114 ? -0.03003 22.27750 -9.14532  1.000 97.51361  ? 114 LYS A CB  1 
ATOM   879  N N   . GLU A 1 115 ? 2.55953  21.82225 -8.71799  1.000 89.53534  ? 115 GLU A N   1 
ATOM   880  C CA  . GLU A 1 115 ? 3.96435  21.82502 -8.32656  1.000 85.31683  ? 115 GLU A CA  1 
ATOM   881  C C   . GLU A 1 115 ? 4.05155  22.00196 -6.81841  1.000 82.30195  ? 115 GLU A C   1 
ATOM   882  O O   . GLU A 1 115 ? 3.49310  22.95888 -6.27770  1.000 84.26391  ? 115 GLU A O   1 
ATOM   883  C CB  . GLU A 1 115 ? 4.72835  22.94682 -9.03235  1.000 86.22821  ? 115 GLU A CB  1 
ATOM   884  C CG  . GLU A 1 115 ? 6.21748  22.91071 -8.78279  1.000 84.21712  ? 115 GLU A CG  1 
ATOM   885  C CD  . GLU A 1 115 ? 6.88111  24.23759 -9.05746  1.000 86.05483  ? 115 GLU A CD  1 
ATOM   886  O OE1 . GLU A 1 115 ? 6.86642  25.10406 -8.15838  0.860 86.97980  ? 115 GLU A OE1 1 
ATOM   887  O OE2 . GLU A 1 115 ? 7.40604  24.41859 -10.17485 1.000 86.83159  ? 115 GLU A OE2 1 
ATOM   888  N N   . ALA A 1 116 ? 4.76199  21.10174 -6.14480  1.000 78.33818  ? 116 ALA A N   1 
ATOM   889  C CA  . ALA A 1 116 ? 4.84526  21.14254 -4.69199  1.000 76.38327  ? 116 ALA A CA  1 
ATOM   890  C C   . ALA A 1 116 ? 6.29868  21.16877 -4.25254  1.000 71.13185  ? 116 ALA A C   1 
ATOM   891  O O   . ALA A 1 116 ? 7.14183  20.46731 -4.81949  1.000 68.66769  ? 116 ALA A O   1 
ATOM   892  C CB  . ALA A 1 116 ? 4.13070  19.94684 -4.05766  1.000 77.11679  ? 116 ALA A CB  1 
ATOM   893  N N   . THR A 1 117 ? 6.58904  21.97384 -3.23587  1.000 69.34777  ? 117 THR A N   1 
ATOM   894  C CA  . THR A 1 117 ? 7.94721  22.05839 -2.73350  1.000 64.37221  ? 117 THR A CA  1 
ATOM   895  C C   . THR A 1 117 ? 7.99732  21.64113 -1.26911  1.000 61.56584  ? 117 THR A C   1 
ATOM   896  O O   . THR A 1 117 ? 7.04217  21.83349 -0.50818  1.000 61.76889  ? 117 THR A O   1 
ATOM   897  C CB  . THR A 1 117 ? 8.53857  23.46602 -2.93944  1.000 63.58048  ? 117 THR A CB  1 
ATOM   898  O OG1 . THR A 1 117 ? 8.02364  24.37444 -1.95943  1.000 64.53564  ? 117 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 117 ? 8.18811  23.97975 -4.33348  1.000 64.37572  ? 117 THR A CG2 1 
ATOM   900  N N   . TYR A 1 118 ? 9.12101  21.02247 -0.91039  1.000 58.67186  ? 118 TYR A N   1 
ATOM   901  C CA  . TYR A 1 118 ? 9.39520  20.53530 0.43019   1.000 57.05927  ? 118 TYR A CA  1 
ATOM   902  C C   . TYR A 1 118 ? 10.75762 21.04310 0.86242   1.000 55.82324  ? 118 TYR A C   1 
ATOM   903  O O   . TYR A 1 118 ? 11.64580 21.27091 0.03725   1.000 54.83532  ? 118 TYR A O   1 
ATOM   904  C CB  . TYR A 1 118 ? 9.37090  19.00242 0.49376   1.000 55.68621  ? 118 TYR A CB  1 
ATOM   905  C CG  . TYR A 1 118 ? 8.09277  18.44195 -0.04833  1.000 57.58225  ? 118 TYR A CG  1 
ATOM   906  C CD1 . TYR A 1 118 ? 7.93157  18.23228 -1.40850  1.000 57.79341  ? 118 TYR A CD1 1 
ATOM   907  C CD2 . TYR A 1 118 ? 7.03006  18.16337 0.79258   1.000 58.98213  ? 118 TYR A CD2 1 
ATOM   908  C CE1 . TYR A 1 118 ? 6.75009  17.74565 -1.91636  1.000 59.62951  ? 118 TYR A CE1 1 
ATOM   909  C CE2 . TYR A 1 118 ? 5.84769  17.67336 0.30054   1.000 60.79948  ? 118 TYR A CE2 1 
ATOM   910  C CZ  . TYR A 1 118 ? 5.71118  17.46618 -1.05417  1.000 61.26696  ? 118 TYR A CZ  1 
ATOM   911  O OH  . TYR A 1 118 ? 4.52678  16.97622 -1.53918  1.000 63.47166  ? 118 TYR A OH  1 
ATOM   912  N N   . LEU A 1 119 ? 10.90624 21.22132 2.16820   1.000 56.03947  ? 119 LEU A N   1 
ATOM   913  C CA  . LEU A 1 119 ? 12.15515 21.64072 2.78435   1.000 54.47242  ? 119 LEU A CA  1 
ATOM   914  C C   . LEU A 1 119 ? 12.60763 20.50029 3.68315   1.000 51.71493  ? 119 LEU A C   1 
ATOM   915  O O   . LEU A 1 119 ? 11.84343 20.05294 4.54275   1.000 51.83526  ? 119 LEU A O   1 
ATOM   916  C CB  . LEU A 1 119 ? 11.94861 22.93079 3.58316   1.000 57.05438  ? 119 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 119 ? 13.02797 24.00968 3.65567   1.000 57.57859  ? 119 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 119 ? 13.39941 24.50172 2.26927   1.000 57.73325  ? 119 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 119 ? 12.53246 25.16248 4.51006   1.000 59.66324  ? 119 LEU A CD2 1 
ATOM   920  N N   . ALA A 1 120 ? 13.82425 20.00907 3.47565   1.000 49.31824  ? 120 ALA A N   1 
ATOM   921  C CA  . ALA A 1 120 ? 14.35162 18.91564 4.27927   1.000 48.72657  ? 120 ALA A CA  1 
ATOM   922  C C   . ALA A 1 120 ? 15.47550 19.42401 5.17100   1.000 48.28246  ? 120 ALA A C   1 
ATOM   923  O O   . ALA A 1 120 ? 16.27572 20.26335 4.75247   1.000 48.73587  ? 120 ALA A O   1 
ATOM   924  C CB  . ALA A 1 120 ? 14.86062 17.77244 3.39470   1.000 47.95805  ? 120 ALA A CB  1 
ATOM   925  N N   . LEU A 1 121 ? 15.52791 18.92985 6.40775   1.000 47.40325  ? 121 LEU A N   1 
ATOM   926  C CA  . LEU A 1 121 ? 16.70090 19.16062 7.24535   1.000 46.53877  ? 121 LEU A CA  1 
ATOM   927  C C   . LEU A 1 121 ? 17.66811 17.99012 7.21834   1.000 44.46626  ? 121 LEU A C   1 
ATOM   928  O O   . LEU A 1 121 ? 18.87148 18.18245 7.41067   1.000 43.13567  ? 121 LEU A O   1 
ATOM   929  C CB  . LEU A 1 121 ? 16.30333 19.45444 8.70126   1.000 47.50911  ? 121 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 121 ? 17.43966 19.59440 9.73731   1.000 47.75803  ? 121 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 121 ? 18.44489 20.68728 9.36060   1.000 47.98035  ? 121 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 121 ? 16.91691 19.81687 11.15438  1.000 49.02097  ? 121 LEU A CD2 1 
ATOM   933  N N   . ASN A 1 122 ? 17.18045 16.78190 6.96899   1.000 44.04736  ? 122 ASN A N   1 
ATOM   934  C CA  . ASN A 1 122 ? 18.06072 15.63506 6.81292   1.000 42.84174  ? 122 ASN A CA  1 
ATOM   935  C C   . ASN A 1 122 ? 18.27670 15.29981 5.34355   1.000 41.78152  ? 122 ASN A C   1 
ATOM   936  O O   . ASN A 1 122 ? 19.40678 15.35809 4.85148   1.000 41.17070  ? 122 ASN A O   1 
ATOM   937  C CB  . ASN A 1 122 ? 17.49405 14.43427 7.57415   1.000 43.29161  ? 122 ASN A CB  1 
ATOM   938  C CG  . ASN A 1 122 ? 18.02298 14.34357 8.98039   1.000 43.96038  ? 122 ASN A CG  1 
ATOM   939  O OD1 . ASN A 1 122 ? 18.86520 15.14248 9.39248   1.000 44.09408  ? 122 ASN A OD1 1 
ATOM   940  N ND2 . ASN A 1 122 ? 17.52676 13.37323 9.73401   1.000 44.31859  ? 122 ASN A ND2 1 
ATOM   941  N N   . GLU A 1 123 ? 17.20739 14.98708 4.62413   1.000 41.54086  ? 123 GLU A N   1 
ATOM   942  C CA  . GLU A 1 123 ? 17.39685 14.51878 3.26746   1.000 41.30268  ? 123 GLU A CA  1 
ATOM   943  C C   . GLU A 1 123 ? 16.04060 14.30967 2.62061   1.000 42.57329  ? 123 GLU A C   1 
ATOM   944  O O   . GLU A 1 123 ? 15.01655 14.19168 3.29992   1.000 42.82206  ? 123 GLU A O   1 
ATOM   945  C CB  . GLU A 1 123 ? 18.20642 13.21462 3.23206   1.000 40.04339  ? 123 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 123 ? 17.43794 11.99941 3.67712   1.000 40.04166  ? 123 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 123 ? 17.14760 11.99922 5.15310   1.000 40.38761  ? 123 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 123 ? 18.10686 11.99676 5.95252   1.000 39.64638  ? 123 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 123 ? 15.95385 12.01036 5.52366   1.000 40.64767  ? 123 GLU A OE2 1 
ATOM   950  N N   . SER A 1 124 ? 16.05176 14.25729 1.29459   1.000 43.34242  ? 124 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 14.87351 13.89292 0.52768   1.000 44.45349  ? 124 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 15.19016 12.64024 -0.25926  1.000 43.20170  ? 124 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 16.12323 12.62609 -1.06832  1.000 41.64265  ? 124 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 14.42911 15.00529 -0.41269  1.000 45.78103  ? 124 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 13.39019 14.52380 -1.24593  1.000 47.39939  ? 124 SER A OG  1 
ATOM   956  N N   . THR A 1 125 ? 14.42544 11.59344 -0.02746  1.000 43.69498  ? 125 THR A N   1 
ATOM   957  C CA  . THR A 1 125 ? 14.65985 10.36927 -0.75899  1.000 43.99654  ? 125 THR A CA  1 
ATOM   958  C C   . THR A 1 125 ? 13.49368 10.09100 -1.69137  1.000 45.83146  ? 125 THR A C   1 
ATOM   959  O O   . THR A 1 125 ? 12.38473 10.61938 -1.53882  1.000 47.75463  ? 125 THR A O   1 
ATOM   960  C CB  . THR A 1 125 ? 14.89345 9.18719  0.18740   1.000 44.06872  ? 125 THR A CB  1 
ATOM   961  O OG1 . THR A 1 125 ? 13.63794 8.75557  0.72827   1.000 45.55446  ? 125 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 125 ? 15.81631 9.60739  1.30717   1.000 43.03523  ? 125 THR A CG2 1 
ATOM   963  N N   . VAL A 1 126 ? 13.80200 9.28205  -2.69686  1.000 45.51067  ? 126 VAL A N   1 
ATOM   964  C CA  . VAL A 1 126 ? 12.86699 8.86630  -3.72427  1.000 46.66898  ? 126 VAL A CA  1 
ATOM   965  C C   . VAL A 1 126 ? 13.00668 7.37807  -3.87546  1.000 47.14624  ? 126 VAL A C   1 
ATOM   966  O O   . VAL A 1 126 ? 14.11204 6.87275  -4.08784  1.000 46.29348  ? 126 VAL A O   1 
ATOM   967  C CB  . VAL A 1 126 ? 13.14066 9.52123  -5.08643  1.000 47.07533  ? 126 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 126 ? 11.85733 9.67130  -5.84902  1.000 48.39254  ? 126 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 126 ? 13.83915 10.77919 -4.91020  1.000 46.58192  ? 126 VAL A CG2 1 
ATOM   970  N N   . LYS A 1 127 ? 11.88856 6.68731  -3.81978  1.000 49.88301  ? 127 LYS A N   1 
ATOM   971  C CA  . LYS A 1 127 ? 11.87226 5.30073  -4.20142  1.000 52.69235  ? 127 LYS A CA  1 
ATOM   972  C C   . LYS A 1 127 ? 10.71320 5.08629  -5.13982  1.000 58.74344  ? 127 LYS A C   1 
ATOM   973  O O   . LYS A 1 127 ? 9.92418  5.99685  -5.41206  1.000 58.97751  ? 127 LYS A O   1 
ATOM   974  C CB  . LYS A 1 127 ? 11.77468 4.38340  -2.98463  0.900 52.60173  ? 127 LYS A CB  1 
ATOM   975  C CG  . LYS A 1 127 ? 12.95982 4.47486  -2.09470  0.800 50.53072  ? 127 LYS A CG  1 
ATOM   976  C CD  . LYS A 1 127 ? 12.73546 3.68499  -0.83964  0.800 50.88007  ? 127 LYS A CD  1 
ATOM   977  C CE  . LYS A 1 127 ? 13.44389 4.38221  0.29359   0.700 49.71004  ? 127 LYS A CE  1 
ATOM   978  N NZ  . LYS A 1 127 ? 13.49631 3.59317  1.54503   0.700 50.16585  ? 127 LYS A NZ  1 
ATOM   979  N N   . SER A 1 128 ? 10.60953 3.86260  -5.61512  1.000 64.65817  ? 128 SER A N   1 
ATOM   980  C CA  . SER A 1 128 ? 9.52659  3.53376  -6.50556  1.000 73.96347  ? 128 SER A CA  1 
ATOM   981  C C   . SER A 1 128 ? 8.35873  2.96112  -5.72389  1.000 81.96951  ? 128 SER A C   1 
ATOM   982  O O   . SER A 1 128 ? 8.51741  2.41586  -4.62901  1.000 82.82931  ? 128 SER A O   1 
ATOM   983  C CB  . SER A 1 128 ? 9.98664  2.54641  -7.56271  1.000 74.21919  ? 128 SER A CB  1 
ATOM   984  O OG  . SER A 1 128 ? 8.87416  2.13802  -8.33482  1.000 77.73695  ? 128 SER A OG  1 
ATOM   985  N N   . SER A 1 129 ? 7.17862  3.10497  -6.30110  1.000 87.90749  ? 129 SER A N   1 
ATOM   986  C CA  . SER A 1 129 ? 5.96196  2.52595  -5.75442  1.000 94.08911  ? 129 SER A CA  1 
ATOM   987  C C   . SER A 1 129 ? 5.67816  1.26344  -6.55492  1.000 99.62726  ? 129 SER A C   1 
ATOM   988  O O   . SER A 1 129 ? 5.18351  1.32927  -7.68289  1.000 100.99002 ? 129 SER A O   1 
ATOM   989  C CB  . SER A 1 129 ? 4.81243  3.51584  -5.84594  1.000 95.11575  ? 129 SER A CB  1 
ATOM   990  O OG  . SER A 1 129 ? 4.43587  3.66189  -7.20070  1.000 96.82915  ? 129 SER A OG  1 
ATOM   991  N N   . GLY A 1 130 ? 6.00333  0.11418  -5.97632  0.970 101.56751 ? 130 GLY A N   1 
ATOM   992  C CA  . GLY A 1 130 ? 5.76914  -1.14315 -6.65501  0.970 105.67277 ? 130 GLY A CA  1 
ATOM   993  C C   . GLY A 1 130 ? 6.87710  -1.54207 -7.60817  0.970 106.14997 ? 130 GLY A C   1 
ATOM   994  O O   . GLY A 1 130 ? 7.68768  -2.41644 -7.28692  0.970 106.13143 ? 130 GLY A O   1 
ATOM   995  N N   . GLY A 1 131 ? 6.93121  -0.89610 -8.78097  1.000 100.24089 ? 131 GLY A N   1 
ATOM   996  C CA  . GLY A 1 131 ? 7.80586  -1.32628 -9.83674  1.000 94.25152  ? 131 GLY A CA  1 
ATOM   997  C C   . GLY A 1 131 ? 9.26425  -0.97887 -9.54885  1.000 87.29320  ? 131 GLY A C   1 
ATOM   998  O O   . GLY A 1 131 ? 9.60472  -0.41812 -8.49447  1.000 88.08842  ? 131 GLY A O   1 
ATOM   999  N N   . PRO A 1 132 ? 10.15016 -1.32614 -10.48157 0.980 79.90621  ? 132 PRO A N   1 
ATOM   1000 C CA  . PRO A 1 132 ? 11.54738 -0.93847 -10.32153 0.980 71.70990  ? 132 PRO A CA  1 
ATOM   1001 C C   . PRO A 1 132 ? 11.69115 0.55252  -10.51427 0.980 66.18162  ? 132 PRO A C   1 
ATOM   1002 O O   . PRO A 1 132 ? 10.91408 1.19797  -11.22729 0.980 67.35229  ? 132 PRO A O   1 
ATOM   1003 C CB  . PRO A 1 132 ? 12.27669 -1.72115 -11.42496 0.980 72.08537  ? 132 PRO A CB  1 
ATOM   1004 C CG  . PRO A 1 132 ? 11.31225 -2.75149 -11.87652 0.980 75.97609  ? 132 PRO A CG  1 
ATOM   1005 C CD  . PRO A 1 132 ? 9.96873  -2.10319 -11.70776 0.980 79.16607  ? 132 PRO A CD  1 
ATOM   1006 N N   . PHE A 1 133 ? 12.70449 1.09317  -9.86547  1.000 59.97883  ? 133 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 133 ? 12.96518 2.51660  -9.90289  1.000 55.83755  ? 133 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 133 ? 13.96132 2.78617  -11.02278 1.000 53.99762  ? 133 PHE A C   1 
ATOM   1009 O O   . PHE A 1 133 ? 15.08332 2.27302  -10.99698 1.000 52.89109  ? 133 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 133 ? 13.47720 2.96181  -8.53744  1.000 52.86147  ? 133 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 133 ? 13.86650 4.39491  -8.46633  1.000 50.32305  ? 133 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 133 ? 12.90910 5.39371  -8.40932  1.000 50.09818  ? 133 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 133 ? 15.20038 4.74362  -8.42294  1.000 47.96543  ? 133 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 133 ? 13.28419 6.71955  -8.32953  1.000 48.46366  ? 133 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 133 ? 15.58313 6.05883  -8.34172  1.000 46.32785  ? 133 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 133 ? 14.62611 7.05202  -8.29561  1.000 46.68870  ? 133 PHE A CZ  1 
ATOM   1017 N N   . VAL A 1 134 ? 13.52370 3.53037  -12.03679 1.000 53.80314  ? 134 VAL A N   1 
ATOM   1018 C CA  . VAL A 1 134 ? 14.35310 3.91091  -13.17495 1.000 51.71809  ? 134 VAL A CA  1 
ATOM   1019 C C   . VAL A 1 134 ? 14.11132 5.38314  -13.43922 1.000 51.01511  ? 134 VAL A C   1 
ATOM   1020 O O   . VAL A 1 134 ? 13.03482 5.76017  -13.91557 1.000 52.21441  ? 134 VAL A O   1 
ATOM   1021 C CB  . VAL A 1 134 ? 14.03644 3.10813  -14.44242 1.000 52.17072  ? 134 VAL A CB  1 
ATOM   1022 C CG1 . VAL A 1 134 ? 15.17701 3.25577  -15.45097 1.000 51.26269  ? 134 VAL A CG1 1 
ATOM   1023 C CG2 . VAL A 1 134 ? 13.74118 1.66097  -14.12885 1.000 52.51093  ? 134 VAL A CG2 1 
ATOM   1024 N N   . VAL A 1 135 ? 15.10395 6.21233  -13.17087 1.000 49.14551  ? 135 VAL A N   1 
ATOM   1025 C CA  . VAL A 1 135 ? 15.02635 7.59507  -13.60731 1.000 49.31569  ? 135 VAL A CA  1 
ATOM   1026 C C   . VAL A 1 135 ? 16.30728 7.94777  -14.35090 1.000 48.81794  ? 135 VAL A C   1 
ATOM   1027 O O   . VAL A 1 135 ? 17.36900 7.35841  -14.12098 1.000 47.84035  ? 135 VAL A O   1 
ATOM   1028 C CB  . VAL A 1 135 ? 14.76763 8.56347  -12.42883 1.000 48.76571  ? 135 VAL A CB  1 
ATOM   1029 C CG1 . VAL A 1 135 ? 13.49836 8.16501  -11.67918 1.000 49.72641  ? 135 VAL A CG1 1 
ATOM   1030 C CG2 . VAL A 1 135 ? 15.95378 8.59171  -11.49678 1.000 46.86270  ? 135 VAL A CG2 1 
ATOM   1031 N N   . ASP A 1 136 ? 16.17629 8.86922  -15.30408 1.000 50.26454  ? 136 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 136 ? 17.31889 9.57902  -15.86180 1.000 49.90416  ? 136 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 136 ? 17.68150 10.71821 -14.91513 1.000 48.34241  ? 136 ASP A C   1 
ATOM   1034 O O   . ASP A 1 136 ? 16.80024 11.39516 -14.38334 1.000 48.34627  ? 136 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 136 ? 16.99037 10.14878 -17.24943 1.000 52.15144  ? 136 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 136 ? 16.76227 9.07522  -18.31542 1.000 53.33184  ? 136 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 136 ? 17.48674 8.05870  -18.33145 0.690 52.79319  ? 136 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 136 ? 15.86313 9.27265  -19.16334 1.000 55.27920  ? 136 ASP A OD2 1 
ATOM   1039 N N   . VAL A 1 137 ? 18.97581 10.93700 -14.70132 1.000 46.96003  ? 137 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 137 ? 19.45708 11.95808 -13.77390 1.000 46.53684  ? 137 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 137 ? 20.02777 13.12156 -14.58468 1.000 48.11211  ? 137 VAL A C   1 
ATOM   1042 O O   . VAL A 1 137 ? 20.88635 12.91453 -15.45155 1.000 49.03570  ? 137 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 137 ? 20.50195 11.37642 -12.80279 1.000 45.49144  ? 137 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 137 ? 21.01369 12.44946 -11.86354 1.000 44.96140  ? 137 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 137 ? 19.91062 10.21196 -12.00453 1.000 44.99202  ? 137 VAL A CG2 1 
ATOM   1046 N N   . VAL A 1 138 ? 19.54601 14.34046 -14.31149 1.000 48.85798  ? 138 VAL A N   1 
ATOM   1047 C CA  . VAL A 1 138 ? 19.92719 15.53107 -15.06988 1.000 50.64034  ? 138 VAL A CA  1 
ATOM   1048 C C   . VAL A 1 138 ? 20.50098 16.58980 -14.13736 1.000 50.77790  ? 138 VAL A C   1 
ATOM   1049 O O   . VAL A 1 138 ? 19.82525 17.01761 -13.18872 1.000 50.25935  ? 138 VAL A O   1 
ATOM   1050 C CB  . VAL A 1 138 ? 18.75106 16.12743 -15.85729 1.000 51.81363  ? 138 VAL A CB  1 
ATOM   1051 C CG1 . VAL A 1 138 ? 19.24507 17.23336 -16.73673 1.000 53.02310  ? 138 VAL A CG1 1 
ATOM   1052 C CG2 . VAL A 1 138 ? 18.05917 15.07423 -16.69795 1.000 51.78808  ? 138 VAL A CG2 1 
ATOM   1053 N N   . ILE A 1 139 ? 21.70258 17.05540 -14.46550 1.000 51.57319  ? 139 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 139 ? 22.46863 17.98830 -13.64370 1.000 51.39534  ? 139 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 139 ? 22.62306 19.27438 -14.44202 1.000 52.87624  ? 139 ILE A C   1 
ATOM   1056 O O   . ILE A 1 139 ? 23.35808 19.28917 -15.44024 1.000 54.08717  ? 139 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 139 ? 23.84201 17.42009 -13.24646 1.000 51.26921  ? 139 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 139 ? 23.69788 16.07256 -12.54964 1.000 49.36181  ? 139 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 139 ? 24.57019 18.36949 -12.35594 1.000 52.02748  ? 139 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 139 ? 25.02990 15.35545 -12.37820 1.000 48.43068  ? 139 ILE A CD1 1 
ATOM   1061 N N   . ASN A 1 140 ? 21.97700 20.36299 -13.99366 1.000 53.80000  ? 140 ASN A N   1 
ATOM   1062 C CA  . ASN A 1 140 ? 22.00283 21.62697 -14.73938 1.000 56.18791  ? 140 ASN A CA  1 
ATOM   1063 C C   . ASN A 1 140 ? 21.69522 21.37370 -16.21732 1.000 57.57157  ? 140 ASN A C   1 
ATOM   1064 O O   . ASN A 1 140 ? 22.44451 21.78110 -17.11163 1.000 59.65146  ? 140 ASN A O   1 
ATOM   1065 C CB  . ASN A 1 140 ? 23.36341 22.31435 -14.60733 1.000 57.53541  ? 140 ASN A CB  1 
ATOM   1066 C CG  . ASN A 1 140 ? 23.74910 22.61018 -13.17750 1.000 57.45059  ? 140 ASN A CG  1 
ATOM   1067 O OD1 . ASN A 1 140 ? 22.95819 23.15629 -12.40880 1.000 57.50643  ? 140 ASN A OD1 1 
ATOM   1068 N ND2 . ASN A 1 140 ? 24.97238 22.25255 -12.81066 1.000 56.88915  ? 140 ASN A ND2 1 
ATOM   1069 N N   . ASP A 1 141 ? 20.60175 20.65375 -16.47017 1.000 57.01227  ? 141 ASP A N   1 
ATOM   1070 C CA  . ASP A 1 141 ? 20.09826 20.35528 -17.81156 1.000 59.85227  ? 141 ASP A CA  1 
ATOM   1071 C C   . ASP A 1 141 ? 21.01794 19.43843 -18.62827 1.000 61.65896  ? 141 ASP A C   1 
ATOM   1072 O O   . ASP A 1 141 ? 20.90289 19.39400 -19.85968 1.000 64.54549  ? 141 ASP A O   1 
ATOM   1073 C CB  . ASP A 1 141 ? 19.81227 21.64549 -18.59011 1.000 61.58881  ? 141 ASP A CB  1 
ATOM   1074 C CG  . ASP A 1 141 ? 18.62725 22.41173 -18.03284 0.560 61.73879  ? 141 ASP A CG  1 
ATOM   1075 O OD1 . ASP A 1 141 ? 17.78220 21.78641 -17.36088 0.770 60.02022  ? 141 ASP A OD1 1 
ATOM   1076 O OD2 . ASP A 1 141 ? 18.53765 23.63698 -18.26771 0.270 63.61878  ? 141 ASP A OD2 1 
ATOM   1077 N N   . ILE A 1 142 ? 21.89193 18.66893 -17.97176 1.000 61.29348  ? 142 ILE A N   1 
ATOM   1078 C CA  A ILE A 1 142 ? 22.82341 17.77729 -18.65190 0.360 60.56288  ? 142 ILE A CA  1 
ATOM   1079 C CA  B ILE A 1 142 ? 22.87457 17.78067 -18.60530 0.640 60.52143  ? 142 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 142 ? 22.49366 16.33997 -18.25097 1.000 58.10141  ? 142 ILE A C   1 
ATOM   1081 O O   . ILE A 1 142 ? 22.53531 15.98285 -17.06725 1.000 55.28533  ? 142 ILE A O   1 
ATOM   1082 C CB  A ILE A 1 142 ? 24.28393 18.13371 -18.32850 0.360 60.46242  ? 142 ILE A CB  1 
ATOM   1083 C CB  B ILE A 1 142 ? 24.30277 18.08588 -18.09754 0.640 60.76438  ? 142 ILE A CB  1 
ATOM   1084 C CG1 A ILE A 1 142 ? 24.57843 19.59486 -18.69955 0.360 62.29671  ? 142 ILE A CG1 1 
ATOM   1085 C CG1 B ILE A 1 142 ? 24.89314 19.39886 -18.63818 0.640 62.08355  ? 142 ILE A CG1 1 
ATOM   1086 C CG2 A ILE A 1 142 ? 25.23419 17.18290 -19.02105 0.360 61.61464  ? 142 ILE A CG2 1 
ATOM   1087 C CG2 B ILE A 1 142 ? 25.25113 16.90682 -18.31076 0.640 60.41652  ? 142 ILE A CG2 1 
ATOM   1088 C CD1 A ILE A 1 142 ? 24.03695 20.02748 -20.05383 0.360 65.00228  ? 142 ILE A CD1 1 
ATOM   1089 C CD1 B ILE A 1 142 ? 26.11901 19.88993 -17.82424 0.640 62.73117  ? 142 ILE A CD1 1 
ATOM   1090 N N   . HIS A 1 143 ? 22.13786 15.49457 -19.24848 1.000 58.03557  ? 143 HIS A N   1 
ATOM   1091 C CA  . HIS A 1 143 ? 21.81846 14.08603 -18.93894 1.000 56.04377  ? 143 HIS A CA  1 
ATOM   1092 C C   . HIS A 1 143 ? 23.07008 13.35125 -18.49603 1.000 52.38670  ? 143 HIS A C   1 
ATOM   1093 O O   . HIS A 1 143 ? 24.01022 13.17535 -19.27897 1.000 53.30259  ? 143 HIS A O   1 
ATOM   1094 C CB  A HIS A 1 143 ? 21.18682 13.31046 -20.10417 0.600 58.08970  ? 143 HIS A CB  1 
ATOM   1095 C CB  B HIS A 1 143 ? 21.21241 13.40001 -20.16261 0.400 58.19964  ? 143 HIS A CB  1 
ATOM   1096 C CG  A HIS A 1 143 ? 20.98361 11.83639 -19.81556 0.600 57.75488  ? 143 HIS A CG  1 
ATOM   1097 C CG  B HIS A 1 143 ? 19.82195 13.84896 -20.49053 0.400 60.11761  ? 143 HIS A CG  1 
ATOM   1098 N ND1 A HIS A 1 143 ? 22.02156 10.92563 -19.78021 0.600 57.41851  ? 143 HIS A ND1 1 
ATOM   1099 N ND1 B HIS A 1 143 ? 18.77165 12.96784 -20.63314 0.400 60.33276  ? 143 HIS A ND1 1 
ATOM   1100 C CD2 A HIS A 1 143 ? 19.85969 11.12149 -19.55553 0.600 57.86019  ? 143 HIS A CD2 1 
ATOM   1101 C CD2 B HIS A 1 143 ? 19.30860 15.08301 -20.70711 0.400 61.46428  ? 143 HIS A CD2 1 
ATOM   1102 C CE1 A HIS A 1 143 ? 21.54941 9.72190  -19.50438 0.600 56.97566  ? 143 HIS A CE1 1 
ATOM   1103 C CE1 B HIS A 1 143 ? 17.67163 13.63944 -20.92296 0.400 61.87815  ? 143 HIS A CE1 1 
ATOM   1104 N NE2 A HIS A 1 143 ? 20.23935 9.81239  -19.36634 0.600 57.25923  ? 143 HIS A NE2 1 
ATOM   1105 N NE2 B HIS A 1 143 ? 17.97036 14.92492 -20.97458 0.400 62.34561  ? 143 HIS A NE2 1 
ATOM   1106 N N   . PHE A 1 144 ? 23.03686 12.84126 -17.27199 1.000 48.52974  ? 144 PHE A N   1 
ATOM   1107 C CA  . PHE A 1 144 ? 24.21165 12.30012 -16.61317 1.000 45.52994  ? 144 PHE A CA  1 
ATOM   1108 C C   . PHE A 1 144 ? 24.23913 10.77923 -16.54649 1.000 43.30423  ? 144 PHE A C   1 
ATOM   1109 O O   . PHE A 1 144 ? 25.25981 10.16255 -16.85012 1.000 43.68260  ? 144 PHE A O   1 
ATOM   1110 C CB  . PHE A 1 144 ? 24.29547 12.88430 -15.20351 1.000 44.23695  ? 144 PHE A CB  1 
ATOM   1111 C CG  . PHE A 1 144 ? 25.46354 12.39971 -14.44346 1.000 43.18496  ? 144 PHE A CG  1 
ATOM   1112 C CD1 . PHE A 1 144 ? 26.71635 12.92157 -14.68826 1.000 44.05347  ? 144 PHE A CD1 1 
ATOM   1113 C CD2 . PHE A 1 144 ? 25.32161 11.40079 -13.50238 1.000 41.63060  ? 144 PHE A CD2 1 
ATOM   1114 C CE1 . PHE A 1 144 ? 27.80622 12.46733 -13.99849 1.000 43.40390  ? 144 PHE A CE1 1 
ATOM   1115 C CE2 . PHE A 1 144 ? 26.40703 10.93841 -12.80687 1.000 40.86255  ? 144 PHE A CE2 1 
ATOM   1116 C CZ  . PHE A 1 144 ? 27.65511 11.47236 -13.05298 1.000 41.90586  ? 144 PHE A CZ  1 
ATOM   1117 N N   . GLU A 1 145 ? 23.15854 10.14671 -16.11532 1.000 41.73793  ? 145 GLU A N   1 
ATOM   1118 C CA  . GLU A 1 145 ? 23.13467 8.69455  -16.05602 1.000 41.56538  ? 145 GLU A CA  1 
ATOM   1119 C C   . GLU A 1 145 ? 21.68080 8.27122  -16.09819 1.000 42.15221  ? 145 GLU A C   1 
ATOM   1120 O O   . GLU A 1 145 ? 20.77960 9.08589  -15.89115 1.000 42.13419  ? 145 GLU A O   1 
ATOM   1121 C CB  . GLU A 1 145 ? 23.83516 8.16215  -14.79351 1.000 39.76359  ? 145 GLU A CB  1 
ATOM   1122 C CG  . GLU A 1 145 ? 23.20262 8.62471  -13.47656 1.000 38.13627  ? 145 GLU A CG  1 
ATOM   1123 C CD  . GLU A 1 145 ? 23.96447 8.20483  -12.22240 1.000 36.13055  ? 145 GLU A CD  1 
ATOM   1124 O OE1 . GLU A 1 145 ? 25.08464 7.65804  -12.32104 0.730 36.06865  ? 145 GLU A OE1 1 
ATOM   1125 O OE2 . GLU A 1 145 ? 23.42976 8.43174  -11.11199 0.620 34.56805  ? 145 GLU A OE2 1 
ATOM   1126 N N   . ARG A 1 146 ? 21.45334 7.00180  -16.39215 1.000 42.94530  ? 146 ARG A N   1 
ATOM   1127 C CA  . ARG A 1 146 ? 20.13057 6.41741  -16.22452 1.000 43.47880  ? 146 ARG A CA  1 
ATOM   1128 C C   . ARG A 1 146 ? 20.20369 5.43983  -15.06117 1.000 42.48948  ? 146 ARG A C   1 
ATOM   1129 O O   . ARG A 1 146 ? 20.77965 4.35306  -15.18765 1.000 42.81424  ? 146 ARG A O   1 
ATOM   1130 C CB  . ARG A 1 146 ? 19.63973 5.73706  -17.49521 1.000 45.08506  ? 146 ARG A CB  1 
ATOM   1131 C CG  . ARG A 1 146 ? 18.37003 4.94799  -17.25729 1.000 45.84630  ? 146 ARG A CG  1 
ATOM   1132 C CD  . ARG A 1 146 ? 17.67978 4.59054  -18.54631 1.000 47.77873  ? 146 ARG A CD  1 
ATOM   1133 N NE  . ARG A 1 146 ? 17.12081 5.76567  -19.19997 1.000 49.13761  ? 146 ARG A NE  1 
ATOM   1134 C CZ  . ARG A 1 146 ? 16.45893 5.73761  -20.34705 1.000 52.50816  ? 146 ARG A CZ  1 
ATOM   1135 N NH1 . ARG A 1 146 ? 16.25667 4.60594  -20.99670 1.000 54.09391  ? 146 ARG A NH1 1 
ATOM   1136 N NH2 . ARG A 1 146 ? 15.98743 6.87202  -20.85240 1.000 53.66561  ? 146 ARG A NH2 1 
ATOM   1137 N N   . PHE A 1 147 ? 19.62583 5.83458  -13.93092 1.000 41.24815  ? 147 PHE A N   1 
ATOM   1138 C CA  . PHE A 1 147 ? 19.76206 5.08309  -12.69397 1.000 40.73655  ? 147 PHE A CA  1 
ATOM   1139 C C   . PHE A 1 147 ? 18.68727 4.01583  -12.59248 1.000 41.98461  ? 147 PHE A C   1 
ATOM   1140 O O   . PHE A 1 147 ? 17.49086 4.31783  -12.65087 1.000 42.57310  ? 147 PHE A O   1 
ATOM   1141 C CB  . PHE A 1 147 ? 19.67183 5.99498  -11.47209 1.000 39.98438  ? 147 PHE A CB  1 
ATOM   1142 C CG  . PHE A 1 147 ? 19.75756 5.25112  -10.16784 1.000 39.32817  ? 147 PHE A CG  1 
ATOM   1143 C CD1 . PHE A 1 147 ? 18.65288 4.59383  -9.64282  1.000 39.64443  ? 147 PHE A CD1 1 
ATOM   1144 C CD2 . PHE A 1 147 ? 20.94767 5.20195  -9.47064  1.000 38.32104  ? 147 PHE A CD2 1 
ATOM   1145 C CE1 . PHE A 1 147 ? 18.73949 3.90423  -8.45948  1.000 39.41534  ? 147 PHE A CE1 1 
ATOM   1146 C CE2 . PHE A 1 147 ? 21.03861 4.51818  -8.27926  1.000 37.79339  ? 147 PHE A CE2 1 
ATOM   1147 C CZ  . PHE A 1 147 ? 19.93171 3.86511  -7.77321  1.000 38.37826  ? 147 PHE A CZ  1 
ATOM   1148 N N   . ARG A 1 148 ? 19.11370 2.78460  -12.35112 1.000 42.83945  ? 148 ARG A N   1 
ATOM   1149 C CA  . ARG A 1 148 ? 18.19037 1.69099  -12.09358 1.000 45.15531  ? 148 ARG A CA  1 
ATOM   1150 C C   . ARG A 1 148 ? 18.62290 0.97917  -10.82110 1.000 46.00396  ? 148 ARG A C   1 
ATOM   1151 O O   . ARG A 1 148 ? 19.66203 0.31404  -10.79984 1.000 45.06333  ? 148 ARG A O   1 
ATOM   1152 C CB  . ARG A 1 148 ? 18.15590 0.73727  -13.27081 1.000 45.98879  ? 148 ARG A CB  1 
ATOM   1153 C CG  . ARG A 1 148 ? 17.10370 -0.28722 -13.14450 0.800 47.55844  ? 148 ARG A CG  1 
ATOM   1154 C CD  . ARG A 1 148 ? 17.18326 -1.13414 -14.35029 0.700 49.18042  ? 148 ARG A CD  1 
ATOM   1155 N NE  . ARG A 1 148 ? 16.35336 -2.31537 -14.22903 0.600 50.77412  ? 148 ARG A NE  1 
ATOM   1156 C CZ  . ARG A 1 148 ? 15.07289 -2.35647 -14.56076 0.600 51.84457  ? 148 ARG A CZ  1 
ATOM   1157 N NH1 . ARG A 1 148 ? 14.45034 -1.29463 -15.04424 0.600 51.65203  ? 148 ARG A NH1 1 
ATOM   1158 N NH2 . ARG A 1 148 ? 14.40217 -3.49031 -14.40689 0.600 53.44507  ? 148 ARG A NH2 1 
ATOM   1159 N N   . GLY A 1 149 ? 17.82656 1.11448  -9.76724  1.000 48.01318  ? 149 GLY A N   1 
ATOM   1160 C CA  . GLY A 1 149 ? 18.17978 0.55660  -8.48057  1.000 47.20194  ? 149 GLY A CA  1 
ATOM   1161 C C   . GLY A 1 149 ? 17.02368 0.60011  -7.50775  1.000 46.86885  ? 149 GLY A C   1 
ATOM   1162 O O   . GLY A 1 149 ? 15.86029 0.52224  -7.91557  1.000 48.24202  ? 149 GLY A O   1 
ATOM   1163 N N   . ASP A 1 150 ? 17.32764 0.71391  -6.21397  1.000 44.20511  ? 150 ASP A N   1 
ATOM   1164 C CA  . ASP A 1 150 ? 16.27970 0.87476  -5.21183  1.000 42.97426  ? 150 ASP A CA  1 
ATOM   1165 C C   . ASP A 1 150 ? 15.87986 2.32901  -4.99374  1.000 42.02362  ? 150 ASP A C   1 
ATOM   1166 O O   . ASP A 1 150 ? 14.70780 2.60275  -4.70450  1.000 42.98986  ? 150 ASP A O   1 
ATOM   1167 C CB  . ASP A 1 150 ? 16.70589 0.25393  -3.87635  1.000 41.26846  ? 150 ASP A CB  1 
ATOM   1168 C CG  . ASP A 1 150 ? 16.75079 -1.26040 -3.92815  1.000 43.11055  ? 150 ASP A CG  1 
ATOM   1169 O OD1 . ASP A 1 150 ? 16.34486 -1.83519 -4.96038  1.000 44.78594  ? 150 ASP A OD1 1 
ATOM   1170 O OD2 . ASP A 1 150 ? 17.19393 -1.87793 -2.93752  1.000 43.34098  ? 150 ASP A OD2 1 
ATOM   1171 N N   . GLY A 1 151 ? 16.79810 3.27586  -5.13367  1.000 41.45029  ? 151 GLY A N   1 
ATOM   1172 C CA  . GLY A 1 151 ? 16.38412 4.65743  -5.03099  1.000 40.75041  ? 151 GLY A CA  1 
ATOM   1173 C C   . GLY A 1 151 ? 17.55799 5.59455  -4.85231  1.000 38.46797  ? 151 GLY A C   1 
ATOM   1174 O O   . GLY A 1 151 ? 18.71669 5.23328  -5.06591  1.000 36.74044  ? 151 GLY A O   1 
ATOM   1175 N N   . LEU A 1 152 ? 17.22149 6.81835  -4.46689  1.000 38.80520  ? 152 LEU A N   1 
ATOM   1176 C CA  . LEU A 1 152 ? 18.21655 7.86242  -4.33182  1.000 38.79741  ? 152 LEU A CA  1 
ATOM   1177 C C   . LEU A 1 152 ? 17.91883 8.69287  -3.09961  1.000 39.17278  ? 152 LEU A C   1 
ATOM   1178 O O   . LEU A 1 152 ? 16.76429 8.87860  -2.70370  1.000 40.48524  ? 152 LEU A O   1 
ATOM   1179 C CB  . LEU A 1 152 ? 18.27242 8.76168  -5.56519  1.000 39.29939  ? 152 LEU A CB  1 
ATOM   1180 C CG  . LEU A 1 152 ? 18.96081 8.17120  -6.79045  1.000 39.71407  ? 152 LEU A CG  1 
ATOM   1181 C CD1 . LEU A 1 152 ? 18.55753 8.97532  -7.99881  1.000 40.42011  ? 152 LEU A CD1 1 
ATOM   1182 C CD2 . LEU A 1 152 ? 20.48159 8.15602  -6.64149  1.000 38.93575  ? 152 LEU A CD2 1 
ATOM   1183 N N   . CYS A 1 153 ? 18.99071 9.18989  -2.50344  1.000 38.85981  ? 153 CYS A N   1 
ATOM   1184 C CA  . CYS A 1 153 ? 18.92885 9.97864  -1.28735  1.000 38.71142  ? 153 CYS A CA  1 
ATOM   1185 C C   . CYS A 1 153 ? 19.68590 11.26305 -1.55584  1.000 39.00778  ? 153 CYS A C   1 
ATOM   1186 O O   . CYS A 1 153 ? 20.84213 11.22576 -1.98826  1.000 38.61916  ? 153 CYS A O   1 
ATOM   1187 C CB  . CYS A 1 153 ? 19.53481 9.21421  -0.10898  1.000 37.80685  ? 153 CYS A CB  1 
ATOM   1188 S SG  . CYS A 1 153 ? 19.68071 10.12575 1.43866   1.000 37.02497  ? 153 CYS A SG  1 
ATOM   1189 N N   . MET A 1 154 ? 19.02464 12.39025 -1.34667  1.000 40.33659  ? 154 MET A N   1 
ATOM   1190 C CA  . MET A 1 154 ? 19.67121 13.68906 -1.40730  1.000 41.73067  ? 154 MET A CA  1 
ATOM   1191 C C   . MET A 1 154 ? 19.71431 14.22218 0.01160   1.000 42.03784  ? 154 MET A C   1 
ATOM   1192 O O   . MET A 1 154 ? 18.66796 14.46201 0.61235   1.000 41.68467  ? 154 MET A O   1 
ATOM   1193 C CB  . MET A 1 154 ? 18.93105 14.64648 -2.33924  1.000 43.41180  ? 154 MET A CB  1 
ATOM   1194 C CG  . MET A 1 154 ? 19.74835 15.88379 -2.71769  1.000 44.92434  ? 154 MET A CG  1 
ATOM   1195 S SD  . MET A 1 154 ? 21.30332 15.55810 -3.57372  1.000 45.39395  ? 154 MET A SD  1 
ATOM   1196 C CE  . MET A 1 154 ? 20.88989 15.98482 -5.26629  1.000 46.18065  ? 154 MET A CE  1 
ATOM   1197 N N   . SER A 1 155 ? 20.92108 14.40385 0.53121   1.000 41.53130  ? 155 SER A N   1 
ATOM   1198 C CA  . SER A 1 155 ? 21.16461 14.70145 1.93213   1.000 40.76166  ? 155 SER A CA  1 
ATOM   1199 C C   . SER A 1 155 ? 21.69642 16.11956 2.08704   1.000 41.21201  ? 155 SER A C   1 
ATOM   1200 O O   . SER A 1 155 ? 22.45517 16.59919 1.23769   1.000 41.73201  ? 155 SER A O   1 
ATOM   1201 C CB  . SER A 1 155 ? 22.16362 13.69454 2.50568   1.000 40.11996  ? 155 SER A CB  1 
ATOM   1202 O OG  . SER A 1 155 ? 22.74320 14.13878 3.71783   1.000 40.51200  ? 155 SER A OG  1 
ATOM   1203 N N   . THR A 1 156 ? 21.27916 16.79367 3.16352   1.000 40.41631  ? 156 THR A N   1 
ATOM   1204 C CA  . THR A 1 156 ? 21.87664 18.06576 3.54855   1.000 41.19682  ? 156 THR A CA  1 
ATOM   1205 C C   . THR A 1 156 ? 23.23787 17.80261 4.19096   1.000 40.95018  ? 156 THR A C   1 
ATOM   1206 O O   . THR A 1 156 ? 23.57649 16.65627 4.49726   1.000 40.49361  ? 156 THR A O   1 
ATOM   1207 C CB  . THR A 1 156 ? 20.97557 18.82141 4.53033   1.000 42.71823  ? 156 THR A CB  1 
ATOM   1208 O OG1 . THR A 1 156 ? 20.99839 18.16200 5.80371   1.000 41.96822  ? 156 THR A OG1 1 
ATOM   1209 C CG2 . THR A 1 156 ? 19.54875 18.91608 4.01093   1.000 43.25584  ? 156 THR A CG2 1 
ATOM   1210 N N   . PRO A 1 157 ? 24.05140 18.86016 4.42693   1.000 41.85236  ? 157 PRO A N   1 
ATOM   1211 C CA  . PRO A 1 157 ? 25.28322 18.67461 5.20877   1.000 42.68408  ? 157 PRO A CA  1 
ATOM   1212 C C   . PRO A 1 157 ? 25.03077 17.99365 6.54507   1.000 41.93971  ? 157 PRO A C   1 
ATOM   1213 O O   . PRO A 1 157 ? 25.61241 16.94304 6.82973   1.000 41.14707  ? 157 PRO A O   1 
ATOM   1214 C CB  . PRO A 1 157 ? 25.79518 20.10565 5.41140   1.000 44.62244  ? 157 PRO A CB  1 
ATOM   1215 C CG  . PRO A 1 157 ? 25.21442 20.88404 4.30988   1.000 44.91277  ? 157 PRO A CG  1 
ATOM   1216 C CD  . PRO A 1 157 ? 23.91238 20.24842 3.94571   1.000 43.24249  ? 157 PRO A CD  1 
ATOM   1217 N N   . SER A 1 158 ? 24.16966 18.58010 7.37914   1.000 42.56554  ? 158 SER A N   1 
ATOM   1218 C CA  . SER A 1 158 ? 23.89295 17.96989 8.67469   1.000 42.29221  ? 158 SER A CA  1 
ATOM   1219 C C   . SER A 1 158 ? 23.15004 16.64835 8.53756   1.000 40.83031  ? 158 SER A C   1 
ATOM   1220 O O   . SER A 1 158 ? 23.14015 15.85461 9.48649   1.000 41.02826  ? 158 SER A O   1 
ATOM   1221 C CB  . SER A 1 158 ? 23.09967 18.93169 9.56026   1.000 43.37381  ? 158 SER A CB  1 
ATOM   1222 O OG  . SER A 1 158 ? 21.83703 19.21356 8.99119   1.000 43.29676  ? 158 SER A OG  1 
ATOM   1223 N N   . GLY A 1 159 ? 22.52940 16.39591 7.38525   1.000 40.26947  ? 159 GLY A N   1 
ATOM   1224 C CA  . GLY A 1 159 ? 21.93460 15.09858 7.15381   1.000 39.27579  ? 159 GLY A CA  1 
ATOM   1225 C C   . GLY A 1 159 ? 22.90788 14.01293 6.75521   1.000 38.55196  ? 159 GLY A C   1 
ATOM   1226 O O   . GLY A 1 159 ? 22.51494 12.84426 6.70382   1.000 38.46747  ? 159 GLY A O   1 
ATOM   1227 N N   . THR A 1 160 ? 24.16697 14.35795 6.46958   1.000 38.26505  ? 160 THR A N   1 
ATOM   1228 C CA  . THR A 1 160 ? 25.09771 13.33748 6.00514   1.000 39.38611  ? 160 THR A CA  1 
ATOM   1229 C C   . THR A 1 160 ? 25.48407 12.36934 7.10529   1.000 40.07332  ? 160 THR A C   1 
ATOM   1230 O O   . THR A 1 160 ? 25.95235 11.27006 6.80495   1.000 39.73963  ? 160 THR A O   1 
ATOM   1231 C CB  . THR A 1 160 ? 26.36340 13.96037 5.41577   1.000 40.27718  ? 160 THR A CB  1 
ATOM   1232 O OG1 . THR A 1 160 ? 26.98291 14.82571 6.37611   1.000 40.85558  ? 160 THR A OG1 1 
ATOM   1233 C CG2 . THR A 1 160 ? 26.03918 14.72326 4.15098   1.000 40.37164  ? 160 THR A CG2 1 
ATOM   1234 N N   . THR A 1 161 ? 25.31094 12.74789 8.36289   1.000 41.21237  ? 161 THR A N   1 
ATOM   1235 C CA  . THR A 1 161 ? 25.51913 11.80577 9.44702   1.000 41.14213  ? 161 THR A CA  1 
ATOM   1236 C C   . THR A 1 161 ? 24.31657 10.90241 9.65397   1.000 39.01125  ? 161 THR A C   1 
ATOM   1237 O O   . THR A 1 161 ? 24.36869 9.99474  10.48838  1.000 38.00513  ? 161 THR A O   1 
ATOM   1238 C CB  . THR A 1 161 ? 25.85678 12.56691 10.72923  1.000 43.13194  ? 161 THR A CB  1 
ATOM   1239 O OG1 . THR A 1 161 ? 24.92307 13.63944 10.91132  1.000 44.04941  ? 161 THR A OG1 1 
ATOM   1240 C CG2 . THR A 1 161 ? 27.24559 13.14399 10.62289  1.000 44.09406  ? 161 THR A CG2 1 
ATOM   1241 N N   . ALA A 1 162 ? 23.25649 11.10704 8.88582   1.000 38.73395  ? 162 ALA A N   1 
ATOM   1242 C CA  . ALA A 1 162 ? 22.00612 10.37934 9.05360   1.000 39.53240  ? 162 ALA A CA  1 
ATOM   1243 C C   . ALA A 1 162 ? 21.92339 9.30227  7.95979   1.000 39.50154  ? 162 ALA A C   1 
ATOM   1244 O O   . ALA A 1 162 ? 22.87908 8.54112  7.80973   1.000 38.44185  ? 162 ALA A O   1 
ATOM   1245 C CB  . ALA A 1 162 ? 20.85200 11.37440 9.05898   1.000 40.02720  ? 162 ALA A CB  1 
ATOM   1246 N N   . TYR A 1 163 ? 20.82179 9.21646  7.21999   1.000 40.03960  ? 163 TYR A N   1 
ATOM   1247 C CA  . TYR A 1 163 ? 20.63456 8.25221  6.15018   1.000 38.91215  ? 163 TYR A CA  1 
ATOM   1248 C C   . TYR A 1 163 ? 21.80994 8.21561  5.18921   1.000 37.38718  ? 163 TYR A C   1 
ATOM   1249 O O   . TYR A 1 163 ? 22.34494 7.14332  4.87276   1.000 36.09701  ? 163 TYR A O   1 
ATOM   1250 C CB  . TYR A 1 163 ? 19.37504 8.65435  5.40922   1.000 39.36781  ? 163 TYR A CB  1 
ATOM   1251 C CG  . TYR A 1 163 ? 18.72828 7.54388  4.70855   1.000 39.78507  ? 163 TYR A CG  1 
ATOM   1252 C CD1 . TYR A 1 163 ? 19.29329 6.28192  4.70878   1.000 39.58400  ? 163 TYR A CD1 1 
ATOM   1253 C CD2 . TYR A 1 163 ? 17.54441 7.74884  4.04074   1.000 40.69360  ? 163 TYR A CD2 1 
ATOM   1254 C CE1 . TYR A 1 163 ? 18.68984 5.25523  4.05838   1.000 40.66752  ? 163 TYR A CE1 1 
ATOM   1255 C CE2 . TYR A 1 163 ? 16.93365 6.73867  3.39120   1.000 41.40999  ? 163 TYR A CE2 1 
ATOM   1256 C CZ  . TYR A 1 163 ? 17.50654 5.49080  3.40060   1.000 41.31061  ? 163 TYR A CZ  1 
ATOM   1257 O OH  . TYR A 1 163 ? 16.87738 4.47198  2.73999   1.000 41.01237  ? 163 TYR A OH  1 
ATOM   1258 N N   . ASN A 1 164 ? 22.17173 9.38658  4.66473   1.000 37.67600  ? 164 ASN A N   1 
ATOM   1259 C CA  . ASN A 1 164 ? 23.31641 9.52494  3.77996   1.000 38.12739  ? 164 ASN A CA  1 
ATOM   1260 C C   . ASN A 1 164 ? 24.49241 8.66606  4.22712   1.000 38.58797  ? 164 ASN A C   1 
ATOM   1261 O O   . ASN A 1 164 ? 25.08240 7.92902  3.42920   1.000 38.29333  ? 164 ASN A O   1 
ATOM   1262 C CB  . ASN A 1 164 ? 23.72764 10.98832 3.73284   1.000 38.91617  ? 164 ASN A CB  1 
ATOM   1263 C CG  . ASN A 1 164 ? 25.02247 11.19133 3.01416   1.000 39.68995  ? 164 ASN A CG  1 
ATOM   1264 O OD1 . ASN A 1 164 ? 26.09208 11.15219 3.61527   1.000 40.42164  ? 164 ASN A OD1 1 
ATOM   1265 N ND2 . ASN A 1 164 ? 24.94101 11.40532 1.71076   1.000 39.43644  ? 164 ASN A ND2 1 
ATOM   1266 N N   . LYS A 1 165 ? 24.83160 8.74878  5.51933   1.000 39.23183  ? 165 LYS A N   1 
ATOM   1267 C CA  . LYS A 1 165 ? 25.97197 8.00073  6.04121   1.000 38.95764  ? 165 LYS A CA  1 
ATOM   1268 C C   . LYS A 1 165 ? 25.80021 6.50168  5.82380   1.000 38.75064  ? 165 LYS A C   1 
ATOM   1269 O O   . LYS A 1 165 ? 26.72812 5.82209  5.37003   1.000 39.25991  ? 165 LYS A O   1 
ATOM   1270 C CB  . LYS A 1 165 ? 26.17682 8.29699  7.52641   1.000 39.58030  ? 165 LYS A CB  1 
ATOM   1271 C CG  . LYS A 1 165 ? 27.36190 7.54086  8.09613   1.000 39.74301  ? 165 LYS A CG  1 
ATOM   1272 C CD  . LYS A 1 165 ? 27.53370 7.71650  9.59153   1.000 40.08887  ? 165 LYS A CD  1 
ATOM   1273 C CE  . LYS A 1 165 ? 28.89672 7.19737  10.03607  1.000 40.77999  ? 165 LYS A CE  1 
ATOM   1274 N NZ  . LYS A 1 165 ? 28.88976 5.77372  10.48519  1.000 40.83559  ? 165 LYS A NZ  1 
ATOM   1275 N N   . SER A 1 166 ? 24.61999 5.96400  6.15749   1.000 38.25632  ? 166 SER A N   1 
ATOM   1276 C CA  . SER A 1 166 ? 24.35671 4.54167  5.94989   1.000 39.23663  ? 166 SER A CA  1 
ATOM   1277 C C   . SER A 1 166 ? 24.41172 4.14446  4.49013   1.000 38.13523  ? 166 SER A C   1 
ATOM   1278 O O   . SER A 1 166 ? 24.59597 2.96275  4.19036   1.000 37.02144  ? 166 SER A O   1 
ATOM   1279 C CB  . SER A 1 166 ? 22.97922 4.14040  6.47010   1.000 41.16497  ? 166 SER A CB  1 
ATOM   1280 O OG  . SER A 1 166 ? 22.78870 4.51123  7.81624   1.000 43.14553  ? 166 SER A OG  1 
ATOM   1281 N N   . LEU A 1 167 ? 24.19564 5.07783  3.57466   1.000 38.83290  ? 167 LEU A N   1 
