data_8QGL
# 
_entry.id   8QGL 
# 
_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   8QGL         pdb_00008qgl 10.2210/pdb8qgl/pdb 
WWPDB D_1292133174 ?            ?                   
# 
_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                        8QGL 
_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 
;(2~{R},3~{R},4~{S},5~{R})-2-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-5-[[[1,1-bis(oxidanyl)-1$l^{6}-thia-3-azabicyclo[1.1.0]butan-1-yl]amino]methyl]oxolane-3,4-diol
;
676.662   1   ?        ? ? ? 
4 water       nat water 18.015    108 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ATP-dependent NAD kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 
;(2~{R},3~{R},4~{S},5~{R})-2-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-5-[[[1,1-bis(oxidanyl)-1$l^{6}-thia-3-azabicyclo[1.1.0]butan-1-yl]amino]methyl]oxolane-3,4-diol
;
UUC 
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 
UUC non-polymer         . 
;(2~{R},3~{R},4~{S},5~{R})-2-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-5-[[[1,1-bis(oxidanyl)-1$l^{6}-thia-3-azabicyclo[1.1.0]butan-1-yl]amino]methyl]oxolane-3,4-diol
;
? 'C25 H32 N12 O9 S' 676.662 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 LYS 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 ?   ?   ?   A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 LEU 265 265 ?   ?   ?   A . n 
A 1 266 GLU 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 HIS 269 269 ?   ?   ?   A . n 
A 1 270 HIS 270 270 ?   ?   ?   A . n 
A 1 271 HIS 271 271 ?   ?   ?   A . n 
A 1 272 HIS 272 272 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        UUC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UUC 
_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 UUC 1   302 1   UUC DRG A . 
D 4 HOH 1   401 119 HOH HOH A . 
D 4 HOH 2   402 54  HOH HOH A . 
D 4 HOH 3   403 46  HOH HOH A . 
D 4 HOH 4   404 75  HOH HOH A . 
D 4 HOH 5   405 51  HOH HOH A . 
D 4 HOH 6   406 18  HOH HOH A . 
D 4 HOH 7   407 150 HOH HOH A . 
D 4 HOH 8   408 50  HOH HOH A . 
D 4 HOH 9   409 164 HOH HOH A . 
D 4 HOH 10  410 59  HOH HOH A . 
D 4 HOH 11  412 17  HOH HOH A . 
D 4 HOH 12  413 2   HOH HOH A . 
D 4 HOH 13  414 10  HOH HOH A . 
D 4 HOH 14  415 49  HOH HOH A . 
D 4 HOH 15  416 37  HOH HOH A . 
D 4 HOH 16  417 58  HOH HOH A . 
D 4 HOH 17  418 27  HOH HOH A . 
D 4 HOH 18  419 15  HOH HOH A . 
D 4 HOH 19  420 22  HOH HOH A . 
D 4 HOH 20  421 34  HOH HOH A . 
D 4 HOH 21  422 151 HOH HOH A . 
D 4 HOH 22  423 36  HOH HOH A . 
D 4 HOH 23  424 28  HOH HOH A . 
D 4 HOH 24  425 39  HOH HOH A . 
D 4 HOH 25  426 66  HOH HOH A . 
D 4 HOH 26  427 1   HOH HOH A . 
D 4 HOH 27  428 7   HOH HOH A . 
D 4 HOH 28  429 4   HOH HOH A . 
D 4 HOH 29  430 44  HOH HOH A . 
D 4 HOH 30  431 62  HOH HOH A . 
D 4 HOH 31  432 38  HOH HOH A . 
D 4 HOH 32  433 70  HOH HOH A . 
D 4 HOH 33  434 167 HOH HOH A . 
D 4 HOH 34  435 55  HOH HOH A . 
D 4 HOH 35  436 20  HOH HOH A . 
D 4 HOH 36  437 113 HOH HOH A . 
D 4 HOH 37  438 5   HOH HOH A . 
D 4 HOH 38  439 130 HOH HOH A . 
D 4 HOH 39  440 74  HOH HOH A . 
D 4 HOH 40  441 102 HOH HOH A . 
D 4 HOH 41  442 6   HOH HOH A . 
D 4 HOH 42  443 63  HOH HOH A . 
D 4 HOH 43  444 95  HOH HOH A . 
D 4 HOH 44  445 23  HOH HOH A . 
D 4 HOH 45  446 111 HOH HOH A . 
D 4 HOH 46  447 8   HOH HOH A . 
D 4 HOH 47  448 31  HOH HOH A . 
D 4 HOH 48  449 13  HOH HOH A . 
D 4 HOH 49  450 35  HOH HOH A . 
D 4 HOH 50  451 73  HOH HOH A . 
D 4 HOH 51  452 128 HOH HOH A . 
D 4 HOH 52  453 97  HOH HOH A . 
D 4 HOH 53  454 21  HOH HOH A . 
D 4 HOH 54  455 14  HOH HOH A . 
D 4 HOH 55  456 71  HOH HOH A . 
D 4 HOH 56  457 30  HOH HOH A . 
D 4 HOH 57  458 40  HOH HOH A . 
D 4 HOH 58  459 171 HOH HOH A . 
D 4 HOH 59  460 25  HOH HOH A . 
D 4 HOH 60  461 64  HOH HOH A . 
D 4 HOH 61  462 52  HOH HOH A . 
D 4 HOH 62  463 16  HOH HOH A . 
D 4 HOH 63  464 173 HOH HOH A . 
D 4 HOH 64  465 33  HOH HOH A . 
D 4 HOH 65  466 12  HOH HOH A . 
D 4 HOH 66  467 41  HOH HOH A . 
D 4 HOH 67  468 56  HOH HOH A . 
D 4 HOH 68  469 26  HOH HOH A . 
D 4 HOH 69  470 53  HOH HOH A . 
D 4 HOH 70  471 72  HOH HOH A . 
D 4 HOH 71  472 32  HOH HOH A . 
D 4 HOH 72  473 57  HOH HOH A . 
D 4 HOH 73  474 19  HOH HOH A . 
D 4 HOH 74  475 45  HOH HOH A . 
D 4 HOH 75  476 24  HOH HOH A . 
D 4 HOH 76  477 107 HOH HOH A . 
D 4 HOH 77  478 99  HOH HOH A . 
D 4 HOH 78  479 131 HOH HOH A . 
D 4 HOH 79  480 88  HOH HOH A . 
D 4 HOH 80  481 136 HOH HOH A . 
D 4 HOH 81  482 157 HOH HOH A . 
D 4 HOH 82  483 48  HOH HOH A . 
D 4 HOH 83  484 11  HOH HOH A . 
D 4 HOH 84  485 3   HOH HOH A . 
D 4 HOH 85  486 127 HOH HOH A . 
D 4 HOH 86  487 118 HOH HOH A . 
D 4 HOH 87  488 155 HOH HOH A . 
D 4 HOH 88  489 140 HOH HOH A . 
D 4 HOH 89  490 154 HOH HOH A . 
D 4 HOH 90  491 153 HOH HOH A . 
D 4 HOH 91  492 76  HOH HOH A . 
D 4 HOH 92  493 161 HOH HOH A . 
D 4 HOH 93  494 152 HOH HOH A . 
D 4 HOH 94  495 42  HOH HOH A . 
D 4 HOH 95  496 103 HOH HOH A . 
D 4 HOH 96  497 160 HOH HOH A . 
D 4 HOH 97  498 60  HOH HOH A . 
D 4 HOH 98  499 159 HOH HOH A . 
D 4 HOH 99  500 110 HOH HOH A . 
D 4 HOH 100 501 156 HOH HOH A . 
D 4 HOH 101 502 67  HOH HOH A . 
D 4 HOH 102 503 68  HOH HOH A . 
D 4 HOH 103 504 47  HOH HOH A . 
D 4 HOH 104 505 172 HOH HOH A . 
D 4 HOH 105 506 166 HOH HOH A . 
D 4 HOH 106 507 98  HOH HOH A . 
D 4 HOH 107 508 162 HOH HOH A . 
D 4 HOH 108 509 141 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 ASP 28  ? CG  ? A ASP 28  CG  
2  1 Y 1 A ASP 28  ? OD1 ? A ASP 28  OD1 
3  1 Y 1 A ASP 28  ? OD2 ? A ASP 28  OD2 
4  1 Y 1 A ARG 79  ? CG  ? A ARG 79  CG  
5  1 Y 1 A ARG 79  ? CD  ? A ARG 79  CD  
6  1 Y 1 A ARG 79  ? NE  ? A ARG 79  NE  
7  1 Y 1 A ARG 79  ? CZ  ? A ARG 79  CZ  
8  1 Y 1 A ARG 79  ? NH1 ? A ARG 79  NH1 
9  1 Y 1 A ARG 79  ? NH2 ? A ARG 79  NH2 
10 1 Y 1 A LYS 92  ? CG  ? A LYS 92  CG  
11 1 Y 1 A LYS 92  ? CD  ? A LYS 92  CD  
12 1 Y 1 A LYS 92  ? CE  ? A LYS 92  CE  
13 1 Y 1 A LYS 92  ? NZ  ? A LYS 92  NZ  
14 1 Y 1 A ARG 193 ? CG  ? A ARG 193 CG  
15 1 Y 1 A ARG 193 ? CD  ? A ARG 193 CD  
16 1 Y 1 A ARG 193 ? NE  ? A ARG 193 NE  
17 1 Y 1 A ARG 193 ? CZ  ? A ARG 193 CZ  
18 1 Y 1 A ARG 193 ? NH1 ? A ARG 193 NH1 
19 1 Y 1 A ARG 193 ? NH2 ? A ARG 193 NH2 
20 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
21 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
22 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
23 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
24 1 Y 1 A GLU 263 ? CG  ? A GLU 263 CG  
25 1 Y 1 A GLU 263 ? CD  ? A GLU 263 CD  
26 1 Y 1 A GLU 263 ? OE1 ? A GLU 263 OE1 
27 1 Y 1 A GLU 263 ? OE2 ? A GLU 263 OE2 
# 
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  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QGL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.860 
_cell.length_a_esd                 ? 
_cell.length_b                     74.700 
_cell.length_b_esd                 ? 
_cell.length_c                     118.530 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         8QGL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_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                   8QGL 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.11 
_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         2013-11-29 
_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   0.979316 
_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        0.979316 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QGL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.83 
_reflns.d_resolution_low                               59.26 
_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                                     24849 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.95 
_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                                0.117 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       159893 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.108 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.83 
_reflns_shell.d_res_low                                     1.87 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           8481 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1509 
_reflns_shell.percent_possible_obs                          99.3 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.6 
_reflns_shell.pdbx_chi_squared                              0.94 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.0 
_reflns_shell.pdbx_Rrim_I_all                               0.866 
_reflns_shell.pdbx_Rpim_I_all                               0.356 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.760 
_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                                  0.786 
_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                               ? 
_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                                 8QGL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.830 
_refine.ls_d_res_low                             55.534 
_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                     24821 
_refine.ls_number_reflns_R_free                  1193 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.22 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1878 
_refine.ls_R_factor_R_free                       0.2161 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1863 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 26.31 
_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                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.830 
_refine_hist.d_res_low                        55.534 
_refine_hist.number_atoms_solvent             109 
_refine_hist.number_atoms_total               2231 
_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        2062 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  ? 2217 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.047  ? 3012 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.017 ? 1300 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.088  ? 329  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 379  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.8300 1.9033 . . 103 2581 99.00  . . . . 0.2978 . . . . . . . . . . . 0.3280 
'X-RAY DIFFRACTION' 1.9033 1.9899 . . 124 2596 99.00  . . . . 0.2675 . . . . . . . . . . . 0.3292 
'X-RAY DIFFRACTION' 1.9899 2.0948 . . 131 2619 100.00 . . . . 0.2111 . . . . . . . . . . . 0.2577 
'X-RAY DIFFRACTION' 2.0948 2.2261 . . 108 2601 99.00  . . . . 0.1946 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 2.2261 2.3979 . . 144 2604 99.00  . . . . 0.2028 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 2.3979 2.6393 . . 134 2613 100.00 . . . . 0.1808 . . . . . . . . . . . 0.2542 
'X-RAY DIFFRACTION' 2.6393 3.0211 . . 137 2618 99.00  . . . . 0.1877 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 3.0211 3.8062 . . 143 2654 100.00 . . . . 0.1707 . . . . . . . . . . . 0.1944 
'X-RAY DIFFRACTION' 3.8062 55.534 . . 169 2742 99.00  . . . . 0.1638 . . . . . . . . . . . 0.1781 
# 
_struct.entry_id                     8QGL 
_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        8QGL 
_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              8QGL 
_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 8QGL LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGL GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGL HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGL HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGL HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGL HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGL HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGL HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10840 ? 
1 MORE         -48   ? 
1 'SSA (A^2)'  40070 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 62.8600000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 62.8600000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 58  ? ILE A 62  ? ARG A 58  ILE A 62  5 ? 5  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? ALA A 91  ? GLU A 82  ALA A 91  1 ? 10 
HELX_P HELX_P6 AA6 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 ALA A 116 ? ALA A 120 ? ALA A 116 ALA A 120 
AA2 2 GLN A 96  ? TYR A 109 ? GLN A 96  TYR A 109 
AA2 3 VAL A 231 ? ARG A 247 ? VAL A 231 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? GLY A 149 ? ILE A 142 GLY A 149 
AA3 1 LEU A 199 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 2 ALA A 178 ? MET A 184 ? ALA A 178 MET A 184 
AA3 3 GLY A 151 ? SER A 155 ? GLY A 151 SER A 155 
AA3 4 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 5 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 6 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA2 3 4 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 1 2 O LEU A 199 ? O LEU A 199 N LEU A 181 ? N LEU A 181 
AA3 2 3 O GLN A 180 ? O GLN A 180 N SER A 155 ? N SER A 155 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 5 6 N ILE A 219 ? N ILE A 219 O ILE A 226 ? O ILE A 226 
# 
_pdbx_entry_details.entry_id                   8QGL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 71  ? ? -103.22 -65.23  
2 1 LYS A 92  ? ? 70.68   -19.82  
3 1 TYR A 95  ? ? -59.77  174.79  
4 1 ASN A 122 ? ? -101.61 -68.46  
5 1 SER A 129 ? ? -94.78  51.06   
6 1 ALA A 162 ? ? -106.96 -129.84 
7 1 HIS A 204 ? ? 76.03   -9.49   
8 1 ASN A 213 ? ? -125.13 -83.89  
9 1 ASP A 222 ? ? 53.93   -128.29 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 12.4273 23.4986 23.1021 0.3764 ? 0.0844 ? 0.0360  ? 0.3555 ? -0.0898 ? 0.2817 ? 2.2707 ? -0.2347 ? 
-1.0578 ? 1.4416 ? 1.4176  ? 4.0400 ? -0.0770 ? -0.2862 ? 0.1725 ? 0.0466  ? -0.0013 ? 0.1049 ? -0.3322 ? -0.0357 ? 0.0859 ? 
2 'X-RAY DIFFRACTION' ? refined 14.4640 24.2619 4.7750  0.2603 ? 0.0914 ? 0.0437  ? 0.2644 ? -0.0299 ? 0.2906 ? 2.7352 ? -0.4773 ? 
-1.0568 ? 2.6000 ? -0.9547 ? 2.3226 ? 0.3469  ? -0.0049 ? 0.5221 ? 0.0555  ? -0.2135 ? 0.4182 ? -0.5241 ? -0.3320 ? 0.3066 ? 
3 'X-RAY DIFFRACTION' ? refined 20.9227 10.5885 -6.5660 0.1265 ? 0.0285 ? -0.0178 ? 0.1697 ? 0.0016  ? 0.1777 ? 1.9283 ? -0.0552 ? 
0.2053  ? 2.1225 ? 0.1148  ? 3.0824 ? 0.0237  ? 0.1715  ? 0.0518 ? -0.1885 ? -0.0489 ? 0.1719 ? 0.0713  ? -0.1975 ? 0.0173 ? 
4 'X-RAY DIFFRACTION' ? refined 18.8014 17.1666 7.2275  0.2019 ? 0.0250 ? 0.0456  ? 0.1908 ? -0.0390 ? 0.2478 ? 1.9422 ? -0.4738 ? 
0.3193  ? 1.5246 ? 0.0511  ? 2.3821 ? 0.0030  ? -0.0893 ? 0.1929 ? 0.0861  ? -0.0263 ? 0.2007 ? -0.1953 ? -0.2944 ? 0.0464 ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 90 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 91 through 122 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 123 through 216 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 217 through 264 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 112 ? A GLY 112 
2  1 Y 1 A LYS 113 ? A LYS 113 
3  1 Y 1 A LYS 114 ? A LYS 114 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
UUC C1   C Y N 393 
UUC C2   C Y N 394 
UUC C3   C Y N 395 
UUC C4   C Y N 396 
UUC N1   N Y N 397 
UUC N2   N Y N 398 
UUC C5   C N R 399 
UUC C6   C Y N 400 
UUC C7   C N R 401 
UUC C8   C N S 402 
UUC C9   C N R 403 
UUC C10  C N N 404 
UUC C11  C N N 405 
UUC C12  C N N 406 
UUC C13  C N N 407 
UUC C14  C N R 408 
UUC C15  C N R 409 
UUC C16  C N R 410 
UUC C17  C N S 411 
UUC C18  C N N 412 
UUC C19  C N N 413 
UUC C20  C N N 414 
UUC C21  C Y N 415 
UUC C22  C Y N 416 
UUC C23  C Y N 417 
UUC C24  C Y N 418 
UUC C25  C Y N 419 
UUC N3   N N N 420 
UUC N4   N Y N 421 
UUC N5   N Y N 422 
UUC N6   N N N 423 
UUC N7   N N N 424 
UUC N8   N Y N 425 
UUC N9   N Y N 426 
UUC N10  N Y N 427 
UUC N11  N Y N 428 
UUC N12  N N N 429 
UUC O1   O N N 430 
UUC O2   O N N 431 
UUC O3   O N N 432 
UUC O4   O N N 433 
UUC O5   O N N 434 
UUC O6   O N N 435 
UUC O7   O N N 436 
UUC O8   O N N 437 
UUC O9   O N N 438 
UUC S1   S N N 439 
UUC H1   H N N 440 
UUC H2   H N N 441 
UUC H3   H N N 442 
UUC H4   H N N 443 
UUC H5   H N N 444 
UUC H6   H N N 445 
UUC H7   H N N 446 
UUC H8   H N N 447 
UUC H9   H N N 448 
UUC H10  H N N 449 
UUC H11  H N N 450 
UUC H12  H N N 451 
UUC H13  H N N 452 
UUC H14  H N N 453 
UUC H15  H N N 454 
UUC H16  H N N 455 
UUC H17  H N N 456 
UUC H18  H N N 457 
UUC H19  H N N 458 
UUC H20  H N N 459 
UUC H21  H N N 460 
UUC H22  H N N 461 
UUC H23  H N N 462 
UUC H24  H N N 463 
UUC H25  H N N 464 
UUC H26  H N N 465 
UUC H27  H N N 466 
UUC H28  H N N 467 
UUC H29  H N N 468 
UUC H30  H N N 469 
UUC H31  H N N 470 
UUC H32  H N N 471 
VAL N    N N N 472 
VAL CA   C N S 473 
VAL C    C N N 474 
VAL O    O N N 475 
VAL CB   C N N 476 
VAL CG1  C N N 477 
VAL CG2  C N N 478 
VAL OXT  O N N 479 
VAL H    H N N 480 
VAL H2   H N N 481 
VAL HA   H N N 482 
VAL HB   H N N 483 
VAL HG11 H N N 484 
VAL HG12 H N N 485 
VAL HG13 H N N 486 
VAL HG21 H N N 487 
VAL HG22 H N N 488 
VAL HG23 H N N 489 
VAL HXT  H N N 490 
# 
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 
UUC C1  C2   doub Y N 378 
UUC C1  N2   sing Y N 379 
UUC C1  N5   sing Y N 380 
UUC C2  C3   sing Y N 381 
UUC C2  N4   sing Y N 382 
UUC C3  N1   doub Y N 383 
UUC C3  N3   sing N N 384 
UUC C4  C18  sing N N 385 
UUC C4  N4   doub Y N 386 
UUC C4  N5   sing Y N 387 
UUC N1  C6   sing Y N 388 
UUC N2  C6   doub Y N 389 
UUC C5  C7   sing N N 390 
UUC C5  N8   sing N N 391 
UUC C5  O3   sing N N 392 
UUC C7  C8   sing N N 393 
UUC C7  O1   sing N N 394 
UUC C8  C9   sing N N 395 
UUC C8  O2   sing N N 396 
UUC C9  C10  sing N N 397 
UUC C9  O3   sing N N 398 
UUC C10 O4   sing N N 399 
UUC C11 N6   sing N N 400 
UUC C11 S1   sing N N 401 
UUC C12 N6   sing N N 402 
UUC C12 S1   sing N N 403 
UUC C13 C14  sing N N 404 
UUC C13 N7   sing N N 405 
UUC C14 C17  sing N N 406 
UUC C14 O7   sing N N 407 
UUC C15 C16  sing N N 408 
UUC C15 N5   sing N N 409 
UUC C15 O7   sing N N 410 
UUC C16 C17  sing N N 411 
UUC C16 O8   sing N N 412 
UUC C17 O9   sing N N 413 
UUC C18 C19  trip N N 414 
UUC C19 C20  sing N N 415 
UUC C20 O4   sing N N 416 
UUC C21 N8   sing Y N 417 
UUC C21 N9   doub Y N 418 
UUC C22 C23  doub Y N 419 
UUC C22 C25  sing Y N 420 
UUC C22 N9   sing Y N 421 
UUC C23 N8   sing Y N 422 
UUC C23 N10  sing Y N 423 
UUC C24 N10  doub Y N 424 
UUC C24 N11  sing Y N 425 
UUC C25 N11  doub Y N 426 
UUC C25 N12  sing N N 427 
UUC N6  S1   sing N N 428 
UUC N7  S1   sing N N 429 
UUC O5  S1   sing N N 430 
UUC O6  S1   sing N N 431 
UUC C5  H1   sing N N 432 
UUC C6  H2   sing N N 433 
UUC C7  H3   sing N N 434 
UUC C8  H4   sing N N 435 
UUC C9  H5   sing N N 436 
UUC C10 H6   sing N N 437 
UUC C10 H7   sing N N 438 
UUC C11 H8   sing N N 439 
UUC C11 H9   sing N N 440 
UUC C12 H10  sing N N 441 
UUC C12 H11  sing N N 442 
UUC C13 H12  sing N N 443 
UUC C13 H13  sing N N 444 
UUC C14 H14  sing N N 445 
UUC C15 H15  sing N N 446 
UUC C16 H16  sing N N 447 
UUC C17 H17  sing N N 448 
UUC C20 H18  sing N N 449 
UUC C20 H19  sing N N 450 
UUC C21 H20  sing N N 451 
UUC C24 H21  sing N N 452 
UUC N3  H22  sing N N 453 
UUC N3  H23  sing N N 454 
UUC N7  H24  sing N N 455 
UUC N12 H25  sing N N 456 
UUC N12 H26  sing N N 457 
UUC O1  H27  sing N N 458 
UUC O2  H28  sing N N 459 
UUC O5  H29  sing N N 460 
UUC O6  H30  sing N N 461 
UUC O8  H31  sing N N 462 
UUC O9  H32  sing N N 463 
VAL N   CA   sing N N 464 
VAL N   H    sing N N 465 
VAL N   H2   sing N N 466 
VAL CA  C    sing N N 467 
VAL CA  CB   sing N N 468 
VAL CA  HA   sing N N 469 
VAL C   O    doub N N 470 
VAL C   OXT  sing N N 471 
VAL CB  CG1  sing N N 472 
VAL CB  CG2  sing N N 473 
VAL CB  HB   sing N N 474 
VAL CG1 HG11 sing N N 475 
VAL CG1 HG12 sing N N 476 
VAL CG1 HG13 sing N N 477 
VAL CG2 HG21 sing N N 478 
VAL CG2 HG22 sing N N 479 
VAL CG2 HG23 sing N N 480 
VAL OXT HXT  sing N N 481 
# 
_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' 
# 
_atom_sites.entry_id                    8QGL 
_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]   0.015908 
_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]   0.013387 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008437 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   ? 10.651 37.042 25.948  0.60 55.92  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.815 36.546 24.587  0.60 54.34  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.905  35.350 24.349  0.60 50.67  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.832  34.447 25.177  0.60 47.54  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 12.277 36.178 24.325  0.60 53.93  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.526 35.496 22.993  0.60 55.07  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.260 35.539 22.502  0.40 55.46  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.036 34.798 23.938  0.30 53.78  ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.206  35.355 23.217  1.00 54.61  ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.268  34.284 22.908  1.00 50.80  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 9.011  32.977 22.655  1.00 45.99  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 10.045 32.955 21.981  1.00 47.87  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.410  34.654 21.695  0.80 48.68  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.457  35.814 21.954  0.70 47.06  ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.443  35.997 20.833  0.60 46.31  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.449  37.103 21.167  0.50 48.30  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.441  37.308 20.092  0.50 51.44  ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.483  31.887 23.216  1.00 41.70  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.083  30.564 23.090  1.00 38.03  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.981  29.513 23.147  1.00 39.08  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.868  29.778 23.615  1.00 37.24  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.114 30.288 24.204  1.00 37.44  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.461  29.917 25.529  1.00 39.10  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.997  30.903 26.396  1.00 37.31  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.289  28.585 25.902  1.00 37.24  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.381  30.577 27.608  1.00 40.22  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.672  28.249 27.109  1.00 35.90  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.221  29.250 27.954  1.00 39.85  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.609  28.921 29.146  1.00 39.27  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.314  28.303 22.688  1.00 37.61  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.479  27.129 22.915  1.00 37.70  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.384  25.917 23.096  1.00 32.97  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.581  25.967 22.817  1.00 32.04  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.477  26.906 21.777  1.00 38.20  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.111  26.472 20.473  1.00 39.98  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.296  24.685 20.372  1.00 43.49  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.584  24.161 20.451  0.80 44.14  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.805  24.817 23.583  1.00 31.39  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.559  23.599 23.871  1.00 29.75  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.757  22.417 23.349  1.00 31.60  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.605  22.225 23.760  1.00 30.15  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.834  23.408 25.381  1.00 30.00  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.453  24.662 26.005  1.00 28.96  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.739  22.218 25.588  1.00 29.07  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.798  24.531 27.510  1.00 34.14  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.359  21.618 22.465  1.00 27.70  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.777  20.338 22.092  1.00 30.82  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.379  19.243 22.943  1.00 35.25  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.528  19.333 23.380  1.00 40.35  ? 6   THR A O   1 
ATOM   50   C CB  A THR A 1 6   ? 8.013  19.997 20.614  0.50 33.16  ? 6   THR A CB  1 
ATOM   51   C CB  B THR A 1 6   ? 8.026  20.010 20.614  0.50 33.18  ? 6   THR A CB  1 
ATOM   52   O OG1 A THR A 1 6   ? 9.418  19.828 20.374  0.50 29.60  ? 6   THR A OG1 1 
ATOM   53   O OG1 B THR A 1 6   ? 8.495  21.175 19.924  0.50 33.60  ? 6   THR A OG1 1 
ATOM   54   C CG2 A THR A 1 6   ? 7.457  21.079 19.699  0.50 34.10  ? 6   THR A CG2 1 
ATOM   55   C CG2 B THR A 1 6   ? 6.752  19.508 19.960  0.50 33.03  ? 6   THR A CG2 1 
ATOM   56   N N   . SER A 1 7   ? 7.607  18.183 23.134  1.00 34.90  ? 7   SER A N   1 
ATOM   57   C CA  . SER A 1 7   ? 8.048  17.025 23.892  1.00 34.41  ? 7   SER A CA  1 
ATOM   58   C C   . SER A 1 7   ? 7.848  15.769 23.060  1.00 34.50  ? 7   SER A C   1 
ATOM   59   O O   . SER A 1 7   ? 6.893  15.665 22.284  1.00 35.08  ? 7   SER A O   1 
ATOM   60   C CB  . SER A 1 7   ? 7.280  16.900 25.209  1.00 34.96  ? 7   SER A CB  1 
ATOM   61   O OG  . SER A 1 7   ? 7.527  15.649 25.817  1.00 38.78  ? 7   SER A OG  1 
ATOM   62   N N   . LYS A 1 8   ? 8.763  14.814 23.229  1.00 31.39  ? 8   LYS A N   1 
ATOM   63   C CA  . LYS A 1 8   ? 8.554  13.481 22.676  1.00 36.94  ? 8   LYS A CA  1 
ATOM   64   C C   . LYS A 1 8   ? 7.303  12.824 23.253  1.00 39.46  ? 8   LYS A C   1 
ATOM   65   O O   . LYS A 1 8   ? 6.747  11.910 22.637  1.00 41.23  ? 8   LYS A O   1 
ATOM   66   C CB  . LYS A 1 8   ? 9.797  12.621 22.937  1.00 37.34  ? 8   LYS A CB  1 
ATOM   67   C CG  . LYS A 1 8   ? 9.630  11.140 22.679  0.80 38.84  ? 8   LYS A CG  1 
ATOM   68   C CD  . LYS A 1 8   ? 10.832 10.357 23.154  0.70 43.16  ? 8   LYS A CD  1 
ATOM   69   C CE  . LYS A 1 8   ? 10.736 8.925  22.668  0.60 47.20  ? 8   LYS A CE  1 
ATOM   70   N NZ  . LYS A 1 8   ? 10.332 8.891  21.230  0.60 47.72  ? 8   LYS A NZ  1 
ATOM   71   N N   . GLY A 1 9   ? 6.845  13.261 24.419  1.00 38.85  ? 9   GLY A N   1 
ATOM   72   C CA  . GLY A 1 9   ? 5.591  12.770 24.947  1.00 39.60  ? 9   GLY A CA  1 
ATOM   73   C C   . GLY A 1 9   ? 5.695  11.591 25.888  1.00 42.17  ? 9   GLY A C   1 
ATOM   74   O O   . GLY A 1 9   ? 4.657  11.092 26.341  1.00 47.31  ? 9   GLY A O   1 
ATOM   75   N N   . ASP A 1 10  ? 6.898  11.113 26.184  1.00 39.95  ? 10  ASP A N   1 
ATOM   76   C CA  . ASP A 1 10  ? 7.054  10.178 27.282  1.00 44.86  ? 10  ASP A CA  1 
ATOM   77   C C   . ASP A 1 10  ? 7.104  10.943 28.605  1.00 47.71  ? 10  ASP A C   1 