ATOM   1282 C CA  . LEU A 1 167 ? 24.30606 4.75735  2.16516   1.000 38.88471  ? 167 LEU A CA  1 
ATOM   1283 C C   . LEU A 1 167 ? 25.72859 4.91388  1.65928   1.000 38.92688  ? 167 LEU A C   1 
ATOM   1284 O O   . LEU A 1 167 ? 25.94809 4.95336  0.44405   1.000 39.30310  ? 167 LEU A O   1 
ATOM   1285 C CB  . LEU A 1 167 ? 23.33695 5.61700  1.35803   1.000 38.21490  ? 167 LEU A CB  1 
ATOM   1286 C CG  . LEU A 1 167 ? 21.88670 5.44447  1.81395   1.000 37.83899  ? 167 LEU A CG  1 
ATOM   1287 C CD1 . LEU A 1 167 ? 21.04340 6.58169  1.32173   1.000 37.13502  ? 167 LEU A CD1 1 
ATOM   1288 C CD2 . LEU A 1 167 ? 21.29626 4.11337  1.36013   1.000 37.85401  ? 167 LEU A CD2 1 
ATOM   1289 N N   . GLY A 1 168 ? 26.70200 4.97550  2.56199   1.000 40.94437  ? 168 GLY A N   1 
ATOM   1290 C CA  . GLY A 1 168 ? 28.06471 5.18955  2.13655   1.000 40.32472  ? 168 GLY A CA  1 
ATOM   1291 C C   . GLY A 1 168 ? 28.37459 6.61390  1.74063   1.000 39.65942  ? 168 GLY A C   1 
ATOM   1292 O O   . GLY A 1 168 ? 29.44921 6.86520  1.17523   1.000 39.59722  ? 168 GLY A O   1 
ATOM   1293 N N   . GLY A 1 169 ? 27.47238 7.55661  2.01549   1.000 39.64030  ? 169 GLY A N   1 
ATOM   1294 C CA  . GLY A 1 169 ? 27.77019 8.94860  1.75485   1.000 39.42225  ? 169 GLY A CA  1 
ATOM   1295 C C   . GLY A 1 169 ? 28.91926 9.45502  2.60411   1.000 39.97806  ? 169 GLY A C   1 
ATOM   1296 O O   . GLY A 1 169 ? 29.31433 8.86137  3.60870   1.000 39.77874  ? 169 GLY A O   1 
ATOM   1297 N N   . ALA A 1 170 ? 29.46871 10.58163 2.17442   1.000 39.87997  ? 170 ALA A N   1 
ATOM   1298 C CA  . ALA A 1 170 ? 30.51278 11.25485 2.92364   1.000 39.86591  ? 170 ALA A CA  1 
ATOM   1299 C C   . ALA A 1 170 ? 29.88541 12.10036 4.02384   1.000 40.31008  ? 170 ALA A C   1 
ATOM   1300 O O   . ALA A 1 170 ? 28.75923 12.58934 3.89496   1.000 40.90224  ? 170 ALA A O   1 
ATOM   1301 C CB  . ALA A 1 170 ? 31.35690 12.13474 1.99958   1.000 40.04791  ? 170 ALA A CB  1 
ATOM   1302 N N   . LEU A 1 171 ? 30.61730 12.26608 5.12080   1.000 40.03253  ? 171 LEU A N   1 
ATOM   1303 C CA  . LEU A 1 171 ? 30.18768 13.17256 6.17812   1.000 40.67932  ? 171 LEU A CA  1 
ATOM   1304 C C   . LEU A 1 171 ? 30.72349 14.56602 5.89382   1.000 41.70878  ? 171 LEU A C   1 
ATOM   1305 O O   . LEU A 1 171 ? 31.92111 14.73667 5.63042   1.000 41.93829  ? 171 LEU A O   1 
ATOM   1306 C CB  . LEU A 1 171 ? 30.66181 12.71525 7.55268   1.000 40.83282  ? 171 LEU A CB  1 
ATOM   1307 C CG  . LEU A 1 171 ? 30.47468 11.24478 7.88954   1.000 40.07283  ? 171 LEU A CG  1 
ATOM   1308 C CD1 . LEU A 1 171 ? 30.75392 11.05479 9.36164   1.000 40.20460  ? 171 LEU A CD1 1 
ATOM   1309 C CD2 . LEU A 1 171 ? 29.08246 10.77017 7.51566   1.000 38.52456  ? 171 LEU A CD2 1 
ATOM   1310 N N   . MET A 1 172 ? 29.83750 15.55656 5.98944   1.000 43.59170  ? 172 MET A N   1 
ATOM   1311 C CA  . MET A 1 172 ? 30.09626 16.91057 5.52818   1.000 44.92451  ? 172 MET A CA  1 
ATOM   1312 C C   . MET A 1 172 ? 29.89159 17.89202 6.67115   1.000 46.07904  ? 172 MET A C   1 
ATOM   1313 O O   . MET A 1 172 ? 28.88083 17.82517 7.37040   1.000 46.34526  ? 172 MET A O   1 
ATOM   1314 C CB  . MET A 1 172 ? 29.15914 17.24938 4.39041   1.000 44.74850  ? 172 MET A CB  1 
ATOM   1315 C CG  . MET A 1 172 ? 29.80517 17.92295 3.22979   0.850 44.98475  ? 172 MET A CG  1 
ATOM   1316 S SD  . MET A 1 172 ? 28.55765 18.05304 1.96508   0.780 45.09235  ? 172 MET A SD  1 
ATOM   1317 C CE  . MET A 1 172 ? 28.37746 16.32875 1.60445   0.750 43.12003  ? 172 MET A CE  1 
ATOM   1318 N N   . HIS A 1 173 ? 30.81122 18.83625 6.82107   1.000 47.22630  ? 173 HIS A N   1 
ATOM   1319 C CA  . HIS A 1 173 ? 30.66837 19.82608 7.88000   1.000 49.76504  ? 173 HIS A CA  1 
ATOM   1320 C C   . HIS A 1 173 ? 29.60017 20.85579 7.50493   1.000 51.56348  ? 173 HIS A C   1 
ATOM   1321 O O   . HIS A 1 173 ? 29.58966 21.35614 6.37490   1.000 52.36551  ? 173 HIS A O   1 
ATOM   1322 C CB  . HIS A 1 173 ? 31.99378 20.52782 8.15614   1.000 51.00670  ? 173 HIS A CB  1 
ATOM   1323 C CG  . HIS A 1 173 ? 31.90013 21.54439 9.24514   1.000 53.24877  ? 173 HIS A CG  1 
ATOM   1324 N ND1 . HIS A 1 173 ? 31.46546 22.83254 9.02129   1.000 54.90776  ? 173 HIS A ND1 1 
ATOM   1325 C CD2 . HIS A 1 173 ? 32.12758 21.44832 10.57597  1.000 54.18522  ? 173 HIS A CD2 1 
ATOM   1326 C CE1 . HIS A 1 173 ? 31.45548 23.49492 10.16366  1.000 56.83788  ? 173 HIS A CE1 1 
ATOM   1327 N NE2 . HIS A 1 173 ? 31.85284 22.67767 11.12243  1.000 56.44428  ? 173 HIS A NE2 1 
ATOM   1328 N N   . PRO A 1 174 ? 28.71778 21.22480 8.44269   1.000 52.21074  ? 174 PRO A N   1 
ATOM   1329 C CA  . PRO A 1 174 ? 27.47452 21.92216 8.05481   1.000 52.41057  ? 174 PRO A CA  1 
ATOM   1330 C C   . PRO A 1 174 ? 27.64831 23.33314 7.48808   1.000 54.13681  ? 174 PRO A C   1 
ATOM   1331 O O   . PRO A 1 174 ? 26.70042 23.83860 6.87793   1.000 55.15632  ? 174 PRO A O   1 
ATOM   1332 C CB  . PRO A 1 174 ? 26.66822 21.96134 9.35993   1.000 53.56044  ? 174 PRO A CB  1 
ATOM   1333 C CG  . PRO A 1 174 ? 27.29208 20.96233 10.26481  1.000 52.67504  ? 174 PRO A CG  1 
ATOM   1334 C CD  . PRO A 1 174 ? 28.73666 20.88830 9.87886   1.000 52.57602  ? 174 PRO A CD  1 
ATOM   1335 N N   . SER A 1 175 ? 28.79509 23.99306 7.67414   1.000 55.19750  ? 175 SER A N   1 
ATOM   1336 C CA  . SER A 1 175 ? 29.00278 25.34256 7.14472   1.000 58.73810  ? 175 SER A CA  1 
ATOM   1337 C C   . SER A 1 175 ? 29.11694 25.37331 5.62754   1.000 58.72057  ? 175 SER A C   1 
ATOM   1338 O O   . SER A 1 175 ? 29.07880 26.45915 5.03329   1.000 60.51522  ? 175 SER A O   1 
ATOM   1339 C CB  . SER A 1 175 ? 30.27301 25.93310 7.73797   1.000 61.33266  ? 175 SER A CB  1 
ATOM   1340 O OG  . SER A 1 175 ? 31.38775 25.18856 7.27983   1.000 60.88414  ? 175 SER A OG  1 
ATOM   1341 N N   . ILE A 1 176 ? 29.29610 24.20856 5.01471   1.000 56.81029  ? 176 ILE A N   1 
ATOM   1342 C CA  . ILE A 1 176 ? 29.45101 24.04908 3.57448   1.000 55.43477  ? 176 ILE A CA  1 
ATOM   1343 C C   . ILE A 1 176 ? 28.07076 24.06850 2.93378   1.000 54.26260  ? 176 ILE A C   1 
ATOM   1344 O O   . ILE A 1 176 ? 27.23322 23.21124 3.22873   1.000 52.86111  ? 176 ILE A O   1 
ATOM   1345 C CB  . ILE A 1 176 ? 30.16151 22.72608 3.25705   1.000 52.66321  ? 176 ILE A CB  1 
ATOM   1346 C CG1 . ILE A 1 176 ? 31.60055 22.70281 3.77100   1.000 52.99733  ? 176 ILE A CG1 1 
ATOM   1347 C CG2 . ILE A 1 176 ? 30.07945 22.41356 1.77950   1.000 50.37625  ? 176 ILE A CG2 1 
ATOM   1348 C CD1 . ILE A 1 176 ? 32.24058 21.33602 3.60986   1.000 50.95912  ? 176 ILE A CD1 1 
ATOM   1349 N N   . GLU A 1 177 ? 27.83918 25.00852 2.02639   1.000 54.79243  ? 177 GLU A N   1 
ATOM   1350 C CA  . GLU A 1 177 ? 26.52616 25.11347 1.39143   1.000 54.64434  ? 177 GLU A CA  1 
ATOM   1351 C C   . GLU A 1 177 ? 26.46778 24.15464 0.20031   1.000 52.18747  ? 177 GLU A C   1 
ATOM   1352 O O   . GLU A 1 177 ? 26.94515 24.47500 -0.89365  1.000 52.69507  ? 177 GLU A O   1 
ATOM   1353 C CB  . GLU A 1 177 ? 26.24868 26.56083 1.00049   1.000 58.01839  ? 177 GLU A CB  1 
ATOM   1354 C CG  . GLU A 1 177 ? 26.20079 27.47478 2.23041   1.000 60.97184  ? 177 GLU A CG  1 
ATOM   1355 C CD  . GLU A 1 177 ? 25.78582 28.89454 1.92230   1.000 64.52566  ? 177 GLU A CD  1 
ATOM   1356 O OE1 . GLU A 1 177 ? 25.56153 29.20008 0.74310   0.710 65.03908  ? 177 GLU A OE1 1 
ATOM   1357 O OE2 . GLU A 1 177 ? 25.68847 29.71127 2.86136   0.790 66.90261  ? 177 GLU A OE2 1 
ATOM   1358 N N   . ALA A 1 178 ? 25.87943 22.96879 0.41265   1.000 49.77547  ? 178 ALA A N   1 
ATOM   1359 C CA  . ALA A 1 178 ? 25.85315 21.92397 -0.61119  1.000 47.58513  ? 178 ALA A CA  1 
ATOM   1360 C C   . ALA A 1 178 ? 24.77606 20.88285 -0.29652  1.000 45.96855  ? 178 ALA A C   1 
ATOM   1361 O O   . ALA A 1 178 ? 24.06470 20.97299 0.70858   1.000 46.36512  ? 178 ALA A O   1 
ATOM   1362 C CB  . ALA A 1 178 ? 27.22801 21.26282 -0.74260  1.000 46.45837  ? 178 ALA A CB  1 
ATOM   1363 N N   . MET A 1 179 ? 24.67664 19.88401 -1.18625  1.000 43.88326  ? 179 MET A N   1 
ATOM   1364 C CA  . MET A 1 179 ? 23.75938 18.74904 -1.11366  1.000 42.65217  ? 179 MET A CA  1 
ATOM   1365 C C   . MET A 1 179 ? 24.45980 17.51446 -1.67502  1.000 40.96732  ? 179 MET A C   1 
ATOM   1366 O O   . MET A 1 179 ? 25.25697 17.61644 -2.61181  1.000 41.14796  ? 179 MET A O   1 
ATOM   1367 C CB  . MET A 1 179 ? 22.46049 18.99910 -1.90317  1.000 43.44490  ? 179 MET A CB  1 
ATOM   1368 C CG  . MET A 1 179 ? 22.63149 19.18267 -3.41450  1.000 42.62070  ? 179 MET A CG  1 
ATOM   1369 S SD  . MET A 1 179 ? 21.06145 19.57939 -4.21339  1.000 44.07915  ? 179 MET A SD  1 
ATOM   1370 C CE  . MET A 1 179 ? 21.58941 20.03321 -5.84932  1.000 43.50701  ? 179 MET A CE  1 
ATOM   1371 N N   . GLN A 1 180 ? 24.16800 16.34210 -1.10966  1.000 39.89775  ? 180 GLN A N   1 
ATOM   1372 C CA  . GLN A 1 180 ? 24.88595 15.11951 -1.46590  1.000 39.76671  ? 180 GLN A CA  1 
ATOM   1373 C C   . GLN A 1 180 ? 23.92601 14.03764 -1.93952  1.000 39.59974  ? 180 GLN A C   1 
ATOM   1374 O O   . GLN A 1 180 ? 22.94905 13.72007 -1.25255  1.000 40.32863  ? 180 GLN A O   1 
ATOM   1375 C CB  . GLN A 1 180 ? 25.71444 14.59032 -0.29232  1.000 39.48986  ? 180 GLN A CB  1 
ATOM   1376 C CG  . GLN A 1 180 ? 26.52666 13.35371 -0.64790  1.000 38.90597  ? 180 GLN A CG  1 
ATOM   1377 C CD  . GLN A 1 180 ? 27.54212 12.96511 0.40902   1.000 39.53639  ? 180 GLN A CD  1 
ATOM   1378 O OE1 . GLN A 1 180 ? 28.40020 12.11580 0.17868   1.000 39.39652  ? 180 GLN A OE1 1 
ATOM   1379 N NE2 . GLN A 1 180 ? 27.44183 13.56833 1.57163   1.000 40.54295  ? 180 GLN A NE2 1 
ATOM   1380 N N   . LEU A 1 181 ? 24.21296 13.46794 -3.10648  1.000 39.35670  ? 181 LEU A N   1 
ATOM   1381 C CA  . LEU A 1 181 ? 23.38154 12.42502 -3.69108  1.000 38.92293  ? 181 LEU A CA  1 
ATOM   1382 C C   . LEU A 1 181 ? 24.06002 11.07781 -3.49719  1.000 37.94364  ? 181 LEU A C   1 
ATOM   1383 O O   . LEU A 1 181 ? 25.19552 10.87558 -3.94013  1.000 37.56597  ? 181 LEU A O   1 
ATOM   1384 C CB  . LEU A 1 181 ? 23.12532 12.67787 -5.17529  1.000 38.86202  ? 181 LEU A CB  1 
ATOM   1385 C CG  . LEU A 1 181 ? 22.14698 11.69309 -5.81936  1.000 37.99649  ? 181 LEU A CG  1 
ATOM   1386 C CD1 . LEU A 1 181 ? 20.71894 11.95475 -5.34853  1.000 38.44059  ? 181 LEU A CD1 1 
ATOM   1387 C CD2 . LEU A 1 181 ? 22.23934 11.73451 -7.33741  1.000 37.69358  ? 181 LEU A CD2 1 
ATOM   1388 N N   . THR A 1 182 ? 23.36653 10.16891 -2.83009  1.000 37.41193  ? 182 THR A N   1 
ATOM   1389 C CA  . THR A 1 182 ? 23.83416 8.81039  -2.63096  1.000 38.16675  ? 182 THR A CA  1 
ATOM   1390 C C   . THR A 1 182 ? 22.92853 7.85862  -3.39295  1.000 39.27880  ? 182 THR A C   1 
ATOM   1391 O O   . THR A 1 182 ? 21.70849 8.04588  -3.43279  1.000 40.28567  ? 182 THR A O   1 
ATOM   1392 C CB  . THR A 1 182 ? 23.84622 8.45091  -1.14717  1.000 38.97663  ? 182 THR A CB  1 
ATOM   1393 O OG1 . THR A 1 182 ? 22.67132 8.98181  -0.52216  1.000 39.94562  ? 182 THR A OG1 1 
ATOM   1394 C CG2 . THR A 1 182 ? 25.06930 9.03247  -0.48779  1.000 38.61546  ? 182 THR A CG2 1 
ATOM   1395 N N   . GLU A 1 183 ? 23.52829 6.85126  -4.01357  1.000 39.44361  ? 183 GLU A N   1 
ATOM   1396 C CA  . GLU A 1 183 ? 22.73103 5.82277  -4.65335  1.000 39.65557  ? 183 GLU A CA  1 
ATOM   1397 C C   . GLU A 1 183 ? 22.18122 4.85627  -3.61003  1.000 39.56745  ? 183 GLU A C   1 
ATOM   1398 O O   . GLU A 1 183 ? 22.72023 4.71618  -2.50718  1.000 38.25090  ? 183 GLU A O   1 
ATOM   1399 C CB  . GLU A 1 183 ? 23.55689 5.04278  -5.67361  1.000 39.93855  ? 183 GLU A CB  1 
ATOM   1400 C CG  . GLU A 1 183 ? 24.18860 5.87556  -6.75276  1.000 39.82347  ? 183 GLU A CG  1 
ATOM   1401 C CD  . GLU A 1 183 ? 24.89027 5.02162  -7.78533  1.000 40.19816  ? 183 GLU A CD  1 
ATOM   1402 O OE1 . GLU A 1 183 ? 24.93344 3.79081  -7.58877  1.000 40.52442  ? 183 GLU A OE1 1 
ATOM   1403 O OE2 . GLU A 1 183 ? 25.39375 5.57501  -8.78374  1.000 40.35316  ? 183 GLU A OE2 1 
ATOM   1404 N N   . MET A 1 184 ? 21.08755 4.18733  -3.97647  1.000 41.08094  ? 184 MET A N   1 
ATOM   1405 C CA  . MET A 1 184 ? 20.56739 3.02532  -3.25469  1.000 41.47962  ? 184 MET A CA  1 
ATOM   1406 C C   . MET A 1 184 ? 20.55426 1.84609  -4.22331  1.000 42.09753  ? 184 MET A C   1 
ATOM   1407 O O   . MET A 1 184 ? 19.63190 1.72713  -5.03587  1.000 43.85781  ? 184 MET A O   1 
ATOM   1408 C CB  . MET A 1 184 ? 19.15699 3.25673  -2.71935  1.000 42.68562  ? 184 MET A CB  1 
ATOM   1409 C CG  . MET A 1 184 ? 18.99855 4.07528  -1.45333  1.000 42.42572  ? 184 MET A CG  1 
ATOM   1410 S SD  . MET A 1 184 ? 17.24030 4.17517  -1.07091  1.000 44.78095  ? 184 MET A SD  1 
ATOM   1411 C CE  . MET A 1 184 ? 17.19059 5.70094  -0.13065  1.000 44.29297  ? 184 MET A CE  1 
ATOM   1412 N N   . ALA A 1 185 ? 21.57377 0.99164  -4.14780  1.000 41.28557  ? 185 ALA A N   1 
ATOM   1413 C CA  . ALA A 1 185 ? 21.58580 -0.32567 -4.79455  1.000 42.38812  ? 185 ALA A CA  1 
ATOM   1414 C C   . ALA A 1 185 ? 21.32655 -0.25068 -6.30131  1.000 42.96496  ? 185 ALA A C   1 
ATOM   1415 O O   . ALA A 1 185 ? 20.36995 -0.82526 -6.82370  1.000 45.21438  ? 185 ALA A O   1 
ATOM   1416 C CB  . ALA A 1 185 ? 20.57721 -1.26475 -4.12801  1.000 43.21618  ? 185 ALA A CB  1 
ATOM   1417 N N   . SER A 1 186 ? 22.21740 0.43630  -7.00643  1.000 41.49167  ? 186 SER A N   1 
ATOM   1418 C CA  A SER A 1 186 ? 22.12757 0.48937  -8.45829  0.710 42.11683  ? 186 SER A CA  1 
ATOM   1419 C CA  B SER A 1 186 ? 22.11735 0.48909  -8.45618  0.290 42.13904  ? 186 SER A CA  1 
ATOM   1420 C C   . SER A 1 186 ? 22.55569 -0.83896 -9.05860  1.000 43.83278  ? 186 SER A C   1 
ATOM   1421 O O   . SER A 1 186 ? 23.45730 -1.50746 -8.54607  1.000 44.10638  ? 186 SER A O   1 
ATOM   1422 C CB  A SER A 1 186 ? 23.00542 1.60823  -9.01065  0.710 41.40031  ? 186 SER A CB  1 
ATOM   1423 C CB  B SER A 1 186 ? 22.96683 1.63631  -9.00484  0.290 41.37788  ? 186 SER A CB  1 
ATOM   1424 O OG  A SER A 1 186 ? 24.34236 1.45543  -8.56749  0.710 40.62496  ? 186 SER A OG  1 
ATOM   1425 O OG  B SER A 1 186 ? 23.16233 1.52704  -10.40370 0.290 42.02477  ? 186 SER A OG  1 
ATOM   1426 N N   . ILE A 1 187 ? 21.89574 -1.23042 -10.13034 1.000 45.37103  ? 187 ILE A N   1 
ATOM   1427 C CA  . ILE A 1 187 ? 22.36756 -2.36615 -10.89774 1.000 48.03094  ? 187 ILE A CA  1 
ATOM   1428 C C   . ILE A 1 187 ? 23.44285 -1.83236 -11.83158 1.000 50.45208  ? 187 ILE A C   1 
ATOM   1429 O O   . ILE A 1 187 ? 23.32198 -0.71410 -12.34551 1.000 49.56743  ? 187 ILE A O   1 
ATOM   1430 C CB  . ILE A 1 187 ? 21.18867 -3.01333 -11.64322 1.000 48.24437  ? 187 ILE A CB  1 
ATOM   1431 C CG1 . ILE A 1 187 ? 21.54281 -4.39891 -12.17472 1.000 48.53182  ? 187 ILE A CG1 1 
ATOM   1432 C CG2 . ILE A 1 187 ? 20.70286 -2.12506 -12.78330 1.000 49.26733  ? 187 ILE A CG2 1 
ATOM   1433 C CD1 . ILE A 1 187 ? 20.45201 -4.97728 -13.05296 0.750 50.55264  ? 187 ILE A CD1 1 
ATOM   1434 N N   . ASN A 1 188 ? 24.53721 -2.56236 -12.01047 1.000 55.08700  ? 188 ASN A N   1 
ATOM   1435 C CA  . ASN A 1 188 ? 25.56575 -2.06618 -12.91714 1.000 59.29131  ? 188 ASN A CA  1 
ATOM   1436 C C   . ASN A 1 188 ? 26.06189 -3.16816 -13.83396 1.000 65.46367  ? 188 ASN A C   1 
ATOM   1437 O O   . ASN A 1 188 ? 26.58751 -4.18756 -13.37374 1.000 65.55497  ? 188 ASN A O   1 
ATOM   1438 C CB  . ASN A 1 188 ? 26.72249 -1.40821 -12.16481 1.000 57.45462  ? 188 ASN A CB  1 
ATOM   1439 C CG  . ASN A 1 188 ? 26.48348 0.06768  -11.94776 1.000 55.18899  ? 188 ASN A CG  1 
ATOM   1440 O OD1 . ASN A 1 188 ? 27.00368 0.91462  -12.67800 1.000 54.50241  ? 188 ASN A OD1 1 
ATOM   1441 N ND2 . ASN A 1 188 ? 25.65045 0.38376  -10.96560 1.000 54.40709  ? 188 ASN A ND2 1 
ATOM   1442 N N   . ASN A 1 189 ? 25.90639 -2.93246 -15.13173 1.000 71.01230  ? 189 ASN A N   1 
ATOM   1443 C CA  . ASN A 1 189 ? 26.34059 -3.83049 -16.18565 1.000 79.51644  ? 189 ASN A CA  1 
ATOM   1444 C C   . ASN A 1 189 ? 26.60357 -2.98629 -17.42755 0.250 86.48338  ? 189 ASN A C   1 
ATOM   1445 O O   . ASN A 1 189 ? 26.33952 -1.78520 -17.44585 0.570 84.65827  ? 189 ASN A O   1 
ATOM   1446 C CB  . ASN A 1 189 ? 25.29035 -4.91646 -16.43785 1.000 81.08001  ? 189 ASN A CB  1 
ATOM   1447 C CG  . ASN A 1 189 ? 23.86907 -4.40442 -16.26320 1.000 81.39991  ? 189 ASN A CG  1 
ATOM   1448 O OD1 . ASN A 1 189 ? 23.58827 -3.23070 -16.49636 1.000 80.30480  ? 189 ASN A OD1 1 
ATOM   1449 N ND2 . ASN A 1 189 ? 22.96817 -5.28539 -15.84226 1.000 82.60624  ? 189 ASN A ND2 1 
ATOM   1450 N N   . ARG A 1 190 ? 27.13168 -3.61850 -18.47677 1.000 95.12253  ? 190 ARG A N   1 
ATOM   1451 C CA  . ARG A 1 190 ? 27.36099 -2.89663 -19.72802 1.000 97.25045  ? 190 ARG A CA  1 
ATOM   1452 C C   . ARG A 1 190 ? 26.12554 -2.10422 -20.15737 1.000 96.26885  ? 190 ARG A C   1 
ATOM   1453 O O   . ARG A 1 190 ? 26.24404 -1.04584 -20.77991 1.000 96.15709  ? 190 ARG A O   1 
ATOM   1454 C CB  . ARG A 1 190 ? 27.75132 -3.88547 -20.82424 1.000 101.50330 ? 190 ARG A CB  1 
ATOM   1455 C CG  . ARG A 1 190 ? 28.37627 -5.17111 -20.30083 0.900 103.85150 ? 190 ARG A CG  1 
ATOM   1456 C CD  . ARG A 1 190 ? 28.36770 -6.27371 -21.35596 0.800 107.72373 ? 190 ARG A CD  1 
ATOM   1457 N NE  . ARG A 1 190 ? 27.08398 -6.96129 -21.44349 0.700 109.88556 ? 190 ARG A NE  1 
ATOM   1458 C CZ  . ARG A 1 190 ? 26.87899 -8.08094 -22.12518 0.600 114.48573 ? 190 ARG A CZ  1 
ATOM   1459 N NH1 . ARG A 1 190 ? 27.85674 -8.67342 -22.79140 0.600 116.91912 ? 190 ARG A NH1 1 
ATOM   1460 N NH2 . ARG A 1 190 ? 25.66563 -8.62292 -22.13525 0.600 116.81961 ? 190 ARG A NH2 1 
ATOM   1461 N N   . VAL A 1 191 ? 24.94047 -2.60522 -19.80182 1.000 88.82954  ? 191 VAL A N   1 
ATOM   1462 C CA  . VAL A 1 191 ? 23.65479 -1.99445 -20.15476 1.000 85.73060  ? 191 VAL A CA  1 
ATOM   1463 C C   . VAL A 1 191 ? 23.37711 -0.77710 -19.30473 1.000 81.72415  ? 191 VAL A C   1 
ATOM   1464 O O   . VAL A 1 191 ? 22.98935 0.29101  -19.79259 1.000 84.80627  ? 191 VAL A O   1 
ATOM   1465 C CB  . VAL A 1 191 ? 22.52328 -2.99448 -19.89739 1.000 88.60241  ? 191 VAL A CB  1 
ATOM   1466 C CG1 . VAL A 1 191 ? 21.15728 -2.33164 -20.11439 1.000 91.27465  ? 191 VAL A CG1 1 
ATOM   1467 C CG2 . VAL A 1 191 ? 22.70019 -4.25445 -20.71449 1.000 93.53147  ? 191 VAL A CG2 1 
ATOM   1468 N N   . TYR A 1 192 ? 23.42735 -0.98565 -18.00444 1.000 73.28219  ? 192 TYR A N   1 
ATOM   1469 C CA  . TYR A 1 192 ? 23.06923 0.00472  -17.01643 1.000 67.52832  ? 192 TYR A CA  1 
ATOM   1470 C C   . TYR A 1 192 ? 24.34745 0.36079  -16.29688 1.000 61.72526  ? 192 TYR A C   1 
ATOM   1471 O O   . TYR A 1 192 ? 25.05597 -0.51659 -15.80668 1.000 60.92184  ? 192 TYR A O   1 
ATOM   1472 C CB  . TYR A 1 192 ? 22.02535 -0.53180 -16.03851 1.000 65.96582  ? 192 TYR A CB  1 
ATOM   1473 C CG  . TYR A 1 192 ? 20.60700 -0.55129 -16.55619 1.000 66.58370  ? 192 TYR A CG  1 
ATOM   1474 C CD1 . TYR A 1 192 ? 19.86650 0.62014  -16.65310 1.000 66.37004  ? 192 TYR A CD1 1 
ATOM   1475 C CD2 . TYR A 1 192 ? 19.99105 -1.74617 -16.89783 1.000 68.42015  ? 192 TYR A CD2 1 
ATOM   1476 C CE1 . TYR A 1 192 ? 18.55632 0.60150  -17.09925 1.000 67.85809  ? 192 TYR A CE1 1 
ATOM   1477 C CE2 . TYR A 1 192 ? 18.68926 -1.77555 -17.34672 1.000 70.25097  ? 192 TYR A CE2 1 
ATOM   1478 C CZ  . TYR A 1 192 ? 17.97505 -0.60283 -17.44858 1.000 70.04741  ? 192 TYR A CZ  1 
ATOM   1479 O OH  . TYR A 1 192 ? 16.67266 -0.65240 -17.88921 1.000 72.38473  ? 192 TYR A OH  1 
ATOM   1480 N N   . ARG A 1 193 ? 24.65363 1.63810  -16.26289 1.000 58.00868  ? 193 ARG A N   1 
ATOM   1481 C CA  . ARG A 1 193 ? 25.93359 2.08271  -15.76011 1.000 55.10663  ? 193 ARG A CA  1 
ATOM   1482 C C   . ARG A 1 193 ? 25.66201 3.36243  -15.00178 1.000 51.02243  ? 193 ARG A C   1 
ATOM   1483 O O   . ARG A 1 193 ? 25.13510 4.31985  -15.57235 1.000 51.60488  ? 193 ARG A O   1 
ATOM   1484 C CB  . ARG A 1 193 ? 26.91555 2.29807  -16.91211 1.000 57.05738  ? 193 ARG A CB  1 
ATOM   1485 C CG  . ARG A 1 193 ? 28.18072 3.02293  -16.52822 0.660 56.77696  ? 193 ARG A CG  1 
ATOM   1486 C CD  . ARG A 1 193 ? 29.11062 2.15083  -15.69743 0.670 57.17735  ? 193 ARG A CD  1 
ATOM   1487 N NE  . ARG A 1 193 ? 29.70541 1.07297  -16.47685 0.380 59.28462  ? 193 ARG A NE  1 
ATOM   1488 C CZ  . ARG A 1 193 ? 29.37586 -0.20640 -16.36289 0.560 60.90603  ? 193 ARG A CZ  1 
ATOM   1489 N NH1 . ARG A 1 193 ? 28.47277 -0.61347 -15.48527 0.860 60.68868  ? 193 ARG A NH1 1 
ATOM   1490 N NH2 . ARG A 1 193 ? 29.97069 -1.10036 -17.14374 0.640 62.76637  ? 193 ARG A NH2 1 
ATOM   1491 N N   . THR A 1 194 ? 25.94675 3.35626  -13.71151 1.000 46.63017  ? 194 THR A N   1 
ATOM   1492 C CA  . THR A 1 194 ? 25.83496 4.56348  -12.91556 1.000 43.90767  ? 194 THR A CA  1 
ATOM   1493 C C   . THR A 1 194 ? 27.19348 4.88941  -12.31472 1.000 42.53763  ? 194 THR A C   1 
ATOM   1494 O O   . THR A 1 194 ? 28.13570 4.09450  -12.37244 1.000 41.88544  ? 194 THR A O   1 
ATOM   1495 C CB  . THR A 1 194 ? 24.77760 4.42721  -11.81238 1.000 42.65990  ? 194 THR A CB  1 
ATOM   1496 O OG1 . THR A 1 194 ? 25.23492 3.50453  -10.81640 1.000 42.13697  ? 194 THR A OG1 1 
ATOM   1497 C CG2 . THR A 1 194 ? 23.45753 3.94506  -12.39247 1.000 44.24537  ? 194 THR A CG2 1 
ATOM   1498 N N   . ILE A 1 195 ? 27.28042 6.08192  -11.72583 1.000 42.04683  ? 195 ILE A N   1 
ATOM   1499 C CA  . ILE A 1 195 ? 28.57496 6.58851  -11.29006 1.000 41.31592  ? 195 ILE A CA  1 
ATOM   1500 C C   . ILE A 1 195 ? 29.07336 5.85308  -10.05211 1.000 40.93352  ? 195 ILE A C   1 
ATOM   1501 O O   . ILE A 1 195 ? 30.28476 5.67312  -9.88088  1.000 40.85987  ? 195 ILE A O   1 
ATOM   1502 C CB  . ILE A 1 195 ? 28.49588 8.10848  -11.05966 1.000 40.10961  ? 195 ILE A CB  1 
ATOM   1503 C CG1 . ILE A 1 195 ? 29.88614 8.66656  -10.76307 1.000 39.57043  ? 195 ILE A CG1 1 
ATOM   1504 C CG2 . ILE A 1 195 ? 27.55735 8.43538  -9.91131  1.000 38.52100  ? 195 ILE A CG2 1 
ATOM   1505 C CD1 . ILE A 1 195 ? 30.92465 8.29360  -11.79152 1.000 39.54943  ? 195 ILE A CD1 1 
ATOM   1506 N N   . GLY A 1 196 ? 28.16785 5.41934  -9.17823  1.000 40.37623  ? 196 GLY A N   1 
ATOM   1507 C CA  . GLY A 1 196 ? 28.53794 4.74137  -7.94995  1.000 39.95962  ? 196 GLY A CA  1 
ATOM   1508 C C   . GLY A 1 196 ? 28.79506 5.67680  -6.78495  1.000 39.61922  ? 196 GLY A C   1 
ATOM   1509 O O   . GLY A 1 196 ? 28.12729 5.59994  -5.74710  1.000 40.50637  ? 196 GLY A O   1 
ATOM   1510 N N   . SER A 1 197 ? 29.76099 6.57340  -6.95804  1.000 39.39895  ? 197 SER A N   1 
ATOM   1511 C CA  . SER A 1 197 ? 30.21226 7.41452  -5.86589  1.000 39.34421  ? 197 SER A CA  1 
ATOM   1512 C C   . SER A 1 197 ? 29.09317 8.33815  -5.39799  1.000 38.74019  ? 197 SER A C   1 
ATOM   1513 O O   . SER A 1 197 ? 28.21564 8.71404  -6.18022  1.000 38.39941  ? 197 SER A O   1 
ATOM   1514 C CB  . SER A 1 197 ? 31.40175 8.25970  -6.30285  1.000 39.48007  ? 197 SER A CB  1 
ATOM   1515 O OG  . SER A 1 197 ? 32.34306 7.46775  -7.00250  1.000 40.44242  ? 197 SER A OG  1 
ATOM   1516 N N   . PRO A 1 198 ? 29.10203 8.72340  -4.12687  1.000 37.96130  ? 198 PRO A N   1 
ATOM   1517 C CA  . PRO A 1 198 ? 28.30191 9.87518  -3.73281  1.000 38.28037  ? 198 PRO A CA  1 
ATOM   1518 C C   . PRO A 1 198 ? 28.75432 11.06997 -4.54511  1.000 38.85130  ? 198 PRO A C   1 
ATOM   1519 O O   . PRO A 1 198 ? 29.94777 11.21413 -4.85226  1.000 38.95940  ? 198 PRO A O   1 
ATOM   1520 C CB  . PRO A 1 198 ? 28.60905 10.03387 -2.23951  1.000 38.06332  ? 198 PRO A CB  1 
ATOM   1521 C CG  . PRO A 1 198 ? 29.16382 8.69898  -1.81600  1.000 37.50598  ? 198 PRO A CG  1 
ATOM   1522 C CD  . PRO A 1 198 ? 29.93865 8.24775  -3.01336  1.000 37.74851  ? 198 PRO A CD  1 
ATOM   1523 N N   . LEU A 1 199 ? 27.78299 11.87209 -4.96525  1.000 37.71574  ? 199 LEU A N   1 
ATOM   1524 C CA  . LEU A 1 199 ? 28.06501 13.11383 -5.65039  1.000 38.31948  ? 199 LEU A CA  1 
ATOM   1525 C C   . LEU A 1 199 ? 27.69200 14.25688 -4.73718  1.000 40.26425  ? 199 LEU A C   1 
ATOM   1526 O O   . LEU A 1 199 ? 26.69820 14.16252 -4.00966  1.000 40.92142  ? 199 LEU A O   1 
ATOM   1527 C CB  . LEU A 1 199 ? 27.29094 13.20006 -6.94666  1.000 36.88540  ? 199 LEU A CB  1 
ATOM   1528 C CG  . LEU A 1 199 ? 27.62888 12.12217 -7.94579  1.000 35.83410  ? 199 LEU A CG  1 
ATOM   1529 C CD1 . LEU A 1 199 ? 26.58456 12.23525 -9.00779  1.000 36.72808  ? 199 LEU A CD1 1 
ATOM   1530 C CD2 . LEU A 1 199 ? 29.00658 12.40878 -8.49101  1.000 35.26593  ? 199 LEU A CD2 1 
ATOM   1531 N N   . VAL A 1 200 ? 28.48102 15.32475 -4.77571  1.000 41.07782  ? 200 VAL A N   1 
ATOM   1532 C CA  . VAL A 1 200 ? 28.29113 16.43596 -3.85892  1.000 42.05688  ? 200 VAL A CA  1 
ATOM   1533 C C   . VAL A 1 200 ? 28.18497 17.71198 -4.67953  1.000 43.37050  ? 200 VAL A C   1 
ATOM   1534 O O   . VAL A 1 200 ? 29.13705 18.08206 -5.37254  1.000 44.08565  ? 200 VAL A O   1 
ATOM   1535 C CB  . VAL A 1 200 ? 29.42724 16.50689 -2.82482  1.000 42.55235  ? 200 VAL A CB  1 
ATOM   1536 C CG1 . VAL A 1 200 ? 29.40640 17.82358 -2.10391  1.000 43.58234  ? 200 VAL A CG1 1 
ATOM   1537 C CG2 . VAL A 1 200 ? 29.29635 15.35350 -1.82382  1.000 41.01675  ? 200 VAL A CG2 1 
ATOM   1538 N N   . PHE A 1 201 ? 27.01137 18.38425 -4.61396  1.000 43.27486  ? 201 PHE A N   1 
ATOM   1539 C CA  . PHE A 1 201 ? 26.66018 19.51301 -5.47476  1.000 44.40424  ? 201 PHE A CA  1 
ATOM   1540 C C   . PHE A 1 201 ? 26.70767 20.82802 -4.73162  1.000 47.86567  ? 201 PHE A C   1 
ATOM   1541 O O   . PHE A 1 201 ? 26.35620 20.89727 -3.55388  1.000 47.28166  ? 201 PHE A O   1 
ATOM   1542 C CB  . PHE A 1 201 ? 25.25896 19.35875 -6.06167  1.000 43.18792  ? 201 PHE A CB  1 
ATOM   1543 C CG  . PHE A 1 201 ? 25.10971 18.11726 -6.80802  1.000 41.98230  ? 201 PHE A CG  1 
ATOM   1544 C CD1 . PHE A 1 201 ? 24.67438 16.97768 -6.17298  1.000 40.54140  ? 201 PHE A CD1 1 
ATOM   1545 C CD2 . PHE A 1 201 ? 25.49994 18.05474 -8.12683  1.000 42.09873  ? 201 PHE A CD2 1 
ATOM   1546 C CE1 . PHE A 1 201 ? 24.58076 15.80423 -6.85314  1.000 39.78953  ? 201 PHE A CE1 1 
ATOM   1547 C CE2 . PHE A 1 201 ? 25.40897 16.88796 -8.81874  1.000 41.18129  ? 201 PHE A CE2 1 
ATOM   1548 C CZ  . PHE A 1 201 ? 24.94724 15.75374 -8.18057  1.000 39.98192  ? 201 PHE A CZ  1 
ATOM   1549 N N   . PRO A 1 202 ? 27.10215 21.89173 -5.40503  1.000 52.03155  ? 202 PRO A N   1 
ATOM   1550 C CA  . PRO A 1 202 ? 27.11172 23.20196 -4.75511  1.000 56.70842  ? 202 PRO A CA  1 
ATOM   1551 C C   . PRO A 1 202 ? 25.79143 23.93932 -4.87033  1.000 60.45641  ? 202 PRO A C   1 
ATOM   1552 O O   . PRO A 1 202 ? 24.81901 23.45227 -5.46549  1.000 60.13383  ? 202 PRO A O   1 
ATOM   1553 C CB  . PRO A 1 202 ? 28.22079 23.94255 -5.50696  1.000 57.17440  ? 202 PRO A CB  1 
ATOM   1554 C CG  . PRO A 1 202 ? 28.11491 23.39083 -6.89254  1.000 56.07193  ? 202 PRO A CG  1 
ATOM   1555 C CD  . PRO A 1 202 ? 27.79138 21.92284 -6.70748  1.000 53.23405  ? 202 PRO A CD  1 
ATOM   1556 N N   . LYS A 1 203 ? 25.77583 25.13457 -4.28945  1.000 63.91163  ? 203 LYS A N   1 
ATOM   1557 C CA  . LYS A 1 203 ? 24.66205 26.04328 -4.48149  1.000 66.90503  ? 203 LYS A CA  1 
ATOM   1558 C C   . LYS A 1 203 ? 24.43412 26.29591 -5.96110  1.000 68.06603  ? 203 LYS A C   1 
ATOM   1559 O O   . LYS A 1 203 ? 25.38215 26.35426 -6.74912  1.000 67.79873  ? 203 LYS A O   1 
ATOM   1560 C CB  . LYS A 1 203 ? 24.94970 27.35439 -3.78671  1.000 70.56824  ? 203 LYS A CB  1 
ATOM   1561 C CG  . LYS A 1 203 ? 24.30716 27.49554 -2.46427  1.000 72.22473  ? 203 LYS A CG  1 
ATOM   1562 C CD  . LYS A 1 203 ? 24.49736 28.91109 -2.03784  1.000 76.12827  ? 203 LYS A CD  1 
ATOM   1563 C CE  . LYS A 1 203 ? 23.33254 29.36525 -1.21394  1.000 79.28861  ? 203 LYS A CE  1 
ATOM   1564 N NZ  . LYS A 1 203 ? 22.06793 29.06280 -1.91308  1.000 80.67902  ? 203 LYS A NZ  1 
ATOM   1565 N N   . HIS A 1 204 ? 23.16533 26.44588 -6.32685  1.000 67.19026  ? 204 HIS A N   1 
ATOM   1566 C CA  . HIS A 1 204 ? 22.71732 26.84744 -7.64777  1.000 66.09659  ? 204 HIS A CA  1 
ATOM   1567 C C   . HIS A 1 204 ? 22.77228 25.69710 -8.64336  1.000 63.10077  ? 204 HIS A C   1 
ATOM   1568 O O   . HIS A 1 204 ? 22.19233 25.82232 -9.71974  1.000 64.64008  ? 204 HIS A O   1 
ATOM   1569 C CB  . HIS A 1 204 ? 23.49489 28.05771 -8.20118  1.000 67.18248  ? 204 HIS A CB  1 
ATOM   1570 C CG  . HIS A 1 204 ? 23.43028 29.24614 -7.30211  1.000 69.99736  ? 204 HIS A CG  1 
ATOM   1571 N ND1 . HIS A 1 204 ? 22.23102 29.73344 -6.83600  1.000 71.84915  ? 204 HIS A ND1 1 
ATOM   1572 C CD2 . HIS A 1 204 ? 24.39318 30.02648 -6.75641  1.000 71.51733  ? 204 HIS A CD2 1 
ATOM   1573 C CE1 . HIS A 1 204 ? 22.45227 30.77969 -6.06232  1.000 73.93726  ? 204 HIS A CE1 1 
ATOM   1574 N NE2 . HIS A 1 204 ? 23.75608 30.97934 -5.99714  1.000 73.70572  ? 204 HIS A NE2 1 
ATOM   1575 N N   . HIS A 1 205 ? 23.41243 24.56908 -8.33165  1.000 59.14660  ? 205 HIS A N   1 
ATOM   1576 C CA  . HIS A 1 205 ? 23.23164 23.40993 -9.18951  1.000 56.35216  ? 205 HIS A CA  1 
ATOM   1577 C C   . HIS A 1 205 ? 21.84180 22.83439 -8.93206  1.000 55.26760  ? 205 HIS A C   1 
ATOM   1578 O O   . HIS A 1 205 ? 21.40303 22.73463 -7.78245  1.000 54.30822  ? 205 HIS A O   1 
ATOM   1579 C CB  . HIS A 1 205 ? 24.34244 22.38621 -8.94496  1.000 53.59769  ? 205 HIS A CB  1 
ATOM   1580 C CG  . HIS A 1 205 ? 25.67769 22.80468 -9.49661  1.000 53.62075  ? 205 HIS A CG  1 
ATOM   1581 N ND1 . HIS A 1 205 ? 26.69999 21.91271 -9.74715  1.000 52.17109  ? 205 HIS A ND1 1 
ATOM   1582 C CD2 . HIS A 1 205 ? 26.15518 24.02438 -9.84593  1.000 55.33915  ? 205 HIS A CD2 1 
ATOM   1583 C CE1 . HIS A 1 205 ? 27.74772 22.56303 -10.22360 1.000 53.13518  ? 205 HIS A CE1 1 
ATOM   1584 N NE2 . HIS A 1 205 ? 27.44291 23.84620 -10.29318 1.000 55.03255  ? 205 HIS A NE2 1 
ATOM   1585 N N   . VAL A 1 206 ? 21.11847 22.52804 -10.00936 1.000 55.53494  ? 206 VAL A N   1 
ATOM   1586 C CA  . VAL A 1 206 ? 19.82162 21.86328 -9.93174  1.000 54.64886  ? 206 VAL A CA  1 
ATOM   1587 C C   . VAL A 1 206 ? 20.01522 20.42836 -10.39102 1.000 52.57560  ? 206 VAL A C   1 
ATOM   1588 O O   . VAL A 1 206 ? 20.38189 20.18284 -11.54826 1.000 52.94533  ? 206 VAL A O   1 
ATOM   1589 C CB  . VAL A 1 206 ? 18.74949 22.56506 -10.78206 1.000 56.36272  ? 206 VAL A CB  1 
ATOM   1590 C CG1 . VAL A 1 206 ? 17.54930 21.63557 -10.98671 1.000 56.03171  ? 206 VAL A CG1 1 
ATOM   1591 C CG2 . VAL A 1 206 ? 18.29538 23.85255 -10.12170 1.000 58.15038  ? 206 VAL A CG2 1 
ATOM   1592 N N   . VAL A 1 207 ? 19.76968 19.48263 -9.49132  1.000 50.54087  ? 207 VAL A N   1 
ATOM   1593 C CA  . VAL A 1 207 ? 19.72903 18.07092 -9.84368  1.000 49.54050  ? 207 VAL A CA  1 
ATOM   1594 C C   . VAL A 1 207 ? 18.27372 17.67957 -10.03608 1.000 51.54895  ? 207 VAL A C   1 
ATOM   1595 O O   . VAL A 1 207 ? 17.45742 17.78494 -9.11079  1.000 51.61189  ? 207 VAL A O   1 
ATOM   1596 C CB  . VAL A 1 207 ? 20.40589 17.18711 -8.78890  1.000 47.53133  ? 207 VAL A CB  1 
ATOM   1597 C CG1 . VAL A 1 207 ? 20.39327 15.74437 -9.26039  1.000 46.76646  ? 207 VAL A CG1 1 
ATOM   1598 C CG2 . VAL A 1 207 ? 21.82771 17.65583 -8.54854  1.000 46.87577  ? 207 VAL A CG2 1 
ATOM   1599 N N   . SER A 1 208 ? 17.96295 17.21227 -11.23911 1.000 52.54942  ? 208 SER A N   1 
ATOM   1600 C CA  . SER A 1 208 ? 16.60719 16.93948 -11.68138 1.000 53.63082  ? 208 SER A CA  1 
ATOM   1601 C C   . SER A 1 208 ? 16.50908 15.47812 -12.09414 1.000 53.05213  ? 208 SER A C   1 
ATOM   1602 O O   . SER A 1 208 ? 17.39797 14.97308 -12.79955 1.000 53.19450  ? 208 SER A O   1 
ATOM   1603 C CB  . SER A 1 208 ? 16.24163 17.87505 -12.84283 1.000 55.18136  ? 208 SER A CB  1 
ATOM   1604 O OG  . SER A 1 208 ? 15.17628 17.34938 -13.61171 1.000 56.30443  ? 208 SER A OG  1 
ATOM   1605 N N   . LEU A 1 209 ? 15.45266 14.79988 -11.63850 1.000 52.96945  ? 209 LEU A N   1 
ATOM   1606 C CA  . LEU A 1 209 ? 15.24652 13.38785 -11.92142 1.000 53.52152  ? 209 LEU A CA  1 
ATOM   1607 C C   . LEU A 1 209 ? 14.09343 13.26949 -12.90794 1.000 57.14871  ? 209 LEU A C   1 
ATOM   1608 O O   . LEU A 1 209 ? 13.10201 14.00171 -12.78791 1.000 59.30990  ? 209 LEU A O   1 
ATOM   1609 C CB  . LEU A 1 209 ? 14.97942 12.60500 -10.62637 1.000 52.65587  ? 209 LEU A CB  1 
ATOM   1610 C CG  . LEU A 1 209 ? 16.10510 12.48788 -9.57218  1.000 50.89732  ? 209 LEU A CG  1 
ATOM   1611 C CD1 . LEU A 1 209 ? 15.67795 11.88512 -8.22165  1.000 50.50948  ? 209 LEU A CD1 1 
ATOM   1612 C CD2 . LEU A 1 209 ? 17.24432 11.68104 -10.13779 1.000 50.11752  ? 209 LEU A CD2 1 
ATOM   1613 N N   . GLN A 1 210 ? 14.20521 12.37623 -13.89010 1.000 57.97637  ? 210 GLN A N   1 
ATOM   1614 C CA  . GLN A 1 210 ? 13.14497 12.28058 -14.88947 1.000 60.14548  ? 210 GLN A CA  1 
ATOM   1615 C C   . GLN A 1 210 ? 12.78132 10.82243 -15.12344 1.000 61.12506  ? 210 GLN A C   1 
ATOM   1616 O O   . GLN A 1 210 ? 13.65830 10.01119 -15.46919 1.000 59.67023  ? 210 GLN A O   1 
ATOM   1617 C CB  . GLN A 1 210 ? 13.54268 13.01177 -16.17726 0.900 60.33206  ? 210 GLN A CB  1 
ATOM   1618 C CG  . GLN A 1 210 ? 13.55721 14.56033 -16.00381 0.800 60.45944  ? 210 GLN A CG  1 
ATOM   1619 C CD  . GLN A 1 210 ? 14.40462 15.29401 -17.04194 0.700 60.59872  ? 210 GLN A CD  1 
ATOM   1620 O OE1 . GLN A 1 210 ? 15.01294 16.32622 -16.74757 0.700 59.94580  ? 210 GLN A OE1 1 
ATOM   1621 N NE2 . GLN A 1 210 ? 14.43766 14.76913 -18.25996 0.700 61.44898  ? 210 GLN A NE2 1 
ATOM   1622 N N   . PRO A 1 211 ? 11.51426 10.45365 -14.93434 1.000 63.77778  ? 211 PRO A N   1 
ATOM   1623 C CA  . PRO A 1 211 ? 11.10939 9.05271  -15.03186 1.000 65.31573  ? 211 PRO A CA  1 
ATOM   1624 C C   . PRO A 1 211 ? 11.09412 8.57804  -16.47154 1.000 67.64367  ? 211 PRO A C   1 
ATOM   1625 O O   . PRO A 1 211 ? 10.86281 9.34423  -17.41056 1.000 69.11636  ? 211 PRO A O   1 
ATOM   1626 C CB  . PRO A 1 211 ? 9.69832  9.04070  -14.43656 1.000 67.06259  ? 211 PRO A CB  1 
ATOM   1627 C CG  . PRO A 1 211 ? 9.49497  10.39946 -13.82744 1.000 66.67805  ? 211 PRO A CG  1 
ATOM   1628 C CD  . PRO A 1 211 ? 10.39900 11.32906 -14.55044 1.000 65.48922  ? 211 PRO A CD  1 
ATOM   1629 N N   . VAL A 1 212 ? 11.30151 7.27816  -16.62296 1.000 68.76283  ? 212 VAL A N   1 
ATOM   1630 C CA  . VAL A 1 212 ? 11.45994 6.65187  -17.92380 1.000 71.42674  ? 212 VAL A CA  1 
ATOM   1631 C C   . VAL A 1 212 ? 10.12577 6.04405  -18.34846 1.000 75.47612  ? 212 VAL A C   1 
ATOM   1632 O O   . VAL A 1 212 ? 9.54475  6.46109  -19.35912 1.000 78.52313  ? 212 VAL A O   1 
ATOM   1633 C CB  . VAL A 1 212 ? 12.60308 5.62271  -17.85916 1.000 69.64163  ? 212 VAL A CB  1 
ATOM   1634 C CG1 . VAL A 1 212 ? 12.62965 4.75259  -19.09012 1.000 71.22782  ? 212 VAL A CG1 1 
ATOM   1635 C CG2 . VAL A 1 212 ? 13.93929 6.34862  -17.68000 1.000 67.02182  ? 212 VAL A CG2 1 
ATOM   1636 N N   . ASN A 1 213 ? 9.61623  5.08423  -17.55720 1.000 76.87352  ? 213 ASN A N   1 
ATOM   1637 C CA  . ASN A 1 213 ? 8.29819  4.47584  -17.76301 1.000 80.20341  ? 213 ASN A CA  1 
ATOM   1638 C C   . ASN A 1 213 ? 7.34459  4.67496  -16.56333 1.000 78.96762  ? 213 ASN A C   1 
ATOM   1639 O O   . ASN A 1 213 ? 6.47695  5.54872  -16.64725 1.000 80.67741  ? 213 ASN A O   1 
ATOM   1640 C CB  . ASN A 1 213 ? 8.44957  2.98784  -18.12095 1.000 81.85848  ? 213 ASN A CB  1 
ATOM   1641 C CG  . ASN A 1 213 ? 9.23558  2.75659  -19.43072 1.000 83.72729  ? 213 ASN A CG  1 
ATOM   1642 O OD1 . ASN A 1 213 ? 9.14886  3.53662  -20.38343 1.000 85.17377  ? 213 ASN A OD1 1 
ATOM   1643 N ND2 . ASN A 1 213 ? 10.00013 1.66886  -19.46949 0.540 83.66471  ? 213 ASN A ND2 1 
ATOM   1644 N N   . ASP A 1 214 ? 7.44765  3.90389  -15.46044 1.000 75.72836  ? 214 ASP A N   1 
ATOM   1645 C CA  . ASP A 1 214 ? 6.54167  4.11635  -14.31577 1.000 73.95159  ? 214 ASP A CA  1 
ATOM   1646 C C   . ASP A 1 214 ? 6.66528  5.55047  -13.81565 1.000 71.48607  ? 214 ASP A C   1 
ATOM   1647 O O   . ASP A 1 214 ? 7.76404  6.10604  -13.74578 1.000 69.53728  ? 214 ASP A O   1 
ATOM   1648 C CB  . ASP A 1 214 ? 6.82874  3.13226  -13.15487 0.800 71.73603  ? 214 ASP A CB  1 
ATOM   1649 C CG  . ASP A 1 214 ? 6.05059  3.46994  -11.83262 0.600 72.69623  ? 214 ASP A CG  1 
ATOM   1650 O OD1 . ASP A 1 214 ? 4.94931  4.06745  -11.86839 0.600 74.95127  ? 214 ASP A OD1 1 
ATOM   1651 O OD2 . ASP A 1 214 ? 6.55484  3.12032  -10.73830 0.600 71.56771  ? 214 ASP A OD2 1 
ATOM   1652 N N   . LYS A 1 215 ? 5.52914  6.16121  -13.47914 1.000 72.53268  ? 215 LYS A N   1 
ATOM   1653 C CA  . LYS A 1 215 ? 5.51111  7.56738  -13.09649 1.000 69.81982  ? 215 LYS A CA  1 
ATOM   1654 C C   . LYS A 1 215 ? 5.16099  7.78021  -11.62346 1.000 67.53943  ? 215 LYS A C   1 
ATOM   1655 O O   . LYS A 1 215 ? 5.04903  8.92898  -11.18618 1.000 66.33704  ? 215 LYS A O   1 
ATOM   1656 C CB  . LYS A 1 215 ? 4.54965  8.34894  -14.00758 1.000 72.19828  ? 215 LYS A CB  1 
ATOM   1657 C CG  . LYS A 1 215 ? 4.97557  8.40847  -15.50704 1.000 72.38720  ? 215 LYS A CG  1 
ATOM   1658 C CD  . LYS A 1 215 ? 3.87678  8.99161  -16.43138 1.000 76.18843  ? 215 LYS A CD  1 
ATOM   1659 C CE  . LYS A 1 215 ? 4.28566  9.00599  -17.91998 0.540 77.71160  ? 215 LYS A CE  1 
ATOM   1660 N NZ  . LYS A 1 215 ? 3.18447  9.45310  -18.83897 0.730 82.30191  ? 215 LYS A NZ  1 
ATOM   1661 N N   . ASP A 1 216 ? 5.02054  6.71522  -10.83802 1.000 66.85955  ? 216 ASP A N   1 
ATOM   1662 C CA  . ASP A 1 216 ? 4.67179  6.84402  -9.42827  1.000 67.14653  ? 216 ASP A CA  1 
ATOM   1663 C C   . ASP A 1 216 ? 5.89157  6.60739  -8.54613  1.000 64.84583  ? 216 ASP A C   1 
ATOM   1664 O O   . ASP A 1 216 ? 6.67969  5.68894  -8.78833  1.000 64.40082  ? 216 ASP A O   1 
ATOM   1665 C CB  . ASP A 1 216 ? 3.54948  5.87599  -9.05419  1.000 69.54034  ? 216 ASP A CB  1 
ATOM   1666 C CG  . ASP A 1 216 ? 2.33071  6.05699  -9.91877  1.000 73.26934  ? 216 ASP A CG  1 
ATOM   1667 O OD1 . ASP A 1 216 ? 2.20354  7.14047  -10.52824 1.000 73.73718  ? 216 ASP A OD1 1 
ATOM   1668 O OD2 . ASP A 1 216 ? 1.50545  5.12647  -9.99482  1.000 75.82851  ? 216 ASP A OD2 1 
ATOM   1669 N N   . PHE A 1 217 ? 6.04069  7.45441  -7.52657  1.000 64.70163  ? 217 PHE A N   1 
ATOM   1670 C CA  . PHE A 1 217 ? 7.18088  7.38506  -6.62568  1.000 61.71722  ? 217 PHE A CA  1 
ATOM   1671 C C   . PHE A 1 217 ? 6.78251  7.72782  -5.21309  1.000 60.99109  ? 217 PHE A C   1 
ATOM   1672 O O   . PHE A 1 217 ? 5.85665  8.50311  -4.96681  1.000 62.77937  ? 217 PHE A O   1 
ATOM   1673 C CB  . PHE A 1 217 ? 8.29965  8.34149  -6.98779  1.000 61.24798  ? 217 PHE A CB  1 
ATOM   1674 C CG  . PHE A 1 217 ? 8.72358  8.22403  -8.37493  1.000 62.19856  ? 217 PHE A CG  1 
ATOM   1675 C CD1 . PHE A 1 217 ? 9.73849  7.36133  -8.72158  1.000 61.15534  ? 217 PHE A CD1 1 
ATOM   1676 C CD2 . PHE A 1 217 ? 8.07564  8.94434  -9.35423  1.000 64.34128  ? 217 PHE A CD2 1 
ATOM   1677 C CE1 . PHE A 1 217 ? 10.11903 7.23677  -10.02418 1.000 62.21230  ? 217 PHE A CE1 1 
ATOM   1678 C CE2 . PHE A 1 217 ? 8.44315  8.82613  -10.65444 1.000 65.27638  ? 217 PHE A CE2 1 
ATOM   1679 C CZ  . PHE A 1 217 ? 9.46992  7.97150  -10.99732 1.000 64.20472  ? 217 PHE A CZ  1 
ATOM   1680 N N   . GLN A 1 218 ? 7.56384  7.18574  -4.29994  1.000 58.37140  ? 218 GLN A N   1 
ATOM   1681 C CA  . GLN A 1 218 ? 7.45527  7.46197  -2.88370  1.000 59.08711  ? 218 GLN A CA  1 
ATOM   1682 C C   . GLN A 1 218 ? 8.56904  8.43444  -2.52892  1.000 58.02313  ? 218 GLN A C   1 
ATOM   1683 O O   . GLN A 1 218 ? 9.75085  8.08388  -2.60262  1.000 55.47141  ? 218 GLN A O   1 
ATOM   1684 C CB  . GLN A 1 218 ? 7.58736  6.17536  -2.08328  0.800 58.96265  ? 218 GLN A CB  1 
ATOM   1685 C CG  . GLN A 1 218 ? 7.00115  6.27808  -0.72595  0.700 59.91862  ? 218 GLN A CG  1 
ATOM   1686 C CD  . GLN A 1 218 ? 5.57916  5.80390  -0.71908  0.600 62.01129  ? 218 GLN A CD  1 
ATOM   1687 O OE1 . GLN A 1 218 ? 5.24449  4.83290  -1.39270  0.600 62.85621  ? 218 GLN A OE1 1 
ATOM   1688 N NE2 . GLN A 1 218 ? 4.72487  6.48739  0.02844   0.600 62.93963  ? 218 GLN A NE2 1 
ATOM   1689 N N   . ILE A 1 219 ? 8.20383  9.65026  -2.14904  1.000 60.32934  ? 219 ILE A N   1 
ATOM   1690 C CA  . ILE A 1 219 ? 9.17895  10.67093 -1.80301  1.000 58.26332  ? 219 ILE A CA  1 