ATOM   78   O O   . ASP A 1 10  ? 7.203  12.175 28.638  1.00 44.69  ? 10  ASP A O   1 
ATOM   79   C CB  . ASP A 1 10  ? 8.306  9.324  27.085  1.00 45.07  ? 10  ASP A CB  1 
ATOM   80   C CG  . ASP A 1 10  ? 9.580  10.120 27.236  0.64 45.99  ? 10  ASP A CG  1 
ATOM   81   O OD1 . ASP A 1 10  ? 10.475 9.679  27.980  0.64 51.22  ? 10  ASP A OD1 1 
ATOM   82   O OD2 . ASP A 1 10  ? 9.676  11.202 26.635  0.62 43.57  ? 10  ASP A OD2 1 
ATOM   83   N N   . GLU A 1 11  ? 7.029  10.194 29.709  1.00 51.43  ? 11  GLU A N   1 
ATOM   84   C CA  . GLU A 1 11  ? 6.944  10.815 31.028  1.00 51.78  ? 11  GLU A CA  1 
ATOM   85   C C   . GLU A 1 11  ? 8.141  11.726 31.286  1.00 48.50  ? 11  GLU A C   1 
ATOM   86   O O   . GLU A 1 11  ? 7.981  12.873 31.715  1.00 49.88  ? 11  GLU A O   1 
ATOM   87   C CB  . GLU A 1 11  ? 6.828  9.724  32.101  1.00 56.03  ? 11  GLU A CB  1 
ATOM   88   C CG  . GLU A 1 11  ? 6.877  10.210 33.531  1.00 59.39  ? 11  GLU A CG  1 
ATOM   89   C CD  . GLU A 1 11  ? 6.459  9.134  34.511  0.40 63.80  ? 11  GLU A CD  1 
ATOM   90   O OE1 . GLU A 1 11  ? 5.746  8.199  34.092  0.40 65.00  ? 11  GLU A OE1 1 
ATOM   91   O OE2 . GLU A 1 11  ? 6.847  9.218  35.694  0.40 65.89  ? 11  GLU A OE2 1 
ATOM   92   N N   . LYS A 1 12  ? 9.349  11.244 30.992  1.00 46.86  ? 12  LYS A N   1 
ATOM   93   C CA  . LYS A 1 12  ? 10.555 12.026 31.258  1.00 45.20  ? 12  LYS A CA  1 
ATOM   94   C C   . LYS A 1 12  ? 10.552 13.352 30.503  1.00 40.32  ? 12  LYS A C   1 
ATOM   95   O O   . LYS A 1 12  ? 10.956 14.390 31.046  1.00 34.83  ? 12  LYS A O   1 
ATOM   96   C CB  . LYS A 1 12  ? 11.793 11.216 30.887  0.80 45.27  ? 12  LYS A CB  1 
ATOM   97   C CG  . LYS A 1 12  ? 13.078 11.973 31.120  0.60 43.95  ? 12  LYS A CG  1 
ATOM   98   C CD  . LYS A 1 12  ? 14.303 11.121 30.874  0.60 43.44  ? 12  LYS A CD  1 
ATOM   99   C CE  . LYS A 1 12  ? 15.548 11.835 31.386  0.50 45.00  ? 12  LYS A CE  1 
ATOM   100  N NZ  . LYS A 1 12  ? 16.808 11.147 30.982  0.50 46.92  ? 12  LYS A NZ  1 
ATOM   101  N N   . SER A 1 13  ? 10.106 13.340 29.247  1.00 39.48  ? 13  SER A N   1 
ATOM   102  C CA  . SER A 1 13  ? 10.166 14.548 28.430  1.00 34.83  ? 13  SER A CA  1 
ATOM   103  C C   . SER A 1 13  ? 9.069  15.530 28.807  1.00 34.57  ? 13  SER A C   1 
ATOM   104  O O   . SER A 1 13  ? 9.289  16.746 28.794  1.00 34.16  ? 13  SER A O   1 
ATOM   105  C CB  . SER A 1 13  ? 10.070 14.187 26.943  1.00 31.06  ? 13  SER A CB  1 
ATOM   106  O OG  . SER A 1 13  ? 11.144 13.331 26.553  1.00 33.14  ? 13  SER A OG  1 
ATOM   107  N N   . ASP A 1 14  ? 7.880  15.024 29.143  1.00 37.94  ? 14  ASP A N   1 
ATOM   108  C CA  . ASP A 1 14  ? 6.792  15.917 29.531  1.00 40.03  ? 14  ASP A CA  1 
ATOM   109  C C   . ASP A 1 14  ? 7.115  16.649 30.827  1.00 40.05  ? 14  ASP A C   1 
ATOM   110  O O   . ASP A 1 14  ? 6.844  17.851 30.954  1.00 35.91  ? 14  ASP A O   1 
ATOM   111  C CB  . ASP A 1 14  ? 5.486  15.132 29.668  1.00 44.80  ? 14  ASP A CB  1 
ATOM   112  C CG  . ASP A 1 14  ? 4.847  14.821 28.322  1.00 48.09  ? 14  ASP A CG  1 
ATOM   113  O OD1 . ASP A 1 14  ? 5.397  15.240 27.276  1.00 45.82  ? 14  ASP A OD1 1 
ATOM   114  O OD2 . ASP A 1 14  ? 3.785  14.162 28.315  1.00 50.89  ? 14  ASP A OD2 1 
ATOM   115  N N   . LEU A 1 15  ? 7.681  15.934 31.804  1.00 42.85  ? 15  LEU A N   1 
ATOM   116  C CA  . LEU A 1 15  ? 8.007  16.556 33.083  1.00 43.53  ? 15  LEU A CA  1 
ATOM   117  C C   . LEU A 1 15  ? 9.108  17.591 32.913  1.00 38.65  ? 15  LEU A C   1 
ATOM   118  O O   . LEU A 1 15  ? 9.025  18.695 33.463  1.00 35.22  ? 15  LEU A O   1 
ATOM   119  C CB  . LEU A 1 15  ? 8.416  15.491 34.102  1.00 46.34  ? 15  LEU A CB  1 
ATOM   120  C CG  . LEU A 1 15  ? 7.354  14.455 34.492  0.78 49.87  ? 15  LEU A CG  1 
ATOM   121  C CD1 . LEU A 1 15  ? 7.949  13.424 35.442  0.74 51.66  ? 15  LEU A CD1 1 
ATOM   122  C CD2 . LEU A 1 15  ? 6.124  15.114 35.121  0.74 47.03  ? 15  LEU A CD2 1 
ATOM   123  N N   . LEU A 1 16  ? 10.139 17.262 32.140  1.00 36.87  ? 16  LEU A N   1 
ATOM   124  C CA  . LEU A 1 16  ? 11.176 18.248 31.865  1.00 38.33  ? 16  LEU A CA  1 
ATOM   125  C C   . LEU A 1 16  ? 10.578 19.499 31.233  1.00 37.76  ? 16  LEU A C   1 
ATOM   126  O O   . LEU A 1 16  ? 10.913 20.622 31.626  1.00 36.63  ? 16  LEU A O   1 
ATOM   127  C CB  . LEU A 1 16  ? 12.250 17.640 30.966  1.00 36.05  ? 16  LEU A CB  1 
ATOM   128  C CG  . LEU A 1 16  ? 13.499 18.501 30.807  1.00 36.05  ? 16  LEU A CG  1 
ATOM   129  C CD1 . LEU A 1 16  ? 14.076 18.833 32.185  1.00 37.59  ? 16  LEU A CD1 1 
ATOM   130  C CD2 . LEU A 1 16  ? 14.540 17.820 29.888  1.00 30.66  ? 16  LEU A CD2 1 
ATOM   131  N N   . ARG A 1 17  ? 9.659  19.319 30.279  1.00 35.66  ? 17  ARG A N   1 
ATOM   132  C CA  . ARG A 1 17  ? 8.981  20.457 29.666  1.00 31.52  ? 17  ARG A CA  1 
ATOM   133  C C   . ARG A 1 17  ? 8.218  21.279 30.705  1.00 31.14  ? 17  ARG A C   1 
ATOM   134  O O   . ARG A 1 17  ? 8.325  22.509 30.741  1.00 34.72  ? 17  ARG A O   1 
ATOM   135  C CB  . ARG A 1 17  ? 8.045  19.962 28.567  1.00 31.88  ? 17  ARG A CB  1 
ATOM   136  C CG  . ARG A 1 17  ? 7.178  21.049 27.973  1.00 33.72  ? 17  ARG A CG  1 
ATOM   137  C CD  . ARG A 1 17  ? 6.314  20.494 26.849  1.00 32.20  ? 17  ARG A CD  1 
ATOM   138  N NE  . ARG A 1 17  ? 5.442  21.521 26.303  1.00 30.10  ? 17  ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 17  ? 4.287  21.869 26.857  1.00 40.86  ? 17  ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 17  ? 3.879  21.260 27.965  1.00 40.33  ? 17  ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 17  ? 3.539  22.818 26.310  1.00 43.08  ? 17  ARG A NH2 1 
ATOM   142  N N   . LEU A 1 18  ? 7.436  20.620 31.561  1.00 32.11  ? 18  LEU A N   1 
ATOM   143  C CA  . LEU A 1 18  ? 6.684  21.367 32.570  1.00 38.12  ? 18  LEU A CA  1 
ATOM   144  C C   . LEU A 1 18  ? 7.614  22.129 33.513  1.00 37.05  ? 18  LEU A C   1 
ATOM   145  O O   . LEU A 1 18  ? 7.311  23.258 33.922  1.00 34.30  ? 18  LEU A O   1 
ATOM   146  C CB  . LEU A 1 18  ? 5.771  20.430 33.362  0.80 37.66  ? 18  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 18  ? 4.526  19.883 32.660  0.60 37.97  ? 18  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 18  ? 3.674  19.095 33.652  0.60 36.29  ? 18  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 18  ? 3.721  21.005 32.017  0.60 34.65  ? 18  LEU A CD2 1 
ATOM   150  N N   . ASN A 1 19  ? 8.749  21.526 33.871  1.00 36.55  ? 19  ASN A N   1 
ATOM   151  C CA  . ASN A 1 19  ? 9.706  22.200 34.745  1.00 36.41  ? 19  ASN A CA  1 
ATOM   152  C C   . ASN A 1 19  ? 10.361 23.395 34.059  1.00 35.95  ? 19  ASN A C   1 
ATOM   153  O O   . ASN A 1 19  ? 10.602 24.422 34.702  1.00 38.82  ? 19  ASN A O   1 
ATOM   154  C CB  . ASN A 1 19  ? 10.776 21.219 35.212  1.00 38.99  ? 19  ASN A CB  1 
ATOM   155  C CG  . ASN A 1 19  ? 10.426 20.560 36.518  1.00 40.85  ? 19  ASN A CG  1 
ATOM   156  O OD1 . ASN A 1 19  ? 9.548  21.027 37.252  1.00 38.96  ? 19  ASN A OD1 1 
ATOM   157  N ND2 . ASN A 1 19  ? 11.122 19.478 36.832  1.00 44.43  ? 19  ASN A ND2 1 
ATOM   158  N N   . MET A 1 20  ? 10.675 23.282 32.760  1.00 32.43  ? 20  MET A N   1 
ATOM   159  C CA  . MET A 1 20  ? 11.276 24.425 32.083  1.00 32.13  ? 20  MET A CA  1 
ATOM   160  C C   . MET A 1 20  ? 10.275 25.561 31.939  1.00 33.64  ? 20  MET A C   1 
ATOM   161  O O   . MET A 1 20  ? 10.629 26.734 32.098  1.00 38.01  ? 20  MET A O   1 
ATOM   162  C CB  . MET A 1 20  ? 11.822 24.017 30.713  1.00 30.91  ? 20  MET A CB  1 
ATOM   163  C CG  . MET A 1 20  ? 13.036 23.120 30.797  1.00 35.03  ? 20  MET A CG  1 
ATOM   164  S SD  . MET A 1 20  ? 13.711 22.733 29.163  1.00 38.10  ? 20  MET A SD  1 
ATOM   165  C CE  . MET A 1 20  ? 14.727 24.178 28.858  1.00 35.63  ? 20  MET A CE  1 
ATOM   166  N N   . ILE A 1 21  ? 9.024  25.232 31.623  1.00 33.74  ? 21  ILE A N   1 
ATOM   167  C CA  . ILE A 1 21  ? 7.981  26.248 31.566  1.00 33.28  ? 21  ILE A CA  1 
ATOM   168  C C   . ILE A 1 21  ? 7.881  26.976 32.902  1.00 34.66  ? 21  ILE A C   1 
ATOM   169  O O   . ILE A 1 21  ? 7.842  28.211 32.959  1.00 35.50  ? 21  ILE A O   1 
ATOM   170  C CB  . ILE A 1 21  ? 6.641  25.610 31.174  1.00 33.28  ? 21  ILE A CB  1 
ATOM   171  C CG1 . ILE A 1 21  ? 6.684  25.147 29.712  1.00 34.68  ? 21  ILE A CG1 1 
ATOM   172  C CG2 . ILE A 1 21  ? 5.520  26.594 31.453  1.00 34.57  ? 21  ILE A CG2 1 
ATOM   173  C CD1 . ILE A 1 21  ? 5.464  24.381 29.287  1.00 34.45  ? 21  ILE A CD1 1 
ATOM   174  N N   . ALA A 1 22  ? 7.850  26.215 33.996  1.00 39.42  ? 22  ALA A N   1 
ATOM   175  C CA  . ALA A 1 22  ? 7.821  26.827 35.322  1.00 40.11  ? 22  ALA A CA  1 
ATOM   176  C C   . ALA A 1 22  ? 9.049  27.703 35.548  1.00 38.85  ? 22  ALA A C   1 
ATOM   177  O O   . ALA A 1 22  ? 8.938  28.825 36.056  1.00 38.12  ? 22  ALA A O   1 
ATOM   178  C CB  . ALA A 1 22  ? 7.714  25.740 36.392  1.00 37.10  ? 22  ALA A CB  1 
ATOM   179  N N   . GLY A 1 23  ? 10.228 27.216 35.168  1.00 41.64  ? 23  GLY A N   1 
ATOM   180  C CA  . GLY A 1 23  ? 11.424 28.036 35.288  1.00 43.79  ? 23  GLY A CA  1 
ATOM   181  C C   . GLY A 1 23  ? 11.375 29.282 34.422  1.00 42.94  ? 23  GLY A C   1 
ATOM   182  O O   . GLY A 1 23  ? 11.780 30.367 34.851  1.00 41.09  ? 23  GLY A O   1 
ATOM   183  N N   . PHE A 1 24  ? 10.876 29.143 33.188  1.00 38.03  ? 24  PHE A N   1 
ATOM   184  C CA  . PHE A 1 24  ? 10.676 30.305 32.329  1.00 38.64  ? 24  PHE A CA  1 
ATOM   185  C C   . PHE A 1 24  ? 9.683  31.284 32.931  1.00 43.08  ? 24  PHE A C   1 
ATOM   186  O O   . PHE A 1 24  ? 9.779  32.492 32.687  1.00 46.16  ? 24  PHE A O   1 
ATOM   187  C CB  . PHE A 1 24  ? 10.195 29.861 30.946  0.90 34.93  ? 24  PHE A CB  1 
ATOM   188  C CG  . PHE A 1 24  ? 11.288 29.340 30.062  0.80 35.65  ? 24  PHE A CG  1 
ATOM   189  C CD1 . PHE A 1 24  ? 11.133 28.149 29.381  0.80 34.47  ? 24  PHE A CD1 1 
ATOM   190  C CD2 . PHE A 1 24  ? 12.465 30.050 29.903  0.80 38.80  ? 24  PHE A CD2 1 
ATOM   191  C CE1 . PHE A 1 24  ? 12.140 27.665 28.562  0.80 36.16  ? 24  PHE A CE1 1 
ATOM   192  C CE2 . PHE A 1 24  ? 13.472 29.574 29.085  0.80 39.16  ? 24  PHE A CE2 1 
ATOM   193  C CZ  . PHE A 1 24  ? 13.309 28.377 28.414  0.80 36.15  ? 24  PHE A CZ  1 
ATOM   194  N N   . GLY A 1 25  ? 8.725  30.792 33.711  1.00 44.75  ? 25  GLY A N   1 
ATOM   195  C CA  . GLY A 1 25  ? 7.773  31.662 34.375  1.00 45.25  ? 25  GLY A CA  1 
ATOM   196  C C   . GLY A 1 25  ? 8.401  32.703 35.279  1.00 49.23  ? 25  GLY A C   1 
ATOM   197  O O   . GLY A 1 25  ? 7.770  33.712 35.609  1.00 46.94  ? 25  GLY A O   1 
ATOM   198  N N   . GLU A 1 26  ? 9.649  32.480 35.684  1.00 54.17  ? 26  GLU A N   1 
ATOM   199  C CA  . GLU A 1 26  ? 10.358 33.411 36.553  1.00 53.13  ? 26  GLU A CA  1 
ATOM   200  C C   . GLU A 1 26  ? 11.141 34.471 35.780  1.00 52.76  ? 26  GLU A C   1 
ATOM   201  O O   . GLU A 1 26  ? 11.876 35.246 36.398  1.00 53.90  ? 26  GLU A O   1 
ATOM   202  C CB  . GLU A 1 26  ? 11.303 32.645 37.486  1.00 53.52  ? 26  GLU A CB  1 
ATOM   203  C CG  . GLU A 1 26  ? 10.677 31.437 38.181  1.00 53.08  ? 26  GLU A CG  1 
ATOM   204  C CD  . GLU A 1 26  ? 9.611  31.812 39.205  1.00 56.74  ? 26  GLU A CD  1 
ATOM   205  O OE1 . GLU A 1 26  ? 8.861  30.906 39.633  1.00 56.92  ? 26  GLU A OE1 1 
ATOM   206  O OE2 . GLU A 1 26  ? 9.521  33.001 39.594  1.00 56.16  ? 26  GLU A OE2 1 
ATOM   207  N N   . TYR A 1 27  ? 11.001 34.528 34.451  1.00 48.39  ? 27  TYR A N   1 
ATOM   208  C CA  . TYR A 1 27  ? 11.683 35.518 33.624  1.00 51.34  ? 27  TYR A CA  1 
ATOM   209  C C   . TYR A 1 27  ? 10.672 36.195 32.701  1.00 54.14  ? 27  TYR A C   1 
ATOM   210  O O   . TYR A 1 27  ? 9.482  35.865 32.690  1.00 54.54  ? 27  TYR A O   1 
ATOM   211  C CB  . TYR A 1 27  ? 12.819 34.879 32.806  1.00 49.50  ? 27  TYR A CB  1 
ATOM   212  C CG  . TYR A 1 27  ? 13.913 34.242 33.644  1.00 48.23  ? 27  TYR A CG  1 
ATOM   213  C CD1 . TYR A 1 27  ? 14.959 35.002 34.157  1.00 50.28  ? 27  TYR A CD1 1 
ATOM   214  C CD2 . TYR A 1 27  ? 13.902 32.878 33.919  1.00 44.39  ? 27  TYR A CD2 1 
ATOM   215  C CE1 . TYR A 1 27  ? 15.963 34.421 34.922  1.00 52.36  ? 27  TYR A CE1 1 
ATOM   216  C CE2 . TYR A 1 27  ? 14.901 32.290 34.687  1.00 45.01  ? 27  TYR A CE2 1 
ATOM   217  C CZ  . TYR A 1 27  ? 15.928 33.065 35.184  1.00 52.67  ? 27  TYR A CZ  1 
ATOM   218  O OH  . TYR A 1 27  ? 16.920 32.482 35.949  1.00 58.15  ? 27  TYR A OH  1 
ATOM   219  N N   . ASP A 1 28  ? 11.160 37.157 31.912  0.87 57.65  ? 28  ASP A N   1 
ATOM   220  C CA  . ASP A 1 28  ? 10.341 37.822 30.895  0.87 61.93  ? 28  ASP A CA  1 
ATOM   221  C C   . ASP A 1 28  ? 10.258 36.914 29.669  0.87 63.83  ? 28  ASP A C   1 
ATOM   222  O O   . ASP A 1 28  ? 10.874 37.141 28.625  0.87 63.22  ? 28  ASP A O   1 
ATOM   223  C CB  . ASP A 1 28  ? 10.912 39.188 30.540  0.87 64.58  ? 28  ASP A CB  1 
ATOM   224  N N   . MET A 1 29  ? 9.479  35.848 29.825  1.00 63.69  ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.320  34.832 28.797  1.00 60.96  ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.843  34.523 28.648  1.00 59.20  ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.160  34.253 29.641  1.00 61.09  ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.097 33.561 29.145  0.92 59.88  ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.605 33.728 29.135  0.76 63.61  ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.228 34.294 27.539  0.75 67.76  ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 13.942 33.799 27.652  0.56 67.82  ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.357  34.564 27.413  1.00 53.86  ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.957  34.325 27.097  1.00 52.89  ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.850  33.048 26.271  1.00 52.16  ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.462  32.945 25.202  1.00 50.60  ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.378  35.518 26.337  1.00 57.84  ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.956  35.340 25.851  1.00 61.13  ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.579  36.379 24.814  0.75 63.88  ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 4.169  37.480 24.837  0.72 65.00  ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.706  36.086 23.968  0.71 64.69  ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.091  32.075 26.770  1.00 49.65  ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.865  30.847 26.018  1.00 45.87  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.909  31.125 24.863  1.00 43.43  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.753  31.500 25.082  1.00 44.73  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.303  29.754 26.922  1.00 45.08  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.323  28.399 26.261  1.00 45.44  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.325  28.020 25.363  1.00 45.27  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.358  27.506 26.506  1.00 45.58  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.357  26.783 24.737  1.00 44.36  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.400  26.267 25.888  1.00 43.72  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.399  25.909 25.005  1.00 44.49  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.453  24.673 24.400  1.00 38.99  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.386  30.944 23.635  1.00 41.30  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.557  31.209 22.461  1.00 44.65  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.972  30.217 21.389  1.00 44.73  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 5.108  30.275 20.902  1.00 42.85  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.726  32.654 21.986  1.00 47.03  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.887  32.984 20.747  0.73 48.59  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.361  32.067 20.077  0.73 44.37  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.758  34.189 20.447  0.73 51.70  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 3.065  29.308 21.028  1.00 43.69  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.363  28.320 20.002  1.00 44.42  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.813  28.712 18.638  1.00 43.59  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.869  27.904 17.708  1.00 42.72  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.856  26.929 20.416  1.00 46.38  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.346  26.858 20.564  1.00 52.00  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.650  27.834 20.222  1.00 54.57  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.854  25.805 21.028  1.00 52.25  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.284  29.924 18.498  1.00 44.07  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.928  30.441 17.182  1.00 45.79  ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.096  31.189 16.557  1.00 46.97  ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.505  30.896 15.432  1.00 47.18  ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.672  31.332 17.272  1.00 50.56  ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.260  31.795 15.880  1.00 52.45  ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.453 30.581 17.946  1.00 50.29  ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.671  32.145 17.282  1.00 48.28  ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.829  32.903 16.806  1.00 52.13  ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.964  32.880 17.829  1.00 49.85  ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.397  33.928 18.315  1.00 54.74  ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.424  34.339 16.483  1.00 60.99  ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.345  34.455 15.422  0.88 68.27  ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.872  35.881 15.236  0.85 75.58  ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 2.680  36.294 14.073  0.85 78.67  ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 2.697  36.588 16.254  0.85 79.00  ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.500  31.703 18.155  1.00 45.32  ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.690  31.674 19.010  1.00 43.47  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.891  32.283 18.302  1.00 43.89  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.986  32.284 17.075  1.00 45.50  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.902  30.179 19.276  1.00 39.06  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.289  29.501 18.104  1.00 40.64  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 6.097  30.344 17.741  1.00 42.70  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.802  32.838 19.092  1.00 40.80  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.135 33.157 18.605  1.00 38.95  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.137 32.065 18.934  1.00 37.96  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.136 31.919 18.225  1.00 38.44  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.610 34.488 19.197  1.00 44.25  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.767 35.679 18.762  0.60 49.36  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 11.011 36.915 19.602  0.60 55.05  ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 12.051 36.980 20.294  0.55 55.20  ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.154 37.823 19.570  0.55 58.39  ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.871 31.294 19.989  1.00 36.22  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.694 30.173 20.421  1.00 32.17  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.822 28.927 20.425  1.00 31.05  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.727 28.933 21.002  1.00 34.07  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.282 30.424 21.825  0.70 33.18  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 14.157 31.680 21.820  0.60 34.96  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 14.083 29.219 22.300  0.60 32.93  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.509 31.480 21.170  0.60 33.48  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.305 27.860 19.797  1.00 29.64  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.625 26.571 19.799  1.00 28.71  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.548 25.543 20.442  1.00 31.97  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.620 25.236 19.907  1.00 31.64  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.213 26.133 18.386  1.00 29.82  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.700 24.721 18.425  1.00 30.48  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.133 27.069 17.848  1.00 29.32  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.133 25.015 21.589  1.00 31.41  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.884 23.996 22.307  1.00 30.60  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.236 22.647 22.056  1.00 28.30  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.030 22.477 22.269  1.00 30.19  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 12.931 24.290 23.815  1.00 33.85  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.463 25.697 24.052  1.00 32.93  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.768 23.224 24.536  1.00 32.30  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.190 26.193 25.419  1.00 32.83  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.037 21.686 21.629  1.00 26.07  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.575 20.340 21.352  1.00 29.32  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.154 19.420 22.415  1.00 31.81  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.374 19.387 22.610  1.00 33.84  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.016 19.905 19.946  1.00 28.13  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.530 18.621 19.647  1.00 35.89  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.294 18.662 23.085  1.00 29.87  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.732 17.768 24.154  1.00 28.02  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.412 16.344 23.730  1.00 30.48  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.243 15.929 23.726  1.00 29.14  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.072 18.104 25.497  1.00 26.89  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.448 19.525 25.926  1.00 27.14  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.495 17.077 26.540  1.00 33.88  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 11.828 19.954 27.238  1.00 27.83  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.449 15.589 23.383  1.00 29.12  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.246 14.255 22.873  1.00 32.44  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.482 13.777 22.161  1.00 34.96  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.596 13.970 22.644  1.00 43.12  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.298 13.138 21.012  1.00 30.23  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.384 12.735 20.174  1.00 30.61  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.412 13.540 18.896  1.00 27.50  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.754 14.580 18.766  1.00 26.16  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.161 13.035 17.921  1.00 31.70  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.236 13.740 16.652  1.00 28.36  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 14.905 13.721 15.912  1.00 29.54  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.606 14.660 15.161  1.00 28.49  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.331 13.122 15.788  1.00 28.56  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.712 13.476 16.273  1.00 31.17  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 18.901 14.608 16.760  1.00 30.32  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.611 12.619 16.158  1.00 33.85  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.129 12.641 16.058  1.00 28.66  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.793 12.619 15.477  1.00 30.51  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 11.908 13.723 16.019  1.00 31.33  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.163 14.365 15.266  1.00 26.96  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 11.975 13.961 17.342  1.00 30.70  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.232 15.070 17.930  1.00 25.92  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.712 16.389 17.350  1.00 28.39  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.902 17.264 17.015  1.00 27.81  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.383 15.062 19.462  1.00 25.87  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.035 13.770 19.961  1.00 31.74  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.469 16.077 20.114  1.00 26.29  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.033 16.539 17.208  1.00 24.06  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.578 17.770 16.650  1.00 25.90  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.115 17.972 15.216  1.00 25.23  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.737 19.083 14.827  1.00 26.76  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.107 17.765 16.704  0.90 25.14  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.707 19.102 16.382  0.80 25.91  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.923 20.030 17.385  0.80 27.13  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 16.015 19.449 15.074  0.80 29.36  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.454 21.269 17.095  0.80 29.41  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.545 20.691 14.780  0.80 30.56  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.764 21.600 15.790  0.80 28.57  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.143 16.908 14.414  1.00 28.41  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.673 17.003 13.034  1.00 28.93  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.217 17.458 12.976  1.00 28.31  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.848 18.276 12.128  1.00 26.19  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.842 15.654 12.336  1.00 28.42  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 13.968 15.465 11.313  1.00 37.20  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 15.198 16.263 11.656  1.00 41.25  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.308 13.993 11.221  1.00 39.26  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.369 16.938 13.870  1.00 29.89  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 8.966  17.361 13.869  1.00 28.99  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.828  18.826 14.263  1.00 29.77  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 7.988  19.548 13.711  1.00 33.51  