ATOM   1691 C C   . ILE A 1 219 ? 9.18177  10.82827 -0.29674  1.000 57.64178  ? 219 ILE A C   1 
ATOM   1692 O O   . ILE A 1 219 ? 8.12137  10.89367 0.33404   1.000 58.84100  ? 219 ILE A O   1 
ATOM   1693 C CB  . ILE A 1 219 ? 8.88566  11.99834 -2.51396  1.000 59.02104  ? 219 ILE A CB  1 
ATOM   1694 C CG1 . ILE A 1 219 ? 9.04565  11.78837 -4.00839  1.000 59.35475  ? 219 ILE A CG1 1 
ATOM   1695 C CG2 . ILE A 1 219 ? 9.84209  13.07770 -2.02069  1.000 57.10713  ? 219 ILE A CG2 1 
ATOM   1696 C CD1 . ILE A 1 219 ? 8.45762  12.88142 -4.80183  1.000 61.16367  ? 219 ILE A CD1 1 
ATOM   1697 N N   . SER A 1 220 ? 10.37515 10.88312 0.27578   1.000 55.74850  ? 220 SER A N   1 
ATOM   1698 C CA  . SER A 1 220 ? 10.54016 10.98474 1.71196   1.000 55.65943  ? 220 SER A CA  1 
ATOM   1699 C C   . SER A 1 220 ? 11.28208 12.26234 2.02886   1.000 54.46139  ? 220 SER A C   1 
ATOM   1700 O O   . SER A 1 220 ? 12.38786 12.49040 1.53555   1.000 53.92072  ? 220 SER A O   1 
ATOM   1701 C CB  . SER A 1 220 ? 11.28828 9.78440  2.27478   1.000 54.97539  ? 220 SER A CB  1 
ATOM   1702 O OG  . SER A 1 220 ? 10.41360 8.70483  2.43581   1.000 57.14128  ? 220 SER A OG  1 
ATOM   1703 N N   . VAL A 1 221 ? 10.69595 13.07341 2.88456   1.000 54.52142  ? 221 VAL A N   1 
ATOM   1704 C CA  . VAL A 1 221 ? 11.34875 14.27317 3.34949   1.000 54.98392  ? 221 VAL A CA  1 
ATOM   1705 C C   . VAL A 1 221 ? 11.43235 14.16828 4.85743   1.000 55.72879  ? 221 VAL A C   1 
ATOM   1706 O O   . VAL A 1 221 ? 10.41561 14.29017 5.55660   1.000 58.42681  ? 221 VAL A O   1 
ATOM   1707 C CB  . VAL A 1 221 ? 10.61898 15.54047 2.90726   1.000 57.53013  ? 221 VAL A CB  1 
ATOM   1708 C CG1 . VAL A 1 221 ? 11.38340 16.72829 3.39063   1.000 57.92781  ? 221 VAL A CG1 1 
ATOM   1709 C CG2 . VAL A 1 221 ? 10.49744 15.53496 1.39740   1.000 58.15600  ? 221 VAL A CG2 1 
ATOM   1710 N N   . ASP A 1 222 ? 12.64980 13.94708 5.35590   1.000 53.93924  ? 222 ASP A N   1 
ATOM   1711 C CA  . ASP A 1 222 ? 12.86676 13.83364 6.78933   1.000 53.72031  ? 222 ASP A CA  1 
ATOM   1712 C C   . ASP A 1 222 ? 11.91529 12.80083 7.38498   1.000 55.96421  ? 222 ASP A C   1 
ATOM   1713 O O   . ASP A 1 222 ? 11.25465 13.05063 8.39742   1.000 58.23258  ? 222 ASP A O   1 
ATOM   1714 C CB  . ASP A 1 222 ? 12.69408 15.19108 7.46888   1.000 53.12559  ? 222 ASP A CB  1 
ATOM   1715 C CG  . ASP A 1 222 ? 13.73849 16.17486 7.04252   1.000 50.97589  ? 222 ASP A CG  1 
ATOM   1716 O OD1 . ASP A 1 222 ? 14.79071 15.72036 6.53987   1.000 48.15410  ? 222 ASP A OD1 1 
ATOM   1717 O OD2 . ASP A 1 222 ? 13.52693 17.39032 7.20185   1.000 52.06663  ? 222 ASP A OD2 1 
ATOM   1718 N N   . HIS A 1 223 ? 11.79166 11.65640 6.70764   1.000 56.46614  ? 223 HIS A N   1 
ATOM   1719 C CA  . HIS A 1 223 ? 11.07917 10.47779 7.15765   1.000 59.91073  ? 223 HIS A CA  1 
ATOM   1720 C C   . HIS A 1 223 ? 9.58375  10.61430 7.01820   1.000 62.96328  ? 223 HIS A C   1 
ATOM   1721 O O   . HIS A 1 223 ? 8.84537  9.69291  7.48039   1.000 64.09719  ? 223 HIS A O   1 
ATOM   1722 C CB  . HIS A 1 223 ? 11.39240 10.12503 8.61379   0.800 61.18015  ? 223 HIS A CB  1 
ATOM   1723 C CG  . HIS A 1 223 ? 11.34082 8.67531  8.86762   0.700 60.60325  ? 223 HIS A CG  1 
ATOM   1724 N ND1 . HIS A 1 223 ? 12.01400 7.78018  8.07113   0.700 58.94657  ? 223 HIS A ND1 1 
ATOM   1725 C CD2 . HIS A 1 223 ? 10.67526 7.95059  9.78957   0.700 61.82182  ? 223 HIS A CD2 1 
ATOM   1726 C CE1 . HIS A 1 223 ? 11.78557 6.55882  8.50941   0.700 59.46636  ? 223 HIS A CE1 1 
ATOM   1727 N NE2 . HIS A 1 223 ? 10.97697 6.63429  9.55122   0.700 61.23217  ? 223 HIS A NE2 1 
ATOM   1728 N N   . LEU A 1 224 ? 9.08854  11.72944 6.49155   1.000 64.41629  ? 224 LEU A N   1 
ATOM   1729 C CA  . LEU A 1 224 ? 7.71606  11.83335 6.05964   1.000 67.34121  ? 224 LEU A CA  1 
ATOM   1730 C C   . LEU A 1 224 ? 7.63796  11.19766 4.68953   1.000 67.53738  ? 224 LEU A C   1 
ATOM   1731 O O   . LEU A 1 224 ? 8.52345  11.47227 3.86762   1.000 65.99242  ? 224 LEU A O   1 
ATOM   1732 C CB  . LEU A 1 224 ? 7.34917  13.30864 6.01984   0.900 68.67990  ? 224 LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 224 ? 6.08202  13.82929 5.40538   0.800 71.89973  ? 224 LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 224 ? 4.93409  13.47779 6.31478   0.800 74.59759  ? 224 LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 224 ? 6.24773  15.32739 5.28948   0.800 72.86078  ? 224 LEU A CD2 1 
ATOM   1736 N N   . SER A 1 225 ? 6.66599  10.31920 4.44104   1.000 69.42892  ? 225 SER A N   1 
ATOM   1737 C CA  . SER A 1 225 ? 6.72703  9.68471  3.14142   1.000 67.63743  ? 225 SER A CA  1 
ATOM   1738 C C   . SER A 1 225 ? 5.40040  9.82268  2.45285   1.000 69.70311  ? 225 SER A C   1 
ATOM   1739 O O   . SER A 1 225 ? 4.41035  9.20474  2.85032   1.000 71.43966  ? 225 SER A O   1 
ATOM   1740 C CB  . SER A 1 225 ? 7.21665  8.25338  3.22731   1.000 66.06614  ? 225 SER A CB  1 
ATOM   1741 O OG  . SER A 1 225 ? 7.60240  7.86266  1.93432   1.000 65.12098  ? 225 SER A OG  1 
ATOM   1742 N N   . ILE A 1 226 ? 5.43846  10.60547 1.42916   1.000 68.96177  ? 226 ILE A N   1 
ATOM   1743 C CA  . ILE A 1 226 ? 4.31410  10.91713 0.58472   1.000 71.79531  ? 226 ILE A CA  1 
ATOM   1744 C C   . ILE A 1 226 ? 4.37530  9.98364  -0.59575  1.000 73.13466  ? 226 ILE A C   1 
ATOM   1745 O O   . ILE A 1 226 ? 5.47443  9.71848  -1.12473  1.000 71.41019  ? 226 ILE A O   1 
ATOM   1746 C CB  . ILE A 1 226 ? 4.37890  12.38702 0.12888   0.700 71.91468  ? 226 ILE A CB  1 
ATOM   1747 C CG1 . ILE A 1 226 ? 4.44568  13.36097 1.31170   0.600 71.90238  ? 226 ILE A CG1 1 
ATOM   1748 C CG2 . ILE A 1 226 ? 3.18953  12.69485 -0.71007  0.600 75.74309  ? 226 ILE A CG2 1 
ATOM   1749 C CD1 . ILE A 1 226 ? 5.84686  13.80354 1.72787   0.600 69.12809  ? 226 ILE A CD1 1 
ATOM   1750 N N   . LEU A 1 227 ? 3.22804  9.47870  -1.04246  1.000 76.71354  ? 227 LEU A N   1 
ATOM   1751 C CA  . LEU A 1 227 ? 3.22469  8.86597  -2.34893  1.000 76.72515  ? 227 LEU A CA  1 
ATOM   1752 C C   . LEU A 1 227 ? 2.81111  9.92083  -3.35885  1.000 77.75275  ? 227 LEU A C   1 
ATOM   1753 O O   . LEU A 1 227 ? 1.82276  10.62162 -3.14359  1.000 79.56549  ? 227 LEU A O   1 
ATOM   1754 C CB  . LEU A 1 227 ? 2.31228  7.65379  -2.40365  1.000 78.89438  ? 227 LEU A CB  1 
ATOM   1755 C CG  . LEU A 1 227 ? 1.97599  7.34724  -3.85205  1.000 79.39195  ? 227 LEU A CG  1 
ATOM   1756 C CD1 . LEU A 1 227 ? 3.20720  6.87168  -4.62107  1.000 76.66916  ? 227 LEU A CD1 1 
ATOM   1757 C CD2 . LEU A 1 227 ? 0.85530  6.34552  -3.96189  1.000 82.02811  ? 227 LEU A CD2 1 
ATOM   1758 N N   . HIS A 1 228 ? 3.58446  10.05994 -4.43235  1.000 76.85504  ? 228 HIS A N   1 
ATOM   1759 C CA  . HIS A 1 228 ? 3.25541  10.97834 -5.51017  1.000 79.08002  ? 228 HIS A CA  1 
ATOM   1760 C C   . HIS A 1 228 ? 2.89741  10.20105 -6.76987  1.000 80.58469  ? 228 HIS A C   1 
ATOM   1761 O O   . HIS A 1 228 ? 3.55065  9.20864  -7.11330  1.000 79.54756  ? 228 HIS A O   1 
ATOM   1762 C CB  . HIS A 1 228 ? 4.40832  11.94730 -5.77382  1.000 77.42957  ? 228 HIS A CB  1 
ATOM   1763 C CG  . HIS A 1 228 ? 4.66989  12.87832 -4.63234  1.000 77.48521  ? 228 HIS A CG  1 
ATOM   1764 N ND1 . HIS A 1 228 ? 4.50245  14.24390 -4.72281  1.000 78.63950  ? 228 HIS A ND1 1 
ATOM   1765 C CD2 . HIS A 1 228 ? 5.06889  12.63273 -3.36382  1.000 76.38660  ? 228 HIS A CD2 1 
ATOM   1766 C CE1 . HIS A 1 228 ? 4.79584  14.79946 -3.56057  1.000 78.02914  ? 228 HIS A CE1 1 
ATOM   1767 N NE2 . HIS A 1 228 ? 5.14843  13.84427 -2.72137  1.000 76.69136  ? 228 HIS A NE2 1 
ATOM   1768 N N   . ARG A 1 229 ? 1.85429  10.67596 -7.44555  1.000 83.34684  ? 229 ARG A N   1 
ATOM   1769 C CA  . ARG A 1 229 ? 1.26595  10.07012 -8.63005  1.000 85.15683  ? 229 ARG A CA  1 
ATOM   1770 C C   . ARG A 1 229 ? 1.50596  10.96753 -9.84523  1.000 84.13569  ? 229 ARG A C   1 
ATOM   1771 O O   . ARG A 1 229 ? 1.55452  12.19351 -9.71809  1.000 83.83592  ? 229 ARG A O   1 
ATOM   1772 C CB  . ARG A 1 229 ? -0.24004 9.86676  -8.41010  1.000 89.71696  ? 229 ARG A CB  1 
ATOM   1773 C CG  . ARG A 1 229 ? -0.86483 8.72914  -9.18399  1.000 92.96084  ? 229 ARG A CG  1 
ATOM   1774 C CD  . ARG A 1 229 ? -0.83516 7.44333  -8.37995  1.000 93.68576  ? 229 ARG A CD  1 
ATOM   1775 N NE  . ARG A 1 229 ? -1.77806 7.46888  -7.26913  0.780 96.43863  ? 229 ARG A NE  1 
ATOM   1776 C CZ  . ARG A 1 229 ? -2.12303 6.40216  -6.56106  0.880 98.08660  ? 229 ARG A CZ  1 
ATOM   1777 N NH1 . ARG A 1 229 ? -1.60988 5.21066  -6.81367  1.000 97.45185  ? 229 ARG A NH1 1 
ATOM   1778 N NH2 . ARG A 1 229 ? -3.00902 6.53179  -5.58089  0.890 100.37988 ? 229 ARG A NH2 1 
ATOM   1779 N N   . ASP A 1 230 ? 1.65706  10.34879 -11.02422 1.000 83.64900  ? 230 ASP A N   1 
ATOM   1780 C CA  . ASP A 1 230 ? 1.85291  11.03389 -12.32117 1.000 83.08705  ? 230 ASP A CA  1 
ATOM   1781 C C   . ASP A 1 230 ? 2.92895  12.12812 -12.24075 1.000 79.18164  ? 230 ASP A C   1 
ATOM   1782 O O   . ASP A 1 230 ? 2.68548  13.30608 -12.51202 1.000 81.26533  ? 230 ASP A O   1 
ATOM   1783 C CB  . ASP A 1 230 ? 0.51816  11.59224 -12.85347 1.000 87.53598  ? 230 ASP A CB  1 
ATOM   1784 C CG  . ASP A 1 230 ? 0.64724  12.29863 -14.22305 1.000 88.81969  ? 230 ASP A CG  1 
ATOM   1785 O OD1 . ASP A 1 230 ? 1.22731  11.72114 -15.16798 1.000 88.29465  ? 230 ASP A OD1 1 
ATOM   1786 O OD2 . ASP A 1 230 ? 0.14466  13.43733 -14.35309 1.000 90.72636  ? 230 ASP A OD2 1 
ATOM   1787 N N   . VAL A 1 231 ? 4.15406  11.70271 -11.89957 1.000 74.19578  ? 231 VAL A N   1 
ATOM   1788 C CA  . VAL A 1 231 ? 5.27446  12.61551 -11.66600 1.000 71.95822  ? 231 VAL A CA  1 
ATOM   1789 C C   . VAL A 1 231 ? 5.95984  12.96602 -12.98258 1.000 71.59147  ? 231 VAL A C   1 
ATOM   1790 O O   . VAL A 1 231 ? 6.21148  12.09197 -13.81955 1.000 72.06602  ? 231 VAL A O   1 
ATOM   1791 C CB  . VAL A 1 231 ? 6.28124  11.98456 -10.68551 1.000 69.17617  ? 231 VAL A CB  1 
ATOM   1792 C CG1 . VAL A 1 231 ? 7.47524  12.91386 -10.46398 1.000 67.26366  ? 231 VAL A CG1 1 
ATOM   1793 C CG2 . VAL A 1 231 ? 5.61088  11.62366 -9.37279  1.000 70.09475  ? 231 VAL A CG2 1 
ATOM   1794 N N   . GLN A 1 232 ? 6.31221  14.24407 -13.15137 1.000 70.79211  ? 232 GLN A N   1 
ATOM   1795 C CA  . GLN A 1 232 ? 7.02163  14.70962 -14.33883 1.000 68.64337  ? 232 GLN A CA  1 
ATOM   1796 C C   . GLN A 1 232 ? 8.47680  15.08533 -14.08737 1.000 65.46184  ? 232 GLN A C   1 
ATOM   1797 O O   . GLN A 1 232 ? 9.30279  14.91691 -14.98809 1.000 64.36782  ? 232 GLN A O   1 
ATOM   1798 C CB  . GLN A 1 232 ? 6.29448  15.91449 -14.95097 1.000 70.19978  ? 232 GLN A CB  1 
ATOM   1799 N N   . GLU A 1 233 ? 8.80369  15.58276 -12.89223 1.000 64.03230  ? 233 GLU A N   1 
ATOM   1800 C CA  . GLU A 1 233 ? 10.14950 15.99708 -12.51641 1.000 61.68983  ? 233 GLU A CA  1 
ATOM   1801 C C   . GLU A 1 233 ? 10.22579 16.03511 -10.99145 1.000 60.29849  ? 233 GLU A C   1 
ATOM   1802 O O   . GLU A 1 233 ? 9.22269  16.27899 -10.31331 1.000 62.04320  ? 233 GLU A O   1 
ATOM   1803 C CB  . GLU A 1 233 ? 10.50674 17.37118 -13.11801 1.000 63.26628  ? 233 GLU A CB  1 
ATOM   1804 C CG  . GLU A 1 233 ? 11.99882 17.63149 -13.41980 1.000 62.02938  ? 233 GLU A CG  1 
ATOM   1805 C CD  . GLU A 1 233 ? 12.28965 19.09409 -13.76430 1.000 63.63589  ? 233 GLU A CD  1 
ATOM   1806 O OE1 . GLU A 1 233 ? 11.34675 19.91238 -13.71011 1.000 66.00451  ? 233 GLU A OE1 1 
ATOM   1807 O OE2 . GLU A 1 233 ? 13.45946 19.43735 -14.05856 1.000 62.84667  ? 233 GLU A OE2 1 
ATOM   1808 N N   . ILE A 1 234 ? 11.41097 15.71181 -10.47150 1.000 57.21988  ? 234 ILE A N   1 
ATOM   1809 C CA  . ILE A 1 234 ? 11.82616 16.01852 -9.10487  1.000 55.48029  ? 234 ILE A CA  1 
ATOM   1810 C C   . ILE A 1 234 ? 13.07702 16.86563 -9.23451  1.000 54.42963  ? 234 ILE A C   1 
ATOM   1811 O O   . ILE A 1 234 ? 13.98013 16.49391 -10.00118 1.000 53.77334  ? 234 ILE A O   1 
ATOM   1812 C CB  . ILE A 1 234 ? 12.12086 14.75853 -8.26344  1.000 53.66626  ? 234 ILE A CB  1 
ATOM   1813 C CG1 . ILE A 1 234 ? 10.91961 13.82005 -8.21601  1.000 54.82260  ? 234 ILE A CG1 1 
ATOM   1814 C CG2 . ILE A 1 234 ? 12.59259 15.12471 -6.84102  1.000 52.96166  ? 234 ILE A CG2 1 
ATOM   1815 C CD1 . ILE A 1 234 ? 11.24914 12.51023 -7.57983  1.000 53.42892  ? 234 ILE A CD1 1 
ATOM   1816 N N   . ARG A 1 235 ? 13.11719 17.99821 -8.53051  1.000 54.48915  ? 235 ARG A N   1 
ATOM   1817 C CA  . ARG A 1 235 ? 14.23803 18.90305 -8.67756  1.000 53.74886  ? 235 ARG A CA  1 
ATOM   1818 C C   . ARG A 1 235 ? 14.81676 19.14082 -7.31282  1.000 52.84740  ? 235 ARG A C   1 
ATOM   1819 O O   . ARG A 1 235 ? 14.05361 19.45945 -6.37751  1.000 53.42056  ? 235 ARG A O   1 
ATOM   1820 C CB  . ARG A 1 235 ? 13.79021 20.18340 -9.38004  0.800 55.34445  ? 235 ARG A CB  1 
ATOM   1821 C CG  . ARG A 1 235 ? 13.20658 19.98254 -10.77938 0.700 56.49652  ? 235 ARG A CG  1 
ATOM   1822 C CD  . ARG A 1 235 ? 12.58852 21.25337 -11.36587 0.600 59.12615  ? 235 ARG A CD  1 
ATOM   1823 N NE  . ARG A 1 235 ? 13.55667 22.32792 -11.52356 0.500 59.31865  ? 235 ARG A NE  1 
ATOM   1824 C CZ  . ARG A 1 235 ? 14.37280 22.47973 -12.55776 0.500 59.24879  ? 235 ARG A CZ  1 
ATOM   1825 N NH1 . ARG A 1 235 ? 14.34310 21.66060 -13.59407 0.500 58.94156  ? 235 ARG A NH1 1 
ATOM   1826 N NH2 . ARG A 1 235 ? 15.25032 23.47497 -12.54395 0.500 59.61112  ? 235 ARG A NH2 1 
ATOM   1827 N N   . TYR A 1 236 ? 16.13468 18.93217 -7.17590  1.000 51.51903  ? 236 TYR A N   1 
ATOM   1828 C CA  . TYR A 1 236 ? 16.79752 19.20508 -5.91718  1.000 50.69713  ? 236 TYR A CA  1 
ATOM   1829 C C   . TYR A 1 236 ? 17.71726 20.38799 -6.08795  1.000 50.57167  ? 236 TYR A C   1 
ATOM   1830 O O   . TYR A 1 236 ? 18.46327 20.44359 -7.06067  1.000 50.55607  ? 236 TYR A O   1 
ATOM   1831 C CB  . TYR A 1 236 ? 17.58141 18.01195 -5.38703  1.000 49.28589  ? 236 TYR A CB  1 
ATOM   1832 C CG  . TYR A 1 236 ? 16.78346 16.75751 -5.14062  1.000 49.87675  ? 236 TYR A CG  1 
ATOM   1833 C CD1 . TYR A 1 236 ? 15.94895 16.64241 -4.03970  1.000 50.65950  ? 236 TYR A CD1 1 
ATOM   1834 C CD2 . TYR A 1 236 ? 16.91164 15.66492 -5.98921  1.000 50.20532  ? 236 TYR A CD2 1 
ATOM   1835 C CE1 . TYR A 1 236 ? 15.24432 15.49108 -3.81006  1.000 51.33739  ? 236 TYR A CE1 1 
ATOM   1836 C CE2 . TYR A 1 236 ? 16.21855 14.52240 -5.76581  1.000 51.01599  ? 236 TYR A CE2 1 
ATOM   1837 C CZ  . TYR A 1 236 ? 15.38942 14.44498 -4.67755  1.000 51.60312  ? 236 TYR A CZ  1 
ATOM   1838 O OH  . TYR A 1 236 ? 14.68873 13.32189 -4.43151  1.000 52.58613  ? 236 TYR A OH  1 
ATOM   1839 N N   . GLU A 1 237 ? 17.68409 21.31216 -5.13403  1.000 50.19369  ? 237 GLU A N   1 
ATOM   1840 C CA  . GLU A 1 237 ? 18.70608 22.33564 -5.08110  1.000 50.06902  ? 237 GLU A CA  1 
ATOM   1841 C C   . GLU A 1 237 ? 18.89626 22.73799 -3.63697  1.000 50.10258  ? 237 GLU A C   1 
ATOM   1842 O O   . GLU A 1 237 ? 18.01949 22.53925 -2.79127  1.000 50.67598  ? 237 GLU A O   1 
ATOM   1843 C CB  . GLU A 1 237 ? 18.33276 23.53860 -5.93561  1.000 52.15010  ? 237 GLU A CB  1 
ATOM   1844 C CG  . GLU A 1 237 ? 16.98106 24.09698 -5.58908  1.000 54.24482  ? 237 GLU A CG  1 
ATOM   1845 C CD  . GLU A 1 237 ? 16.40422 24.89843 -6.71979  0.400 56.01541  ? 237 GLU A CD  1 
ATOM   1846 O OE1 . GLU A 1 237 ? 17.15648 25.68479 -7.33224  1.000 56.65637  ? 237 GLU A OE1 1 
ATOM   1847 O OE2 . GLU A 1 237 ? 15.20184 24.73105 -7.00554  0.810 56.87813  ? 237 GLU A OE2 1 
ATOM   1848 N N   . VAL A 1 238 ? 20.06479 23.30535 -3.36773  1.000 49.71349  ? 238 VAL A N   1 
ATOM   1849 C CA  . VAL A 1 238 ? 20.29730 23.89173 -2.06448  1.000 49.98747  ? 238 VAL A CA  1 
ATOM   1850 C C   . VAL A 1 238 ? 19.35053 25.06971 -1.88255  1.000 52.60695  ? 238 VAL A C   1 
ATOM   1851 O O   . VAL A 1 238 ? 19.26511 25.95973 -2.73889  1.000 54.09048  ? 238 VAL A O   1 
ATOM   1852 C CB  . VAL A 1 238 ? 21.77003 24.29428 -1.92882  1.000 48.88417  ? 238 VAL A CB  1 
ATOM   1853 C CG1 . VAL A 1 238 ? 21.98547 25.05376 -0.63719  1.000 50.24558  ? 238 VAL A CG1 1 
ATOM   1854 C CG2 . VAL A 1 238 ? 22.65210 23.05395 -1.97890  1.000 46.28370  ? 238 VAL A CG2 1 
ATOM   1855 N N   . SER A 1 239 ? 18.61275 25.06149 -0.77248  1.000 52.37677  ? 239 SER A N   1 
ATOM   1856 C CA  . SER A 1 239 ? 17.59484 26.06847 -0.50123  1.000 53.93552  ? 239 SER A CA  1 
ATOM   1857 C C   . SER A 1 239 ? 18.22262 27.42887 -0.21868  1.000 55.61983  ? 239 SER A C   1 
ATOM   1858 O O   . SER A 1 239 ? 19.37241 27.53774 0.21042   1.000 55.28435  ? 239 SER A O   1 
ATOM   1859 C CB  . SER A 1 239 ? 16.73586 25.65692 0.69595   1.000 52.85058  ? 239 SER A CB  1 
ATOM   1860 O OG  . SER A 1 239 ? 15.87297 26.70609 1.10099   1.000 54.30321  ? 239 SER A OG  1 
ATOM   1861 N N   . ALA A 1 240 ? 17.43792 28.48252 -0.44772  1.000 57.34334  ? 240 ALA A N   1 
ATOM   1862 C CA  . ALA A 1 240 ? 17.86539 29.79720 0.01341   1.000 58.86984  ? 240 ALA A CA  1 
ATOM   1863 C C   . ALA A 1 240 ? 17.66315 29.95327 1.51612   1.000 58.46998  ? 240 ALA A C   1 
ATOM   1864 O O   . ALA A 1 240 ? 18.46124 30.62546 2.17878   1.000 59.90138  ? 240 ALA A O   1 
ATOM   1865 C CB  . ALA A 1 240 ? 17.12621 30.89852 -0.74833  1.000 61.49491  ? 240 ALA A CB  1 
ATOM   1866 N N   . LYS A 1 241 ? 16.62967 29.32660 2.07212   1.000 56.73202  ? 241 LYS A N   1 
ATOM   1867 C CA  . LYS A 1 241 ? 16.39687 29.38049 3.50839   1.000 56.41366  ? 241 LYS A CA  1 
ATOM   1868 C C   . LYS A 1 241 ? 17.44260 28.55178 4.25860   1.000 54.60797  ? 241 LYS A C   1 
ATOM   1869 O O   . LYS A 1 241 ? 18.07044 27.63429 3.69227   1.000 53.33899  ? 241 LYS A O   1 
ATOM   1870 C CB  . LYS A 1 241 ? 14.97934 28.89951 3.81124   0.800 55.72337  ? 241 LYS A CB  1 
ATOM   1871 C CG  . LYS A 1 241 ? 13.98234 29.45361 2.81238   0.700 57.27480  ? 241 LYS A CG  1 
ATOM   1872 C CD  . LYS A 1 241 ? 12.62220 28.82434 2.93871   0.600 56.70574  ? 241 LYS A CD  1 
ATOM   1873 C CE  . LYS A 1 241 ? 11.60977 29.55665 2.08538   0.500 58.45031  ? 241 LYS A CE  1 
ATOM   1874 N NZ  . LYS A 1 241 ? 10.35378 28.77324 2.02811   0.500 57.91911  ? 241 LYS A NZ  1 
ATOM   1875 N N   . LYS A 1 242 ? 17.65234 28.90990 5.53713   1.000 55.71799  ? 242 LYS A N   1 
ATOM   1876 C CA  . LYS A 1 242 ? 18.61614 28.25006 6.40190   1.000 54.09136  ? 242 LYS A CA  1 
ATOM   1877 C C   . LYS A 1 242 ? 17.92625 28.02954 7.73199   1.000 54.95973  ? 242 LYS A C   1 
ATOM   1878 O O   . LYS A 1 242 ? 16.98523 28.75678 8.06680   1.000 56.70106  ? 242 LYS A O   1 
ATOM   1879 C CB  . LYS A 1 242 ? 19.91892 29.09485 6.52385   0.700 54.19212  ? 242 LYS A CB  1 
ATOM   1880 C CG  . LYS A 1 242 ? 20.66475 29.40291 5.18282   0.600 53.99506  ? 242 LYS A CG  1 
ATOM   1881 C CD  . LYS A 1 242 ? 21.90845 30.33517 5.28752   0.500 55.45324  ? 242 LYS A CD  1 
ATOM   1882 C CE  . LYS A 1 242 ? 23.14824 29.66645 5.90236   0.500 54.21376  ? 242 LYS A CE  1 
ATOM   1883 N NZ  . LYS A 1 242 ? 23.74199 28.55665 5.09652   0.500 52.32087  ? 242 LYS A NZ  1 
ATOM   1884 N N   . ILE A 1 243 ? 18.34324 27.01983 8.49406   1.000 53.95158  ? 243 ILE A N   1 
ATOM   1885 C CA  . ILE A 1 243 ? 17.81875 26.88230 9.84721   1.000 54.48013  ? 243 ILE A CA  1 
ATOM   1886 C C   . ILE A 1 243 ? 18.78965 27.54159 10.79693  1.000 55.92391  ? 243 ILE A C   1 
ATOM   1887 O O   . ILE A 1 243 ? 20.00368 27.50264 10.55927  1.000 55.68756  ? 243 ILE A O   1 
ATOM   1888 C CB  . ILE A 1 243 ? 17.56982 25.41695 10.24623  1.000 52.20901  ? 243 ILE A CB  1 
ATOM   1889 C CG1 . ILE A 1 243 ? 17.01765 25.35015 11.68110  1.000 52.80863  ? 243 ILE A CG1 1 
ATOM   1890 C CG2 . ILE A 1 243 ? 18.84012 24.61064 10.13867  1.000 50.09267  ? 243 ILE A CG2 1 
ATOM   1891 C CD1 . ILE A 1 243 ? 16.72633 23.96781 12.19291  1.000 51.25756  ? 243 ILE A CD1 1 
ATOM   1892 N N   . HIS A 1 244 ? 18.26716 28.16557 11.85979  1.000 57.72025  ? 244 HIS A N   1 
ATOM   1893 C CA  . HIS A 1 244 ? 19.10736 28.82729 12.83845  1.000 59.70220  ? 244 HIS A CA  1 
ATOM   1894 C C   . HIS A 1 244 ? 19.08867 28.06489 14.15033  1.000 59.29416  ? 244 HIS A C   1 
ATOM   1895 O O   . HIS A 1 244 ? 18.01809 27.63926 14.60763  1.000 58.89797  ? 244 HIS A O   1 
ATOM   1896 C CB  . HIS A 1 244 ? 18.66512 30.27285 13.03687  1.000 63.24176  ? 244 HIS A CB  1 
ATOM   1897 C CG  . HIS A 1 244 ? 18.69977 31.07181 11.77361  1.000 64.76993  ? 244 HIS A CG  1 
ATOM   1898 N ND1 . HIS A 1 244 ? 19.87657 31.51295 11.20824  1.000 65.33875  ? 244 HIS A ND1 1 
ATOM   1899 C CD2 . HIS A 1 244 ? 17.70671 31.49657 10.95681  1.000 65.84261  ? 244 HIS A CD2 1 
ATOM   1900 C CE1 . HIS A 1 244 ? 19.60665 32.18192 10.10164  1.000 66.47141  ? 244 HIS A CE1 1 
ATOM   1901 N NE2 . HIS A 1 244 ? 18.29734 32.18703 9.92660   1.000 66.69456  ? 244 HIS A NE2 1 
ATOM   1902 N N   . PHE A 1 245 ? 20.26743 27.90535 14.75190  1.000 59.93706  ? 245 PHE A N   1 
ATOM   1903 C CA  . PHE A 1 245 ? 20.40664 27.23887 16.03515  1.000 60.37581  ? 245 PHE A CA  1 
ATOM   1904 C C   . PHE A 1 245 ? 20.86558 28.24715 17.07140  1.000 64.40467  ? 245 PHE A C   1 
ATOM   1905 O O   . PHE A 1 245 ? 21.70455 29.10193 16.77953  1.000 65.30843  ? 245 PHE A O   1 
ATOM   1906 C CB  . PHE A 1 245 ? 21.40219 26.08469 15.94800  1.000 58.43399  ? 245 PHE A CB  1 
ATOM   1907 C CG  . PHE A 1 245 ? 20.89698 24.90991 15.16279  1.000 56.55896  ? 245 PHE A CG  1 
ATOM   1908 C CD1 . PHE A 1 245 ? 20.19185 23.90171 15.79404  1.000 56.09313  ? 245 PHE A CD1 1 
ATOM   1909 C CD2 . PHE A 1 245 ? 21.13832 24.80417 13.80339  1.000 55.85605  ? 245 PHE A CD2 1 
ATOM   1910 C CE1 . PHE A 1 245 ? 19.73015 22.81734 15.08822  1.000 54.90006  ? 245 PHE A CE1 1 
ATOM   1911 C CE2 . PHE A 1 245 ? 20.67539 23.72014 13.09079  1.000 54.69211  ? 245 PHE A CE2 1 
ATOM   1912 C CZ  . PHE A 1 245 ? 19.96929 22.72491 13.73118  1.000 54.21198  ? 245 PHE A CZ  1 
ATOM   1913 N N   . ALA A 1 246 ? 20.33133 28.14837 18.28223  1.000 67.70306  ? 246 ALA A N   1 
ATOM   1914 C CA  . ALA A 1 246 ? 20.89189 28.92613 19.37382  1.000 74.47692  ? 246 ALA A CA  1 
ATOM   1915 C C   . ALA A 1 246 ? 22.12577 28.20030 19.89093  1.000 77.77217  ? 246 ALA A C   1 
ATOM   1916 O O   . ALA A 1 246 ? 22.07505 27.00191 20.18057  1.000 75.42161  ? 246 ALA A O   1 
ATOM   1917 C CB  . ALA A 1 246 ? 19.86912 29.13648 20.48874  1.000 77.12736  ? 246 ALA A CB  1 
ATOM   1918 N N   . ARG A 1 247 ? 23.24135 28.91449 19.95999  1.000 84.53583  ? 247 ARG A N   1 
ATOM   1919 C CA  . ARG A 1 247 ? 24.51477 28.35546 20.39105  1.000 89.91199  ? 247 ARG A CA  1 
ATOM   1920 C C   . ARG A 1 247 ? 24.90993 29.00813 21.70368  1.000 97.47239  ? 247 ARG A C   1 
ATOM   1921 O O   . ARG A 1 247 ? 25.15072 30.21941 21.75375  1.000 100.43934 ? 247 ARG A O   1 
ATOM   1922 C CB  . ARG A 1 247 ? 25.59899 28.57749 19.33735  0.700 89.00977  ? 247 ARG A CB  1 
ATOM   1923 N N   . PHE A 1 248 ? 24.98655 28.20879 22.76019  1.000 100.11806 ? 248 PHE A N   1 
ATOM   1924 C CA  . PHE A 1 248 ? 25.43196 28.74216 24.03259  1.000 104.64127 ? 248 PHE A CA  1 
ATOM   1925 C C   . PHE A 1 248 ? 26.86177 28.36972 24.37163  1.000 104.64201 ? 248 PHE A C   1 
ATOM   1926 O O   . PHE A 1 248 ? 27.48814 29.06151 25.17987  1.000 108.30700 ? 248 PHE A O   1 
ATOM   1927 C CB  . PHE A 1 248 ? 24.48209 28.29721 25.14274  1.000 107.62790 ? 248 PHE A CB  1 
ATOM   1928 C CG  . PHE A 1 248 ? 23.16781 28.98349 25.07193  0.870 110.63873 ? 248 PHE A CG  1 
ATOM   1929 C CD1 . PHE A 1 248 ? 23.09312 30.34017 25.30942  1.000 114.39946 ? 248 PHE A CD1 1 
ATOM   1930 C CD2 . PHE A 1 248 ? 22.02311 28.30491 24.69838  0.620 110.35317 ? 248 PHE A CD2 1 
ATOM   1931 C CE1 . PHE A 1 248 ? 21.89626 31.00388 25.22518  0.910 116.42668 ? 248 PHE A CE1 1 
ATOM   1932 C CE2 . PHE A 1 248 ? 20.81606 28.96832 24.60975  1.000 112.36366 ? 248 PHE A CE2 1 
ATOM   1933 C CZ  . PHE A 1 248 ? 20.75596 30.32137 24.87133  0.530 115.29572 ? 248 PHE A CZ  1 
ATOM   1934 N N   . ARG A 1 249 ? 27.40950 27.33258 23.75198  1.000 98.29156  ? 249 ARG A N   1 
ATOM   1935 C CA  . ARG A 1 249 ? 28.79171 26.97727 24.00975  1.000 95.90266  ? 249 ARG A CA  1 
ATOM   1936 C C   . ARG A 1 249 ? 29.35417 26.27162 22.78820  1.000 92.32467  ? 249 ARG A C   1 
ATOM   1937 O O   . ARG A 1 249 ? 28.66055 26.05605 21.78680  1.000 91.42998  ? 249 ARG A O   1 
ATOM   1938 C CB  . ARG A 1 249 ? 28.91921 26.12086 25.27753  1.000 94.16385  ? 249 ARG A CB  1 
ATOM   1939 C CG  . ARG A 1 249 ? 28.10713 24.83541 25.25429  0.550 90.72629  ? 249 ARG A CG  1 
ATOM   1940 C CD  . ARG A 1 249 ? 28.35288 23.95237 26.48352  1.000 89.78016  ? 249 ARG A CD  1 
ATOM   1941 N NE  . ARG A 1 249 ? 27.79855 22.62202 26.26156  0.570 85.65123  ? 249 ARG A NE  1 
ATOM   1942 C CZ  . ARG A 1 249 ? 27.58169 21.71242 27.20305  0.360 84.40271  ? 249 ARG A CZ  1 
ATOM   1943 N NH1 . ARG A 1 249 ? 27.86404 21.94794 28.47590  0.780 86.48669  ? 249 ARG A NH1 1 
ATOM   1944 N NH2 . ARG A 1 249 ? 27.05885 20.53872 26.85962  1.000 81.89897  ? 249 ARG A NH2 1 
ATOM   1945 N N   . SER A 1 250 ? 30.63573 25.93035 22.87602  1.000 90.15162  ? 250 SER A N   1 
ATOM   1946 C CA  . SER A 1 250 ? 31.26961 25.19391 21.79965  1.000 85.84404  ? 250 SER A CA  1 
ATOM   1947 C C   . SER A 1 250 ? 30.86701 23.73787 21.91099  1.000 81.35115  ? 250 SER A C   1 
ATOM   1948 O O   . SER A 1 250 ? 31.04883 23.10192 22.95041  1.000 82.04581  ? 250 SER A O   1 
ATOM   1949 C CB  . SER A 1 250 ? 32.78701 25.32988 21.83362  1.000 86.81770  ? 250 SER A CB  1 
ATOM   1950 O OG  . SER A 1 250 ? 33.34161 24.70357 20.69560  0.920 85.20071  ? 250 SER A OG  1 
ATOM   1951 N N   . PHE A 1 251 ? 30.28424 23.23147 20.84497  1.000 74.52261  ? 251 PHE A N   1 
ATOM   1952 C CA  . PHE A 1 251 ? 30.10657 21.80376 20.65735  1.000 68.30968  ? 251 PHE A CA  1 
ATOM   1953 C C   . PHE A 1 251 ? 30.38026 21.63124 19.18040  1.000 63.54698  ? 251 PHE A C   1 
ATOM   1954 O O   . PHE A 1 251 ? 29.46288 21.63424 18.35222  1.000 62.34307  ? 251 PHE A O   1 
ATOM   1955 C CB  . PHE A 1 251 ? 28.71256 21.34992 21.07121  1.000 66.57340  ? 251 PHE A CB  1 
ATOM   1956 C CG  . PHE A 1 251 ? 28.60271 19.88020 21.27708  1.000 65.24050  ? 251 PHE A CG  1 
ATOM   1957 C CD1 . PHE A 1 251 ? 29.72623 19.06400 21.27756  1.000 64.80031  ? 251 PHE A CD1 1 
ATOM   1958 C CD2 . PHE A 1 251 ? 27.36500 19.30895 21.45975  1.000 64.66693  ? 251 PHE A CD2 1 
ATOM   1959 C CE1 . PHE A 1 251 ? 29.60101 17.70102 21.46547  1.000 63.25262  ? 251 PHE A CE1 1 
ATOM   1960 C CE2 . PHE A 1 251 ? 27.23296 17.95570 21.64512  1.000 63.22473  ? 251 PHE A CE2 1 
ATOM   1961 C CZ  . PHE A 1 251 ? 28.35014 17.14673 21.64860  1.000 62.51899  ? 251 PHE A CZ  1 
ATOM   1962 N N   . PRO A 1 252 ? 31.65737 21.56284 18.80720  1.000 60.90461  ? 252 PRO A N   1 
ATOM   1963 C CA  . PRO A 1 252 ? 31.98818 21.45573 17.39760  1.000 58.41789  ? 252 PRO A CA  1 
ATOM   1964 C C   . PRO A 1 252 ? 31.38081 20.21055 16.81748  1.000 54.92438  ? 252 PRO A C   1 
ATOM   1965 O O   . PRO A 1 252 ? 31.27237 19.16027 17.47696  1.000 54.27802  ? 252 PRO A O   1 
ATOM   1966 C CB  . PRO A 1 252 ? 33.52031 21.40555 17.36900  1.000 59.33882  ? 252 PRO A CB  1 
ATOM   1967 C CG  . PRO A 1 252 ? 33.93970 21.93310 18.62437  1.000 61.75047  ? 252 PRO A CG  1 
ATOM   1968 C CD  . PRO A 1 252 ? 32.86847 21.64613 19.63355  1.000 61.95869  ? 252 PRO A CD  1 
ATOM   1969 N N   . PHE A 1 253 ? 31.00835 20.37524 15.57546  1.000 53.36276  ? 253 PHE A N   1 
ATOM   1970 C CA  . PHE A 1 253 ? 30.42633 19.31806 14.80539  1.000 50.65940  ? 253 PHE A CA  1 
ATOM   1971 C C   . PHE A 1 253 ? 31.30547 18.05972 14.80309  1.000 48.83238  ? 253 PHE A C   1 
ATOM   1972 O O   . PHE A 1 253 ? 30.81443 16.93992 15.01795  1.000 47.01289  ? 253 PHE A O   1 
ATOM   1973 C CB  . PHE A 1 253 ? 30.23090 19.89364 13.43860  1.000 50.79370  ? 253 PHE A CB  1 
ATOM   1974 C CG  . PHE A 1 253 ? 29.78960 18.93754 12.52450  1.000 49.43570  ? 253 PHE A CG  1 
ATOM   1975 C CD1 . PHE A 1 253 ? 28.47387 18.55637 12.54574  1.000 48.79261  ? 253 PHE A CD1 1 
ATOM   1976 C CD2 . PHE A 1 253 ? 30.67441 18.36983 11.64011  1.000 49.45334  ? 253 PHE A CD2 1 
ATOM   1977 C CE1 . PHE A 1 253 ? 28.03417 17.64723 11.68016  1.000 47.97343  ? 253 PHE A CE1 1 
ATOM   1978 C CE2 . PHE A 1 253 ? 30.23912 17.45691 10.77503  1.000 48.76490  ? 253 PHE A CE2 1 
ATOM   1979 C CZ  . PHE A 1 253 ? 28.91613 17.08934 10.78655  1.000 48.09179  ? 253 PHE A CZ  1 
ATOM   1980 N N   . TRP A 1 254 ? 32.59270 18.21334 14.48609  1.000 49.66710  ? 254 TRP A N   1 
ATOM   1981 C CA  . TRP A 1 254 ? 33.40658 17.00390 14.47663  1.000 49.19409  ? 254 TRP A CA  1 
ATOM   1982 C C   . TRP A 1 254 ? 33.47142 16.39242 15.86738  1.000 49.69562  ? 254 TRP A C   1 
ATOM   1983 O O   . TRP A 1 254 ? 33.43028 15.16367 15.99780  1.000 48.91648  ? 254 TRP A O   1 
ATOM   1984 C CB  . TRP A 1 254 ? 34.80906 17.26108 13.93331  1.000 50.42476  ? 254 TRP A CB  1 
ATOM   1985 C CG  . TRP A 1 254 ? 34.82937 17.78070 12.53578  1.000 50.62769  ? 254 TRP A CG  1 
ATOM   1986 C CD1 . TRP A 1 254 ? 35.29007 18.99637 12.14394  1.000 52.35895  ? 254 TRP A CD1 1 
ATOM   1987 C CD2 . TRP A 1 254 ? 34.38258 17.11475 11.33686  1.000 49.25575  ? 254 TRP A CD2 1 
ATOM   1988 N NE1 . TRP A 1 254 ? 35.16876 19.13702 10.78781  1.000 52.26975  ? 254 TRP A NE1 1 
ATOM   1989 C CE2 . TRP A 1 254 ? 34.61256 18.00017 10.26649  1.000 50.33849  ? 254 TRP A CE2 1 
ATOM   1990 C CE3 . TRP A 1 254 ? 33.81292 15.86535 11.06601  1.000 47.78477  ? 254 TRP A CE3 1 
ATOM   1991 C CZ2 . TRP A 1 254 ? 34.29400 17.68301 8.94742   1.000 49.30342  ? 254 TRP A CZ2 1 
ATOM   1992 C CZ3 . TRP A 1 254 ? 33.49557 15.55164 9.75071   1.000 46.87210  ? 254 TRP A CZ3 1 
ATOM   1993 C CH2 . TRP A 1 254 ? 33.74048 16.45809 8.70842   1.000 47.60325  ? 254 TRP A CH2 1 
ATOM   1994 N N   . ARG A 1 255 ? 33.54245 17.21324 16.91999  1.000 50.95298  ? 255 ARG A N   1 
ATOM   1995 C CA  . ARG A 1 255 ? 33.40430 16.65113 18.25964  1.000 51.67188  ? 255 ARG A CA  1 
ATOM   1996 C C   . ARG A 1 255 ? 32.11032 15.86333 18.36500  1.000 50.01845  ? 255 ARG A C   1 
ATOM   1997 O O   . ARG A 1 255 ? 32.09121 14.72777 18.85540  1.000 50.15037  ? 255 ARG A O   1 
ATOM   1998 C CB  . ARG A 1 255 ? 33.43415 17.73501 19.33619  0.900 53.64785  ? 255 ARG A CB  1 
ATOM   1999 C CG  . ARG A 1 255 ? 32.96257 17.15790 20.66868  0.800 54.09263  ? 255 ARG A CG  1 
ATOM   2000 C CD  . ARG A 1 255 ? 33.45192 17.90575 21.89401  0.700 56.63321  ? 255 ARG A CD  1 
ATOM   2001 N NE  . ARG A 1 255 ? 34.89269 18.12110 21.89829  0.600 58.06917  ? 255 ARG A NE  1 
ATOM   2002 C CZ  . ARG A 1 255 ? 35.80760 17.16387 21.99094  0.500 58.25163  ? 255 ARG A CZ  1 
ATOM   2003 N NH1 . ARG A 1 255 ? 35.47447 15.88319 22.03285  0.500 56.95101  ? 255 ARG A NH1 1 
ATOM   2004 N NH2 . ARG A 1 255 ? 37.09038 17.49872 22.03916  0.500 59.92232  ? 255 ARG A NH2 1 
ATOM   2005 N N   . ARG A 1 256 ? 31.02201 16.44614 17.87105  1.000 48.11349  ? 256 ARG A N   1 
ATOM   2006 C CA  . ARG A 1 256 ? 29.73260 15.77466 17.90145  1.000 47.06879  ? 256 ARG A CA  1 
ATOM   2007 C C   . ARG A 1 256 ? 29.77150 14.44832 17.14945  1.000 45.61831  ? 256 ARG A C   1 
ATOM   2008 O O   . ARG A 1 256 ? 29.20504 13.44673 17.60312  1.000 44.94104  ? 256 ARG A O   1 
ATOM   2009 C CB  . ARG A 1 256 ? 28.68150 16.69666 17.30868  1.000 47.23750  ? 256 ARG A CB  1 
ATOM   2010 C CG  . ARG A 1 256 ? 27.32460 16.33787 17.74482  1.000 47.73959  ? 256 ARG A CG  1 
ATOM   2011 C CD  . ARG A 1 256 ? 26.52824 17.57845 17.92966  0.800 48.28456  ? 256 ARG A CD  1 
ATOM   2012 N NE  . ARG A 1 256 ? 26.17299 18.15228 16.63869  0.700 46.45057  ? 256 ARG A NE  1 
ATOM   2013 C CZ  . ARG A 1 256 ? 26.45372 19.39245 16.26147  0.600 46.76474  ? 256 ARG A CZ  1 
ATOM   2014 N NH1 . ARG A 1 256 ? 27.10947 20.22878 17.06085  0.600 48.11701  ? 256 ARG A NH1 1 
ATOM   2015 N NH2 . ARG A 1 256 ? 26.05097 19.81396 15.06169  0.600 46.39426  ? 256 ARG A NH2 1 
ATOM   2016 N N   . VAL A 1 257 ? 30.43388 14.43628 15.98909  1.000 44.83028  ? 257 VAL A N   1 
ATOM   2017 C CA  . VAL A 1 257 ? 30.60653 13.21608 15.20316  1.000 43.44871  ? 257 VAL A CA  1 
ATOM   2018 C C   . VAL A 1 257 ? 31.35267 12.15466 16.00400  1.000 44.12650  ? 257 VAL A C   1 
ATOM   2019 O O   . VAL A 1 257 ? 30.98265 10.97388 15.99564  1.000 43.57588  ? 257 VAL A O   1 
ATOM   2020 C CB  . VAL A 1 257 ? 31.34110 13.54604 13.88872  1.000 42.85549  ? 257 VAL A CB  1 
ATOM   2021 C CG1 . VAL A 1 257 ? 31.87800 12.27763 13.23054  1.000 41.69881  ? 257 VAL A CG1 1 
ATOM   2022 C CG2 . VAL A 1 257 ? 30.43595 14.32431 12.94693  1.000 42.12612  ? 257 VAL A CG2 1 
ATOM   2023 N N   . HIS A 1 258 ? 32.43195 12.55770 16.68168  1.000 45.22721  ? 258 HIS A N   1 
ATOM   2024 C CA  . HIS A 1 258 ? 33.24065 11.62831 17.46694  1.000 46.12395  ? 258 HIS A CA  1 
ATOM   2025 C C   . HIS A 1 258 ? 32.40552 10.92472 18.52155  1.000 46.61011  ? 258 HIS A C   1 
ATOM   2026 O O   . HIS A 1 258 ? 32.48802 9.70177  18.68302  1.000 47.01312  ? 258 HIS A O   1 
ATOM   2027 C CB  . HIS A 1 258 ? 34.39248 12.38340 18.13536  1.000 47.69719  ? 258 HIS A CB  1 
ATOM   2028 C CG  . HIS A 1 258 ? 35.18791 11.56030 19.10542  1.000 49.18571  ? 258 HIS A CG  1 
ATOM   2029 N ND1 . HIS A 1 258 ? 34.77884 11.31612 20.40032  1.000 50.18353  ? 258 HIS A ND1 1 
ATOM   2030 C CD2 . HIS A 1 258 ? 36.38556 10.94557 18.97167  1.000 49.81148  ? 258 HIS A CD2 1 
ATOM   2031 C CE1 . HIS A 1 258 ? 35.68443 10.57444 21.01441  1.000 51.20041  ? 258 HIS A CE1 1 
ATOM   2032 N NE2 . HIS A 1 258 ? 36.66919 10.33503 20.16817  1.000 51.27786  ? 258 HIS A NE2 1 
ATOM   2033 N N   . ASP A 1 259 ? 31.61718 11.69207 19.27381  1.000 47.21449  ? 259 ASP A N   1 
ATOM   2034 C CA  . ASP A 1 259 ? 30.89935 11.11314 20.39934  1.000 48.56577  ? 259 ASP A CA  1 
ATOM   2035 C C   . ASP A 1 259 ? 29.82629 10.13771 19.93177  1.000 47.84313  ? 259 ASP A C   1 
ATOM   2036 O O   . ASP A 1 259 ? 29.53618 9.15935  20.63001  1.000 48.14254  ? 259 ASP A O   1 
ATOM   2037 C CB  . ASP A 1 259 ? 30.30618 12.22959 21.26380  1.000 49.87165  ? 259 ASP A CB  1 
ATOM   2038 C CG  . ASP A 1 259 ? 31.37241 13.17291 21.82145  1.000 51.71427  ? 259 ASP A CG  1 
ATOM   2039 O OD1 . ASP A 1 259 ? 32.57141 12.81853 21.79760  1.000 52.32920  ? 259 ASP A OD1 1 
ATOM   2040 O OD2 . ASP A 1 259 ? 31.00681 14.26919 22.29637  1.000 52.75069  ? 259 ASP A OD2 1 
ATOM   2041 N N   . SER A 1 260 ? 29.26238 10.35675 18.73871  1.000 47.34710  ? 260 SER A N   1 
ATOM   2042 C CA  . SER A 1 260 ? 28.17267 9.51232  18.26017  1.000 46.11898  ? 260 SER A CA  1 
ATOM   2043 C C   . SER A 1 260 ? 28.65660 8.22189  17.59735  1.000 45.67527  ? 260 SER A C   1 
ATOM   2044 O O   . SER A 1 260 ? 27.90936 7.23932  17.56873  1.000 46.27363  ? 260 SER A O   1 
ATOM   2045 C CB  . SER A 1 260 ? 27.29111 10.28683 17.27730  1.000 44.90576  ? 260 SER A CB  1 
ATOM   2046 O OG  . SER A 1 260 ? 26.74164 11.44997 17.87009  1.000 45.20725  ? 260 SER A OG  1 
ATOM   2047 N N   . PHE A 1 261 ? 29.87289 8.17866  17.04949  1.000 45.13340  ? 261 PHE A N   1 
ATOM   2048 C CA  . PHE A 1 261 ? 30.26202 6.99612  16.28381  1.000 45.65500  ? 261 PHE A CA  1 
ATOM   2049 C C   . PHE A 1 261 ? 31.53605 6.29811  16.76804  1.000 49.07112  ? 261 PHE A C   1 
ATOM   2050 O O   . PHE A 1 261 ? 31.64667 5.08669  16.59568  1.000 49.62713  ? 261 PHE A O   1 
ATOM   2051 C CB  . PHE A 1 261 ? 30.38171 7.35310  14.78468  1.000 43.67598  ? 261 PHE A CB  1 
ATOM   2052 C CG  . PHE A 1 261 ? 29.09103 7.88377  14.17942  1.000 41.87748  ? 261 PHE A CG  1 
ATOM   2053 C CD1 . PHE A 1 261 ? 28.05059 7.02194  13.85076  1.000 40.90735  ? 261 PHE A CD1 1 
ATOM   2054 C CD2 . PHE A 1 261 ? 28.91757 9.24389  13.94784  1.000 41.18853  ? 261 PHE A CD2 1 
ATOM   2055 C CE1 . PHE A 1 261 ? 26.86187 7.50890  13.30294  1.000 40.24751  ? 261 PHE A CE1 1 
ATOM   2056 C CE2 . PHE A 1 261 ? 27.73482 9.73066  13.40162  1.000 40.87219  ? 261 PHE A CE2 1 
ATOM   2057 C CZ  . PHE A 1 261 ? 26.70904 8.86113  13.08057  1.000 40.26127  ? 261 PHE A CZ  1 
ATOM   2058 N N   . ILE A 1 262 ? 32.46777 6.99629  17.41666  1.000 52.50580  ? 262 ILE A N   1 
ATOM   2059 C CA  . ILE A 1 262 ? 33.76129 6.42129  17.80941  1.000 58.55521  ? 262 ILE A CA  1 
ATOM   2060 C C   . ILE A 1 262 ? 33.75109 5.95729  19.26400  1.000 65.92547  ? 262 ILE A C   1 
ATOM   2061 O O   . ILE A 1 262 ? 34.08252 4.81437  19.55790  1.000 67.25407  ? 262 ILE A O   1 
ATOM   2062 C CB  . ILE A 1 262 ? 34.91458 7.42325  17.55108  1.000 57.02476  ? 262 ILE A CB  1 
ATOM   2063 C CG1 . ILE A 1 262 ? 34.84091 7.93469  16.11827  1.000 55.61489  ? 262 ILE A CG1 1 
ATOM   2064 C CG2 . ILE A 1 262 ? 36.25130 6.75026  17.79343  1.000 58.71283  ? 262 ILE A CG2 1 
ATOM   2065 C CD1 . ILE A 1 262 ? 34.94427 6.83420  15.09087  1.000 54.20879  ? 262 ILE A CD1 1 
ATOM   2066 N N   . GLU A 1 263 ? 33.45685 6.84656  20.20010  1.000 70.85897  ? 263 GLU A N   1 
ATOM   2067 C CA  . GLU A 1 263 ? 33.58834 6.50999  21.61674  1.000 74.27546  ? 263 GLU A CA  1 
ATOM   2068 C C   . GLU A 1 263 ? 32.46705 7.15259  22.43310  1.000 74.68503  ? 263 GLU A C   1 
ATOM   2069 O O   . GLU A 1 263 ? 32.65258 8.19345  23.05838  1.000 76.40355  ? 263 GLU A O   1 
ATOM   2070 C CB  . GLU A 1 263 ? 34.97041 6.94644  22.13320  0.800 76.52075  ? 263 GLU A CB  1 
ATOM   2071 C CG  . GLU A 1 263 ? 35.32372 6.53705  23.57710  0.700 80.04106  ? 263 GLU A CG  1 
ATOM   2072 C CD  . GLU A 1 263 ? 35.34263 5.03151  23.81352  0.600 82.40709  ? 263 GLU A CD  1 
ATOM   2073 O OE1 . GLU A 1 263 ? 35.58776 4.26451  22.85866  0.600 82.15915  ? 263 GLU A OE1 1 
ATOM   2074 O OE2 . GLU A 1 263 ? 35.10792 4.61629  24.96926  0.600 84.53827  ? 263 GLU A OE2 1 
HETATM 2075 C C1  . CIT B 2 .   ? 31.76929 23.83989 14.28279  0.930 68.40162  ? 301 CIT A C1  1 
HETATM 2076 O O1  . CIT B 2 .   ? 31.58949 22.63033 14.01963  0.930 68.11350  ? 301 CIT A O1  1 
HETATM 2077 O O2  . CIT B 2 .   ? 32.92202 24.21707 14.57834  0.930 68.21890  ? 301 CIT A O2  1 
HETATM 2078 C C2  . CIT B 2 .   ? 30.64727 24.85658 14.24499  0.930 69.14039  ? 301 CIT A C2  1 
HETATM 2079 C C3  . CIT B 2 .   ? 29.52530 24.54400 15.23366  0.930 70.14105  ? 301 CIT A C3  1 
HETATM 2080 O O7  . CIT B 2 .   ? 30.04544 23.98524 16.46290  0.930 70.27095  ? 301 CIT A O7  1 
HETATM 2081 C C4  . CIT B 2 .   ? 28.65538 25.75436 15.55196  0.930 70.44993  ? 301 CIT A C4  1 
HETATM 2082 C C5  . CIT B 2 .   ? 29.16313 26.41096 16.81307  0.930 71.06127  ? 301 CIT A C5  1 
HETATM 2083 O O3  . CIT B 2 .   ? 29.65889 27.55625 16.76500  0.930 71.22280  ? 301 CIT A O3  1 
HETATM 2084 O O4  . CIT B 2 .   ? 29.09485 25.82285 17.91513  0.930 71.15792  ? 301 CIT A O4  1 
HETATM 2085 C C6  . CIT B 2 .   ? 28.67102 23.47008 14.61723  0.930 70.45655  ? 301 CIT A C6  1 
HETATM 2086 O O5  . CIT B 2 .   ? 27.99392 23.71946 13.59945  0.930 70.47928  ? 301 CIT A O5  1 
HETATM 2087 O O6  . CIT B 2 .   ? 28.67048 22.32860 15.12055  0.930 70.55673  ? 301 CIT A O6  1 
HETATM 2088 C C4  . UYP C 3 .   ? 20.86838 11.60423 12.94882  1.000 48.44165  ? 302 UYP A C4  1 
HETATM 2089 C C5  . UYP C 3 .   ? 20.53548 12.72182 12.19468  1.000 48.00929  ? 302 UYP A C5  1 
HETATM 2090 C C6  . UYP C 3 .   ? 21.53564 13.56122 11.71925  1.000 47.16805  ? 302 UYP A C6  1 
HETATM 2091 C C8  . UYP C 3 .   ? 18.75214 11.68155 12.73955  1.000 48.34504  ? 302 UYP A C8  1 
HETATM 2092 N N1  . UYP C 3 .   ? 22.79921 13.25486 12.01450  1.000 47.29703  ? 302 UYP A N1  1 
HETATM 2093 N N3  . UYP C 3 .   ? 22.14711 11.35904 13.20487  1.000 48.43945  ? 302 UYP A N3  1 
HETATM 2094 C C2  . UYP C 3 .   ? 23.06082 12.16725 12.71769  1.000 47.90953  ? 302 UYP A C2  1 
HETATM 2095 C CAA . UYP C 3 .   ? 13.13445 9.03551  12.44794  1.000 48.65815  ? 302 UYP A CAA 1 
HETATM 2096 C CAC . UYP C 3 .   ? 14.83637 10.69351 13.08549  1.000 48.80497  ? 302 UYP A CAC 1 
HETATM 2097 C CAD . UYP C 3 .   ? 16.22989 11.07218 12.94446  1.000 48.95111  ? 302 UYP A CAD 1 
HETATM 2098 C CAE . UYP C 3 .   ? 17.37425 11.35970 12.84792  1.000 48.55118  ? 302 UYP A CAE 1 
HETATM 2099 C CAP . UYP C 3 .   ? 19.56357 9.70861  14.12335  1.000 49.20835  ? 302 UYP A CAP 1 