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.141  16.478 14.810  1.00 36.26  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.121  15.137 14.356  1.00 43.71  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.638  19.277 15.227  1.00 26.89  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.657  20.688 15.605  1.00 28.10  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.022 21.577 14.425  1.00 28.06  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.367  22.594 14.170  1.00 31.24  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.654 20.897 16.740  1.00 25.27  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.096 21.225 13.717  1.00 26.31  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.478 21.959 12.513  1.00 26.15  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.316 22.065 11.522  1.00 31.82  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 9.998  23.153 11.025  1.00 30.68  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.692 21.276 11.868  1.00 25.57  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 12.976 21.749 10.479  1.00 26.22  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.565 22.989 10.261  1.00 31.23  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.639 20.967 9.395   1.00 26.36  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.826 23.427 8.970   1.00 29.09  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 12.889 21.401 8.106   1.00 31.45  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.482 22.627 7.893   1.00 32.71  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.658  20.941 11.230  1.00 28.31  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.587  20.969 10.241  1.00 29.24  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.349  21.680 10.762  1.00 34.41  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.591  22.255 9.969   1.00 35.32  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.285  19.550 9.773   1.00 28.49  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.322  19.038 8.816   1.00 29.50  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.435  19.514 7.529   1.00 30.88  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.354 18.176 8.989   1.00 28.00  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.463 18.931 6.933   1.00 30.23  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.039 18.116 7.797   1.00 28.88  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.149  21.696 12.079  1.00 33.08  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 6.006  22.425 12.622  1.00 31.95  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.137  23.922 12.364  1.00 37.88  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.125  24.622 12.253  1.00 44.96  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.856  22.115 14.119  1.00 30.21  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.679  22.789 14.812  0.94 34.05  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.551  22.375 16.283  0.58 32.62  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.142  21.385 16.716  0.55 29.00  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.777  23.134 17.050  0.55 32.01  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.364  24.428 12.208  1.00 39.20  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.585  25.860 12.036  1.00 38.70  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.388  26.192 10.781  1.00 39.19  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.109  27.193 10.748  1.00 38.39  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.265  26.437 13.272  1.00 35.84  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.396  26.327 14.500  1.00 39.81  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.413  27.275 14.764  1.00 43.24  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.543  25.271 15.395  1.00 37.47  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.608  27.181 15.891  1.00 41.68  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.738  25.170 16.526  1.00 39.92  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.769  26.129 16.769  1.00 41.75  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.954  26.045 17.895  1.00 38.32  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.258  25.392 9.723   1.00 39.80  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.088  25.666 8.552   1.00 40.06  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.668  26.922 7.793   1.00 40.46  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.405  27.348 6.895   1.00 42.73  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.116  24.469 7.593   0.90 37.47  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.802  23.763 7.363   0.80 34.59  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.903  22.764 6.227   0.70 38.47  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 7.730  23.187 5.066   0.70 41.95  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 8.178  21.573 6.482   0.70 35.90  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.528  27.530 8.123   1.00 40.85  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.151  28.802 7.513   1.00 48.03  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.726  30.013 8.242   1.00 47.20  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.623  31.130 7.725   1.00 47.28  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.625  28.944 7.442   1.00 53.88  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.017  28.572 6.102   0.85 61.05  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 5.135  27.096 5.799   0.81 63.24  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 5.599  26.750 4.697   0.54 64.13  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 4.775  26.281 6.675   0.53 64.90  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.331  29.826 9.418   1.00 39.94  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.896  30.936 10.176  1.00 42.52  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.347 30.661 10.564  1.00 42.31  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.806 31.093 11.626  1.00 39.36  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.042  31.241 11.410  1.00 41.06  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.690  31.874 11.049  0.78 46.41  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.905  32.348 12.276  0.76 49.73  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.620  33.349 13.064  0.75 50.67  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.252  33.087 14.208  0.72 49.48  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.261  31.855 14.700  0.72 47.77  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.877  34.056 14.862  0.72 45.47  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.089 29.972 9.688   1.00 41.23  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.480 29.635 9.980   1.00 39.42  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.348 30.871 10.161  1.00 41.73  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.345 30.825 10.890  1.00 44.82  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.052 28.771 8.860   1.00 36.31  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.444 27.381 8.741   1.00 36.42  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.030 26.685 7.531   1.00 33.72  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.711 26.585 9.997   1.00 34.24  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 12.997 31.974 9.504   1.00 43.33  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 13.791 33.191 9.613   1.00 52.60  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.671 33.832 10.988  1.00 52.78  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.588 34.540 11.420  1.00 56.66  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.364 34.189 8.537   1.00 62.11  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 14.346 34.260 7.396   1.00 74.11  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 15.566 34.172 7.663   1.00 76.45  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 13.901 34.401 6.236   1.00 80.39  ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.557 33.610 11.678  1.00 48.26  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.273 34.274 12.940  1.00 47.60  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.604 33.419 14.155  1.00 46.73  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.429 33.885 15.285  1.00 50.42  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 10.793 34.685 12.996  1.00 49.54  ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.351 35.680 11.924  1.00 57.96  ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 9.909  35.019 10.624  0.70 62.28  ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 9.002  35.566 9.959   0.61 65.24  ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 10.463 33.958 10.266  0.61 62.15  ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.088 32.193 13.963  1.00 40.79  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.159 31.206 15.037  1.00 41.52  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.589 30.706 15.214  1.00 40.37  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.313 30.495 14.235  1.00 38.78  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.202 30.030 14.749  1.00 41.44  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.752 30.489 14.892  1.00 40.44  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.486 28.835 15.649  1.00 39.32  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.759  29.445 14.472  1.00 38.50  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 14.993 30.519 16.471  1.00 33.67  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.194 29.767 16.805  1.00 34.48  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.801 28.518 17.581  1.00 33.52  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.053 28.599 18.564  1.00 35.96  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.179 30.609 17.615  1.00 38.46  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.318 27.375 17.144  1.00 32.82  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 15.991 26.072 17.700  1.00 28.79  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.036 25.622 18.715  1.00 31.69  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.223 25.938 18.592  1.00 30.92  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.905 25.019 16.595  1.00 26.71  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.725 25.175 15.695  1.00 30.54  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 13.557 24.464 15.934  1.00 28.41  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 14.787 26.005 14.576  1.00 30.12  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 12.459 24.593 15.089  1.00 28.57  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 13.695 26.139 13.729  1.00 31.49  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.529 25.433 13.985  1.00 32.31  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.580 24.849 19.707  1.00 28.51  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.446 24.188 20.684  1.00 28.13  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.897 22.791 20.932  1.00 30.71  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.697 22.631 21.187  1.00 32.45  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.522 24.961 22.023  0.70 27.62  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 17.904 26.418 21.792  0.70 33.25  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.528 24.308 22.978  0.70 27.90  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.734 27.285 23.002  0.70 36.39  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.774 21.791 20.914  1.00 26.59  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.402 20.410 21.207  1.00 28.89  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 17.950 19.939 22.540  1.00 31.87  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.126 20.159 22.867  1.00 29.62  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.088 19.275 23.315  1.00 32.92  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.476 18.591 24.546  1.00 29.80  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.258 17.101 24.334  1.00 31.31  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.172 16.698 23.904  1.00 34.31  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.648 19.095 25.740  1.00 28.22  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 16.898 20.587 25.958  1.00 28.19  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 16.934 18.248 26.972  1.00 29.88  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.147 21.158 27.162  1.00 32.00  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.261 16.267 24.634  1.00 33.74  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.108 14.843 24.333  1.00 38.24  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.633 14.060 25.550  1.00 37.82  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.337 13.956 26.562  1.00 41.17  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.358 14.195 23.718  0.80 45.14  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.627 14.389 24.479  0.70 49.41  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.414 15.512 24.338  0.70 51.06  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.296 13.563 25.316  0.70 51.59  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.490 15.389 25.094  0.70 52.62  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.443 14.215 25.697  0.70 53.30  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.415 13.538 25.438  0.70 34.72  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 15.892 12.489 26.296  0.70 37.77  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 15.646 11.219 25.492  0.70 47.43  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 15.062 10.263 26.015  0.70 53.16  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.596 12.944 26.968  0.70 32.13  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 13.628 13.227 25.958  0.70 33.89  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.815 14.211 27.782  0.70 29.85  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 16.050 11.202 24.220  0.50 45.19  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 15.913 10.036 23.369  0.50 42.58  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 17.133 9.138  23.433  0.50 43.21  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 17.726 8.966  24.504  0.50 44.09  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 17.535 8.569  22.295  0.50 41.43  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 18.637 7.615  22.303  0.50 44.72  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 19.941 8.222  21.788  0.50 43.83  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.906 8.342  22.549  0.50 45.46  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 18.256 6.375  21.494  0.50 48.12  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 16.978 5.736  21.944  0.50 48.72  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 16.888 4.979  23.092  0.50 50.77  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 15.737 5.749  21.403  0.50 48.39  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 15.647 4.550  23.237  0.50 52.21  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 14.929 5.003  22.225  0.50 50.61  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 19.997 8.603  20.509  0.70 42.96  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 21.232 9.169  19.966  0.70 39.72  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 21.284 10.693 20.065  0.70 36.56  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.280 11.250 20.540  0.70 32.81  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 21.423 8.745  18.508  0.70 39.45  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 22.751 9.257  17.939  0.70 41.37  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 23.925 8.571  18.643  0.70 43.90  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 22.826 9.078  16.428  0.70 38.21  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 20.246 11.381 19.587  0.70 35.85  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 20.152 12.827 19.713  0.70 38.95  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 21.253 13.633 19.048  0.70 37.14  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 22.036 14.301 19.724  0.70 38.99  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 21.299 13.610 17.716  1.00 36.65  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.364 14.288 16.993  1.00 29.49  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.155 15.799 16.930  1.00 31.78  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.130 16.552 16.930  1.00 41.66  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 22.478 13.704 15.582  1.00 33.89  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 23.660 14.190 14.845  1.00 28.97  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.877 13.560 15.002  1.00 27.74  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 23.578 15.312 14.041  1.00 35.83  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 26.015 14.022 14.344  1.00 41.58  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 24.702 15.775 13.365  1.00 46.63  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 25.925 15.124 13.526  1.00 46.27  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 20.909 16.271 16.812  1.00 28.84  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.630 17.707 16.813  1.00 26.89  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 20.522 18.265 18.232  1.00 34.31  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.188 19.438 18.418  1.00 36.28  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.346 18.009 16.034  1.00 25.02  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.485 17.826 14.542  1.00 30.54  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 18.867 16.765 13.880  1.00 29.01  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 20.262 18.703 13.792  1.00 25.89  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 19.017 16.588 12.493  1.00 25.03  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 20.411 18.539 12.401  1.00 26.54  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.791 17.480 11.763  1.00 27.09  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 19.949 17.325 10.385  1.00 25.26  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 20.826 17.447 19.223  1.00 33.78  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 20.686 17.825 20.625  1.00 31.51  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 21.989 18.435 21.130  1.00 32.94  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 23.083 17.967 20.795  1.00 36.54  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 20.321 16.597 21.436  1.00 26.49  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.874 19.500 21.917  1.00 44.33  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 23.045 20.134 22.509  1.00 45.64  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 23.036 20.080 24.020  1.00 44.18  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.008 20.519 24.649  1.00 42.36  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.157 21.598 22.071  1.00 50.03  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.403 21.739 20.585  1.00 53.45  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 23.932 20.777 19.978  1.00 46.15  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 23.069 22.815 20.038  1.00 60.20  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 21.969 19.581 24.617  1.00 37.22  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.830 19.608 26.058  1.00 43.59  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.344 18.259 26.550  1.00 40.21  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.516 17.607 25.901  1.00 35.52  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 20.880 20.738 26.480  0.92 44.59  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.383 22.059 26.009  0.82 46.30  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.163 22.630 24.788  0.82 47.84  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.248 22.953 26.721  0.82 49.87  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 21.821 23.837 24.706  0.82 48.89  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.494 24.057 25.879  0.82 50.60  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.826 22.935 27.997  0.82 53.05  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.296 25.133 26.269  0.82 51.35  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.621 24.003 28.383  0.82 54.11  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.847 25.087 27.523  0.82 54.80  ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 21.922 17.828 27.670  1.00 40.96  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.355 16.782 28.495  1.00 41.91  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.268 17.382 29.381  1.00 43.67  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.285 18.582 29.666  1.00 42.81  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.434 16.136 29.364  1.00 41.87  ? 79  ARG A CB  1 
ATOM   633  N N   . PRO A 1 80  ? 19.298 16.572 29.801  1.00 42.32  ? 80  PRO A N   1 
ATOM   634  C CA  . PRO A 1 80  ? 18.245 17.080 30.694  1.00 46.19  ? 80  PRO A CA  1 
ATOM   635  C C   . PRO A 1 80  ? 18.781 17.746 31.947  1.00 51.51  ? 80  PRO A C   1 
ATOM   636  O O   . PRO A 1 80  ? 18.164 18.698 32.447  1.00 49.41  ? 80  PRO A O   1 
ATOM   637  C CB  . PRO A 1 80  ? 17.447 15.815 31.035  1.00 46.23  ? 80  PRO A CB  1 
ATOM   638  C CG  . PRO A 1 80  ? 17.668 14.907 29.849  1.00 44.54  ? 80  PRO A CG  1 
ATOM   639  C CD  . PRO A 1 80  ? 19.071 15.173 29.397  1.00 43.34  ? 80  PRO A CD  1 
ATOM   640  N N   . ALA A 1 81  ? 19.921 17.278 32.462  1.00 53.37  ? 81  ALA A N   1 
ATOM   641  C CA  . ALA A 1 81  ? 20.474 17.812 33.700  1.00 57.83  ? 81  ALA A CA  1 
ATOM   642  C C   . ALA A 1 81  ? 20.882 19.272 33.575  1.00 55.78  ? 81  ALA A C   1 
ATOM   643  O O   . ALA A 1 81  ? 21.006 19.956 34.597  1.00 56.91  ? 81  ALA A O   1 
ATOM   644  C CB  . ALA A 1 81  ? 21.673 16.971 34.141  1.00 62.21  ? 81  ALA A CB  1 
ATOM   645  N N   . GLU A 1 82  ? 21.077 19.767 32.353  1.00 49.69  ? 82  GLU A N   1 
ATOM   646  C CA  . GLU A 1 82  ? 21.466 21.150 32.119  1.00 50.01  ? 82  GLU A CA  1 
ATOM   647  C C   . GLU A 1 82  ? 20.282 22.046 31.767  1.00 50.39  ? 82  GLU A C   1 
ATOM   648  O O   . GLU A 1 82  ? 20.482 23.148 31.242  1.00 50.28  ? 82  GLU A O   1 
ATOM   649  C CB  . GLU A 1 82  ? 22.511 21.215 31.007  0.80 49.18  ? 82  GLU A CB  1 
ATOM   650  C CG  . GLU A 1 82  ? 23.779 20.435 31.302  0.70 49.14  ? 82  GLU A CG  1 
ATOM   651  C CD  . GLU A 1 82  ? 24.619 20.225 30.066  0.60 43.59  ? 82  GLU A CD  1 
ATOM   652  O OE1 . GLU A 1 82  ? 24.119 19.612 29.099  0.60 39.95  ? 82  GLU A OE1 1 
ATOM   653  O OE2 . GLU A 1 82  ? 25.778 20.678 30.062  0.60 43.04  ? 82  GLU A OE2 1 
ATOM   654  N N   . ALA A 1 83  ? 19.054 21.595 32.043  1.00 46.18  ? 83  ALA A N   1 
ATOM   655  C CA  . ALA A 1 83  ? 17.876 22.341 31.612  1.00 48.39  ? 83  ALA A CA  1 
ATOM   656  C C   . ALA A 1 83  ? 17.768 23.681 32.328  1.00 47.71  ? 83  ALA A C   1 
ATOM   657  O O   . ALA A 1 83  ? 17.518 24.714 31.693  1.00 44.69  ? 83  ALA A O   1 
ATOM   658  C CB  . ALA A 1 83  ? 16.616 21.509 31.840  1.00 51.68  ? 83  ALA A CB  1 
ATOM   659  N N   . ASP A 1 84  ? 17.941 23.688 33.654  1.00 51.22  ? 84  ASP A N   1 
ATOM   660  C CA  . ASP A 1 84  ? 17.823 24.945 34.386  1.00 50.80  ? 84  ASP A CA  1 
ATOM   661  C C   . ASP A 1 84  ? 18.925 25.912 33.987  1.00 51.58  ? 84  ASP A C   1 
ATOM   662  O O   . ASP A 1 84  ? 18.690 27.123 33.908  1.00 51.20  ? 84  ASP A O   1 
ATOM   663  C CB  . ASP A 1 84  ? 17.841 24.695 35.894  1.00 56.94  ? 84  ASP A CB  1 
ATOM   664  C CG  . ASP A 1 84  ? 16.655 23.869 36.361  0.90 58.57  ? 84  ASP A CG  1 
ATOM   665  O OD1 . ASP A 1 84  ? 16.855 22.954 37.190  0.62 59.34  ? 84  ASP A OD1 1 
ATOM   666  O OD2 . ASP A 1 84  ? 15.527 24.123 35.881  0.60 55.53  ? 84  ASP A OD2 1 
ATOM   667  N N   . LYS A 1 85  ? 20.119 25.388 33.704  1.00 50.25  ? 85  LYS A N   1 
ATOM   668  C CA  . LYS A 1 85  ? 21.194 26.216 33.171  1.00 52.68  ? 85  LYS A CA  1 
ATOM   669  C C   . LYS A 1 85  ? 20.797 26.823 31.831  1.00 52.10  ? 85  LYS A C   1 
ATOM   670  O O   . LYS A 1 85  ? 21.113 27.984 31.545  1.00 53.91  ? 85  LYS A O   1 
ATOM   671  C CB  . LYS A 1 85  ? 22.463 25.369 33.049  1.00 54.11  ? 85  LYS A CB  1 
ATOM   672  C CG  . LYS A 1 85  ? 23.696 26.086 32.535  0.88 58.69  ? 85  LYS A CG  1 
ATOM   673  C CD  . LYS A 1 85  ? 24.957 25.356 32.991  0.69 63.65  ? 85  LYS A CD  1 
ATOM   674  C CE  . LYS A 1 85  ? 25.197 25.565 34.484  0.73 67.17  ? 85  LYS A CE  1 
ATOM   675  N NZ  . LYS A 1 85  ? 26.192 24.616 35.063  0.68 69.62  ? 85  LYS A NZ  1 
ATOM   676  N N   . LEU A 1 86  ? 20.073 26.056 31.012  1.00 47.30  ? 86  LEU A N   1 
ATOM   677  C CA  . LEU A 1 86  ? 19.619 26.541 29.716  1.00 43.89  ? 86  LEU A CA  1 
ATOM   678  C C   . LEU A 1 86  ? 18.507 27.577 29.852  1.00 46.53  ? 86  LEU A C   1 
ATOM   679  O O   . LEU A 1 86  ? 18.475 28.564 29.101  1.00 46.79  ? 86  LEU A O   1 
ATOM   680  C CB  . LEU A 1 86  ? 19.150 25.356 28.877  1.00 44.89  ? 86  LEU A CB  1 
ATOM   681  C CG  . LEU A 1 86  ? 18.750 25.632 27.438  0.90 43.87  ? 86  LEU A CG  1 
ATOM   682  C CD1 . LEU A 1 86  ? 19.906 26.269 26.708  0.90 46.19  ? 86  LEU A CD1 1 
ATOM   683  C CD2 . LEU A 1 86  ? 18.346 24.326 26.781  0.90 40.82  ? 86  LEU A CD2 1 
ATOM   684  N N   . VAL A 1 87  ? 17.551 27.337 30.757  1.00 41.76  ? 87  VAL A N   1 
ATOM   685  C CA  . VAL A 1 87  ? 16.538 28.344 31.072  1.00 44.15  ? 87  VAL A CA  1 
ATOM   686  C C   . VAL A 1 87  ? 17.215 29.665 31.398  1.00 49.22  ? 87  VAL A C   1 
ATOM   687  O O   . VAL A 1 87  ? 16.918 30.710 30.805  1.00 49.81  ? 87  VAL A O   1 
ATOM   688  C CB  . VAL A 1 87  ? 15.659 27.874 32.249  0.71 38.07  ? 87  VAL A CB  1 
ATOM   689  C CG1 . VAL A 1 87  ? 14.862 29.054 32.837  0.73 35.78  ? 87  VAL A CG1 1 
ATOM   690  C CG2 . VAL A 1 87  ? 14.738 26.737 31.823  0.72 35.26  ? 87  VAL A CG2 1 
ATOM   691  N N   . LYS A 1 88  ? 18.155 29.618 32.345  1.00 51.60  ? 88  LYS A N   1 
ATOM   692  C CA  . LYS A 1 88  ? 18.836 30.823 32.799  1.00 50.90  ? 88  LYS A CA  1 
ATOM   693  C C   . LYS A 1 88  ? 19.630 31.468 31.671  1.00 53.83  ? 88  LYS A C   1 
ATOM   694  O O   . LYS A 1 88  ? 19.655 32.694 31.553  1.00 57.83  ? 88  LYS A O   1 
ATOM   695  C CB  . LYS A 1 88  ? 19.741 30.481 33.985  0.80 47.83  ? 88  LYS A CB  1 
ATOM   696  C CG  . LYS A 1 88  ? 20.400 31.662 34.653  0.70 46.39  ? 88  LYS A CG  1 
ATOM   697  C CD  . LYS A 1 88  ? 21.383 31.179 35.712  0.50 48.24  ? 88  LYS A CD  1 
ATOM   698  C CE  . LYS A 1 88  ? 22.114 32.329 36.369  0.50 51.95  ? 88  LYS A CE  1 
ATOM   699  N NZ  . LYS A 1 88  ? 21.335 32.929 37.493  0.50 55.22  ? 88  LYS A NZ  1 
ATOM   700  N N   . LEU A 1 89  ? 20.288 30.662 30.829  1.00 50.62  ? 89  LEU A N   1 
ATOM   701  C CA  . LEU A 1 89  ? 21.085 31.238 29.748  1.00 50.06  ? 89  LEU A CA  1 
ATOM   702  C C   . LEU A 1 89  ? 20.196 31.833 28.662  1.00 49.88  ? 89  LEU A C   1 
ATOM   703  O O   . LEU A 1 89  ? 20.498 32.909 28.133  1.00 49.05  ? 89  LEU A O   1 
ATOM   704  C CB  . LEU A 1 89  ? 22.024 30.187 29.155  0.73 48.80  ? 89  LEU A CB  1 
ATOM   705  C CG  . LEU A 1 89  ? 23.241 29.777 29.985  0.73 52.99  ? 89  LEU A CG  1 
ATOM   706  C CD1 . LEU A 1 89  ? 24.206 28.937 29.160  0.73 52.11  ? 89  LEU A CD1 1 
ATOM   707  C CD2 . LEU A 1 89  ? 23.940 30.998 30.574  0.73 57.90  ? 89  LEU A CD2 1 
ATOM   708  N N   . LEU A 1 90  ? 19.101 31.140 28.318  1.00 49.87  ? 90  LEU A N   1 
ATOM   709  C CA  . LEU A 1 90  ? 18.147 31.656 27.338  1.00 51.10  ? 90  LEU A CA  1 
ATOM   710  C C   . LEU A 1 90  ? 17.527 32.962 27.808  1.00 57.74  ? 90  LEU A C   1 
ATOM   711  O O   . LEU A 1 90  ? 17.444 33.932 27.047  1.00 63.29  ? 90  LEU A O   1 
ATOM   712  C CB  . LEU A 1 90  ? 17.055 30.624 27.076  1.00 50.43  ? 90  LEU A CB  1 
ATOM   713  C CG  . LEU A 1 90  ? 17.120 29.852 25.769  1.00 53.13  ? 90  LEU A CG  1 
ATOM   714  C CD1 . LEU A 1 90  ? 15.941 28.903 25.722  1.00 52.03  ? 90  LEU A CD1 1 
ATOM   715  C CD2 . LEU A 1 90  ? 17.132 30.806 24.571  1.00 54.70  ? 90  LEU A CD2 1 
ATOM   716  N N   . ALA A 1 91  ? 17.040 32.991 29.048  0.93 79.07  ? 91  ALA A N   1 
ATOM   717  C CA  . ALA A 1 91  ? 16.805 34.265 29.704  0.93 81.58  ? 91  ALA A CA  1 
ATOM   718  C C   . ALA A 1 91  ? 18.118 35.027 29.741  0.93 81.59  ? 91  ALA A C   1 
ATOM   719  O O   . ALA A 1 91  ? 19.187 34.426 29.834  0.93 80.21  ? 91  ALA A O   1 
ATOM   720  C CB  . ALA A 1 91  ? 16.262 34.053 31.116  0.93 84.66  ? 91  ALA A CB  1 
ATOM   721  N N   . LYS A 1 92  ? 18.042 36.349 29.608  1.00 85.42  ? 92  LYS A N   1 
ATOM   722  C CA  . LYS A 1 92  ? 19.221 37.202 29.451  1.00 90.92  ? 92  LYS A CA  1 
ATOM   723  C C   . LYS A 1 92  ? 19.862 37.002 28.081  1.00 89.22  ? 92  LYS A C   1 
ATOM   724  O O   . LYS A 1 92  ? 20.628 37.859 27.628  1.00 92.55  ? 92  LYS A O   1 
ATOM   725  C CB  . LYS A 1 92  ? 20.252 36.962 30.565  1.00 94.88  ? 92  LYS A CB  1 
ATOM   726  N N   . GLY A 1 93  ? 19.564 35.873 27.429  1.00 84.76  ? 93  GLY A N   1 
ATOM   727  C CA  . GLY A 1 93  ? 19.898 35.593 26.043  1.00 79.29  ? 93  GLY A CA  1 
ATOM   728  C C   . GLY A 1 93  ? 21.236 36.073 25.527  1.00 79.93  ? 93  GLY A C   1 
ATOM   729  O O   . GLY A 1 93  ? 22.288 35.706 26.059  1.00 78.71  ? 93  GLY A O   1 
ATOM   730  N N   . GLU A 1 94  ? 21.192 36.891 24.473  1.00 84.23  ? 94  GLU A N   1 
ATOM   731  C CA  . GLU A 1 94  ? 22.378 37.406 23.783  1.00 90.96  ? 94  GLU A CA  1 
ATOM   732  C C   . GLU A 1 94  ? 23.339 36.289 23.375  1.00 92.14  ? 94  GLU A C   1 
ATOM   733  O O   . GLU A 1 94  ? 24.541 36.520 23.201  1.00 95.19  ? 94  GLU A O   1 
ATOM   734  C CB  . GLU A 1 94  ? 23.099 38.469 24.620  1.00 97.56  ? 94  GLU A CB  1 
ATOM   735  C CG  . GLU A 1 94  ? 22.505 39.868 24.460  0.80 100.56 ? 94  GLU A CG  1 
ATOM   736  C CD  . GLU A 1 94  ? 21.555 40.243 25.582  0.70 102.00 ? 94  GLU A CD  1 
ATOM   737  O OE1 . GLU A 1 94  ? 22.020 40.352 26.734  0.70 105.13 ? 94  GLU A OE1 1 
ATOM   738  O OE2 . GLU A 1 94  ? 20.347 40.427 25.318  0.70 100.73 ? 94  GLU A OE2 1 
ATOM   739  N N   . TYR A 1 95  ? 22.804 35.079 23.218  1.00 88.60  ? 95  TYR A N   1 
ATOM   740  C CA  . TYR A 1 95  ? 23.495 33.944 22.621  1.00 83.62  ? 95  TYR A CA  1 
ATOM   741  C C   . TYR A 1 95  ? 23.918 34.251 21.192  1.00 78.47  ? 95  TYR A C   1 
ATOM   742  O O   . TYR A 1 95  ? 23.569 35.298 20.637  1.00 81.92  ? 95  TYR A O   1 
ATOM   743  C CB  . TYR A 1 95  ? 22.576 32.720 22.628  1.00 81.28  ? 95  TYR A CB  1 
ATOM   744  C CG  . TYR A 1 95  ? 21.173 33.083 22.194  1.00 80.28  ? 95  TYR A CG  1 
ATOM   745  C CD1 . TYR A 1 95  ? 20.824 33.113 20.850  1.00 76.64  ? 95  TYR A CD1 1 
ATOM   746  C CD2 . TYR A 1 95  ? 20.208 33.439 23.130  1.00 84.83  ? 95  TYR A CD2 1 
ATOM   747  C CE1 . TYR A 1 95  ? 19.550 33.468 20.451  1.00 77.20  ? 95  TYR A CE1 1 
ATOM   748  C CE2 . TYR A 1 95  ? 18.934 33.794 22.743  1.00 85.64  ? 95  TYR A CE2 1 
ATOM   749  C CZ  . TYR A 1 95  ? 18.610 33.806 21.403  1.00 82.69  ? 95  TYR A CZ  1 
ATOM   750  O OH  . TYR A 1 95  ? 17.337 34.160 21.023  1.00 84.92  ? 95  TYR A OH  1 
ATOM   751  N N   . GLN A 1 96  ? 24.650 33.333 20.579  1.00 70.23  ? 96  GLN A N   1 
ATOM   752  C CA  . GLN A 1 96  ? 24.954 33.408 19.163  1.00 64.99  ? 96  GLN A CA  1 
ATOM   753  C C   . GLN A 1 96  ? 24.097 32.399 18.411  1.00 62.23  ? 96  GLN A C   1 
ATOM   754  O O   . GLN A 1 96  ? 23.707 31.360 18.954  1.00 64.39  ? 96  GLN A O   1 
ATOM   755  C CB  . GLN A 1 96  ? 26.439 33.145 18.899  1.00 62.22  ? 96  GLN A CB  1 
ATOM   756  C CG  . GLN A 1 96  ? 27.339 34.323 19.225  1.00 65.82  ? 96  GLN A CG  1 
ATOM   757  C CD  . GLN A 1 96  ? 28.806 33.953 19.198  0.50 63.23  ? 96  GLN A CD  1 
ATOM   758  O OE1 . GLN A 1 96  ? 29.159 32.778 19.096  0.50 59.67  ? 96  GLN A OE1 1 
ATOM   759  N NE2 . GLN A 1 96  ? 29.671 34.956 19.293  0.50 64.55  ? 96  GLN A NE2 1 
ATOM   760  N N   . LYS A 1 97  ? 23.794 32.723 17.161  1.00 56.69  ? 97  LYS A N   1 
ATOM   761  C CA  . LYS A 1 97  ? 23.048 31.832 16.291  1.00 51.39  ? 97  LYS A CA  1 
ATOM   762  C C   . LYS A 1 97  ? 23.987 31.243 15.250  1.00 47.78  ? 97  LYS A C   1 
ATOM   763  O O   . LYS A 1 97  ? 24.910 31.917 14.788  1.00 50.19  ? 97  LYS A O   1 
ATOM   764  C CB  . LYS A 1 97  ? 21.887 32.565 15.614  1.00 51.88  ? 97  LYS A CB  1 
ATOM   765  C CG  . LYS A 1 97  ? 20.797 32.988 16.592  0.80 55.70  ? 97  LYS A CG  1 
ATOM   766  C CD  . LYS A 1 97  ? 19.688 33.753 15.899  0.70 55.62  ? 97  LYS A CD  1 
ATOM   767  C CE  . LYS A 1 97  ? 19.676 35.205 16.332  0.60 56.29  ? 97  LYS A CE  1 
ATOM   768  N NZ  . LYS A 1 97  ? 18.594 35.963 15.650  0.50 56.63  ? 97  LYS A NZ  1 
ATOM   769  N N   . VAL A 1 98  ? 23.772 29.970 14.920  1.00 42.95  ? 98  VAL A N   1 
ATOM   770  C CA  . VAL A 1 98  ? 24.444 29.333 13.796  1.00 43.74  ? 98  VAL A CA  1 
ATOM   771  C C   . VAL A 1 98  ? 23.376 28.827 12.834  1.00 36.90  ? 98  VAL A C   1 
ATOM   772  O O   . VAL A 1 98  ? 22.271 28.450 13.235  1.00 35.32  ? 98  VAL A O   1 
ATOM   773  C CB  . VAL A 1 98  ? 25.384 28.185 14.232  1.00 45.09  ? 98  VAL A CB  1 
ATOM   774  C CG1 . VAL A 1 98  ? 26.327 28.663 15.311  1.00 46.97  ? 98  VAL A CG1 1 
ATOM   775  C CG2 . VAL A 1 98  ? 24.590 26.986 14.703  1.00 48.63  ? 98  VAL A CG2 1 
ATOM   776  N N   . SER A 1 99  ? 23.709 28.834 11.553  1.00 35.33  ? 99  SER A N   1 
ATOM   777  C CA  . SER A 1 99  ? 22.776 28.442 10.506  1.00 36.62  ? 99  SER A CA  1 
ATOM   778  C C   . SER A 1 99  ? 23.320 27.239 9.749   1.00 33.80  ? 99  SER A C   1 
ATOM   779  O O   . SER A 1 99  ? 24.500 27.204 9.398   1.00 33.77  ? 99  SER A O   1 
ATOM   780  C CB  . SER A 1 99  ? 22.526 29.606 9.537   1.00 42.26  ? 99  SER A CB  1 
ATOM   781  O OG  . SER A 1 99  ? 22.035 30.728 10.245  1.00 49.37  ? 99  SER A OG  1 
ATOM   782  N N   . TYR A 1 100 ? 22.453 26.243 9.517   1.00 33.06  ? 100 TYR A N   1 
ATOM   783  C CA  . TYR A 1 100 ? 22.745 25.091 8.675   1.00 28.33  ? 100 TYR A CA  1 
ATOM   784  C C   . TYR A 1 100 ? 21.933 25.174 7.380   1.00 28.17  ? 100 TYR A C   1 
ATOM   785  O O   . TYR A 1 100 ? 20.801 25.666 7.384   1.00 25.15  ? 100 TYR A O   1 
ATOM   786  C CB  . TYR A 1 100 ? 22.412 23.761 9.363   1.00 27.20  ? 100 TYR A CB  1 
ATOM   787  C CG  . TYR A 1 100 ? 23.354 23.339 10.484  1.00 31.88  ? 100 TYR A CG  1 
ATOM   788  C CD1 . TYR A 1 100 ? 24.463 24.103 10.823  1.00 35.95  ? 100 TYR A CD1 1 
ATOM   789  C CD2 . TYR A 1 100 ? 23.136 22.157 11.181  1.00 32.64  ? 100 TYR A CD2 1 
ATOM   790  C CE1 . TYR A 1 100 ? 25.323 23.708 11.850  1.00 35.76  ? 100 TYR A CE1 1 
ATOM   791  C CE2 . TYR A 1 100 ? 23.982 21.756 12.204  1.00 32.75  ? 100 TYR A CE2 1 
ATOM   792  C CZ  . TYR A 1 100 ? 25.075 22.529 12.529  1.00 36.20  ? 100 TYR A CZ  1 
ATOM   793  O OH  . TYR A 1 100 ? 25.925 22.129 13.544  1.00 44.61  ? 100 TYR A OH  1 
ATOM   794  N N   . PRO A 1 101 ? 22.471 24.692 6.264   1.00 28.85  ? 101 PRO A N   1 
ATOM   795  C CA  . PRO A 1 101 ? 21.731 24.758 5.002   1.00 26.84  ? 101 PRO A CA  1 
ATOM   796  C C   . PRO A 1 101 ? 20.621 23.718 4.957   1.00 26.77  ? 101 PRO A C   1 
ATOM   797  O O   . PRO A 1 101 ? 20.640 22.710 5.668   1.00 26.34  ? 101 PRO A O   1 
ATOM   798  C CB  . PRO A 1 101 ? 22.798 24.472 3.931   1.00 27.90  ? 101 PRO A CB  1 
ATOM   799  C CG  . PRO A 1 101 ? 24.154 24.531 4.672   1.00 26.39  ? 101 PRO A CG  1 
ATOM   800  C CD  . PRO A 1 101 ? 23.833 24.156 6.088   1.00 27.33  ? 101 PRO A CD  1 
ATOM   801  N N   . LEU A 1 102 ? 19.661 23.965 4.059   1.00 25.41  ? 102 LEU A N   1 
ATOM   802  C CA  . LEU A 1 102 ? 18.506 23.099 3.884   1.00 25.41  ? 102 LEU A CA  1 
ATOM   803  C C   . LEU A 1 102 ? 18.384 22.700 2.416   1.00 24.11  ? 102 LEU A C   1 
ATOM   804  O O   . LEU A 1 102 ? 18.987 23.308 1.531   1.00 24.44  ? 102 LEU A O   1 
ATOM   805  C CB  . LEU A 1 102 ? 17.218 23.787 4.357   1.00 23.15  ? 102 LEU A CB  1 
ATOM   806  C CG  . LEU A 1 102 ? 17.233 24.240 5.835   1.00 22.42  ? 102 LEU A CG  1 
ATOM   807  C CD1 . LEU A 1 102 ? 16.053 25.123 6.112   1.00 24.74  ? 102 LEU A CD1 1 
ATOM   808  C CD2 . LEU A 1 102 ? 17.254 23.044 6.764   1.00 25.79  ? 102 LEU A CD2 1 
ATOM   809  N N   . LEU A 1 103 ? 17.603 21.655 2.172   1.00 24.51  ? 103 LEU A N   1 
ATOM   810  C CA  . LEU A 1 103 ? 17.397 21.117 0.832   1.00 23.78  ? 103 LEU A CA  1 
ATOM   811  C C   . LEU A 1 103 ? 15.981 21.425 0.374   1.00 26.77  ? 103 LEU A C   1 
ATOM   812  O O   . LEU A 1 103 ? 15.022 21.181 1.109   1.00 25.66  ? 103 LEU A O   1 
ATOM   813  C CB  . LEU A 1 103 ? 17.626 19.607 0.827   1.00 24.43  ? 103 LEU A CB  1 
ATOM   814  C CG  . LEU A 1 103 ? 17.204 18.892 -0.460  1.00 25.26  ? 103 LEU A CG  1 
ATOM   815  C CD1 . LEU A 1 103 ? 18.155 19.237 -1.588  1.00 22.96  ? 103 LEU A CD1 1 
ATOM   816  C CD2 . LEU A 1 103 ? 17.187 17.403 -0.190  1.00 25.32  ? 103 LEU A CD2 1 
ATOM   817  N N   . LYS A 1 104 ? 15.841 21.955 -0.839  1.00 26.85  ? 104 LYS A N   1 
ATOM   818  C CA  . LYS A 1 104 ? 14.527 22.216 -1.406  1.00 24.26  ? 104 LYS A CA  1 
ATOM   819  C C   . LYS A 1 104 ? 14.206 21.136 -2.432  1.00 29.89  ? 104 LYS A C   1 
ATOM   820  O O   . LYS A 1 104 ? 15.036 20.825 -3.297  1.00 28.51  ? 104 LYS A O   1 
ATOM   821  C CB  . LYS A 1 104 ? 14.468 23.602 -2.045  1.00 26.53  ? 104 LYS A CB  1 
ATOM   822  C CG  . LYS A 1 104 ? 13.137 23.911 -2.751  1.00 31.99  ? 104 LYS A CG  1 
ATOM   823  C CD  . LYS A 1 104 ? 13.248 25.217 -3.514  1.00 37.21  ? 104 LYS A CD  1 
ATOM   824  C CE  . LYS A 1 104 ? 11.925 25.610 -4.134  1.00 42.66  ? 104 LYS A CE  1 
ATOM   825  N NZ  . LYS A 1 104 ? 12.112 26.778 -5.043  0.83 50.02  ? 104 LYS A NZ  1 
ATOM   826  N N   . THR A 1 105 ? 13.021 20.541 -2.310  1.00 32.59  ? 105 THR A N   1 
ATOM   827  C CA  . THR A 1 105 ? 12.545 19.526 -3.243  1.00 31.38  ? 105 THR A CA  1 
ATOM   828  C C   . THR A 1 105 ? 11.301 20.049 -3.936  1.00 31.25  ? 105 THR A C   1 
ATOM   829  O O   . THR A 1 105 ? 10.353 20.481 -3.272  1.00 33.89  ? 105 THR A O   1 
ATOM   830  C CB  . THR A 1 105 ? 12.215 18.209 -2.533  1.00 31.45  ? 105 THR A CB  1 
ATOM   831  O OG1 . THR A 1 105 ? 13.355 17.774 -1.791  1.00 31.45  ? 105 THR A OG1 1 
ATOM   832  C CG2 . THR A 1 105 ? 11.828 17.127 -3.547  1.00 31.42  ? 105 THR A CG2 1 
ATOM   833  N N   . THR A 1 106 ? 11.296 19.994 -5.262  1.00 29.45  ? 106 THR A N   1 
ATOM   834  C CA  . THR A 1 106 ? 10.141 20.391 -6.045  1.00 31.50  ? 106 THR A CA  1 
ATOM   835  C C   . THR A 1 106 ? 9.632  19.183 -6.811  1.00 35.29  ? 106 THR A C   1 
ATOM   836  O O   . THR A 1 106 ? 10.404 18.501 -7.490  1.00 35.29  ? 106 THR A O   1 
ATOM   837  C CB  . THR A 1 106 ? 10.484 21.532 -7.000  1.00 33.03  ? 106 THR A CB  1 
ATOM   838  O OG1 . THR A 1 106 ? 10.936 22.659 -6.239  1.00 35.81  ? 106 THR A OG1 1 
ATOM   839  C CG2 . THR A 1 106 ? 9.244  21.933 -7.790  1.00 32.55  ? 106 THR A CG2 1 
ATOM   840  N N   . VAL A 1 107 ? 8.339  18.911 -6.684  1.00 36.01  ? 107 VAL A N   1 
ATOM   841  C CA  . VAL A 1 107 ? 7.701  17.791 -7.360  1.00 34.15  ? 107 VAL A CA  1 
ATOM   842  C C   . VAL A 1 107 ? 6.674  18.371 -8.312  1.00 37.74  ? 107 VAL A C   1 
ATOM   843  O O   . VAL A 1 107 ? 5.717  19.022 -7.874  1.00 37.95  ? 107 VAL A O   1 
ATOM   844  C CB  . VAL A 1 107 ? 7.051  16.813 -6.366  1.00 33.96  ? 107 VAL A CB  1 
ATOM   845  C CG1 . VAL A 1 107 ? 6.432  15.627 -7.098  1.00 33.35  ? 107 VAL A CG1 1 
ATOM   846  C CG2 . VAL A 1 107 ? 8.084  16.336 -5.308  1.00 31.58  ? 107 VAL A CG2 1 
ATOM   847  N N   . LYS A 1 108 ? 6.872  18.140 -9.607  1.00 37.75  ? 108 LYS A N   1 
ATOM   848  C CA  . LYS A 1 108 ? 5.952  18.595 -10.638 1.00 41.02  ? 108 LYS A CA  1 
ATOM   849  C C   . LYS A 1 108 ? 5.155  17.417 -11.178 1.00 46.08  ? 108 LYS A C   1 
ATOM   850  O O   . LYS A 1 108 ? 5.684  16.306 -11.317 1.00 43.69  ? 108 LYS A O   1 
ATOM   851  C CB  . LYS A 1 108 ? 6.704  19.287 -11.775 0.80 44.52  ? 108 LYS A CB  1 
ATOM   852  C CG  . LYS A 1 108 ? 7.524  20.478 -11.314 0.60 45.45  ? 108 LYS A CG  1 
ATOM   853  C CD  . LYS A 1 108 ? 8.149  21.204 -12.488 0.60 50.23  ? 108 LYS A CD  1 
ATOM   854  C CE  . LYS A 1 108 ? 8.812  22.490 -12.044 0.50 50.57  ? 108 LYS A CE  1 
ATOM   855  N NZ  . LYS A 1 108 ? 9.219  23.343 -13.192 0.50 51.72  ? 108 LYS A NZ  1 
ATOM   856  N N   . TYR A 1 109 ? 3.891  17.678 -11.501 0.80 44.10  ? 109 TYR A N   1 
ATOM   857  C CA  . TYR A 1 109 ? 2.938  16.665 -11.919 0.80 57.60  ? 109 TYR A CA  1 
ATOM   858  C C   . TYR A 1 109 ? 2.488  16.912 -13.346 0.80 64.94  ? 109 TYR A C   1 
ATOM   859  O O   . TYR A 1 109 ? 2.621  18.014 -13.885 0.80 66.61  ? 109 TYR A O   1 
ATOM   860  C CB  . TYR A 1 109 ? 1.706  16.656 -11.012 0.80 52.82  ? 109 TYR A CB  1 
ATOM   861  C CG  . TYR A 1 109 ? 2.065  16.496 -9.557  0.80 47.80  ? 109 TYR A CG  1 
ATOM   862  C CD1 . TYR A 1 109 ? 2.170  15.239 -8.991  0.80 43.48  ? 109 TYR A CD1 1 
ATOM   863  C CD2 . TYR A 1 109 ? 2.312  17.603 -8.755  0.80 45.01  ? 109 TYR A CD2 1 
ATOM   864  C CE1 . TYR A 1 109 ? 2.496  15.085 -7.678  0.80 46.54  ? 109 TYR A CE1 1 
ATOM   865  C CE2 . TYR A 1 109 ? 2.643  17.459 -7.432  0.80 40.49  ? 109 TYR A CE2 1 
ATOM   866  C CZ  . TYR A 1 109 ? 2.736  16.193 -6.897  0.80 47.00  ? 109 TYR A CZ  1 
ATOM   867  O OH  . TYR A 1 109 ? 3.077  16.019 -5.572  0.80 43.46  ? 109 TYR A OH  1 
ATOM   868  N N   . GLY A 1 110 ? 1.945  15.863 -13.954 1.00 70.09  ? 110 GLY A N   1 
ATOM   869  C CA  . GLY A 1 110 ? 1.200  16.046 -15.181 1.00 76.28  ? 110 GLY A CA  1 
ATOM   870  C C   . GLY A 1 110 ? -0.066 16.845 -14.951 1.00 81.53  ? 110 GLY A C   1 
ATOM   871  O O   . GLY A 1 110 ? -0.523 17.026 -13.819 1.00 78.64  ? 110 GLY A O   1 
ATOM   872  N N   . ILE A 1 111 ? -0.630 17.332 -16.060 1.00 88.70  ? 111 ILE A N   1 
ATOM   873  C CA  . ILE A 1 111 ? -1.852 18.144 -16.085 1.00 90.07  ? 111 ILE A CA  1 
ATOM   874  C C   . ILE A 1 111 ? -1.624 19.496 -15.400 1.00 83.60  ? 111 ILE A C   1 
ATOM   875  O O   . ILE A 1 111 ? -2.117 19.759 -14.301 1.00 80.74  ? 111 ILE A O   1 
ATOM   876  C CB  . ILE A 1 111 ? -3.044 17.379 -15.462 1.00 95.82  ? 111 ILE A CB  1 
ATOM   877  C CG1 . ILE A 1 111 ? -3.202 16.012 -16.132 1.00 99.01  ? 111 ILE A CG1 1 
ATOM   878  C CG2 . ILE A 1 111 ? -4.339 18.166 -15.626 1.00 100.39 ? 111 ILE A CG2 1 
ATOM   879  C CD1 . ILE A 1 111 ? -4.305 15.160 -15.541 1.00 100.61 ? 111 ILE A CD1 1 
ATOM   880  N N   . GLU A 1 115 ? 2.734  21.950 -9.003  1.00 43.76  ? 115 GLU A N   1 
ATOM   881  C CA  . GLU A 1 115 ? 4.006  21.933 -8.277  1.00 41.11  ? 115 GLU A CA  1 
ATOM   882  C C   . GLU A 1 115 ? 3.796  21.818 -6.777  1.00 45.30  ? 115 GLU A C   1 
ATOM   883  O O   . GLU A 1 115 ? 2.984  22.534 -6.209  1.00 47.33  ? 115 GLU A O   1 
ATOM   884  C CB  . GLU A 1 115 ? 4.797  23.207 -8.550  0.80 44.10  ? 115 GLU A CB  1 
ATOM   885  C CG  . GLU A 1 115 ? 6.190  23.002 -9.026  0.70 43.19  ? 115 GLU A CG  1 
ATOM   886  C CD  . GLU A 1 115 ? 6.928  24.311 -9.210  0.60 45.23  ? 115 GLU A CD  1 
ATOM   887  O OE1 . GLU A 1 115 ? 7.043  25.076 -8.230  0.60 44.43  ? 115 GLU A OE1 1 
ATOM   888  O OE2 . GLU A 1 115 ? 7.374  24.582 -10.344 0.60 47.22  ? 115 GLU A OE2 1 
ATOM   889  N N   . ALA A 1 116 ? 4.550  20.938 -6.129  1.00 41.61  ? 116 ALA A N   1 
ATOM   890  C CA  . ALA A 1 116 ? 4.635  20.896 -4.678  1.00 40.80  ? 116 ALA A CA  1 
ATOM   891  C C   . ALA A 1 116 ? 6.092  21.053 -4.284  1.00 39.73  ? 116 ALA A C   1 
ATOM   892  O O   . ALA A 1 116 ? 6.968  20.435 -4.897  1.00 37.33  ? 116 ALA A O   1 
ATOM   893  C CB  . ALA A 1 116 ? 4.090  19.584 -4.117  1.00 43.37  ? 116 ALA A CB  1 
ATOM   894  N N   . THR A 1 117 ? 6.351  21.870 -3.261  1.00 38.15  ? 117 THR A N   1 
ATOM   895  C CA  . THR A 1 117 ? 7.695  22.049 -2.730  1.00 37.53  ? 117 THR A CA  1 
ATOM   896  C C   . THR A 1 117 ? 7.750  21.616 -1.271  1.00 35.92  ? 117 THR A C   1 
ATOM   897  O O   . THR A 1 117 ? 6.776  21.757 -0.522  1.00 32.88  ? 117 THR A O   1 
ATOM   898  C CB  . THR A 1 117 ? 8.170  23.506 -2.844  1.00 41.45  ? 117 THR A CB  1 
ATOM   899  O OG1 . THR A 1 117 ? 7.271  24.357 -2.123  1.00 46.06  ? 117 THR A OG1 1 
ATOM   900  C CG2 . THR A 1 117 ? 8.221  23.951 -4.311  1.00 40.42  ? 117 THR A CG2 1 
ATOM   901  N N   . TYR A 1 118 ? 8.911  21.096 -0.885  1.00 32.75  ? 118 TYR A N   1 
ATOM   902  C CA  . TYR A 1 118 ? 9.177  20.606 0.455   1.00 31.89  ? 118 TYR A CA  1 
ATOM   903  C C   . TYR A 1 118 ? 10.557 21.071 0.867   1.00 31.93  ? 118 TYR A C   1 
ATOM   904  O O   . TYR A 1 118 ? 11.459 21.188 0.036   1.00 32.33  ? 118 TYR A O   1 
ATOM   905  C CB  . TYR A 1 118 ? 9.128  19.072 0.531   1.00 25.69  ? 118 TYR A CB  1 
ATOM   906  C CG  . TYR A 1 118 ? 7.846  18.531 -0.004  0.80 27.90  ? 118 TYR A CG  1 
ATOM   907  C CD1 . TYR A 1 118 ? 6.741  18.383 0.821   0.80 31.92  ? 118 TYR A CD1 1 
ATOM   908  C CD2 . TYR A 1 118 ? 7.716  18.207 -1.356  0.80 28.98  ? 118 TYR A CD2 1 
ATOM   909  C CE1 . TYR A 1 118 ? 5.546  17.913 0.327   0.80 35.60  ? 118 TYR A CE1 1 
ATOM   910  C CE2 . TYR A 1 118 ? 6.515  17.732 -1.856  0.80 33.97  ? 118 TYR A CE2 1 
ATOM   911  C CZ  . TYR A 1 118 ? 5.437  17.588 -1.009  0.80 36.68  ? 118 TYR A CZ  1 
ATOM   912  O OH  . TYR A 1 118 ? 4.240  17.116 -1.500  0.80 42.59  ? 118 TYR A OH  1 
ATOM   913  N N   . LEU A 1 119 ? 10.720 21.295 2.162   1.00 27.22  ? 119 LEU A N   1 
ATOM   914  C CA  . LEU A 1 119 ? 12.007 21.629 2.756   1.00 27.93  ? 119 LEU A CA  1 
ATOM   915  C C   . LEU A 1 119 ? 12.478 20.471 3.631   1.00 27.11  ? 119 LEU A C   1 
ATOM   916  O O   . LEU A 1 119 ? 11.688 19.893 4.381   1.00 27.08  ? 119 LEU A O   1 
ATOM   917  C CB  . LEU A 1 119 ? 11.873 22.908 3.581   0.70 28.26  ? 119 LEU A CB  1 
ATOM   918  C CG  . LEU A 1 119 ? 13.009 23.911 3.731   0.60 29.84  ? 119 LEU A CG  1 
ATOM   919  C CD1 . LEU A 1 119 ? 13.564 24.297 2.390   0.60 26.88  ? 119 LEU A CD1 1 
ATOM   920  C CD2 . LEU A 1 119 ? 12.471 25.146 4.433   0.60 32.19  ? 119 LEU A CD2 1 
ATOM   921  N N   . ALA A 1 120 ? 13.754 20.113 3.529   1.00 25.82  ? 120 ALA A N   1 
ATOM   922  C CA  . ALA A 1 120 ? 14.291 19.000 4.304   1.00 24.82  ? 120 ALA A CA  1 
ATOM   923  C C   . ALA A 1 120 ? 15.476 19.450 5.153   1.00 26.18  ? 120 ALA A C   1 
ATOM   924  O O   . ALA A 1 120 ? 16.323 20.220 4.690   1.00 22.05  ? 120 ALA A O   1 
ATOM   925  C CB  . ALA A 1 120 ? 14.705 17.848 3.383   1.00 28.14  ? 120 ALA A CB  1 
ATOM   926  N N   . LEU A 1 121 ? 15.517 18.986 6.413   1.00 21.43  ? 121 LEU A N   1 
ATOM   927  C CA  . LEU A 1 121 ? 16.664 19.201 7.293   1.00 22.79  ? 121 LEU A CA  1 
ATOM   928  C C   . LEU A 1 121 ? 17.665 18.055 7.214   1.00 23.89  ? 121 LEU A C   1 
ATOM   929  O O   . LEU A 1 121 ? 18.875 18.274 7.366   1.00 24.73  ? 121 LEU A O   1 
ATOM   930  C CB  . LEU A 1 121 ? 16.186 19.372 8.748   1.00 20.63  ? 121 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 121 ? 17.217 19.428 9.890   1.00 22.91  ? 121 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 121 ? 18.258 20.484 9.596   1.00 20.67  ? 121 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 121 ? 16.526 19.671 11.285  1.00 21.01  ? 121 LEU A CD2 1 
ATOM   934  N N   . ASN A 1 122 ? 17.183 16.835 6.989   1.00 22.80  ? 122 ASN A N   1 
ATOM   935  C CA  . ASN A 1 122 ? 18.055 15.680 6.820   1.00 21.04  ? 122 ASN A CA  1 
ATOM   936  C C   . ASN A 1 122 ? 18.175 15.344 5.343   1.00 20.97  ? 122 ASN A C   1 
ATOM   937  O O   . ASN A 1 122 ? 19.254 15.482 4.763   1.00 22.13  ? 122 ASN A O   1 
ATOM   938  C CB  . ASN A 1 122 ? 17.518 14.463 7.562   1.00 19.94  ? 122 ASN A CB  1 
ATOM   939  C CG  . ASN A 1 122 ? 18.072 14.345 8.981   1.00 23.37  ? 122 ASN A CG  1 
ATOM   940  O OD1 . ASN A 1 122 ? 18.897 15.152 9.432   1.00 24.31  ? 122 ASN A OD1 1 
ATOM   941  N ND2 . ASN A 1 122 ? 17.635 13.322 9.674   1.00 20.89  ? 122 ASN A ND2 1 
ATOM   942  N N   . GLU A 1 123 ? 17.093 14.872 4.732   1.00 19.69  ? 123 GLU A N   1 
ATOM   943  C CA  . GLU A 1 123 ? 17.242 14.431 3.348   1.00 19.90  ? 123 GLU A CA  1 
ATOM   944  C C   . GLU A 1 123 ? 15.874 14.257 2.711   1.00 23.27  ? 123 GLU A C   1 
ATOM   945  O O   . GLU A 1 123 ? 14.840 14.212 3.385   1.00 21.95  ? 123 GLU A O   1 
ATOM   946  C CB  . GLU A 1 123 ? 18.027 13.117 3.236   1.00 20.97  ? 123 GLU A CB  1 
ATOM   947  C CG  . GLU A 1 123 ? 17.225 11.881 3.627   1.00 21.66  ? 123 GLU A CG  1 
ATOM   948  C CD  . GLU A 1 123 ? 17.062 11.793 5.140   1.00 25.65  ? 123 GLU A CD  1 
ATOM   949  O OE1 . GLU A 1 123 ? 15.908 11.793 5.630   1.00 24.48  ? 123 GLU A OE1 1 
ATOM   950  O OE2 . GLU A 1 123 ? 18.106 11.745 5.834   1.00 22.16  ? 123 GLU A OE2 1 
ATOM   951  N N   . SER A 1 124 ? 15.890 14.160 1.385   1.00 23.38  ? 124 SER A N   1 
ATOM   952  C CA  . SER A 1 124 ? 14.739 13.731 0.611   1.00 23.81  ? 124 SER A CA  1 
ATOM   953  C C   . SER A 1 124 ? 15.140 12.489 -0.174  1.00 22.15  ? 124 SER A C   1 
ATOM   954  O O   . SER A 1 124 ? 16.217 12.462 -0.773  1.00 23.60  ? 124 SER A O   1 
ATOM   955  C CB  . SER A 1 124 ? 14.284 14.840 -0.341  1.00 28.66  ? 124 SER A CB  1 
ATOM   956  O OG  . SER A 1 124 ? 13.178 14.412 -1.092  1.00 26.58  ? 124 SER A OG  1 
ATOM   957  N N   . THR A 1 125 ? 14.295 11.459 -0.168  1.00 21.97  ? 125 THR A N   1 
ATOM   958  C CA  . THR A 1 125 ? 14.610 10.264 -0.945  1.00 20.77  ? 125 THR A CA  1 
ATOM   959  C C   . THR A 1 125 ? 13.476 9.952  -1.901  1.00 23.44  ? 125 THR A C   1 
ATOM   960  O O   . THR A 1 125 ? 12.346 10.397 -1.723  1.00 23.61  ? 125 THR A O   1 
ATOM   961  C CB  . THR A 1 125 ? 14.877 9.032  -0.082  1.00 23.00  ? 125 THR A CB  1 
ATOM   962  O OG1 . THR A 1 125 ? 13.640 8.518  0.423   1.00 25.54  ? 125 THR A OG1 1 
ATOM   963  C CG2 . THR A 1 125 ? 15.828 9.386  1.087   1.00 21.92  ? 125 THR A CG2 1 
ATOM   964  N N   . VAL A 1 126 ? 13.806 9.180  -2.932  1.00 25.90  ? 126 VAL A N   1 
ATOM   965  C CA  . VAL A 1 126 ? 12.838 8.746  -3.933  1.00 26.49  ? 126 VAL A CA  1 
ATOM   966  C C   . VAL A 1 126 ? 13.006 7.253  -4.144  1.00 23.14  ? 126 VAL A C   1 
ATOM   967  O O   . VAL A 1 126 ? 14.129 6.780  -4.354  1.00 21.79  ? 126 VAL A O   1 
ATOM   968  C CB  . VAL A 1 126 ? 13.027 9.462  -5.279  1.00 25.87  ? 126 VAL A CB  1 
ATOM   969  C CG1 . VAL A 1 126 ? 11.763 9.275  -6.128  1.00 23.36  ? 126 VAL A CG1 1 
ATOM   970  C CG2 . VAL A 1 126 ? 13.338 10.911 -5.082  1.00 31.59  ? 126 VAL A CG2 1 
ATOM   971  N N   . LYS A 1 127 ? 11.897 6.526  -4.107  1.00 22.29  ? 127 LYS A N   1 
ATOM   972  C CA  . LYS A 1 127 ? 11.829 5.120  -4.475  1.00 27.15  ? 127 LYS A CA  1 
ATOM   973  C C   . LYS A 1 127 ? 10.614 4.923  -5.374  1.00 28.42  ? 127 LYS A C   1 
ATOM   974  O O   . LYS A 1 127 ? 9.781  5.824  -5.538  1.00 27.47  ? 127 LYS A O   1 
ATOM   975  C CB  . LYS A 1 127 ? 11.756 4.221  -3.230  1.00 32.19  ? 127 LYS A CB  1 
ATOM   976  C CG  . LYS A 1 127 ? 12.925 4.443  -2.242  1.00 34.65  ? 127 LYS A CG  1 
ATOM   977  C CD  . LYS A 1 127 ? 12.681 3.780  -0.874  0.60 34.43  ? 127 LYS A CD  1 
ATOM   978  C CE  . LYS A 1 127 ? 13.923 3.904  0.027   0.60 36.37  ? 127 LYS A CE  1 
ATOM   979  N NZ  . LYS A 1 127 ? 13.706 3.520  1.460   0.60 32.51  ? 127 LYS A NZ  1 
ATOM   980  N N   . SER A 1 128 ? 10.503 3.737  -5.972  1.00 29.44  ? 128 SER A N   1 
ATOM   981  C CA  . SER A 1 128 ? 9.335  3.517  -6.804  1.00 35.38  ? 128 SER A CA  1 
ATOM   982  C C   . SER A 1 128 ? 8.155  3.101  -5.938  1.00 41.12  ? 128 SER A C   1 
ATOM   983  O O   . SER A 1 128 ? 8.288  2.808  -4.747  1.00 40.30  ? 128 SER A O   1 
ATOM   984  C CB  . SER A 1 128 ? 9.588  2.452  -7.866  1.00 43.27  ? 128 SER A CB  1 
ATOM   985  O OG  . SER A 1 128 ? 9.528  1.159  -7.288  0.90 46.24  ? 128 SER A OG  1 
ATOM   986  N N   . SER A 1 129 ? 6.984  3.074  -6.557  1.00 44.95  ? 129 SER A N   1 
ATOM   987  C CA  . SER A 1 129 ? 5.767  2.632  -5.886  1.00 53.59  ? 129 SER A CA  1 
ATOM   988  C C   . SER A 1 129 ? 5.500  1.155  -6.152  1.00 59.10  ? 129 SER A C   1 
ATOM   989  O O   . SER A 1 129 ? 4.420  0.775  -6.582  1.00 64.76  ? 129 SER A O   1 
ATOM   990  C CB  . SER A 1 129 ? 4.601  3.488  -6.350  1.00 57.65  ? 129 SER A CB  1 
ATOM   991  O OG  . SER A 1 129 ? 4.557  3.493  -7.764  1.00 61.45  ? 129 SER A OG  1 
ATOM   992  N N   . GLY A 1 130 ? 6.498  0.309  -5.930  0.84 60.81  ? 130 GLY A N   1 
ATOM   993  C CA  . GLY A 1 130 ? 6.335  -1.107 -6.198  0.84 65.26  ? 130 GLY A CA  1 
ATOM   994  C C   . GLY A 1 130 ? 7.215  -1.642 -7.311  0.84 65.55  ? 130 GLY A C   1 
ATOM   995  O O   . GLY A 1 130 ? 8.083  -2.488 -7.067  0.84 67.05  ? 130 GLY A O   1 
ATOM   996  N N   . GLY A 1 131 ? 7.007  -1.157 -8.535  0.90 62.30  ? 131 GLY A N   1 
ATOM   997  C CA  . GLY A 1 131 ? 7.752  -1.623 -9.681  0.90 58.15  ? 131 GLY A CA  1 
ATOM   998  C C   . GLY A 1 131 ? 9.223  -1.250 -9.631  0.90 51.93  ? 131 GLY A C   1 
ATOM   999  O O   . GLY A 1 131 ? 9.733  -0.751 -8.620  0.90 47.28  ? 131 GLY A O   1 
ATOM   1000 N N   . PRO A 1 132 ? 9.942  -1.498 -10.727 0.89 46.43  ? 132 PRO A N   1 
ATOM   1001 C CA  . PRO A 1 132 ? 11.357 -1.110 -10.773 0.89 40.29  ? 132 PRO A CA  1 
ATOM   1002 C C   . PRO A 1 132 ? 11.503 0.405  -10.769 0.89 34.93  ? 132 PRO A C   1 
ATOM   1003 O O   . PRO A 1 132 ? 10.703 1.124  -11.371 0.89 34.69  ? 132 PRO A O   1 
ATOM   1004 C CB  . PRO A 1 132 ? 11.857 -1.713 -12.094 0.89 40.25  ? 132 PRO A CB  1 
ATOM   1005 C CG  . PRO A 1 132 ? 10.812 -2.691 -12.515 0.89 44.80  ? 132 PRO A CG  1 