HETATM 2100 C CAR . UYP C 3 .   ? 18.37662 7.70218  14.59236  1.000 50.27224  ? 302 UYP A CAR 1 
HETATM 2101 C CAS . UYP C 3 .   ? 16.94635 8.17375  14.41748  1.000 50.98744  ? 302 UYP A CAS 1 
HETATM 2102 C CAU . UYP C 3 .   ? 16.44747 6.36322  12.71535  1.000 52.80586  ? 302 UYP A CAU 1 
HETATM 2103 C CAX . UYP C 3 .   ? 15.72891 4.93328  10.91342  1.000 54.07888  ? 302 UYP A CAX 1 
HETATM 2104 C CAY . UYP C 3 .   ? 14.94715 4.85380  9.77256   1.000 54.51456  ? 302 UYP A CAY 1 
HETATM 2105 C CAZ . UYP C 3 .   ? 14.91470 3.69532  9.00991   1.000 54.68030  ? 302 UYP A CAZ 1 
HETATM 2106 C CBA . UYP C 3 .   ? 15.75190 2.62972  9.31802   1.000 55.00929  ? 302 UYP A CBA 1 
HETATM 2107 C CBB . UYP C 3 .   ? 16.59858 2.72724  10.41313  1.000 54.68431  ? 302 UYP A CBB 1 
HETATM 2108 C CBC . UYP C 3 .   ? 16.60750 3.87786  11.18155  1.000 54.55066  ? 302 UYP A CBC 1 
HETATM 2109 C CBD . UYP C 3 .   ? 18.82401 8.41772  15.87784  1.000 49.77153  ? 302 UYP A CBD 1 
HETATM 2110 C CBF . UYP C 3 .   ? 18.75161 9.86829  15.40401  1.000 49.41088  ? 302 UYP A CBF 1 
HETATM 2111 C CBH . UYP C 3 .   ? 14.43895 9.93000  10.63591  1.000 49.04717  ? 302 UYP A CBH 1 
HETATM 2112 C CBI . UYP C 3 .   ? 15.77335 9.83171  9.88995   1.000 49.65819  ? 302 UYP A CBI 1 
HETATM 2113 C CBK . UYP C 3 .   ? 17.29254 8.46828  8.84788   1.000 49.88784  ? 302 UYP A CBK 1 
HETATM 2114 C CBL . UYP C 3 .   ? 17.00982 9.75911  8.06738   1.000 49.75397  ? 302 UYP A CBL 1 
HETATM 2115 C CBN . UYP C 3 .   ? 15.56812 10.06390 8.39854   1.000 49.12274  ? 302 UYP A CBN 1 
HETATM 2116 C CBQ . UYP C 3 .   ? 16.17206 6.71675  7.40799   1.000 49.72127  ? 302 UYP A CBQ 1 
HETATM 2117 C CBS . UYP C 3 .   ? 17.75816 5.24044  7.56864   1.000 49.75198  ? 302 UYP A CBS 1 
HETATM 2118 C CBT . UYP C 3 .   ? 18.10169 6.34289  8.30577   1.000 49.76781  ? 302 UYP A CBT 1 
HETATM 2119 C CBV . UYP C 3 .   ? 20.09419 5.37567  8.94044   1.000 49.32678  ? 302 UYP A CBV 1 
HETATM 2120 C CBX . UYP C 3 .   ? 18.65827 4.18410  7.54978   1.000 49.31589  ? 302 UYP A CBX 1 
HETATM 2121 N N6  . UYP C 3 .   ? 21.26676 14.64419 10.98990  1.000 46.94752  ? 302 UYP A N6  1 
HETATM 2122 N N7  . UYP C 3 .   ? 19.22184 12.73771 12.08419  1.000 48.48679  ? 302 UYP A N7  1 
HETATM 2123 N N9  . UYP C 3 .   ? 19.74821 10.96867 13.26551  1.000 48.44243  ? 302 UYP A N9  1 
HETATM 2124 N NAB . UYP C 3 .   ? 14.43043 9.65217  12.10226  1.000 48.87343  ? 302 UYP A NAB 1 
HETATM 2125 N NAT . UYP C 3 .   ? 16.29308 7.61777  13.18750  1.000 52.10902  ? 302 UYP A NAT 1 
HETATM 2126 N NAW . UYP C 3 .   ? 15.75731 6.10249  11.59556  1.000 53.61419  ? 302 UYP A NAW 1 
HETATM 2127 N NBP . UYP C 3 .   ? 17.10692 7.19820  8.22572   1.000 50.31890  ? 302 UYP A NBP 1 
HETATM 2128 N NBR . UYP C 3 .   ? 16.56666 5.49396  7.02578   1.000 49.94585  ? 302 UYP A NBR 1 
HETATM 2129 N NBU . UYP C 3 .   ? 19.25957 6.39571  8.97713   1.000 49.65550  ? 302 UYP A NBU 1 
HETATM 2130 N NBW . UYP C 3 .   ? 19.80773 4.28746  8.24149   1.000 49.10209  ? 302 UYP A NBW 1 
HETATM 2131 N NBY . UYP C 3 .   ? 18.39616 3.08011  6.85798   1.000 48.82908  ? 302 UYP A NBY 1 
HETATM 2132 O OAQ . UYP C 3 .   ? 19.03110 8.46084  13.51911  1.000 50.17333  ? 302 UYP A OAQ 1 
HETATM 2133 O OAV . UYP C 3 .   ? 16.90833 5.46288  13.42178  1.000 52.62086  ? 302 UYP A OAV 1 
HETATM 2134 O OBE . UYP C 3 .   ? 20.10546 8.01636  16.39128  1.000 50.28339  ? 302 UYP A OBE 1 
HETATM 2135 O OBG . UYP C 3 .   ? 19.51355 10.69054 16.29393  1.000 49.12938  ? 302 UYP A OBG 1 
HETATM 2136 O OBJ . UYP C 3 .   ? 16.09679 8.44996  9.72014   1.000 49.76571  ? 302 UYP A OBJ 1 
HETATM 2137 O OBM . UYP C 3 .   ? 18.00606 10.77198 8.16123   1.000 50.31808  ? 302 UYP A OBM 1 
HETATM 2138 O OBO . UYP C 3 .   ? 15.41701 11.47066 8.20062   1.000 47.61384  ? 302 UYP A OBO 1 
HETATM 2139 O O   . HOH D 4 .   ? 24.29666 7.90280  -8.99783  1.000 27.64552  ? 401 HOH A O   1 
HETATM 2140 O O   . HOH D 4 .   ? 22.90402 11.12947 0.51502   1.000 35.86110  ? 402 HOH A O   1 
HETATM 2141 O O   . HOH D 4 .   ? 29.34764 6.77010  4.87832   1.000 32.43863  ? 403 HOH A O   1 
HETATM 2142 O O   . HOH D 4 .   ? 20.12222 26.63657 2.70817   1.000 41.40888  ? 404 HOH A O   1 
HETATM 2143 O O   . HOH D 4 .   ? 9.46159  16.50496 6.25280   1.000 51.63583  ? 405 HOH A O   1 
HETATM 2144 O O   . HOH D 4 .   ? 20.74106 11.50027 5.02930   1.000 44.16285  ? 406 HOH A O   1 
HETATM 2145 O O   . HOH D 4 .   ? 13.77177 11.06905 4.43906   1.000 41.90589  ? 407 HOH A O   1 
HETATM 2146 O O   . HOH D 4 .   ? 32.24554 25.64821 18.47354  1.000 59.04221  ? 408 HOH A O   1 
HETATM 2147 O O   . HOH D 4 .   ? 13.35907 19.19020 0.60417   1.000 53.98044  ? 409 HOH A O   1 
HETATM 2148 O O   . HOH D 4 .   ? 12.30545 1.63832  -5.37287  1.000 49.60808  ? 410 HOH A O   1 
HETATM 2149 O O   . HOH D 4 .   ? 25.60647 9.25970  -6.62826  1.000 35.67720  ? 411 HOH A O   1 
HETATM 2150 O O   . HOH D 4 .   ? 24.66798 1.26778  -5.84199  1.000 40.20990  ? 412 HOH A O   1 
HETATM 2151 O O   . HOH D 4 .   ? 26.26010 6.78277  -3.61781  1.000 36.30632  ? 413 HOH A O   1 
HETATM 2152 O O   . HOH D 4 .   ? 22.62894 20.96046 6.90775   1.000 48.76575  ? 414 HOH A O   1 
HETATM 2153 O O   . HOH D 4 .   ? 15.38994 28.32504 12.18563  1.000 48.15860  ? 415 HOH A O   1 
HETATM 2154 O O   . HOH D 4 .   ? 31.55350 5.23322  0.00000   0.50  49.52154  ? 416 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 23.42363 7.30732  11.18102  1.000 45.64718  ? 417 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 15.03424 16.85708 20.68716  1.000 56.37304  ? 418 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 32.28552 15.97362 24.32634  1.000 52.59113  ? 419 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 15.58708 38.46608 7.44967   1.000 69.13304  ? 420 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 20.57210 8.19977  11.01009  1.000 48.55559  ? 421 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 31.12626 4.63791  12.18002  1.000 63.12141  ? 422 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 12.96461 11.42756 18.67880  1.000 41.04434  ? 423 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 29.587   3.630    14.573    1.000 64.34913  ? 424 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 19.53649 27.65070 -8.86113  1.000 57.32224  ? 425 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 24.02452 0.16896  -1.90679  1.000 46.37261  ? 426 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? -0.96177 12.63351 -6.68479  1.000 64.57984  ? 427 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 24.01237 22.99238 16.59614  1.000 52.76211  ? 428 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 15.81276 28.52236 -3.71180  1.000 61.63412  ? 429 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 0.26198  14.02674 -2.85525  1.000 63.00325  ? 430 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 32.000   4.547    -4.286    1.000 45.01737  ? 431 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 1.74690 1.26392 1.18735 0.06940  0.05909  -0.31429 1   MET A N   
2    C CA  . MET A 1   ? 1.77727 1.22516 1.18618 0.08212  0.04532  -0.28697 1   MET A CA  
3    C C   . MET A 1   ? 1.68330 1.20087 1.13247 0.10367  0.02393  -0.26327 1   MET A C   
4    O O   . MET A 1   ? 1.60430 1.21172 1.09699 0.09320  0.02460  -0.26214 1   MET A O   
5    C CB  . MET A 1   ? 1.82206 1.21486 1.18894 0.04136  0.05729  -0.28081 1   MET A CB  
6    C CG  . MET A 1   ? 1.76469 1.23682 1.15831 0.00442  0.06584  -0.28561 1   MET A CG  
7    S SD  . MET A 1   ? 1.82890 1.23607 1.17282 -0.04646 0.08635  -0.29024 1   MET A SD  
8    C CE  . MET A 1   ? 1.85627 1.27405 1.20306 -0.07657 0.11183  -0.33472 1   MET A CE  
9    N N   . LYS A 2   ? 1.66537 1.14071 1.09879 0.13430  0.00533  -0.24515 2   LYS A N   
10   C CA  . LYS A 2   ? 1.56371 1.10717 1.03955 0.15528  -0.01533 -0.22863 2   LYS A CA  
11   C C   . LYS A 2   ? 1.46479 1.06184 0.96169 0.12336  -0.01393 -0.21661 2   LYS A C   
12   O O   . LYS A 2   ? 1.48582 1.04811 0.95108 0.09198  -0.00395 -0.21380 2   LYS A O   
13   C CB  . LYS A 2   ? 1.60568 1.09312 1.05298 0.18929  -0.03663 -0.21270 2   LYS A CB  
14   C CG  . LYS A 2   ? 1.66080 1.11573 1.10079 0.23173  -0.04216 -0.22438 2   LYS A CG  
15   C CD  . LYS A 2   ? 1.71036 1.11307 1.11878 0.27118  -0.06519 -0.20839 2   LYS A CD  
16   C CE  . LYS A 2   ? 1.75258 1.12468 1.15487 0.31872  -0.07112 -0.22166 2   LYS A CE  
17   N NZ  . LYS A 2   ? 1.80275 1.12473 1.16956 0.36308  -0.09601 -0.20483 2   LYS A NZ  
18   N N   . TYR A 3   ? 1.36020 1.04286 0.91189 0.13109  -0.02209 -0.21095 3   TYR A N   
19   C CA  . TYR A 3   ? 1.25586 0.99264 0.83260 0.10408  -0.01846 -0.20140 3   TYR A CA  
20   C C   . TYR A 3   ? 1.17526 0.97993 0.80467 0.11930  -0.03161 -0.19113 3   TYR A C   
21   O O   . TYR A 3   ? 1.17027 1.00253 0.82641 0.14631  -0.03836 -0.19641 3   TYR A O   
22   C CB  . TYR A 3   ? 1.21628 0.99430 0.80355 0.08073  0.00188  -0.21432 3   TYR A CB  
23   C CG  . TYR A 3   ? 1.16207 1.02032 0.79655 0.09309  0.00683  -0.21930 3   TYR A CG  
24   C CD1 . TYR A 3   ? 1.18595 1.04828 0.82347 0.11209  0.01221  -0.23734 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 1.09830 1.02516 0.77115 0.08545  0.00821  -0.20585 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 1.14883 1.08860 0.82656 0.12246  0.01889  -0.24174 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 1.07026 1.06684 0.78059 0.09511  0.01585  -0.20691 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 1.09269 1.09910 0.80517 0.11300  0.02141  -0.22497 3   TYR A CZ  
29   O OH  . TYR A 3   ? 1.06695 1.14660 0.81383 0.12192  0.03106  -0.22612 3   TYR A OH  
30   N N   . MET A 4   ? 1.11312 0.94419 0.75816 0.10081  -0.03415 -0.17857 4   MET A N   
31   C CA  . MET A 4   ? 1.05067 0.94656 0.74896 0.10593  -0.04127 -0.17039 4   MET A CA  
32   C C   . MET A 4   ? 1.00323 0.92777 0.71564 0.07937  -0.03268 -0.16048 4   MET A C   
33   O O   . MET A 4   ? 1.01888 0.91256 0.69921 0.06043  -0.02745 -0.15978 4   MET A O   
34   C CB  . MET A 4   ? 1.06677 0.95194 0.77056 0.12464  -0.06411 -0.16628 4   MET A CB  
35   C CG  . MET A 4   ? 1.05749 0.92441 0.74871 0.10833  -0.07324 -0.15658 4   MET A CG  
36   S SD  . MET A 4   ? 0.99457 0.92856 0.74471 0.09000  -0.07132 -0.14952 4   MET A SD  
37   C CE  . MET A 4   ? 0.98103 0.97684 0.78935 0.11233  -0.07955 -0.15640 4   MET A CE  
38   N N   . ILE A 5   ? 0.95558 0.93869 0.71662 0.07880  -0.03044 -0.15319 5   ILE A N   
39   C CA  . ILE A 5   ? 0.92919 0.94279 0.70756 0.05962  -0.01930 -0.14215 5   ILE A CA  
40   C C   . ILE A 5   ? 0.91791 0.96160 0.74034 0.05766  -0.02528 -0.13303 5   ILE A C   
41   O O   . ILE A 5   ? 0.92174 1.00121 0.78046 0.06847  -0.02671 -0.13514 5   ILE A O   
42   C CB  . ILE A 5   ? 0.90947 0.96595 0.69760 0.05877  -0.00034 -0.14199 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.93116 0.96493 0.68101 0.05891  0.00661  -0.15771 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.88729 0.96882 0.68513 0.04447  0.01014  -0.12779 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.91459 0.99845 0.67269 0.06008  0.02333  -0.16117 5   ILE A CD1 
46   N N   . THR A 6   ? 0.91533 0.94695 0.73669 0.04244  -0.02731 -0.12558 6   THR A N   
47   C CA  . THR A 6   ? 0.90500 0.95209 0.76327 0.03590  -0.03367 -0.12092 6   THR A CA  
48   C C   . THR A 6   ? 0.87700 0.94654 0.75691 0.02273  -0.01647 -0.10656 6   THR A C   
49   O O   . THR A 6   ? 0.86717 0.93054 0.72224 0.01885  -0.00621 -0.10102 6   THR A O   
50   C CB  . THR A 6   ? 0.93405 0.94224 0.76940 0.03084  -0.05034 -0.12582 6   THR A CB  
51   O OG1 . THR A 6   ? 0.97657 0.95501 0.78049 0.04597  -0.06519 -0.13478 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.92775 0.95250 0.80230 0.02291  -0.05820 -0.12696 6   THR A CG2 
53   N N   . SER A 7   ? 0.85376 0.94865 0.77879 0.01598  -0.01269 -0.10105 7   SER A N   
54   C CA  . SER A 7   ? 0.84634 0.95135 0.78292 0.00640  0.00638  -0.08338 7   SER A CA  
55   C C   . SER A 7   ? 0.85436 0.94545 0.81672 -0.00818 0.00485  -0.08044 7   SER A C   
56   O O   . SER A 7   ? 0.85991 0.95798 0.85187 -0.01350 -0.00602 -0.09220 7   SER A O   
57   C CB  . SER A 7   ? 0.84315 0.99076 0.80165 0.01047  0.02475  -0.07365 7   SER A CB  
58   O OG  . SER A 7   ? 0.86029 1.01456 0.83259 0.00166  0.04401  -0.05271 7   SER A OG  
59   N N   . LYS A 8   ? 0.86706 0.93992 0.81762 -0.01290 0.01508  -0.06718 8   LYS A N   
60   C CA  . LYS A 8   ? 0.86278 0.91795 0.83932 -0.02633 0.01924  -0.06237 8   LYS A CA  
61   C C   . LYS A 8   ? 0.86891 0.94839 0.89273 -0.03767 0.03336  -0.05554 8   LYS A C   
62   O O   . LYS A 8   ? 0.87226 0.94301 0.92960 -0.05368 0.03236  -0.06257 8   LYS A O   
63   C CB  . LYS A 8   ? 0.86044 0.89457 0.81491 -0.02257 0.03102  -0.04589 8   LYS A CB  
64   C CG  . LYS A 8   ? 0.87678 0.88141 0.85403 -0.03369 0.03868  -0.03884 8   LYS A CG  
65   C CD  . LYS A 8   ? 0.89984 0.89279 0.86120 -0.02334 0.05788  -0.01256 8   LYS A CD  
66   C CE  . LYS A 8   ? 0.93443 0.88377 0.89704 -0.02524 0.05885  -0.01135 8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.93021 0.86981 0.87123 -0.02201 0.03858  -0.03464 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.87621 0.98944 0.90458 -0.03162 0.04763  -0.04482 9   GLY A N   
69   C CA  . GLY A 9   ? 0.90348 1.04863 0.97717 -0.04388 0.06268  -0.04103 9   GLY A CA  
70   C C   . GLY A 9   ? 0.95479 1.09016 1.03869 -0.05500 0.09116  -0.01361 9   GLY A C   
71   O O   . GLY A 9   ? 0.97431 1.13411 1.09684 -0.07060 0.10857  -0.00908 9   GLY A O   
72   N N   . ASP A 10  ? 0.98872 1.08888 1.03900 -0.04716 0.09726  0.00472  10  ASP A N   
73   C CA  . ASP A 10  ? 1.03938 1.13019 1.08471 -0.04806 0.12532  0.03692  10  ASP A CA  
74   C C   . ASP A 10  ? 1.04183 1.17491 1.06350 -0.03121 0.13653  0.05020  10  ASP A C   
75   O O   . ASP A 10  ? 1.01005 1.17299 1.01901 -0.01938 0.12233  0.03248  10  ASP A O   
76   C CB  . ASP A 10  ? 1.06198 1.10279 1.07852 -0.03919 0.12628  0.05142  10  ASP A CB  
77   C CG  . ASP A 10  ? 1.03894 1.08652 1.00963 -0.01485 0.11133  0.04701  10  ASP A CG  
78   O OD1 . ASP A 10  ? 1.00600 1.08534 0.96701 -0.00891 0.09810  0.02922  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 1.05930 1.08024 1.00433 -0.00161 0.11355  0.05992  10  ASP A OD2 
80   N N   . GLU A 11  ? 1.09992 1.23199 1.11241 -0.02951 0.16317  0.08179  11  GLU A N   
81   C CA  . GLU A 11  ? 1.09781 1.27667 1.09050 -0.01540 0.17710  0.09463  11  GLU A CA  
82   C C   . GLU A 11  ? 1.05890 1.25354 1.00659 0.01048  0.16149  0.08675  11  GLU A C   
83   O O   . GLU A 11  ? 1.03217 1.26985 0.97280 0.01926  0.15716  0.07204  11  GLU A O   
84   C CB  . GLU A 11  ? 1.16673 1.33295 1.14896 -0.01673 0.20900  0.13423  11  GLU A CB  
85   C CG  . GLU A 11  ? 1.18983 1.40839 1.15811 -0.00759 0.22843  0.14877  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.26894 1.46931 1.23695 -0.01855 0.26370  0.18746  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.30998 1.45122 1.28990 -0.03338 0.27115  0.20011  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.30333 1.54500 1.25772 -0.01318 0.28524  0.20482  11  GLU A OE2 
89   N N   . LYS A 12  ? 1.04272 1.20480 0.96141 0.02248  0.15392  0.09388  12  LYS A N   
90   C CA  . LYS A 12  ? 1.00503 1.18805 0.88319 0.04457  0.14186  0.08549  12  LYS A CA  
91   C C   . LYS A 12  ? 0.94224 1.14161 0.82207 0.04128  0.12084  0.04971  12  LYS A C   
92   O O   . LYS A 12  ? 0.93719 1.17248 0.79513 0.05272  0.11836  0.03836  12  LYS A O   
93   C CB  . LYS A 12  ? 1.03266 1.17936 0.88926 0.05568  0.13504  0.09305  12  LYS A CB  
94   C CG  . LYS A 12  ? 1.03384 1.20846 0.85106 0.07830  0.12411  0.08389  12  LYS A CG  
95   C CD  . LYS A 12  ? 1.05591 1.19628 0.86030 0.08904  0.11666  0.08777  12  LYS A CD  
96   C CE  . LYS A 12  ? 1.04404 1.21888 0.81564 0.10996  0.10493  0.07386  12  LYS A CE  
97   N NZ  . LYS A 12  ? 1.02500 1.26058 0.77717 0.11797  0.10401  0.06091  12  LYS A NZ  
98   N N   . SER A 13  ? 0.90288 1.07427 0.80662 0.02606  0.10629  0.03139  13  SER A N   
99   C CA  . SER A 13  ? 0.85838 1.03001 0.75656 0.02460  0.08587  0.00123  13  SER A CA  
100  C C   . SER A 13  ? 0.83598 1.03794 0.75229 0.02410  0.08603  -0.01149 13  SER A C   
101  O O   . SER A 13  ? 0.82469 1.03260 0.72382 0.03060  0.07498  -0.03200 13  SER A O   
102  C CB  . SER A 13  ? 0.85391 0.98510 0.76489 0.01236  0.06941  -0.01178 13  SER A CB  
103  O OG  . SER A 13  ? 0.86685 0.97034 0.76158 0.01451  0.06787  -0.00502 13  SER A OG  
104  N N   . ASP A 14  ? 0.83393 1.05315 0.78596 0.01579  0.09876  -0.00195 14  ASP A N   
105  C CA  . ASP A 14  ? 0.82346 1.08070 0.79526 0.01888  0.09955  -0.01603 14  ASP A CA  
106  C C   . ASP A 14  ? 0.82950 1.12444 0.77555 0.03427  0.11072  -0.01435 14  ASP A C   
107  O O   . ASP A 14  ? 0.81705 1.12992 0.75828 0.04395  0.10317  -0.03578 14  ASP A O   
108  C CB  . ASP A 14  ? 0.81634 1.09393 0.83593 0.00381  0.11375  -0.00825 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.80468 1.06390 0.85735 -0.00912 0.09665  -0.02547 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.78704 1.01863 0.82136 -0.00296 0.07322  -0.04231 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.80961 1.08425 0.90563 -0.02644 0.10753  -0.02312 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.85106 1.15682 0.77789 0.03874  0.12831  0.01025  15  LEU A N   
113  C CA  . LEU A 15  ? 0.86311 1.21082 0.76161 0.05464  0.13838  0.01119  15  LEU A CA  
114  C C   . LEU A 15  ? 0.83277 1.17571 0.69967 0.06379  0.12127  -0.01433 15  LEU A C   
115  O O   . LEU A 15  ? 0.82496 1.19531 0.68326 0.07200  0.12032  -0.03477 15  LEU A O   
116  C CB  . LEU A 15  ? 0.91032 1.26434 0.78630 0.06162  0.15649  0.04426  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.95308 1.33948 0.83806 0.06077  0.18402  0.07007  15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.97354 1.38921 0.81346 0.08187  0.19479  0.08831  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.94397 1.37235 0.85706 0.05703  0.18824  0.05006  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.82059 1.12976 0.66938 0.06161  0.11000  -0.01431 16  LEU A N   
121  C CA  . LEU A 16  ? 0.80646 1.10974 0.62666 0.06443  0.09661  -0.03920 16  LEU A CA  
122  C C   . LEU A 16  ? 0.78847 1.07193 0.61514 0.05968  0.08392  -0.06617 16  LEU A C   
123  O O   . LEU A 16  ? 0.79726 1.08432 0.60194 0.06256  0.07989  -0.08924 16  LEU A O   
124  C CB  . LEU A 16  ? 0.81715 1.08837 0.62435 0.06026  0.08768  -0.03516 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.82475 1.08692 0.60554 0.05676  0.07573  -0.06125 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.83698 1.14304 0.59710 0.06453  0.08111  -0.07826 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.82826 1.08079 0.59739 0.05806  0.07246  -0.05339 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.77039 1.03344 0.62658 0.05350  0.07804  -0.06450 17  ARG A N   
129  C CA  . ARG A 17  ? 0.76311 1.00662 0.62260 0.05544  0.06442  -0.08727 17  ARG A CA  
130  C C   . ARG A 17  ? 0.76451 1.04470 0.62849 0.06813  0.07199  -0.10009 17  ARG A C   
131  O O   . ARG A 17  ? 0.73280 0.99717 0.57747 0.07473  0.06478  -0.12275 17  ARG A O   
132  C CB  . ARG A 17  ? 0.74952 0.97376 0.64095 0.04907  0.05436  -0.08416 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.75259 0.96566 0.64868 0.05853  0.04015  -0.10467 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.74990 0.94388 0.66980 0.05385  0.02475  -0.10604 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.75838 0.95007 0.68296 0.07002  0.01065  -0.12414 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.75289 0.98891 0.71416 0.08006  0.01340  -0.13042 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.73691 1.02168 0.73385 0.07091  0.03205  -0.11913 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.76652 0.99773 0.72728 0.10074  -0.00177 -0.14809 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.75729 1.08389 0.64529 0.07120  0.08830  -0.08635 18  LEU A N   
140  C CA  . LEU A 18  ? 0.75423 1.12282 0.64844 0.08429  0.09690  -0.10030 18  LEU A CA  
141  C C   . LEU A 18  ? 0.75084 1.13558 0.60800 0.09199  0.10209  -0.11364 18  LEU A C   
142  O O   . LEU A 18  ? 0.74774 1.13695 0.59665 0.10223  0.09969  -0.13931 18  LEU A O   
143  C CB  . LEU A 18  ? 0.72943 1.14764 0.65637 0.08235  0.11669  -0.08133 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.72422 1.13836 0.69648 0.07148  0.11360  -0.07546 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.73227 1.19252 0.73448 0.06229  0.13908  -0.05433 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.72331 1.13662 0.71521 0.08282  0.09655  -0.10283 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.74498 1.13863 0.57947 0.08846  0.10825  -0.09940 19  ASN A N   
148  C CA  . ASN A 19  ? 0.75163 1.17012 0.55310 0.09476  0.11147  -0.11652 19  ASN A CA  
149  C C   . ASN A 19  ? 0.76035 1.13542 0.54091 0.08852  0.09731  -0.14667 19  ASN A C   
150  O O   . ASN A 19  ? 0.77063 1.16102 0.53283 0.09230  0.09986  -0.17315 19  ASN A O   
151  C CB  . ASN A 19  ? 0.75118 1.19330 0.53328 0.09630  0.11841  -0.09504 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.76668 1.25939 0.55287 0.10665  0.13799  -0.06849 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.78108 1.31159 0.57506 0.11382  0.14848  -0.07615 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.77098 1.26259 0.54907 0.10864  0.14425  -0.03675 19  ASN A ND2 
155  N N   . MET A 20  ? 0.76026 1.07986 0.54148 0.07763  0.08403  -0.14425 20  MET A N   
156  C CA  . MET A 20  ? 0.77938 1.05070 0.53664 0.06957  0.07391  -0.16964 20  MET A CA  
157  C C   . MET A 20  ? 0.80567 1.05455 0.56607 0.07961  0.07026  -0.18946 20  MET A C   
158  O O   . MET A 20  ? 0.83482 1.06713 0.57251 0.07899  0.07173  -0.21603 20  MET A O   
159  C CB  . MET A 20  ? 0.77998 1.00026 0.53282 0.05649  0.06202  -0.16009 20  MET A CB  
160  C CG  . MET A 20  ? 0.77183 1.00458 0.51025 0.04679  0.06403  -0.15355 20  MET A CG  
161  S SD  . MET A 20  ? 0.77282 0.94813 0.49711 0.02956  0.05201  -0.15369 20  MET A SD  
162  C CE  . MET A 20  ? 0.80387 0.93739 0.49433 0.01659  0.05121  -0.18628 20  MET A CE  
163  N N   . ILE A 21  ? 0.80355 1.05339 0.59326 0.08969  0.06600  -0.17895 21  ILE A N   
164  C CA  . ILE A 21  ? 0.83200 1.06798 0.62801 0.10622  0.06114  -0.19734 21  ILE A CA  
165  C C   . ILE A 21  ? 0.81168 1.08972 0.60327 0.11749  0.07419  -0.21760 21  ILE A C   
166  O O   . ILE A 21  ? 0.84388 1.09303 0.62000 0.12725  0.07181  -0.24335 21  ILE A O   
167  C CB  . ILE A 21  ? 0.82546 1.07812 0.66173 0.11562  0.05530  -0.18426 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.78410 0.98825 0.62025 0.10730  0.03864  -0.17330 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.80953 1.06969 0.65827 0.13923  0.05207  -0.20447 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.76735 0.99953 0.64780 0.10925  0.03426  -0.16068 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.92614 1.27022 0.72842 0.11769  0.08880  -0.20644 22  ALA A N   
172  C CA  . ALA A 22  ? 0.93111 1.32274 0.72603 0.12869  0.10149  -0.22715 22  ALA A CA  
173  C C   . ALA A 22  ? 0.94832 1.31764 0.70685 0.12031  0.10101  -0.25478 22  ALA A C   
174  O O   . ALA A 22  ? 0.96481 1.32628 0.71283 0.12854  0.10336  -0.28598 22  ALA A O   
175  C CB  . ALA A 22  ? 0.79072 1.25558 0.59567 0.13034  0.11790  -0.20538 22  ALA A CB  
176  N N   . GLY A 23  ? 0.91950 1.27922 0.66034 0.10321  0.09871  -0.24642 23  GLY A N   
177  C CA  . GLY A 23  ? 0.94902 1.29100 0.65976 0.08978  0.09900  -0.27547 23  GLY A CA  
178  C C   . GLY A 23  ? 0.96705 1.22815 0.66273 0.08440  0.09200  -0.29724 23  GLY A C   
179  O O   . GLY A 23  ? 1.00445 1.24968 0.68031 0.07877  0.09713  -0.33059 23  GLY A O   
180  N N   . PHE A 24  ? 0.95094 1.15794 0.65352 0.08641  0.08073  -0.27902 24  PHE A N   
181  C CA  . PHE A 24  ? 0.99233 1.11781 0.67540 0.08801  0.07381  -0.29432 24  PHE A CA  
182  C C   . PHE A 24  ? 1.02574 1.15123 0.71407 0.11158  0.07678  -0.31626 24  PHE A C   
183  O O   . PHE A 24  ? 1.08559 1.14917 0.74842 0.11241  0.07762  -0.34042 24  PHE A O   
184  C CB  . PHE A 24  ? 0.98629 1.06631 0.67546 0.09111  0.05920  -0.26918 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.98610 1.03191 0.65564 0.06703  0.05556  -0.25845 24  PHE A CG  
186  C CD1 . PHE A 24  ? 1.02473 1.02132 0.65843 0.04675  0.06083  -0.27769 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.94990 1.01422 0.63780 0.06286  0.04890  -0.23148 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 1.01833 0.99063 0.63533 0.02371  0.05938  -0.26965 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.94387 0.98023 0.61430 0.04273  0.04582  -0.22421 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.97449 0.96828 0.60968 0.02354  0.05112  -0.24311 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.99668 1.18851 0.71716 0.13074  0.08001  -0.30861 25  GLY A N   
192  C CA  . GLY A 25  ? 1.03399 1.23928 0.76250 0.15502  0.08432  -0.33264 25  GLY A CA  
193  C C   . GLY A 25  ? 1.07996 1.29958 0.78724 0.14960  0.09705  -0.36810 25  GLY A C   
194  O O   . GLY A 25  ? 1.13117 1.32899 0.83244 0.16622  0.09973  -0.39701 25  GLY A O   
195  N N   . GLU A 26  ? 1.27255 1.90890 0.95545 0.05996  0.06717  -0.50818 26  GLU A N   
196  C CA  . GLU A 26  ? 1.35317 1.96671 0.99958 0.03441  0.05843  -0.55659 26  GLU A CA  
197  C C   . GLU A 26  ? 1.41574 1.93104 1.06721 0.01245  0.05931  -0.58070 26  GLU A C   
198  O O   . GLU A 26  ? 1.48098 1.96665 1.10483 -0.01319 0.05096  -0.62379 26  GLU A O   
199  C CB  . GLU A 26  ? 1.31055 2.00594 0.96269 -0.00078 0.03308  -0.54849 26  GLU A CB  
200  C CG  . GLU A 26  ? 1.25238 2.04810 0.90476 0.01796  0.03261  -0.52039 26  GLU A CG  
201  C CD  . GLU A 26  ? 1.19119 1.99590 0.80296 0.05961  0.05223  -0.54045 26  GLU A CD  
202  O OE1 . GLU A 26  ? 1.28050 2.01943 0.85173 0.07115  0.06410  -0.58482 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 1.14818 2.02672 0.76906 0.08177  0.05718  -0.51036 26  GLU A OE2 
204  N N   . TYR A 27  ? 1.40606 1.87580 1.09361 0.01949  0.06756  -0.55249 27  TYR A N   
205  C CA  . TYR A 27  ? 1.49059 1.85701 1.18450 0.01856  0.08064  -0.56763 27  TYR A CA  
206  C C   . TYR A 27  ? 1.55426 1.89061 1.24287 0.07015  0.10816  -0.55593 27  TYR A C   
207  O O   . TYR A 27  ? 1.53137 1.92869 1.20865 0.09905  0.11345  -0.54328 27  TYR A O   
208  C CB  . TYR A 27  ? 1.40733 1.76098 1.14963 -0.01191 0.06794  -0.53601 27  TYR A CB  
209  C CG  . TYR A 27  ? 1.35990 1.77896 1.11339 -0.05634 0.03975  -0.53181 27  TYR A CG  
210  C CD1 . TYR A 27  ? 1.28040 1.79597 1.04378 -0.05633 0.02734  -0.50010 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 1.40474 1.79098 1.16097 -0.09807 0.02632  -0.55781 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 1.24968 1.82762 1.02311 -0.09299 0.00432  -0.49307 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 1.37286 1.82601 1.14080 -0.13694 0.00066  -0.55104 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 1.29346 1.84257 1.06908 -0.13250 -0.00932 -0.51779 27  TYR A CZ  
215  O OH  . TYR A 27  ? 1.25958 1.87747 1.04730 -0.16793 -0.03243 -0.50765 27  TYR A OH  
216  N N   . ASP A 28  ? 1.62598 1.87480 1.32465 0.08381  0.12666  -0.55691 28  ASP A N   
217  C CA  . ASP A 28  ? 1.66232 1.90224 1.36075 0.13485  0.15084  -0.53659 28  ASP A CA  
218  C C   . ASP A 28  ? 1.63183 1.85683 1.37581 0.13870  0.15139  -0.49192 28  ASP A C   
219  O O   . ASP A 28  ? 1.65563 1.80260 1.40829 0.15307  0.16960  -0.49066 28  ASP A O   
220  C CB  . ASP A 28  ? 1.76293 1.92439 1.42576 0.16461  0.17900  -0.57188 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.76097 1.92983 1.42418 0.22005  0.20366  -0.54669 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.67728 1.91258 1.37043 0.23109  0.19577  -0.50306 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 1.84406 1.95215 1.47787 0.25233  0.23114  -0.57019 28  ASP A OD2 
224  N N   . MET A 29  ? 1.56524 1.86563 1.33649 0.12704  0.13233  -0.45469 29  MET A N   
225  C CA  . MET A 29  ? 1.45375 1.75546 1.26255 0.13478  0.13106  -0.40972 29  MET A CA  
226  C C   . MET A 29  ? 1.36895 1.71458 1.17900 0.17684  0.14101  -0.38469 29  MET A C   
227  O O   . MET A 29  ? 1.32177 1.74762 1.13014 0.17836  0.13085  -0.37416 29  MET A O   
228  C CB  . MET A 29  ? 1.38945 1.74456 1.22448 0.09806  0.10566  -0.38447 29  MET A CB  
229  C CG  . MET A 29  ? 1.41356 1.72944 1.25910 0.05685  0.09518  -0.39742 29  MET A CG  
230  S SD  . MET A 29  ? 1.41117 1.65310 1.29163 0.05839  0.10420  -0.36854 29  MET A SD  
231  C CE  . MET A 29  ? 1.31067 1.62011 1.22222 0.03960  0.08332  -0.32067 29  MET A CE  
232  N N   . GLU A 30  ? 1.34428 1.64103 1.16025 0.21045  0.16078  -0.37262 30  GLU A N   
233  C CA  . GLU A 30  ? 1.28084 1.62086 1.10136 0.25057  0.16961  -0.34691 30  GLU A CA  
234  C C   . GLU A 30  ? 1.17501 1.57250 1.02698 0.24241  0.15070  -0.30465 30  GLU A C   
235  O O   . GLU A 30  ? 1.15233 1.51571 1.02418 0.23655  0.14783  -0.28425 30  GLU A O   
236  C CB  . GLU A 30  ? 1.31979 1.59068 1.13686 0.28984  0.19712  -0.34552 30  GLU A CB  
237  C CG  . GLU A 30  ? 1.27344 1.58790 1.10506 0.32742  0.20256  -0.31007 30  GLU A CG  
238  C CD  . GLU A 30  ? 1.30869 1.55781 1.13881 0.36702  0.23015  -0.30440 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.37288 1.53924 1.18794 0.36602  0.24777  -0.33174 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 1.27400 1.55521 1.11873 0.39854  0.23420  -0.27217 30  GLU A OE2 
241  N N   . TYR A 31  ? 1.11822 1.60084 0.97395 0.24247  0.13888  -0.29135 31  TYR A N   
242  C CA  . TYR A 31  ? 1.02158 1.55641 0.90490 0.23981  0.12363  -0.25244 31  TYR A CA  
243  C C   . TYR A 31  ? 1.02228 1.54776 0.91476 0.27903  0.13574  -0.23039 31  TYR A C   
244  O O   . TYR A 31  ? 1.03953 1.57984 0.92242 0.31263  0.15119  -0.23414 31  TYR A O   
245  C CB  . TYR A 31  ? 0.95708 1.58391 0.84542 0.23087  0.11035  -0.24275 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.87027 1.54660 0.78712 0.22047  0.09279  -0.20543 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.84759 1.55310 0.77928 0.24675  0.09390  -0.18052 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.82359 1.51794 0.75161 0.18404  0.07524  -0.19552 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.79386 1.54001 0.74865 0.23388  0.07637  -0.15047 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.77020 1.50139 0.72025 0.17426  0.06109  -0.16414 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.76005 1.51469 0.72234 0.19773  0.06095  -0.14359 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.71638 1.50274 0.69777 0.18440  0.04551  -0.11624 31  TYR A OH  
253  N N   . ASP A 32  ? 0.99817 1.50405 0.90861 0.27585  0.12858  -0.20541 32  ASP A N   
254  C CA  . ASP A 32  ? 1.01740 1.52143 0.93784 0.30988  0.13537  -0.18014 32  ASP A CA  
255  C C   . ASP A 32  ? 0.99692 1.52469 0.93583 0.29045  0.11403  -0.15178 32  ASP A C   
256  O O   . ASP A 32  ? 1.00230 1.48976 0.94400 0.26676  0.10834  -0.15058 32  ASP A O   
257  C CB  . ASP A 32  ? 1.05359 1.47164 0.96647 0.33280  0.15795  -0.18711 32  ASP A CB  
258  C CG  . ASP A 32  ? 1.05090 1.47026 0.97064 0.37522  0.16907  -0.16174 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.99665 1.47561 0.93005 0.37969  0.15357  -0.13570 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 1.10256 1.46204 1.01413 0.40397  0.19375  -0.16776 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.96294 1.55603 0.91450 0.29765  0.10178  -0.12950 33  ASP A N   
262  C CA  . ASP A 33  ? 0.92914 1.53392 0.89320 0.28021  0.08273  -0.10530 33  ASP A CA  
263  C C   . ASP A 33  ? 0.93863 1.52471 0.90533 0.30955  0.08553  -0.08415 33  ASP A C   
264  O O   . ASP A 33  ? 0.91415 1.51929 0.88775 0.30214  0.06909  -0.06343 33  ASP A O   
265  C CB  . ASP A 33  ? 0.88148 1.56477 0.85871 0.26001  0.06370  -0.09413 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.86375 1.60844 0.85208 0.28459  0.06216  -0.08084 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.89411 1.62734 0.87795 0.31998  0.07751  -0.08162 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.81902 1.62571 0.82297 0.26798  0.04609  -0.06773 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.98376 1.53169 0.94307 0.34361  0.10683  -0.08914 34  VAL A N   
270  C CA  . VAL A 34  ? 1.02551 1.55578 0.98597 0.37677  0.11294  -0.06804 34  VAL A CA  
271  C C   . VAL A 34  ? 1.07258 1.51731 1.02641 0.38154  0.12742  -0.06859 34  VAL A C   
272  O O   . VAL A 34  ? 1.07801 1.50467 1.03277 0.38697  0.12193  -0.04788 34  VAL A O   
273  C CB  . VAL A 34  ? 1.06635 1.62440 1.02709 0.41833  0.12911  -0.06538 34  VAL A CB  
274  C CG1 . VAL A 34  ? 1.10434 1.63298 1.06396 0.45699  0.14158  -0.04514 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 1.03576 1.68729 1.01036 0.41472  0.11144  -0.05431 34  VAL A CG2 
276  N N   . GLU A 35  ? 1.11539 1.50618 1.06227 0.37736  0.14552  -0.09263 35  GLU A N   
277  C CA  . GLU A 35  ? 1.14836 1.45697 1.09443 0.37512  0.15936  -0.09428 35  GLU A CA  
278  C C   . GLU A 35  ? 1.15148 1.43046 1.09696 0.33397  0.15598  -0.11884 35  GLU A C   
279  O O   . GLU A 35  ? 1.20223 1.42048 1.14396 0.33405  0.17394  -0.13817 35  GLU A O   
280  C CB  . GLU A 35  ? 1.22329 1.48009 1.16406 0.41549  0.18976  -0.09776 35  GLU A CB  
281  C CG  . GLU A 35  ? 1.24494 1.51251 1.18820 0.45929  0.19732  -0.06744 35  GLU A CG  
282  C CD  . GLU A 35  ? 1.32543 1.53589 1.26435 0.49993  0.23174  -0.06958 35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.36592 1.56648 1.29622 0.50675  0.24725  -0.09361 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.34959 1.52258 1.29213 0.52639  0.24503  -0.04693 35  GLU A OE2 
285  N N   . PRO A 36  ? 1.06756 1.38864 1.01752 0.29793  0.13315  -0.11757 36  PRO A N   
286  C CA  . PRO A 36  ? 1.04829 1.34705 0.99928 0.25944  0.12907  -0.13758 36  PRO A CA  
287  C C   . PRO A 36  ? 1.03205 1.25902 0.99181 0.25199  0.13799  -0.13035 36  PRO A C   
288  O O   . PRO A 36  ? 1.02951 1.23127 0.99422 0.27243  0.14347  -0.10496 36  PRO A O   
289  C CB  . PRO A 36  ? 0.98662 1.34962 0.94313 0.22924  0.10450  -0.12737 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.95727 1.35447 0.91712 0.24806  0.09571  -0.09962 36  PRO A CG  
291  C CD  . PRO A 36  ? 1.00615 1.39858 0.96089 0.28942  0.11101  -0.09969 36  PRO A CD  
292  N N   . GLU A 37  ? 1.01738 1.21280 0.97939 0.22282  0.13977  -0.15277 37  GLU A N   
293  C CA  . GLU A 37  ? 1.00076 1.13866 0.97772 0.20618  0.14466  -0.14425 37  GLU A CA  
294  C C   . GLU A 37  ? 0.93688 1.10662 0.92439 0.16637  0.12440  -0.13511 37  GLU A C   
295  O O   . GLU A 37  ? 0.93304 1.06881 0.93613 0.15392  0.12597  -0.11760 37  GLU A O   
296  C CB  . GLU A 37  ? 1.06252 1.13581 1.03918 0.19954  0.16185  -0.17439 37  GLU A CB  
297  C CG  . GLU A 37  ? 1.11249 1.14247 1.07916 0.24182  0.18748  -0.18129 37  GLU A CG  
298  C CD  . GLU A 37  ? 1.18569 1.15052 1.14650 0.23458  0.20521  -0.21729 37  GLU A CD  
299  O OE1 . GLU A 37  ? 1.19490 1.16107 1.15419 0.19554  0.19375  -0.24408 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 1.23851 1.15024 1.19518 0.26875  0.23114  -0.21885 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.92814 0.72214 0.80438 0.10549  0.07722  -0.19792 38  ILE A N   
302  C CA  . ILE A 38  ? 0.86991 0.71972 0.74863 0.07995  0.06955  -0.19513 38  ILE A CA  
303  C C   . ILE A 38  ? 0.81658 0.71623 0.70179 0.09702  0.06032  -0.18940 38  ILE A C   
304  O O   . ILE A 38  ? 0.78611 0.69387 0.67485 0.11068  0.06278  -0.20648 38  ILE A O   
305  C CB  . ILE A 38  ? 0.88302 0.74509 0.75825 0.04957  0.07446  -0.22382 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.93914 0.74330 0.80890 0.03043  0.08846  -0.23591 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.84420 0.76736 0.71926 0.02797  0.06411  -0.21960 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.93971 0.73095 0.80827 0.01478  0.08983  -0.21483 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.77877 0.70906 0.66640 0.09649  0.05210  -0.16715 39  VAL A N   
310  C CA  . VAL A 39  ? 0.74064 0.71123 0.63298 0.10936  0.04667  -0.16142 39  VAL A CA  
311  C C   . VAL A 39  ? 0.72256 0.73249 0.61004 0.09052  0.04129  -0.15506 39  VAL A C   
312  O O   . VAL A 39  ? 0.70227 0.71830 0.59108 0.08203  0.03683  -0.13911 39  VAL A O   
313  C CB  . VAL A 39  ? 0.71540 0.68299 0.61409 0.13224  0.04301  -0.14154 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.66764 0.67788 0.57053 0.13360  0.03899  -0.13300 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.73804 0.68542 0.64153 0.15980  0.04538  -0.15096 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.73426 0.77079 0.61440 0.08485  0.04231  -0.16762 40  ILE A N   
317  C CA  . ILE A 40  ? 0.72657 0.79703 0.59549 0.07157  0.03676  -0.15961 40  ILE A CA  
318  C C   . ILE A 40  ? 0.70808 0.79575 0.57480 0.08248  0.03781  -0.14701 40  ILE A C   
319  O O   . ILE A 40  ? 0.70111 0.79013 0.56937 0.09014  0.04514  -0.15817 40  ILE A O   
320  C CB  . ILE A 40  ? 0.74074 0.82691 0.59423 0.05455  0.03805  -0.18024 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.76904 0.83608 0.62639 0.03975  0.03976  -0.19736 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.72733 0.84917 0.56455 0.04635  0.02986  -0.16734 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.79872 0.86989 0.64514 0.02692  0.04584  -0.22734 40  ILE A CD1 
324  N N   . SER A 41  ? 0.70002 0.80145 0.56454 0.08238  0.03209  -0.12617 41  SER A N   
325  C CA  . SER A 41  ? 0.69447 0.80434 0.55596 0.09061  0.03536  -0.11302 41  SER A CA  
326  C C   . SER A 41  ? 0.71147 0.83802 0.55050 0.08392  0.03307  -0.10349 41  SER A C   
327  O O   . SER A 41  ? 0.71301 0.85345 0.54751 0.07885  0.02329  -0.09719 41  SER A O   
328  C CB  . SER A 41  ? 0.67712 0.78268 0.55377 0.10039  0.03230  -0.09582 41  SER A CB  
329  O OG  . SER A 41  ? 0.67277 0.78327 0.54746 0.10648  0.03790  -0.08703 41  SER A OG  
330  N N   . ILE A 42  ? 0.72652 0.85293 0.54995 0.08397  0.04261  -0.10268 42  ILE A N   
331  C CA  . ILE A 42  ? 0.76339 0.89794 0.55562 0.07890  0.04264  -0.09283 42  ILE A CA  
332  C C   . ILE A 42  ? 0.77762 0.89873 0.55906 0.08504  0.05223  -0.07536 42  ILE A C   
333  O O   . ILE A 42  ? 0.77997 0.89182 0.56086 0.08105  0.06740  -0.08445 42  ILE A O   
334  C CB  . ILE A 42  ? 0.78397 0.92497 0.55553 0.06656  0.04962  -0.11206 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.78420 0.93512 0.56442 0.05888  0.04136  -0.13115 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.82143 0.96784 0.55284 0.06279  0.05074  -0.09775 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.81291 0.97792 0.56697 0.04528  0.04506  -0.14871 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.78969 0.91069 0.56331 0.09428  0.04476  -0.05264 43  GLY A N   
339  C CA  . GLY A 43  ? 0.80476 0.90444 0.56603 0.10147  0.05520  -0.03503 43  GLY A CA  
340  C C   . GLY A 43  ? 0.79198 0.89321 0.56728 0.11684  0.04593  -0.01657 43  GLY A C   
341  O O   . GLY A 43  ? 0.81550 0.92655 0.57618 0.12692  0.03505  -0.00026 43  GLY A O   
342  N N   . GLY A 44  ? 0.75408 0.85058 0.55792 0.12011  0.04979  -0.02024 44  GLY A N   
343  C CA  . GLY A 44  ? 0.74596 0.84620 0.56645 0.13326  0.04376  -0.00673 44  GLY A CA  
344  C C   . GLY A 44  ? 0.72290 0.83436 0.57596 0.13163  0.04024  -0.01706 44  GLY A C   
345  O O   . GLY A 44  ? 0.72130 0.83367 0.58237 0.12373  0.04178  -0.03259 44  GLY A O   
346  N N   . ASP A 45  ? 0.71238 0.83194 0.58222 0.14101  0.03600  -0.00763 45  ASP A N   
347  C CA  . ASP A 45  ? 0.67322 0.80140 0.56800 0.13924  0.03415  -0.01409 45  ASP A CA  