ATOM   1006 C CD  . PRO A 1 132 ? 9.517  -2.182 -11.957 0.89 49.79  ? 132 PRO A CD  1 
ATOM   1007 N N   . PHE A 1 133 ? 12.540 0.885  -10.086 1.00 30.20  ? 133 PHE A N   1 
ATOM   1008 C CA  . PHE A 1 133 ? 12.850 2.310  -10.035 1.00 32.12  ? 133 PHE A CA  1 
ATOM   1009 C C   . PHE A 1 133 ? 13.843 2.655  -11.137 1.00 31.20  ? 133 PHE A C   1 
ATOM   1010 O O   . PHE A 1 133 ? 14.970 2.159  -11.127 1.00 27.49  ? 133 PHE A O   1 
ATOM   1011 C CB  . PHE A 1 133 ? 13.439 2.687  -8.679  1.00 26.62  ? 133 PHE A CB  1 
ATOM   1012 C CG  . PHE A 1 133 ? 13.757 4.152  -8.535  1.00 25.81  ? 133 PHE A CG  1 
ATOM   1013 C CD1 . PHE A 1 133 ? 12.745 5.093  -8.475  1.00 27.28  ? 133 PHE A CD1 1 
ATOM   1014 C CD2 . PHE A 1 133 ? 15.075 4.584  -8.453  1.00 26.93  ? 133 PHE A CD2 1 
ATOM   1015 C CE1 . PHE A 1 133 ? 13.036 6.433  -8.332  1.00 28.18  ? 133 PHE A CE1 1 
ATOM   1016 C CE2 . PHE A 1 133 ? 15.377 5.928  -8.309  1.00 27.38  ? 133 PHE A CE2 1 
ATOM   1017 C CZ  . PHE A 1 133 ? 14.358 6.854  -8.245  1.00 25.59  ? 133 PHE A CZ  1 
ATOM   1018 N N   . VAL A 1 134 ? 13.427 3.508  -12.076 1.00 29.81  ? 134 VAL A N   1 
ATOM   1019 C CA  . VAL A 1 134 ? 14.273 3.965  -13.177 1.00 29.74  ? 134 VAL A CA  1 
ATOM   1020 C C   . VAL A 1 134 ? 14.010 5.449  -13.383 1.00 30.58  ? 134 VAL A C   1 
ATOM   1021 O O   . VAL A 1 134 ? 12.883 5.834  -13.718 1.00 31.52  ? 134 VAL A O   1 
ATOM   1022 C CB  . VAL A 1 134 ? 13.998 3.222  -14.499 1.00 34.05  ? 134 VAL A CB  1 
ATOM   1023 C CG1 . VAL A 1 134 ? 15.077 3.563  -15.518 1.00 34.66  ? 134 VAL A CG1 1 
ATOM   1024 C CG2 . VAL A 1 134 ? 13.869 1.724  -14.298 1.00 37.74  ? 134 VAL A CG2 1 
ATOM   1025 N N   . VAL A 1 135 ? 15.040 6.279  -13.218 1.00 25.66  ? 135 VAL A N   1 
ATOM   1026 C CA  . VAL A 1 135 ? 14.932 7.699  -13.535 1.00 27.03  ? 135 VAL A CA  1 
ATOM   1027 C C   . VAL A 1 135 ? 16.158 8.135  -14.319 1.00 27.73  ? 135 VAL A C   1 
ATOM   1028 O O   . VAL A 1 135 ? 17.257 7.595  -14.144 1.00 27.73  ? 135 VAL A O   1 
ATOM   1029 C CB  . VAL A 1 135 ? 14.789 8.585  -12.275 1.00 25.66  ? 135 VAL A CB  1 
ATOM   1030 C CG1 . VAL A 1 135 ? 13.481 8.316  -11.578 1.00 27.86  ? 135 VAL A CG1 1 
ATOM   1031 C CG2 . VAL A 1 135 ? 15.957 8.349  -11.347 1.00 24.19  ? 135 VAL A CG2 1 
ATOM   1032 N N   . ASP A 1 136 ? 15.967 9.139  -15.174 1.00 27.41  ? 136 ASP A N   1 
ATOM   1033 C CA  . ASP A 1 136 ? 17.083 9.867  -15.766 1.00 25.57  ? 136 ASP A CA  1 
ATOM   1034 C C   . ASP A 1 136 ? 17.510 10.978 -14.813 1.00 26.73  ? 136 ASP A C   1 
ATOM   1035 O O   . ASP A 1 136 ? 16.671 11.723 -14.298 1.00 28.25  ? 136 ASP A O   1 
ATOM   1036 C CB  . ASP A 1 136 ? 16.712 10.452 -17.135 1.00 27.49  ? 136 ASP A CB  1 
ATOM   1037 C CG  . ASP A 1 136 ? 16.726 9.405  -18.235 1.00 31.56  ? 136 ASP A CG  1 
ATOM   1038 O OD1 . ASP A 1 136 ? 15.870 9.471  -19.154 1.00 35.30  ? 136 ASP A OD1 1 
ATOM   1039 O OD2 . ASP A 1 136 ? 17.596 8.513  -18.183 1.00 31.61  ? 136 ASP A OD2 1 
ATOM   1040 N N   . VAL A 1 137 ? 18.811 11.075 -14.568 1.00 24.08  ? 137 VAL A N   1 
ATOM   1041 C CA  . VAL A 1 137 ? 19.375 12.067 -13.662 1.00 23.06  ? 137 VAL A CA  1 
ATOM   1042 C C   . VAL A 1 137 ? 19.942 13.196 -14.502 1.00 26.62  ? 137 VAL A C   1 
ATOM   1043 O O   . VAL A 1 137 ? 20.857 12.974 -15.305 1.00 25.81  ? 137 VAL A O   1 
ATOM   1044 C CB  . VAL A 1 137 ? 20.465 11.447 -12.781 1.00 21.22  ? 137 VAL A CB  1 
ATOM   1045 C CG1 . VAL A 1 137 ? 20.959 12.447 -11.750 1.00 21.19  ? 137 VAL A CG1 1 
ATOM   1046 C CG2 . VAL A 1 137 ? 19.924 10.207 -12.114 1.00 22.57  ? 137 VAL A CG2 1 
ATOM   1047 N N   . VAL A 1 138 ? 19.396 14.396 -14.336 1.00 23.56  ? 138 VAL A N   1 
ATOM   1048 C CA  . VAL A 1 138 ? 19.752 15.544 -15.170 1.00 28.23  ? 138 VAL A CA  1 
ATOM   1049 C C   . VAL A 1 138 ? 20.336 16.625 -14.265 1.00 32.27  ? 138 VAL A C   1 
ATOM   1050 O O   . VAL A 1 138 ? 19.679 17.077 -13.317 1.00 29.97  ? 138 VAL A O   1 
ATOM   1051 C CB  . VAL A 1 138 ? 18.541 16.069 -15.953 1.00 27.50  ? 138 VAL A CB  1 
ATOM   1052 C CG1 . VAL A 1 138 ? 18.906 17.287 -16.768 1.00 30.72  ? 138 VAL A CG1 1 
ATOM   1053 C CG2 . VAL A 1 138 ? 17.962 14.967 -16.851 1.00 25.89  ? 138 VAL A CG2 1 
ATOM   1054 N N   . ILE A 1 139 ? 21.569 17.033 -14.549 1.00 27.34  ? 139 ILE A N   1 
ATOM   1055 C CA  . ILE A 1 139 ? 22.281 18.000 -13.717 1.00 23.23  ? 139 ILE A CA  1 
ATOM   1056 C C   . ILE A 1 139 ? 22.450 19.270 -14.528 1.00 26.01  ? 139 ILE A C   1 
ATOM   1057 O O   . ILE A 1 139 ? 23.136 19.263 -15.561 1.00 26.50  ? 139 ILE A O   1 
ATOM   1058 C CB  . ILE A 1 139 ? 23.643 17.472 -13.248 1.00 24.39  ? 139 ILE A CB  1 
ATOM   1059 C CG1 . ILE A 1 139 ? 23.488 16.155 -12.477 1.00 23.97  ? 139 ILE A CG1 1 
ATOM   1060 C CG2 . ILE A 1 139 ? 24.313 18.511 -12.349 1.00 26.82  ? 139 ILE A CG2 1 
ATOM   1061 C CD1 . ILE A 1 139 ? 24.833 15.489 -12.113 1.00 21.42  ? 139 ILE A CD1 1 
ATOM   1062 N N   . ASN A 1 140 ? 21.816 20.354 -14.078 1.00 22.04  ? 140 ASN A N   1 
ATOM   1063 C CA  . ASN A 1 140 ? 21.855 21.627 -14.791 1.00 25.10  ? 140 ASN A CA  1 
ATOM   1064 C C   . ASN A 1 140 ? 21.562 21.422 -16.271 1.00 29.32  ? 140 ASN A C   1 
ATOM   1065 O O   . ASN A 1 140 ? 22.288 21.902 -17.144 1.00 27.72  ? 140 ASN A O   1 
ATOM   1066 C CB  . ASN A 1 140 ? 23.203 22.313 -14.586 1.00 26.14  ? 140 ASN A CB  1 
ATOM   1067 C CG  . ASN A 1 140 ? 23.517 22.501 -13.119 1.00 30.19  ? 140 ASN A CG  1 
ATOM   1068 O OD1 . ASN A 1 140 ? 22.626 22.835 -12.337 1.00 29.66  ? 140 ASN A OD1 1 
ATOM   1069 N ND2 . ASN A 1 140 ? 24.770 22.269 -12.731 1.00 30.91  ? 140 ASN A ND2 1 
ATOM   1070 N N   . ASP A 1 141 ? 20.496 20.672 -16.545 1.00 31.45  ? 141 ASP A N   1 
ATOM   1071 C CA  . ASP A 1 141 ? 19.980 20.393 -17.893 1.00 34.22  ? 141 ASP A CA  1 
ATOM   1072 C C   . ASP A 1 141 ? 20.867 19.450 -18.704 1.00 34.06  ? 141 ASP A C   1 
ATOM   1073 O O   . ASP A 1 141 ? 20.597 19.232 -19.891 1.00 40.51  ? 141 ASP A O   1 
ATOM   1074 C CB  . ASP A 1 141 ? 19.749 21.674 -18.700 0.80 36.45  ? 141 ASP A CB  1 
ATOM   1075 C CG  . ASP A 1 141 ? 18.905 22.697 -17.959 0.60 40.56  ? 141 ASP A CG  1 
ATOM   1076 O OD1 . ASP A 1 141 ? 17.996 22.314 -17.191 0.60 37.52  ? 141 ASP A OD1 1 
ATOM   1077 O OD2 . ASP A 1 141 ? 19.158 23.901 -18.160 0.60 43.32  ? 141 ASP A OD2 1 
ATOM   1078 N N   . ILE A 1 142 ? 21.897 18.866 -18.106 1.00 32.12  ? 142 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 142 ? 22.783 17.929 -18.786 1.00 36.31  ? 142 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 142 ? 22.408 16.519 -18.356 1.00 28.62  ? 142 ILE A C   1 
ATOM   1081 O O   . ILE A 1 142 ? 22.357 16.227 -17.155 1.00 27.54  ? 142 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 142 ? 24.255 18.241 -18.464 1.00 44.93  ? 142 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 142 ? 24.764 19.359 -19.380 0.76 52.17  ? 142 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 142 ? 25.120 16.989 -18.569 0.76 46.69  ? 142 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 142 ? 26.185 19.763 -19.108 0.77 57.29  ? 142 ILE A CD1 1 
ATOM   1086 N N   . HIS A 1 143 ? 22.126 15.641 -19.323 1.00 26.84  ? 143 HIS A N   1 
ATOM   1087 C CA  . HIS A 1 143 ? 21.755 14.278 -18.953 1.00 27.61  ? 143 HIS A CA  1 
ATOM   1088 C C   . HIS A 1 143 ? 22.970 13.541 -18.435 1.00 28.69  ? 143 HIS A C   1 
ATOM   1089 O O   . HIS A 1 143 ? 23.916 13.282 -19.181 1.00 26.92  ? 143 HIS A O   1 
ATOM   1090 C CB  A HIS A 1 143 ? 21.155 13.476 -20.111 0.56 29.69  ? 143 HIS A CB  1 
ATOM   1091 C CB  B HIS A 1 143 ? 21.139 13.565 -20.156 0.44 29.61  ? 143 HIS A CB  1 
ATOM   1092 C CG  A HIS A 1 143 ? 20.942 12.032 -19.750 0.56 32.92  ? 143 HIS A CG  1 
ATOM   1093 C CG  B HIS A 1 143 ? 19.742 14.008 -20.449 0.44 27.64  ? 143 HIS A CG  1 
ATOM   1094 N ND1 A HIS A 1 143 ? 21.933 11.078 -19.867 0.56 32.68  ? 143 HIS A ND1 1 
ATOM   1095 N ND1 B HIS A 1 143 ? 18.677 13.133 -20.513 0.44 31.10  ? 143 HIS A ND1 1 
ATOM   1096 C CD2 A HIS A 1 143 ? 19.888 11.404 -19.171 0.56 34.13  ? 143 HIS A CD2 1 
ATOM   1097 C CD2 B HIS A 1 143 ? 19.226 15.242 -20.652 0.44 27.57  ? 143 HIS A CD2 1 
ATOM   1098 C CE1 A HIS A 1 143 ? 21.480 9.916  -19.428 0.56 32.49  ? 143 HIS A CE1 1 
ATOM   1099 C CE1 B HIS A 1 143 ? 17.571 13.809 -20.771 0.44 30.43  ? 143 HIS A CE1 1 
ATOM   1100 N NE2 A HIS A 1 143 ? 20.242 10.085 -18.999 0.56 31.68  ? 143 HIS A NE2 1 
ATOM   1101 N NE2 B HIS A 1 143 ? 17.876 15.090 -20.856 0.44 29.19  ? 143 HIS A NE2 1 
ATOM   1102 N N   . PHE A 1 144 ? 22.934 13.173 -17.162 1.00 21.92  ? 144 PHE A N   1 
ATOM   1103 C CA  . PHE A 1 144 ? 24.113 12.621 -16.522 1.00 24.38  ? 144 PHE A CA  1 
ATOM   1104 C C   . PHE A 1 144 ? 24.123 11.103 -16.491 1.00 25.33  ? 144 PHE A C   1 
ATOM   1105 O O   . PHE A 1 144 ? 25.152 10.495 -16.773 1.00 25.06  ? 144 PHE A O   1 
ATOM   1106 C CB  . PHE A 1 144 ? 24.223 13.167 -15.096 1.00 24.38  ? 144 PHE A CB  1 
ATOM   1107 C CG  . PHE A 1 144 ? 25.419 12.659 -14.355 1.00 23.07  ? 144 PHE A CG  1 
ATOM   1108 C CD1 . PHE A 1 144 ? 26.694 13.143 -14.652 1.00 19.71  ? 144 PHE A CD1 1 
ATOM   1109 C CD2 . PHE A 1 144 ? 25.276 11.692 -13.378 1.00 21.37  ? 144 PHE A CD2 1 
ATOM   1110 C CE1 . PHE A 1 144 ? 27.822 12.667 -13.977 1.00 22.87  ? 144 PHE A CE1 1 
ATOM   1111 C CE2 . PHE A 1 144 ? 26.387 11.205 -12.672 1.00 21.47  ? 144 PHE A CE2 1 
ATOM   1112 C CZ  . PHE A 1 144 ? 27.668 11.691 -12.972 1.00 23.17  ? 144 PHE A CZ  1 
ATOM   1113 N N   . GLU A 1 145 ? 23.009 10.469 -16.146 1.00 21.81  ? 145 GLU A N   1 
ATOM   1114 C CA  . GLU A 1 145 ? 22.987 9.018  -16.054 1.00 23.61  ? 145 GLU A CA  1 
ATOM   1115 C C   . GLU A 1 145 ? 21.536 8.587  -16.039 1.00 23.27  ? 145 GLU A C   1 
ATOM   1116 O O   . GLU A 1 145 ? 20.643 9.378  -15.734 1.00 25.05  ? 145 GLU A O   1 
ATOM   1117 C CB  . GLU A 1 145 ? 23.715 8.512  -14.792 1.00 20.67  ? 145 GLU A CB  1 
ATOM   1118 C CG  . GLU A 1 145 ? 22.918 8.785  -13.522 1.00 21.18  ? 145 GLU A CG  1 
ATOM   1119 C CD  . GLU A 1 145 ? 23.646 8.382  -12.246 1.00 26.51  ? 145 GLU A CD  1 
ATOM   1120 O OE1 . GLU A 1 145 ? 23.071 8.617  -11.166 1.00 22.29  ? 145 GLU A OE1 1 
ATOM   1121 O OE2 . GLU A 1 145 ? 24.776 7.851  -12.318 1.00 26.03  ? 145 GLU A OE2 1 
ATOM   1122 N N   . ARG A 1 146 ? 21.306 7.322  -16.378 1.00 22.31  ? 146 ARG A N   1 
ATOM   1123 C CA  . ARG A 1 146 ? 20.011 6.687  -16.153 1.00 24.20  ? 146 ARG A CA  1 
ATOM   1124 C C   . ARG A 1 146 ? 20.186 5.769  -14.954 1.00 24.00  ? 146 ARG A C   1 
ATOM   1125 O O   . ARG A 1 146 ? 20.961 4.809  -15.012 1.00 27.18  ? 146 ARG A O   1 
ATOM   1126 C CB  . ARG A 1 146 ? 19.534 5.911  -17.381 1.00 28.14  ? 146 ARG A CB  1 
ATOM   1127 C CG  . ARG A 1 146 ? 18.213 5.175  -17.134 1.00 26.65  ? 146 ARG A CG  1 
ATOM   1128 C CD  . ARG A 1 146 ? 17.563 4.761  -18.450 0.80 27.18  ? 146 ARG A CD  1 
ATOM   1129 N NE  . ARG A 1 146 ? 16.983 5.903  -19.143 0.70 25.44  ? 146 ARG A NE  1 
ATOM   1130 C CZ  . ARG A 1 146 ? 16.284 5.800  -20.269 0.70 28.49  ? 146 ARG A CZ  1 
ATOM   1131 N NH1 . ARG A 1 146 ? 16.098 4.608  -20.818 0.70 27.58  ? 146 ARG A NH1 1 
ATOM   1132 N NH2 . ARG A 1 146 ? 15.776 6.880  -20.848 0.70 26.97  ? 146 ARG A NH2 1 
ATOM   1133 N N   . PHE A 1 147 ? 19.507 6.088  -13.860 1.00 22.92  ? 147 PHE A N   1 
ATOM   1134 C CA  . PHE A 1 147 ? 19.671 5.333  -12.621 1.00 22.76  ? 147 PHE A CA  1 
ATOM   1135 C C   . PHE A 1 147 ? 18.638 4.212  -12.532 1.00 26.12  ? 147 PHE A C   1 
ATOM   1136 O O   . PHE A 1 147 ? 17.435 4.458  -12.633 1.00 27.23  ? 147 PHE A O   1 
ATOM   1137 C CB  . PHE A 1 147 ? 19.545 6.242  -11.402 1.00 23.23  ? 147 PHE A CB  1 
ATOM   1138 C CG  . PHE A 1 147 ? 19.737 5.497  -10.110 1.00 20.67  ? 147 PHE A CG  1 
ATOM   1139 C CD1 . PHE A 1 147 ? 18.663 4.899  -9.467  1.00 23.81  ? 147 PHE A CD1 1 
ATOM   1140 C CD2 . PHE A 1 147 ? 21.015 5.324  -9.587  1.00 22.45  ? 147 PHE A CD2 1 
ATOM   1141 C CE1 . PHE A 1 147 ? 18.851 4.170  -8.282  1.00 21.87  ? 147 PHE A CE1 1 
ATOM   1142 C CE2 . PHE A 1 147 ? 21.194 4.591  -8.403  1.00 21.03  ? 147 PHE A CE2 1 
ATOM   1143 C CZ  . PHE A 1 147 ? 20.117 4.020  -7.773  1.00 22.25  ? 147 PHE A CZ  1 
ATOM   1144 N N   . ARG A 1 148 ? 19.117 2.984  -12.339 1.00 25.02  ? 148 ARG A N   1 
ATOM   1145 C CA  . ARG A 1 148 ? 18.276 1.821  -12.090 1.00 24.81  ? 148 ARG A CA  1 
ATOM   1146 C C   . ARG A 1 148 ? 18.699 1.184  -10.782 1.00 21.54  ? 148 ARG A C   1 
ATOM   1147 O O   . ARG A 1 148 ? 19.882 0.906  -10.589 1.00 25.01  ? 148 ARG A O   1 
ATOM   1148 C CB  . ARG A 1 148 ? 18.401 0.778  -13.199 0.90 27.74  ? 148 ARG A CB  1 
ATOM   1149 C CG  . ARG A 1 148 ? 17.687 1.130  -14.439 0.80 35.75  ? 148 ARG A CG  1 
ATOM   1150 C CD  . ARG A 1 148 ? 17.714 -0.039 -15.395 0.70 39.09  ? 148 ARG A CD  1 
ATOM   1151 N NE  . ARG A 1 148 ? 17.176 0.345  -16.690 0.70 44.32  ? 148 ARG A NE  1 
ATOM   1152 C CZ  . ARG A 1 148 ? 17.800 1.159  -17.532 0.70 43.57  ? 148 ARG A CZ  1 
ATOM   1153 N NH1 . ARG A 1 148 ? 18.974 1.681  -17.201 0.70 39.61  ? 148 ARG A NH1 1 
ATOM   1154 N NH2 . ARG A 1 148 ? 17.250 1.452  -18.704 0.70 47.07  ? 148 ARG A NH2 1 
ATOM   1155 N N   . GLY A 1 149 ? 17.749 0.949  -9.889  1.00 23.59  ? 149 GLY A N   1 
ATOM   1156 C CA  . GLY A 1 149 ? 18.124 0.469  -8.562  1.00 22.54  ? 149 GLY A CA  1 
ATOM   1157 C C   . GLY A 1 149 ? 16.968 0.606  -7.592  1.00 24.50  ? 149 GLY A C   1 
ATOM   1158 O O   . GLY A 1 149 ? 15.807 0.602  -7.993  1.00 23.90  ? 149 GLY A O   1 
ATOM   1159 N N   . ASP A 1 150 ? 17.300 0.722  -6.308  1.00 18.29  ? 150 ASP A N   1 
ATOM   1160 C CA  . ASP A 1 150 ? 16.243 0.832  -5.311  1.00 24.65  ? 150 ASP A CA  1 
ATOM   1161 C C   . ASP A 1 150 ? 15.750 2.257  -5.145  1.00 25.58  ? 150 ASP A C   1 
ATOM   1162 O O   . ASP A 1 150 ? 14.572 2.452  -4.839  1.00 27.67  ? 150 ASP A O   1 
ATOM   1163 C CB  . ASP A 1 150 ? 16.710 0.315  -3.947  1.00 22.76  ? 150 ASP A CB  1 
ATOM   1164 C CG  . ASP A 1 150 ? 16.708 -1.183 -3.864  1.00 26.46  ? 150 ASP A CG  1 
ATOM   1165 O OD1 . ASP A 1 150 ? 16.326 -1.835 -4.853  1.00 28.98  ? 150 ASP A OD1 1 
ATOM   1166 O OD2 . ASP A 1 150 ? 17.102 -1.717 -2.807  1.00 26.13  ? 150 ASP A OD2 1 
ATOM   1167 N N   . GLY A 1 151 ? 16.611 3.246  -5.329  1.00 22.74  ? 151 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 151 ? 16.234 4.622  -5.070  1.00 22.94  ? 151 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 151 ? 17.448 5.512  -4.906  1.00 19.36  ? 151 GLY A C   1 
ATOM   1170 O O   . GLY A 1 151 ? 18.594 5.088  -5.071  1.00 22.34  ? 151 GLY A O   1 
ATOM   1171 N N   . LEU A 1 152 ? 17.166 6.778  -4.599  1.00 19.08  ? 152 LEU A N   1 
ATOM   1172 C CA  . LEU A 1 152 ? 18.186 7.815  -4.472  1.00 17.45  ? 152 LEU A CA  1 
ATOM   1173 C C   . LEU A 1 152 ? 17.915 8.661  -3.228  1.00 21.34  ? 152 LEU A C   1 
ATOM   1174 O O   . LEU A 1 152 ? 16.779 8.787  -2.773  1.00 21.41  ? 152 LEU A O   1 
ATOM   1175 C CB  . LEU A 1 152 ? 18.214 8.720  -5.715  1.00 19.74  ? 152 LEU A CB  1 
ATOM   1176 C CG  . LEU A 1 152 ? 18.765 8.114  -7.009  1.00 20.10  ? 152 LEU A CG  1 
ATOM   1177 C CD1 . LEU A 1 152 ? 18.279 8.929  -8.203  1.00 21.66  ? 152 LEU A CD1 1 
ATOM   1178 C CD2 . LEU A 1 152 ? 20.277 8.097  -6.974  1.00 16.48  ? 152 LEU A CD2 1 
ATOM   1179 N N   . CYS A 1 153 ? 18.970 9.272  -2.698  1.00 21.22  ? 153 CYS A N   1 
ATOM   1180 C CA  . CYS A 1 153 ? 18.896 10.035 -1.450  1.00 21.66  ? 153 CYS A CA  1 
ATOM   1181 C C   . CYS A 1 153 ? 19.663 11.334 -1.636  1.00 20.38  ? 153 CYS A C   1 
ATOM   1182 O O   . CYS A 1 153 ? 20.842 11.311 -2.012  1.00 18.65  ? 153 CYS A O   1 
ATOM   1183 C CB  . CYS A 1 153 ? 19.479 9.232  -0.281  1.00 17.82  ? 153 CYS A CB  1 
ATOM   1184 S SG  . CYS A 1 153 ? 19.606 10.168 1.286   1.00 19.93  ? 153 CYS A SG  1 
ATOM   1185 N N   . MET A 1 154 ? 18.997 12.460 -1.400  1.00 18.24  ? 154 MET A N   1 
ATOM   1186 C CA  . MET A 1 154 ? 19.634 13.770 -1.475  1.00 21.43  ? 154 MET A CA  1 
ATOM   1187 C C   . MET A 1 154 ? 19.666 14.361 -0.074  1.00 20.80  ? 154 MET A C   1 
ATOM   1188 O O   . MET A 1 154 ? 18.611 14.646 0.504   1.00 18.78  ? 154 MET A O   1 
ATOM   1189 C CB  . MET A 1 154 ? 18.900 14.714 -2.419  1.00 16.97  ? 154 MET A CB  1 
ATOM   1190 C CG  . MET A 1 154 ? 19.692 15.993 -2.688  1.00 19.47  ? 154 MET A CG  1 
ATOM   1191 S SD  . MET A 1 154 ? 21.242 15.693 -3.579  1.00 21.92  ? 154 MET A SD  1 
ATOM   1192 C CE  . MET A 1 154 ? 20.704 16.028 -5.279  1.00 21.26  ? 154 MET A CE  1 
ATOM   1193 N N   . SER A 1 155 ? 20.872 14.596 0.434   1.00 20.84  ? 155 SER A N   1 
ATOM   1194 C CA  . SER A 1 155 ? 21.086 14.918 1.840   1.00 20.37  ? 155 SER A CA  1 
ATOM   1195 C C   . SER A 1 155 ? 21.611 16.339 1.971   1.00 22.20  ? 155 SER A C   1 
ATOM   1196 O O   . SER A 1 155 ? 22.361 16.817 1.111   1.00 21.89  ? 155 SER A O   1 
ATOM   1197 C CB  . SER A 1 155 ? 22.074 13.933 2.466   1.00 21.97  ? 155 SER A CB  1 
ATOM   1198 O OG  . SER A 1 155 ? 22.318 14.247 3.829   1.00 27.04  ? 155 SER A OG  1 
ATOM   1199 N N   . THR A 1 156 ? 21.158 17.030 3.017   1.00 19.53  ? 156 THR A N   1 
ATOM   1200 C CA  . THR A 1 156 ? 21.792 18.252 3.481   1.00 21.05  ? 156 THR A CA  1 
ATOM   1201 C C   . THR A 1 156 ? 23.115 17.917 4.170   1.00 19.75  ? 156 THR A C   1 
ATOM   1202 O O   . THR A 1 156 ? 23.402 16.752 4.462   1.00 20.87  ? 156 THR A O   1 
ATOM   1203 C CB  . THR A 1 156 ? 20.896 18.979 4.494   1.00 24.57  ? 156 THR A CB  1 
ATOM   1204 O OG1 . THR A 1 156 ? 20.875 18.223 5.717   1.00 22.14  ? 156 THR A OG1 1 
ATOM   1205 C CG2 . THR A 1 156 ? 19.477 19.180 3.983   1.00 22.72  ? 156 THR A CG2 1 
ATOM   1206 N N   . PRO A 1 157 ? 23.936 18.931 4.463   1.00 22.28  ? 157 PRO A N   1 
ATOM   1207 C CA  . PRO A 1 157 ? 25.144 18.673 5.273   1.00 20.65  ? 157 PRO A CA  1 
ATOM   1208 C C   . PRO A 1 157 ? 24.851 18.026 6.621   1.00 18.61  ? 157 PRO A C   1 
ATOM   1209 O O   . PRO A 1 157 ? 25.450 16.991 6.945   1.00 20.01  ? 157 PRO A O   1 
ATOM   1210 C CB  . PRO A 1 157 ? 25.755 20.071 5.421   1.00 22.32  ? 157 PRO A CB  1 
ATOM   1211 C CG  . PRO A 1 157 ? 25.299 20.816 4.208   1.00 24.96  ? 157 PRO A CG  1 
ATOM   1212 C CD  . PRO A 1 157 ? 23.914 20.307 3.913   1.00 22.66  ? 157 PRO A CD  1 
ATOM   1213 N N   . SER A 1 158 ? 23.950 18.600 7.426   1.00 22.82  ? 158 SER A N   1 
ATOM   1214 C CA  . SER A 1 158 ? 23.669 17.976 8.720   1.00 21.86  ? 158 SER A CA  1 
ATOM   1215 C C   . SER A 1 158 ? 22.963 16.635 8.548   1.00 20.97  ? 158 SER A C   1 
ATOM   1216 O O   . SER A 1 158 ? 23.041 15.776 9.430   1.00 22.48  ? 158 SER A O   1 
ATOM   1217 C CB  . SER A 1 158 ? 22.868 18.925 9.618   1.00 25.27  ? 158 SER A CB  1 
ATOM   1218 O OG  . SER A 1 158 ? 21.606 19.273 9.076   1.00 23.65  ? 158 SER A OG  1 
ATOM   1219 N N   . GLY A 1 159 ? 22.320 16.414 7.405   1.00 19.33  ? 159 GLY A N   1 
ATOM   1220 C CA  . GLY A 1 159 ? 21.771 15.110 7.120   1.00 21.59  ? 159 GLY A CA  1 
ATOM   1221 C C   . GLY A 1 159 ? 22.799 14.082 6.717   1.00 19.66  ? 159 GLY A C   1 
ATOM   1222 O O   . GLY A 1 159 ? 22.463 12.893 6.652   1.00 22.51  ? 159 GLY A O   1 
ATOM   1223 N N   . THR A 1 160 ? 24.042 14.495 6.445   1.00 19.19  ? 160 THR A N   1 
ATOM   1224 C CA  . THR A 1 160 ? 24.998 13.514 5.942   1.00 19.47  ? 160 THR A CA  1 
ATOM   1225 C C   . THR A 1 160 ? 25.328 12.462 6.980   1.00 20.71  ? 160 THR A C   1 
ATOM   1226 O O   . THR A 1 160 ? 25.783 11.376 6.615   1.00 20.72  ? 160 THR A O   1 
ATOM   1227 C CB  . THR A 1 160 ? 26.305 14.164 5.444   1.00 20.15  ? 160 THR A CB  1 
ATOM   1228 O OG1 . THR A 1 160 ? 26.939 14.948 6.471   1.00 21.92  ? 160 THR A OG1 1 
ATOM   1229 C CG2 . THR A 1 160 ? 26.032 15.016 4.229   1.00 27.26  ? 160 THR A CG2 1 
ATOM   1230 N N   . THR A 1 161 ? 25.085 12.738 8.255   1.00 17.55  ? 161 THR A N   1 
ATOM   1231 C CA  . THR A 1 161 ? 25.349 11.739 9.279   1.00 20.50  ? 161 THR A CA  1 
ATOM   1232 C C   . THR A 1 161 ? 24.186 10.774 9.470   1.00 24.80  ? 161 THR A C   1 
ATOM   1233 O O   . THR A 1 161 ? 24.261 9.895  10.342  1.00 24.99  ? 161 THR A O   1 
ATOM   1234 C CB  . THR A 1 161 ? 25.665 12.419 10.613  1.00 24.28  ? 161 THR A CB  1 
ATOM   1235 O OG1 . THR A 1 161 ? 24.778 13.515 10.796  1.00 24.01  ? 161 THR A OG1 1 
ATOM   1236 C CG2 . THR A 1 161 ? 27.113 12.937 10.634  1.00 25.22  ? 161 THR A CG2 1 
ATOM   1237 N N   . ALA A 1 162 ? 23.124 10.915 8.690   1.00 22.09  ? 162 ALA A N   1 
ATOM   1238 C CA  . ALA A 1 162 ? 21.900 10.133 8.868   1.00 23.03  ? 162 ALA A CA  1 
ATOM   1239 C C   . ALA A 1 162 ? 21.809 9.098  7.749   1.00 23.86  ? 162 ALA A C   1 
ATOM   1240 O O   . ALA A 1 162 ? 22.783 8.359  7.539   1.00 19.86  ? 162 ALA A O   1 
ATOM   1241 C CB  . ALA A 1 162 ? 20.702 11.073 8.959   1.00 24.56  ? 162 ALA A CB  1 
ATOM   1242 N N   . TYR A 1 163 ? 20.679 8.988  7.043   1.00 20.36  ? 163 TYR A N   1 
ATOM   1243 C CA  . TYR A 1 163 ? 20.523 7.988  5.988   1.00 17.24  ? 163 TYR A CA  1 
ATOM   1244 C C   . TYR A 1 163 ? 21.713 8.001  5.031   1.00 17.25  ? 163 TYR A C   1 
ATOM   1245 O O   . TYR A 1 163 ? 22.224 6.945  4.652   1.00 18.41  ? 163 TYR A O   1 
ATOM   1246 C CB  . TYR A 1 163 ? 19.216 8.282  5.250   1.00 20.04  ? 163 TYR A CB  1 
ATOM   1247 C CG  . TYR A 1 163 ? 18.567 7.136  4.524   0.80 20.69  ? 163 TYR A CG  1 
ATOM   1248 C CD1 . TYR A 1 163 ? 19.195 5.912  4.395   0.80 19.83  ? 163 TYR A CD1 1 
ATOM   1249 C CD2 . TYR A 1 163 ? 17.300 7.289  3.971   0.80 26.91  ? 163 TYR A CD2 1 
ATOM   1250 C CE1 . TYR A 1 163 ? 18.581 4.856  3.724   0.80 25.44  ? 163 TYR A CE1 1 
ATOM   1251 C CE2 . TYR A 1 163 ? 16.678 6.246  3.295   0.80 29.47  ? 163 TYR A CE2 1 
ATOM   1252 C CZ  . TYR A 1 163 ? 17.329 5.037  3.165   0.80 28.98  ? 163 TYR A CZ  1 
ATOM   1253 O OH  . TYR A 1 163 ? 16.711 4.005  2.502   0.80 27.52  ? 163 TYR A OH  1 
ATOM   1254 N N   . ASN A 1 164 ? 22.168 9.195  4.658   1.00 16.91  ? 164 ASN A N   1 
ATOM   1255 C CA  . ASN A 1 164 ? 23.303 9.365  3.750   1.00 19.31  ? 164 ASN A CA  1 
ATOM   1256 C C   . ASN A 1 164 ? 24.499 8.536  4.193   1.00 20.35  ? 164 ASN A C   1 
ATOM   1257 O O   . ASN A 1 164 ? 25.187 7.912  3.374   1.00 19.64  ? 164 ASN A O   1 
ATOM   1258 C CB  . ASN A 1 164 ? 23.674 10.853 3.702   1.00 17.06  ? 164 ASN A CB  1 
ATOM   1259 C CG  . ASN A 1 164 ? 24.992 11.120 2.994   1.00 21.56  ? 164 ASN A CG  1 
ATOM   1260 O OD1 . ASN A 1 164 ? 25.018 11.334 1.789   1.00 21.95  ? 164 ASN A OD1 1 
ATOM   1261 N ND2 . ASN A 1 164 ? 26.094 11.150 3.755   1.00 18.08  ? 164 ASN A ND2 1 
ATOM   1262 N N   . LYS A 1 165 ? 24.768 8.521  5.495   1.00 16.88  ? 165 LYS A N   1 
ATOM   1263 C CA  . LYS A 1 165 ? 25.925 7.789  5.992   1.00 13.95  ? 165 LYS A CA  1 
ATOM   1264 C C   . LYS A 1 165 ? 25.758 6.296  5.761   1.00 19.11  ? 165 LYS A C   1 
ATOM   1265 O O   . LYS A 1 165 ? 26.699 5.609  5.338   1.00 17.15  ? 165 LYS A O   1 
ATOM   1266 C CB  . LYS A 1 165 ? 26.104 8.092  7.494   1.00 17.61  ? 165 LYS A CB  1 
ATOM   1267 C CG  . LYS A 1 165 ? 27.365 7.470  8.079   1.00 19.13  ? 165 LYS A CG  1 
ATOM   1268 C CD  . LYS A 1 165 ? 27.532 7.851  9.518   1.00 18.39  ? 165 LYS A CD  1 
ATOM   1269 C CE  . LYS A 1 165 ? 28.900 7.429  10.017  0.90 24.73  ? 165 LYS A CE  1 
ATOM   1270 N NZ  . LYS A 1 165 ? 29.082 5.956  9.969   0.80 27.41  ? 165 LYS A NZ  1 
ATOM   1271 N N   . SER A 1 166 ? 24.556 5.778  6.018   1.00 19.24  ? 166 SER A N   1 
ATOM   1272 C CA  . SER A 1 166 ? 24.291 4.357  5.832   1.00 19.31  ? 166 SER A CA  1 
ATOM   1273 C C   . SER A 1 166 ? 24.403 3.938  4.375   1.00 17.99  ? 166 SER A C   1 
ATOM   1274 O O   . SER A 1 166 ? 24.624 2.756  4.099   1.00 19.06  ? 166 SER A O   1 
ATOM   1275 C CB  . SER A 1 166 ? 22.887 4.017  6.334   1.00 19.41  ? 166 SER A CB  1 
ATOM   1276 O OG  . SER A 1 166 ? 22.819 4.230  7.731   1.00 25.47  ? 166 SER A OG  1 
ATOM   1277 N N   . LEU A 1 167 ? 24.211 4.870  3.457   1.00 19.53  ? 167 LEU A N   1 
ATOM   1278 C CA  . LEU A 1 167 ? 24.324 4.608  2.021   1.00 19.11  ? 167 LEU A CA  1 
ATOM   1279 C C   . LEU A 1 167 ? 25.738 4.820  1.497   1.00 22.38  ? 167 LEU A C   1 
ATOM   1280 O O   . LEU A 1 167 ? 25.956 4.771  0.281   1.00 20.11  ? 167 LEU A O   1 
ATOM   1281 C CB  . LEU A 1 167 ? 23.335 5.486  1.256   1.00 18.42  ? 167 LEU A CB  1 
ATOM   1282 C CG  . LEU A 1 167 ? 21.862 5.216  1.596   1.00 19.51  ? 167 LEU A CG  1 
ATOM   1283 C CD1 . LEU A 1 167 ? 20.933 6.221  0.901   1.00 19.25  ? 167 LEU A CD1 1 
ATOM   1284 C CD2 . LEU A 1 167 ? 21.486 3.789  1.234   1.00 17.50  ? 167 LEU A CD2 1 
ATOM   1285 N N   . GLY A 1 168 ? 26.703 5.071  2.374   1.00 20.37  ? 168 GLY A N   1 
ATOM   1286 C CA  . GLY A 1 168 ? 28.073 5.228  1.931   1.00 18.79  ? 168 GLY A CA  1 
ATOM   1287 C C   . GLY A 1 168 ? 28.461 6.647  1.600   1.00 23.46  ? 168 GLY A C   1 
ATOM   1288 O O   . GLY A 1 168 ? 29.569 6.863  1.104   1.00 25.62  ? 168 GLY A O   1 
ATOM   1289 N N   . GLY A 1 169 ? 27.601 7.627  1.894   1.00 19.29  ? 169 GLY A N   1 
ATOM   1290 C CA  . GLY A 1 169 ? 27.926 9.012  1.623   1.00 19.12  ? 169 GLY A CA  1 
ATOM   1291 C C   . GLY A 1 169 ? 29.016 9.559  2.531   1.00 23.67  ? 169 GLY A C   1 
ATOM   1292 O O   . GLY A 1 169 ? 29.354 8.991  3.576   1.00 20.22  ? 169 GLY A O   1 
ATOM   1293 N N   . ALA A 1 170 ? 29.584 10.685 2.098   1.00 17.58  ? 170 ALA A N   1 
ATOM   1294 C CA  . ALA A 1 170 ? 30.580 11.410 2.877   1.00 21.72  ? 170 ALA A CA  1 
ATOM   1295 C C   . ALA A 1 170 ? 29.899 12.221 3.973   1.00 21.81  ? 170 ALA A C   1 
ATOM   1296 O O   . ALA A 1 170 ? 28.746 12.631 3.834   1.00 20.53  ? 170 ALA A O   1 
ATOM   1297 C CB  . ALA A 1 170 ? 31.385 12.348 1.979   1.00 21.70  ? 170 ALA A CB  1 
ATOM   1298 N N   . LEU A 1 171 ? 30.608 12.433 5.083   1.00 19.92  ? 171 LEU A N   1 
ATOM   1299 C CA  . LEU A 1 171 ? 30.118 13.329 6.128   1.00 18.38  ? 171 LEU A CA  1 
ATOM   1300 C C   . LEU A 1 171 ? 30.644 14.721 5.822   1.00 19.96  ? 171 LEU A C   1 
ATOM   1301 O O   . LEU A 1 171 ? 31.849 14.894 5.657   1.00 27.09  ? 171 LEU A O   1 
ATOM   1302 C CB  . LEU A 1 171 ? 30.594 12.874 7.510   1.00 17.58  ? 171 LEU A CB  1 
ATOM   1303 C CG  . LEU A 1 171 ? 30.365 11.399 7.854   1.00 22.04  ? 171 LEU A CG  1 
ATOM   1304 C CD1 . LEU A 1 171 ? 30.720 11.125 9.308   1.00 24.27  ? 171 LEU A CD1 1 
ATOM   1305 C CD2 . LEU A 1 171 ? 28.917 10.971 7.558   1.00 24.56  ? 171 LEU A CD2 1 
ATOM   1306 N N   . MET A 1 172 ? 29.767 15.719 5.728   1.00 19.94  ? 172 MET A N   1 
ATOM   1307 C CA  . MET A 1 172 ? 30.267 17.039 5.365   1.00 22.03  ? 172 MET A CA  1 
ATOM   1308 C C   . MET A 1 172 ? 29.889 18.091 6.401   1.00 24.62  ? 172 MET A C   1 
ATOM   1309 O O   . MET A 1 172 ? 28.755 18.129 6.887   1.00 26.03  ? 172 MET A O   1 
ATOM   1310 C CB  . MET A 1 172 ? 29.804 17.466 3.944   0.80 24.97  ? 172 MET A CB  1 
ATOM   1311 C CG  . MET A 1 172 ? 28.365 17.325 3.591   0.80 30.41  ? 172 MET A CG  1 
ATOM   1312 S SD  . MET A 1 172 ? 28.171 17.454 1.763   0.80 30.27  ? 172 MET A SD  1 
ATOM   1313 C CE  . MET A 1 172 ? 29.137 18.929 1.516   0.80 26.03  ? 172 MET A CE  1 
ATOM   1314 N N   . HIS A 1 173 ? 30.855 18.945 6.711   1.00 24.27  ? 173 HIS A N   1 
ATOM   1315 C CA  . HIS A 1 173 ? 30.641 20.020 7.665   1.00 24.04  ? 173 HIS A CA  1 
ATOM   1316 C C   . HIS A 1 173 ? 29.531 20.953 7.192   1.00 28.18  ? 173 HIS A C   1 
ATOM   1317 O O   . HIS A 1 173 ? 29.498 21.342 6.012   1.00 30.01  ? 173 HIS A O   1 
ATOM   1318 C CB  . HIS A 1 173 ? 31.906 20.832 7.873   1.00 24.79  ? 173 HIS A CB  1 
ATOM   1319 C CG  . HIS A 1 173 ? 31.826 21.736 9.060   1.00 26.57  ? 173 HIS A CG  1 
ATOM   1320 N ND1 . HIS A 1 173 ? 31.319 23.015 8.988   1.00 29.22  ? 173 HIS A ND1 1 
ATOM   1321 C CD2 . HIS A 1 173 ? 32.130 21.524 10.362  1.00 28.52  ? 173 HIS A CD2 1 
ATOM   1322 C CE1 . HIS A 1 173 ? 31.348 23.567 10.188  1.00 30.61  ? 173 HIS A CE1 1 
ATOM   1323 N NE2 . HIS A 1 173 ? 31.834 22.682 11.041  1.00 27.73  ? 173 HIS A NE2 1 
ATOM   1324 N N   . PRO A 1 174 ? 28.632 21.364 8.091   1.00 27.06  ? 174 PRO A N   1 
ATOM   1325 C CA  . PRO A 1 174 ? 27.436 22.113 7.676   1.00 26.20  ? 174 PRO A CA  1 
ATOM   1326 C C   . PRO A 1 174 ? 27.683 23.573 7.338   1.00 32.40  ? 174 PRO A C   1 
ATOM   1327 O O   . PRO A 1 174 ? 26.746 24.262 6.919   1.00 37.32  ? 174 PRO A O   1 
ATOM   1328 C CB  . PRO A 1 174 ? 26.499 21.967 8.893   1.00 31.89  ? 174 PRO A CB  1 
ATOM   1329 C CG  . PRO A 1 174 ? 27.402 21.624 10.051  1.00 32.63  ? 174 PRO A CG  1 
ATOM   1330 C CD  . PRO A 1 174 ? 28.545 20.861 9.472   1.00 27.66  ? 174 PRO A CD  1 
ATOM   1331 N N   . SER A 1 175 ? 28.908 24.072 7.485   1.00 30.81  ? 175 SER A N   1 
ATOM   1332 C CA  . SER A 1 175 ? 29.235 25.374 6.924   1.00 31.94  ? 175 SER A CA  1 
ATOM   1333 C C   . SER A 1 175 ? 29.334 25.341 5.398   1.00 32.84  ? 175 SER A C   1 
ATOM   1334 O O   . SER A 1 175 ? 29.456 26.399 4.773   1.00 33.42  ? 175 SER A O   1 
ATOM   1335 C CB  . SER A 1 175 ? 30.551 25.863 7.517   1.00 34.74  ? 175 SER A CB  1 
ATOM   1336 O OG  . SER A 1 175 ? 31.579 24.968 7.134   1.00 35.56  ? 175 SER A OG  1 
ATOM   1337 N N   . ILE A 1 176 ? 29.292 24.163 4.788   1.00 28.66  ? 176 ILE A N   1 
ATOM   1338 C CA  . ILE A 1 176 ? 29.383 24.042 3.338   1.00 30.19  ? 176 ILE A CA  1 
ATOM   1339 C C   . ILE A 1 176 ? 27.967 24.051 2.784   1.00 28.80  ? 176 ILE A C   1 
ATOM   1340 O O   . ILE A 1 176 ? 27.131 23.233 3.178   1.00 29.40  ? 176 ILE A O   1 
ATOM   1341 C CB  . ILE A 1 176 ? 30.132 22.767 2.934   1.00 25.22  ? 176 ILE A CB  1 
ATOM   1342 C CG1 . ILE A 1 176 ? 31.515 22.752 3.584   1.00 28.55  ? 176 ILE A CG1 1 
ATOM   1343 C CG2 . ILE A 1 176 ? 30.244 22.667 1.404   1.00 25.63  ? 176 ILE A CG2 1 
ATOM   1344 C CD1 . ILE A 1 176 ? 32.231 21.428 3.450   1.00 31.35  ? 176 ILE A CD1 1 
ATOM   1345 N N   . GLU A 1 177 ? 27.685 24.985 1.888   1.00 26.51  ? 177 GLU A N   1 
ATOM   1346 C CA  . GLU A 1 177 ? 26.339 25.103 1.334   1.00 26.68  ? 177 GLU A CA  1 
ATOM   1347 C C   . GLU A 1 177 ? 26.259 24.148 0.154   1.00 28.87  ? 177 GLU A C   1 
ATOM   1348 O O   . GLU A 1 177 ? 26.640 24.479 -0.969  1.00 29.82  ? 177 GLU A O   1 
ATOM   1349 C CB  . GLU A 1 177 ? 26.045 26.539 0.942   1.00 25.93  ? 177 GLU A CB  1 
ATOM   1350 C CG  . GLU A 1 177 ? 26.119 27.519 2.102   0.80 26.13  ? 177 GLU A CG  1 
ATOM   1351 C CD  . GLU A 1 177 ? 25.599 28.884 1.712   0.60 32.66  ? 177 GLU A CD  1 
ATOM   1352 O OE1 . GLU A 1 177 ? 24.435 29.191 2.034   0.60 37.41  ? 177 GLU A OE1 1 
ATOM   1353 O OE2 . GLU A 1 177 ? 26.337 29.634 1.045   0.60 34.84  ? 177 GLU A OE2 1 
ATOM   1354 N N   . ALA A 1 178 ? 25.771 22.938 0.419   1.00 25.84  ? 178 ALA A N   1 
ATOM   1355 C CA  . ALA A 1 178 ? 25.828 21.873 -0.565  1.00 22.67  ? 178 ALA A CA  1 
ATOM   1356 C C   . ALA A 1 178 ? 24.734 20.857 -0.280  1.00 24.13  ? 178 ALA A C   1 
ATOM   1357 O O   . ALA A 1 178 ? 24.101 20.866 0.783   1.00 23.67  ? 178 ALA A O   1 
ATOM   1358 C CB  . ALA A 1 178 ? 27.203 21.197 -0.562  1.00 23.65  ? 178 ALA A CB  1 
ATOM   1359 N N   . MET A 1 179 ? 24.518 19.970 -1.245  1.00 19.88  ? 179 MET A N   1 
ATOM   1360 C CA  . MET A 1 179 ? 23.663 18.808 -1.068  1.00 18.94  ? 179 MET A CA  1 
ATOM   1361 C C   . MET A 1 179 ? 24.388 17.603 -1.631  1.00 21.24  ? 179 MET A C   1 
ATOM   1362 O O   . MET A 1 179 ? 25.238 17.739 -2.518  1.00 18.63  ? 179 MET A O   1 
ATOM   1363 C CB  . MET A 1 179 ? 22.291 18.995 -1.762  1.00 19.44  ? 179 MET A CB  1 
ATOM   1364 C CG  . MET A 1 179 ? 22.419 19.289 -3.277  1.00 21.65  ? 179 MET A CG  1 
ATOM   1365 S SD  . MET A 1 179 ? 20.818 19.584 -4.050  1.00 22.50  ? 179 MET A SD  1 
ATOM   1366 C CE  . MET A 1 179 ? 21.354 19.845 -5.761  1.00 21.64  ? 179 MET A CE  1 
ATOM   1367 N N   . GLN A 1 180 ? 24.062 16.413 -1.128  1.00 20.36  ? 180 GLN A N   1 
ATOM   1368 C CA  . GLN A 1 180 ? 24.801 15.226 -1.536  1.00 21.31  ? 180 GLN A CA  1 
ATOM   1369 C C   . GLN A 1 180 ? 23.845 14.133 -1.988  1.00 20.56  ? 180 GLN A C   1 
ATOM   1370 O O   . GLN A 1 180 ? 22.914 13.780 -1.262  1.00 19.57  ? 180 GLN A O   1 
ATOM   1371 C CB  . GLN A 1 180 ? 25.701 14.703 -0.403  1.00 17.56  ? 180 GLN A CB  1 
ATOM   1372 C CG  . GLN A 1 180 ? 26.451 13.417 -0.789  1.00 16.30  ? 180 GLN A CG  1 
ATOM   1373 C CD  . GLN A 1 180 ? 27.494 12.993 0.230   1.00 19.14  ? 180 GLN A CD  1 
ATOM   1374 O OE1 . GLN A 1 180 ? 28.193 11.999 0.030   1.00 19.10  ? 180 GLN A OE1 1 
ATOM   1375 N NE2 . GLN A 1 180 ? 27.590 13.731 1.351   1.00 16.88  ? 180 GLN A NE2 1 
ATOM   1376 N N   . LEU A 1 181 ? 24.101 13.567 -3.167  1.00 18.58  ? 181 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 181 ? 23.250 12.532 -3.743  1.00 16.65  ? 181 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 181 ? 23.925 11.175 -3.586  1.00 20.04  ? 181 LEU A C   1 
ATOM   1379 O O   . LEU A 1 181 ? 25.046 10.983 -4.072  1.00 22.23  ? 181 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 181 ? 22.997 12.837 -5.228  1.00 19.22  ? 181 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 181 ? 22.123 11.845 -5.982  1.00 21.51  ? 181 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 181 ? 20.660 12.025 -5.534  1.00 20.02  ? 181 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 181 ? 22.309 12.035 -7.541  1.00 18.23  ? 181 LEU A CD2 1 
ATOM   1384 N N   . THR A 1 182 ? 23.238 10.222 -2.944  1.00 18.00  ? 182 THR A N   1 
ATOM   1385 C CA  . THR A 1 182 ? 23.743 8.858  -2.813  1.00 15.78  ? 182 THR A CA  1 
ATOM   1386 C C   . THR A 1 182 ? 22.787 7.877  -3.472  1.00 19.24  ? 182 THR A C   1 
ATOM   1387 O O   . THR A 1 182 ? 21.575 8.104  -3.520  1.00 22.40  ? 182 THR A O   1 
ATOM   1388 C CB  . THR A 1 182 ? 23.944 8.441  -1.332  1.00 20.46  ? 182 THR A CB  1 
ATOM   1389 O OG1 . THR A 1 182 ? 22.756 8.741  -0.597  1.00 21.84  ? 182 THR A OG1 1 
ATOM   1390 C CG2 . THR A 1 182 ? 25.102 9.195  -0.734  1.00 17.80  ? 182 THR A CG2 1 
ATOM   1391 N N   . GLU A 1 183 ? 23.350 6.771  -3.959  1.00 17.66  ? 183 GLU A N   1 
ATOM   1392 C CA  . GLU A 1 183 ? 22.591 5.697  -4.590  1.00 19.95  ? 183 GLU A CA  1 
ATOM   1393 C C   . GLU A 1 183 ? 22.133 4.668  -3.567  1.00 22.37  ? 183 GLU A C   1 
ATOM   1394 O O   . GLU A 1 183 ? 22.850 4.353  -2.616  1.00 18.16  ? 183 GLU A O   1 
ATOM   1395 C CB  . GLU A 1 183 ? 23.442 4.975  -5.637  1.00 24.94  ? 183 GLU A CB  1 
ATOM   1396 C CG  . GLU A 1 183 ? 24.114 5.896  -6.645  1.00 23.52  ? 183 GLU A CG  1 
ATOM   1397 C CD  . GLU A 1 183 ? 24.906 5.140  -7.715  1.00 27.22  ? 183 GLU A CD  1 
ATOM   1398 O OE1 . GLU A 1 183 ? 25.236 3.946  -7.516  1.00 29.09  ? 183 GLU A OE1 1 
ATOM   1399 O OE2 . GLU A 1 183 ? 25.227 5.758  -8.748  1.00 27.26  ? 183 GLU A OE2 1 
ATOM   1400 N N   . MET A 1 184 ? 20.958 4.085  -3.807  1.00 18.06  ? 184 MET A N   1 
ATOM   1401 C CA  . MET A 1 184 ? 20.522 2.893  -3.080  1.00 21.79  ? 184 MET A CA  1 
ATOM   1402 C C   . MET A 1 184 ? 20.539 1.712  -4.042  1.00 24.01  ? 184 MET A C   1 
ATOM   1403 O O   . MET A 1 184 ? 19.673 1.621  -4.921  1.00 29.38  ? 184 MET A O   1 
ATOM   1404 C CB  . MET A 1 184 ? 19.119 3.066  -2.494  1.00 21.34  ? 184 MET A CB  1 
ATOM   1405 C CG  . MET A 1 184 ? 18.894 4.332  -1.711  0.80 21.90  ? 184 MET A CG  1 
ATOM   1406 S SD  . MET A 1 184 ? 17.157 4.323  -1.264  0.80 31.16  ? 184 MET A SD  1 
ATOM   1407 C CE  . MET A 1 184 ? 17.011 6.035  -0.804  0.80 31.03  ? 184 MET A CE  1 
ATOM   1408 N N   . ALA A 1 185 ? 21.512 0.816  -3.874  1.00 18.59  ? 185 ALA A N   1 
ATOM   1409 C CA  . ALA A 1 185 ? 21.570 -0.465 -4.572  1.00 20.28  ? 185 ALA A CA  1 
ATOM   1410 C C   . ALA A 1 185 ? 21.390 -0.300 -6.086  1.00 25.99  ? 185 ALA A C   1 
ATOM   1411 O O   . ALA A 1 185 ? 20.437 -0.800 -6.673  1.00 24.50  ? 185 ALA A O   1 
ATOM   1412 C CB  . ALA A 1 185 ? 20.518 -1.429 -4.024  1.00 21.09  ? 185 ALA A CB  1 
ATOM   1413 N N   . SER A 1 186 ? 22.306 0.426  -6.715  1.00 25.03  ? 186 SER A N   1 
ATOM   1414 C CA  . SER A 1 186 ? 22.202 0.562  -8.164  1.00 28.83  ? 186 SER A CA  1 
ATOM   1415 C C   . SER A 1 186 ? 22.626 -0.723 -8.855  1.00 29.06  ? 186 SER A C   1 
ATOM   1416 O O   . SER A 1 186 ? 23.458 -1.484 -8.352  1.00 27.77  ? 186 SER A O   1 
ATOM   1417 C CB  . SER A 1 186 ? 23.059 1.714  -8.671  1.00 32.07  ? 186 SER A CB  1 
ATOM   1418 O OG  . SER A 1 186 ? 24.381 1.581  -8.187  1.00 37.72  ? 186 SER A OG  1 
ATOM   1419 N N   . ILE A 1 187 ? 22.053 -0.954 -10.032 1.00 28.42  ? 187 ILE A N   1 
ATOM   1420 C CA  . ILE A 1 187 ? 22.461 -2.055 -10.899 1.00 29.82  ? 187 ILE A CA  1 
ATOM   1421 C C   . ILE A 1 187 ? 23.611 -1.585 -11.773 1.00 31.57  ? 187 ILE A C   1 
ATOM   1422 O O   . ILE A 1 187 ? 23.554 -0.502 -12.368 1.00 28.93  ? 187 ILE A O   1 
ATOM   1423 C CB  . ILE A 1 187 ? 21.289 -2.526 -11.765 0.80 32.59  ? 187 ILE A CB  1 
ATOM   1424 C CG1 . ILE A 1 187 ? 20.009 -2.338 -10.963 0.70 42.98  ? 187 ILE A CG1 1 
ATOM   1425 C CG2 . ILE A 1 187 ? 21.516 -3.957 -12.265 0.70 31.38  ? 187 ILE A CG2 1 
ATOM   1426 C CD1 . ILE A 1 187 ? 19.132 -3.469 -11.017 0.70 44.65  ? 187 ILE A CD1 1 
ATOM   1427 N N   . ASN A 1 188 ? 24.648 -2.399 -11.874 1.00 28.67  ? 188 ASN A N   1 
ATOM   1428 C CA  . ASN A 1 188 ? 25.756 -2.085 -12.770 1.00 32.92  ? 188 ASN A CA  1 
ATOM   1429 C C   . ASN A 1 188 ? 26.186 -3.377 -13.441 1.00 30.49  ? 188 ASN A C   1 
ATOM   1430 O O   . ASN A 1 188 ? 26.658 -4.303 -12.776 1.00 33.86  ? 188 ASN A O   1 
ATOM   1431 C CB  . ASN A 1 188 ? 26.910 -1.412 -12.022 1.00 35.39  ? 188 ASN A CB  1 
ATOM   1432 C CG  . ASN A 1 188 ? 26.696 0.089  -11.867 1.00 37.69  ? 188 ASN A CG  1 
ATOM   1433 O OD1 . ASN A 1 188 ? 27.128 0.876  -12.710 1.00 42.33  ? 188 ASN A OD1 1 
ATOM   1434 N ND2 . ASN A 1 188 ? 26.009 0.490  -10.802 1.00 37.01  ? 188 ASN A ND2 1 
ATOM   1435 N N   . ASN A 1 189 ? 25.964 -3.460 -14.745 1.00 30.56  ? 189 ASN A N   1 
ATOM   1436 C CA  . ASN A 1 189 ? 26.440 -4.580 -15.536 1.00 32.19  ? 189 ASN A CA  1 
ATOM   1437 C C   . ASN A 1 189 ? 26.825 -4.031 -16.904 1.00 34.66  ? 189 ASN A C   1 
ATOM   1438 O O   . ASN A 1 189 ? 26.998 -2.822 -17.077 1.00 38.61  ? 189 ASN A O   1 
ATOM   1439 C CB  . ASN A 1 189 ? 25.387 -5.697 -15.602 1.00 37.88  ? 189 ASN A CB  1 
ATOM   1440 C CG  . ASN A 1 189 ? 24.018 -5.195 -16.047 1.00 41.21  ? 189 ASN A CG  1 
ATOM   1441 O OD1 . ASN A 1 189 ? 23.912 -4.284 -16.873 1.00 38.51  ? 189 ASN A OD1 1 
ATOM   1442 N ND2 . ASN A 1 189 ? 22.961 -5.788 -15.488 1.00 40.31  ? 189 ASN A ND2 1 
ATOM   1443 N N   . ARG A 1 190 ? 26.971 -4.930 -17.873 1.00 40.49  ? 190 ARG A N   1 
ATOM   1444 C CA  . ARG A 1 190 ? 27.295 -4.527 -19.239 1.00 48.28  ? 190 ARG A CA  1 
ATOM   1445 C C   . ARG A 1 190 ? 26.294 -3.507 -19.780 1.00 47.85  ? 190 ARG A C   1 
ATOM   1446 O O   . ARG A 1 190 ? 26.666 -2.591 -20.521 1.00 51.80  ? 190 ARG A O   1 
ATOM   1447 C CB  . ARG A 1 190 ? 27.328 -5.773 -20.130 0.80 50.96  ? 190 ARG A CB  1 
ATOM   1448 C CG  . ARG A 1 190 ? 27.685 -5.547 -21.583 0.80 53.68  ? 190 ARG A CG  1 
ATOM   1449 C CD  . ARG A 1 190 ? 26.937 -6.530 -22.488 0.70 55.36  ? 190 ARG A CD  1 
ATOM   1450 N NE  . ARG A 1 190 ? 26.780 -7.838 -21.858 0.70 55.21  ? 190 ARG A NE  1 
ATOM   1451 C CZ  . ARG A 1 190 ? 25.749 -8.651 -22.071 0.70 57.63  ? 190 ARG A CZ  1 
ATOM   1452 N NH1 . ARG A 1 190 ? 24.774 -8.289 -22.895 0.60 56.31  ? 190 ARG A NH1 1 
ATOM   1453 N NH2 . ARG A 1 190 ? 25.686 -9.823 -21.451 0.60 60.88  ? 190 ARG A NH2 1 
ATOM   1454 N N   . VAL A 1 191 ? 25.025 -3.644 -19.400 1.00 43.19  ? 191 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 191 ? 23.936 -2.879 -19.998 1.00 41.48  ? 191 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 191 ? 23.598 -1.624 -19.195 1.00 38.32  ? 191 VAL A C   1 
ATOM   1457 O O   . VAL A 1 191 ? 23.243 -0.596 -19.773 1.00 38.89  ? 191 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 191 ? 22.710 -3.801 -20.160 0.85 45.09  ? 191 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 191 ? 21.503 -3.018 -20.645 0.76 49.55  ? 191 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 191 ? 23.032 -4.934 -21.138 0.75 46.45  ? 191 VAL A CG2 1 
ATOM   1461 N N   . TYR A 1 192 ? 23.703 -1.661 -17.864 0.94 32.81  ? 192 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 192 ? 23.296 -0.547 -17.013 0.94 30.95  ? 192 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 192 ? 24.502 -0.005 -16.254 0.94 34.09  ? 192 TYR A C   1 
ATOM   1464 O O   . TYR A 1 192 ? 25.262 -0.783 -15.670 0.94 34.24  ? 192 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 192 ? 22.230 -0.990 -16.015 0.94 34.83  ? 192 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 192 ? 21.037 -1.681 -16.635 0.94 38.46  ? 192 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 192 ? 20.559 -2.873 -16.111 0.94 40.54  ? 192 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 192 ? 20.375 -1.129 -17.722 0.94 43.25  ? 192 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 192 ? 19.460 -3.509 -16.656 0.94 47.03  ? 192 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 192 ? 19.267 -1.761 -18.285 0.94 47.96  ? 192 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 192 ? 18.814 -2.949 -17.743 0.94 48.97  ? 192 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 192 ? 17.721 -3.585 -18.283 0.94 53.32  ? 192 TYR A OH  1 
ATOM   1473 N N   . ARG A 1 193 ? 24.658 1.323  -16.241 1.00 31.14  ? 193 ARG A N   1 
ATOM   1474 C CA  . ARG A 1 193 ? 25.814 1.968  -15.625 1.00 33.45  ? 193 ARG A CA  1 
ATOM   1475 C C   . ARG A 1 193 ? 25.387 3.226  -14.879 1.00 31.59  ? 193 ARG A C   1 
ATOM   1476 O O   . ARG A 1 193 ? 24.708 4.091  -15.446 1.00 30.77  ? 193 ARG A O   1 
ATOM   1477 C CB  . ARG A 1 193 ? 26.868 2.335  -16.679 1.00 40.70  ? 193 ARG A CB  1 
ATOM   1478 N N   . THR A 1 194 ? 25.796 3.329  -13.618 1.00 21.83  ? 194 THR A N   1 
ATOM   1479 C CA  . THR A 1 194 ? 25.682 4.558  -12.847 1.00 21.67  ? 194 THR A CA  1 
ATOM   1480 C C   . THR A 1 194 ? 27.067 4.984  -12.378 1.00 21.68  ? 194 THR A C   1 
ATOM   1481 O O   . THR A 1 194 ? 28.042 4.251  -12.529 1.00 23.55  ? 194 THR A O   1 
ATOM   1482 C CB  . THR A 1 194 ? 24.748 4.396  -11.637 1.00 28.20  ? 194 THR A CB  1 
ATOM   1483 O OG1 . THR A 1 194 ? 25.315 3.461  -10.701 1.00 27.87  ? 194 THR A OG1 1 
ATOM   1484 C CG2 . THR A 1 194 ? 23.392 3.898  -12.113 1.00 27.77  ? 194 THR A CG2 1 
ATOM   1485 N N   . ILE A 1 195 ? 27.148 6.188  -11.803 1.00 19.87  ? 195 ILE A N   1 
ATOM   1486 C CA  . ILE A 1 195 ? 28.449 6.695  -11.367 1.00 22.17  ? 195 ILE A CA  1 
ATOM   1487 C C   . ILE A 1 195 ? 28.943 5.932  -10.133 1.00 23.23  ? 195 ILE A C   1 
ATOM   1488 O O   . ILE A 1 195 ? 30.159 5.796  -9.921  1.00 24.49  ? 195 ILE A O   1 
ATOM   1489 C CB  . ILE A 1 195 ? 28.367 8.217  -11.120 1.00 20.57  ? 195 ILE A CB  1 
ATOM   1490 C CG1 . ILE A 1 195 ? 29.760 8.805  -10.841 1.00 23.84  ? 195 ILE A CG1 1 
ATOM   1491 C CG2 . ILE A 1 195 ? 27.428 8.541  -9.943  1.00 20.81  ? 195 ILE A CG2 1 
ATOM   1492 C CD1 . ILE A 1 195 ? 30.754 8.762  -12.027 1.00 23.34  ? 195 ILE A CD1 1 
ATOM   1493 N N   A GLY A 1 196 ? 28.013 5.395  -9.344  0.50 21.89  ? 196 GLY A N   1 
ATOM   1494 N N   B GLY A 1 196 ? 28.043 5.419  -9.300  0.50 22.07  ? 196 GLY A N   1 
ATOM   1495 C CA  A GLY A 1 196 ? 28.276 4.688  -8.079  0.50 22.16  ? 196 GLY A CA  1 
ATOM   1496 C CA  B GLY A 1 196 ? 28.499 4.574  -8.200  0.50 21.98  ? 196 GLY A CA  1 
ATOM   1497 C C   A GLY A 1 196 ? 28.571 5.630  -6.943  0.50 22.86  ? 196 GLY A C   1 
ATOM   1498 C C   B GLY A 1 196 ? 29.402 5.243  -7.182  0.50 22.19  ? 196 GLY A C   1 
ATOM   1499 O O   A GLY A 1 196 ? 27.960 5.540  -5.871  0.50 18.39  ? 196 GLY A O   1 
ATOM   1500 O O   B GLY A 1 196 ? 30.078 4.548  -6.416  0.50 27.55  ? 196 GLY A O   1 
ATOM   1501 N N   . SER A 1 197 ? 29.464 6.576  -7.174  1.00 24.11  ? 197 SER A N   1 
ATOM   1502 C CA  . SER A 1 197 ? 29.991 7.400  -6.104  1.00 21.29  ? 197 SER A CA  1 
ATOM   1503 C C   . SER A 1 197 ? 28.934 8.401  -5.652  1.00 18.46  ? 197 SER A C   1 
ATOM   1504 O O   . SER A 1 197 ? 28.119 8.850  -6.460  1.00 19.26  ? 197 SER A O   1 
ATOM   1505 C CB  . SER A 1 197 ? 31.238 8.162  -6.567  1.00 15.99  ? 197 SER A CB  1 
ATOM   1506 O OG  . SER A 1 197 ? 32.171 7.252  -7.108  1.00 19.20  ? 197 SER A OG  1 
ATOM   1507 N N   . PRO A 1 198 ? 28.934 8.787  -4.370  1.00 17.48  ? 198 PRO A N   1 
ATOM   1508 C CA  . PRO A 1 198 ? 28.148 9.957  -3.965  1.00 20.59  ? 198 PRO A CA  1 
ATOM   1509 C C   . PRO A 1 198 ? 28.594 11.184 -4.747  1.00 19.36  ? 198 PRO A C   1 
ATOM   1510 O O   . PRO A 1 198 ? 29.768 11.329 -5.098  1.00 19.78  ? 198 PRO A O   1 
ATOM   1511 C CB  . PRO A 1 198 ? 28.463 10.111 -2.461  1.00 21.72  ? 198 PRO A CB  1 
ATOM   1512 C CG  . PRO A 1 198 ? 29.061 8.799  -2.043  1.00 19.29  ? 198 PRO A CG  1 
ATOM   1513 C CD  . PRO A 1 198 ? 29.747 8.246  -3.265  1.00 18.85  ? 198 PRO A CD  1 
ATOM   1514 N N   . LEU A 1 199 ? 27.645 12.089 -4.995  1.00 16.38  ? 199 LEU A N   1 
ATOM   1515 C CA  . LEU A 1 199 ? 27.911 13.344 -5.681  1.00 17.44  ? 199 LEU A CA  1 
ATOM   1516 C C   . LEU A 1 199 ? 27.579 14.505 -4.761  1.00 19.97  ? 199 LEU A C   1 
ATOM   1517 O O   . LEU A 1 199 ? 26.491 14.542 -4.175  1.00 22.74  ? 199 LEU A O   1 
ATOM   1518 C CB  . LEU A 1 199 ? 27.066 13.452 -6.964  1.00 17.68  ? 199 LEU A CB  1 
ATOM   1519 C CG  . LEU A 1 199 ? 27.164 12.271 -7.917  1.00 17.97  ? 199 LEU A CG  1 
ATOM   1520 C CD1 . LEU A 1 199 ? 26.330 12.603 -9.176  1.00 19.38  ? 199 LEU A CD1 1 
ATOM   1521 C CD2 . LEU A 1 199 ? 28.620 12.006 -8.296  1.00 20.73  ? 199 LEU A CD2 1 
ATOM   1522 N N   . VAL A 1 200 ? 28.485 15.473 -4.669  1.00 18.31  ? 200 VAL A N   1 
ATOM   1523 C CA  . VAL A 1 200 ? 28.274 16.662 -3.841  1.00 20.61  ? 200 VAL A CA  1 
ATOM   1524 C C   . VAL A 1 200 ? 28.125 17.872 -4.753  1.00 21.85  ? 200 VAL A C   1 
ATOM   1525 O O   . VAL A 1 200 ? 29.015 18.162 -5.569  1.00 20.24  ? 200 VAL A O   1 
ATOM   1526 C CB  . VAL A 1 200 ? 29.421 16.865 -2.839  1.00 21.10  ? 200 VAL A CB  1 
ATOM   1527 C CG1 . VAL A 1 200 ? 29.269 18.198 -2.114  1.00 20.40  ? 200 VAL A CG1 1 
ATOM   1528 C CG2 . VAL A 1 200 ? 29.453 15.720 -1.823  1.00 22.53  ? 200 VAL A CG2 1 
ATOM   1529 N N   . PHE A 1 201 ? 26.978 18.579 -4.624  1.00 20.83  ? 201 PHE A N   1 
ATOM   1530 C CA  . PHE A 1 201 ? 26.558 19.712 -5.440  1.00 22.08  ? 201 PHE A CA  1 
ATOM   1531 C C   . PHE A 1 201 ? 26.603 21.013 -4.652  1.00 26.13  ? 201 PHE A C   1 
ATOM   1532 O O   . PHE A 1 201 ? 26.200 21.038 -3.481  1.00 24.09  ? 201 PHE A O   1 
ATOM   1533 C CB  . PHE A 1 201 ? 25.133 19.485 -5.957  1.00 18.32  ? 201 PHE A CB  1 
ATOM   1534 C CG  . PHE A 1 201 ? 25.008 18.268 -6.808  1.00 21.40  ? 201 PHE A CG  1 
ATOM   1535 C CD1 . PHE A 1 201 ? 24.601 17.069 -6.261  1.00 20.05  ? 201 PHE A CD1 1 
ATOM   1536 C CD2 . PHE A 1 201 ? 25.338 18.316 -8.158  1.00 22.86  ? 201 PHE A CD2 1 
ATOM   1537 C CE1 . PHE A 1 201 ? 24.500 15.937 -7.032  1.00 21.70  ? 201 PHE A CE1 1 
ATOM   1538 C CE2 . PHE A 1 201 ? 25.247 17.194 -8.938  1.00 22.58  ? 201 PHE A CE2 1 
ATOM   1539 C CZ  . PHE A 1 201 ? 24.830 15.999 -8.393  1.00 22.36  ? 201 PHE A CZ  1 
ATOM   1540 N N   . PRO A 1 202 ? 27.056 22.107 -5.262  1.00 26.81  ? 202 PRO A N   1 
ATOM   1541 C CA  . PRO A 1 202 ? 27.037 23.403 -4.582  1.00 24.97  ? 202 PRO A CA  1 
ATOM   1542 C C   . PRO A 1 202 ? 25.681 24.088 -4.731  1.00 27.11  ? 202 PRO A C   1 
ATOM   1543 O O   . PRO A 1 202 ? 24.772 23.603 -5.415  1.00 24.45  ? 202 PRO A O   1 
ATOM   1544 C CB  . PRO A 1 202 ? 28.140 24.188 -5.314  1.00 29.12  ? 202 PRO A CB  1 
ATOM   1545 C CG  . PRO A 1 202 ? 28.070 23.664 -6.705  1.00 26.73  ? 202 PRO A CG  1 
ATOM   1546 C CD  . PRO A 1 202 ? 27.691 22.199 -6.596  1.00 24.60  ? 202 PRO A CD  1 
ATOM   1547 N N   . LYS A 1 203 ? 25.553 25.228 -4.045  1.00 27.75  ? 203 LYS A N   1 
ATOM   1548 C CA  . LYS A 1 203 ? 24.419 26.115 -4.272  1.00 33.52  ? 203 LYS A CA  1 
ATOM   1549 C C   . LYS A 1 203 ? 24.254 26.369 -5.757  1.00 33.67  ? 203 LYS A C   1 
ATOM   1550 O O   . LYS A 1 203 ? 25.235 26.442 -6.501  1.00 32.74  ? 203 LYS A O   1 
ATOM   1551 C CB  . LYS A 1 203 ? 24.616 27.476 -3.605  1.00 37.24  ? 203 LYS A CB  1 
ATOM   1552 C CG  . LYS A 1 203 ? 24.578 27.513 -2.131  1.00 41.80  ? 203 LYS A CG  1 
ATOM   1553 C CD  A LYS A 1 203 ? 24.279 28.931 -1.662  0.46 42.61  ? 203 LYS A CD  1 
ATOM   1554 C CD  B LYS A 1 203 ? 24.721 28.957 -1.659  0.54 42.76  ? 203 LYS A CD  1 
ATOM   1555 C CE  A LYS A 1 203 ? 22.825 29.301 -1.901  0.46 42.65  ? 203 LYS A CE  1 
ATOM   1556 C CE  B LYS A 1 203 ? 26.007 29.598 -2.176  0.54 40.29  ? 203 LYS A CE  1 
ATOM   1557 N NZ  A LYS A 1 203 ? 21.957 28.728 -0.835  0.46 41.27  ? 203 LYS A NZ  1 
ATOM   1558 N NZ  B LYS A 1 203 ? 27.232 29.039 -1.521  0.54 34.27  ? 203 LYS A NZ  1 
ATOM   1559 N N   . HIS A 1 204 ? 23.004 26.548 -6.176  1.00 33.22  ? 204 HIS A N   1 
ATOM   1560 C CA  . HIS A 1 204 ? 22.588 26.962 -7.510  1.00 35.33  ? 204 HIS A CA  1 
ATOM   1561 C C   . HIS A 1 204 ? 22.689 25.834 -8.532  1.00 37.30  ? 204 HIS A C   1 
ATOM   1562 O O   . HIS A 1 204 ? 22.194 26.000 -9.642  1.00 41.48  ? 204 HIS A O   1 
ATOM   1563 C CB  . HIS A 1 204 ? 23.364 28.185 -8.042  1.00 32.88  ? 204 HIS A CB  1 
ATOM   1564 C CG  . HIS A 1 204 ? 23.391 29.337 -7.088  0.70 33.75  ? 204 HIS A CG  1 
ATOM   1565 N ND1 . HIS A 1 204 ? 22.253 30.016 -6.711  0.70 36.36  ? 204 HIS A ND1 1 
ATOM   1566 C CD2 . HIS A 1 204 ? 24.415 29.926 -6.429  0.70 35.46  ? 204 HIS A CD2 1 
ATOM   1567 C CE1 . HIS A 1 204 ? 22.575 30.975 -5.863  0.70 35.52  ? 204 HIS A CE1 1 
ATOM   1568 N NE2 . HIS A 1 204 ? 23.881 30.942 -5.676  0.70 36.44  ? 204 HIS A NE2 1 
ATOM   1569 N N   . HIS A 1 205 ? 23.293 24.696 -8.209  1.00 30.92  ? 205 HIS A N   1 
ATOM   1570 C CA  . HIS A 1 205 ? 23.163 23.535 -9.077  1.00 27.09  ? 205 HIS A CA  1 
ATOM   1571 C C   . HIS A 1 205 ? 21.800 22.880 -8.867  1.00 30.03  ? 205 HIS A C   1 
ATOM   1572 O O   . HIS A 1 205 ? 21.310 22.773 -7.741  1.00 26.61  ? 205 HIS A O   1 
ATOM   1573 C CB  . HIS A 1 205 ? 24.284 22.528 -8.818  1.00 22.79  ? 205 HIS A CB  1 
ATOM   1574 C CG  . HIS A 1 205 ? 25.583 22.887 -9.474  1.00 24.19  ? 205 HIS A CG  1 
ATOM   1575 N ND1 . HIS A 1 205 ? 26.508 21.940 -9.858  1.00 26.96  ? 205 HIS A ND1 1 
ATOM   1576 C CD2 . HIS A 1 205 ? 26.109 24.088 -9.817  1.00 28.07  ? 205 HIS A CD2 1 
ATOM   1577 C CE1 . HIS A 1 205 ? 27.551 22.542 -10.405 1.00 29.82  ? 205 HIS A CE1 1 
ATOM   1578 N NE2 . HIS A 1 205 ? 27.335 23.846 -10.392 1.00 28.15  ? 205 HIS A NE2 1 
ATOM   1579 N N   . VAL A 1 206 ? 21.189 22.431 -9.962  1.00 24.96  ? 206 VAL A N   1 
ATOM   1580 C CA  . VAL A 1 206 ? 19.868 21.820 -9.929  1.00 27.71  ? 206 VAL A CA  1 
ATOM   1581 C C   . VAL A 1 206 ? 19.991 20.383 -10.407 1.00 28.04  ? 206 VAL A C   1 
ATOM   1582 O O   . VAL A 1 206 ? 20.520 20.123 -11.495 1.00 28.20  ? 206 VAL A O   1 
ATOM   1583 C CB  . VAL A 1 206 ? 18.856 22.597 -10.791 1.00 35.54  ? 206 VAL A CB  1 
ATOM   1584 C CG1 . VAL A 1 206 ? 17.573 21.807 -10.929 1.00 37.70  ? 206 VAL A CG1 1 
ATOM   1585 C CG2 . VAL A 1 206 ? 18.581 23.973 -10.188 1.00 35.85  ? 206 VAL A CG2 1 
ATOM   1586 N N   . VAL A 1 207 ? 19.488 19.454 -9.609  1.00 22.62  ? 207 VAL A N   1 
ATOM   1587 C CA  . VAL A 1 207 ? 19.484 18.044 -9.964  1.00 25.51  ? 207 VAL A CA  1 
ATOM   1588 C C   . VAL A 1 207 ? 18.035 17.650 -10.189 1.00 25.98  ? 207 VAL A C   1 
ATOM   1589 O O   . VAL A 1 207 ? 17.205 17.787 -9.282  1.00 26.10  ? 207 VAL A O   1 
ATOM   1590 C CB  . VAL A 1 207 ? 20.140 17.187 -8.871  1.00 27.92  ? 207 VAL A CB  1 
ATOM   1591 C CG1 . VAL A 1 207 ? 20.036 15.709 -9.218  1.00 29.58  ? 207 VAL A CG1 1 
ATOM   1592 C CG2 . VAL A 1 207 ? 21.593 17.614 -8.682  1.00 26.16  ? 207 VAL A CG2 1 
ATOM   1593 N N   . SER A 1 208 ? 17.729 17.182 -11.397 1.00 20.87  ? 208 SER A N   1 
ATOM   1594 C CA  . SER A 1 208 ? 16.370 16.838 -11.807 1.00 23.22  ? 208 SER A CA  1 
ATOM   1595 C C   . SER A 1 208 ? 16.282 15.341 -12.074 1.00 30.41  ? 208 SER A C   1 
ATOM   1596 O O   . SER A 1 208 ? 17.111 14.790 -12.807 1.00 29.40  ? 208 SER A O   1 
ATOM   1597 C CB  . SER A 1 208 ? 15.976 17.623 -13.072 1.00 28.65  ? 208 SER A CB  1 
ATOM   1598 O OG  . SER A 1 208 ? 14.795 17.105 -13.657 0.67 33.42  ? 208 SER A OG  1 
ATOM   1599 N N   . LEU A 1 209 ? 15.284 14.682 -11.490 1.00 28.62  ? 209 LEU A N   1 
ATOM   1600 C CA  . LEU A 1 209 ? 15.010 13.274 -11.762 1.00 26.82  ? 209 LEU A CA  1 
ATOM   1601 C C   . LEU A 1 209 ? 13.790 13.189 -12.660 1.00 27.37  ? 209 LEU A C   1 
ATOM   1602 O O   . LEU A 1 209 ? 12.753 13.782 -12.353 1.00 29.69  ? 209 LEU A O   1 
ATOM   1603 C CB  . LEU A 1 209 ? 14.765 12.474 -10.475 1.00 24.15  ? 209 LEU A CB  1 
ATOM   1604 C CG  . LEU A 1 209 ? 15.836 12.579 -9.390  1.00 26.20  ? 209 LEU A CG  1 
ATOM   1605 C CD1 . LEU A 1 209 ? 15.497 11.680 -8.189  1.00 27.98  ? 209 LEU A CD1 1 
ATOM   1606 C CD2 . LEU A 1 209 ? 17.238 12.267 -9.948  1.00 22.92  ? 209 LEU A CD2 1 
ATOM   1607 N N   . GLN A 1 210 ? 13.912 12.465 -13.769 1.00 25.71  ? 210 GLN A N   1 
ATOM   1608 C CA  . GLN A 1 210 ? 12.831 12.397 -14.731 1.00 29.30  ? 210 GLN A CA  1 
ATOM   1609 C C   . GLN A 1 210 ? 12.457 10.944 -14.988 1.00 32.25  ? 210 GLN A C   1 
ATOM   1610 O O   . GLN A 1 210 ? 13.327 10.135 -15.342 1.00 34.14  ? 210 GLN A O   1 
ATOM   1611 C CB  . GLN A 1 210 ? 13.243 13.105 -16.041 0.80 33.46  ? 210 GLN A CB  1 
ATOM   1612 C CG  . GLN A 1 210 ? 13.505 14.588 -15.786 0.80 37.03  ? 210 GLN A CG  1 
ATOM   1613 C CD  . GLN A 1 210 ? 14.205 15.307 -16.916 0.70 36.19  ? 210 GLN A CD  1 
ATOM   1614 O OE1 . GLN A 1 210 ? 14.183 14.869 -18.064 0.70 32.64  ? 210 GLN A OE1 1 
ATOM   1615 N NE2 . GLN A 1 210 ? 14.831 16.435 -16.589 0.70 38.74  ? 210 GLN A NE2 1 
ATOM   1616 N N   . PRO A 1 211 ? 11.192 10.570 -14.819 1.00 35.30  ? 211 PRO A N   1 
ATOM   1617 C CA  . PRO A 1 211 ? 10.822 9.162  -14.968 1.00 36.49  ? 211 PRO A CA  1 