348  C C   . ASP A 45  ? 0.64846 0.76459 0.54816 0.13670  0.04496  -0.02552 45  ASP A C   
349  O O   . ASP A 45  ? 0.62678 0.74691 0.53761 0.13485  0.04228  -0.03365 45  ASP A O   
350  C CB  . ASP A 45  ? 0.66405 0.80405 0.57437 0.14886  0.03204  -0.00378 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.65840 0.82643 0.57555 0.14996  0.01892  0.00153  45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.65493 0.83425 0.57303 0.13816  0.01171  -0.00631 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.65730 0.83804 0.58088 0.16285  0.01676  0.01138  45  ASP A OD2 
354  N N   . GLY A 46  ? 0.65225 0.75397 0.54286 0.13692  0.05787  -0.02667 46  GLY A N   
355  C CA  . GLY A 46  ? 0.64516 0.74606 0.54227 0.13188  0.06836  -0.04279 46  GLY A CA  
356  C C   . GLY A 46  ? 0.65100 0.75890 0.54738 0.12650  0.06557  -0.05730 46  GLY A C   
357  O O   . GLY A 46  ? 0.63898 0.75819 0.54946 0.12976  0.06318  -0.06845 46  GLY A O   
358  N N   . THR A 47  ? 0.67099 0.77303 0.54929 0.12026  0.06591  -0.05761 47  THR A N   
359  C CA  . THR A 47  ? 0.66575 0.77466 0.54421 0.11577  0.06389  -0.07366 47  THR A CA  
360  C C   . THR A 47  ? 0.64870 0.76171 0.54158 0.12179  0.05132  -0.07468 47  THR A C   
361  O O   . THR A 47  ? 0.64723 0.76324 0.55024 0.12638  0.05082  -0.08808 47  THR A O   
362  C CB  . THR A 47  ? 0.68835 0.79308 0.54246 0.10747  0.06437  -0.07250 47  THR A CB  
363  O OG1 . THR A 47  ? 0.71305 0.80409 0.54573 0.10275  0.07721  -0.06457 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.69339 0.80551 0.54838 0.10169  0.06716  -0.09424 47  THR A CG2 
365  N N   . PHE A 48  ? 0.64117 0.75379 0.53471 0.12250  0.04226  -0.06068 48  PHE A N   
366  C CA  . PHE A 48  ? 0.64788 0.75790 0.55127 0.12324  0.03423  -0.06081 48  PHE A CA  
367  C C   . PHE A 48  ? 0.64352 0.75135 0.55951 0.13294  0.03522  -0.05990 48  PHE A C   
368  O O   . PHE A 48  ? 0.64445 0.74191 0.56317 0.13786  0.03288  -0.06508 48  PHE A O   
369  C CB  . PHE A 48  ? 0.64480 0.76321 0.54911 0.11861  0.02679  -0.04886 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.65209 0.76439 0.56340 0.11258  0.02264  -0.05110 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.64931 0.75543 0.57002 0.11639  0.02375  -0.04375 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.66308 0.77275 0.56861 0.10112  0.01985  -0.06179 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.66252 0.75419 0.58448 0.10838  0.02359  -0.04428 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.67363 0.76975 0.58386 0.09203  0.01992  -0.06559 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.67598 0.75991 0.59329 0.09547  0.02258  -0.05554 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.65031 0.76632 0.57167 0.13701  0.03870  -0.05260 49  LEU A N   
377  C CA  . LEU A 49  ? 0.65676 0.77804 0.58692 0.14593  0.03952  -0.05342 49  LEU A CA  
378  C C   . LEU A 49  ? 0.66422 0.78984 0.59676 0.15343  0.04044  -0.06909 49  LEU A C   
379  O O   . LEU A 49  ? 0.66661 0.78881 0.60064 0.16453  0.03524  -0.06893 49  LEU A O   
380  C CB  . LEU A 49  ? 0.65055 0.78251 0.58557 0.14658  0.04657  -0.05093 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.65172 0.78963 0.59300 0.14876  0.04598  -0.03940 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.65939 0.79306 0.60059 0.14592  0.03861  -0.02851 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.65139 0.78843 0.59312 0.14729  0.05294  -0.03509 49  LEU A CD2 
384  N N   . SER A 50  ? 0.66536 0.79864 0.59686 0.14834  0.04775  -0.08261 50  SER A N   
385  C CA  . SER A 50  ? 0.66576 0.81286 0.60410 0.15506  0.04949  -0.10208 50  SER A CA  
386  C C   . SER A 50  ? 0.67382 0.80616 0.61000 0.16271  0.04250  -0.10539 50  SER A C   
387  O O   . SER A 50  ? 0.68138 0.82064 0.62498 0.17885  0.03876  -0.11468 50  SER A O   
388  C CB  . SER A 50  ? 0.67517 0.83201 0.61082 0.14248  0.06214  -0.11693 50  SER A CB  
389  O OG  . SER A 50  ? 0.67344 0.84274 0.61387 0.13667  0.07207  -0.12094 50  SER A OG  
390  N N   . ALA A 51  ? 0.67447 0.78735 0.60035 0.15243  0.04090  -0.09948 51  ALA A N   
391  C CA  . ALA A 51  ? 0.69026 0.78306 0.61359 0.15661  0.03710  -0.10518 51  ALA A CA  
392  C C   . ALA A 51  ? 0.68517 0.75809 0.60870 0.16919  0.03128  -0.09283 51  ALA A C   
393  O O   . ALA A 51  ? 0.69983 0.75763 0.62369 0.18493  0.02943  -0.09869 51  ALA A O   
394  C CB  . ALA A 51  ? 0.70436 0.78623 0.61669 0.13940  0.03682  -0.10399 51  ALA A CB  
395  N N   . PHE A 52  ? 0.66914 0.74086 0.59068 0.16396  0.02947  -0.07523 52  PHE A N   
396  C CA  . PHE A 52  ? 0.67448 0.72676 0.59088 0.17268  0.02658  -0.06102 52  PHE A CA  
397  C C   . PHE A 52  ? 0.66678 0.72993 0.58499 0.19621  0.02319  -0.06286 52  PHE A C   
398  O O   . PHE A 52  ? 0.68894 0.72732 0.59829 0.21266  0.02024  -0.05785 52  PHE A O   
399  C CB  . PHE A 52  ? 0.65445 0.71472 0.57108 0.16111  0.02726  -0.04562 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.67072 0.71938 0.57975 0.16867  0.02673  -0.03067 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.70623 0.71837 0.60286 0.16400  0.02907  -0.02140 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.65731 0.73012 0.56867 0.17816  0.02589  -0.02670 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.72987 0.72688 0.61296 0.16968  0.03081  -0.00504 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.67855 0.74304 0.57787 0.18487  0.02562  -0.01220 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.71736 0.74241 0.60066 0.18113  0.02821  0.00045  52  PHE A CZ  
406  N N   . HIS A 53  ? 0.64013 0.74030 0.56855 0.19870  0.02399  -0.07079 53  HIS A N   
407  C CA  . HIS A 53  ? 0.64483 0.76870 0.57725 0.22020  0.01921  -0.07608 53  HIS A CA  
408  C C   . HIS A 53  ? 0.66694 0.79681 0.60614 0.23778  0.01653  -0.09373 53  HIS A C   
409  O O   . HIS A 53  ? 0.69026 0.82707 0.62793 0.26375  0.00887  -0.09333 53  HIS A O   
410  C CB  . HIS A 53  ? 0.61357 0.77801 0.55715 0.21333  0.02330  -0.08514 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.60965 0.77296 0.54770 0.20559  0.02464  -0.06923 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.62396 0.78492 0.55086 0.21801  0.01894  -0.05526 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.59128 0.75425 0.53189 0.18828  0.03160  -0.06463 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.61459 0.77791 0.53977 0.20596  0.02342  -0.04545 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.59333 0.75830 0.52871 0.18954  0.03066  -0.05143 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.65922 0.78887 0.60477 0.22619  0.02250  -0.10942 54  GLN A N   
417  C CA  . GLN A 54  ? 0.69076 0.82653 0.64467 0.24276  0.02159  -0.12883 54  GLN A CA  
418  C C   . GLN A 54  ? 0.75145 0.84259 0.69349 0.26292  0.01622  -0.11861 54  GLN A C   
419  O O   . GLN A 54  ? 0.77455 0.87004 0.72322 0.28854  0.01267  -0.13103 54  GLN A O   
420  C CB  . GLN A 54  ? 0.67970 0.81893 0.63736 0.22301  0.03106  -0.14645 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.68397 0.85053 0.65723 0.23634  0.03372  -0.17439 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.68006 0.84052 0.65032 0.21741  0.04372  -0.19011 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.66727 0.81756 0.62465 0.19230  0.04915  -0.18217 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.69719 0.86590 0.67812 0.23150  0.04587  -0.21283 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.78531 0.83307 0.71007 0.25261  0.01690  -0.09708 55  TYR A N   
426  C CA  . TYR A 55  ? 0.84174 0.83473 0.75135 0.26547  0.01695  -0.08813 55  TYR A CA  
427  C C   . TYR A 55  ? 0.86249 0.82435 0.75140 0.26891  0.01519  -0.05986 55  TYR A C   
428  O O   . TYR A 55  ? 0.90273 0.80927 0.77434 0.26352  0.02082  -0.04839 55  TYR A O   
429  C CB  . TYR A 55  ? 0.86231 0.82478 0.76940 0.24194  0.02523  -0.09759 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.85861 0.84420 0.78012 0.24279  0.02841  -0.12586 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.89528 0.86878 0.82170 0.26967  0.02826  -0.14046 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.82616 0.84539 0.75451 0.21853  0.03251  -0.13755 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.89737 0.89698 0.83856 0.26960  0.03301  -0.16915 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.83153 0.87227 0.76913 0.21692  0.03788  -0.16337 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.86510 0.89875 0.81087 0.24119  0.03853  -0.18068 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.86741 0.92685 0.82406 0.23878  0.04562  -0.20915 55  TYR A OH  
437  N N   . GLU A 56  ? 0.84202 0.83787 0.73071 0.27647  0.00939  -0.05010 56  GLU A N   
438  C CA  . GLU A 56  ? 0.87291 0.84535 0.74036 0.27358  0.01003  -0.02402 56  GLU A CA  
439  C C   . GLU A 56  ? 0.94815 0.87616 0.78918 0.30301  0.00695  -0.00588 56  GLU A C   
440  O O   . GLU A 56  ? 0.97391 0.87352 0.79072 0.29894  0.01031  0.01778  56  GLU A O   
441  C CB  . GLU A 56  ? 0.82694 0.85095 0.70099 0.27067  0.00629  -0.02168 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.82033 0.88631 0.69822 0.30059  -0.00408 -0.02886 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.77222 0.88884 0.65705 0.29249  -0.00519 -0.03127 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.72613 0.85841 0.62564 0.26625  0.00237  -0.03955 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.78566 0.92527 0.65934 0.31350  -0.01337 -0.02500 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.99325 0.91311 0.83617 0.33365  0.00166  -0.01536 57  GLU A N   
447  C CA  . GLU A 57  ? 1.07513 0.93998 0.88839 0.36555  -0.00027 0.00469  57  GLU A CA  
448  C C   . GLU A 57  ? 1.12277 0.91048 0.92424 0.35832  0.01219  0.00477  57  GLU A C   
449  O O   . GLU A 57  ? 1.18077 0.90712 0.95467 0.38472  0.01415  0.02148  57  GLU A O   
450  C CB  . GLU A 57  ? 1.10061 1.00365 0.92139 0.41182  -0.01502 -0.00420 57  GLU A CB  
451  C CG  . GLU A 57  ? 1.07216 1.05334 0.90255 0.41913  -0.02687 -0.00696 57  GLU A CG  
452  C CD  . GLU A 57  ? 1.10588 1.13605 0.94647 0.46494  -0.04272 -0.01926 57  GLU A CD  
453  O OE1 . GLU A 57  ? 1.13603 1.15610 0.98954 0.48651  -0.04371 -0.03484 57  GLU A OE1 
454  O OE2 . GLU A 57  ? 1.10505 1.18865 0.94195 0.47981  -0.05425 -0.01565 57  GLU A OE2 
455  N N   . ARG A 58  ? 1.10344 0.89090 0.92252 0.32366  0.02128  -0.01363 58  ARG A N   
456  C CA  . ARG A 58  ? 1.15699 0.87537 0.96548 0.30901  0.03505  -0.01770 58  ARG A CA  
457  C C   . ARG A 58  ? 1.14231 0.85161 0.94954 0.26161  0.04598  -0.01512 58  ARG A C   
458  O O   . ARG A 58  ? 1.16152 0.84324 0.97229 0.23735  0.05635  -0.03036 58  ARG A O   
459  C CB  . ARG A 58  ? 1.16110 0.88943 0.99172 0.31633  0.03560  -0.04890 58  ARG A CB  
460  C CG  . ARG A 58  ? 1.21527 0.92762 1.04154 0.36712  0.02880  -0.04935 58  ARG A CG  
461  C CD  . ARG A 58  ? 1.23008 0.94828 1.07791 0.38023  0.03115  -0.08165 58  ARG A CD  
462  N NE  . ARG A 58  ? 1.27630 0.93415 1.11792 0.35584  0.04741  -0.09446 58  ARG A NE  
463  C CZ  . ARG A 58  ? 1.24299 0.92704 1.10094 0.31880  0.05365  -0.11816 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 1.17058 0.92984 1.04834 0.30175  0.04655  -0.12735 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 1.28628 0.91842 1.13799 0.29853  0.06812  -0.13327 58  ARG A NH2 
466  N N   . LEU A 59  ? 1.11841 0.85455 0.92123 0.24884  0.04386  0.00214  59  LEU A N   
467  C CA  . LEU A 59  ? 1.11392 0.85942 0.92265 0.20685  0.05199  0.00154  59  LEU A CA  
468  C C   . LEU A 59  ? 1.21611 0.89211 1.00631 0.18391  0.06882  0.00449  59  LEU A C   
469  O O   . LEU A 59  ? 1.21646 0.89690 1.01947 0.15182  0.07560  -0.01305 59  LEU A O   
470  C CB  . LEU A 59  ? 1.06059 0.84019 0.86575 0.20163  0.04899  0.01985  59  LEU A CB  
471  C CG  . LEU A 59  ? 0.98953 0.84015 0.81641 0.21336  0.03627  0.01176  59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.96457 0.84135 0.78818 0.20196  0.03730  0.02636  59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.93498 0.82170 0.78844 0.19709  0.03451  -0.01169 59  LEU A CD2 
474  N N   . ASP A 60  ? 1.30577 0.91611 1.06366 0.19972  0.07655  0.02570  60  ASP A N   
475  C CA  . ASP A 60  ? 1.41464 0.94842 1.15068 0.17469  0.09726  0.02902  60  ASP A CA  
476  C C   . ASP A 60  ? 1.45848 0.96220 1.20551 0.16665  0.10433  0.00077  60  ASP A C   
477  O O   . ASP A 60  ? 1.50682 0.95143 1.24111 0.13858  0.12358  -0.00506 60  ASP A O   
478  C CB  . ASP A 60  ? 1.49574 0.95451 1.18766 0.19950  0.10512  0.06057  60  ASP A CB  
479  C CG  . ASP A 60  ? 1.54751 0.95108 1.21224 0.16205  0.12818  0.07593  60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.50613 0.94954 1.19105 0.11947  0.13430  0.06371  60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.64043 0.96021 1.26228 0.17599  0.14109  0.10031  60  ASP A OD2 
482  N N   . GLU A 61  ? 1.45612 1.00313 1.22741 0.18627  0.09118  -0.02028 61  GLU A N   
483  C CA  . GLU A 61  ? 1.49617 1.01731 1.27628 0.18331  0.09788  -0.04883 61  GLU A CA  
484  C C   . GLU A 61  ? 1.41421 1.00626 1.22535 0.16372  0.09031  -0.07817 61  GLU A C   
485  O O   . GLU A 61  ? 1.43301 1.01592 1.25219 0.16704  0.09355  -0.10367 61  GLU A O   
486  C CB  . GLU A 61  ? 1.55660 1.04557 1.32971 0.23286  0.09330  -0.04852 61  GLU A CB  
487  C CG  . GLU A 61  ? 1.66923 1.07662 1.40493 0.25925  0.10091  -0.01873 61  GLU A CG  
488  C CD  . GLU A 61  ? 1.69439 1.12170 1.42689 0.31553  0.08352  -0.00518 61  GLU A CD  
489  O OE1 . GLU A 61  ? 1.68668 1.13818 1.44012 0.34264  0.07576  -0.02729 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 1.71455 1.14047 1.42452 0.33172  0.07754  0.02544  61  GLU A OE2 
491  N N   . ILE A 62  ? 1.28131 0.94065 1.10740 0.14499  0.08135  -0.07514 62  ILE A N   
492  C CA  . ILE A 62  ? 1.16993 0.89418 1.01851 0.13093  0.07342  -0.09698 62  ILE A CA  
493  C C   . ILE A 62  ? 1.11523 0.87426 0.97075 0.09371  0.07402  -0.09695 62  ILE A C   
494  O O   . ILE A 62  ? 1.11369 0.88085 0.96632 0.08798  0.07362  -0.07678 62  ILE A O   
495  C CB  . ILE A 62  ? 1.10238 0.88434 0.96416 0.15606  0.05907  -0.09332 62  ILE A CB  
496  C CG1 . ILE A 62  ? 1.11595 0.88490 0.97868 0.19338  0.05630  -0.10036 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 1.06020 0.90259 0.93756 0.13760  0.05350  -0.10890 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 1.06230 0.88981 0.93831 0.21383  0.04445  -0.09734 62  ILE A CD1 
499  N N   . ALA A 63  ? 1.07626 0.86332 0.94142 0.07040  0.07396  -0.12051 63  ALA A N   
500  C CA  . ALA A 63  ? 1.01039 0.85187 0.88627 0.04347  0.06867  -0.12234 63  ALA A CA  
501  C C   . ALA A 63  ? 0.93864 0.83993 0.82404 0.05407  0.05533  -0.12514 63  ALA A C   
502  O O   . ALA A 63  ? 0.94159 0.85070 0.82643 0.05725  0.05447  -0.14366 63  ALA A O   
503  C CB  . ALA A 63  ? 1.03684 0.87366 0.91356 0.00792  0.07733  -0.14639 63  ALA A CB  
504  N N   . PHE A 64  ? 0.88032 0.81997 0.77243 0.05853  0.04731  -0.10737 64  PHE A N   
505  C CA  . PHE A 64  ? 0.82680 0.81532 0.72415 0.06621  0.03761  -0.10625 64  PHE A CA  
506  C C   . PHE A 64  ? 0.81917 0.84985 0.71963 0.04489  0.03203  -0.11354 64  PHE A C   
507  O O   . PHE A 64  ? 0.82781 0.86496 0.73369 0.02515  0.03369  -0.11511 64  PHE A O   
508  C CB  . PHE A 64  ? 0.78366 0.78699 0.68582 0.08328  0.03364  -0.08489 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.78527 0.76270 0.68425 0.10808  0.03556  -0.07856 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.80981 0.75114 0.70143 0.11430  0.03992  -0.06588 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.76544 0.76000 0.66760 0.12509  0.03306  -0.08482 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.81874 0.74418 0.70521 0.14143  0.03856  -0.05889 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.77096 0.75560 0.67367 0.14907  0.03259  -0.08214 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.79714 0.74900 0.69160 0.15947  0.03368  -0.06848 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.81193 0.87335 0.70737 0.04865  0.02599  -0.11905 65  ILE A N   
516  C CA  . ILE A 65  ? 0.80563 0.91335 0.69860 0.03752  0.01717  -0.12110 65  ILE A CA  
517  C C   . ILE A 65  ? 0.77250 0.90050 0.65861 0.05468  0.01239  -0.10673 65  ILE A C   
518  O O   . ILE A 65  ? 0.76500 0.87886 0.64364 0.06465  0.01737  -0.11020 65  ILE A O   
519  C CB  . ILE A 65  ? 0.83931 0.95805 0.72169 0.02058  0.01693  -0.14577 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.87759 0.97498 0.76574 -0.00206 0.02442  -0.16500 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.83044 1.00226 0.70295 0.01739  0.00496  -0.14376 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.90623 0.95115 0.78957 0.00256  0.03624  -0.17875 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.76124 0.92184 0.64922 0.05762  0.00435  -0.09304 66  GLY A N   
524  C CA  . GLY A 66  ? 0.74889 0.92049 0.62552 0.07280  0.00214  -0.07863 66  GLY A CA  
525  C C   . GLY A 66  ? 0.77067 0.97393 0.62784 0.06937  -0.00649 -0.08029 66  GLY A C   
526  O O   . GLY A 66  ? 0.77436 1.01099 0.63653 0.06122  -0.01619 -0.08429 66  GLY A O   
527  N N   . ILE A 67  ? 0.79232 0.98712 0.62685 0.07525  -0.00213 -0.07759 67  ILE A N   
528  C CA  . ILE A 67  ? 0.84056 1.05969 0.64735 0.07752  -0.00934 -0.07115 67  ILE A CA  
529  C C   . ILE A 67  ? 0.88427 1.08759 0.67682 0.09512  -0.00445 -0.04761 67  ILE A C   
530  O O   . ILE A 67  ? 0.88980 1.06360 0.67853 0.09613  0.00939  -0.04812 67  ILE A O   
531  C CB  . ILE A 67  ? 0.85543 1.07472 0.63897 0.06455  -0.00491 -0.08992 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.85820 1.08948 0.65498 0.04580  -0.00795 -0.11600 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.88588 1.12738 0.63195 0.06908  -0.01144 -0.07843 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.88616 1.11749 0.66317 0.03257  -0.00189 -0.13912 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.92584 1.14908 0.71204 0.10927  -0.01473 -0.02881 68  HIS A N   
536  C CA  . HIS A 68  ? 0.98812 1.18764 0.75734 0.12718  -0.00808 -0.00564 68  HIS A CA  
537  C C   . HIS A 68  ? 1.11067 1.30675 0.83400 0.13004  -0.00752 0.00415  68  HIS A C   
538  O O   . HIS A 68  ? 1.14507 1.37561 0.85136 0.13508  -0.02292 0.00850  68  HIS A O   
539  C CB  . HIS A 68  ? 0.93635 1.15186 0.72263 0.14642  -0.01720 0.01109  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.92179 1.18332 0.69901 0.15695  -0.03649 0.01781  68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.89758 1.20774 0.69939 0.14620  -0.05005 0.00148  68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.95430 1.22316 0.69990 0.17809  -0.04455 0.03857  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.91954 1.27457 0.70922 0.15979  -0.06730 0.00889  68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.95957 1.28980 0.71354 0.18202  -0.06556 0.03330  68  HIS A NE2 
545  N N   . THR A 69  ? 0.92471 1.28147 0.75800 0.23207  -0.01081 0.14327  69  THR A N   
546  C CA  . THR A 69  ? 0.95798 1.31023 0.77429 0.24252  -0.01859 0.13405  69  THR A CA  
547  C C   . THR A 69  ? 0.97956 1.30001 0.79995 0.22746  -0.02358 0.14028  69  THR A C   
548  O O   . THR A 69  ? 0.97155 1.29007 0.77552 0.23852  -0.03028 0.13515  69  THR A O   
549  C CB  . THR A 69  ? 0.97475 1.29566 0.78450 0.23675  -0.00213 0.15324  69  THR A CB  
550  O OG1 . THR A 69  ? 0.95461 1.22362 0.78554 0.20257  0.01089  0.17581  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.98901 1.33134 0.78856 0.25328  0.00669  0.15105  69  THR A CG2 
552  N N   . GLY A 70  ? 0.94348 1.23988 0.78296 0.20470  -0.01989 0.15143  70  GLY A N   
553  C CA  . GLY A 70  ? 0.91244 1.18710 0.75099 0.19688  -0.02854 0.15051  70  GLY A CA  
554  C C   . GLY A 70  ? 0.92952 1.25224 0.77316 0.21444  -0.04449 0.12651  70  GLY A C   
555  O O   . GLY A 70  ? 1.00301 1.38050 0.84006 0.24130  -0.05786 0.09671  70  GLY A O   
556  N N   . HIS A 71  ? 0.81963 1.12946 0.67937 0.19888  -0.04519 0.13146  71  HIS A N   
557  C CA  . HIS A 71  ? 0.79293 1.15651 0.66892 0.21044  -0.06053 0.10483  71  HIS A CA  
558  C C   . HIS A 71  ? 0.74580 1.14887 0.65294 0.20229  -0.05686 0.10351  71  HIS A C   
559  O O   . HIS A 71  ? 0.71792 1.08405 0.62920 0.18344  -0.03580 0.13764  71  HIS A O   
560  C CB  . HIS A 71  ? 0.76437 1.10080 0.64337 0.20083  -0.06428 0.10961  71  HIS A CB  
561  C CG  . HIS A 71  ? 0.78843 1.09514 0.64045 0.21175  -0.06962 0.11122  71  HIS A CG  
562  N ND1 . HIS A 71  ? 0.81892 1.16527 0.65735 0.24205  -0.08306 0.08516  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 0.79412 1.04151 0.63214 0.19681  -0.06363 0.13315  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 0.84753 1.15684 0.66180 0.24783  -0.08250 0.09884  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 0.83405 1.08667 0.64838 0.22073  -0.07156 0.12714  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.72684 1.19983 0.66929 0.20811  -0.07181 0.05356  72  LEU A N   
567  C CA  . LEU A 72  ? 0.74057 1.20718 0.74136 0.16861  -0.04711 0.02589  72  LEU A CA  
568  C C   . LEU A 72  ? 0.76673 1.18557 0.77752 0.14363  -0.02707 0.07086  72  LEU A C   
569  O O   . LEU A 72  ? 0.78268 1.19749 0.77697 0.15128  -0.03898 0.09742  72  LEU A O   
570  C CB  . LEU A 72  ? 0.70109 1.22965 0.74550 0.16254  -0.05949 -0.03687 72  LEU A CB  
571  C CG  . LEU A 72  ? 0.67501 1.21067 0.78515 0.12023  -0.03641 -0.07655 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.68778 1.20162 0.81790 0.10035  -0.01131 -0.10000 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.66992 1.28530 0.80931 0.12619  -0.05898 -0.13615 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.75754 1.13863 0.79158 0.11661  0.00442  0.08052  73  GLY A N   
575  C CA  . GLY A 73  ? 0.74369 1.09145 0.79758 0.09133  0.02667  0.11154  73  GLY A CA  
576  C C   . GLY A 73  ? 0.74802 1.10458 0.86020 0.05984  0.04703  0.06813  73  GLY A C   
577  O O   . GLY A 73  ? 0.78407 1.17200 0.92074 0.05579  0.04359  0.01371  73  GLY A O   
578  N N   . PHE A 74  ? 0.65280 0.98254 0.78659 0.03669  0.07033  0.09230  74  PHE A N   
579  C CA  . PHE A 74  ? 0.59644 0.92483 0.78367 0.00370  0.09664  0.05804  74  PHE A CA  
580  C C   . PHE A 74  ? 0.61526 0.89350 0.80926 -0.00975 0.13181  0.06065  74  PHE A C   
581  O O   . PHE A 74  ? 0.64112 0.91577 0.87593 -0.03533 0.15306  0.01819  74  PHE A O   
582  C CB  . PHE A 74  ? 0.52825 0.85214 0.73569 -0.01363 0.10850  0.08127  74  PHE A CB  
583  C CG  . PHE A 74  ? 0.48667 0.86586 0.71437 -0.01337 0.08419  0.04960  74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.45374 0.85958 0.64642 0.01692  0.04809  0.05887  74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.47627 0.88332 0.75714 -0.04176 0.09745  0.00571  74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.42356 0.88138 0.63160 0.02288  0.02505  0.02900  74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.44719 0.91497 0.74741 -0.03877 0.07369  -0.02694 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.42130 0.91504 0.68388 -0.00388 0.03645  -0.01516 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.61452 0.85308 0.76961 0.00630  0.14049  0.10941  75  TYR A N   
590  C CA  . TYR A 75  ? 0.64334 0.83330 0.79665 0.00200  0.17194  0.11340  75  TYR A CA  
591  C C   . TYR A 75  ? 0.66639 0.86728 0.79684 0.02240  0.15645  0.08854  75  TYR A C   
592  O O   . TYR A 75  ? 0.69572 0.87186 0.84050 0.01357  0.17743  0.05901  75  TYR A O   
593  C CB  . TYR A 75  ? 0.62856 0.77732 0.75307 0.01101  0.19182  0.17835  75  TYR A CB  
594  C CG  . TYR A 75  ? 0.60232 0.74341 0.74228 -0.00500 0.19940  0.19788  75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.61514 0.74576 0.79916 -0.03385 0.22526  0.17385  75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.57549 0.70877 0.67905 0.00963  0.16159  0.21241  75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.61376 0.73173 0.79089 -0.04278 0.21227  0.17526  75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.56720 0.68970 0.67512 0.00029  0.15326  0.20678  75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.59081 0.70651 0.72897 -0.02388 0.17770  0.19243  75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.58517 0.69449 0.72043 -0.02998 0.16927  0.18889  75  TYR A OH  
601  N N   . ALA A 76  ? 0.65932 0.89584 0.75374 0.04975  0.12124  0.09890  76  ALA A N   
602  C CA  . ALA A 76  ? 0.70380 0.95977 0.77072 0.07427  0.10311  0.07894  76  ALA A CA  
603  C C   . ALA A 76  ? 0.71551 1.03007 0.80605 0.07458  0.07865  0.01538  76  ALA A C   
604  O O   . ALA A 76  ? 0.69861 1.05747 0.76616 0.09834  0.04534  0.01243  76  ALA A O   
605  C CB  . ALA A 76  ? 0.68999 0.95097 0.70210 0.10412  0.08240  0.12795  76  ALA A CB  
606  N N   . ASP A 77  ? 0.75557 1.07154 0.89263 0.04806  0.09702  -0.03751 77  ASP A N   
607  C CA  . ASP A 77  ? 0.76521 1.14867 0.93210 0.04462  0.07531  -0.10398 77  ASP A CA  
608  C C   . ASP A 77  ? 0.78789 1.19203 0.95414 0.05349  0.07177  -0.15385 77  ASP A C   
609  O O   . ASP A 77  ? 0.81479 1.23460 1.02675 0.02683  0.08501  -0.21517 77  ASP A O   
610  C CB  . ASP A 77  ? 0.77831 1.16761 1.00503 0.00395  0.09496  -0.13712 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.82846 1.15270 1.08448 -0.02969 0.14134  -0.14266 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.86387 1.14797 1.09911 -0.02060 0.15532  -0.13713 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.83850 1.15003 1.13646 -0.06375 0.16528  -0.15168 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.77517 1.18039 0.88998 0.08946  0.05542  -0.12850 78  TRP A N   
615  C CA  . TRP A 78  ? 0.80577 1.24226 0.90989 0.10753  0.04505  -0.17186 78  TRP A CA  
616  C C   . TRP A 78  ? 0.79243 1.26369 0.83803 0.15384  0.01116  -0.14196 78  TRP A C   
617  O O   . TRP A 78  ? 0.78255 1.21699 0.78780 0.16809  0.01226  -0.07657 78  TRP A O   
618  C CB  . TRP A 78  ? 0.83982 1.21424 0.93965 0.10002  0.07714  -0.16591 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.87546 1.22028 1.02821 0.06020  0.11010  -0.21413 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.88216 1.15858 1.05967 0.02877  0.14826  -0.19159 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.91339 1.29319 1.10052 0.04623  0.11131  -0.29453 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.92570 1.18385 1.15021 -0.00578 0.17579  -0.25063 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.94388 1.26598 1.17736 0.00196  0.15348  -0.31720 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.92541 1.38197 1.10809 0.06721  0.08180  -0.35056 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.98870 1.32352 1.26687 -0.02678 0.16819  -0.39639 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.96529 1.44430 1.19323 0.04100  0.09343  -0.43137 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.99697 1.41337 1.27344 -0.00794 0.13687  -0.45498 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.79672 1.33793 0.83736 0.17642  -0.01592 -0.18920 79  ARG A N   
629  C CA  . ARG A 79  ? 0.77599 1.34751 0.75680 0.22345  -0.04459 -0.16139 79  ARG A CA  
630  C C   . ARG A 79  ? 0.76437 1.31399 0.71416 0.23947  -0.03473 -0.15146 79  ARG A C   
631  O O   . ARG A 79  ? 0.78108 1.31326 0.76018 0.21934  -0.01332 -0.18904 79  ARG A O   
632  C CB  . ARG A 79  ? 0.79638 1.45917 0.77929 0.24866  -0.07815 -0.21527 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.79121 1.47682 0.72760 0.28613  -0.10675 -0.17559 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.80608 1.58563 0.74866 0.31270  -0.13837 -0.23059 79  ARG A CD  
635  N NE  . ARG A 79  ? 0.82652 1.66511 0.81539 0.29808  -0.13732 -0.31228 79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.85650 1.75467 0.82681 0.32845  -0.15327 -0.35086 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.87586 1.75414 0.79236 0.36963  -0.15500 -0.30456 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.87724 1.82806 0.89681 0.30790  -0.14974 -0.43061 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.74124 1.28739 0.63116 0.27464  -0.04727 -0.10038 80  PRO A N   
640  C CA  . PRO A 80  ? 0.75310 1.28777 0.61385 0.29190  -0.03860 -0.09407 80  PRO A CA  
641  C C   . PRO A 80  ? 0.77581 1.36749 0.65193 0.30250  -0.04840 -0.16779 80  PRO A C   
642  O O   . PRO A 80  ? 0.80247 1.37126 0.68998 0.29349  -0.02864 -0.19088 80  PRO A O   
643  C CB  . PRO A 80  ? 0.75109 1.29224 0.54602 0.32939  -0.05586 -0.03447 80  PRO A CB  
644  C CG  . PRO A 80  ? 0.72366 1.24420 0.51657 0.31991  -0.06052 0.00577  80  PRO A CG  
645  C CD  . PRO A 80  ? 0.71660 1.26772 0.56147 0.30010  -0.06755 -0.04812 80  PRO A CD  
646  N N   . ALA A 81  ? 0.77349 1.44150 0.65015 0.32293  -0.07830 -0.20762 81  ALA A N   
647  C CA  . ALA A 81  ? 0.81360 1.55310 0.70124 0.33826  -0.09209 -0.28089 81  ALA A CA  
648  C C   . ALA A 81  ? 0.82078 1.54045 0.76835 0.29588  -0.06574 -0.34206 81  ALA A C   
649  O O   . ALA A 81  ? 0.85329 1.60316 0.80538 0.30342  -0.06557 -0.39337 81  ALA A O   
650  C CB  . ALA A 81  ? 0.81841 1.64713 0.70970 0.36066  -0.12537 -0.31981 81  ALA A CB  
651  N N   . GLU A 82  ? 0.79510 1.46004 0.78697 0.25131  -0.04090 -0.33664 82  GLU A N   
652  C CA  . GLU A 82  ? 0.79767 1.43390 0.84574 0.20837  -0.01105 -0.39255 82  GLU A CA  
653  C C   . GLU A 82  ? 0.80107 1.34883 0.83653 0.19989  0.02324  -0.36115 82  GLU A C   
654  O O   . GLU A 82  ? 0.82015 1.32011 0.89764 0.16303  0.05545  -0.39510 82  GLU A O   
655  C CB  . GLU A 82  ? 0.77202 1.39232 0.87385 0.16469  0.00307  -0.40383 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.74516 1.45035 0.85631 0.17637  -0.03022 -0.42671 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.73920 1.43915 0.91008 0.13057  -0.01465 -0.45026 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.71212 1.35638 0.88004 0.11783  -0.00207 -0.39240 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.76434 1.51934 0.98639 0.10599  -0.01381 -0.52869 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.78633 1.31237 0.76401 0.23407  0.01851  -0.29847 83  ALA A N   
661  C CA  . ALA A 83  ? 0.80522 1.24994 0.76769 0.22990  0.05090  -0.25952 83  ALA A CA  
662  C C   . ALA A 83  ? 0.86755 1.30051 0.84722 0.22420  0.06885  -0.31979 83  ALA A C   
663  O O   . ALA A 83  ? 0.90581 1.26399 0.91023 0.19666  0.10595  -0.32439 83  ALA A O   
664  C CB  . ALA A 83  ? 0.78709 1.22843 0.68514 0.26846  0.03965  -0.18706 83  ALA A CB  
665  N N   . ASP A 84  ? 0.88154 1.38565 0.84557 0.25226  0.04432  -0.36609 84  ASP A N   
666  C CA  . ASP A 84  ? 0.88096 1.37451 0.85801 0.24916  0.06081  -0.42506 84  ASP A CA  
667  C C   . ASP A 84  ? 0.91389 1.37793 0.95878 0.19752  0.08755  -0.49218 84  ASP A C   
668  O O   . ASP A 84  ? 0.96327 1.35643 1.02329 0.17888  0.12268  -0.51172 84  ASP A O   
669  C CB  . ASP A 84  ? 0.89779 1.48756 0.85125 0.28721  0.02728  -0.47181 84  ASP A CB  
670  C CG  . ASP A 84  ? 0.88277 1.49064 0.76576 0.33799  0.00937  -0.40785 84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.87989 1.42061 0.73459 0.34379  0.03011  -0.34661 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.87770 1.57159 0.73273 0.37344  -0.02470 -0.42006 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.89228 1.40865 0.97785 0.17403  0.07333  -0.52831 85  LYS A N   
674  C CA  . LYS A 85  ? 0.92175 1.41052 1.07482 0.11902  0.10178  -0.58755 85  LYS A CA  
675  C C   . LYS A 85  ? 0.94845 1.31908 1.11124 0.08924  0.14630  -0.53523 85  LYS A C   
676  O O   . LYS A 85  ? 1.00674 1.30953 1.20196 0.05553  0.18539  -0.56959 85  LYS A O   
677  C CB  . LYS A 85  ? 0.88823 1.45875 1.07919 0.10221  0.07775  -0.62260 85  LYS A CB  
678  N N   . LEU A 86  ? 0.89513 1.23985 1.02790 0.10289  0.14200  -0.45203 86  LEU A N   
679  C CA  . LEU A 86  ? 0.89376 1.13847 1.02948 0.08216  0.18065  -0.39473 86  LEU A CA  
680  C C   . LEU A 86  ? 0.95032 1.11148 1.06739 0.08886  0.21580  -0.38539 86  LEU A C   
681  O O   . LEU A 86  ? 0.98624 1.06838 1.13330 0.05622  0.25831  -0.40061 86  LEU A O   
682  C CB  . LEU A 86  ? 0.82939 1.07623 0.92413 0.10704  0.16346  -0.30862 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.79133 0.98924 0.90461 0.08057  0.18419  -0.26195 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.83069 1.01324 1.00766 0.03132  0.20875  -0.31883 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.72837 0.98721 0.82316 0.09770  0.14686  -0.22775 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.95491 1.13122 1.01897 0.13358  0.19966  -0.35653 87  VAL A N   
687  C CA  . VAL A 87  ? 1.01736 1.12633 1.05677 0.14947  0.22815  -0.34871 87  VAL A CA  
688  C C   . VAL A 87  ? 1.10122 1.17445 1.18332 0.11835  0.25633  -0.43058 87  VAL A C   
689  O O   . VAL A 87  ? 1.15226 1.12827 1.23906 0.10553  0.30020  -0.42500 87  VAL A O   
690  C CB  . VAL A 87  ? 1.00331 1.16558 0.98757 0.20044  0.19881  -0.33102 87  VAL A CB  
691  C CG1 . VAL A 87  ? 1.06032 1.15748 1.01777 0.22022  0.22760  -0.32247 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.93459 1.13028 0.87960 0.22501  0.17355  -0.25402 87  VAL A CG2 
693  N N   . LYS A 88  ? 1.12511 1.27759 1.23725 0.10726  0.23234  -0.50887 88  LYS A N   
694  C CA  . LYS A 88  ? 1.21108 1.34574 1.36692 0.07515  0.25517  -0.59837 88  LYS A CA  
695  C C   . LYS A 88  ? 1.26215 1.30731 1.46633 0.02105  0.30254  -0.60768 88  LYS A C   
696  O O   . LYS A 88  ? 1.32755 1.26975 1.53169 0.01009  0.34718  -0.60849 88  LYS A O   
697  C CB  . LYS A 88  ? 1.19547 1.45102 1.38042 0.07018  0.21713  -0.67930 88  LYS A CB  
698  C CG  . LYS A 88  ? 1.22164 1.53223 1.38065 0.10554  0.19647  -0.72562 88  LYS A CG  
699  C CD  . LYS A 88  ? 1.17148 1.61736 1.31541 0.13767  0.14205  -0.74282 88  LYS A CD  
700  C CE  . LYS A 88  ? 1.19476 1.68995 1.29307 0.18689  0.12050  -0.75821 88  LYS A CE  
701  N NZ  . LYS A 88  ? 1.14509 1.75358 1.20674 0.23178  0.07025  -0.74009 88  LYS A NZ  
702  N N   . LEU A 89  ? 1.23827 1.32109 1.48154 -0.01090 0.29449  -0.61362 89  LEU A N   
703  C CA  . LEU A 89  ? 1.28875 1.29392 1.57877 -0.06386 0.33969  -0.61973 89  LEU A CA  
704  C C   . LEU A 89  ? 1.32481 1.21340 1.58189 -0.05330 0.37825  -0.53465 89  LEU A C   
705  O O   . LEU A 89  ? 1.39294 1.17942 1.66937 -0.08298 0.42969  -0.54189 89  LEU A O   
706  C CB  . LEU A 89  ? 1.23154 1.30785 1.55884 -0.08945 0.31873  -0.62506 89  LEU A CB  
707  C CG  . LEU A 89  ? 1.20480 1.41533 1.54644 -0.07924 0.26987  -0.69271 89  LEU A CG  
708  C CD1 . LEU A 89  ? 1.12232 1.41468 1.45723 -0.06370 0.22966  -0.65712 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 1.26100 1.49517 1.67043 -0.13195 0.28784  -0.79585 89  LEU A CD2 
710  N N   . LEU A 90  ? 1.29062 1.19411 1.49603 -0.00976 0.35527  -0.45385 90  LEU A N   
711  C CA  . LEU A 90  ? 1.33611 1.14666 1.50597 0.00746  0.38722  -0.37194 90  LEU A CA  
712  C C   . LEU A 90  ? 1.48086 1.19953 1.63047 0.01986  0.42595  -0.38055 90  LEU A C   
713  O O   . LEU A 90  ? 1.51542 1.13724 1.64883 0.02323  0.46737  -0.33045 90  LEU A O   
714  C CB  . LEU A 90  ? 1.24871 1.10571 1.36512 0.05416  0.35243  -0.29659 90  LEU A CB  
715  C CG  . LEU A 90  ? 1.19713 1.02381 1.30266 0.05384  0.36313  -0.21734 90  LEU A CG  
716  C CD1 . LEU A 90  ? 1.24273 0.98356 1.38535 0.01340  0.41294  -0.21954 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 1.11171 1.02897 1.22331 0.05306  0.31927  -0.20651 90  LEU A CD2 
718  N N   . ALA A 91  ? 1.57614 1.32507 1.72285 0.03119  0.41311  -0.44226 91  ALA A N   
719  C CA  . ALA A 91  ? 1.73392 1.39645 1.85855 0.04680  0.44837  -0.45392 91  ALA A CA  
720  C C   . ALA A 91  ? 1.87639 1.45393 2.05015 -0.00462 0.49768  -0.51756 91  ALA A C   
721  O O   . ALA A 91  ? 1.95303 1.41114 2.11563 -0.00699 0.54863  -0.49004 91  ALA A O   
722  C CB  . ALA A 91  ? 1.74014 1.47116 1.83731 0.08368  0.41461  -0.49167 91  ALA A CB  
723  N N   . LYS A 92  ? 1.90929 1.54842 2.13715 -0.04594 0.48465  -0.60313 92  LYS A N   
724  C CA  . LYS A 92  ? 2.00949 1.57779 2.29034 -0.10238 0.53118  -0.67387 92  LYS A CA  
725  C C   . LYS A 92  ? 2.01769 1.49402 2.32030 -0.13905 0.57808  -0.63109 92  LYS A C   
726  O O   . LYS A 92  ? 2.11008 1.49452 2.44031 -0.17859 0.62711  -0.65941 92  LYS A O   
727  C CB  . LYS A 92  ? 2.01727 1.69666 2.35431 -0.13903 0.50127  -0.77193 92  LYS A CB  
728  C CG  . LYS A 92  ? 2.13586 1.78191 2.53007 -0.20015 0.53102  -0.83362 92  LYS A CG  
729  C CD  . LYS A 92  ? 2.13166 1.91940 2.57799 -0.22791 0.48886  -0.91157 92  LYS A CD  
730  C CE  . LYS A 92  ? 2.04554 1.92194 2.51113 -0.23400 0.45965  -0.90091 92  LYS A CE  
731  N NZ  . LYS A 92  ? 2.01727 2.04426 2.52773 -0.24992 0.41423  -0.96939 92  LYS A NZ  
732  N N   . GLY A 93  ? 1.90110 1.15616 1.14738 0.20571  -0.03316 -0.31997 93  GLY A N   
733  C CA  . GLY A 93  ? 1.84774 1.08265 1.11864 0.18288  -0.03033 -0.31312 93  GLY A CA  
734  C C   . GLY A 93  ? 1.83211 1.06224 1.12448 0.13708  -0.04997 -0.32775 93  GLY A C   
735  O O   . GLY A 93  ? 1.81100 1.08517 1.12000 0.12618  -0.06152 -0.33371 93  GLY A O   
736  N N   . GLU A 94  ? 1.85513 1.03480 1.14871 0.10973  -0.05360 -0.33267 94  GLU A N   
737  C CA  . GLU A 94  ? 1.87236 1.04875 1.19089 0.06185  -0.07149 -0.34727 94  GLU A CA  
738  C C   . GLU A 94  ? 1.83714 1.07419 1.19904 0.04411  -0.07636 -0.34112 94  GLU A C   
739  O O   . GLU A 94  ? 1.84534 1.10540 1.23030 0.01171  -0.09506 -0.35515 94  GLU A O   
740  C CB  . GLU A 94  ? 1.87454 1.04003 1.17311 0.05158  -0.09112 -0.37252 94  GLU A CB  
741  C CG  . GLU A 94  ? 1.91200 1.01562 1.16396 0.06922  -0.08809 -0.38046 94  GLU A CG  
742  C CD  . GLU A 94  ? 1.91485 0.99409 1.15748 0.04076  -0.10868 -0.40749 94  GLU A CD  
743  O OE1 . GLU A 94  ? 1.87144 0.97650 1.15154 0.00095  -0.12280 -0.41775 94  GLU A OE1 
744  O OE2 . GLU A 94  ? 1.96514 1.00316 1.16500 0.05802  -0.11106 -0.41892 94  GLU A OE2 
745  N N   . TYR A 95  ? 1.78563 1.06441 1.16983 0.06558  -0.05896 -0.31661 95  TYR A N   
746  C CA  . TYR A 95  ? 1.72245 1.08009 1.16962 0.05025  -0.05652 -0.29730 95  TYR A CA  
747  C C   . TYR A 95  ? 1.70349 1.05473 1.18480 0.02815  -0.04617 -0.28078 95  TYR A C   
748  O O   . TYR A 95  ? 1.75073 1.04226 1.20519 0.03504  -0.03610 -0.27827 95  TYR A O   
749  C CB  . TYR A 95  ? 1.69382 1.10687 1.14940 0.08537  -0.04253 -0.27859 95  TYR A CB  
750  C CG  . TYR A 95  ? 1.72037 1.11513 1.15822 0.11924  -0.02127 -0.26382 95  TYR A CG  
751  C CD1 . TYR A 95  ? 1.68166 1.09693 1.15532 0.11692  -0.00763 -0.24166 95  TYR A CD1 
752  C CD2 . TYR A 95  ? 1.78572 1.14682 1.17099 0.15581  -0.01536 -0.27260 95  TYR A CD2 
753  C CE1 . TYR A 95  ? 1.69660 1.10143 1.15618 0.14949  0.00964  -0.22943 95  TYR A CE1 
754  C CE2 . TYR A 95  ? 1.80031 1.15209 1.17239 0.18918  0.00360  -0.25981 95  TYR A CE2 
755  C CZ  . TYR A 95  ? 1.75746 1.13278 1.16802 0.18565  0.01521  -0.23855 95  TYR A CZ  
756  O OH  . TYR A 95  ? 1.77252 1.14427 1.17205 0.22011  0.03191  -0.22704 95  TYR A OH  
757  N N   . GLN A 96  ? 1.64070 1.05254 1.17796 0.00411  -0.04830 -0.26908 96  GLN A N   
758  C CA  . GLN A 96  ? 1.61566 1.03140 1.18929 -0.01874 -0.03899 -0.25287 96  GLN A CA  
759  C C   . GLN A 96  ? 1.53125 0.99834 1.13534 0.00169  -0.02306 -0.22587 96  GLN A C   
760  O O   . GLN A 96  ? 1.50388 1.02324 1.11984 0.01995  -0.02246 -0.21953 96  GLN A O   
761  C CB  . GLN A 96  ? 1.61536 1.06523 1.23228 -0.06124 -0.05235 -0.25973 96  GLN A CB  
762  C CG  . GLN A 96  ? 1.70578 1.10463 1.30587 -0.09440 -0.06619 -0.28447 96  GLN A CG  
763  C CD  . GLN A 96  ? 1.69283 1.14637 1.33811 -0.12982 -0.08342 -0.29558 96  GLN A CD  
764  O OE1 . GLN A 96  ? 1.62507 1.15089 1.31092 -0.12696 -0.08461 -0.28385 96  GLN A OE1 
765  N NE2 . GLN A 96  ? 1.75795 1.17732 1.39582 -0.16289 -0.09728 -0.31917 96  GLN A NE2 
766  N N   . LYS A 97  ? 1.49600 0.94622 1.11146 -0.00295 -0.01031 -0.21021 97  LYS A N   