ATOM   1618 C C   . PRO A 1 211 ? 10.993 8.689  -16.400 1.00 35.68  ? 211 PRO A C   1 
ATOM   1619 O O   . PRO A 1 211 ? 10.861 9.454  -17.361 1.00 34.29  ? 211 PRO A O   1 
ATOM   1620 C CB  . PRO A 1 211 ? 9.352  9.129  -14.541 1.00 43.02  ? 211 PRO A CB  1 
ATOM   1621 C CG  . PRO A 1 211 ? 8.872  10.530 -14.731 1.00 44.73  ? 211 PRO A CG  1 
ATOM   1622 C CD  . PRO A 1 211 ? 10.038 11.429 -14.487 1.00 39.50  ? 211 PRO A CD  1 
ATOM   1623 N N   . VAL A 1 212 ? 11.284 7.402  -16.527 0.80 34.44  ? 212 VAL A N   1 
ATOM   1624 C CA  . VAL A 1 212 ? 11.482 6.765  -17.821 0.80 33.42  ? 212 VAL A CA  1 
ATOM   1625 C C   . VAL A 1 212 ? 10.253 5.976  -18.241 0.80 37.95  ? 212 VAL A C   1 
ATOM   1626 O O   . VAL A 1 212 ? 9.785  6.100  -19.372 0.80 35.71  ? 212 VAL A O   1 
ATOM   1627 C CB  . VAL A 1 212 ? 12.747 5.881  -17.775 0.80 29.97  ? 212 VAL A CB  1 
ATOM   1628 C CG1 . VAL A 1 212 ? 12.937 5.134  -19.076 0.80 33.02  ? 212 VAL A CG1 1 
ATOM   1629 C CG2 . VAL A 1 212 ? 13.951 6.752  -17.468 0.80 26.83  ? 212 VAL A CG2 1 
ATOM   1630 N N   . ASN A 1 213 ? 9.700  5.180  -17.325 1.00 40.59  ? 213 ASN A N   1 
ATOM   1631 C CA  . ASN A 1 213 ? 8.480  4.424  -17.581 1.00 48.79  ? 213 ASN A CA  1 
ATOM   1632 C C   . ASN A 1 213 ? 7.420  4.725  -16.526 1.00 51.78  ? 213 ASN A C   1 
ATOM   1633 O O   . ASN A 1 213 ? 6.545  5.565  -16.751 1.00 55.37  ? 213 ASN A O   1 
ATOM   1634 C CB  . ASN A 1 213 ? 8.780  2.927  -17.635 0.80 52.09  ? 213 ASN A CB  1 
ATOM   1635 C CG  . ASN A 1 213 ? 9.258  2.484  -19.001 0.50 56.17  ? 213 ASN A CG  1 
ATOM   1636 O OD1 . ASN A 1 213 ? 8.468  2.359  -19.935 0.50 59.05  ? 213 ASN A OD1 1 
ATOM   1637 N ND2 . ASN A 1 213 ? 10.561 2.255  -19.129 0.50 57.15  ? 213 ASN A ND2 1 
ATOM   1638 N N   . ASP A 1 214 ? 7.478  4.046  -15.384 1.00 49.38  ? 214 ASP A N   1 
ATOM   1639 C CA  . ASP A 1 214 ? 6.532  4.324  -14.308 1.00 52.17  ? 214 ASP A CA  1 
ATOM   1640 C C   . ASP A 1 214 ? 6.684  5.765  -13.832 1.00 45.32  ? 214 ASP A C   1 
ATOM   1641 O O   . ASP A 1 214 ? 7.791  6.305  -13.772 1.00 44.21  ? 214 ASP A O   1 
ATOM   1642 C CB  . ASP A 1 214 ? 6.749  3.350  -13.143 1.00 55.66  ? 214 ASP A CB  1 
ATOM   1643 C CG  . ASP A 1 214 ? 5.735  3.533  -12.015 0.88 61.73  ? 214 ASP A CG  1 
ATOM   1644 O OD1 . ASP A 1 214 ? 4.706  4.208  -12.222 0.77 66.33  ? 214 ASP A OD1 1 
ATOM   1645 O OD2 . ASP A 1 214 ? 5.971  2.996  -10.909 0.76 65.16  ? 214 ASP A OD2 1 
ATOM   1646 N N   . LYS A 1 215 ? 5.561  6.394  -13.498 1.00 45.39  ? 215 LYS A N   1 
ATOM   1647 C CA  . LYS A 1 215 ? 5.558  7.790  -13.081 1.00 43.20  ? 215 LYS A CA  1 
ATOM   1648 C C   . LYS A 1 215 ? 5.096  7.978  -11.640 1.00 40.51  ? 215 LYS A C   1 
ATOM   1649 O O   . LYS A 1 215 ? 4.885  9.118  -11.213 1.00 38.88  ? 215 LYS A O   1 
ATOM   1650 C CB  . LYS A 1 215 ? 4.681  8.612  -14.029 1.00 45.00  ? 215 LYS A CB  1 
ATOM   1651 C CG  . LYS A 1 215 ? 5.169  8.591  -15.471 1.00 48.59  ? 215 LYS A CG  1 
ATOM   1652 C CD  . LYS A 1 215 ? 4.264  9.421  -16.385 1.00 56.82  ? 215 LYS A CD  1 
ATOM   1653 C CE  . LYS A 1 215 ? 4.432  10.921 -16.150 0.76 59.01  ? 215 LYS A CE  1 
ATOM   1654 N NZ  . LYS A 1 215 ? 3.360  11.717 -16.823 0.77 64.73  ? 215 LYS A NZ  1 
ATOM   1655 N N   . ASP A 1 216 ? 4.922  6.900  -10.883 1.00 39.44  ? 216 ASP A N   1 
ATOM   1656 C CA  . ASP A 1 216 ? 4.524  6.981  -9.483  1.00 36.81  ? 216 ASP A CA  1 
ATOM   1657 C C   . ASP A 1 216 ? 5.740  6.698  -8.614  1.00 35.44  ? 216 ASP A C   1 
ATOM   1658 O O   . ASP A 1 216 ? 6.475  5.734  -8.864  1.00 37.41  ? 216 ASP A O   1 
ATOM   1659 C CB  . ASP A 1 216 ? 3.412  5.995  -9.157  1.00 34.81  ? 216 ASP A CB  1 
ATOM   1660 C CG  . ASP A 1 216 ? 2.161  6.238  -9.963  1.00 42.00  ? 216 ASP A CG  1 
ATOM   1661 O OD1 . ASP A 1 216 ? 2.102  7.241  -10.707 1.00 45.44  ? 216 ASP A OD1 1 
ATOM   1662 O OD2 . ASP A 1 216 ? 1.233  5.415  -9.855  1.00 46.67  ? 216 ASP A OD2 1 
ATOM   1663 N N   . PHE A 1 217 ? 5.955  7.538  -7.602  1.00 34.31  ? 217 PHE A N   1 
ATOM   1664 C CA  . PHE A 1 217 ? 7.117  7.400  -6.737  1.00 29.36  ? 217 PHE A CA  1 
ATOM   1665 C C   . PHE A 1 217 ? 6.738  7.630  -5.287  1.00 33.61  ? 217 PHE A C   1 
ATOM   1666 O O   . PHE A 1 217 ? 5.826  8.404  -4.982  1.00 29.71  ? 217 PHE A O   1 
ATOM   1667 C CB  . PHE A 1 217 ? 8.208  8.396  -7.107  1.00 31.08  ? 217 PHE A CB  1 
ATOM   1668 C CG  . PHE A 1 217 ? 8.627  8.296  -8.529  1.00 31.22  ? 217 PHE A CG  1 
ATOM   1669 C CD1 . PHE A 1 217 ? 9.685  7.477  -8.889  1.00 28.58  ? 217 PHE A CD1 1 
ATOM   1670 C CD2 . PHE A 1 217 ? 7.959  9.004  -9.508  1.00 33.90  ? 217 PHE A CD2 1 
ATOM   1671 C CE1 . PHE A 1 217 ? 10.082 7.368  -10.207 1.00 28.63  ? 217 PHE A CE1 1 
ATOM   1672 C CE2 . PHE A 1 217 ? 8.343  8.901  -10.840 1.00 33.68  ? 217 PHE A CE2 1 
ATOM   1673 C CZ  . PHE A 1 217 ? 9.404  8.083  -11.188 1.00 32.94  ? 217 PHE A CZ  1 
ATOM   1674 N N   . GLN A 1 218 ? 7.486  6.981  -4.397  1.00 27.97  ? 218 GLN A N   1 
ATOM   1675 C CA  . GLN A 1 218 ? 7.391  7.212  -2.961  1.00 29.43  ? 218 GLN A CA  1 
ATOM   1676 C C   . GLN A 1 218 ? 8.474  8.220  -2.608  1.00 31.65  ? 218 GLN A C   1 
ATOM   1677 O O   . GLN A 1 218 ? 9.667  7.919  -2.722  1.00 28.75  ? 218 GLN A O   1 
ATOM   1678 C CB  . GLN A 1 218 ? 7.575  5.907  -2.192  1.00 35.94  ? 218 GLN A CB  1 
ATOM   1679 C CG  . GLN A 1 218 ? 7.210  5.991  -0.712  0.85 36.75  ? 218 GLN A CG  1 
ATOM   1680 C CD  . GLN A 1 218 ? 5.720  5.880  -0.508  0.81 40.63  ? 218 GLN A CD  1 
ATOM   1681 O OE1 . GLN A 1 218 ? 5.020  5.287  -1.330  0.74 40.36  ? 218 GLN A OE1 1 
ATOM   1682 N NE2 . GLN A 1 218 ? 5.219  6.459  0.578   0.74 43.58  ? 218 GLN A NE2 1 
ATOM   1683 N N   . ILE A 1 219 ? 8.074  9.434  -2.240  1.00 25.67  ? 219 ILE A N   1 
ATOM   1684 C CA  . ILE A 1 219 ? 9.020  10.503 -1.951  1.00 24.31  ? 219 ILE A CA  1 
ATOM   1685 C C   . ILE A 1 219 ? 8.993  10.763 -0.453  1.00 23.92  ? 219 ILE A C   1 
ATOM   1686 O O   . ILE A 1 219 ? 7.925  10.986 0.125   1.00 28.31  ? 219 ILE A O   1 
ATOM   1687 C CB  . ILE A 1 219 ? 8.702  11.777 -2.747  1.00 30.93  ? 219 ILE A CB  1 
ATOM   1688 C CG1 . ILE A 1 219 ? 8.705  11.449 -4.251  1.00 29.70  ? 219 ILE A CG1 1 
ATOM   1689 C CG2 . ILE A 1 219 ? 9.727  12.856 -2.406  1.00 30.59  ? 219 ILE A CG2 1 
ATOM   1690 C CD1 . ILE A 1 219 ? 8.254  12.572 -5.135  1.00 32.17  ? 219 ILE A CD1 1 
ATOM   1691 N N   . SER A 1 220 ? 10.155 10.700 0.177   1.00 22.60  ? 220 SER A N   1 
ATOM   1692 C CA  . SER A 1 220 ? 10.276 10.981 1.599   1.00 27.69  ? 220 SER A CA  1 
ATOM   1693 C C   . SER A 1 220 ? 10.977 12.319 1.775   1.00 32.58  ? 220 SER A C   1 
ATOM   1694 O O   . SER A 1 220 ? 11.871 12.669 0.997   1.00 33.31  ? 220 SER A O   1 
ATOM   1695 C CB  . SER A 1 220 ? 11.068 9.897  2.302   1.00 25.93  ? 220 SER A CB  1 
ATOM   1696 O OG  . SER A 1 220 ? 12.454 10.163 2.077   1.00 31.80  ? 220 SER A OG  1 
ATOM   1697 N N   . VAL A 1 221 ? 10.548 13.084 2.774   1.00 26.17  ? 221 VAL A N   1 
ATOM   1698 C CA  . VAL A 1 221 ? 11.255 14.280 3.209   1.00 23.88  ? 221 VAL A CA  1 
ATOM   1699 C C   . VAL A 1 221 ? 11.414 14.124 4.711   1.00 27.67  ? 221 VAL A C   1 
ATOM   1700 O O   . VAL A 1 221 ? 10.420 14.147 5.437   1.00 27.38  ? 221 VAL A O   1 
ATOM   1701 C CB  . VAL A 1 221 ? 10.500 15.575 2.881   1.00 30.70  ? 221 VAL A CB  1 
ATOM   1702 C CG1 . VAL A 1 221 ? 11.220 16.769 3.510   1.00 32.33  ? 221 VAL A CG1 1 
ATOM   1703 C CG2 . VAL A 1 221 ? 10.353 15.765 1.375   1.00 33.78  ? 221 VAL A CG2 1 
ATOM   1704 N N   . ASP A 1 222 ? 12.642 13.932 5.175   1.00 23.48  ? 222 ASP A N   1 
ATOM   1705 C CA  . ASP A 1 222 ? 12.882 13.679 6.597   1.00 27.31  ? 222 ASP A CA  1 
ATOM   1706 C C   . ASP A 1 222 ? 12.009 12.498 7.021   1.00 29.26  ? 222 ASP A C   1 
ATOM   1707 O O   . ASP A 1 222 ? 11.995 11.459 6.348   1.00 28.73  ? 222 ASP A O   1 
ATOM   1708 C CB  . ASP A 1 222 ? 12.652 14.976 7.376   1.00 23.27  ? 222 ASP A CB  1 
ATOM   1709 C CG  . ASP A 1 222 ? 13.667 16.051 7.029   1.00 21.81  ? 222 ASP A CG  1 
ATOM   1710 O OD1 . ASP A 1 222 ? 14.759 15.683 6.551   1.00 25.27  ? 222 ASP A OD1 1 
ATOM   1711 O OD2 . ASP A 1 222 ? 13.395 17.255 7.255   1.00 27.75  ? 222 ASP A OD2 1 
ATOM   1712 N N   . HIS A 1 223 ? 11.223 12.619 8.085   1.00 28.14  ? 223 HIS A N   1 
ATOM   1713 C CA  A HIS A 1 223 ? 10.472 11.491 8.619   0.50 37.55  ? 223 HIS A CA  1 
ATOM   1714 C CA  B HIS A 1 223 ? 10.471 11.492 8.621   0.50 37.55  ? 223 HIS A CA  1 
ATOM   1715 C C   . HIS A 1 223 ? 9.250  11.111 7.785   1.00 41.35  ? 223 HIS A C   1 
ATOM   1716 O O   . HIS A 1 223 ? 8.672  10.043 8.021   1.00 47.84  ? 223 HIS A O   1 
ATOM   1717 C CB  A HIS A 1 223 ? 10.034 11.824 10.048  0.30 42.08  ? 223 HIS A CB  1 
ATOM   1718 C CB  B HIS A 1 223 ? 10.037 11.826 10.054  0.50 42.12  ? 223 HIS A CB  1 
ATOM   1719 C CG  A HIS A 1 223 ? 9.455  13.198 10.185  0.20 45.88  ? 223 HIS A CG  1 
ATOM   1720 C CG  B HIS A 1 223 ? 9.484  13.212 10.204  0.50 45.95  ? 223 HIS A CG  1 
ATOM   1721 N ND1 A HIS A 1 223 ? 10.206 14.341 10.011  0.20 45.80  ? 223 HIS A ND1 1 
ATOM   1722 N ND1 B HIS A 1 223 ? 10.219 14.342 9.911   0.50 45.44  ? 223 HIS A ND1 1 
ATOM   1723 C CD2 A HIS A 1 223 ? 8.200  13.614 10.477  0.20 48.48  ? 223 HIS A CD2 1 
ATOM   1724 C CD2 B HIS A 1 223 ? 8.272  13.649 10.622  0.50 48.62  ? 223 HIS A CD2 1 
ATOM   1725 C CE1 A HIS A 1 223 ? 9.438  15.401 10.187  0.20 47.12  ? 223 HIS A CE1 1 
ATOM   1726 C CE1 B HIS A 1 223 ? 9.481  15.414 10.131  0.50 47.25  ? 223 HIS A CE1 1 
ATOM   1727 N NE2 A HIS A 1 223 ? 8.216  14.987 10.472  0.20 48.63  ? 223 HIS A NE2 1 
ATOM   1728 N NE2 B HIS A 1 223 ? 8.297  15.022 10.568  0.50 48.94  ? 223 HIS A NE2 1 
ATOM   1729 N N   . LEU A 1 224 ? 8.846  11.936 6.822   1.00 32.82  ? 224 LEU A N   1 
ATOM   1730 C CA  . LEU A 1 224 ? 7.560  11.782 6.154   1.00 29.65  ? 224 LEU A CA  1 
ATOM   1731 C C   . LEU A 1 224 ? 7.730  11.206 4.752   1.00 35.23  ? 224 LEU A C   1 
ATOM   1732 O O   . LEU A 1 224 ? 8.623  11.615 4.008   1.00 35.81  ? 224 LEU A O   1 
ATOM   1733 C CB  . LEU A 1 224 ? 6.855  13.133 6.067   1.00 31.05  ? 224 LEU A CB  1 
ATOM   1734 C CG  . LEU A 1 224 ? 5.479  13.181 5.395   0.78 36.07  ? 224 LEU A CG  1 
ATOM   1735 C CD1 . LEU A 1 224 ? 4.478  12.252 6.093   0.54 34.70  ? 224 LEU A CD1 1 
ATOM   1736 C CD2 . LEU A 1 224 ? 4.963  14.611 5.355   0.55 35.50  ? 224 LEU A CD2 1 
ATOM   1737 N N   . SER A 1 225 ? 6.856  10.272 4.392   1.00 35.20  ? 225 SER A N   1 
ATOM   1738 C CA  . SER A 1 225 ? 6.931  9.559  3.123   1.00 38.86  ? 225 SER A CA  1 
ATOM   1739 C C   . SER A 1 225 ? 5.556  9.567  2.467   1.00 39.86  ? 225 SER A C   1 
ATOM   1740 O O   . SER A 1 225 ? 4.580  9.111  3.071   1.00 42.02  ? 225 SER A O   1 
ATOM   1741 C CB  . SER A 1 225 ? 7.426  8.127  3.344   1.00 40.13  ? 225 SER A CB  1 
ATOM   1742 O OG  . SER A 1 225 ? 7.499  7.409  2.130   1.00 42.54  ? 225 SER A OG  1 
ATOM   1743 N N   . ILE A 1 226 ? 5.476  10.086 1.236   1.00 39.18  ? 226 ILE A N   1 
ATOM   1744 C CA  . ILE A 1 226 ? 4.206  10.266 0.534   1.00 40.00  ? 226 ILE A CA  1 
ATOM   1745 C C   . ILE A 1 226 ? 4.287  9.567  -0.816  1.00 38.83  ? 226 ILE A C   1 
ATOM   1746 O O   . ILE A 1 226 ? 5.317  9.630  -1.497  1.00 32.51  ? 226 ILE A O   1 
ATOM   1747 C CB  . ILE A 1 226 ? 3.876  11.761 0.324   0.80 44.38  ? 226 ILE A CB  1 
ATOM   1748 C CG1 . ILE A 1 226 ? 4.020  12.551 1.629   0.70 48.38  ? 226 ILE A CG1 1 
ATOM   1749 C CG2 . ILE A 1 226 ? 2.486  11.928 -0.271  0.70 46.88  ? 226 ILE A CG2 1 
ATOM   1750 C CD1 . ILE A 1 226 ? 4.894  13.791 1.481   0.70 50.45  ? 226 ILE A CD1 1 
ATOM   1751 N N   . LEU A 1 227 ? 3.200  8.918  -1.217  0.84 32.44  ? 227 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 227 ? 3.102  8.421  -2.582  0.84 37.37  ? 227 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 227 ? 2.634  9.550  -3.490  0.84 40.70  ? 227 LEU A C   1 
ATOM   1754 O O   . LEU A 1 227 ? 1.521  10.059 -3.328  0.84 44.32  ? 227 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 227 ? 2.144  7.238  -2.658  0.84 39.54  ? 227 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 227 ? 1.727  6.821  -4.069  0.84 41.62  ? 227 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 227 ? 2.916  6.288  -4.833  0.84 43.95  ? 227 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 227 ? 0.632  5.781  -4.010  0.84 46.20  ? 227 LEU A CD2 1 
ATOM   1759 N N   . HIS A 1 228 ? 3.482  9.944  -4.440  1.00 39.73  ? 228 HIS A N   1 
ATOM   1760 C CA  . HIS A 1 228 ? 3.132  10.923 -5.464  1.00 43.75  ? 228 HIS A CA  1 
ATOM   1761 C C   . HIS A 1 228 ? 2.836  10.198 -6.771  1.00 43.76  ? 228 HIS A C   1 
ATOM   1762 O O   . HIS A 1 228 ? 3.616  9.336  -7.193  1.00 42.10  ? 228 HIS A O   1 
ATOM   1763 C CB  . HIS A 1 228 ? 4.263  11.933 -5.679  1.00 43.14  ? 228 HIS A CB  1 
ATOM   1764 C CG  . HIS A 1 228 ? 4.539  12.799 -4.491  1.00 43.48  ? 228 HIS A CG  1 
ATOM   1765 N ND1 . HIS A 1 228 ? 4.248  14.146 -4.470  1.00 44.53  ? 228 HIS A ND1 1 
ATOM   1766 C CD2 . HIS A 1 228 ? 5.073  12.510 -3.280  1.00 44.64  ? 228 HIS A CD2 1 
ATOM   1767 C CE1 . HIS A 1 228 ? 4.595  14.650 -3.299  1.00 45.46  ? 228 HIS A CE1 1 
ATOM   1768 N NE2 . HIS A 1 228 ? 5.096  13.678 -2.557  1.00 43.19  ? 228 HIS A NE2 1 
ATOM   1769 N N   . ARG A 1 229 ? 1.725  10.555 -7.413  1.00 43.79  ? 229 ARG A N   1 
ATOM   1770 C CA  . ARG A 1 229 ? 1.321  9.950  -8.675  1.00 43.99  ? 229 ARG A CA  1 
ATOM   1771 C C   . ARG A 1 229 ? 1.469  10.939 -9.825  1.00 43.26  ? 229 ARG A C   1 
ATOM   1772 O O   . ARG A 1 229 ? 1.371  12.154 -9.639  1.00 43.81  ? 229 ARG A O   1 
ATOM   1773 C CB  . ARG A 1 229 ? -0.128 9.458  -8.616  1.00 46.32  ? 229 ARG A CB  1 
ATOM   1774 C CG  . ARG A 1 229 ? -0.354 8.308  -7.655  0.90 45.20  ? 229 ARG A CG  1 
ATOM   1775 C CD  . ARG A 1 229 ? -1.791 7.844  -7.727  0.70 46.35  ? 229 ARG A CD  1 
ATOM   1776 N NE  . ARG A 1 229 ? -2.129 6.970  -6.613  0.60 51.46  ? 229 ARG A NE  1 
ATOM   1777 C CZ  . ARG A 1 229 ? -1.966 5.653  -6.623  0.50 58.93  ? 229 ARG A CZ  1 
ATOM   1778 N NH1 . ARG A 1 229 ? -1.466 5.051  -7.693  0.50 61.01  ? 229 ARG A NH1 1 
ATOM   1779 N NH2 . ARG A 1 229 ? -2.304 4.938  -5.559  0.50 63.16  ? 229 ARG A NH2 1 
ATOM   1780 N N   . ASP A 1 230 ? 1.701  10.394 -11.023 1.00 45.27  ? 230 ASP A N   1 
ATOM   1781 C CA  . ASP A 1 230 ? 1.771  11.180 -12.258 1.00 46.75  ? 230 ASP A CA  1 
ATOM   1782 C C   . ASP A 1 230 ? 2.875  12.233 -12.184 1.00 46.86  ? 230 ASP A C   1 
ATOM   1783 O O   . ASP A 1 230 ? 2.676  13.398 -12.537 1.00 47.80  ? 230 ASP A O   1 
ATOM   1784 C CB  . ASP A 1 230 ? 0.420  11.826 -12.576 0.70 43.97  ? 230 ASP A CB  1 
ATOM   1785 C CG  . ASP A 1 230 ? 0.352  12.366 -13.984 0.50 44.09  ? 230 ASP A CG  1 
ATOM   1786 O OD1 . ASP A 1 230 ? 1.054  11.829 -14.869 0.50 44.18  ? 230 ASP A OD1 1 
ATOM   1787 O OD2 . ASP A 1 230 ? -0.398 13.338 -14.201 0.50 46.55  ? 230 ASP A OD2 1 
ATOM   1788 N N   . VAL A 1 231 ? 4.051  11.821 -11.714 1.00 41.32  ? 231 VAL A N   1 
ATOM   1789 C CA  . VAL A 1 231 ? 5.168  12.743 -11.546 1.00 33.83  ? 231 VAL A CA  1 
ATOM   1790 C C   . VAL A 1 231 ? 5.843  12.971 -12.892 1.00 38.67  ? 231 VAL A C   1 
ATOM   1791 O O   . VAL A 1 231 ? 6.111  12.020 -13.637 1.00 39.03  ? 231 VAL A O   1 
ATOM   1792 C CB  . VAL A 1 231 ? 6.169  12.205 -10.509 1.00 35.62  ? 231 VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 231 ? 7.467  12.937 -10.632 1.00 33.84  ? 231 VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 231 ? 5.612  12.371 -9.102  1.00 37.34  ? 231 VAL A CG2 1 
ATOM   1795 N N   . GLN A 1 232 ? 6.105  14.243 -13.212 1.00 36.46  ? 232 GLN A N   1 
ATOM   1796 C CA  . GLN A 1 232 ? 6.883  14.615 -14.387 1.00 38.00  ? 232 GLN A CA  1 
ATOM   1797 C C   . GLN A 1 232 ? 8.346  14.859 -14.054 1.00 39.67  ? 232 GLN A C   1 
ATOM   1798 O O   . GLN A 1 232 ? 9.222  14.613 -14.897 1.00 42.57  ? 232 GLN A O   1 
ATOM   1799 C CB  . GLN A 1 232 ? 6.295  15.875 -15.029 1.00 38.59  ? 232 GLN A CB  1 
ATOM   1800 N N   . GLU A 1 233 ? 8.633  15.320 -12.837 1.00 36.21  ? 233 GLU A N   1 
ATOM   1801 C CA  . GLU A 1 233 ? 9.983  15.738 -12.489 1.00 34.96  ? 233 GLU A CA  1 
ATOM   1802 C C   . GLU A 1 233 ? 10.080 15.889 -10.984 1.00 35.83  ? 233 GLU A C   1 
ATOM   1803 O O   . GLU A 1 233 ? 9.129  16.347 -10.340 1.00 33.72  ? 233 GLU A O   1 
ATOM   1804 C CB  . GLU A 1 233 ? 10.327 17.070 -13.166 0.90 40.67  ? 233 GLU A CB  1 
ATOM   1805 C CG  . GLU A 1 233 ? 11.769 17.494 -13.058 0.80 41.72  ? 233 GLU A CG  1 
ATOM   1806 C CD  . GLU A 1 233 ? 11.997 18.890 -13.600 0.70 42.19  ? 233 GLU A CD  1 
ATOM   1807 O OE1 . GLU A 1 233 ? 11.009 19.611 -13.815 0.70 45.01  ? 233 GLU A OE1 1 
ATOM   1808 O OE2 . GLU A 1 233 ? 13.164 19.268 -13.814 0.70 45.00  ? 233 GLU A OE2 1 
ATOM   1809 N N   . ILE A 1 234 ? 11.225 15.498 -10.433 1.00 30.54  ? 234 ILE A N   1 
ATOM   1810 C CA  . ILE A 1 234 ? 11.599 15.836 -9.069  1.00 29.13  ? 234 ILE A CA  1 
ATOM   1811 C C   . ILE A 1 234 ? 12.876 16.655 -9.149  1.00 31.57  ? 234 ILE A C   1 
ATOM   1812 O O   . ILE A 1 234 ? 13.840 16.245 -9.809  1.00 35.45  ? 234 ILE A O   1 
ATOM   1813 C CB  . ILE A 1 234 ? 11.804 14.590 -8.189  1.00 32.34  ? 234 ILE A CB  1 
ATOM   1814 C CG1 . ILE A 1 234 ? 10.545 13.724 -8.179  1.00 35.66  ? 234 ILE A CG1 1 
ATOM   1815 C CG2 . ILE A 1 234 ? 12.191 15.022 -6.773  1.00 29.27  ? 234 ILE A CG2 1 
ATOM   1816 C CD1 . ILE A 1 234 ? 10.824 12.257 -8.010  1.00 37.51  ? 234 ILE A CD1 1 
ATOM   1817 N N   . ARG A 1 235 ? 12.872 17.812 -8.496  1.00 26.90  ? 235 ARG A N   1 
ATOM   1818 C CA  . ARG A 1 235 ? 13.927 18.805 -8.619  1.00 27.97  ? 235 ARG A CA  1 
ATOM   1819 C C   . ARG A 1 235 ? 14.548 19.062 -7.252  1.00 26.29  ? 235 ARG A C   1 
ATOM   1820 O O   . ARG A 1 235 ? 13.835 19.388 -6.299  1.00 25.61  ? 235 ARG A O   1 
ATOM   1821 C CB  . ARG A 1 235 ? 13.352 20.092 -9.188  1.00 35.80  ? 235 ARG A CB  1 
ATOM   1822 C CG  . ARG A 1 235 ? 14.360 21.001 -9.797  1.00 42.42  ? 235 ARG A CG  1 
ATOM   1823 C CD  . ARG A 1 235 ? 13.888 21.495 -11.149 0.70 45.92  ? 235 ARG A CD  1 
ATOM   1824 N NE  . ARG A 1 235 ? 12.667 22.291 -11.088 0.60 48.70  ? 235 ARG A NE  1 
ATOM   1825 C CZ  . ARG A 1 235 ? 12.586 23.501 -10.540 0.50 53.80  ? 235 ARG A CZ  1 
ATOM   1826 N NH1 . ARG A 1 235 ? 11.431 24.155 -10.544 0.50 54.44  ? 235 ARG A NH1 1 
ATOM   1827 N NH2 . ARG A 1 235 ? 13.654 24.056 -9.971  0.50 52.68  ? 235 ARG A NH2 1 
ATOM   1828 N N   . TYR A 1 236 ? 15.871 18.936 -7.166  1.00 22.57  ? 236 TYR A N   1 
ATOM   1829 C CA  . TYR A 1 236 ? 16.615 19.174 -5.930  1.00 25.90  ? 236 TYR A CA  1 
ATOM   1830 C C   . TYR A 1 236 ? 17.547 20.362 -6.095  1.00 28.08  ? 236 TYR A C   1 
ATOM   1831 O O   . TYR A 1 236 ? 18.234 20.487 -7.115  1.00 26.39  ? 236 TYR A O   1 
ATOM   1832 C CB  . TYR A 1 236 ? 17.447 17.955 -5.524  1.00 26.98  ? 236 TYR A CB  1 
ATOM   1833 C CG  . TYR A 1 236 ? 16.624 16.768 -5.122  1.00 26.95  ? 236 TYR A CG  1 
ATOM   1834 C CD1 . TYR A 1 236 ? 15.771 16.841 -4.028  1.00 27.86  ? 236 TYR A CD1 1 
ATOM   1835 C CD2 . TYR A 1 236 ? 16.686 15.575 -5.837  1.00 30.40  ? 236 TYR A CD2 1 
ATOM   1836 C CE1 . TYR A 1 236 ? 15.021 15.756 -3.642  1.00 28.76  ? 236 TYR A CE1 1 
ATOM   1837 C CE2 . TYR A 1 236 ? 15.930 14.483 -5.452  1.00 32.50  ? 236 TYR A CE2 1 
ATOM   1838 C CZ  . TYR A 1 236 ? 15.101 14.587 -4.355  1.00 33.77  ? 236 TYR A CZ  1 
ATOM   1839 O OH  . TYR A 1 236 ? 14.332 13.526 -3.949  1.00 45.46  ? 236 TYR A OH  1 
ATOM   1840 N N   . GLU A 1 237 ? 17.588 21.212 -5.073  1.00 26.31  ? 237 GLU A N   1 
ATOM   1841 C CA  . GLU A 1 237 ? 18.485 22.356 -5.035  1.00 23.69  ? 237 GLU A CA  1 
ATOM   1842 C C   . GLU A 1 237 ? 18.705 22.736 -3.571  1.00 23.12  ? 237 GLU A C   1 
ATOM   1843 O O   . GLU A 1 237 ? 17.834 22.501 -2.726  1.00 21.54  ? 237 GLU A O   1 
ATOM   1844 C CB  A GLU A 1 237 ? 17.938 23.548 -5.833  0.57 26.85  ? 237 GLU A CB  1 
ATOM   1845 C CB  B GLU A 1 237 ? 17.900 23.537 -5.817  0.43 26.89  ? 237 GLU A CB  1 
ATOM   1846 C CG  A GLU A 1 237 ? 16.479 23.860 -5.590  0.57 30.22  ? 237 GLU A CG  1 
ATOM   1847 C CG  B GLU A 1 237 ? 18.880 24.659 -6.077  0.43 28.97  ? 237 GLU A CG  1 
ATOM   1848 C CD  A GLU A 1 237 ? 15.835 24.570 -6.776  0.57 34.16  ? 237 GLU A CD  1 
ATOM   1849 C CD  B GLU A 1 237 ? 18.268 25.797 -6.864  0.43 33.49  ? 237 GLU A CD  1 
ATOM   1850 O OE1 A GLU A 1 237 ? 16.274 25.686 -7.115  0.57 35.36  ? 237 GLU A OE1 1 
ATOM   1851 O OE1 B GLU A 1 237 ? 17.198 25.578 -7.473  0.43 34.74  ? 237 GLU A OE1 1 
ATOM   1852 O OE2 A GLU A 1 237 ? 14.901 24.005 -7.385  0.57 34.12  ? 237 GLU A OE2 1 
ATOM   1853 O OE2 B GLU A 1 237 ? 18.854 26.903 -6.872  0.43 31.24  ? 237 GLU A OE2 1 
ATOM   1854 N N   . VAL A 1 238 ? 19.876 23.303 -3.281  1.00 24.24  ? 238 VAL A N   1 
ATOM   1855 C CA  . VAL A 1 238 ? 20.116 23.861 -1.953  1.00 27.94  ? 238 VAL A CA  1 
ATOM   1856 C C   . VAL A 1 238 ? 19.160 25.026 -1.734  1.00 31.47  ? 238 VAL A C   1 
ATOM   1857 O O   . VAL A 1 238 ? 19.086 25.963 -2.543  1.00 30.49  ? 238 VAL A O   1 
ATOM   1858 C CB  . VAL A 1 238 ? 21.585 24.275 -1.793  1.00 25.15  ? 238 VAL A CB  1 
ATOM   1859 C CG1 . VAL A 1 238 ? 21.820 24.905 -0.398  1.00 26.39  ? 238 VAL A CG1 1 
ATOM   1860 C CG2 . VAL A 1 238 ? 22.476 23.062 -1.961  1.00 21.77  ? 238 VAL A CG2 1 
ATOM   1861 N N   . SER A 1 239 ? 18.400 24.961 -0.647  1.00 27.52  ? 239 SER A N   1 
ATOM   1862 C CA  . SER A 1 239 ? 17.430 26.012 -0.368  1.00 28.01  ? 239 SER A CA  1 
ATOM   1863 C C   . SER A 1 239 ? 18.129 27.332 -0.075  1.00 29.75  ? 239 SER A C   1 
ATOM   1864 O O   . SER A 1 239 ? 19.260 27.366 0.412   1.00 33.17  ? 239 SER A O   1 
ATOM   1865 C CB  . SER A 1 239 ? 16.548 25.620 0.822   1.00 26.43  ? 239 SER A CB  1 
ATOM   1866 O OG  . SER A 1 239 ? 15.682 26.685 1.190   1.00 32.09  ? 239 SER A OG  1 
ATOM   1867 N N   . ALA A 1 240 ? 17.439 28.433 -0.386  1.00 30.44  ? 240 ALA A N   1 
ATOM   1868 C CA  . ALA A 1 240 ? 17.858 29.735 0.120   1.00 31.59  ? 240 ALA A CA  1 
ATOM   1869 C C   . ALA A 1 240 ? 17.527 29.914 1.597   1.00 34.98  ? 240 ALA A C   1 
ATOM   1870 O O   . ALA A 1 240 ? 18.064 30.827 2.230   1.00 34.85  ? 240 ALA A O   1 
ATOM   1871 C CB  . ALA A 1 240 ? 17.200 30.857 -0.680  1.00 36.28  ? 240 ALA A CB  1 
ATOM   1872 N N   . LYS A 1 241 ? 16.649 29.077 2.149   1.00 36.84  ? 241 LYS A N   1 
ATOM   1873 C CA  . LYS A 1 241 ? 16.291 29.146 3.561   1.00 34.83  ? 241 LYS A CA  1 
ATOM   1874 C C   . LYS A 1 241 ? 17.294 28.366 4.402   1.00 31.87  ? 241 LYS A C   1 
ATOM   1875 O O   . LYS A 1 241 ? 17.894 27.391 3.945   1.00 28.88  ? 241 LYS A O   1 
ATOM   1876 C CB  . LYS A 1 241 ? 14.880 28.592 3.778   1.00 33.95  ? 241 LYS A CB  1 
ATOM   1877 C CG  . LYS A 1 241 ? 13.811 29.353 3.004   1.00 35.45  ? 241 LYS A CG  1 
ATOM   1878 C CD  . LYS A 1 241 ? 12.493 28.585 2.919   0.60 37.44  ? 241 LYS A CD  1 
ATOM   1879 C CE  . LYS A 1 241 ? 11.450 29.387 2.145   0.60 38.87  ? 241 LYS A CE  1 
ATOM   1880 N NZ  . LYS A 1 241 ? 10.100 28.765 2.199   0.60 42.40  ? 241 LYS A NZ  1 
ATOM   1881 N N   . LYS A 1 242 ? 17.478 28.804 5.645   1.00 32.76  ? 242 LYS A N   1 
ATOM   1882 C CA  . LYS A 1 242 ? 18.388 28.131 6.559   1.00 34.44  ? 242 LYS A CA  1 
ATOM   1883 C C   . LYS A 1 242 ? 17.687 27.928 7.894   1.00 32.14  ? 242 LYS A C   1 
ATOM   1884 O O   . LYS A 1 242 ? 16.789 28.690 8.257   1.00 32.50  ? 242 LYS A O   1 
ATOM   1885 C CB  . LYS A 1 242 ? 19.677 28.935 6.757   1.00 39.44  ? 242 LYS A CB  1 
ATOM   1886 C CG  . LYS A 1 242 ? 20.355 29.355 5.458   1.00 44.27  ? 242 LYS A CG  1 
ATOM   1887 C CD  . LYS A 1 242 ? 21.822 29.699 5.669   1.00 49.23  ? 242 LYS A CD  1 
ATOM   1888 C CE  . LYS A 1 242 ? 22.702 28.447 5.673   1.00 48.92  ? 242 LYS A CE  1 
ATOM   1889 N NZ  . LYS A 1 242 ? 24.116 28.735 6.052   0.39 46.66  ? 242 LYS A NZ  1 
ATOM   1890 N N   . ILE A 1 243 ? 18.086 26.881 8.613   1.00 30.75  ? 243 ILE A N   1 
ATOM   1891 C CA  . ILE A 1 243 ? 17.646 26.686 9.992   1.00 30.41  ? 243 ILE A CA  1 
ATOM   1892 C C   . ILE A 1 243 ? 18.666 27.349 10.899  1.00 31.52  ? 243 ILE A C   1 
ATOM   1893 O O   . ILE A 1 243 ? 19.873 27.277 10.659  1.00 29.72  ? 243 ILE A O   1 
ATOM   1894 C CB  . ILE A 1 243 ? 17.484 25.192 10.338  1.00 27.42  ? 243 ILE A CB  1 
ATOM   1895 C CG1 . ILE A 1 243 ? 16.956 25.014 11.775  1.00 31.54  ? 243 ILE A CG1 1 
ATOM   1896 C CG2 . ILE A 1 243 ? 18.795 24.456 10.164  1.00 25.85  ? 243 ILE A CG2 1 
ATOM   1897 C CD1 . ILE A 1 243 ? 16.835 23.563 12.181  1.00 29.60  ? 243 ILE A CD1 1 
ATOM   1898 N N   . HIS A 1 244 ? 18.181 28.013 11.935  1.00 30.44  ? 244 HIS A N   1 
ATOM   1899 C CA  . HIS A 1 244 ? 19.034 28.720 12.876  1.00 33.77  ? 244 HIS A CA  1 
ATOM   1900 C C   . HIS A 1 244 ? 18.980 28.021 14.225  1.00 32.70  ? 244 HIS A C   1 
ATOM   1901 O O   . HIS A 1 244 ? 17.892 27.715 14.727  1.00 30.82  ? 244 HIS A O   1 
ATOM   1902 C CB  . HIS A 1 244 ? 18.594 30.175 13.008  1.00 35.96  ? 244 HIS A CB  1 
ATOM   1903 C CG  . HIS A 1 244 ? 18.518 30.893 11.697  0.70 37.62  ? 244 HIS A CG  1 
ATOM   1904 N ND1 . HIS A 1 244 ? 19.637 31.326 11.022  0.70 36.61  ? 244 HIS A ND1 1 
ATOM   1905 C CD2 . HIS A 1 244 ? 17.457 31.241 10.932  0.70 38.19  ? 244 HIS A CD2 1 
ATOM   1906 C CE1 . HIS A 1 244 ? 19.270 31.915 9.899   0.70 38.09  ? 244 HIS A CE1 1 
ATOM   1907 N NE2 . HIS A 1 244 ? 17.952 31.875 9.819   0.70 38.46  ? 244 HIS A NE2 1 
ATOM   1908 N N   . PHE A 1 245 ? 20.151 27.781 14.802  1.00 33.43  ? 245 PHE A N   1 
ATOM   1909 C CA  . PHE A 1 245 ? 20.278 27.204 16.133  1.00 33.37  ? 245 PHE A CA  1 
ATOM   1910 C C   . PHE A 1 245 ? 20.721 28.267 17.130  1.00 37.48  ? 245 PHE A C   1 
ATOM   1911 O O   . PHE A 1 245 ? 21.534 29.135 16.808  1.00 35.84  ? 245 PHE A O   1 
ATOM   1912 C CB  . PHE A 1 245 ? 21.286 26.059 16.128  1.00 32.85  ? 245 PHE A CB  1 
ATOM   1913 C CG  . PHE A 1 245 ? 20.873 24.896 15.285  1.00 32.54  ? 245 PHE A CG  1 
ATOM   1914 C CD1 . PHE A 1 245 ? 20.117 23.871 15.826  1.00 34.00  ? 245 PHE A CD1 1 
ATOM   1915 C CD2 . PHE A 1 245 ? 21.234 24.827 13.946  1.00 33.13  ? 245 PHE A CD2 1 
ATOM   1916 C CE1 . PHE A 1 245 ? 19.734 22.791 15.052  1.00 34.83  ? 245 PHE A CE1 1 
ATOM   1917 C CE2 . PHE A 1 245 ? 20.855 23.749 13.167  1.00 34.56  ? 245 PHE A CE2 1 
ATOM   1918 C CZ  . PHE A 1 245 ? 20.102 22.728 13.722  1.00 33.44  ? 245 PHE A CZ  1 
ATOM   1919 N N   . ALA A 1 246 ? 20.174 28.211 18.340  1.00 39.09  ? 246 ALA A N   1 
ATOM   1920 C CA  . ALA A 1 246 ? 20.727 28.989 19.438  1.00 40.21  ? 246 ALA A CA  1 
ATOM   1921 C C   . ALA A 1 246 ? 21.858 28.177 20.056  1.00 44.56  ? 246 ALA A C   1 
ATOM   1922 O O   . ALA A 1 246 ? 21.648 27.027 20.459  1.00 48.52  ? 246 ALA A O   1 
ATOM   1923 C CB  . ALA A 1 246 ? 19.640 29.311 20.458  1.00 41.78  ? 246 ALA A CB  1 