767  C CA  . LYS A 97  ? 1.41129 0.90608 1.05585 0.01346  0.00335  -0.18604 97  LYS A CA  
768  C C   . LYS A 97  ? 1.33376 0.87214 1.02930 -0.01698 0.00210  -0.17546 97  LYS A C   
769  O O   . LYS A 97  ? 1.36100 0.87173 1.06240 -0.04665 0.00028  -0.17946 97  LYS A O   
770  C CB  . LYS A 97  ? 1.44116 0.88831 1.05857 0.03592  0.01791  -0.17561 97  LYS A CB  
771  C CG  . LYS A 97  ? 1.51340 0.90498 1.07350 0.06864  0.02060  -0.18691 97  LYS A CG  
772  C CD  . LYS A 97  ? 1.53045 0.89325 1.06753 0.10265  0.03567  -0.17356 97  LYS A CD  
773  C CE  . LYS A 97  ? 1.52395 0.85889 1.06927 0.08776  0.04279  -0.15979 97  LYS A CE  
774  N NZ  . LYS A 97  ? 1.53541 0.84433 1.05625 0.12384  0.05529  -0.14704 97  LYS A NZ  
775  N N   . VAL A 98  ? 1.24207 0.84717 0.97330 -0.01056 0.00378  -0.16242 98  VAL A N   
776  C CA  . VAL A 98  ? 1.14773 0.79092 0.92281 -0.03031 0.00672  -0.14843 98  VAL A CA  
777  C C   . VAL A 98  ? 1.07575 0.73904 0.86083 -0.00749 0.02022  -0.12805 98  VAL A C   
778  O O   . VAL A 98  ? 1.06492 0.74426 0.84037 0.01987  0.02438  -0.12458 98  VAL A O   
779  C CB  . VAL A 98  ? 1.09071 0.79354 0.90165 -0.04694 -0.00484 -0.15150 98  VAL A CB  
780  C CG1 . VAL A 98  ? 1.09734 0.80580 0.88944 -0.04110 -0.01853 -0.16912 98  VAL A CG1 
781  C CG2 . VAL A 98  ? 1.01514 0.77408 0.85954 -0.03778 0.00161  -0.13242 98  VAL A CG2 
782  N N   . SER A 99  ? 1.03464 0.69639 0.83778 -0.01909 0.02735  -0.11538 99  SER A N   
783  C CA  . SER A 99  ? 1.00111 0.67773 0.81234 0.00059  0.03829  -0.09750 99  SER A CA  
784  C C   . SER A 99  ? 0.92569 0.65725 0.77960 -0.01223 0.03795  -0.08602 99  SER A C   
785  O O   . SER A 99  ? 0.92189 0.65754 0.79417 -0.03851 0.03558  -0.08667 99  SER A O   
786  C CB  . SER A 99  ? 1.05840 0.67784 0.84405 0.00413  0.04748  -0.09185 99  SER A CB  
787  O OG  . SER A 99  ? 1.09441 0.69604 0.89059 -0.02845 0.04779  -0.09193 99  SER A OG  
788  N N   . TYR A 100 ? 0.87337 0.64733 0.74308 0.00565  0.04071  -0.07616 100 TYR A N   
789  C CA  . TYR A 100 ? 0.80312 0.62088 0.70786 -0.00417 0.04098  -0.06497 100 TYR A CA  
790  C C   . TYR A 100 ? 0.78297 0.59785 0.68914 0.00925  0.04997  -0.05071 100 TYR A C   
791  O O   . TYR A 100 ? 0.79048 0.59167 0.67829 0.03277  0.05463  -0.04871 100 TYR A O   
792  C CB  . TYR A 100 ? 0.74790 0.61543 0.67092 0.00172  0.03656  -0.06397 100 TYR A CB  
793  C CG  . TYR A 100 ? 0.74042 0.62314 0.66730 -0.01119 0.02576  -0.07543 100 TYR A CG  
794  C CD1 . TYR A 100 ? 0.76857 0.63046 0.69084 -0.03096 0.01835  -0.08780 100 TYR A CD1 
795  C CD2 . TYR A 100 ? 0.70954 0.62778 0.64379 -0.00337 0.02279  -0.07390 100 TYR A CD2 
796  C CE1 . TYR A 100 ? 0.77060 0.65188 0.69694 -0.04016 0.00605  -0.09964 100 TYR A CE1 
797  C CE2 . TYR A 100 ? 0.71657 0.64808 0.64985 -0.01069 0.01206  -0.08376 100 TYR A CE2 
798  C CZ  . TYR A 100 ? 0.74696 0.66258 0.67709 -0.02791 0.00263  -0.09719 100 TYR A CZ  
799  O OH  . TYR A 100 ? 0.75365 0.68676 0.68319 -0.03316 -0.01034 -0.10846 100 TYR A OH  
800  N N   . PRO A 101 ? 0.75523 0.58380 0.68123 -0.00296 0.05225  -0.04127 101 PRO A N   
801  C CA  . PRO A 101 ? 0.75026 0.57570 0.67406 0.01152  0.05926  -0.02845 101 PRO A CA  
802  C C   . PRO A 101 ? 0.71373 0.58215 0.65242 0.03052  0.05802  -0.02341 101 PRO A C   
803  O O   . PRO A 101 ? 0.68892 0.59275 0.64480 0.02720  0.05346  -0.02639 101 PRO A O   
804  C CB  . PRO A 101 ? 0.73648 0.57024 0.67824 -0.00843 0.06169  -0.02108 101 PRO A CB  
805  C CG  . PRO A 101 ? 0.72439 0.57308 0.68299 -0.03320 0.05549  -0.03056 101 PRO A CG  
806  C CD  . PRO A 101 ? 0.72512 0.58247 0.67822 -0.02631 0.04775  -0.04186 101 PRO A CD  
807  N N   . LEU A 102 ? 0.71655 0.58085 0.64745 0.05030  0.06213  -0.01574 102 LEU A N   
808  C CA  . LEU A 102 ? 0.68443 0.59033 0.63101 0.06750  0.06090  -0.01200 102 LEU A CA  
809  C C   . LEU A 102 ? 0.67041 0.58954 0.62674 0.07131  0.06104  -0.00190 102 LEU A C   
810  O O   . LEU A 102 ? 0.68564 0.57657 0.63058 0.06554  0.06427  0.00359  102 LEU A O   
811  C CB  . LEU A 102 ? 0.69954 0.59754 0.62809 0.09374  0.06365  -0.01554 102 LEU A CB  
812  C CG  . LEU A 102 ? 0.73121 0.60644 0.64007 0.09578  0.06451  -0.02613 102 LEU A CG  
813  C CD1 . LEU A 102 ? 0.76374 0.62417 0.64945 0.12593  0.06872  -0.02843 102 LEU A CD1 
814  C CD2 . LEU A 102 ? 0.69708 0.60947 0.62455 0.08656  0.06198  -0.03065 102 LEU A CD2 
815  N N   . LEU A 103 ? 0.64762 0.60930 0.62384 0.08064  0.05794  0.00022  103 LEU A N   
816  C CA  . LEU A 103 ? 0.61943 0.59960 0.60587 0.08511  0.05542  0.00745  103 LEU A CA  
817  C C   . LEU A 103 ? 0.61242 0.60611 0.59501 0.11151  0.05398  0.00803  103 LEU A C   
818  O O   . LEU A 103 ? 0.60298 0.62619 0.59774 0.12006  0.05328  0.00316  103 LEU A O   
819  C CB  . LEU A 103 ? 0.58168 0.60164 0.59622 0.07077  0.05076  0.00772  103 LEU A CB  
820  C CG  . LEU A 103 ? 0.56154 0.60726 0.58931 0.07427  0.04590  0.01218  103 LEU A CG  
821  C CD1 . LEU A 103 ? 0.57516 0.59701 0.58862 0.07519  0.04749  0.01918  103 LEU A CD1 
822  C CD2 . LEU A 103 ? 0.52616 0.60130 0.57601 0.05894  0.04203  0.01085  103 LEU A CD2 
823  N N   . LYS A 104 ? 0.62000 0.59460 0.58559 0.12523  0.05393  0.01409  104 LYS A N   
824  C CA  . LYS A 104 ? 0.62080 0.61415 0.58389 0.15259  0.04980  0.01447  104 LYS A CA  
825  C C   . LYS A 104 ? 0.59403 0.62623 0.57916 0.14974  0.04203  0.01636  104 LYS A C   
826  O O   . LYS A 104 ? 0.58542 0.60521 0.56694 0.13835  0.04197  0.02180  104 LYS A O   
827  C CB  . LYS A 104 ? 0.66252 0.60698 0.58657 0.17391  0.05343  0.01991  104 LYS A CB  
828  C CG  . LYS A 104 ? 0.68088 0.64180 0.59691 0.20863  0.04873  0.01859  104 LYS A CG  
829  C CD  . LYS A 104 ? 0.72943 0.63699 0.60235 0.22854  0.05184  0.02682  104 LYS A CD  
830  C CE  . LYS A 104 ? 0.74823 0.66618 0.60616 0.26842  0.04656  0.02550  104 LYS A CE  
831  N NZ  . LYS A 104 ? 0.80950 0.65357 0.61425 0.28666  0.05431  0.03201  104 LYS A NZ  
832  N N   . THR A 105 ? 0.58694 0.66715 0.59555 0.15868  0.03593  0.01102  105 THR A N   
833  C CA  . THR A 105 ? 0.56929 0.68677 0.59712 0.15881  0.02641  0.01014  105 THR A CA  
834  C C   . THR A 105 ? 0.59538 0.72987 0.61674 0.18981  0.01988  0.00820  105 THR A C   
835  O O   . THR A 105 ? 0.60424 0.75589 0.62994 0.20554  0.02147  0.00359  105 THR A O   
836  C CB  . THR A 105 ? 0.53486 0.69725 0.59839 0.13982  0.02404  0.00420  105 THR A CB  
837  O OG1 . THR A 105 ? 0.52231 0.66751 0.58772 0.11514  0.02899  0.00619  105 THR A OG1 
838  C CG2 . THR A 105 ? 0.51426 0.71229 0.59643 0.13865  0.01293  0.00119  105 THR A CG2 
839  N N   . THR A 106 ? 0.61429 0.74444 0.62298 0.20124  0.01258  0.01152  106 THR A N   
840  C CA  . THR A 106 ? 0.64164 0.79074 0.64239 0.23350  0.00356  0.00913  106 THR A CA  
841  C C   . THR A 106 ? 0.62525 0.82257 0.65128 0.23008  -0.01061 0.00291  106 THR A C   
842  O O   . THR A 106 ? 0.61796 0.80343 0.63998 0.21577  -0.01315 0.00586  106 THR A O   
843  C CB  . THR A 106 ? 0.69058 0.78324 0.64309 0.25608  0.00700  0.01872  106 THR A CB  
844  O OG1 . THR A 106 ? 0.72368 0.76796 0.65231 0.25627  0.01980  0.02279  106 THR A OG1 
845  C CG2 . THR A 106 ? 0.71602 0.82792 0.65613 0.29427  -0.00377 0.01620  106 THR A CG2 
846  N N   . VAL A 107 ? 0.62721 0.88016 0.67967 0.24303  -0.01982 -0.00667 107 VAL A N   
847  C CA  . VAL A 107 ? 0.63339 0.94025 0.71763 0.23507  -0.03433 -0.01620 107 VAL A CA  
848  C C   . VAL A 107 ? 0.69370 1.02814 0.77068 0.27061  -0.04881 -0.02135 107 VAL A C   
849  O O   . VAL A 107 ? 0.69572 1.06982 0.78932 0.28918  -0.05098 -0.02768 107 VAL A O   
850  C CB  . VAL A 107 ? 0.59373 0.95193 0.72436 0.21207  -0.03213 -0.02476 107 VAL A CB  
851  C CG1 . VAL A 107 ? 0.57329 0.97985 0.73553 0.19762  -0.04665 -0.03516 107 VAL A CG1 
852  C CG2 . VAL A 107 ? 0.57770 0.90685 0.70988 0.18349  -0.01728 -0.01926 107 VAL A CG2 
853  N N   . LYS A 108 ? 0.74969 1.06788 0.80233 0.28201  -0.05931 -0.01944 108 LYS A N   
854  C CA  . LYS A 108 ? 0.81579 1.15759 0.85569 0.31857  -0.07541 -0.02444 108 LYS A CA  
855  C C   . LYS A 108 ? 0.83047 1.23838 0.90841 0.31011  -0.09515 -0.03992 108 LYS A C   
856  O O   . LYS A 108 ? 0.80410 1.21089 0.89296 0.28208  -0.09851 -0.04272 108 LYS A O   
857  C CB  . LYS A 108 ? 0.84556 1.12802 0.82968 0.33984  -0.07546 -0.01303 108 LYS A CB  
858  C CG  . LYS A 108 ? 0.87149 1.08560 0.81027 0.35534  -0.05828 0.00168  108 LYS A CG  
859  C CD  . LYS A 108 ? 0.91542 1.07370 0.79777 0.37746  -0.05761 0.01356  108 LYS A CD  
860  C CE  . LYS A 108 ? 0.95748 1.04187 0.79464 0.38689  -0.03851 0.02835  108 LYS A CE  
861  N NZ  . LYS A 108 ? 1.01485 1.04028 0.79274 0.40968  -0.03460 0.04189  108 LYS A NZ  
862  N N   . TYR A 109 ? 0.89290 1.34105 0.98152 0.32438  -0.10462 -0.05013 109 TYR A N   
863  C CA  . TYR A 109 ? 0.91166 1.41901 1.03689 0.30953  -0.12125 -0.06658 109 TYR A CA  
864  C C   . TYR A 109 ? 0.95279 1.46084 1.05012 0.33347  -0.13825 -0.07288 109 TYR A C   
865  O O   . TYR A 109 ? 0.98438 1.44308 1.03018 0.36066  -0.13661 -0.06326 109 TYR A O   
866  C CB  . TYR A 109 ? 0.92882 1.49395 1.09898 0.29994  -0.11798 -0.07588 109 TYR A CB  
867  C CG  . TYR A 109 ? 0.91632 1.48381 1.11213 0.27837  -0.09975 -0.07059 109 TYR A CG  
868  C CD1 . TYR A 109 ? 0.88768 1.47686 1.12074 0.24071  -0.09724 -0.07457 109 TYR A CD1 
869  C CD2 . TYR A 109 ? 0.94023 1.48528 1.11930 0.29605  -0.08482 -0.06224 109 TYR A CD2 
870  C CE1 . TYR A 109 ? 0.87393 1.46369 1.12632 0.22191  -0.07943 -0.06958 109 TYR A CE1 
871  C CE2 . TYR A 109 ? 0.92352 1.46964 1.12257 0.27791  -0.06803 -0.05831 109 TYR A CE2 
872  C CZ  . TYR A 109 ? 0.89169 1.46127 1.12725 0.24121  -0.06503 -0.06168 109 TYR A CZ  
873  O OH  . TYR A 109 ? 0.87798 1.44606 1.12855 0.22373  -0.04737 -0.05746 109 TYR A OH  
874  N N   . LYS A 114 ? 0.99392 1.55220 1.11279 0.38185  -0.10283 -0.07001 114 LYS A N   
875  C CA  . LYS A 114 ? 1.03165 1.52022 1.09521 0.40819  -0.09223 -0.05646 114 LYS A CA  
876  C C   . LYS A 114 ? 0.99847 1.43205 1.04798 0.39102  -0.08049 -0.04409 114 LYS A C   
877  O O   . LYS A 114 ? 0.98135 1.39942 1.02549 0.37939  -0.08630 -0.04177 114 LYS A O   
878  C CB  . LYS A 114 ? 1.04912 1.54459 1.11136 0.42449  -0.08159 -0.05620 114 LYS A CB  
879  N N   . GLU A 115 ? 0.98488 1.38955 1.02751 0.39048  -0.06411 -0.03690 115 GLU A N   
880  C CA  . GLU A 115 ? 0.95444 1.30535 0.98187 0.37695  -0.05180 -0.02568 115 GLU A CA  
881  C C   . GLU A 115 ? 0.90996 1.26247 0.95466 0.36683  -0.03620 -0.02523 115 GLU A C   
882  O O   . GLU A 115 ? 0.94390 1.28621 0.97154 0.38663  -0.03021 -0.02534 115 GLU A O   
883  C CB  . GLU A 115 ? 1.01346 1.28515 0.97767 0.40009  -0.04711 -0.01277 115 GLU A CB  
884  C CG  . GLU A 115 ? 1.01186 1.22750 0.96050 0.38413  -0.03456 -0.00121 115 GLU A CG  
885  C CD  . GLU A 115 ? 1.08348 1.21529 0.97092 0.40394  -0.02368 0.01193  115 GLU A CD  
886  O OE1 . GLU A 115 ? 1.11046 1.21195 0.98242 0.41116  -0.01248 0.01362  115 GLU A OE1 
887  O OE2 . GLU A 115 ? 1.11773 1.21136 0.97012 0.41108  -0.02559 0.02039  115 GLU A OE2 
888  N N   . ALA A 116 ? 0.84760 1.20816 0.92073 0.33540  -0.02928 -0.02482 116 ALA A N   
889  C CA  . ALA A 116 ? 0.81829 1.17866 0.90526 0.31954  -0.01408 -0.02512 116 ALA A CA  
890  C C   . ALA A 116 ? 0.78192 1.07567 0.84509 0.29259  -0.00247 -0.01598 116 ALA A C   
891  O O   . ALA A 116 ? 0.75634 1.03359 0.81912 0.26985  -0.00560 -0.01242 116 ALA A O   
892  C CB  . ALA A 116 ? 0.78435 1.21778 0.92795 0.29472  -0.01460 -0.03444 116 ALA A CB  
893  N N   . THR A 117 ? 0.77788 1.03562 0.82140 0.29604  0.01032  -0.01333 117 THR A N   
894  C CA  . THR A 117 ? 0.74073 0.94068 0.76444 0.27053  0.02011  -0.00678 117 THR A CA  
895  C C   . THR A 117 ? 0.69306 0.90843 0.73773 0.25000  0.02989  -0.01062 117 THR A C   
896  O O   . THR A 117 ? 0.67994 0.92919 0.73780 0.26395  0.03392  -0.01624 117 THR A O   
897  C CB  . THR A 117 ? 0.77278 0.89883 0.74416 0.28913  0.02595  0.00023  117 THR A CB  
898  O OG1 . THR A 117 ? 0.79365 0.90795 0.75046 0.30860  0.03338  -0.00339 117 THR A OG1 
899  C CG2 . THR A 117 ? 0.79522 0.90956 0.74121 0.31845  0.01724  0.00442  117 THR A CG2 
900  N N   . TYR A 118 ? 0.66305 0.85599 0.71022 0.21815  0.03370  -0.00745 118 TYR A N   
901  C CA  . TYR A 118 ? 0.63593 0.83539 0.69667 0.19690  0.04221  -0.00978 118 TYR A CA  
902  C C   . TYR A 118 ? 0.64980 0.78906 0.68217 0.18301  0.04763  -0.00593 118 TYR A C   
903  O O   . TYR A 118 ? 0.65481 0.75869 0.66999 0.17757  0.04511  -0.00060 118 TYR A O   
904  C CB  . TYR A 118 ? 0.59246 0.83383 0.68954 0.16970  0.03956  -0.01118 118 TYR A CB  
905  C CG  . TYR A 118 ? 0.58572 0.88786 0.71428 0.17786  0.03271  -0.01641 118 TYR A CG  
906  C CD1 . TYR A 118 ? 0.58417 0.89652 0.71520 0.18468  0.02027  -0.01679 118 TYR A CD1 
907  C CD2 . TYR A 118 ? 0.57805 0.92943 0.73357 0.17942  0.03876  -0.02164 118 TYR A CD2 
908  C CE1 . TYR A 118 ? 0.57761 0.94911 0.73893 0.19185  0.01159  -0.02388 118 TYR A CE1 
909  C CE2 . TYR A 118 ? 0.56921 0.98249 0.75840 0.18469  0.03229  -0.02784 118 TYR A CE2 
910  C CZ  . TYR A 118 ? 0.57040 0.99426 0.76321 0.19055  0.01749  -0.02976 118 TYR A CZ  
911  O OH  . TYR A 118 ? 0.56461 1.05403 0.79300 0.19484  0.00883  -0.03816 118 TYR A OH  
912  N N   . LEU A 119 ? 0.65698 0.78734 0.68493 0.17726  0.05531  -0.00922 119 LEU A N   
913  C CA  . LEU A 119 ? 0.66102 0.74212 0.66656 0.16188  0.05902  -0.00862 119 LEU A CA  
914  C C   . LEU A 119 ? 0.61215 0.71459 0.63819 0.13674  0.06074  -0.00997 119 LEU A C   
915  O O   . LEU A 119 ? 0.59809 0.73306 0.63835 0.13856  0.06544  -0.01310 119 LEU A O   
916  C CB  . LEU A 119 ? 0.71600 0.76134 0.69047 0.18045  0.06485  -0.01301 119 LEU A CB  
917  C CG  . LEU A 119 ? 0.75704 0.73519 0.69549 0.17549  0.06652  -0.01295 119 LEU A CG  
918  C CD1 . LEU A 119 ? 0.77410 0.72238 0.69712 0.17972  0.06402  -0.00558 119 LEU A CD1 
919  C CD2 . LEU A 119 ? 0.80384 0.75144 0.71166 0.19738  0.07162  -0.01934 119 LEU A CD2 
920  N N   . ALA A 120 ? 0.58723 0.67272 0.61392 0.11478  0.05781  -0.00711 120 ALA A N   
921  C CA  . ALA A 120 ? 0.57005 0.67056 0.61078 0.09386  0.05840  -0.00777 120 ALA A CA  
922  C C   . ALA A 120 ? 0.58282 0.64777 0.60392 0.08400  0.05951  -0.01102 120 ALA A C   
923  O O   . ALA A 120 ? 0.60582 0.63544 0.61048 0.08182  0.05804  -0.01085 120 ALA A O   
924  C CB  . ALA A 120 ? 0.54948 0.66487 0.60784 0.07831  0.05272  -0.00332 120 ALA A CB  
925  N N   . LEU A 121 ? 0.56842 0.64249 0.59019 0.07762  0.06226  -0.01429 121 LEU A N   
926  C CA  . LEU A 121 ? 0.57134 0.61903 0.57790 0.06605  0.06003  -0.01872 121 LEU A CA  
927  C C   . LEU A 121 ? 0.53678 0.59629 0.55644 0.04753  0.05529  -0.01597 121 LEU A C   
928  O O   . LEU A 121 ? 0.52793 0.56995 0.54108 0.03656  0.05057  -0.01897 121 LEU A O   
929  C CB  . LEU A 121 ? 0.59026 0.63412 0.58075 0.07401  0.06476  -0.02505 121 LEU A CB  
930  C CG  . LEU A 121 ? 0.60653 0.62796 0.58010 0.06344  0.06027  -0.03190 121 LEU A CG  
931  C CD1 . LEU A 121 ? 0.62646 0.61005 0.58653 0.05646  0.05467  -0.03694 121 LEU A CD1 
932  C CD2 . LEU A 121 ? 0.63005 0.64865 0.58388 0.07469  0.06533  -0.03801 121 LEU A CD2 
933  N N   . ASN A 122 ? 0.51570 0.60446 0.55344 0.04391  0.05617  -0.01098 122 ASN A N   
934  C CA  . ASN A 122 ? 0.49534 0.59086 0.54159 0.02977  0.05159  -0.00788 122 ASN A CA  
935  C C   . ASN A 122 ? 0.47590 0.57671 0.53490 0.02647  0.04753  -0.00320 122 ASN A C   
936  O O   . ASN A 122 ? 0.47225 0.56196 0.53010 0.01938  0.04344  -0.00253 122 ASN A O   
937  C CB  . ASN A 122 ? 0.49296 0.60785 0.54407 0.02637  0.05583  -0.00538 122 ASN A CB  
938  C CG  . ASN A 122 ? 0.51094 0.61512 0.54423 0.02526  0.05680  -0.00854 122 ASN A CG  
939  O OD1 . ASN A 122 ? 0.52337 0.60867 0.54333 0.02573  0.05217  -0.01438 122 ASN A OD1 
940  N ND2 . ASN A 122 ? 0.51255 0.62750 0.54385 0.02328  0.06286  -0.00501 122 ASN A ND2 
941  N N   . GLU A 123 ? 0.46248 0.58227 0.53362 0.03214  0.04855  -0.00071 123 GLU A N   
942  C CA  . GLU A 123 ? 0.45483 0.57970 0.53479 0.02990  0.04354  0.00283  123 GLU A CA  
943  C C   . GLU A 123 ? 0.45833 0.60771 0.55155 0.03787  0.04302  0.00281  123 GLU A C   
944  O O   . GLU A 123 ? 0.45220 0.62134 0.55350 0.04085  0.04749  0.00077  123 GLU A O   
945  C CB  . GLU A 123 ? 0.43642 0.56440 0.52065 0.01743  0.04007  0.00491  123 GLU A CB  
946  C CG  . GLU A 123 ? 0.42765 0.57309 0.52066 0.01157  0.04179  0.00554  123 GLU A CG  
947  C CD  . GLU A 123 ? 0.43409 0.57990 0.52056 0.01067  0.04846  0.00441  123 GLU A CD  
948  O OE1 . GLU A 123 ? 0.43405 0.56502 0.50732 0.00820  0.04772  0.00371  123 GLU A OE1 
949  O OE2 . GLU A 123 ? 0.42885 0.59233 0.52325 0.01339  0.05451  0.00382  123 GLU A OE2 
950  N N   . SER A 124 ? 0.46678 0.61752 0.56251 0.04159  0.03754  0.00465  124 SER A N   
951  C CA  . SER A 124 ? 0.46700 0.64501 0.57702 0.04799  0.03339  0.00295  124 SER A CA  
952  C C   . SER A 124 ? 0.44688 0.63070 0.56389 0.03715  0.02692  0.00351  124 SER A C   
953  O O   . SER A 124 ? 0.43656 0.60265 0.54302 0.03720  0.02374  0.00634  124 SER A O   
954  C CB  . SER A 124 ? 0.48839 0.66159 0.58949 0.06736  0.03078  0.00333  124 SER A CB  
955  O OG  . SER A 124 ? 0.49358 0.69766 0.60972 0.07353  0.02364  0.00026  124 SER A OG  
956  N N   . THR A 125 ? 0.43994 0.64697 0.57331 0.02754  0.02592  0.00069  125 THR A N   
957  C CA  . THR A 125 ? 0.44271 0.64986 0.57910 0.01719  0.01919  -0.00017 125 THR A CA  
958  C C   . THR A 125 ? 0.45124 0.68674 0.60341 0.02028  0.01107  -0.00589 125 THR A C   
959  O O   . THR A 125 ? 0.46150 0.72481 0.62815 0.02777  0.01185  -0.00932 125 THR A O   
960  C CB  . THR A 125 ? 0.44504 0.64689 0.58248 0.00010  0.02357  0.00088  125 THR A CB  
961  O OG1 . THR A 125 ? 0.44881 0.67725 0.60480 -0.00809 0.02764  -0.00206 125 THR A OG1 
962  C CG2 . THR A 125 ? 0.44316 0.62525 0.56673 0.00029  0.03055  0.00472  125 THR A CG2 
963  N N   . VAL A 126 ? 0.45071 0.67979 0.59869 0.01638  0.00235  -0.00780 126 VAL A N   
964  C CA  . VAL A 126 ? 0.45349 0.70641 0.61331 0.01800  -0.00885 -0.01523 126 VAL A CA  
965  C C   . VAL A 126 ? 0.46171 0.70700 0.62263 -0.00059 -0.01323 -0.01881 126 VAL A C   
966  O O   . VAL A 126 ? 0.46745 0.68243 0.60906 -0.00251 -0.01341 -0.01534 126 VAL A O   
967  C CB  . VAL A 126 ? 0.46679 0.71143 0.61042 0.03728  -0.01728 -0.01494 126 VAL A CB  
968  C CG1 . VAL A 126 ? 0.46703 0.74660 0.62507 0.04713  -0.02835 -0.02327 126 VAL A CG1 
969  C CG2 . VAL A 126 ? 0.47331 0.69651 0.60008 0.05075  -0.00942 -0.00717 126 VAL A CG2 
970  N N   . LYS A 127 ? 0.47986 0.75265 0.66282 -0.01374 -0.01685 -0.02631 127 LYS A N   
971  C CA  . LYS A 127 ? 0.51938 0.78163 0.70106 -0.03143 -0.02338 -0.03184 127 LYS A CA  
972  C C   . LYS A 127 ? 0.57783 0.87482 0.77933 -0.03315 -0.03712 -0.04395 127 LYS A C   
973  O O   . LYS A 127 ? 0.56398 0.89598 0.78092 -0.01896 -0.04092 -0.04723 127 LYS A O   
974  C CB  . LYS A 127 ? 0.51967 0.77270 0.70626 -0.05418 -0.01219 -0.02897 127 LYS A CB  
975  C CG  . LYS A 127 ? 0.51212 0.73134 0.67648 -0.05087 -0.00171 -0.01865 127 LYS A CG  
976  C CD  . LYS A 127 ? 0.51887 0.72974 0.68460 -0.06967 0.01017  -0.01485 127 LYS A CD  
977  C CE  . LYS A 127 ? 0.51200 0.71111 0.66565 -0.06062 0.02119  -0.00611 127 LYS A CE  
978  N NZ  . LYS A 127 ? 0.52694 0.70822 0.67091 -0.07440 0.03305  -0.00041 127 LYS A NZ  
979  N N   . SER A 128 ? 0.65693 0.94331 0.85647 -0.04989 -0.04534 -0.05148 128 SER A N   
980  C CA  . SER A 128 ? 0.75700 1.07706 0.97621 -0.05491 -0.06075 -0.06562 128 SER A CA  
981  C C   . SER A 128 ? 0.83503 1.18973 1.08971 -0.08148 -0.05551 -0.07147 128 SER A C   
982  O O   . SER A 128 ? 0.85155 1.18916 1.10642 -0.10011 -0.04064 -0.06463 128 SER A O   
983  C CB  . SER A 128 ? 0.77807 1.06745 0.97447 -0.05877 -0.07446 -0.07324 128 SER A CB  
984  O OG  . SER A 128 ? 0.80429 1.12781 1.02155 -0.06748 -0.09090 -0.08935 128 SER A OG  
985  N N   . SER A 129 ? 0.88332 1.28898 1.16779 -0.08226 -0.06751 -0.08410 129 SER A N   
986  C CA  . SER A 129 ? 0.93380 1.38270 1.25846 -0.10981 -0.06409 -0.09227 129 SER A CA  
987  C C   . SER A 129 ? 1.00627 1.44657 1.33254 -0.13365 -0.07929 -0.10672 129 SER A C   
988  O O   . SER A 129 ? 1.01220 1.47889 1.34607 -0.12533 -0.09985 -0.12070 129 SER A O   
989  C CB  . SER A 129 ? 0.91172 1.43002 1.27222 -0.09460 -0.06820 -0.09857 129 SER A CB  
990  O OG  . SER A 129 ? 0.92548 1.46608 1.28751 -0.07983 -0.09163 -0.11194 129 SER A OG  
991  N N   . GLY A 130 ? 1.04820 1.44768 1.36323 -0.16201 -0.06982 -0.10376 130 GLY A N   
992  C CA  . GLY A 130 ? 1.10752 1.48848 1.41908 -0.18715 -0.08301 -0.11768 130 GLY A CA  
993  C C   . GLY A 130 ? 1.14850 1.47160 1.41312 -0.17184 -0.09553 -0.11892 130 GLY A C   
994  O O   . GLY A 130 ? 1.17869 1.44232 1.41151 -0.18209 -0.08835 -0.11289 130 GLY A O   
995  N N   . GLY A 131 ? 1.07071 1.41013 1.32785 -0.14469 -0.11349 -0.12614 131 GLY A N   
996  C CA  . GLY A 131 ? 1.02441 1.31705 1.23966 -0.13073 -0.12665 -0.13014 131 GLY A CA  
997  C C   . GLY A 131 ? 0.96523 1.20931 1.14220 -0.10881 -0.11347 -0.11228 131 GLY A C   
998  O O   . GLY A 131 ? 0.97341 1.21788 1.15566 -0.10584 -0.09540 -0.09759 131 GLY A O   
999  N N   . PRO A 132 ? 0.89813 1.10168 1.03627 -0.09323 -0.12257 -0.11430 132 PRO A N   
1000 C CA  . PRO A 132 ? 0.81721 0.98407 0.92337 -0.07120 -0.11087 -0.09861 132 PRO A CA  
1001 C C   . PRO A 132 ? 0.73557 0.93139 0.84764 -0.04411 -0.10761 -0.08998 132 PRO A C   
1002 O O   . PRO A 132 ? 0.73368 0.96628 0.85912 -0.03280 -0.11936 -0.09752 132 PRO A O   
1003 C CB  . PRO A 132 ? 0.84957 0.97386 0.91549 -0.06092 -0.12273 -0.10572 132 PRO A CB  
1004 C CG  . PRO A 132 ? 0.89590 1.02140 0.96945 -0.08457 -0.13864 -0.12470 132 PRO A CG  
1005 C CD  . PRO A 132 ? 0.89944 1.08876 1.01975 -0.09445 -0.14343 -0.13141 132 PRO A CD  
1006 N N   . PHE A 133 ? 0.66726 0.84435 0.76732 -0.03341 -0.09195 -0.07448 133 PHE A N   
1007 C CA  . PHE A 133 ? 0.60834 0.80288 0.71035 -0.01088 -0.08578 -0.06478 133 PHE A CA  
1008 C C   . PHE A 133 ? 0.60435 0.77478 0.67254 0.01302  -0.08938 -0.06152 133 PHE A C   
1009 O O   . PHE A 133 ? 0.60951 0.74574 0.65437 0.01515  -0.08342 -0.05611 133 PHE A O   
1010 C CB  . PHE A 133 ? 0.57007 0.75909 0.67934 -0.01562 -0.06731 -0.05157 133 PHE A CB  
1011 C CG  . PHE A 133 ? 0.53557 0.73321 0.64327 0.00441  -0.05963 -0.04168 133 PHE A CG  
1012 C CD1 . PHE A 133 ? 0.51446 0.74696 0.64208 0.01228  -0.06083 -0.04306 133 PHE A CD1 
1013 C CD2 . PHE A 133 ? 0.52196 0.69240 0.60810 0.01506  -0.05070 -0.03134 133 PHE A CD2 
1014 C CE1 . PHE A 133 ? 0.49646 0.72780 0.61713 0.03058  -0.05316 -0.03387 133 PHE A CE1 
1015 C CE2 . PHE A 133 ? 0.50096 0.67457 0.58472 0.02962  -0.04282 -0.02265 133 PHE A CE2 
1016 C CZ  . PHE A 133 ? 0.49191 0.69167 0.59038 0.03735  -0.04392 -0.02368 133 PHE A CZ  
1017 N N   . VAL A 134 ? 0.59705 0.78615 0.66108 0.03211  -0.09923 -0.06520 134 VAL A N   
1018 C CA  . VAL A 134 ? 0.58869 0.75744 0.61893 0.05654  -0.10102 -0.06105 134 VAL A CA  
1019 C C   . VAL A 134 ? 0.57356 0.76025 0.60453 0.07725  -0.09767 -0.05358 134 VAL A C   
1020 O O   . VAL A 134 ? 0.57587 0.79142 0.61663 0.08552  -0.11011 -0.06170 134 VAL A O   
1021 C CB  . VAL A 134 ? 0.60313 0.76553 0.61358 0.06222  -0.11997 -0.07543 134 VAL A CB  
1022 C CG1 . VAL A 134 ? 0.61514 0.74758 0.58503 0.08560  -0.11673 -0.06887 134 VAL A CG1 
1023 C CG2 . VAL A 134 ? 0.60956 0.75974 0.62588 0.03701  -0.12735 -0.08745 134 VAL A CG2 
1024 N N   . VAL A 135 ? 0.55967 0.72879 0.57884 0.08632  -0.08165 -0.03887 135 VAL A N   
1025 C CA  . VAL A 135 ? 0.56408 0.73681 0.57289 0.10775  -0.07753 -0.03077 135 VAL A CA  
1026 C C   . VAL A 135 ? 0.57914 0.72100 0.55471 0.12214  -0.06733 -0.01969 135 VAL A C   
1027 O O   . VAL A 135 ? 0.57484 0.69856 0.54431 0.11395  -0.05895 -0.01573 135 VAL A O   
1028 C CB  . VAL A 135 ? 0.54599 0.73035 0.57654 0.10296  -0.06591 -0.02357 135 VAL A CB  
1029 C CG1 . VAL A 135 ? 0.53504 0.75442 0.59991 0.08867  -0.07350 -0.03405 135 VAL A CG1 
1030 C CG2 . VAL A 135 ? 0.52881 0.69190 0.55985 0.09075  -0.04929 -0.01344 135 VAL A CG2 
1031 N N   . ASP A 136 ? 0.60676 0.74387 0.55919 0.14520  -0.06822 -0.01497 136 ASP A N   
1032 C CA  . ASP A 136 ? 0.62110 0.73051 0.54452 0.15792  -0.05290 -0.00073 136 ASP A CA  
1033 C C   . ASP A 136 ? 0.59975 0.70283 0.53421 0.15200  -0.03608 0.01113  136 ASP A C   
1034 O O   . ASP A 136 ? 0.59082 0.70690 0.53922 0.15377  -0.03866 0.00975  136 ASP A O   
1035 C CB  . ASP A 136 ? 0.66396 0.76511 0.55245 0.18577  -0.05919 0.00090  136 ASP A CB  
1036 C CG  . ASP A 136 ? 0.68454 0.78723 0.55459 0.19430  -0.07631 -0.01152 136 ASP A CG  
1037 O OD1 . ASP A 136 ? 0.68198 0.77471 0.54921 0.18440  -0.07494 -0.01470 136 ASP A OD1 
1038 O OD2 . ASP A 136 ? 0.71079 0.82339 0.56617 0.21318  -0.09193 -0.01871 136 ASP A OD2 
1039 N N   . VAL A 137 ? 0.59040 0.67499 0.51887 0.14533  -0.01922 0.02173  137 VAL A N   
1040 C CA  . VAL A 137 ? 0.58447 0.66058 0.52313 0.13613  -0.00387 0.03120  137 VAL A CA  
1041 C C   . VAL A 137 ? 0.62320 0.67298 0.53186 0.14991  0.00980  0.04452  137 VAL A C   
1042 O O   . VAL A 137 ? 0.64562 0.68366 0.53385 0.15561  0.01709  0.05032  137 VAL A O   
1043 C CB  . VAL A 137 ? 0.56397 0.64247 0.52203 0.11551  0.00451  0.03202  137 VAL A CB  
1044 C CG1 . VAL A 137 ? 0.55678 0.62701 0.52454 0.10526  0.01829  0.03959  137 VAL A CG1 
1045 C CG2 . VAL A 137 ? 0.54375 0.64073 0.52501 0.10253  -0.00731 0.02056  137 VAL A CG2 
1046 N N   . VAL A 138 ? 0.63833 0.67643 0.54162 0.15601  0.01445  0.04975  138 VAL A N   
1047 C CA  . VAL A 138 ? 0.68312 0.68838 0.55260 0.16959  0.02792  0.06319  138 VAL A CA  
1048 C C   . VAL A 138 ? 0.68923 0.67476 0.56534 0.15480  0.04395  0.07090  138 VAL A C   
1049 O O   . VAL A 138 ? 0.67617 0.66622 0.56723 0.15155  0.03995  0.06624  138 VAL A O   
1050 C CB  . VAL A 138 ? 0.70875 0.70762 0.55231 0.19748  0.01757  0.06273  138 VAL A CB  
1051 C CG1 . VAL A 138 ? 0.75206 0.70963 0.55295 0.21248  0.03310  0.07838  138 VAL A CG1 
1052 C CG2 . VAL A 138 ? 0.70155 0.72431 0.54186 0.21057  -0.00213 0.05147  138 VAL A CG2 
1053 N N   . ILE A 139 ? 0.71106 0.67445 0.57404 0.14684  0.06225  0.08225  139 ILE A N   
1054 C CA  . ILE A 139 ? 0.71266 0.65706 0.58307 0.12770  0.07805  0.08841  139 ILE A CA  
1055 C C   . ILE A 139 ? 0.75953 0.65923 0.59029 0.13842  0.09331  0.10260  139 ILE A C   
1056 O O   . ILE A 139 ? 0.78606 0.67333 0.59567 0.14173  0.10559  0.11259  139 ILE A O   
1057 C CB  . ILE A 139 ? 0.69754 0.65856 0.59190 0.10450  0.08753  0.08867  139 ILE A CB  
1058 C CG1 . ILE A 139 ? 0.65078 0.64883 0.57592 0.09764  0.07274  0.07600  139 ILE A CG1 
1059 C CG2 . ILE A 139 ? 0.70860 0.65446 0.61375 0.08302  0.10070  0.09202  139 ILE A CG2 
1060 C CD1 . ILE A 139 ? 0.62682 0.64354 0.56978 0.08294  0.07991  0.07609  139 ILE A CD1 
1061 N N   . ASN A 140 ? 0.78467 0.65708 0.60240 0.14422  0.09433  0.10424  140 ASN A N   
1062 C CA  . ASN A 140 ? 0.84722 0.66781 0.61985 0.15725  0.10856  0.11832  140 ASN A CA  
1063 C C   . ASN A 140 ? 0.87863 0.69305 0.61578 0.18460  0.10614  0.12499  140 ASN A C   
1064 O O   . ASN A 140 ? 0.92480 0.70997 0.63172 0.18601  0.12369  0.13888  140 ASN A O   
1065 C CB  . ASN A 140 ? 0.87425 0.66712 0.64472 0.13090  0.13221  0.12874  140 ASN A CB  
1066 C CG  . ASN A 140 ? 0.86099 0.65840 0.66347 0.10374  0.13347  0.12090  140 ASN A CG  
1067 O OD1 . ASN A 140 ? 0.86649 0.65125 0.66725 0.10926  0.12601  0.11502  140 ASN A OD1 
1068 N ND2 . ASN A 140 ? 0.83771 0.65514 0.66868 0.07609  0.14246  0.12005  140 ASN A ND2 
1069 N N   . ASP A 141 ? 0.86007 0.70451 0.60163 0.20539  0.08430  0.11434  141 ASP A N   
1070 C CA  . ASP A 141 ? 0.90749 0.75097 0.61565 0.23474  0.07586  0.11647  141 ASP A CA  
1071 C C   . ASP A 141 ? 0.92719 0.78283 0.63274 0.22962  0.08135  0.11908  141 ASP A C   
1072 O O   . ASP A 141 ? 0.98094 0.82340 0.64810 0.25320  0.08080  0.12473  141 ASP A O   
1073 C CB  . ASP A 141 ? 0.96550 0.75611 0.61848 0.26004  0.08589  0.13090  141 ASP A CB  
1074 C CG  . ASP A 141 ? 0.97173 0.75447 0.61960 0.27779  0.07494  0.12604  141 ASP A CG  
1075 O OD1 . ASP A 141 ? 0.92286 0.75049 0.60715 0.27776  0.05564  0.11035  141 ASP A OD1 
1076 O OD2 . ASP A 141 ? 1.02688 0.75749 0.63286 0.29234  0.08661  0.13817  141 ASP A OD2 
1077 N N   . ILE A 142 ? 0.90135 0.78292 0.64460 0.20255  0.08542  0.11426  142 ILE A N   
1078 C CA  A ILE A 142 ? 0.88789 0.78299 0.63023 0.19892  0.09145  0.11599  142 ILE A CA  
1079 C CA  B ILE A 142 ? 0.88673 0.78215 0.63065 0.19743  0.09215  0.11609  142 ILE A CA  
1080 C C   . ILE A 142 ? 0.83165 0.76914 0.60680 0.19403  0.07094  0.09888  142 ILE A C   
1081 O O   . ILE A 142 ? 0.77613 0.73467 0.58979 0.17375  0.06630  0.09066  142 ILE A O   
1082 C CB  A ILE A 142 ? 0.88499 0.77274 0.63956 0.17332  0.11627  0.12627  142 ILE A CB  
1083 C CB  B ILE A 142 ? 0.88484 0.77676 0.64716 0.16928  0.11525  0.12454  142 ILE A CB  
1084 C CG1 A ILE A 142 ? 0.93575 0.77502 0.65622 0.17405  0.13810  0.14343  142 ILE A CG1 
1085 C CG1 B ILE A 142 ? 0.92776 0.77478 0.65635 0.16820  0.14051  0.14304  142 ILE A CG1 
1086 C CG2 A ILE A 142 ? 0.89306 0.80019 0.64783 0.17304  0.12287  0.12751  142 ILE A CG2 
1087 C CG2 B ILE A 142 ? 0.86422 0.78712 0.64422 0.16155  0.11745  0.12091  142 ILE A CG2 
1088 C CD1 A ILE A 142 ? 0.99959 0.80608 0.66411 0.20636  0.13985  0.15362  142 ILE A CD1 
1089 C CD1 B ILE A 142 ? 0.92670 0.77356 0.68324 0.13405  0.16049  0.14787  142 ILE A CD1 
1090 N N   . HIS A 143 ? 0.83407 0.78071 0.59031 0.21320  0.05820  0.09306  143 HIS A N   
1091 C CA  . HIS A 143 ? 0.78913 0.76865 0.57163 0.20739  0.03899  0.07645  143 HIS A CA  
1092 C C   . HIS A 143 ? 0.73153 0.72329 0.53563 0.18805  0.04969  0.07684  143 HIS A C   
1093 O O   . HIS A 143 ? 0.75176 0.73678 0.53671 0.19368  0.06257  0.08421  143 HIS A O   
1094 C CB  A HIS A 143 ? 0.82243 0.80633 0.57838 0.23060  0.02142  0.06777  143 HIS A CB  
1095 C CB  B HIS A 143 ? 0.82553 0.80713 0.57866 0.23177  0.02269  0.06902  143 HIS A CB  
1096 C CG  A HIS A 143 ? 0.80194 0.81136 0.58112 0.22127  0.00390  0.05097  143 HIS A CG  
1097 C CG  B HIS A 143 ? 0.85366 0.83671 0.59383 0.25163  0.00506  0.06322  143 HIS A CG  
1098 N ND1 A HIS A 143 ? 0.79466 0.80763 0.57936 0.21201  0.01058  0.05004  143 HIS A ND1 
1099 N ND1 B HIS A 143 ? 0.84422 0.85332 0.59483 0.25747  -0.02071 0.04548  143 HIS A ND1 
1100 C CD2 A HIS A 143 ? 0.79037 0.82095 0.58710 0.21962  -0.01927 0.03457  143 HIS A CD2 
1101 C CD2 B HIS A 143 ? 0.88507 0.84782 0.60248 0.26787  0.00914  0.07220  143 HIS A CD2 
1102 C CE1 A HIS A 143 ? 0.77881 0.80703 0.57898 0.20569  -0.00761 0.03439  143 HIS A CE1 
1103 C CE1 B HIS A 143 ? 0.86687 0.87865 0.60556 0.27704  -0.03249 0.04316  143 HIS A CE1 
1104 N NE2 A HIS A 143 ? 0.77567 0.81520 0.58472 0.20798  -0.02544 0.02478  143 HIS A NE2 
1105 N NE2 B HIS A 143 ? 0.89026 0.87221 0.60639 0.28574  -0.01484 0.05959  143 HIS A NE2 
1106 N N   . PHE A 144 ? 0.66327 0.67521 0.50543 0.16811  0.04341  0.06821  144 PHE A N   
1107 C CA  . PHE A 144 ? 0.61324 0.63810 0.47860 0.15018  0.05305  0.06867  144 PHE A CA  
1108 C C   . PHE A 144 ? 0.57670 0.61795 0.45071 0.14992  0.03950  0.05649  144 PHE A C   
1109 O O   . PHE A 144 ? 0.58130 0.62702 0.45142 0.15130  0.04704  0.05814  144 PHE A O   
1110 C CB  . PHE A 144 ? 0.58456 0.61501 0.48124 0.12893  0.05727  0.06876  144 PHE A CB  
1111 C CG  . PHE A 144 ? 0.55753 0.60447 0.47883 0.11195  0.06495  0.06817  144 PHE A CG  
1112 C CD1 . PHE A 144 ? 0.56903 0.61515 0.48966 0.10558  0.08440  0.07822  144 PHE A CD1 
1113 C CD2 . PHE A 144 ? 0.52430 0.58878 0.46869 0.10293  0.05307  0.05764  144 PHE A CD2 
1114 C CE1 . PHE A 144 ? 0.54499 0.61336 0.49080 0.09194  0.08987  0.07632  144 PHE A CE1 
1115 C CE2 . PHE A 144 ? 0.50290 0.58300 0.46670 0.09137  0.05868  0.05686  144 PHE A CE2 
1116 C CZ  . PHE A 144 ? 0.51367 0.59876 0.47980 0.08664  0.07608  0.06547  144 PHE A CZ  
1117 N N   . GLU A 145 ? 0.55002 0.59997 0.43586 0.14755  0.02058  0.04419  145 GLU A N   
1118 C CA  . GLU A 145 ? 0.54416 0.60133 0.43380 0.14556  0.00807  0.03259  145 GLU A CA  
1119 C C   . GLU A 145 ? 0.54860 0.61155 0.44144 0.14697  -0.01255 0.02006  145 GLU A C   
1120 O O   . GLU A 145 ? 0.54411 0.61250 0.44430 0.14784  -0.01616 0.02041  145 GLU A O   
1121 C CB  . GLU A 145 ? 0.50885 0.57609 0.42589 0.12723  0.01237  0.03124  145 GLU A CB  
1122 C CG  . GLU A 145 ? 0.47591 0.55188 0.42122 0.11064  0.01013  0.02956  145 GLU A CG  
1123 C CD  . GLU A 145 ? 0.44039 0.52461 0.40780 0.09516  0.01485  0.02919  145 GLU A CD  
1124 O OE1 . GLU A 145 ? 0.44004 0.52628 0.40413 0.09728  0.02088  0.03103  145 GLU A OE1 
1125 O OE2 . GLU A 145 ? 0.41206 0.50221 0.39916 0.08277  0.01238  0.02684  145 GLU A OE2 
1126 N N   . ARG A 146 ? 0.56099 0.62301 0.44773 0.14759  -0.02602 0.00837  146 ARG A N   
1127 C CA  . ARG A 146 ? 0.56046 0.63265 0.45888 0.14118  -0.04543 -0.00560 146 ARG A CA  
1128 C C   . ARG A 146 ? 0.53956 0.61390 0.46094 0.12003  -0.04718 -0.01127 146 ARG A C   
1129 O O   . ARG A 146 ? 0.55231 0.61275 0.46168 0.11937  -0.04926 -0.01573 146 ARG A O   
1130 C CB  . ARG A 146 ? 0.59212 0.65772 0.46318 0.15611  -0.06174 -0.01671 146 ARG A CB  
1131 C CG  . ARG A 146 ? 0.59163 0.67054 0.47978 0.14370  -0.08212 -0.03344 146 ARG A CG  
1132 C CD  . ARG A 146 ? 0.62465 0.70276 0.48797 0.15940  -0.10115 -0.04598 146 ARG A CD  
1133 N NE  . ARG A 146 ? 0.64133 0.73089 0.49479 0.17904  -0.10342 -0.04149 146 ARG A NE  
1134 C CZ  . ARG A 146 ? 0.69083 0.78364 0.52060 0.19789  -0.12045 -0.05104 146 ARG A CZ  
1135 N NH1 . ARG A 146 ? 0.71839 0.80411 0.53283 0.19792  -0.13746 -0.06698 146 ARG A NH1 
1136 N NH2 . ARG A 146 ? 0.70676 0.80746 0.52482 0.21839  -0.12121 -0.04506 146 ARG A NH2 
1137 N N   . PHE A 147 ? 0.50937 0.59819 0.45968 0.10495  -0.04558 -0.01062 147 PHE A N   
1138 C CA  . PHE A 147 ? 0.49661 0.58518 0.46601 0.08574  -0.04357 -0.01275 147 PHE A CA  
1139 C C   . PHE A 147 ? 0.50892 0.60032 0.48598 0.07338  -0.05856 -0.02628 147 PHE A C   
1140 O O   . PHE A 147 ? 0.50465 0.61622 0.49671 0.07011  -0.06740 -0.03261 147 PHE A O   
1141 C CB  . PHE A 147 ? 0.47476 0.57586 0.46861 0.07548  -0.03356 -0.00573 147 PHE A CB  
1142 C CG  . PHE A 147 ? 0.46162 0.56155 0.47111 0.05774  -0.03129 -0.00730 147 PHE A CG  
1143 C CD1 . PHE A 147 ? 0.45812 0.56586 0.48233 0.04357  -0.03922 -0.01556 147 PHE A CD1 
1144 C CD2 . PHE A 147 ? 0.45169 0.54385 0.46048 0.05544  -0.02089 -0.00050 147 PHE A CD2 
1145 C CE1 . PHE A 147 ? 0.45434 0.55597 0.48730 0.02819  -0.03515 -0.01528 147 PHE A CE1 
1146 C CE2 . PHE A 147 ? 0.44344 0.53166 0.46088 0.04257  -0.01929 -0.00137 147 PHE A CE2 
1147 C CZ  . PHE A 147 ? 0.44708 0.53693 0.47419 0.02922  -0.02561 -0.00793 147 PHE A CZ  
1148 N N   . ARG A 148 ? 0.52925 0.60107 0.49738 0.06552  -0.06052 -0.03064 148 ARG A N   
1149 C CA  . ARG A 148 ? 0.55774 0.62535 0.53260 0.04823  -0.07198 -0.04269 148 ARG A CA  
1150 C C   . ARG A 148 ? 0.57186 0.62401 0.55207 0.03294  -0.06359 -0.03885 148 ARG A C   
1151 O O   . ARG A 148 ? 0.57541 0.60235 0.53445 0.03939  -0.05966 -0.03612 148 ARG A O   
1152 C CB  . ARG A 148 ? 0.58434 0.63152 0.53151 0.05554  -0.08559 -0.05419 148 ARG A CB  
1153 C CG  . ARG A 148 ? 0.60301 0.64611 0.55788 0.03508  -0.09868 -0.06839 148 ARG A CG  
1154 C CD  . ARG A 148 ? 0.64229 0.66117 0.56517 0.04443  -0.11265 -0.08052 148 ARG A CD  
1155 N NE  . ARG A 148 ? 0.66661 0.67100 0.59157 0.02156  -0.12495 -0.09537 148 ARG A NE  
1156 C CZ  . ARG A 148 ? 0.66531 0.69462 0.60993 0.00840  -0.13983 -0.10902 148 ARG A CZ  
1157 N NH1 . ARG A 148 ? 0.64388 0.71351 0.60516 0.01977  -0.14544 -0.10970 148 ARG A NH1 
1158 N NH2 . ARG A 148 ? 0.69015 0.70337 0.63714 -0.01660 -0.14937 -0.12262 148 ARG A NH2 
1159 N N   . GLY A 149 ? 0.58348 0.65112 0.58969 0.01510  -0.06052 -0.03846 149 GLY A N   
1160 C CA  . GLY A 149 ? 0.57732 0.63017 0.58597 0.00221  -0.05134 -0.03328 149 GLY A CA  
1161 C C   . GLY A 149 ? 0.55781 0.62938 0.59361 -0.01845 -0.04887 -0.03490 149 GLY A C   
1162 O O   . GLY A 149 ? 0.56354 0.65441 0.61502 -0.02792 -0.05761 -0.04414 149 GLY A O   
1163 N N   . ASP A 150 ? 0.52300 0.59186 0.56473 -0.02496 -0.03704 -0.02653 150 ASP A N   
1164 C CA  . ASP A 150 ? 0.49240 0.58148 0.55894 -0.04231 -0.03134 -0.02629 150 ASP A CA  
1165 C C   . ASP A 150 ? 0.46117 0.58571 0.54983 -0.03423 -0.02715 -0.02286 150 ASP A C   
1166 O O   . ASP A 150 ? 0.45580 0.60898 0.56864 -0.04359 -0.02687 -0.02662 150 ASP A O   
1167 C CB  . ASP A 150 ? 0.48178 0.54751 0.53872 -0.05192 -0.02032 -0.01904 150 ASP A CB  
1168 C CG  . ASP A 150 ? 0.52554 0.55227 0.56020 -0.06370 -0.02321 -0.02271 150 ASP A CG  
1169 O OD1 . ASP A 150 ? 0.55052 0.57052 0.58063 -0.06766 -0.03435 -0.03257 150 ASP A OD1 
1170 O OD2 . ASP A 150 ? 0.54302 0.54250 0.56124 -0.06801 -0.01483 -0.01611 150 ASP A OD2 
1171 N N   . GLY A 151 ? 0.45679 0.58035 0.53778 -0.01726 -0.02346 -0.01626 151 GLY A N   
1172 C CA  . GLY A 151 ? 0.43441 0.58331 0.53061 -0.00881 -0.02014 -0.01374 151 GLY A CA  
1173 C C   . GLY A 151 ? 0.41205 0.55144 0.49812 0.00347  -0.01281 -0.00546 151 GLY A C   
1174 O O   . GLY A 151 ? 0.40178 0.52243 0.47176 0.00806  -0.01168 -0.00232 151 GLY A O   
1175 N N   . LEU A 152 ? 0.40818 0.56188 0.50436 0.00874  -0.00780 -0.00272 152 LEU A N   
1176 C CA  . LEU A 152 ? 0.41385 0.55823 0.50204 0.01746  -0.00095 0.00386  152 LEU A CA  
1177 C C   . LEU A 152 ? 0.41328 0.56426 0.51086 0.01464  0.00664  0.00573  152 LEU A C   
1178 O O   . LEU A 152 ? 0.41967 0.58826 0.53032 0.01297  0.00687  0.00266  152 LEU A O   
1179 C CB  . LEU A 152 ? 0.42339 0.56699 0.50281 0.03230  -0.00312 0.00559  152 LEU A CB  
1180 C CG  . LEU A 152 ? 0.43792 0.57007 0.50096 0.03902  -0.00766 0.00570  152 LEU A CG  
1181 C CD1 . LEU A 152 ? 0.44963 0.58350 0.50264 0.05457  -0.01103 0.00650  152 LEU A CD1 
1182 C CD2 . LEU A 152 ? 0.43570 0.55411 0.48957 0.03894  -0.00003 0.01162  152 LEU A CD2 
1183 N N   . CYS A 153 ? 0.41558 0.55435 0.50656 0.01459  0.01263  0.00987  153 CYS A N   
1184 C CA  . CYS A 153 ? 0.41243 0.55166 0.50677 0.01253  0.01906  0.01057  153 CYS A CA  
1185 C C   . CYS A 153 ? 0.42244 0.55020 0.50947 0.01875  0.02280  0.01349  153 CYS A C   
1186 O O   . CYS A 153 ? 0.42226 0.54161 0.50348 0.01789  0.02357  0.01607  153 CYS A O   
1187 C CB  . CYS A 153 ? 0.40398 0.53722 0.49528 0.00376  0.02141  0.01097  153 CYS A CB  
1188 S SG  . CYS A 153 ? 0.39566 0.52615 0.48498 0.00262  0.02785  0.01051  153 CYS A SG  
1189 N N   . MET A 154 ? 0.43968 0.56662 0.52630 0.02515  0.02583  0.01306  154 MET A N   
1190 C CA  . MET A 154 ? 0.46697 0.57529 0.54331 0.02849  0.03082  0.01553  154 MET A CA  
1191 C C   . MET A 154 ? 0.47273 0.57598 0.54853 0.02411  0.03461  0.01237  154 MET A C   
1192 O O   . MET A 154 ? 0.46503 0.57571 0.54309 0.02946  0.03582  0.00973  154 MET A O   
1193 C CB  . MET A 154 ? 0.49341 0.59510 0.56094 0.04284  0.03114  0.01756  154 MET A CB  
1194 C CG  . MET A 154 ? 0.52743 0.60076 0.57873 0.04460  0.03773  0.02219  154 MET A CG  
1195 S SD  . MET A 154 ? 0.53678 0.60284 0.58514 0.03548  0.04115  0.02758  154 MET A SD  
1196 C CE  . MET A 154 ? 0.55691 0.61114 0.58661 0.05218  0.04194  0.03424  154 MET A CE  
1197 N N   . SER A 155 ? 0.47054 0.56393 0.54353 0.01527  0.03615  0.01184  155 SER A N   
1198 C CA  . SER A 155 ? 0.46305 0.55223 0.53347 0.01025  0.03724  0.00719  155 SER A CA  
1199 C C   . SER A 155 ? 0.47966 0.54611 0.54010 0.00839  0.04062  0.00523  155 SER A C   
1200 O O   . SER A 155 ? 0.49036 0.54627 0.54900 0.00446  0.04289  0.00838  155 SER A O   
1201 C CB  . SER A 155 ? 0.45066 0.54862 0.52509 0.00185  0.03370  0.00599  155 SER A CB  
1202 O OG  . SER A 155 ? 0.45917 0.55157 0.52853 -0.00272 0.03297  0.00067  155 SER A OG  
1203 N N   . THR A 156 ? 0.47573 0.53229 0.52761 0.01087  0.04196  0.00000  156 THR A N   
1204 C CA  . THR A 156 ? 0.49860 0.52856 0.53814 0.00620  0.04391  -0.00438 156 THR A CA  
1205 C C   . THR A 156 ? 0.49158 0.52702 0.53732 -0.00874 0.03963  -0.00935 156 THR A C   
1206 O O   . THR A 156 ? 0.47514 0.53293 0.53050 -0.01091 0.03536  -0.00915 156 THR A O   
1207 C CB  . THR A 156 ? 0.52729 0.54366 0.55215 0.01617  0.04587  -0.00989 156 THR A CB  
1208 O OG1 . THR A 156 ? 0.51272 0.54305 0.53883 0.01393  0.04310  -0.01492 156 THR A OG1 
1209 C CG2 . THR A 156 ? 0.53237 0.55530 0.55586 0.03367  0.04903  -0.00608 156 THR A CG2 
1210 N N   . PRO A 157 ? 0.51199 0.52674 0.55147 -0.01920 0.04014  -0.01466 157 PRO A N   
1211 C CA  . PRO A 157 ? 0.51604 0.54219 0.56357 -0.03285 0.03379  -0.02243 157 PRO A CA  
1212 C C   . PRO A 157 ? 0.50402 0.54276 0.54674 -0.02690 0.02740  -0.02836 157 PRO A C   
1213 O O   . PRO A 157 ? 0.48298 0.54556 0.53486 -0.02803 0.02200  -0.02840 157 PRO A O   
1214 C CB  . PRO A 157 ? 0.55416 0.54976 0.59153 -0.04464 0.03545  -0.02942 157 PRO A CB  
1215 C CG  . PRO A 157 ? 0.57045 0.53907 0.59696 -0.03955 0.04472  -0.02122 157 PRO A CG  
1216 C CD  . PRO A 157 ? 0.54667 0.52572 0.57063 -0.01958 0.04622  -0.01408 157 PRO A CD  
1217 N N   . SER A 158 ? 0.52378 0.54479 0.54873 -0.01846 0.02874  -0.03295 158 SER A N   
1218 C CA  . SER A 158 ? 0.52017 0.55064 0.53610 -0.01170 0.02490  -0.03750 158 SER A CA  
1219 C C   . SER A 158 ? 0.49231 0.54424 0.51481 -0.00343 0.02793  -0.02863 158 SER A C   
1220 O O   . SER A 158 ? 0.49404 0.55516 0.50968 0.00007  0.02567  -0.02967 158 SER A O   
1221 C CB  . SER A 158 ? 0.54943 0.55589 0.54268 -0.00263 0.02753  -0.04427 158 SER A CB  
1222 O OG  . SER A 158 ? 0.55122 0.55213 0.54173 0.00984  0.03611  -0.03783 158 SER A OG  
1223 N N   . GLY A 159 ? 0.47975 0.53738 0.51293 -0.00057 0.03283  -0.02028 159 GLY A N   
1224 C CA  . GLY A 159 ? 0.45816 0.53481 0.49933 0.00292  0.03449  -0.01333 159 GLY A CA  
1225 C C   . GLY A 159 ? 0.44177 0.53115 0.49188 -0.00299 0.02940  -0.01038 159 GLY A C   
1226 O O   . GLY A 159 ? 0.43701 0.53572 0.48885 -0.00109 0.03014  -0.00554 159 GLY A O   
1227 N N   . THR A 160 ? 0.43611 0.52610 0.49169 -0.01020 0.02484  -0.01346 160 THR A N   
1228 C CA  . THR A 160 ? 0.44215 0.54774 0.50661 -0.01223 0.02061  -0.01072 160 THR A CA  
1229 C C   . THR A 160 ? 0.45161 0.56411 0.50689 -0.00818 0.01507  -0.01287 160 THR A C   
1230 O O   . THR A 160 ? 0.44393 0.56539 0.50061 -0.00494 0.01229  -0.00927 160 THR A O   
1231 C CB  . THR A 160 ? 0.44753 0.55903 0.52379 -0.02113 0.01877  -0.01346 160 THR A CB  
1232 O OG1 . THR A 160 ? 0.45702 0.56481 0.53049 -0.02807 0.01440  -0.02312 160 THR A OG1 
1233 C CG2 . THR A 160 ? 0.45093 0.55167 0.53134 -0.02342 0.02593  -0.00829 160 THR A CG2 
1234 N N   . THR A 161 ? 0.47287 0.57837 0.51464 -0.00611 0.01340  -0.01860 161 THR A N   
1235 C CA  . THR A 161 ? 0.47651 0.58399 0.50272 0.00082  0.00931  -0.01910 161 THR A CA  
1236 C C   . THR A 161 ? 0.45554 0.55545 0.47125 0.00575  0.01737  -0.01094 161 THR A C   
1237 O O   . THR A 161 ? 0.45012 0.54553 0.44836 0.01166  0.01674  -0.00858 161 THR A O   
1238 C CB  . THR A 161 ? 0.50808 0.61044 0.52029 0.00213  0.00380  -0.02921 161 THR A CB  
1239 O OG1 . THR A 161 ? 0.52637 0.61380 0.53350 0.00130  0.01026  -0.03169 161 THR A OG1 
1240 C CG2 . THR A 161 ? 0.51168 0.62714 0.53656 -0.00535 -0.00629 -0.03846 161 THR A CG2 
1241 N N   . ALA A 162 ? 0.44899 0.54798 0.47474 0.00323  0.02494  -0.00655 162 ALA A N   
1242 C CA  . ALA A 162 ? 0.46088 0.55840 0.48277 0.00421  0.03345  -0.00029 162 ALA A CA  
1243 C C   . ALA A 162 ? 0.45637 0.55693 0.48758 0.00063  0.03305  0.00570  162 ALA A C   
1244 O O   . ALA A 162 ? 0.44549 0.54356 0.47156 0.00226  0.02725  0.00670  162 ALA A O   
1245 C CB  . ALA A 162 ? 0.46467 0.56429 0.49189 0.00578  0.04061  -0.00181 162 ALA A CB  
1246 N N   . TYR A 163 ? 0.45709 0.56368 0.50055 -0.00269 0.03807  0.00851  163 TYR A N   
1247 C CA  . TYR A 163 ? 0.43996 0.54776 0.49076 -0.00667 0.03643  0.01205  163 TYR A CA  
1248 C C   . TYR A 163 ? 0.41987 0.52701 0.47366 -0.00427 0.02888  0.01126  163 TYR A C   
1249 O O   . TYR A 163 ? 0.40807 0.50860 0.45486 -0.00334 0.02549  0.01341  163 TYR A O   
1250 C CB  . TYR A 163 ? 0.43583 0.55679 0.50318 -0.00871 0.03986  0.01172  163 TYR A CB  
1251 C CG  . TYR A 163 ? 0.43819 0.56175 0.51170 -0.01555 0.03955  0.01375  163 TYR A CG  
1252 C CD1 . TYR A 163 ? 0.44521 0.55277 0.50603 -0.01911 0.03720  0.01639  163 TYR A CD1 
1253 C CD2 . TYR A 163 ? 0.43807 0.57937 0.52874 -0.01769 0.04066  0.01201  163 TYR A CD2 
1254 C CE1 . TYR A 163 ? 0.45904 0.56338 0.52276 -0.02717 0.03640  0.01691  163 TYR A CE1 
1255 C CE2 . TYR A 163 ? 0.44355 0.58855 0.54128 -0.02629 0.03874  0.01170  163 TYR A CE2 
1256 C CZ  . TYR A 163 ? 0.45399 0.57806 0.53756 -0.03235 0.03683  0.01398  163 TYR A CZ  
1257 O OH  . TYR A 163 ? 0.44920 0.57173 0.53736 -0.04279 0.03440  0.01232  163 TYR A OH  
1258 N N   . ASN A 164 ? 0.41882 0.53117 0.48153 -0.00285 0.02754  0.00859  164 ASN A N   
1259 C CA  . ASN A 164 ? 0.42210 0.53717 0.48940 -0.00177 0.02332  0.00837  164 ASN A CA  
1260 C C   . ASN A 164 ? 0.43023 0.54615 0.48979 0.00107  0.01844  0.00792  164 ASN A C   
1261 O O   . ASN A 164 ? 0.42597 0.54366 0.48534 0.00457  0.01578  0.00979  164 ASN A O   
1262 C CB  . ASN A 164 ? 0.43028 0.54544 0.50292 -0.00358 0.02455  0.00524  164 ASN A CB  
1263 C CG  . ASN A 164 ? 0.43585 0.55712 0.51507 -0.00547 0.02265  0.00514  164 ASN A CG  
1264 O OD1 . ASN A 164 ? 0.44213 0.57110 0.52261 -0.00736 0.01894  0.00149  164 ASN A OD1 
1265 N ND2 . ASN A 164 ? 0.43142 0.55204 0.51495 -0.00425 0.02534  0.00894  164 ASN A ND2 
1266 N N   . LYS A 165 ? 0.44183 0.55648 0.49232 0.00227  0.01670  0.00494  165 LYS A N   
1267 C CA  . LYS A 165 ? 0.44031 0.55829 0.48160 0.00865  0.01037  0.00365  165 LYS A CA  
1268 C C   . LYS A 165 ? 0.44668 0.55198 0.47369 0.01427  0.01024  0.00905  165 LYS A C   
1269 O O   . LYS A 165 ? 0.45298 0.56174 0.47698 0.02187  0.00560  0.00937  165 LYS A O   
1270 C CB  . LYS A 165 ? 0.45294 0.56923 0.48170 0.01113  0.00758  -0.00081 165 LYS A CB  
1271 C CG  . LYS A 165 ? 0.45668 0.57913 0.47425 0.02124  -0.00094 -0.00290 165 LYS A CG  
1272 C CD  . LYS A 165 ? 0.46814 0.58735 0.46771 0.02660  -0.00528 -0.00759 165 LYS A CD  
1273 C CE  . LYS A 165 ? 0.47425 0.60800 0.46720 0.03863  -0.01686 -0.01210 165 LYS A CE  
1274 N NZ  . LYS A 165 ? 0.49101 0.60606 0.45449 0.05337  -0.01746 -0.00524 165 LYS A NZ  
1275 N N   . SER A 166 ? 0.44879 0.53866 0.46612 0.01045  0.01598  0.01303  166 SER A N   
1276 C CA  . SER A 166 ? 0.47298 0.54352 0.47432 0.01207  0.01688  0.01788  166 SER A CA  
1277 C C   . SER A 166 ? 0.45621 0.52709 0.46567 0.01179  0.01452  0.01805  166 SER A C   
1278 O O   . SER A 166 ? 0.45358 0.50626 0.44680 0.01616  0.01263  0.02022  166 SER A O   
1279 C CB  . SER A 166 ? 0.50384 0.56130 0.49894 0.00276  0.02551  0.02174  166 SER A CB  
1280 O OG  . SER A 166 ? 0.53302 0.58885 0.51746 0.00406  0.02980  0.02223  166 SER A OG  
1281 N N   . LEU A 167 ? 0.45311 0.53965 0.48272 0.00794  0.01490  0.01594  167 LEU A N   
1282 C CA  . LEU A 167 ? 0.45234 0.53916 0.48594 0.01015  0.01243  0.01590  167 LEU A CA  
1283 C C   . LEU A 167 ? 0.44820 0.54674 0.48410 0.01956  0.00916  0.01492  167 LEU A C   
1284 O O   . LEU A 167 ? 0.45009 0.55293 0.49032 0.02275  0.00885  0.01509  167 LEU A O   
1285 C CB  . LEU A 167 ? 0.43536 0.53168 0.48496 0.00426  0.01463  0.01497  167 LEU A CB  
1286 C CG  . LEU A 167 ? 0.43036 0.52431 0.48304 -0.00467 0.01812  0.01499  167 LEU A CG  
1287 C CD1 . LEU A 167 ? 0.41098 0.52014 0.47984 -0.00588 0.01981  0.01336  167 LEU A CD1 
1288 C CD2 . LEU A 167 ? 0.43812 0.51763 0.48253 -0.00973 0.01614  0.01491  167 LEU A CD2 
1289 N N   . GLY A 168 ? 0.52139 0.58860 0.44571 0.04504  0.08100  0.04434  168 GLY A N   
1290 C CA  . GLY A 168 ? 0.51577 0.58797 0.42842 0.05059  0.07867  0.05187  168 GLY A CA  
1291 C C   . GLY A 168 ? 0.50290 0.58227 0.42171 0.04732  0.07117  0.04849  168 GLY A C   
1292 O O   . GLY A 168 ? 0.50270 0.58773 0.41409 0.04988  0.06857  0.05529  168 GLY A O   
1293 N N   . GLY A 169 ? 0.49863 0.57733 0.43019 0.04224  0.06843  0.03896  169 GLY A N   
1294 C CA  . GLY A 169 ? 0.49492 0.57367 0.42928 0.03895  0.06237  0.03599  169 GLY A CA  
1295 C C   . GLY A 169 ? 0.49989 0.59271 0.42639 0.03357  0.06365  0.03889  169 GLY A C   
1296 O O   . GLY A 169 ? 0.49481 0.60105 0.41555 0.03329  0.06917  0.04167  169 GLY A O   
1297 N N   . ALA A 170 ? 0.49987 0.58999 0.42540 0.02825  0.05799  0.03892  170 ALA A N   
1298 C CA  . ALA A 170 ? 0.49735 0.60091 0.41647 0.01873  0.05717  0.03986  170 ALA A CA  
1299 C C   . ALA A 170 ? 0.50480 0.60196 0.42483 0.01287  0.05820  0.02669  170 ALA A C   
1300 O O   . ALA A 170 ? 0.51576 0.59538 0.44296 0.01653  0.05808  0.01790  170 ALA A O   
1301 C CB  . ALA A 170 ? 0.50118 0.60228 0.41818 0.01229  0.05120  0.04570  170 ALA A CB  
1302 N N   . LEU A 171 ? 0.49860 0.61209 0.41036 0.00491  0.05928  0.02517  171 LEU A N   
1303 C CA  . LEU A 171 ? 0.51081 0.61671 0.41812 -0.00155 0.06007  0.01112  171 LEU A CA  
1304 C C   . LEU A 171 ? 0.53075 0.62110 0.43289 -0.01401 0.05340  0.00644  171 LEU A C   
1305 O O   . LEU A 171 ? 0.53044 0.63442 0.42861 -0.02435 0.04888  0.01455  171 LEU A O   
1306 C CB  . LEU A 171 ? 0.50799 0.63811 0.40536 -0.00513 0.06375  0.01023  171 LEU A CB  
1307 C CG  . LEU A 171 ? 0.49259 0.63904 0.39096 0.00540  0.07077  0.01936  171 LEU A CG  
1308 C CD1 . LEU A 171 ? 0.49137 0.65843 0.37779 0.00226  0.07444  0.01681  171 LEU A CD1 
1309 C CD2 . LEU A 171 ? 0.47475 0.60465 0.38436 0.01495  0.07583  0.01621  171 LEU A CD2 
1310 N N   . MET A 172 ? 0.56407 0.62630 0.46591 -0.01298 0.05348  -0.00616 172 MET A N   
1311 C CA  . MET A 172 ? 0.59203 0.62675 0.48814 -0.02242 0.04804  -0.01028 172 MET A CA  
1312 C C   . MET A 172 ? 0.61706 0.63421 0.49952 -0.02976 0.04927  -0.02756 172 MET A C   
1313 O O   . MET A 172 ? 0.62193 0.63429 0.50469 -0.01905 0.05538  -0.03824 172 MET A O   
1314 C CB  . MET A 172 ? 0.59499 0.60459 0.50065 -0.01026 0.04703  -0.00844 172 MET A CB  
1315 C CG  . MET A 172 ? 0.60363 0.59819 0.50739 -0.01712 0.04100  0.00121  172 MET A CG  
1316 S SD  . MET A 172 ? 0.60839 0.58169 0.52322 0.00152  0.03971  0.00464  172 MET A SD  
1317 C CE  . MET A 172 ? 0.56853 0.57523 0.49460 0.01139  0.04181  0.01307  172 MET A CE  
1318 N N   . HIS A 173 ? 0.63949 0.64563 0.50927 -0.04837 0.04383  -0.03081 173 HIS A N   
1319 C CA  . HIS A 173 ? 0.68522 0.66847 0.53715 -0.05702 0.04439  -0.04949 173 HIS A CA  
1320 C C   . HIS A 173 ? 0.72484 0.66007 0.57426 -0.04604 0.04683  -0.05933 173 HIS A C   
1321 O O   . HIS A 173 ? 0.74095 0.65344 0.59526 -0.04492 0.04351  -0.05100 173 HIS A O   
1322 C CB  . HIS A 173 ? 0.70505 0.68994 0.54303 -0.08379 0.03683  -0.05083 173 HIS A CB  
1323 C CG  . HIS A 173 ? 0.75020 0.70765 0.56537 -0.09502 0.03654  -0.07219 173 HIS A CG  
1324 N ND1 . HIS A 173 ? 0.79367 0.69618 0.59640 -0.09745 0.03644  -0.08367 173 HIS A ND1 
1325 C CD2 . HIS A 173 ? 0.76150 0.73607 0.56122 -0.10255 0.03688  -0.08488 173 HIS A CD2 
1326 C CE1 . HIS A 173 ? 0.83189 0.71628 0.61141 -0.10678 0.03689  -0.10396 173 HIS A CE1 
1327 N NE2 . HIS A 173 ? 0.81268 0.74204 0.58991 -0.11055 0.03678  -0.10535 173 HIS A NE2 
1328 N N   . PRO A 174 ? 0.74138 0.66077 0.58162 -0.03660 0.05309  -0.07639 174 PRO A N   
1329 C CA  . PRO A 174 ? 0.75495 0.63818 0.59823 -0.01722 0.05761  -0.08308 174 PRO A CA  
1330 C C   . PRO A 174 ? 0.79903 0.62937 0.62856 -0.02348 0.05367  -0.08678 174 PRO A C   
1331 O O   . PRO A 174 ? 0.81936 0.62211 0.65422 -0.00479 0.05626  -0.08661 174 PRO A O   
1332 C CB  . PRO A 174 ? 0.77228 0.65665 0.60612 -0.00683 0.06655  -0.10089 174 PRO A CB  
1333 C CG  . PRO A 174 ? 0.74741 0.67524 0.57876 -0.01681 0.06720  -0.09922 174 PRO A CG  
1334 C CD  . PRO A 174 ? 0.74324 0.68317 0.57124 -0.03936 0.05743  -0.08856 174 PRO A CD  
1335 N N   . SER A 175 ? 0.82334 0.63864 0.63527 -0.04908 0.04759  -0.08947 175 SER A N   
1336 C CA  . SER A 175 ? 0.89190 0.65147 0.68841 -0.05819 0.04436  -0.09200 175 SER A CA  
1337 C C   . SER A 175 ? 0.88889 0.64247 0.69976 -0.05490 0.04041  -0.07118 175 SER A C   
1338 O O   . SER A 175 ? 0.93178 0.63600 0.73152 -0.05707 0.03906  -0.06987 175 SER A O   
1339 C CB  . SER A 175 ? 0.93443 0.68587 0.71006 -0.09152 0.03805  -0.09920 175 SER A CB  
1340 O OG  . SER A 175 ? 0.90869 0.70657 0.69806 -0.10834 0.03175  -0.08160 175 SER A OG  
1341 N N   . ILE A 176 ? 0.84194 0.64247 0.67413 -0.05010 0.03884  -0.05499 176 ILE A N   
1342 C CA  . ILE A 176 ? 0.81943 0.62271 0.66413 -0.04631 0.03521  -0.03503 176 ILE A CA  
1343 C C   . ILE A 176 ? 0.80587 0.59444 0.66141 -0.01737 0.03823  -0.03336 176 ILE A C   
1344 O O   . ILE A 176 ? 0.77428 0.59041 0.64379 -0.00042 0.04203  -0.03663 176 ILE A O   
1345 C CB  . ILE A 176 ? 0.76082 0.61945 0.62070 -0.05049 0.03321  -0.02089 176 ILE A CB  
1346 C CG1 . ILE A 176 ? 0.75995 0.64146 0.61225 -0.07777 0.02940  -0.01902 176 ILE A CG1 
1347 C CG2 . ILE A 176 ? 0.72639 0.58963 0.59804 -0.04074 0.03084  -0.00258 176 ILE A CG2 
1348 C CD1 . ILE A 176 ? 0.71107 0.64803 0.57712 -0.07652 0.02914  -0.00593 176 ILE A CD1 
1349 N N   . GLU A 177 ? 0.82789 0.57614 0.67783 -0.01214 0.03631  -0.02662 177 GLU A N   
1350 C CA  . GLU A 177 ? 0.82634 0.56329 0.68660 0.01662  0.03800  -0.02395 177 GLU A CA  
1351 C C   . GLU A 177 ? 0.77732 0.54970 0.65587 0.02416  0.03366  -0.00610 177 GLU A C   
1352 O O   . GLU A 177 ? 0.78879 0.54956 0.66383 0.01961  0.02922  0.00901  177 GLU A O   
1353 C CB  . GLU A 177 ? 0.89518 0.57067 0.73859 0.02221  0.03824  -0.02423 177 GLU A CB  
1354 C CG  . GLU A 177 ? 0.95319 0.58857 0.77488 0.01688  0.04336  -0.04528 177 GLU A CG  
1355 C CD  . GLU A 177 ? 1.02754 0.59437 0.82977 0.02680  0.04530  -0.04723 177 GLU A CD  
1356 O OE1 . GLU A 177 ? 1.03775 0.58957 0.84387 0.03753  0.04233  -0.03031 177 GLU A OE1 
1357 O OE2 . GLU A 177 ? 1.07862 0.60423 0.85914 0.02460  0.05004  -0.06568 177 GLU A OE2 
1358 N N   . ALA A 178 ? 0.72699 0.54115 0.62309 0.03497  0.03532  -0.00801 178 ALA A N   
1359 C CA  . ALA A 178 ? 0.68352 0.53069 0.59381 0.04013  0.03125  0.00578  178 ALA A CA  
1360 C C   . ALA A 178 ? 0.64605 0.52583 0.57472 0.05513  0.03388  0.00017  178 ALA A C   
1361 O O   . ALA A 178 ? 0.64969 0.53034 0.58163 0.06214  0.03964  -0.01284 178 ALA A O   
1362 C CB  . ALA A 178 ? 0.66262 0.53349 0.56910 0.02031  0.02948  0.01453  178 ALA A CB  
1363 N N   . MET A 179 ? 0.60724 0.51356 0.54657 0.05895  0.02996  0.01017  179 MET A N   
1364 C CA  . MET A 179 ? 0.57535 0.51330 0.53193 0.06849  0.03102  0.00746  179 MET A CA  
1365 C C   . MET A 179 ? 0.54601 0.50789 0.50267 0.06052  0.02867  0.01631  179 MET A C   
1366 O O   . MET A 179 ? 0.55313 0.50943 0.50088 0.05584  0.02434  0.02714  179 MET A O   
1367 C CB  . MET A 179 ? 0.58092 0.51922 0.55057 0.08754  0.02680  0.00940  179 MET A CB  
1368 C CG  . MET A 179 ? 0.57426 0.50545 0.53968 0.09152  0.01807  0.02319  179 MET A CG  
1369 S SD  . MET A 179 ? 0.58600 0.52210 0.56671 0.11548  0.01201  0.02545  179 MET A SD  
1370 C CE  . MET A 179 ? 0.58886 0.50878 0.55543 0.11758  0.00264  0.04278  179 MET A CE  
1371 N N   . GLN A 180 ? 0.52127 0.50823 0.48643 0.05970  0.03250  0.01226  180 GLN A N   
1372 C CA  . GLN A 180 ? 0.51499 0.51939 0.47657 0.05345  0.03221  0.01934  180 GLN A CA  
1373 C C   . GLN A 180 ? 0.50368 0.52396 0.47697 0.06002  0.03046  0.01882  180 GLN A C   
1374 O O   . GLN A 180 ? 0.50490 0.53630 0.49110 0.06306  0.03415  0.01134  180 GLN A O   
1375 C CB  . GLN A 180 ? 0.50966 0.52579 0.46499 0.04345  0.03891  0.01697  180 GLN A CB  
1376 C CG  . GLN A 180 ? 0.49904 0.53053 0.44867 0.04045  0.03973  0.02555  180 GLN A CG  
1377 C CD  . GLN A 180 ? 0.50518 0.55012 0.44690 0.03227  0.04520  0.02663  180 GLN A CD  
1378 O OE1 . GLN A 180 ? 0.50159 0.55859 0.43671 0.03160  0.04656  0.03504  180 GLN A OE1 
1379 N NE2 . GLN A 180 ? 0.51849 0.56244 0.45952 0.02760  0.04842  0.01812  180 GLN A NE2 
1380 N N   . LEU A 181 ? 0.50187 0.52384 0.46966 0.06105  0.02510  0.02648  181 LEU A N   
1381 C CA  . LEU A 181 ? 0.49009 0.52366 0.46514 0.06431  0.02175  0.02512  181 LEU A CA  
1382 C C   . LEU A 181 ? 0.47885 0.51816 0.44468 0.05834  0.02652  0.02708  181 LEU A C   
1383 O O   . LEU A 181 ? 0.48038 0.51580 0.43116 0.05703  0.02704  0.03438  181 LEU A O   
1384 C CB  . LEU A 181 ? 0.49195 0.52120 0.46343 0.07091  0.01186  0.03069  181 LEU A CB  
1385 C CG  . LEU A 181 ? 0.47434 0.51635 0.45300 0.07236  0.00612  0.02716  181 LEU A CG  
1386 C CD1 . LEU A 181 ? 0.46729 0.52417 0.46911 0.07640  0.00483  0.02007  181 LEU A CD1 
1387 C CD2 . LEU A 181 ? 0.47569 0.51387 0.44263 0.07737  -0.00364 0.03332  181 LEU A CD2 
1388 N N   . THR A 182 ? 0.46612 0.51469 0.44068 0.05550  0.03083  0.02157  182 THR A N   
1389 C CA  . THR A 182 ? 0.47891 0.52753 0.44373 0.05134  0.03600  0.02366  182 THR A CA  
1390 C C   . THR A 182 ? 0.49201 0.54034 0.46006 0.04985  0.03129  0.02030  182 THR A C   
1391 O O   . THR A 182 ? 0.49548 0.55415 0.48104 0.04898  0.02736  0.01474  182 THR A O   
1392 C CB  . THR A 182 ? 0.48545 0.54149 0.45399 0.04690  0.04595  0.02139  182 THR A CB  
1393 O OG1 . THR A 182 ? 0.48831 0.55411 0.47533 0.04687  0.04710  0.01401  182 THR A OG1 
1394 C CG2 . THR A 182 ? 0.48404 0.54085 0.44233 0.04604  0.04978  0.02547  182 THR A CG2 
1395 N N   . GLU A 183 ? 0.50359 0.54092 0.45417 0.04970  0.03154  0.02335  183 GLU A N   
1396 C CA  . GLU A 183 ? 0.50845 0.54056 0.45772 0.04519  0.02737  0.01832  183 GLU A CA  
1397 C C   . GLU A 183 ? 0.50477 0.53758 0.46104 0.03639  0.03550  0.01530  183 GLU A C   
1398 O O   . GLU A 183 ? 0.48855 0.52207 0.44274 0.03640  0.04535  0.01905  183 GLU A O   
1399 C CB  . GLU A 183 ? 0.52654 0.54087 0.45008 0.04917  0.02598  0.02110  183 GLU A CB  
1400 C CG  . GLU A 183 ? 0.52840 0.54280 0.44192 0.05747  0.01957  0.02607  183 GLU A CG  
1401 C CD  . GLU A 183 ? 0.54729 0.54598 0.43408 0.06274  0.01925  0.02757  183 GLU A CD  
1402 O OE1 . GLU A 183 ? 0.56036 0.54398 0.43540 0.06061  0.02450  0.02431  183 GLU A OE1 
1403 O OE2 . GLU A 183 ? 0.55267 0.55212 0.42844 0.06960  0.01463  0.03226  183 GLU A OE2 
1404 N N   . MET A 184 ? 0.52083 0.55500 0.48506 0.02767  0.03091  0.00908  184 MET A N   
1405 C CA  . MET A 184 ? 0.52691 0.55575 0.49338 0.01611  0.03822  0.00721  184 MET A CA  
1406 C C   . MET A 184 ? 0.54955 0.55374 0.49623 0.01015  0.03396  0.00354  184 MET A C   
1407 O O   . MET A 184 ? 0.56746 0.57762 0.52131 0.00224  0.02350  -0.00353 184 MET A O   
1408 C CB  . MET A 184 ? 0.52363 0.57859 0.51964 0.00695  0.03741  0.00248  184 MET A CB  
1409 C CG  . MET A 184 ? 0.50797 0.58314 0.52087 0.01091  0.04582  0.00431  184 MET A CG  
1410 S SD  . MET A 184 ? 0.51467 0.62444 0.56236 0.00155  0.04503  -0.00109 184 MET A SD  
1411 C CE  . MET A 184 ? 0.49702 0.62688 0.55903 0.01577  0.05046  -0.00144 184 MET A CE  
1412 N N   . ALA A 185 ? 0.55699 0.53400 0.47767 0.01475  0.04172  0.00797  185 ALA A N   
1413 C CA  . ALA A 185 ? 0.58973 0.53404 0.48679 0.00922  0.04159  0.00381  185 ALA A CA  
1414 C C   . ALA A 185 ? 0.60209 0.54143 0.48895 0.00916  0.02799  -0.00422 185 ALA A C   
1415 O O   . ALA A 185 ? 0.63184 0.56602 0.52008 -0.00514 0.02035  -0.01335 185 ALA A O   
1416 C CB  . ALA A 185 ? 0.59939 0.53701 0.50561 -0.00927 0.04596  0.00055  185 ALA A CB  
1417 N N   . SER A 186 ? 0.58652 0.52839 0.46159 0.02424  0.02498  -0.00037 186 SER A N   
1418 C CA  A SER A 186 ? 0.60144 0.53764 0.46117 0.02679  0.01327  -0.00641 186 SER A CA  
1419 C CA  B SER A 186 ? 0.60163 0.53793 0.46153 0.02667  0.01323  -0.00646 186 SER A CA  
1420 C C   . SER A 186 ? 0.64794 0.54488 0.47263 0.02725  0.01637  -0.01181 186 SER A C   
1421 O O   . SER A 186 ? 0.66448 0.53954 0.47182 0.03544  0.02888  -0.00620 186 SER A O   
1422 C CB  A SER A 186 ? 0.58917 0.53886 0.44498 0.04246  0.01106  0.00136  186 SER A CB  
1423 C CB  B SER A 186 ? 0.58826 0.53884 0.44508 0.04216  0.01076  0.00126  186 SER A CB  
1424 O OG  A SER A 186 ? 0.58726 0.52784 0.42846 0.05420  0.02304  0.01053  186 SER A OG  
1425 O OG  B SER A 186 ? 0.60744 0.54825 0.44106 0.04776  0.00259  -0.00236 186 SER A OG  
1426 N N   . ILE A 187 ? 0.67449 0.56201 0.48739 0.01917  0.00488  -0.02295 187 ILE A N   
1427 C CA  . ILE A 187 ? 0.73507 0.58134 0.50855 0.02207  0.00685  -0.03016 187 ILE A CA  
1428 C C   . ILE A 187 ? 0.77213 0.62057 0.52425 0.04290  0.00663  -0.02519 187 ILE A C   
1429 O O   . ILE A 187 ? 0.74650 0.62494 0.51190 0.04697  -0.00223 -0.02166 187 ILE A O   
1430 C CB  . ILE A 187 ? 0.74320 0.57888 0.51099 0.00191  -0.00635 -0.04588 187 ILE A CB  
1431 C CG1 . ILE A 187 ? 0.77914 0.56100 0.50384 0.00061  -0.00221 -0.05597 187 ILE A CG1 
1432 C CG2 . ILE A 187 ? 0.74461 0.60964 0.51769 0.00311  -0.02333 -0.04996 187 ILE A CG2 
1433 C CD1 . ILE A 187 ? 0.81163 0.58275 0.52639 -0.02108 -0.01745 -0.07344 187 ILE A CD1 
1434 N N   . ASN A 188 ? 0.85137 0.67027 0.57141 0.05775  0.01763  -0.02282 188 ASN A N   
1435 C CA  . ASN A 188 ? 0.90875 0.73464 0.60941 0.07738  0.01870  -0.01705 188 ASN A CA  
1436 C C   . ASN A 188 ? 1.01551 0.80098 0.67083 0.08739  0.02250  -0.02586 188 ASN A C   
1437 O O   . ASN A 188 ? 1.03415 0.78662 0.67001 0.09438  0.03500  -0.02563 188 ASN A O   
1438 C CB  . ASN A 188 ? 0.87417 0.72193 0.58692 0.09201  0.03032  -0.00009 188 ASN A CB  
1439 C CG  . ASN A 188 ? 0.82116 0.70916 0.56661 0.08789  0.02338  0.00754  188 ASN A CG  
1440 O OD1 . ASN A 188 ? 0.80781 0.71306 0.54997 0.09670  0.02037  0.01407  188 ASN A OD1 
1441 N ND2 . ASN A 188 ? 0.79682 0.69792 0.57248 0.07446  0.02125  0.00672  188 ASN A ND2 
1442 N N   . ASN A 189 ? 1.09130 0.87887 0.72797 0.08981  0.01209  -0.03312 189 ASN A N   
1443 C CA  . ASN A 189 ? 1.22670 0.97815 0.81642 0.10056  0.01424  -0.04352 189 ASN A CA  
1444 C C   . ASN A 189 ? 1.31067 1.08637 0.88894 0.11075  0.00619  -0.04135 189 ASN A C   
1445 O O   . ASN A 189 ? 1.26489 1.08001 0.87173 0.10731  -0.00176 -0.03229 189 ASN A O   
1446 C CB  . ASN A 189 ? 1.26518 0.97816 0.83734 0.08069  0.00608  -0.06354 189 ASN A CB  
1447 C CG  . ASN A 189 ? 1.24817 0.98911 0.85555 0.05473  -0.01059 -0.06896 189 ASN A CG  
1448 O OD1 . ASN A 189 ? 1.21155 0.99565 0.84402 0.05504  -0.02002 -0.06201 189 ASN A OD1 
1449 N ND2 . ASN A 189 ? 1.27083 0.98750 0.88033 0.03256  -0.01357 -0.08042 189 ASN A ND2 
1450 N N   . ARG A 190 ? 1.44360 1.19330 0.97732 0.12445  0.00907  -0.04932 190 ARG A N   
1451 C CA  . ARG A 190 ? 1.46864 1.23999 0.98644 0.13425  0.00191  -0.04721 190 ARG A CA  
1452 C C   . ARG A 190 ? 1.44005 1.23859 0.97914 0.11594  -0.01886 -0.05157 190 ARG A C   
1453 O O   . ARG A 190 ? 1.42584 1.25657 0.97113 0.12226  -0.02484 -0.04142 190 ARG A O   
1454 C CB  . ARG A 190 ? 1.55375 1.28679 1.01613 0.14698  0.00522  -0.06147 190 ARG A CB  
1455 C CG  . ARG A 190 ? 1.60763 1.29352 1.04473 0.15772  0.02193  -0.06666 190 ARG A CG  
1456 C CD  . ARG A 190 ? 1.69237 1.32848 1.07216 0.16408  0.02176  -0.08752 190 ARG A CD  
1457 N NE  . ARG A 190 ? 1.73273 1.33712 1.10530 0.13645  0.00702  -0.10891 190 ARG A NE  
1458 C CZ  . ARG A 190 ? 1.82528 1.37554 1.14911 0.13424  0.00561  -0.13081 190 ARG A CZ  
1459 N NH1 . ARG A 190 ? 1.88273 1.40152 1.15814 0.16111  0.01900  -0.13510 190 ARG A NH1 
1460 N NH2 . ARG A 190 ? 1.86276 1.39008 1.18577 0.10407  -0.00921 -0.14919 190 ARG A NH2 
1461 N N   . VAL A 191 ? 1.34545 1.13285 0.89683 0.09348  -0.02940 -0.06510 191 VAL A N   
1462 C CA  . VAL A 191 ? 1.28919 1.10540 0.86278 0.07580  -0.04974 -0.07021 191 VAL A CA  
1463 C C   . VAL A 191 ? 1.20808 1.06563 0.83144 0.07324  -0.05090 -0.05416 191 VAL A C   
1464 O O   . VAL A 191 ? 1.23100 1.12194 0.86932 0.07506  -0.06199 -0.04703 191 VAL A O   
1465 C CB  . VAL A 191 ? 1.33259 1.12672 0.90718 0.05063  -0.05853 -0.08876 191 VAL A CB  
1466 C CG1 . VAL A 191 ? 1.34273 1.17695 0.94833 0.03246  -0.07924 -0.09193 191 VAL A CG1 
1467 C CG2 . VAL A 191 ? 1.42908 1.17377 0.95092 0.05009  -0.05823 -0.10781 191 VAL A CG2 
1468 N N   . TYR A 192 ? 1.09438 0.94741 0.74260 0.06763  -0.04046 -0.04985 192 TYR A N   
1469 C CA  . TYR A 192 ? 0.99541 0.88133 0.68902 0.06314  -0.04036 -0.03818 192 TYR A CA  
1470 C C   . TYR A 192 ? 0.92036 0.80718 0.61774 0.07835  -0.02337 -0.02294 192 TYR A C   
1471 O O   . TYR A 192 ? 0.92388 0.78498 0.60589 0.08347  -0.01014 -0.02333 192 TYR A O   
1472 C CB  . TYR A 192 ? 0.96755 0.85186 0.68699 0.04249  -0.04223 -0.04591 192 TYR A CB  
1473 C CG  . TYR A 192 ? 0.96559 0.86738 0.69690 0.02445  -0.06088 -0.05747 192 TYR A CG  
1474 C CD1 . TYR A 192 ? 0.93816 0.88275 0.70085 0.02439  -0.07229 -0.05103 192 TYR A CD1 
1475 C CD2 . TYR A 192 ? 1.00393 0.87985 0.71587 0.00699  -0.06698 -0.07453 192 TYR A CD2 
1476 C CE1 . TYR A 192 ? 0.94452 0.91263 0.72114 0.00918  -0.08977 -0.06023 192 TYR A CE1 
1477 C CE2 . TYR A 192 ? 1.01526 0.91342 0.74054 -0.01205 -0.08512 -0.08496 192 TYR A CE2 
1478 C CZ  . TYR A 192 ? 0.98494 0.93270 0.74384 -0.01013 -0.09667 -0.07725 192 TYR A CZ  
1479 O OH  . TYR A 192 ? 0.99985 0.97630 0.77414 -0.02793 -0.11517 -0.08658 192 TYR A OH  
1480 N N   . ARG A 193 ? 0.85732 0.77317 0.57357 0.08558  -0.02405 -0.00922 193 ARG A N   
1481 C CA  . ARG A 193 ? 0.81799 0.73976 0.53605 0.09824  -0.01001 0.00549  193 ARG A CA  
1482 C C   . ARG A 193 ? 0.74485 0.69403 0.49974 0.09379  -0.01209 0.01548  193 ARG A C   
1483 O O   . ARG A 193 ? 0.74346 0.70960 0.50769 0.09352  -0.02271 0.01870  193 ARG A O   
1484 C CB  . ARG A 193 ? 0.85225 0.77500 0.54067 0.11414  -0.00730 0.01228  193 ARG A CB  
1485 C CG  . ARG A 193 ? 0.84055 0.78058 0.53614 0.12451  0.00473  0.02983  193 ARG A CG  
1486 C CD  . ARG A 193 ? 0.85156 0.78003 0.54089 0.13154  0.02029  0.03211  193 ARG A CD  
1487 N NE  . ARG A 193 ? 0.89889 0.80428 0.54938 0.14544  0.02710  0.02656  193 ARG A NE  
1488 C CZ  . ARG A 193 ? 0.93720 0.80832 0.56863 0.14470  0.02946  0.01313  193 ARG A CZ  
1489 N NH1 . ARG A 193 ? 0.93262 0.79147 0.58180 0.12922  0.02598  0.00519  193 ARG A NH1 
1490 N NH2 . ARG A 193 ? 0.98188 0.82884 0.57411 0.15990  0.03636  0.00776  193 ARG A NH2 
1491 N N   . THR A 194 ? 0.68210 0.63361 0.45602 0.09071  -0.00239 0.01965  194 THR A N   
1492 C CA  . THR A 194 ? 0.63038 0.60337 0.43454 0.08751  -0.00245 0.02797  194 THR A CA  
1493 C C   . THR A 194 ? 0.61130 0.59028 0.41466 0.09432  0.00998  0.04025  194 THR A C   
1494 O O   . THR A 194 ? 0.61263 0.58260 0.39623 0.10238  0.01933  0.04275  194 THR A O   
1495 C CB  . THR A 194 ? 0.60419 0.58135 0.43535 0.07529  -0.00367 0.02092  194 THR A CB  
1496 O OG1 . THR A 194 ? 0.60265 0.56743 0.43093 0.07343  0.00819  0.02024  194 THR A OG1 
1497 C CG2 . THR A 194 ? 0.62395 0.59999 0.45718 0.06622  -0.01586 0.00877  194 THR A CG2 
1498 N N   . ILE A 195 ? 0.59263 0.58752 0.41744 0.09119  0.00989  0.04776  195 ILE A N   
1499 C CA  . ILE A 195 ? 0.57979 0.58536 0.40467 0.09451  0.01907  0.05989  195 ILE A CA  
1500 C C   . ILE A 195 ? 0.57349 0.57933 0.40247 0.09338  0.02945  0.05968  195 ILE A C   
1501 O O   . ILE A 195 ? 0.57252 0.58696 0.39301 0.09963  0.03813  0.06864  195 ILE A O   
1502 C CB  . ILE A 195 ? 0.55481 0.57132 0.39785 0.08932  0.01517  0.06659  195 ILE A CB  
1503 C CG1 . ILE A 195 ? 0.54431 0.57338 0.38580 0.08908  0.02322  0.07928  195 ILE A CG1 
1504 C CG2 . ILE A 195 ? 0.52635 0.54376 0.39351 0.08122  0.01348  0.05918  195 ILE A CG2 
1505 C CD1 . ILE A 195 ? 0.54974 0.58413 0.36883 0.09846  0.02776  0.08814  195 ILE A CD1 
1506 N N   . GLY A 196 ? 0.56405 0.56387 0.40619 0.08605  0.02903  0.05095  196 GLY A N   
1507 C CA  . GLY A 196 ? 0.55777 0.55745 0.40306 0.08502  0.03870  0.05187  196 GLY A CA  
1508 C C   . GLY A 196 ? 0.54107 0.55854 0.40574 0.07899  0.04134  0.05623  196 GLY A C   
1509 O O   . GLY A 196 ? 0.54732 0.56579 0.42595 0.07224  0.04297  0.05111  196 GLY A O   
1510 N N   . SER A 197 ? 0.53365 0.56529 0.39804 0.08029  0.04193  0.06545  197 SER A N   
1511 C CA  . SER A 197 ? 0.52338 0.57031 0.40121 0.07313  0.04446  0.06901  197 SER A CA  
1512 C C   . SER A 197 ? 0.51115 0.55403 0.40677 0.06498  0.03877  0.06091  197 SER A C   
1513 O O   . SER A 197 ? 0.50855 0.54291 0.40754 0.06586  0.03142  0.05688  197 SER A O   
1514 C CB  . SER A 197 ? 0.52138 0.58323 0.39546 0.07253  0.04490  0.08026  197 SER A CB  
1515 O OG  . SER A 197 ? 0.53704 0.60509 0.39449 0.08330  0.05013  0.08817  197 SER A OG  
1516 N N   . PRO A 198 ? 0.49533 0.54565 0.40138 0.05855  0.04215  0.05849  198 PRO A N   
1517 C CA  . PRO A 198 ? 0.49603 0.54253 0.41592 0.05310  0.03799  0.05209  198 PRO A CA  
1518 C C   . PRO A 198 ? 0.50567 0.54784 0.42266 0.05167  0.03287  0.05812  198 PRO A C   
1519 O O   . PRO A 198 ? 0.50733 0.55757 0.41537 0.04976  0.03470  0.06762  198 PRO A O   
1520 C CB  . PRO A 198 ? 0.48855 0.54467 0.41301 0.04683  0.04383  0.04948  198 PRO A CB  
1521 C CG  . PRO A 198 ? 0.48150 0.54591 0.39764 0.05033  0.05062  0.05373  198 PRO A CG  
1522 C CD  . PRO A 198 ? 0.48909 0.55269 0.39249 0.05720  0.04975  0.06222  198 PRO A CD  
1523 N N   . LEU A 199 ? 0.49263 0.52335 0.41705 0.05354  0.02676  0.05407  199 LEU A N   
1524 C CA  . LEU A 199 ? 0.50476 0.52540 0.42580 0.05236  0.02233  0.06042  199 LEU A CA  
1525 C C   . LEU A 199 ? 0.53027 0.54006 0.45952 0.04762  0.02275  0.05424  199 LEU A C   
1526 O O   . LEU A 199 ? 0.53496 0.54472 0.47515 0.05067  0.02384  0.04423  199 LEU A O   
1527 C CB  . LEU A 199 ? 0.48966 0.50299 0.40882 0.06124  0.01473  0.06244  199 LEU A CB  
1528 C CG  . LEU A 199 ? 0.47853 0.49825 0.38475 0.06631  0.01388  0.06657  199 LEU A CG  
1529 C CD1 . LEU A 199 ? 0.49149 0.50620 0.39780 0.07390  0.00468  0.06508  199 LEU A CD1 
1530 C CD2 . LEU A 199 ? 0.47450 0.49840 0.36705 0.06414  0.01707  0.07917  199 LEU A CD2 
1531 N N   . VAL A 200 ? 0.54597 0.54590 0.46890 0.03975  0.02249  0.05999  200 VAL A N   
1532 C CA  . VAL A 200 ? 0.56303 0.54659 0.48836 0.03371  0.02355  0.05279  200 VAL A CA  
1533 C C   . VAL A 200 ? 0.59031 0.54750 0.51007 0.03474  0.01914  0.05905  200 VAL A C   
1534 O O   . VAL A 200 ? 0.60329 0.55809 0.51367 0.02715  0.01824  0.07085  200 VAL A O   
1535 C CB  . VAL A 200 ? 0.56745 0.56137 0.48798 0.01879  0.02787  0.05184  200 VAL A CB  
1536 C CG1 . VAL A 200 ? 0.58965 0.55986 0.50642 0.00978  0.02778  0.04460  200 VAL A CG1 
1537 C CG2 . VAL A 200 ? 0.53911 0.55478 0.46456 0.02071  0.03275  0.04512  200 VAL A CG2 
1538 N N   . PHE A 201 ? 0.59350 0.53175 0.51900 0.04531  0.01708  0.05249  201 PHE A N   
1539 C CA  . PHE A 201 ? 0.61881 0.52952 0.53883 0.05208  0.01272  0.05958  201 PHE A CA  
1540 C C   . PHE A 201 ? 0.67607 0.55315 0.58946 0.04663  0.01534  0.05394  201 PHE A C   
1541 O O   . PHE A 201 ? 0.66801 0.54320 0.58528 0.04595  0.01954  0.04017  201 PHE A O   
1542 C CB  . PHE A 201 ? 0.59876 0.51293 0.52926 0.07158  0.00785  0.05794  201 PHE A CB  
1543 C CG  . PHE A 201 ? 0.57307 0.51476 0.50730 0.07543  0.00425  0.06108  201 PHE A CG  
1544 C CD1 . PHE A 201 ? 0.54340 0.50829 0.48870 0.07525  0.00665  0.05147  201 PHE A CD1 
1545 C CD2 . PHE A 201 ? 0.57792 0.52024 0.50140 0.07768  -0.00072 0.07377  201 PHE A CD2 
1546 C CE1 . PHE A 201 ? 0.52760 0.51145 0.47277 0.07696  0.00360  0.05318  201 PHE A CE1 
1547 C CE2 . PHE A 201 ? 0.55943 0.52335 0.48193 0.08084  -0.00386 0.07468  201 PHE A CE2 
1548 C CZ  . PHE A 201 ? 0.53451 0.51714 0.46749 0.08004  -0.00190 0.06374  201 PHE A CZ  
1549 N N   . PRO A 202 ? 0.74279 0.59019 0.64398 0.04299  0.01339  0.06415  202 PRO A N   
1550 C CA  . PRO A 202 ? 0.81929 0.62514 0.71023 0.03757  0.01592  0.05808  202 PRO A CA  
1551 C C   . PRO A 202 ? 0.87508 0.65392 0.76807 0.06018  0.01518  0.05419  202 PRO A C   
1552 O O   . PRO A 202 ? 0.86070 0.65829 0.76581 0.07947  0.01162  0.05676  202 PRO A O   
1553 C CB  . PRO A 202 ? 0.83685 0.62264 0.71288 0.02113  0.01474  0.07350  202 PRO A CB  
1554 C CG  . PRO A 202 ? 0.81565 0.62082 0.69401 0.03217  0.01053  0.08910  202 PRO A CG  
1555 C CD  . PRO A 202 ? 0.76019 0.60961 0.65286 0.03957  0.01014  0.08217  202 PRO A CD  
1556 N N   . LYS A 203 ? 0.93789 0.67242 0.81804 0.05761  0.01846  0.04772  203 LYS A N   
1557 C CA  . LYS A 203 ? 0.98780 0.68864 0.86564 0.08102  0.01876  0.04672  203 LYS A CA  
1558 C C   . LYS A 203 ? 1.00531 0.69994 0.88096 0.09357  0.01273  0.06656  203 LYS A C   
1559 O O   . LYS A 203 ? 1.00611 0.69798 0.87196 0.07881  0.01037  0.08119  203 LYS A O   
1560 C CB  . LYS A 203 ? 1.06008 0.70402 0.91717 0.07306  0.02350  0.03877  203 LYS A CB  
1561 C CG  . LYS A 203 ? 1.08307 0.72014 0.94099 0.08089  0.02978  0.01736  203 LYS A CG  
1562 C CD  . LYS A 203 ? 1.16322 0.73365 0.99566 0.07652  0.03375  0.01066  203 LYS A CD  
1563 C CE  . LYS A 203 ? 1.20989 0.76128 1.04143 0.10186  0.04046  -0.00590 203 LYS A CE  
1564 N NZ  . LYS A 203 ? 1.21236 0.78870 1.06437 0.13485  0.03884  0.00239  203 LYS A NZ  
1565 N N   . HIS A 204 ? 0.99059 0.68681 0.87553 0.12147  0.01040  0.06763  204 HIS A N   
1566 C CA  . HIS A 204 ? 0.98074 0.66846 0.86217 0.13893  0.00414  0.08571  204 HIS A CA  
1567 C C   . HIS A 204 ? 0.92318 0.65963 0.81473 0.13840  -0.00329 0.09535  204 HIS A C   
1568 O O   . HIS A 204 ? 0.94108 0.68246 0.83250 0.15571  -0.01004 0.10829  204 HIS A O   
1569 C CB  . HIS A 204 ? 1.02118 0.65418 0.87727 0.12988  0.00526  0.10028  204 HIS A CB  
1570 C CG  . HIS A 204 ? 1.08092 0.65659 0.92207 0.13009  0.01224  0.09015  204 HIS A CG  
1571 N ND1 . HIS A 204 ? 1.10824 0.66794 0.95376 0.15796  0.01509  0.08083  204 HIS A ND1 
1572 C CD2 . HIS A 204 ? 1.12176 0.65274 0.94283 0.10593  0.01711  0.08653  204 HIS A CD2 
1573 C CE1 . HIS A 204 ? 1.16040 0.66269 0.98619 0.15291  0.02202  0.07135  204 HIS A CE1 
1574 N NE2 . HIS A 204 ? 1.16913 0.65193 0.97943 0.11982  0.02272  0.07410  204 HIS A NE2 
1575 N N   . HIS A 205 ? 0.85895 0.63086 0.75750 0.12084  -0.00246 0.08929  205 HIS A N   
1576 C CA  . HIS A 205 ? 0.80627 0.62126 0.71359 0.12436  -0.00901 0.09448  205 HIS A CA  
1577 C C   . HIS A 205 ? 0.77542 0.62015 0.70434 0.14244  -0.01217 0.08418  205 HIS A C   
1578 O O   . HIS A 205 ? 0.75789 0.60717 0.69840 0.14325  -0.00652 0.06954  205 HIS A O   
1579 C CB  . HIS A 205 ? 0.76362 0.60316 0.66969 0.10281  -0.00608 0.09194  205 HIS A CB  
1580 C CG  . HIS A 205 ? 0.77500 0.59923 0.66311 0.08625  -0.00429 0.10587  205 HIS A CG  
1581 N ND1 . HIS A 205 ? 0.74879 0.59968 0.63380 0.07245  -0.00279 0.11001  205 HIS A ND1 
1582 C CD2 . HIS A 205 ? 0.81485 0.60048 0.68731 0.08117  -0.00299 0.11752  205 HIS A CD2 
1583 C CE1 . HIS A 205 ? 0.77102 0.60625 0.64163 0.05932  -0.00060 0.12382  205 HIS A CE1 
1584 N NE2 . HIS A 205 ? 0.81141 0.60566 0.67391 0.06262  -0.00084 0.12875  205 HIS A NE2 
1585 N N   . VAL A 206 ? 0.77008 0.63608 0.70391 0.15693  -0.02129 0.09236  206 VAL A N   
1586 C CA  . VAL A 206 ? 0.73890 0.64216 0.69534 0.17072  -0.02617 0.08429  206 VAL A CA  
1587 C C   . VAL A 206 ? 0.69927 0.63909 0.65927 0.15919  -0.03100 0.08187  206 VAL A C   
1588 O O   . VAL A 206 ? 0.70685 0.65108 0.65376 0.15831  -0.03778 0.09247  206 VAL A O   
1589 C CB  . VAL A 206 ? 0.75885 0.66344 0.71924 0.19611  -0.03450 0.09434  206 VAL A CB  
1590 C CG1 . VAL A 206 ? 0.72960 0.68539 0.71397 0.20491  -0.04258 0.08823  206 VAL A CG1 
1591 C CG2 . VAL A 206 ? 0.79320 0.66301 0.75323 0.21232  -0.02809 0.09314  206 VAL A CG2 
1592 N N   . VAL A 207 ? 0.66061 0.62395 0.63575 0.15084  -0.02687 0.06809  207 VAL A N   
1593 C CA  . VAL A 207 ? 0.63623 0.63063 0.61546 0.14165  -0.03110 0.06392  207 VAL A CA  
1594 C C   . VAL A 207 ? 0.64323 0.67099 0.64441 0.15257  -0.03880 0.05906  207 VAL A C   
1595 O O   . VAL A 207 ? 0.63324 0.67329 0.65449 0.15772  -0.03427 0.05065  207 VAL A O   
1596 C CB  . VAL A 207 ? 0.60902 0.60760 0.58935 0.12459  -0.02172 0.05406  207 VAL A CB  
1597 C CG1 . VAL A 207 ? 0.59173 0.61360 0.57159 0.11644  -0.02572 0.05082  207 VAL A CG1 
1598 C CG2 . VAL A 207 ? 0.61565 0.58809 0.57733 0.11365  -0.01496 0.05936  207 VAL A CG2 
1599 N N   . SER A 208 ? 0.65145 0.69681 0.64838 0.15535  -0.05042 0.06424  208 SER A N   
1600 C CA  . SER A 208 ? 0.64680 0.72784 0.66309 0.16506  -0.06113 0.06209  208 SER A CA  
1601 C C   . SER A 208 ? 0.63160 0.73674 0.64739 0.14983  -0.06719 0.05451  208 SER A C   
1602 O O   . SER A 208 ? 0.64547 0.73799 0.63769 0.14159  -0.06890 0.05733  208 SER A O   
1603 C CB  . SER A 208 ? 0.66989 0.74852 0.67823 0.18399  -0.07183 0.07611  208 SER A CB  
1604 O OG  . SER A 208 ? 0.66662 0.78542 0.68727 0.18913  -0.08584 0.07529  208 SER A OG  
1605 N N   . LEU A 209 ? 0.61126 0.74951 0.65182 0.14572  -0.06944 0.04488  209 LEU A N   
1606 C CA  . LEU A 209 ? 0.61193 0.76909 0.65256 0.12868  -0.07476 0.03608  209 LEU A CA  
1607 C C   . LEU A 209 ? 0.64199 0.83559 0.69381 0.13408  -0.09167 0.03687  209 LEU A C   
1608 O O   . LEU A 209 ? 0.65329 0.87194 0.72827 0.14884  -0.09552 0.04031  209 LEU A O   
1609 C CB  . LEU A 209 ? 0.59164 0.75844 0.65060 0.11500  -0.06406 0.02519  209 LEU A CB  
1610 C CG  . LEU A 209 ? 0.58316 0.72003 0.63068 0.10721  -0.04826 0.02323  209 LEU A CG  
1611 C CD1 . LEU A 209 ? 0.56748 0.71729 0.63436 0.09730  -0.03743 0.01455  209 LEU A CD1 
1612 C CD2 . LEU A 209 ? 0.59007 0.70494 0.60923 0.09680  -0.04794 0.02399  209 LEU A CD2 
1613 N N   . GLN A 210 ? 0.65669 0.85477 0.69137 0.12350  -0.10206 0.03360  210 GLN A N   
1614 C CA  . GLN A 210 ? 0.66914 0.90427 0.71184 0.12722  -0.12027 0.03400  210 GLN A CA  
1615 C C   . GLN A 210 ? 0.67683 0.92738 0.71827 0.10406  -0.12725 0.02038  210 GLN A C   
1616 O O   . GLN A 210 ? 0.67752 0.89967 0.69000 0.09237  -0.12488 0.01532  210 GLN A O   
1617 C CB  . GLN A 210 ? 0.68365 0.90815 0.70055 0.14257  -0.13008 0.04647  210 GLN A CB  
1618 C CG  . GLN A 210 ? 0.68729 0.90013 0.70976 0.16668  -0.12562 0.06120  210 GLN A CG  
1619 C CD  . GLN A 210 ? 0.70911 0.89417 0.69920 0.17819  -0.12842 0.07585  210 GLN A CD  
1620 O OE1 . GLN A 210 ? 0.71354 0.86745 0.69667 0.18871  -0.11887 0.08622  210 GLN A OE1 
1621 N NE2 . GLN A 210 ? 0.72345 0.91910 0.69223 0.17518  -0.14134 0.07665  210 GLN A NE2 
1622 N N   . PRO A 211 ? 0.68579 0.98005 0.75743 0.09674  -0.13523 0.01427  211 PRO A N   
1623 C CA  . PRO A 211 ? 0.70123 1.00722 0.77325 0.07045  -0.14102 0.00051  211 PRO A CA  
1624 C C   . PRO A 211 ? 0.73868 1.04764 0.78383 0.06516  -0.15903 -0.00310 211 PRO A C   
1625 O O   . PRO A 211 ? 0.75373 1.07920 0.79317 0.08188  -0.17166 0.00567  211 PRO A O   
1626 C CB  . PRO A 211 ? 0.69076 1.05023 0.80708 0.06587  -0.14468 -0.00198 211 PRO A CB  
1627 C CG  . PRO A 211 ? 0.67571 1.04472 0.81303 0.09222  -0.13670 0.00939  211 PRO A CG  
1628 C CD  . PRO A 211 ? 0.68183 1.01678 0.78968 0.11246  -0.13782 0.02017  211 PRO A CD  
1629 N N   . VAL A 212 ? 0.76458 1.05644 0.79165 0.04180  -0.16005 -0.01639 212 VAL A N   
1630 C CA  . VAL A 212 ? 0.81236 1.09619 0.80534 0.03436  -0.17473 -0.02350 212 VAL A CA  
1631 C C   . VAL A 212 ? 0.84194 1.17220 0.85361 0.01569  -0.19364 -0.03366 212 VAL A C   
1632 O O   . VAL A 212 ? 0.86990 1.23349 0.88013 0.02340  -0.21231 -0.03060 212 VAL A O   
1633 C CB  . VAL A 212 ? 0.82000 1.04977 0.77630 0.02264  -0.16309 -0.03234 212 VAL A CB  
1634 C CG1 . VAL A 212 ? 0.85555 1.07505 0.77572 0.01129  -0.17730 -0.04432 212 VAL A CG1 
1635 C CG2 . VAL A 212 ? 0.80495 0.99923 0.74234 0.04253  -0.14789 -0.02021 212 VAL A CG2 
1636 N N   . ASN A 213 ? 0.85166 1.18714 0.88204 -0.00948 -0.18905 -0.04456 213 ASN A N   
1637 C CA  . ASN A 213 ? 0.86951 1.25342 0.92443 -0.03244 -0.20531 -0.05400 213 ASN A CA  
1638 C C   . ASN A 213 ? 0.82199 1.24913 0.92929 -0.03753 -0.19766 -0.04998 213 ASN A C   
1639 O O   . ASN A 213 ? 0.81471 1.29632 0.95434 -0.02260 -0.20622 -0.04106 213 ASN A O   
1640 C CB  . ASN A 213 ? 0.91132 1.26263 0.93630 -0.06376 -0.20942 -0.07238 213 ASN A CB  
1641 C CG  . ASN A 213 ? 0.96444 1.28042 0.93640 -0.05812 -0.21889 -0.07830 213 ASN A CG  
1642 O OD1 . ASN A 213 ? 0.97797 1.31676 0.94148 -0.03989 -0.23243 -0.07132 213 ASN A OD1 
1643 N ND2 . ASN A 213 ? 0.99486 1.25449 0.92953 -0.07248 -0.21085 -0.09059 213 ASN A ND2 
1644 N N   . ASP A 214 ? 0.78466 1.19164 0.90103 -0.05637 -0.18147 -0.05524 214 ASP A N   
1645 C CA  . ASP A 214 ? 0.73130 1.18225 0.89626 -0.06009 -0.17276 -0.05056 214 ASP A CA  
1646 C C   . ASP A 214 ? 0.68960 1.15364 0.87291 -0.02517 -0.16343 -0.03594 214 ASP A C   
1647 O O   . ASP A 214 ? 0.68839 1.10738 0.84633 -0.00591 -0.15327 -0.03028 214 ASP A O   
1648 C CB  . ASP A 214 ? 0.71390 1.13255 0.87919 -0.08233 -0.15378 -0.05584 214 ASP A CB  
1649 C CG  . ASP A 214 ? 0.69637 1.15696 0.90880 -0.08169 -0.14019 -0.04892 214 ASP A CG  
1650 O OD1 . ASP A 214 ? 0.69035 1.21596 0.94150 -0.07535 -0.14858 -0.04416 214 ASP A OD1 
1651 O OD2 . ASP A 214 ? 0.69331 1.12295 0.90298 -0.08634 -0.12038 -0.04780 214 ASP A OD2 
1652 N N   . LYS A 215 ? 0.66750 1.19379 0.89462 -0.01696 -0.16681 -0.02987 215 LYS A N   
1653 C CA  . LYS A 215 ? 0.62365 1.16230 0.86689 0.01821  -0.15944 -0.01689 215 LYS A CA  
1654 C C   . LYS A 215 ? 0.57902 1.13276 0.85441 0.02116  -0.13956 -0.01428 215 LYS A C   
1655 O O   . LYS A 215 ? 0.55571 1.11938 0.84542 0.05001  -0.13197 -0.00532 215 LYS A O   
1656 C CB  . LYS A 215 ? 0.62776 1.22449 0.89095 0.03639  -0.17905 -0.00940 215 LYS A CB  
1657 C CG  . LYS A 215 ? 0.64759 1.22843 0.87436 0.04109  -0.19828 -0.00907 215 LYS A CG  
1658 C CD  . LYS A 215 ? 0.66633 1.31406 0.91442 0.05514  -0.22049 -0.00182 215 LYS A CD  
1659 C CE  . LYS A 215 ? 0.70344 1.33701 0.91224 0.05899  -0.23974 -0.00141 215 LYS A CE  
1660 N NZ  . LYS A 215 ? 0.73185 1.43511 0.96013 0.07039  -0.26339 0.00551  215 LYS A NZ  
1661 N N   . ASP A 216 ? 0.56844 1.11984 0.85208 -0.00712 -0.12997 -0.02171 216 ASP A N   
1662 C CA  . ASP A 216 ? 0.55706 1.12508 0.86912 -0.00565 -0.11044 -0.01901 216 ASP A CA  
1663 C C   . ASP A 216 ? 0.55875 1.06259 0.84251 -0.00706 -0.09067 -0.02038 216 ASP A C   
1664 O O   . ASP A 216 ? 0.57886 1.03686 0.83121 -0.02540 -0.09046 -0.02626 216 ASP A O   
1665 C CB  . ASP A 216 ? 0.55924 1.17799 0.90498 -0.03628 -0.11203 -0.02344 216 ASP A CB  
1666 C CG  . ASP A 216 ? 0.57251 1.26267 0.94873 -0.03733 -0.13300 -0.02205 216 ASP A CG  
1667 O OD1 . ASP A 216 ? 0.57151 1.27959 0.95058 -0.00663 -0.14215 -0.01486 216 ASP A OD1 
1668 O OD2 . ASP A 216 ? 0.58524 1.31384 0.98206 -0.06907 -0.14062 -0.02741 216 ASP A OD2 
1669 N N   . PHE A 217 ? 0.55432 1.05589 0.84817 0.01375  -0.07426 -0.01510 217 PHE A N   
1670 C CA  . PHE A 217 ? 0.54280 0.99049 0.81168 0.01503  -0.05627 -0.01553 217 PHE A CA  
1671 C C   . PHE A 217 ? 0.51903 0.98677 0.81158 0.02179  -0.03762 -0.01350 217 PHE A C   
1672 O O   . PHE A 217 ? 0.51615 1.02978 0.83940 0.03861  -0.03666 -0.01014 217 PHE A O   
1673 C CB  . PHE A 217 ? 0.56190 0.96455 0.80070 0.03856  -0.05593 -0.01163 217 PHE A CB  
1674 C CG  . PHE A 217 ? 0.58806 0.97297 0.80223 0.03784  -0.07261 -0.01181 217 PHE A CG  
1675 C CD1 . PHE A 217 ? 0.60148 0.94088 0.78126 0.02316  -0.07233 -0.01591 217 PHE A CD1 
1676 C CD2 . PHE A 217 ? 0.60140 1.01740 0.82588 0.05312  -0.08850 -0.00742 217 PHE A CD2 
1677 C CE1 . PHE A 217 ? 0.62826 0.95252 0.78301 0.02345  -0.08690 -0.01671 217 PHE A CE1 
1678 C CE2 . PHE A 217 ? 0.62628 1.02813 0.82579 0.05257  -0.10404 -0.00730 217 PHE A CE2 
1679 C CZ  . PHE A 217 ? 0.63996 0.99562 0.80391 0.03738  -0.10300 -0.01254 217 PHE A CZ  
1680 N N   . GLN A 218 ? 0.50405 0.93502 0.77878 0.01148  -0.02234 -0.01512 218 GLN A N   
1681 C CA  . GLN A 218 ? 0.50647 0.94534 0.79323 0.01762  -0.00285 -0.01377 218 GLN A CA  
1682 C C   . GLN A 218 ? 0.51644 0.91124 0.77693 0.03975  0.00477  -0.01277 218 GLN A C   
1683 O O   . GLN A 218 ? 0.51066 0.85792 0.73908 0.03388  0.00638  -0.01328 218 GLN A O   
1684 C CB  . GLN A 218 ? 0.50999 0.93799 0.79233 -0.00963 0.00863  -0.01498 218 GLN A CB  
1685 C CG  . GLN A 218 ? 0.50469 0.96253 0.80942 -0.00819 0.02663  -0.01286 218 GLN A CG  
1686 C CD  . GLN A 218 ? 0.49707 1.01735 0.84172 -0.02372 0.02433  -0.01161 218 GLN A CD  
1687 O OE1 . GLN A 218 ? 0.50460 1.03114 0.85251 -0.04938 0.01355  -0.01323 218 GLN A OE1 
1688 N NE2 . GLN A 218 ? 0.48283 1.05082 0.85777 -0.00869 0.03444  -0.00912 218 GLN A NE2 
1689 N N   . ILE A 219 ? 0.53619 0.94648 0.80956 0.06498  0.00956  -0.01141 219 ILE A N   
1690 C CA  . ILE A 219 ? 0.53222 0.90037 0.78116 0.08423  0.01616  -0.01147 219 ILE A CA  
1691 C C   . ILE A 219 ? 0.52286 0.89252 0.77474 0.08730  0.03561  -0.01440 219 ILE A C   
1692 O O   . ILE A 219 ? 0.51411 0.92725 0.79433 0.09160  0.04336  -0.01489 219 ILE A O   
1693 C CB  . ILE A 219 ? 0.53928 0.91089 0.79236 0.11165  0.00753  -0.00829 219 ILE A CB  
1694 C CG1 . ILE A 219 ? 0.54845 0.91472 0.79204 0.10759  -0.01159 -0.00466 219 ILE A CG1 
1695 C CG2 . ILE A 219 ? 0.53888 0.86416 0.76677 0.12840  0.01601  -0.00919 219 ILE A CG2 
1696 C CD1 . ILE A 219 ? 0.56253 0.94524 0.81617 0.13266  -0.02195 0.00085  219 ILE A CD1 
1697 N N   . SER A 220 ? 0.52333 0.84911 0.74575 0.08518  0.04345  -0.01604 220 SER A N   
1698 C CA  . SER A 220 ? 0.52447 0.84752 0.74281 0.08664  0.06105  -0.01937 220 SER A CA  
1699 C C   . SER A 220 ? 0.52788 0.81632 0.72508 0.10573  0.06462  -0.02282 220 SER A C   
1700 O O   . SER A 220 ? 0.54257 0.79186 0.71431 0.10419  0.05834  -0.02158 220 SER A O   
1701 C CB  . SER A 220 ? 0.52748 0.83257 0.72877 0.06431  0.06779  -0.01807 220 SER A CB  
1702 O OG  . SER A 220 ? 0.53672 0.87502 0.75936 0.04679  0.07049  -0.01583 220 SER A OG  
1703 N N   . VAL A 221 ? 0.52097 0.82317 0.72742 0.12268  0.07554  -0.02744 221 VAL A N   
1704 C CA  . VAL A 221 ? 0.54660 0.81212 0.73041 0.13871  0.08059  -0.03300 221 VAL A CA  
1705 C C   . VAL A 221 ? 0.55742 0.82619 0.73384 0.13650  0.09775  -0.03948 221 VAL A C   
1706 O O   . VAL A 221 ? 0.57352 0.87693 0.76950 0.14654  0.10859  -0.04235 221 VAL A O   
1707 C CB  . VAL A 221 ? 0.57422 0.84307 0.76859 0.16615  0.07757  -0.03387 221 VAL A CB  
1708 C CG1 . VAL A 221 ? 0.60466 0.82577 0.77057 0.17888  0.08287  -0.04057 221 VAL A CG1 
1709 C CG2 . VAL A 221 ? 0.57915 0.85011 0.78041 0.16747  0.05989  -0.02571 221 VAL A CG2 
1710 N N   . ASP A 222 ? 0.55514 0.79124 0.70307 0.12414  0.10031  -0.04117 222 ASP A N   
1711 C CA  . ASP A 222 ? 0.55603 0.79348 0.69162 0.12119  0.11532  -0.04694 222 ASP A CA  
1712 C C   . ASP A 222 ? 0.56163 0.84431 0.72044 0.11268  0.12527  -0.04323 222 ASP A C   
1713 O O   . ASP A 222 ? 0.58065 0.88590 0.74602 0.12176  0.13926  -0.04804 222 ASP A O   
1714 C CB  . ASP A 222 ? 0.55685 0.77970 0.68198 0.14235  0.12327  -0.05790 222 ASP A CB  
1715 C CG  . ASP A 222 ? 0.55516 0.72820 0.65349 0.14575  0.11499  -0.06151 222 ASP A CG  
1716 O OD1 . ASP A 222 ? 0.53054 0.68401 0.61508 0.12960  0.10615  -0.05588 222 ASP A OD1 
1717 O OD2 . ASP A 222 ? 0.57852 0.73100 0.66878 0.16430  0.11786  -0.06951 222 ASP A OD2 
1718 N N   . HIS A 223 ? 0.55948 0.85533 0.73065 0.09514  0.11828  -0.03469 223 HIS A N   
1719 C CA  . HIS A 223 ? 0.58534 0.91610 0.77489 0.07962  0.12618  -0.02911 223 HIS A CA  
1720 C C   . HIS A 223 ? 0.59489 0.97577 0.82166 0.08711  0.12856  -0.02851 223 HIS A C   
1721 O O   . HIS A 223 ? 0.59095 1.00746 0.83700 0.07288  0.13691  -0.02348 223 HIS A O   
1722 C CB  . HIS A 223 ? 0.60631 0.93784 0.78041 0.07457  0.14282  -0.02980 223 HIS A CB  
1723 C CG  . HIS A 223 ? 0.59453 0.93646 0.77166 0.05200  0.14752  -0.02048 223 HIS A CG  
1724 N ND1 . HIS A 223 ? 0.58517 0.90245 0.75208 0.03628  0.13719  -0.01438 223 HIS A ND1 
1725 C CD2 . HIS A 223 ? 0.59630 0.96821 0.78443 0.04259  0.16197  -0.01557 223 HIS A CD2 
1726 C CE1 . HIS A 223 ? 0.58767 0.91438 0.75740 0.01816  0.14494  -0.00651 223 HIS A CE1 
1727 N NE2 . HIS A 223 ? 0.59432 0.95474 0.77748 0.02047  0.15992  -0.00627 223 HIS A NE2 
1728 N N   . LEU A 224 ? 0.60741 0.99479 0.84533 0.10925  0.12307  -0.03241 224 LEU A N   
1729 C CA  . LEU A 224 ? 0.61470 1.05347 0.89049 0.11745  0.12101  -0.02976 224 LEU A CA  
1730 C C   . LEU A 224 ? 0.61237 1.05503 0.89871 0.10293  0.10243  -0.02389 224 LEU A C   
1731 O O   . LEU A 224 ? 0.61375 1.01551 0.87816 0.10416  0.09016  -0.02411 224 LEU A O   
1732 C CB  . LEU A 224 ? 0.63160 1.06843 0.90949 0.15020  0.12228  -0.03541 224 LEU A CB  
1733 C CG  . LEU A 224 ? 0.64531 1.12850 0.95805 0.16957  0.11768  -0.03248 224 LEU A CG  
1734 C CD1 . LEU A 224 ? 0.64914 1.19298 0.99225 0.17083  0.13348  -0.03132 224 LEU A CD1 
1735 C CD2 . LEU A 224 ? 0.67320 1.12449 0.97069 0.20182  0.11758  -0.03801 224 LEU A CD2 
1736 N N   . SER A 225 ? 0.61064 1.09997 0.92737 0.08706  0.10026  -0.01891 225 SER A N   
1737 C CA  . SER A 225 ? 0.58845 1.07376 0.90770 0.07121  0.08165  -0.01563 225 SER A CA  
1738 C C   . SER A 225 ? 0.58219 1.12587 0.94033 0.07592  0.07260  -0.01285 225 SER A C   
1739 O O   . SER A 225 ? 0.57710 1.17184 0.96544 0.06298  0.07865  -0.00993 225 SER A O   
1740 C CB  . SER A 225 ? 0.57891 1.04593 0.88537 0.03968  0.08238  -0.01296 225 SER A CB  
1741 O OG  . SER A 225 ? 0.57750 1.02322 0.87358 0.02988  0.06433  -0.01260 225 SER A OG  
1742 N N   . ILE A 226 ? 0.57598 1.11215 0.93211 0.09321  0.05815  -0.01266 226 ILE A N   
1743 C CA  . ILE A 226 ? 0.58354 1.17196 0.97239 0.10300  0.04583  -0.00909 226 ILE A CA  
1744 C C   . ILE A 226 ? 0.60118 1.18934 0.98827 0.07802  0.02686  -0.00769 226 ILE A C   
1745 O O   . ILE A 226 ? 0.60867 1.14272 0.96188 0.06958  0.01990  -0.00937 226 ILE A O   
1746 C CB  . ILE A 226 ? 0.59205 1.16604 0.97434 0.13942  0.04103  -0.00849 226 ILE A CB  
1747 C CG1 . ILE A 226 ? 0.59843 1.15950 0.97403 0.16460  0.06028  -0.01264 226 ILE A CG1 
1748 C CG2 . ILE A 226 ? 0.60939 1.24229 1.02621 0.15220  0.02833  -0.00298 226 ILE A CG2 
1749 C CD1 . ILE A 226 ? 0.60214 1.09032 0.93410 0.16694  0.06609  -0.01795 226 ILE A CD1 
1750 N N   . LEU A 227 ? 0.61469 1.26338 1.03669 0.06574  0.01807  -0.00507 227 LEU A N   
1751 C CA  . LEU A 227 ? 0.61628 1.26485 1.03407 0.04787  -0.00334 -0.00536 227 LEU A CA  
1752 C C   . LEU A 227 ? 0.61903 1.28929 1.04593 0.07579  -0.01880 -0.00158 227 LEU A C   
1753 O O   . LEU A 227 ? 0.61338 1.33705 1.07270 0.09703  -0.01623 0.00255  227 LEU A O   
1754 C CB  . LEU A 227 ? 0.61855 1.31506 1.06401 0.01375  -0.00755 -0.00550 227 LEU A CB  
1755 C CG  . LEU A 227 ? 0.61810 1.33199 1.06644 0.00264  -0.03264 -0.00663 227 LEU A CG  
1756 C CD1 . LEU A 227 ? 0.62281 1.26558 1.02469 -0.00821 -0.04176 -0.01154 227 LEU A CD1 
1757 C CD2 . LEU A 227 ? 0.62017 1.39390 1.10262 -0.02996 -0.03916 -0.00700 227 LEU A CD2 
1758 N N   . HIS A 228 ? 0.63141 1.26020 1.02853 0.07813  -0.03354 -0.00190 228 HIS A N   
1759 C CA  . HIS A 228 ? 0.65280 1.29810 1.05377 0.10293  -0.04972 0.00350  228 HIS A CA  
1760 C C   . HIS A 228 ? 0.66310 1.33231 1.06645 0.08173  -0.07233 0.00258  228 HIS A C   
1761 O O   . HIS A 228 ? 0.66990 1.30405 1.04849 0.05444  -0.07689 -0.00330 228 HIS A O   
1762 C CB  . HIS A 228 ? 0.66627 1.24622 1.02949 0.12584  -0.04830 0.00552  228 HIS A CB  
1763 C CG  . HIS A 228 ? 0.67544 1.23327 1.03537 0.14867  -0.02870 0.00526  228 HIS A CG  
1764 N ND1 . HIS A 228 ? 0.69172 1.24437 1.05185 0.18437  -0.02741 0.01032  228 HIS A ND1 
1765 C CD2 . HIS A 228 ? 0.67001 1.20825 1.02408 0.14086  -0.00965 0.00004  228 HIS A CD2 
1766 C CE1 . HIS A 228 ? 0.69434 1.22271 1.04770 0.19644  -0.00849 0.00643  228 HIS A CE1 
1767 N NE2 . HIS A 228 ? 0.68088 1.20246 1.03058 0.17046  0.00215  0.00024  228 HIS A NE2 
1768 N N   . ARG A 229 ? 0.66857 1.39778 1.10044 0.09604  -0.08635 0.00823  229 ARG A N   
1769 C CA  . ARG A 229 ? 0.67571 1.44382 1.11604 0.07831  -0.10990 0.00745  229 ARG A CA  
1770 C C   . ARG A 229 ? 0.67291 1.42970 1.09417 0.10493  -0.12663 0.01425  229 ARG A C   
1771 O O   . ARG A 229 ? 0.67176 1.42071 1.09291 0.14127  -0.12095 0.02249  229 ARG A O   
1772 C CB  . ARG A 229 ? 0.68503 1.54532 1.17849 0.07227  -0.11376 0.01023  229 ARG A CB  
1773 C CG  . ARG A 229 ? 0.70840 1.60964 1.21405 0.03481  -0.13333 0.00479  229 ARG A CG  
1774 C CD  . ARG A 229 ? 0.71977 1.61111 1.22875 -0.00629 -0.12178 -0.00325 229 ARG A CD  
1775 N NE  . ARG A 229 ? 0.71978 1.67074 1.27371 -0.00690 -0.10617 0.00121  229 ARG A NE  
1776 C CZ  . ARG A 229 ? 0.73055 1.69637 1.29993 -0.04289 -0.09687 -0.00232 229 ARG A CZ  
1777 N NH1 . ARG A 229 ? 0.74638 1.66730 1.28904 -0.08081 -0.10133 -0.01093 229 ARG A NH1 
1778 N NH2 . ARG A 229 ? 0.72558 1.75151 1.33689 -0.04005 -0.08189 0.00348  229 ARG A NH2 
1779 N N   . ASP A 230 ? 0.67422 1.42737 1.07669 0.08670  -0.14681 0.01078  230 ASP A N   
1780 C CA  . ASP A 230 ? 0.67626 1.42291 1.05776 0.10757  -0.16505 0.01773  230 ASP A CA  
1781 C C   . ASP A 230 ? 0.65944 1.34032 1.00878 0.13774  -0.15402 0.02485  230 ASP A C   
1782 O O   . ASP A 230 ? 0.68138 1.37112 1.03521 0.17224  -0.15626 0.03626  230 ASP A O   
1783 C CB  . ASP A 230 ? 0.69221 1.52178 1.11197 0.12623  -0.18079 0.02679  230 ASP A CB  
1784 C CG  . ASP A 230 ? 0.71663 1.54389 1.11422 0.14911  -0.20065 0.03612  230 ASP A CG  
1785 O OD1 . ASP A 230 ? 0.73072 1.52964 1.09443 0.13128  -0.21410 0.03076  230 ASP A OD1 
1786 O OD2 . ASP A 230 ? 0.72673 1.58076 1.13970 0.18649  -0.20225 0.04944  230 ASP A OD2 
1787 N N   . VAL A 231 ? 0.63019 1.24347 0.94543 0.12345  -0.14246 0.01849  231 VAL A N   
1788 C CA  . VAL A 231 ? 0.63297 1.18274 0.91838 0.14462  -0.13015 0.02378  231 VAL A CA  
1789 C C   . VAL A 231 ? 0.65026 1.16961 0.90027 0.15345  -0.14408 0.03003  231 VAL A C   
1790 O O   . VAL A 231 ? 0.66413 1.17912 0.89493 0.13275  -0.15642 0.02445  231 VAL A O   
1791 C CB  . VAL A 231 ? 0.62073 1.11985 0.88780 0.12528  -0.11191 0.01537  231 VAL A CB  
1792 C CG1 . VAL A 231 ? 0.62716 1.06457 0.86398 0.14348  -0.10067 0.02041  231 VAL A CG1 
1793 C CG2 . VAL A 231 ? 0.61156 1.14077 0.91095 0.11643  -0.09728 0.01043  231 VAL A CG2 
1794 N N   . GLN A 232 ? 0.65277 1.14628 0.89073 0.18387  -0.14088 0.04153  232 GLN A N   
1795 C CA  . GLN A 232 ? 0.64782 1.10951 0.85081 0.19428  -0.15136 0.05038  232 GLN A CA  
1796 C C   . GLN A 232 ? 0.64312 1.03338 0.81075 0.19493  -0.13748 0.05225  232 GLN A C   
1797 O O   . GLN A 232 ? 0.64979 1.01132 0.78457 0.18954  -0.14378 0.05509  232 GLN A O   
1798 C CB  . GLN A 232 ? 0.65552 1.14295 0.86881 0.22873  -0.16091 0.06564  232 GLN A CB  
1799 N N   . GLU A 233 ? 0.63180 0.99601 0.80512 0.20085  -0.11896 0.05055  233 GLU A N   
1800 C CA  . GLU A 233 ? 0.63278 0.93465 0.77650 0.19984  -0.10566 0.05196  233 GLU A CA  
1801 C C   . GLU A 233 ? 0.61395 0.90554 0.77158 0.19617  -0.08696 0.04368  233 GLU A C   
1802 O O   . GLU A 233 ? 0.61478 0.94021 0.80237 0.20666  -0.08280 0.04152  233 GLU A O   
1803 C CB  . GLU A 233 ? 0.66941 0.94004 0.79437 0.22571  -0.10726 0.06688  233 GLU A CB  
1804 C CG  . GLU A 233 ? 0.68567 0.89852 0.77264 0.21908  -0.10157 0.07188  233 GLU A CG  
1805 C CD  . GLU A 233 ? 0.72305 0.90053 0.79429 0.24305  -0.09974 0.08700  233 GLU A CD  
1806 O OE1 . GLU A 233 ? 0.74208 0.93545 0.83034 0.26746  -0.10191 0.09305  233 GLU A OE1 
1807 O OE2 . GLU A 233 ? 0.73750 0.87084 0.77954 0.23778  -0.09525 0.09345  233 GLU A OE2 
1808 N N   . ILE A 234 ? 0.59624 0.84591 0.73194 0.18078  -0.07598 0.03905  234 ILE A N   
1809 C CA  . ILE A 234 ? 0.58148 0.80779 0.71873 0.17994  -0.05821 0.03338  234 ILE A CA  
1810 C C   . ILE A 234 ? 0.59654 0.76866 0.70288 0.18461  -0.05320 0.03968  234 ILE A C   
1811 O O   . ILE A 234 ? 0.60258 0.75529 0.68528 0.17391  -0.05808 0.04349  234 ILE A O   
1812 C CB  . ILE A 234 ? 0.55607 0.78671 0.69629 0.15455  -0.04976 0.02261  234 ILE A CB  
1813 C CG1 . ILE A 234 ? 0.54356 0.82635 0.71310 0.14437  -0.05516 0.01713  234 ILE A CG1 
1814 C CG2 . ILE A 234 ? 0.55528 0.76312 0.69390 0.15464  -0.03201 0.01731  234 ILE A CG2 
1815 C CD1 . ILE A 234 ? 0.52740 0.80782 0.69483 0.11825  -0.04804 0.00875  234 ILE A CD1 
1816 N N   . ARG A 235 ? 0.60547 0.75375 0.71112 0.20016  -0.04354 0.04072  235 ARG A N   
1817 C CA  . ARG A 235 ? 0.62284 0.71932 0.70005 0.20269  -0.03955 0.04727  235 ARG A CA  
1818 C C   . ARG A 235 ? 0.62150 0.69248 0.69397 0.19548  -0.02427 0.03797  235 ARG A C   
1819 O O   . ARG A 235 ? 0.61935 0.70172 0.70867 0.20611  -0.01638 0.03074  235 ARG A O   
1820 C CB  . ARG A 235 ? 0.64891 0.73170 0.72223 0.22884  -0.04508 0.05929  235 ARG A CB  
1821 C CG  . ARG A 235 ? 0.65291 0.76473 0.72897 0.23735  -0.06177 0.06977  235 ARG A CG  
1822 C CD  . ARG A 235 ? 0.68933 0.79265 0.76454 0.26768  -0.06671 0.08311  235 ARG A CD  
1823 N NE  . ARG A 235 ? 0.72150 0.76501 0.76733 0.27219  -0.06109 0.09259  235 ARG A NE  
1824 C CZ  . ARG A 235 ? 0.73676 0.75748 0.75695 0.26682  -0.06713 0.10501  235 ARG A CZ  
1825 N NH1 . ARG A 235 ? 0.72394 0.77460 0.74097 0.25951  -0.07958 0.10900  235 ARG A NH1 
1826 N NH2 . ARG A 235 ? 0.76774 0.73375 0.76347 0.26763  -0.06008 0.11326  235 ARG A NH2 
1827 N N   . TYR A 236 ? 0.62182 0.66360 0.67206 0.17764  -0.02005 0.03786  236 TYR A N   
1828 C CA  . TYR A 236 ? 0.62197 0.63984 0.66445 0.16930  -0.00724 0.02947  236 TYR A CA  
1829 C C   . TYR A 236 ? 0.64450 0.61427 0.66273 0.17087  -0.00527 0.03584  236 TYR A C   
1830 O O   . TYR A 236 ? 0.65412 0.61033 0.65645 0.16518  -0.01134 0.04657  236 TYR A O   
1831 C CB  . TYR A 236 ? 0.60244 0.62935 0.64085 0.14656  -0.00274 0.02373  236 TYR A CB  
1832 C CG  . TYR A 236 ? 0.58955 0.65698 0.64856 0.14038  -0.00324 0.01759  236 TYR A CG  
1833 C CD1 . TYR A 236 ? 0.58622 0.67423 0.66438 0.14370  0.00513  0.00868  236 TYR A CD1 
1834 C CD2 . TYR A 236 ? 0.58929 0.67209 0.64620 0.12974  -0.01116 0.02051  236 TYR A CD2 
1835 C CE1 . TYR A 236 ? 0.57651 0.70066 0.67342 0.13493  0.00538  0.00453  236 TYR A CE1 
1836 C CE2 . TYR A 236 ? 0.58382 0.69751 0.65705 0.12094  -0.01154 0.01474  236 TYR A CE2 
1837 C CZ  . TYR A 236 ? 0.57728 0.71200 0.67140 0.12258  -0.00330 0.00755  236 TYR A CZ  
1838 O OH  . TYR A 236 ? 0.57392 0.73921 0.68490 0.11140  -0.00286 0.00311  236 TYR A OH  
1839 N N   . GLU A 237 ? 0.65000 0.59328 0.66385 0.17722  0.00375  0.02892  237 GLU A N   
1840 C CA  . GLU A 237 ? 0.67332 0.56707 0.66201 0.17122  0.00689  0.03230  237 GLU A CA  
1841 C C   . GLU A 237 ? 0.68174 0.55687 0.66506 0.16646  0.01822  0.01769  237 GLU A C   
1842 O O   . GLU A 237 ? 0.67710 0.57272 0.67564 0.17617  0.02424  0.00694  237 GLU A O   
1843 C CB  . GLU A 237 ? 0.71262 0.57617 0.69268 0.19114  0.00245  0.04374  237 GLU A CB  
1844 C CG  . GLU A 237 ? 0.73185 0.60199 0.72721 0.21866  0.00507  0.03916  237 GLU A CG  
1845 C CD  . GLU A 237 ? 0.75906 0.61746 0.75181 0.24213  -0.00266 0.05433  237 GLU A CD  
1846 O OE1 . GLU A 237 ? 0.78957 0.60438 0.75874 0.23919  -0.00436 0.06554  237 GLU A OE1 
1847 O OE2 . GLU A 237 ? 0.75041 0.64569 0.76501 0.26302  -0.00718 0.05624  237 GLU A OE2 
1848 N N   . VAL A 238 ? 0.69657 0.53487 0.65744 0.15030  0.02104  0.01748  238 VAL A N   
1849 C CA  . VAL A 238 ? 0.71210 0.52527 0.66192 0.14536  0.03039  0.00295  238 VAL A CA  
1850 C C   . VAL A 238 ? 0.75665 0.53872 0.70346 0.17055  0.03449  -0.00136 238 VAL A C   
1851 O O   . VAL A 238 ? 0.78946 0.53913 0.72660 0.18209  0.03055  0.00950  238 VAL A O   
1852 C CB  . VAL A 238 ? 0.71618 0.49845 0.64274 0.12026  0.03052  0.00456  238 VAL A CB  
1853 C CG1 . VAL A 238 ? 0.74920 0.49987 0.66003 0.11457  0.03858  -0.01177 238 VAL A CG1 
1854 C CG2 . VAL A 238 ? 0.66940 0.48845 0.60073 0.09980  0.02816  0.00830  238 VAL A CG2 
1855 N N   . SER A 239 ? 0.69461 0.66825 0.62722 0.27487  0.10450  -0.00413 239 SER A N   
1856 C CA  . SER A 239 ? 0.72539 0.67401 0.64990 0.29329  0.10351  -0.01162 239 SER A CA  
1857 C C   . SER A 239 ? 0.77292 0.66176 0.67862 0.28582  0.10799  0.00646  239 SER A C   
1858 O O   . SER A 239 ? 0.77560 0.64352 0.68143 0.25826  0.11170  0.01840  239 SER A O   
1859 C CB  . SER A 239 ? 0.70188 0.66301 0.64320 0.28667  0.10309  -0.03868 239 SER A CB  
1860 O OG  . SER A 239 ? 0.73229 0.66660 0.66439 0.30416  0.10345  -0.04626 239 SER A OG  
1861 N N   . ALA A 240 ? 0.80922 0.66968 0.69988 0.31095  0.10643  0.00758  240 ALA A N   
1862 C CA  . ALA A 240 ? 0.85587 0.65133 0.72958 0.30353  0.10885  0.01933  240 ALA A CA  
1863 C C   . ALA A 240 ? 0.85613 0.63073 0.73474 0.28768  0.10858  -0.00337 240 ALA A C   
1864 O O   . ALA A 240 ? 0.89222 0.62031 0.76345 0.26570  0.10927  0.00261  240 ALA A O   
1865 C CB  . ALA A 240 ? 0.90620 0.67177 0.75855 0.33833  0.10671  0.02937  240 ALA A CB  
1866 N N   . LYS A 241 ? 0.81790 0.62827 0.70938 0.29768  0.10751  -0.02927 241 LYS A N   
1867 C CA  . LYS A 241 ? 0.81718 0.61521 0.71106 0.28511  0.10908  -0.05066 241 LYS A CA  
1868 C C   . LYS A 241 ? 0.78726 0.59588 0.69171 0.24851  0.11095  -0.05099 241 LYS A C   
1869 O O   . LYS A 241 ? 0.75637 0.59742 0.67285 0.23649  0.11122  -0.04063 241 LYS A O   
1870 C CB  . LYS A 241 ? 0.78948 0.63072 0.69703 0.30644  0.10972  -0.07474 241 LYS A CB  
1871 C CG  . LYS A 241 ? 0.80867 0.65649 0.71102 0.34486  0.10589  -0.07290 241 LYS A CG  
1872 C CD  . LYS A 241 ? 0.77381 0.68034 0.70041 0.35655  0.10359  -0.09355 241 LYS A CD  
1873 C CE  . LYS A 241 ? 0.79495 0.70766 0.71823 0.38261  0.09495  -0.09043 241 LYS A CE  
1874 N NZ  . LYS A 241 ? 0.75606 0.73412 0.71048 0.38125  0.08989  -0.10564 241 LYS A NZ  
1875 N N   . LYS A 242 ? 0.81334 0.59303 0.71066 0.23314  0.11134  -0.06345 242 LYS A N   
1876 C CA  . LYS A 242 ? 0.78869 0.57427 0.69227 0.20074  0.11161  -0.06527 242 LYS A CA  
1877 C C   . LYS A 242 ? 0.79781 0.59090 0.69951 0.20075  0.11425  -0.09006 242 LYS A C   
1878 O O   . LYS A 242 ? 0.82893 0.60560 0.71986 0.22248  0.11531  -0.10374 242 LYS A O   
1879 C CB  . LYS A 242 ? 0.81016 0.54576 0.70313 0.17810  0.10757  -0.04970 242 LYS A CB  
1880 C CG  . LYS A 242 ? 0.80943 0.53810 0.70404 0.17720  0.10788  -0.02035 242 LYS A CG  
1881 C CD  . LYS A 242 ? 0.84607 0.52555 0.73535 0.15242  0.10475  -0.00280 242 LYS A CD  
1882 C CE  . LYS A 242 ? 0.81968 0.51701 0.72318 0.11815  0.10278  -0.00034 242 LYS A CE  
1883 N NZ  . LYS A 242 ? 0.77229 0.52294 0.69273 0.11315  0.10716  0.01476  242 LYS A NZ  
1884 N N   . ILE A 243 ? 0.77316 0.59281 0.68394 0.17930  0.11612  -0.09551 243 ILE A N   
1885 C CA  . ILE A 243 ? 0.78088 0.60418 0.68494 0.17785  0.11997  -0.11602 243 ILE A CA  
1886 C C   . ILE A 243 ? 0.82061 0.59900 0.70524 0.15861  0.11435  -0.11865 243 ILE A C   
1887 O O   . ILE A 243 ? 0.82074 0.58695 0.70819 0.13679  0.10873  -0.10408 243 ILE A O   
1888 C CB  . ILE A 243 ? 0.72851 0.60440 0.65080 0.16770  0.12575  -0.12081 243 ILE A CB  
1889 C CG1 . ILE A 243 ? 0.73836 0.61800 0.65013 0.16748  0.13211  -0.13915 243 ILE A CG1 
1890 C CG2 . ILE A 243 ? 0.69683 0.58041 0.62605 0.14185  0.12194  -0.10702 243 ILE A CG2 
1891 C CD1 . ILE A 243 ? 0.69783 0.62402 0.62570 0.15649  0.13947  -0.14160 243 ILE A CD1 
1892 N N   . HIS A 244 ? 0.85735 0.61306 0.72269 0.16753  0.11515  -0.13807 244 HIS A N   
1893 C CA  . HIS A 244 ? 0.90417 0.61574 0.74850 0.15119  0.10722  -0.14550 244 HIS A CA  
1894 C C   . HIS A 244 ? 0.89339 0.62924 0.73028 0.14162  0.11089  -0.15968 244 HIS A C   
1895 O O   . HIS A 244 ? 0.87791 0.64504 0.71490 0.15774  0.12124  -0.17164 244 HIS A O   
1896 C CB  . HIS A 244 ? 0.97545 0.63101 0.79644 0.17026  0.10253  -0.15775 244 HIS A CB  
1897 C CG  . HIS A 244 ? 1.00343 0.62943 0.82811 0.18042  0.09918  -0.14086 244 HIS A CG  
1898 N ND1 . HIS A 244 ? 1.02023 0.61393 0.84842 0.15873  0.09149  -0.12125 244 HIS A ND1 
1899 C CD2 . HIS A 244 ? 1.01665 0.64304 0.84203 0.21058  0.10292  -0.13890 244 HIS A CD2 
1900 C CE1 . HIS A 244 ? 1.04158 0.61411 0.86992 0.17496  0.09182  -0.10637 244 HIS A CE1 
1901 N NE2 . HIS A 244 ? 1.03930 0.63016 0.86463 0.20758  0.09774  -0.11729 244 HIS A NE2 
1902 N N   . PHE A 245 ? 0.90753 0.63129 0.73851 0.11593  0.10267  -0.15725 245 PHE A N   
1903 C CA  . PHE A 245 ? 0.91119 0.65309 0.72972 0.10669  0.10429  -0.16874 245 PHE A CA  
1904 C C   . PHE A 245 ? 0.98830 0.68195 0.77683 0.10276  0.09298  -0.18625 245 PHE A C   
1905 O O   . PHE A 245 ? 1.01439 0.66571 0.80133 0.09035  0.08014  -0.18237 245 PHE A O   
1906 C CB  . PHE A 245 ? 0.87074 0.64376 0.70573 0.08252  0.10215  -0.15311 245 PHE A CB  
1907 C CG  . PHE A 245 ? 0.82241 0.64355 0.68303 0.08669  0.11240  -0.14090 245 PHE A CG  
1908 C CD1 . PHE A 245 ? 0.80361 0.66158 0.66609 0.09025  0.12300  -0.14596 245 PHE A CD1 
1909 C CD2 . PHE A 245 ? 0.80377 0.63263 0.68587 0.08670  0.11112  -0.12430 245 PHE A CD2 
1910 C CE1 . PHE A 245 ? 0.76670 0.66473 0.65452 0.09179  0.13026  -0.13645 245 PHE A CE1 
1911 C CE2 . PHE A 245 ? 0.76780 0.63859 0.67166 0.09136  0.11791  -0.11660 245 PHE A CE2 
1912 C CZ  . PHE A 245 ? 0.74931 0.65306 0.65744 0.09288  0.12654  -0.12349 245 PHE A CZ  
1913 N N   . ALA A 246 ? 1.03584 0.73598 0.80059 0.11278  0.09745  -0.20547 246 ALA A N   
1914 C CA  . ALA A 246 ? 1.14589 0.80467 0.87923 0.10756  0.08433  -0.22442 246 ALA A CA  
1915 C C   . ALA A 246 ? 1.18216 0.85551 0.91732 0.07959  0.07503  -0.21732 246 ALA A C   
1916 O O   . ALA A 246 ? 1.13507 0.85407 0.87654 0.07531  0.08407  -0.20930 246 ALA A O   
1917 C CB  . ALA A 246 ? 1.18887 0.85044 0.89118 0.13254  0.09281  -0.24855 246 ALA A CB  
1918 N N   . ARG A 247 ? 1.28158 0.91654 1.01385 0.06018  0.05650  -0.21901 247 ARG A N   
1919 C CA  . ARG A 247 ? 1.34338 0.99228 1.08058 0.03367  0.04456  -0.21271 247 ARG A CA  
1920 C C   . ARG A 247 ? 1.46136 1.07818 1.16397 0.03091  0.02854  -0.23839 247 ARG A C   
1921 O O   . ARG A 247 ? 1.51983 1.08377 1.21263 0.02824  0.01434  -0.25177 247 ARG A O   
1922 C CB  . ARG A 247 ? 1.32414 0.96461 1.09321 0.01021  0.03524  -0.19185 247 ARG A CB  
1923 N N   . PHE A 248 ? 1.49164 1.13805 1.17435 0.03189  0.02986  -0.24526 248 PHE A N   
1924 C CA  . PHE A 248 ? 1.56945 1.19022 1.21622 0.03025  0.01280  -0.27040 248 PHE A CA  
1925 C C   . PHE A 248 ? 1.56287 1.19505 1.21800 0.00280  -0.00615 -0.26504 248 PHE A C   
1926 O O   . PHE A 248 ? 1.62632 1.22871 1.26014 -0.00502 -0.02740 -0.28598 248 PHE A O   
1927 C CB  . PHE A 248 ? 1.61261 1.25476 1.22200 0.05497  0.02627  -0.28526 248 PHE A CB  
1928 C CG  . PHE A 248 ? 1.66150 1.28574 1.25653 0.08388  0.03955  -0.29920 248 PHE A CG  
1929 C CD1 . PHE A 248 ? 1.73581 1.30237 1.30848 0.09330  0.02564  -0.32381 248 PHE A CD1 
1930 C CD2 . PHE A 248 ? 1.64067 1.30435 1.24789 0.10136  0.06455  -0.28777 248 PHE A CD2 
1931 C CE1 . PHE A 248 ? 1.77182 1.32108 1.33078 0.12329  0.03708  -0.33720 248 PHE A CE1 
1932 C CE2 . PHE A 248 ? 1.67333 1.32544 1.27053 0.12962  0.07610  -0.30093 248 PHE A CE2 
1933 C CZ  . PHE A 248 ? 1.73794 1.33290 1.30988 0.14218  0.06265  -0.32550 248 PHE A CZ  
1934 N N   . ARG A 249 ? 1.45811 1.13205 1.14447 -0.01115 -0.00073 -0.23906 249 ARG A N   
1935 C CA  . ARG A 249 ? 1.41868 1.10841 1.11677 -0.03527 -0.01880 -0.23297 249 ARG A CA  
1936 C C   . ARG A 249 ? 1.34776 1.06945 1.09071 -0.04942 -0.01237 -0.20278 249 ARG A C   
1937 O O   . ARG A 249 ? 1.32765 1.05725 1.08903 -0.04026 0.00485  -0.18828 249 ARG A O   
1938 C CB  . ARG A 249 ? 1.39776 1.11579 1.06425 -0.02885 -0.02094 -0.24052 249 ARG A CB  
1939 C CG  . ARG A 249 ? 1.34119 1.10037 1.00562 -0.01355 0.00331  -0.22439 249 ARG A CG  
1940 C CD  . ARG A 249 ? 1.33097 1.11642 0.96384 -0.00879 0.00120  -0.22669 249 ARG A CD  
1941 N NE  . ARG A 249 ? 1.26314 1.08650 0.90472 -0.00132 0.02286  -0.20477 249 ARG A NE  
1942 C CZ  . ARG A 249 ? 1.24885 1.09535 0.86272 0.00802  0.03073  -0.20084 249 ARG A CZ  
1943 N NH1 . ARG A 249 ? 1.29155 1.13170 0.86285 0.01403  0.01921  -0.21766 249 ARG A NH1 
1944 N NH2 . ARG A 249 ? 1.20286 1.07810 0.83082 0.01170  0.05023  -0.17939 249 ARG A NH2 
1945 N N   . SER A 250 ? 1.30774 1.04982 1.06778 -0.07035 -0.02746 -0.19463 250 SER A N   
1946 C CA  . SER A 250 ? 1.22808 1.00548 1.02812 -0.08144 -0.02184 -0.16709 250 SER A CA  
1947 C C   . SER A 250 ? 1.15901 0.97776 0.95419 -0.06786 -0.00677 -0.15523 250 SER A C   
1948 O O   . SER A 250 ? 1.17037 1.00490 0.94209 -0.06429 -0.01144 -0.16130 250 SER A O   
1949 C CB  . SER A 250 ? 1.22817 1.01863 1.05188 -0.10729 -0.04251 -0.16195 250 SER A CB  
1950 O OG  . SER A 250 ? 1.18331 1.00838 1.04555 -0.11466 -0.03474 -0.13526 250 SER A OG  
1951 N N   . PHE A 251 ? 1.06082 0.89426 0.87644 -0.05962 0.01070  -0.13863 251 PHE A N   
1952 C CA  . PHE A 251 ? 0.96728 0.83881 0.78937 -0.05181 0.02277  -0.12353 251 PHE A CA  
1953 C C   . PHE A 251 ? 0.88987 0.77578 0.74885 -0.05566 0.02856  -0.10393 251 PHE A C   
1954 O O   . PHE A 251 ? 0.87285 0.75603 0.73988 -0.04399 0.04242  -0.09959 251 PHE A O   
1955 C CB  . PHE A 251 ? 0.95222 0.82458 0.75269 -0.03237 0.04028  -0.12969 251 PHE A CB  
1956 C CG  . PHE A 251 ? 0.92475 0.82937 0.72471 -0.02751 0.04928  -0.11707 251 PHE A CG  
1957 C CD1 . PHE A 251 ? 0.90807 0.83547 0.71857 -0.03666 0.03986  -0.10439 251 PHE A CD1 
1958 C CD2 . PHE A 251 ? 0.91807 0.83022 0.70876 -0.01365 0.06719  -0.11727 251 PHE A CD2 
1959 C CE1 . PHE A 251 ? 0.88171 0.83189 0.68971 -0.03077 0.04765  -0.09234 251 PHE A CE1 
1960 C CE2 . PHE A 251 ? 0.89151 0.82784 0.68290 -0.01124 0.07553  -0.10439 251 PHE A CE2 
1961 C CZ  . PHE A 251 ? 0.87506 0.82701 0.67337 -0.01925 0.06545  -0.09191 251 PHE A CZ  
1962 N N   . PRO A 252 ? 0.84295 0.74609 0.72505 -0.07123 0.01747  -0.09241 252 PRO A N   
1963 C CA  . PRO A 252 ? 0.79516 0.71454 0.70991 -0.07345 0.02371  -0.07316 252 PRO A CA  
1964 C C   . PRO A 252 ? 0.74085 0.68569 0.66034 -0.05755 0.03797  -0.06318 252 PRO A C   
1965 O O   . PRO A 252 ? 0.73150 0.69219 0.63863 -0.05157 0.03941  -0.06416 252 PRO A O   
1966 C CB  . PRO A 252 ? 0.79139 0.73488 0.72834 -0.09185 0.00956  -0.06345 252 PRO A CB  
1967 C CG  . PRO A 252 ? 0.83315 0.76113 0.75196 -0.10271 -0.00702 -0.08042 252 PRO A CG  
1968 C CD  . PRO A 252 ? 0.85396 0.76568 0.73450 -0.08680 -0.00171 -0.09681 252 PRO A CD  
1969 N N   . PHE A 253 ? 0.71491 0.66102 0.65161 -0.05109 0.04738  -0.05343 253 PHE A N   
1970 C CA  . PHE A 253 ? 0.67071 0.63861 0.61551 -0.03637 0.05888  -0.04551 253 PHE A CA  
1971 C C   . PHE A 253 ? 0.63333 0.63454 0.58754 -0.03723 0.05518  -0.03523 253 PHE A C   
1972 O O   . PHE A 253 ? 0.60913 0.62046 0.55669 -0.02761 0.06033  -0.03582 253 PHE A O   
1973 C CB  . PHE A 253 ? 0.66770 0.63302 0.62921 -0.03117 0.06509  -0.03588 253 PHE A CB  
1974 C CG  . PHE A 253 ? 0.63973 0.62762 0.61098 -0.01679 0.07349  -0.02904 253 PHE A CG  
1975 C CD1 . PHE A 253 ? 0.63564 0.61932 0.59893 -0.00314 0.08183  -0.03839 253 PHE A CD1 
1976 C CD2 . PHE A 253 ? 0.62450 0.64067 0.61383 -0.01604 0.07275  -0.01429 253 PHE A CD2 
1977 C CE1 . PHE A 253 ? 0.61508 0.61875 0.58895 0.00925  0.08730  -0.03439 253 PHE A CE1 
1978 C CE2 . PHE A 253 ? 0.60750 0.64214 0.60321 -0.00068 0.07883  -0.01093 253 PHE A CE2 
1979 C CZ  . PHE A 253 ? 0.60401 0.63090 0.59235 0.01112  0.08508  -0.02160 253 PHE A CZ  
1980 N N   . TRP A 254 ? 0.63197 0.65117 0.60399 -0.04798 0.04681  -0.02462 254 TRP A N   
1981 C CA  . TRP A 254 ? 0.61237 0.66432 0.59246 -0.04458 0.04316  -0.01569 254 TRP A CA  
1982 C C   . TRP A 254 ? 0.62688 0.67646 0.58486 -0.04565 0.03611  -0.02398 254 TRP A C   
1983 O O   . TRP A 254 ? 0.61430 0.67685 0.56746 -0.03554 0.03813  -0.01986 254 TRP A O   
1984 C CB  . TRP A 254 ? 0.61014 0.68983 0.61594 -0.05481 0.03605  -0.00247 254 TRP A CB  
1985 C CG  . TRP A 254 ? 0.60400 0.69010 0.62952 -0.05237 0.04482  0.00980  254 TRP A CG  
1986 C CD1 . TRP A 254 ? 0.62352 0.70227 0.66362 -0.06711 0.04350  0.01671  254 TRP A CD1 
1987 C CD2 . TRP A 254 ? 0.58005 0.68019 0.61125 -0.03377 0.05584  0.01733  254 TRP A CD2 
1988 N NE1 . TRP A 254 ? 0.61490 0.70351 0.66761 -0.05805 0.05460  0.03055  254 TRP A NE1 
1989 C CE2 . TRP A 254 ? 0.58771 0.69076 0.63416 -0.03650 0.06160  0.02976  254 TRP A CE2 
1990 C CE3 . TRP A 254 ? 0.56089 0.66951 0.58521 -0.01545 0.06046  0.01444  254 TRP A CE3 
1991 C CZ2 . TRP A 254 ? 0.56815 0.68540 0.61976 -0.01896 0.07171  0.03866  254 TRP A CZ2 
1992 C CZ3 . TRP A 254 ? 0.54269 0.66363 0.57461 0.00050  0.06863  0.02064  254 TRP A CZ3 
1993 C CH2 . TRP A 254 ? 0.54602 0.67284 0.58985 -0.00005 0.07415  0.03233  254 TRP A CH2 
1994 N N   . ARG A 255 ? 0.65459 0.68515 0.59624 -0.05634 0.02755  -0.03580 255 ARG A N   
1995 C CA  . ARG A 255 ? 0.67441 0.70097 0.58791 -0.05354 0.02299  -0.04396 255 ARG A CA  
1996 C C   . ARG A 255 ? 0.66168 0.67911 0.55968 -0.03951 0.03801  -0.04542 255 ARG A C   
1997 O O   . ARG A 255 ? 0.66401 0.69054 0.55094 -0.03278 0.03952  -0.04027 255 ARG A O   
1998 C CB  . ARG A 255 ? 0.71413 0.71738 0.60686 -0.06341 0.01260  -0.06042 255 ARG A CB  
1999 C CG  . ARG A 255 ? 0.73386 0.73108 0.59034 -0.05529 0.01282  -0.06880 255 ARG A CG  
2000 C CD  . ARG A 255 ? 0.77780 0.76347 0.61054 -0.06318 -0.00378 -0.08462 255 ARG A CD  
2001 N NE  . ARG A 255 ? 0.78289 0.78851 0.63497 -0.07725 -0.02328 -0.08185 255 ARG A NE  
2002 C CZ  . ARG A 255 ? 0.77161 0.80965 0.63203 -0.07544 -0.03072 -0.07020 255 ARG A CZ  
2003 N NH1 . ARG A 255 ? 0.75486 0.80378 0.60523 -0.06051 -0.02063 -0.05898 255 ARG A NH1 
2004 N NH2 . ARG A 255 ? 0.77862 0.83862 0.65954 -0.08893 -0.04924 -0.06965 255 ARG A NH2 
2005 N N   . ARG A 256 ? 0.64288 0.64303 0.54218 -0.03511 0.04911  -0.05126 256 ARG A N   
2006 C CA  . ARG A 256 ? 0.63350 0.62997 0.52493 -0.02379 0.06357  -0.05306 256 ARG A CA  
2007 C C   . ARG A 256 ? 0.60342 0.61885 0.51102 -0.01681 0.06792  -0.04079 256 ARG A C   
2008 O O   . ARG A 256 ? 0.59756 0.61392 0.49607 -0.01200 0.07443  -0.03856 256 ARG A O   
2009 C CB  . ARG A 256 ? 0.63929 0.62004 0.53548 -0.01882 0.07251  -0.06102 256 ARG A CB  
2010 C CG  . ARG A 256 ? 0.65053 0.62802 0.53534 -0.00972 0.08581  -0.06758 256 ARG A CG  
2011 C CD  . ARG A 256 ? 0.66768 0.62467 0.54225 -0.00529 0.08966  -0.08140 256 ARG A CD  
2012 N NE  . ARG A 256 ? 0.63853 0.59243 0.53395 0.00020  0.09239  -0.07953 256 ARG A NE  
2013 C CZ  . ARG A 256 ? 0.64907 0.58221 0.54556 -0.00193 0.08660  -0.08279 256 ARG A CZ  
2014 N NH1 . ARG A 256 ? 0.67843 0.59067 0.55913 -0.01141 0.07614  -0.09049 256 ARG A NH1 
2015 N NH2 . ARG A 256 ? 0.63955 0.57091 0.55231 0.00582  0.09056  -0.07841 256 ARG A NH2 
2016 N N   . VAL A 257 ? 0.58096 0.61043 0.51195 -0.01588 0.06459  -0.03258 257 VAL A N   
2017 C CA  . VAL A 257 ? 0.55320 0.59965 0.49801 -0.00680 0.06621  -0.02331 257 VAL A CA  
2018 C C   . VAL A 257 ? 0.56261 0.61705 0.49694 -0.00621 0.05924  -0.01706 257 VAL A C   
2019 O O   . VAL A 257 ? 0.55674 0.61005 0.48890 0.00126  0.06293  -0.01324 257 VAL A O   
2020 C CB  . VAL A 257 ? 0.53234 0.59590 0.50007 -0.00428 0.06370  -0.01561 257 VAL A CB  
2021 C CG1 . VAL A 257 ? 0.50754 0.59127 0.48555 0.00690  0.06171  -0.00731 257 VAL A CG1 
2022 C CG2 . VAL A 257 ? 0.52341 0.57813 0.49906 0.00038  0.07187  -0.01931 257 VAL A CG2 
2023 N N   . HIS A 258 ? 0.57596 0.63787 0.50461 -0.01392 0.04779  -0.01581 258 HIS A N   
2024 C CA  . HIS A 258 ? 0.58777 0.65969 0.50504 -0.01109 0.03896  -0.00945 258 HIS A CA  
2025 C C   . HIS A 258 ? 0.60897 0.66279 0.49921 -0.00787 0.04514  -0.01056 258 HIS A C   
2026 O O   . HIS A 258 ? 0.61597 0.66983 0.50048 0.00013  0.04540  -0.00181 258 HIS A O   
2027 C CB  . HIS A 258 ? 0.60438 0.68821 0.51969 -0.02147 0.02416  -0.01145 258 HIS A CB  
2028 C CG  . HIS A 258 ? 0.62490 0.71973 0.52421 -0.01713 0.01308  -0.00651 258 HIS A CG  
2029 N ND1 . HIS A 258 ? 0.65393 0.73295 0.51986 -0.01585 0.01244  -0.01022 258 HIS A ND1 
2030 C CD2 . HIS A 258 ? 0.61985 0.74202 0.53074 -0.01167 0.00211  0.00247  258 HIS A CD2 
2031 C CE1 . HIS A 258 ? 0.66525 0.75882 0.52132 -0.00966 0.00081  -0.00306 258 HIS A CE1 
2032 N NE2 . HIS A 258 ? 0.64799 0.76822 0.53212 -0.00671 -0.00612 0.00407  258 HIS A NE2 
2033 N N   . ASP A 259 ? 0.62804 0.66562 0.50027 -0.01330 0.05050  -0.02048 259 ASP A N   
2034 C CA  . ASP A 259 ? 0.65864 0.68390 0.50275 -0.01057 0.05781  -0.01970 259 ASP A CA  
2035 C C   . ASP A 259 ? 0.64863 0.66766 0.50152 -0.00560 0.07226  -0.01378 259 ASP A C   
2036 O O   . ASP A 259 ? 0.65996 0.67231 0.49693 -0.00307 0.07733  -0.00504 259 ASP A O   
2037 C CB  . ASP A 259 ? 0.68666 0.69928 0.50895 -0.01477 0.06083  -0.03343 259 ASP A CB  
2038 C CG  . ASP A 259 ? 0.71240 0.72732 0.52518 -0.02158 0.04346  -0.04182 259 ASP A CG  
2039 O OD1 . ASP A 259 ? 0.71245 0.74346 0.53237 -0.02313 0.02963  -0.03499 259 ASP A OD1 
2040 O OD2 . ASP A 259 ? 0.73477 0.73579 0.53373 -0.02495 0.04272  -0.05633 259 ASP A OD2 
2041 N N   . SER A 260 ? 0.63307 0.65419 0.51171 -0.00442 0.07799  -0.01759 260 SER A N   
2042 C CA  . SER A 260 ? 0.61489 0.63176 0.50566 -0.00142 0.08954  -0.01530 260 SER A CA  
2043 C C   . SER A 260 ? 0.60448 0.62311 0.50786 0.00465  0.08432  -0.00583 260 SER A C   
2044 O O   . SER A 260 ? 0.61371 0.62320 0.52128 0.00496  0.09119  -0.00182 260 SER A O   
2045 C CB  . SER A 260 ? 0.59181 0.61147 0.50293 -0.00022 0.09610  -0.02531 260 SER A CB  
2046 O OG  . SER A 260 ? 0.60162 0.61578 0.50027 -0.00288 0.10128  -0.03518 260 SER A OG  
2047 N N   . PHE A 261 ? 0.59123 0.62153 0.50211 0.00975  0.07237  -0.00242 261 PHE A N   
2048 C CA  . PHE A 261 ? 0.59347 0.62507 0.51614 0.01970  0.06761  0.00366  261 PHE A CA  
2049 C C   . PHE A 261 ? 0.63886 0.67538 0.55023 0.02649  0.05611  0.01365  261 PHE A C   
2050 O O   . PHE A 261 ? 0.64934 0.67593 0.56033 0.03543  0.05357  0.01984  261 PHE A O   
2051 C CB  . PHE A 261 ? 0.55546 0.60159 0.50244 0.02652  0.06590  -0.00173 261 PHE A CB  
2052 C CG  . PHE A 261 ? 0.53005 0.57226 0.48884 0.02396  0.07547  -0.01135 261 PHE A CG  
2053 C CD1 . PHE A 261 ? 0.51820 0.55031 0.48578 0.02566  0.08049  -0.01478 261 PHE A CD1 
2054 C CD2 . PHE A 261 ? 0.51821 0.56633 0.48043 0.01993  0.07831  -0.01706 261 PHE A CD2 
2055 C CE1 . PHE A 261 ? 0.50466 0.53894 0.48562 0.02438  0.08780  -0.02441 261 PHE A CE1 
2056 C CE2 . PHE A 261 ? 0.51171 0.55753 0.48372 0.02086  0.08616  -0.02565 261 PHE A CE2 
2057 C CZ  . PHE A 261 ? 0.50188 0.54392 0.48394 0.02359  0.09072  -0.02965 261 PHE A CZ  
2058 N N   . ILE A 262 ? 0.68102 0.73108 0.58288 0.02294  0.04796  0.01473  262 ILE A N   
2059 C CA  . ILE A 262 ? 0.75574 0.81847 0.65062 0.03113  0.03499  0.02333  262 ILE A CA  
2060 C C   . ILE A 262 ? 0.86441 0.91284 0.72762 0.03043  0.03314  0.02992  262 ILE A C   
2061 O O   . ILE A 262 ? 0.88787 0.92745 0.74002 0.04105  0.02912  0.04031  262 ILE A O   
2062 C CB  . ILE A 262 ? 0.72141 0.81466 0.63061 0.02734  0.02482  0.02100  262 ILE A CB  
2063 C CG1 . ILE A 262 ? 0.68988 0.79630 0.62693 0.02826  0.02960  0.01756  262 ILE A CG1 
2064 C CG2 . ILE A 262 ? 0.73589 0.85041 0.64451 0.03832  0.01114  0.02955  262 ILE A CG2 
2065 C CD1 . ILE A 262 ? 0.66699 0.77719 0.61550 0.04525  0.03026  0.02135  262 ILE A CD1 
2066 N N   . GLU A 263 ? 0.93367 0.97942 0.77922 0.02018  0.03491  0.02422  263 GLU A N   
2067 C CA  . GLU A 263 ? 0.99133 1.02862 0.80218 0.02189  0.03181  0.03039  263 GLU A CA  
2068 C C   . GLU A 263 ? 1.00825 1.03109 0.79836 0.01313  0.04428  0.02380  263 GLU A C   
2069 O O   . GLU A 263 ? 1.03248 1.06104 0.80947 0.00762  0.03903  0.01337  263 GLU A O   
2070 C CB  . GLU A 263 ? 1.01378 1.07483 0.81883 0.02364  0.01284  0.02902  263 GLU A CB  
2071 C CG  . GLU A 263 ? 1.07265 1.12967 0.83888 0.02973  0.00527  0.03564  263 GLU A CG  
2072 C CD  . GLU A 263 ? 1.11291 1.15418 0.86401 0.04395  0.00727  0.05358  263 GLU A CD  
2073 O OE1 . GLU A 263 ? 1.10249 1.14340 0.87578 0.05199  0.00670  0.05930  263 GLU A OE1 
2074 O OE2 . GLU A 263 ? 1.15677 1.18395 0.87135 0.04816  0.00939  0.06223  263 GLU A OE2 
# 