ATOM   1924 N N   . ARG A 1 247 ? 23.067 28.738 20.088  1.00 45.98  ? 247 ARG A N   1 
ATOM   1925 C CA  . ARG A 1 247 ? 24.207 28.054 20.690  1.00 48.93  ? 247 ARG A CA  1 
ATOM   1926 C C   . ARG A 1 247 ? 24.717 28.865 21.872  1.00 50.80  ? 247 ARG A C   1 
ATOM   1927 O O   . ARG A 1 247 ? 24.912 30.081 21.765  1.00 53.00  ? 247 ARG A O   1 
ATOM   1928 C CB  . ARG A 1 247 ? 25.328 27.804 19.675  1.00 49.13  ? 247 ARG A CB  1 
ATOM   1929 C CG  . ARG A 1 247 ? 24.915 26.909 18.487  1.00 50.62  ? 247 ARG A CG  1 
ATOM   1930 C CD  . ARG A 1 247 ? 25.139 25.395 18.699  1.00 49.15  ? 247 ARG A CD  1 
ATOM   1931 N NE  . ARG A 1 247 ? 25.230 24.686 17.413  1.00 51.49  ? 247 ARG A NE  1 
ATOM   1932 C CZ  . ARG A 1 247 ? 24.385 23.745 16.990  1.00 47.14  ? 247 ARG A CZ  1 
ATOM   1933 N NH1 . ARG A 1 247 ? 23.376 23.355 17.758  1.00 43.34  ? 247 ARG A NH1 1 
ATOM   1934 N NH2 . ARG A 1 247 ? 24.556 23.183 15.799  1.00 44.22  ? 247 ARG A NH2 1 
ATOM   1935 N N   . PHE A 1 248 ? 24.908 28.189 23.003  1.00 52.38  ? 248 PHE A N   1 
ATOM   1936 C CA  . PHE A 1 248 ? 25.338 28.825 24.239  1.00 52.13  ? 248 PHE A CA  1 
ATOM   1937 C C   . PHE A 1 248 ? 26.751 28.441 24.646  1.00 51.34  ? 248 PHE A C   1 
ATOM   1938 O O   . PHE A 1 248 ? 27.287 29.020 25.600  1.00 52.99  ? 248 PHE A O   1 
ATOM   1939 C CB  . PHE A 1 248 ? 24.367 28.471 25.372  0.90 54.89  ? 248 PHE A CB  1 
ATOM   1940 C CG  . PHE A 1 248 ? 23.007 29.069 25.198  0.80 55.21  ? 248 PHE A CG  1 
ATOM   1941 C CD1 . PHE A 1 248 ? 22.048 28.434 24.420  0.80 55.05  ? 248 PHE A CD1 1 
ATOM   1942 C CD2 . PHE A 1 248 ? 22.694 30.275 25.793  0.80 53.55  ? 248 PHE A CD2 1 
ATOM   1943 C CE1 . PHE A 1 248 ? 20.800 28.994 24.255  0.80 52.72  ? 248 PHE A CE1 1 
ATOM   1944 C CE2 . PHE A 1 248 ? 21.452 30.837 25.634  0.80 52.90  ? 248 PHE A CE2 1 
ATOM   1945 C CZ  . PHE A 1 248 ? 20.505 30.198 24.865  0.80 50.90  ? 248 PHE A CZ  1 
ATOM   1946 N N   . ARG A 1 249 ? 27.362 27.493 23.944  1.00 41.52  ? 249 ARG A N   1 
ATOM   1947 C CA  . ARG A 1 249 ? 28.703 27.011 24.227  1.00 42.54  ? 249 ARG A CA  1 
ATOM   1948 C C   . ARG A 1 249 ? 29.201 26.325 22.962  1.00 40.70  ? 249 ARG A C   1 
ATOM   1949 O O   . ARG A 1 249 ? 28.432 26.058 22.038  1.00 37.72  ? 249 ARG A O   1 
ATOM   1950 C CB  . ARG A 1 249 ? 28.711 26.058 25.428  1.00 42.60  ? 249 ARG A CB  1 
ATOM   1951 C CG  . ARG A 1 249 ? 27.823 24.840 25.220  0.80 39.76  ? 249 ARG A CG  1 
ATOM   1952 C CD  . ARG A 1 249 ? 27.661 23.993 26.466  0.70 42.01  ? 249 ARG A CD  1 
ATOM   1953 N NE  . ARG A 1 249 ? 26.839 22.819 26.182  0.70 44.70  ? 249 ARG A NE  1 
ATOM   1954 C CZ  . ARG A 1 249 ? 26.381 21.979 27.104  0.70 48.22  ? 249 ARG A CZ  1 
ATOM   1955 N NH1 . ARG A 1 249 ? 25.640 20.938 26.739  0.70 47.26  ? 249 ARG A NH1 1 
ATOM   1956 N NH2 . ARG A 1 249 ? 26.657 22.179 28.388  0.70 46.62  ? 249 ARG A NH2 1 
ATOM   1957 N N   . SER A 1 250 ? 30.502 26.058 22.922  1.00 45.25  ? 250 SER A N   1 
ATOM   1958 C CA  . SER A 1 250 ? 31.095 25.386 21.771  1.00 43.06  ? 250 SER A CA  1 
ATOM   1959 C C   . SER A 1 250 ? 30.831 23.890 21.858  1.00 40.05  ? 250 SER A C   1 
ATOM   1960 O O   . SER A 1 250 ? 31.176 23.242 22.854  1.00 39.75  ? 250 SER A O   1 
ATOM   1961 C CB  . SER A 1 250 ? 32.595 25.659 21.698  1.00 48.03  ? 250 SER A CB  1 
ATOM   1962 O OG  . SER A 1 250 ? 33.197 24.899 20.662  0.70 44.92  ? 250 SER A OG  1 
ATOM   1963 N N   . PHE A 1 251 ? 30.206 23.352 20.818  1.00 38.85  ? 251 PHE A N   1 
ATOM   1964 C CA  . PHE A 1 251 ? 30.062 21.911 20.628  1.00 38.17  ? 251 PHE A CA  1 
ATOM   1965 C C   . PHE A 1 251 ? 30.277 21.686 19.138  1.00 35.93  ? 251 PHE A C   1 
ATOM   1966 O O   . PHE A 1 251 ? 29.321 21.636 18.353  1.00 34.87  ? 251 PHE A O   1 
ATOM   1967 C CB  . PHE A 1 251 ? 28.688 21.419 21.097  1.00 41.67  ? 251 PHE A CB  1 
ATOM   1968 C CG  . PHE A 1 251 ? 28.529 19.915 21.095  1.00 44.82  ? 251 PHE A CG  1 
ATOM   1969 C CD1 . PHE A 1 251 ? 29.626 19.077 20.986  0.90 44.95  ? 251 PHE A CD1 1 
ATOM   1970 C CD2 . PHE A 1 251 ? 27.271 19.345 21.208  0.90 48.30  ? 251 PHE A CD2 1 
ATOM   1971 C CE1 . PHE A 1 251 ? 29.469 17.701 20.990  0.90 44.06  ? 251 PHE A CE1 1 
ATOM   1972 C CE2 . PHE A 1 251 ? 27.110 17.972 21.215  0.90 48.59  ? 251 PHE A CE2 1 
ATOM   1973 C CZ  . PHE A 1 251 ? 28.213 17.150 21.105  0.90 46.65  ? 251 PHE A CZ  1 
ATOM   1974 N N   . PRO A 1 252 ? 31.537 21.595 18.706  1.00 32.19  ? 252 PRO A N   1 
ATOM   1975 C CA  . PRO A 1 252 ? 31.831 21.547 17.272  1.00 31.48  ? 252 PRO A CA  1 
ATOM   1976 C C   . PRO A 1 252 ? 31.223 20.332 16.593  1.00 30.85  ? 252 PRO A C   1 
ATOM   1977 O O   . PRO A 1 252 ? 31.138 19.243 17.166  1.00 29.58  ? 252 PRO A O   1 
ATOM   1978 C CB  . PRO A 1 252 ? 33.364 21.490 17.227  1.00 31.97  ? 252 PRO A CB  1 
ATOM   1979 C CG  . PRO A 1 252 ? 33.803 22.090 18.526  1.00 30.31  ? 252 PRO A CG  1 
ATOM   1980 C CD  . PRO A 1 252 ? 32.761 21.674 19.521  1.00 32.56  ? 252 PRO A CD  1 
ATOM   1981 N N   . PHE A 1 253 ? 30.847 20.528 15.325  1.00 30.82  ? 253 PHE A N   1 
ATOM   1982 C CA  . PHE A 1 253 ? 30.267 19.447 14.528  1.00 28.78  ? 253 PHE A CA  1 
ATOM   1983 C C   . PHE A 1 253 ? 31.119 18.180 14.566  1.00 25.18  ? 253 PHE A C   1 
ATOM   1984 O O   . PHE A 1 253 ? 30.603 17.078 14.772  1.00 22.47  ? 253 PHE A O   1 
ATOM   1985 C CB  . PHE A 1 253 ? 30.081 19.929 13.088  1.00 26.77  ? 253 PHE A CB  1 
ATOM   1986 C CG  . PHE A 1 253 ? 29.488 18.903 12.174  1.00 26.37  ? 253 PHE A CG  1 
ATOM   1987 C CD1 . PHE A 1 253 ? 28.117 18.698 12.141  1.00 28.20  ? 253 PHE A CD1 1 
ATOM   1988 C CD2 . PHE A 1 253 ? 30.297 18.169 11.313  1.00 27.67  ? 253 PHE A CD2 1 
ATOM   1989 C CE1 . PHE A 1 253 ? 27.558 17.763 11.273  1.00 31.42  ? 253 PHE A CE1 1 
ATOM   1990 C CE2 . PHE A 1 253 ? 29.744 17.240 10.433  1.00 26.75  ? 253 PHE A CE2 1 
ATOM   1991 C CZ  . PHE A 1 253 ? 28.382 17.036 10.418  1.00 27.88  ? 253 PHE A CZ  1 
ATOM   1992 N N   . TRP A 1 254 ? 32.438 18.312 14.383  1.00 25.44  ? 254 TRP A N   1 
ATOM   1993 C CA  . TRP A 1 254 ? 33.262 17.105 14.353  1.00 24.31  ? 254 TRP A CA  1 
ATOM   1994 C C   . TRP A 1 254 ? 33.328 16.427 15.723  1.00 23.83  ? 254 TRP A C   1 
ATOM   1995 O O   . TRP A 1 254 ? 33.456 15.196 15.797  1.00 24.38  ? 254 TRP A O   1 
ATOM   1996 C CB  . TRP A 1 254 ? 34.671 17.432 13.842  1.00 26.31  ? 254 TRP A CB  1 
ATOM   1997 C CG  . TRP A 1 254 ? 34.695 17.920 12.402  1.00 25.16  ? 254 TRP A CG  1 
ATOM   1998 C CD1 . TRP A 1 254 ? 35.199 19.109 11.937  1.00 25.20  ? 254 TRP A CD1 1 
ATOM   1999 C CD2 . TRP A 1 254 ? 34.174 17.230 11.255  1.00 23.85  ? 254 TRP A CD2 1 
ATOM   2000 N NE1 . TRP A 1 254 ? 35.027 19.188 10.559  1.00 24.37  ? 254 TRP A NE1 1 
ATOM   2001 C CE2 . TRP A 1 254 ? 34.404 18.049 10.125  1.00 22.93  ? 254 TRP A CE2 1 
ATOM   2002 C CE3 . TRP A 1 254 ? 33.553 15.993 11.071  1.00 23.21  ? 254 TRP A CE3 1 
ATOM   2003 C CZ2 . TRP A 1 254 ? 34.031 17.664 8.836   1.00 25.29  ? 254 TRP A CZ2 1 
ATOM   2004 C CZ3 . TRP A 1 254 ? 33.179 15.618 9.794   1.00 25.08  ? 254 TRP A CZ3 1 
ATOM   2005 C CH2 . TRP A 1 254 ? 33.416 16.455 8.696   1.00 25.73  ? 254 TRP A CH2 1 
ATOM   2006 N N   . ARG A 1 255 ? 33.251 17.196 16.812  1.00 24.17  ? 255 ARG A N   1 
ATOM   2007 C CA  . ARG A 1 255 ? 33.116 16.565 18.124  1.00 24.11  ? 255 ARG A CA  1 
ATOM   2008 C C   . ARG A 1 255 ? 31.762 15.885 18.250  1.00 25.33  ? 255 ARG A C   1 
ATOM   2009 O O   . ARG A 1 255 ? 31.655 14.773 18.783  1.00 25.43  ? 255 ARG A O   1 
ATOM   2010 C CB  . ARG A 1 255 ? 33.292 17.598 19.243  0.80 22.11  ? 255 ARG A CB  1 
ATOM   2011 C CG  . ARG A 1 255 ? 32.837 17.093 20.594  0.70 31.90  ? 255 ARG A CG  1 
ATOM   2012 C CD  . ARG A 1 255 ? 33.998 16.761 21.507  0.60 34.83  ? 255 ARG A CD  1 
ATOM   2013 N NE  . ARG A 1 255 ? 34.741 17.949 21.903  0.50 30.02  ? 255 ARG A NE  1 
ATOM   2014 C CZ  . ARG A 1 255 ? 36.043 17.956 22.177  0.40 29.97  ? 255 ARG A CZ  1 
ATOM   2015 N NH1 . ARG A 1 255 ? 36.753 16.839 22.080  0.40 27.11  ? 255 ARG A NH1 1 
ATOM   2016 N NH2 . ARG A 1 255 ? 36.638 19.085 22.539  0.40 30.55  ? 255 ARG A NH2 1 
ATOM   2017 N N   . ARG A 1 256 ? 30.722 16.547 17.758  1.00 25.17  ? 256 ARG A N   1 
ATOM   2018 C CA  A ARG A 1 256 ? 29.400 15.933 17.714  0.50 29.46  ? 256 ARG A CA  1 
ATOM   2019 C CA  B ARG A 1 256 ? 29.401 15.934 17.714  0.50 29.46  ? 256 ARG A CA  1 
ATOM   2020 C C   . ARG A 1 256 ? 29.439 14.608 16.963  1.00 28.27  ? 256 ARG A C   1 
ATOM   2021 O O   . ARG A 1 256 ? 28.854 13.613 17.409  1.00 25.08  ? 256 ARG A O   1 
ATOM   2022 C CB  A ARG A 1 256 ? 28.414 16.909 17.071  0.50 32.33  ? 256 ARG A CB  1 
ATOM   2023 C CB  B ARG A 1 256 ? 28.424 16.925 17.078  0.50 32.32  ? 256 ARG A CB  1 
ATOM   2024 C CG  A ARG A 1 256 ? 26.959 16.483 17.121  0.50 33.58  ? 256 ARG A CG  1 
ATOM   2025 C CG  B ARG A 1 256 ? 27.029 16.407 16.823  0.50 33.29  ? 256 ARG A CG  1 
ATOM   2026 C CD  A ARG A 1 256 ? 26.086 17.386 16.241  0.50 32.02  ? 256 ARG A CD  1 
ATOM   2027 C CD  B ARG A 1 256 ? 26.199 17.461 16.083  0.50 32.14  ? 256 ARG A CD  1 
ATOM   2028 N NE  A ARG A 1 256 ? 26.101 18.775 16.683  0.50 31.80  ? 256 ARG A NE  1 
ATOM   2029 N NE  B ARG A 1 256 ? 25.732 18.517 16.968  0.50 32.46  ? 256 ARG A NE  1 
ATOM   2030 C CZ  A ARG A 1 256 ? 25.351 19.243 17.681  0.50 33.60  ? 256 ARG A CZ  1 
ATOM   2031 C CZ  B ARG A 1 256 ? 26.246 19.742 17.044  0.50 35.08  ? 256 ARG A CZ  1 
ATOM   2032 N NH1 A ARG A 1 256 ? 24.531 18.430 18.329  0.50 29.65  ? 256 ARG A NH1 1 
ATOM   2033 N NH1 B ARG A 1 256 ? 25.721 20.611 17.901  0.50 35.93  ? 256 ARG A NH1 1 
ATOM   2034 N NH2 A ARG A 1 256 ? 25.415 20.521 18.031  0.50 35.17  ? 256 ARG A NH2 1 
ATOM   2035 N NH2 B ARG A 1 256 ? 27.268 20.111 16.277  0.50 31.19  ? 256 ARG A NH2 1 
ATOM   2036 N N   . VAL A 1 257 ? 30.152 14.569 15.828  1.00 24.55  ? 257 VAL A N   1 
ATOM   2037 C CA  . VAL A 1 257 ? 30.319 13.329 15.081  1.00 22.47  ? 257 VAL A CA  1 
ATOM   2038 C C   . VAL A 1 257 ? 31.097 12.316 15.902  1.00 22.19  ? 257 VAL A C   1 
ATOM   2039 O O   . VAL A 1 257 ? 30.765 11.123 15.926  1.00 21.89  ? 257 VAL A O   1 
ATOM   2040 C CB  . VAL A 1 257 ? 31.023 13.607 13.742  1.00 20.69  ? 257 VAL A CB  1 
ATOM   2041 C CG1 . VAL A 1 257 ? 31.374 12.293 13.057  1.00 19.60  ? 257 VAL A CG1 1 
ATOM   2042 C CG2 . VAL A 1 257 ? 30.144 14.500 12.835  1.00 19.99  ? 257 VAL A CG2 1 
ATOM   2043 N N   . HIS A 1 258 ? 32.184 12.762 16.549  1.00 21.59  ? 258 HIS A N   1 
ATOM   2044 C CA  . HIS A 1 258 ? 32.958 11.844 17.376  1.00 24.94  ? 258 HIS A CA  1 
ATOM   2045 C C   . HIS A 1 258 ? 32.087 11.238 18.471  1.00 22.67  ? 258 HIS A C   1 
ATOM   2046 O O   . HIS A 1 258 ? 32.103 10.023 18.697  1.00 25.27  ? 258 HIS A O   1 
ATOM   2047 C CB  . HIS A 1 258 ? 34.144 12.567 18.003  1.00 23.74  ? 258 HIS A CB  1 
ATOM   2048 C CG  . HIS A 1 258 ? 34.855 11.764 19.042  1.00 22.90  ? 258 HIS A CG  1 
ATOM   2049 N ND1 . HIS A 1 258 ? 34.476 11.758 20.373  1.00 28.50  ? 258 HIS A ND1 1 
ATOM   2050 C CD2 . HIS A 1 258 ? 35.933 10.952 18.954  1.00 23.11  ? 258 HIS A CD2 1 
ATOM   2051 C CE1 . HIS A 1 258 ? 35.286 10.967 21.058  1.00 24.30  ? 258 HIS A CE1 1 
ATOM   2052 N NE2 . HIS A 1 258 ? 36.183 10.471 20.224  1.00 30.30  ? 258 HIS A NE2 1 
ATOM   2053 N N   . ASP A 1 259 ? 31.328 12.084 19.166  1.00 26.53  ? 259 ASP A N   1 
ATOM   2054 C CA  . ASP A 1 259 ? 30.544 11.623 20.308  1.00 26.67  ? 259 ASP A CA  1 
ATOM   2055 C C   . ASP A 1 259 ? 29.466 10.629 19.890  1.00 31.23  ? 259 ASP A C   1 
ATOM   2056 O O   . ASP A 1 259 ? 29.099 9.740  20.671  1.00 34.03  ? 259 ASP A O   1 
ATOM   2057 C CB  . ASP A 1 259 ? 29.925 12.826 21.019  1.00 27.00  ? 259 ASP A CB  1 
ATOM   2058 C CG  . ASP A 1 259 ? 30.949 13.613 21.824  1.00 32.08  ? 259 ASP A CG  1 
ATOM   2059 O OD1 . ASP A 1 259 ? 32.102 13.139 21.961  1.00 31.01  ? 259 ASP A OD1 1 
ATOM   2060 O OD2 . ASP A 1 259 ? 30.603 14.705 22.316  1.00 35.90  ? 259 ASP A OD2 1 
ATOM   2061 N N   . SER A 1 260 ? 28.959 10.756 18.669  1.00 29.49  ? 260 SER A N   1 
ATOM   2062 C CA  . SER A 1 260 ? 27.867 9.915  18.198  1.00 31.05  ? 260 SER A CA  1 
ATOM   2063 C C   . SER A 1 260 ? 28.338 8.623  17.550  1.00 32.83  ? 260 SER A C   1 
ATOM   2064 O O   . SER A 1 260 ? 27.600 7.631  17.574  1.00 33.46  ? 260 SER A O   1 
ATOM   2065 C CB  . SER A 1 260 ? 27.004 10.684 17.192  1.00 35.57  ? 260 SER A CB  1 
ATOM   2066 O OG  . SER A 1 260 ? 26.428 11.838 17.773  1.00 37.53  ? 260 SER A OG  1 
ATOM   2067 N N   . PHE A 1 261 ? 29.546 8.599  16.958  1.00 27.23  ? 261 PHE A N   1 
ATOM   2068 C CA  . PHE A 1 261 ? 29.986 7.427  16.218  1.00 26.35  ? 261 PHE A CA  1 
ATOM   2069 C C   . PHE A 1 261 ? 31.259 6.774  16.742  1.00 29.46  ? 261 PHE A C   1 
ATOM   2070 O O   . PHE A 1 261 ? 31.463 5.582  16.480  1.00 26.90  ? 261 PHE A O   1 
ATOM   2071 C CB  . PHE A 1 261 ? 30.184 7.778  14.732  1.00 22.31  ? 261 PHE A CB  1 
ATOM   2072 C CG  . PHE A 1 261 ? 28.915 8.237  14.050  1.00 24.13  ? 261 PHE A CG  1 
ATOM   2073 C CD1 . PHE A 1 261 ? 28.651 9.588  13.885  1.00 24.81  ? 261 PHE A CD1 1 
ATOM   2074 C CD2 . PHE A 1 261 ? 27.971 7.307  13.603  1.00 25.15  ? 261 PHE A CD2 1 
ATOM   2075 C CE1 . PHE A 1 261 ? 27.469 10.016 13.274  1.00 28.92  ? 261 PHE A CE1 1 
ATOM   2076 C CE2 . PHE A 1 261 ? 26.793 7.722  12.991  1.00 26.50  ? 261 PHE A CE2 1 
ATOM   2077 C CZ  . PHE A 1 261 ? 26.541 9.074  12.820  1.00 25.02  ? 261 PHE A CZ  1 
ATOM   2078 N N   . ILE A 1 262 ? 32.121 7.500  17.455  1.00 21.70  ? 262 ILE A N   1 
ATOM   2079 C CA  . ILE A 1 262 ? 33.408 6.927  17.835  1.00 24.62  ? 262 ILE A CA  1 
ATOM   2080 C C   . ILE A 1 262 ? 33.345 6.451  19.285  1.00 30.66  ? 262 ILE A C   1 
ATOM   2081 O O   . ILE A 1 262 ? 33.577 5.271  19.568  1.00 35.19  ? 262 ILE A O   1 
ATOM   2082 C CB  . ILE A 1 262 ? 34.559 7.927  17.619  1.00 25.47  ? 262 ILE A CB  1 
ATOM   2083 C CG1 . ILE A 1 262 ? 34.609 8.360  16.153  1.00 28.74  ? 262 ILE A CG1 1 
ATOM   2084 C CG2 . ILE A 1 262 ? 35.891 7.287  17.993  1.00 28.70  ? 262 ILE A CG2 1 
ATOM   2085 C CD1 . ILE A 1 262 ? 34.988 7.251  15.221  1.00 28.55  ? 262 ILE A CD1 1 
ATOM   2086 N N   . GLU A 1 263 ? 33.016 7.353  20.206  1.00 30.14  ? 263 GLU A N   1 
ATOM   2087 C CA  . GLU A 1 263 ? 32.881 6.978  21.617  1.00 44.45  ? 263 GLU A CA  1 
ATOM   2088 C C   . GLU A 1 263 ? 32.398 8.187  22.406  1.00 51.27  ? 263 GLU A C   1 
ATOM   2089 O O   . GLU A 1 263 ? 32.604 9.334  21.999  1.00 52.30  ? 263 GLU A O   1 
ATOM   2090 C CB  . GLU A 1 263 ? 34.204 6.470  22.213  0.99 50.15  ? 263 GLU A CB  1 
ATOM   2091 N N   . ASP A 1 264 ? 31.771 7.921  23.551  1.00 60.86  ? 264 ASP A N   1 
ATOM   2092 C CA  . ASP A 1 264 ? 31.290 8.996  24.416  1.00 70.11  ? 264 ASP A CA  1 
ATOM   2093 C C   . ASP A 1 264 ? 31.075 8.496  25.846  1.00 74.06  ? 264 ASP A C   1 
ATOM   2094 O O   . ASP A 1 264 ? 31.803 8.871  26.766  1.00 76.84  ? 264 ASP A O   1 
ATOM   2095 C CB  . ASP A 1 264 ? 29.992 9.591  23.865  1.00 74.55  ? 264 ASP A CB  1 
ATOM   2096 C CG  . ASP A 1 264 ? 29.599 10.889 24.562  1.00 80.32  ? 264 ASP A CG  1 
ATOM   2097 O OD1 . ASP A 1 264 ? 30.430 11.433 25.327  1.00 81.47  ? 264 ASP A OD1 1 
ATOM   2098 O OD2 . ASP A 1 264 ? 28.462 11.366 24.343  1.00 81.58  ? 264 ASP A OD2 1 
HETATM 2099 C C1  . CIT B 2 .   ? 31.668 24.198 14.248  0.93 48.86  ? 301 CIT A C1  1 
HETATM 2100 O O1  . CIT B 2 .   ? 31.539 23.016 13.862  0.93 42.71  ? 301 CIT A O1  1 
HETATM 2101 O O2  . CIT B 2 .   ? 32.788 24.549 14.672  0.93 48.38  ? 301 CIT A O2  1 
HETATM 2102 C C2  . CIT B 2 .   ? 30.517 25.185 14.217  0.93 56.17  ? 301 CIT A C2  1 
HETATM 2103 C C3  . CIT B 2 .   ? 29.370 24.701 15.109  0.93 64.95  ? 301 CIT A C3  1 
HETATM 2104 O O7  . CIT B 2 .   ? 29.906 24.000 16.260  0.93 67.69  ? 301 CIT A O7  1 
HETATM 2105 C C4  . CIT B 2 .   ? 28.493 25.860 15.583  0.93 69.39  ? 301 CIT A C4  1 
HETATM 2106 C C5  . CIT B 2 .   ? 28.933 26.424 16.921  0.93 73.97  ? 301 CIT A C5  1 
HETATM 2107 O O3  . CIT B 2 .   ? 29.250 27.631 17.025  0.93 74.84  ? 301 CIT A O3  1 
HETATM 2108 O O4  . CIT B 2 .   ? 28.968 25.704 17.948  0.93 74.12  ? 301 CIT A O4  1 
HETATM 2109 C C6  . CIT B 2 .   ? 28.490 23.744 14.318  0.93 64.34  ? 301 CIT A C6  1 
HETATM 2110 O O5  . CIT B 2 .   ? 28.553 23.702 13.074  0.93 63.00  ? 301 CIT A O5  1 
HETATM 2111 O O6  . CIT B 2 .   ? 27.703 22.978 14.916  0.93 66.01  ? 301 CIT A O6  1 
HETATM 2112 C C1  . UUC C 3 .   ? 20.484 11.017 13.025  1.00 25.78  ? 302 UUC A C1  1 
HETATM 2113 C C2  . UUC C 3 .   ? 20.286 12.159 12.320  1.00 26.42  ? 302 UUC A C2  1 
HETATM 2114 C C3  . UUC C 3 .   ? 21.381 12.895 11.939  1.00 26.77  ? 302 UUC A C3  1 
HETATM 2115 C C4  . UUC C 3 .   ? 18.431 11.246 12.734  1.00 23.81  ? 302 UUC A C4  1 
HETATM 2116 N N1  . UUC C 3 .   ? 22.571 12.437 12.287  1.00 24.16  ? 302 UUC A N1  1 
HETATM 2117 N N2  . UUC C 3 .   ? 21.675 10.637 13.319  1.00 23.38  ? 302 UUC A N2  1 
HETATM 2118 C C5  . UUC C 3 .   ? 16.838 8.303  8.938   1.00 27.64  ? 302 UUC A C5  1 
HETATM 2119 C C6  . UUC C 3 .   ? 22.672 11.343 12.965  1.00 22.59  ? 302 UUC A C6  1 
HETATM 2120 C C7  . UUC C 3 .   ? 16.687 9.412  7.879   1.00 26.11  ? 302 UUC A C7  1 
HETATM 2121 C C8  . UUC C 3 .   ? 15.468 10.173 8.365   1.00 25.41  ? 302 UUC A C8  1 
HETATM 2122 C C9  . UUC C 3 .   ? 15.438 9.694  9.818   1.00 27.59  ? 302 UUC A C9  1 
HETATM 2123 C C10 . UUC C 3 .   ? 14.070 9.887  10.508  1.00 27.72  ? 302 UUC A C10 1 
HETATM 2124 C C11 . UUC C 3 .   ? 15.504 4.279  10.247  0.70 47.74  ? 302 UUC A C11 1 
HETATM 2125 C C12 . UUC C 3 .   ? 13.955 5.859  11.240  0.70 43.32  ? 302 UUC A C12 1 
HETATM 2126 C C13 . UUC C 3 .   ? 16.910 7.061  12.754  0.80 40.03  ? 302 UUC A C13 1 
HETATM 2127 C C14 . UUC C 3 .   ? 18.147 7.285  13.717  1.00 36.69  ? 302 UUC A C14 1 
HETATM 2128 C C15 . UUC C 3 .   ? 19.235 9.247  13.957  1.00 28.86  ? 302 UUC A C15 1 
HETATM 2129 C C16 . UUC C 3 .   ? 18.273 9.193  15.077  1.00 32.95  ? 302 UUC A C16 1 
HETATM 2130 C C17 . UUC C 3 .   ? 18.120 7.734  15.184  1.00 37.41  ? 302 UUC A C17 1 
HETATM 2131 C C18 . UUC C 3 .   ? 17.064 11.041 12.749  1.00 23.93  ? 302 UUC A C18 1 
HETATM 2132 C C19 . UUC C 3 .   ? 16.014 10.854 12.761  1.00 24.77  ? 302 UUC A C19 1 
HETATM 2133 C C20 . UUC C 3 .   ? 14.577 10.561 12.790  1.00 28.83  ? 302 UUC A C20 1 
HETATM 2134 C C21 . UUC C 3 .   ? 15.999 6.383  7.665   1.00 27.30  ? 302 UUC A C21 1 
HETATM 2135 C C22 . UUC C 3 .   ? 17.647 5.106  7.636   1.00 26.80  ? 302 UUC A C22 1 
HETATM 2136 C C23 . UUC C 3 .   ? 17.946 6.229  8.327   1.00 26.64  ? 302 UUC A C23 1 
HETATM 2137 C C24 . UUC C 3 .   ? 19.968 5.399  8.671   1.00 28.26  ? 302 UUC A C24 1 
HETATM 2138 C C25 . UUC C 3 .   ? 18.612 4.130  7.489   1.00 27.99  ? 302 UUC A C25 1 
HETATM 2139 N N3  . UUC C 3 .   ? 21.238 14.001 11.267  1.00 27.13  ? 302 UUC A N3  1 
HETATM 2140 N N4  . UUC C 3 .   ? 18.993 12.251 12.177  1.00 27.22  ? 302 UUC A N4  1 
HETATM 2141 N N5  . UUC C 3 .   ? 19.344 10.491 13.261  1.00 28.44  ? 302 UUC A N5  1 
HETATM 2142 N N6  . UUC C 3 .   ? 15.345 5.342  11.170  0.70 46.52  ? 302 UUC A N6  1 
HETATM 2143 N N7  . UUC C 3 .   ? 15.964 6.095  13.211  0.80 43.59  ? 302 UUC A N7  1 
HETATM 2144 N N8  . UUC C 3 .   ? 16.924 7.001  8.325   1.00 25.93  ? 302 UUC A N8  1 
HETATM 2145 N N9  . UUC C 3 .   ? 16.419 5.237  7.233   1.00 27.82  ? 302 UUC A N9  1 
HETATM 2146 N N10 . UUC C 3 .   ? 19.128 6.349  8.843   1.00 27.28  ? 302 UUC A N10 1 
HETATM 2147 N N11 . UUC C 3 .   ? 19.763 4.331  8.030   1.00 25.78  ? 302 UUC A N11 1 
HETATM 2148 N N12 . UUC C 3 .   ? 18.418 3.039  6.865   1.00 25.29  ? 302 UUC A N12 1 
HETATM 2149 O O1  . UUC C 3 .   ? 17.808 10.187 7.843   1.00 25.73  ? 302 UUC A O1  1 
HETATM 2150 O O2  . UUC C 3 .   ? 15.609 11.502 8.261   1.00 24.46  ? 302 UUC A O2  1 
HETATM 2151 O O3  . UUC C 3 .   ? 15.722 8.382  9.695   1.00 29.27  ? 302 UUC A O3  1 
HETATM 2152 O O4  . UUC C 3 .   ? 14.062 9.567  11.851  1.00 31.87  ? 302 UUC A O4  1 
HETATM 2153 O O5  . UUC C 3 .   ? 14.926 4.060  12.984  0.70 50.41  ? 302 UUC A O5  1 
HETATM 2154 O O6  . UUC C 3 .   ? 16.969 4.137  12.512  0.70 48.93  ? 302 UUC A O6  1 
HETATM 2155 O O7  . UUC C 3 .   ? 18.764 8.302  13.080  1.00 33.03  ? 302 UUC A O7  1 
HETATM 2156 O O8  . UUC C 3 .   ? 18.876 9.626  16.209  1.00 34.83  ? 302 UUC A O8  1 
HETATM 2157 O O9  . UUC C 3 .   ? 19.262 7.239  15.775  1.00 37.03  ? 302 UUC A O9  1 
HETATM 2158 S S1  . UUC C 3 .   ? 15.818 4.933  12.435  0.70 46.70  ? 302 UUC A S1  1 
HETATM 2159 O O   . HOH D 4 .   ? 23.370 12.059 22.484  1.00 52.48  ? 401 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 2.766  24.162 22.733  1.00 53.00  ? 402 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 9.705  6.556  1.418   1.00 41.53  ? 403 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 26.480 21.820 23.940  1.00 44.55  ? 404 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 15.790 30.669 7.121   1.00 42.14  ? 405 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 24.146 8.144  -8.939  1.00 25.10  ? 406 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 10.451 5.616  -14.373 1.00 34.66  ? 407 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 13.329 18.846 0.510   1.00 33.30  ? 408 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 25.881 27.058 6.780   1.00 58.67  ? 409 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 32.086 15.805 24.098  1.00 46.30  ? 410 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 20.121 26.491 2.701   1.00 29.51  ? 412 HOH A O   1 
HETATM 2170 O O   . HOH D 4 .   ? 22.005 23.283 -5.278  1.00 26.21  ? 413 HOH A O   1 
HETATM 2171 O O   . HOH D 4 .   ? 13.598 22.215 -5.984  1.00 35.50  ? 414 HOH A O   1 
HETATM 2172 O O   . HOH D 4 .   ? 10.204 13.517 12.977  1.00 46.52  ? 415 HOH A O   1 
HETATM 2173 O O   . HOH D 4 .   ? 8.243  4.541  -10.391 1.00 42.87  ? 416 HOH A O   1 
HETATM 2174 O O   . HOH D 4 .   ? 26.950 3.419  -4.696  1.00 41.03  ? 417 HOH A O   1 
HETATM 2175 O O   . HOH D 4 .   ? 13.555 26.710 -0.365  1.00 37.91  ? 418 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 11.211 7.343  -0.666  1.00 26.92  ? 419 HOH A O   1 
HETATM 2177 O O   . HOH D 4 .   ? 33.384 21.145 13.628  1.00 32.18  ? 420 HOH A O   1 
HETATM 2178 O O   . HOH D 4 .   ? 8.869  16.095 6.309   1.00 35.64  ? 421 HOH A O   1 
HETATM 2179 O O   . HOH D 4 .   ? 8.652  17.994 18.186  1.00 35.81  ? 422 HOH A O   1 
HETATM 2180 O O   . HOH D 4 .   ? 17.512 10.539 18.284  1.00 35.04  ? 423 HOH A O   1 
HETATM 2181 O O   . HOH D 4 .   ? 13.685 10.913 4.379   1.00 21.56  ? 424 HOH A O   1 
HETATM 2182 O O   . HOH D 4 .   ? 25.250 3.397  -1.997  1.00 34.82  ? 425 HOH A O   1 
HETATM 2183 O O   . HOH D 4 .   ? 27.570 5.558  -1.681  1.00 47.97  ? 426 HOH A O   1 
HETATM 2184 O O   . HOH D 4 .   ? 29.260 6.646  4.828   1.00 18.47  ? 427 HOH A O   1 
HETATM 2185 O O   . HOH D 4 .   ? 30.743 5.129  11.883  1.00 33.51  ? 428 HOH A O   1 
HETATM 2186 O O   . HOH D 4 .   ? 7.881  31.651 42.007  1.00 25.75  ? 429 HOH A O   1 
HETATM 2187 O O   . HOH D 4 .   ? 12.272 14.484 33.377  1.00 36.81  ? 430 HOH A O   1 
HETATM 2188 O O   . HOH D 4 .   ? 22.722 11.393 0.403   1.00 15.76  ? 431 HOH A O   1 
HETATM 2189 O O   . HOH D 4 .   ? 20.525 26.792 -4.654  1.00 35.04  ? 432 HOH A O   1 
HETATM 2190 O O   . HOH D 4 .   ? 25.486 9.375  -6.631  1.00 20.01  ? 433 HOH A O   1 
HETATM 2191 O O   . HOH D 4 .   ? 14.575 -3.823 -5.445  1.00 36.99  ? 434 HOH A O   1 
HETATM 2192 O O   . HOH D 4 .   ? 12.115 1.540  -5.560  1.00 31.41  ? 435 HOH A O   1 
HETATM 2193 O O   . HOH D 4 .   ? 20.663 11.654 4.893   1.00 18.49  ? 436 HOH A O   1 
HETATM 2194 O O   . HOH D 4 .   ? 5.567  26.141 -6.188  1.00 53.30  ? 437 HOH A O   1 
HETATM 2195 O O   . HOH D 4 .   ? 20.217 22.000 19.697  1.00 33.56  ? 438 HOH A O   1 
HETATM 2196 O O   . HOH D 4 .   ? 14.520 21.638 -14.070 1.00 65.23  ? 439 HOH A O   1 
HETATM 2197 O O   . HOH D 4 .   ? 13.310 10.399 -18.801 1.00 44.52  ? 440 HOH A O   1 
HETATM 2198 O O   . HOH D 4 .   ? 1.234  8.785  0.710   1.00 43.82  ? 441 HOH A O   1 
HETATM 2199 O O   . HOH D 4 .   ? 27.994 26.196 -2.648  1.00 37.26  ? 442 HOH A O   1 
HETATM 2200 O O   . HOH D 4 .   ? 31.698 4.694  -4.180  1.00 33.38  ? 443 HOH A O   1 
HETATM 2201 O O   . HOH D 4 .   ? 10.468 25.117 -7.423  1.00 57.19  ? 444 HOH A O   1 
HETATM 2202 O O   . HOH D 4 .   ? 22.361 21.042 7.083   1.00 21.32  ? 445 HOH A O   1 
HETATM 2203 O O   . HOH D 4 .   ? 2.012  17.009 0.143   1.00 57.87  ? 446 HOH A O   1 
HETATM 2204 O O   . HOH D 4 .   ? 23.260 7.377  10.929  1.00 29.52  ? 447 HOH A O   1 
HETATM 2205 O O   . HOH D 4 .   ? 14.428 -1.392 -9.345  1.00 49.46  ? 448 HOH A O   1 
HETATM 2206 O O   . HOH D 4 .   ? 26.128 6.748  -3.816  1.00 26.51  ? 449 HOH A O   1 
HETATM 2207 O O   . HOH D 4 .   ? 20.434 7.845  10.794  1.00 30.15  ? 450 HOH A O   1 
HETATM 2208 O O   . HOH D 4 .   ? 16.830 34.418 14.146  1.00 58.30  ? 451 HOH A O   1 
HETATM 2209 O O   . HOH D 4 .   ? 18.796 35.612 12.886  1.00 60.29  ? 452 HOH A O   1 
HETATM 2210 O O   . HOH D 4 .   ? 15.121 28.327 -1.959  1.00 43.28  ? 453 HOH A O   1 
HETATM 2211 O O   . HOH D 4 .   ? 24.416 5.007  9.900   1.00 29.61  ? 454 HOH A O   1 
HETATM 2212 O O   . HOH D 4 .   ? 15.319 28.505 12.137  1.00 33.13  ? 455 HOH A O   1 
HETATM 2213 O O   . HOH D 4 .   ? 23.434 0.787  -1.816  1.00 37.47  ? 456 HOH A O   1 
HETATM 2214 O O   . HOH D 4 .   ? 8.477  20.548 3.869   1.00 39.22  ? 457 HOH A O   1 
HETATM 2215 O O   . HOH D 4 .   ? 5.659  18.494 12.489  1.00 40.46  ? 458 HOH A O   1 
HETATM 2216 O O   . HOH D 4 .   ? 18.319 6.873  18.422  1.00 42.13  ? 459 HOH A O   1 
HETATM 2217 O O   . HOH D 4 .   ? 27.430 27.239 -8.109  1.00 47.40  ? 460 HOH A O   1 
HETATM 2218 O O   . HOH D 4 .   ? 26.278 -1.778 -8.502  1.00 38.55  ? 461 HOH A O   1 
HETATM 2219 O O   . HOH D 4 .   ? 2.766  5.244  -14.048 1.00 56.16  ? 462 HOH A O   1 
HETATM 2220 O O   . HOH D 4 .   ? 14.759 16.978 20.360  1.00 37.04  ? 463 HOH A O   1 
HETATM 2221 O O   . HOH D 4 .   ? 8.051  12.745 15.956  1.00 64.80  ? 464 HOH A O   1 
HETATM 2222 O O   . HOH D 4 .   ? 21.468 1.379  -13.031 1.00 36.85  ? 465 HOH A O   1 
HETATM 2223 O O   . HOH D 4 .   ? 24.523 1.509  -5.207  1.00 37.42  ? 466 HOH A O   1 
HETATM 2224 O O   . HOH D 4 .   ? 10.441 3.931  -12.018 1.00 34.61  ? 467 HOH A O   1 
HETATM 2225 O O   . HOH D 4 .   ? 5.299  26.983 9.888   1.00 38.48  ? 468 HOH A O   1 
HETATM 2226 O O   . HOH D 4 .   ? 4.663  18.560 29.185  1.00 34.29  ? 469 HOH A O   1 
HETATM 2227 O O   . HOH D 4 .   ? 22.981 -7.980 -13.554 1.00 36.55  ? 470 HOH A O   1 
HETATM 2228 O O   . HOH D 4 .   ? 25.370 0.671  6.016   1.00 46.82  ? 471 HOH A O   1 
HETATM 2229 O O   . HOH D 4 .   ? 15.282 -0.606 -12.065 1.00 68.06  ? 472 HOH A O   1 
HETATM 2230 O O   . HOH D 4 .   ? 17.925 22.956 -14.323 1.00 53.25  ? 473 HOH A O   1 
HETATM 2231 O O   . HOH D 4 .   ? 21.204 21.087 1.240   1.00 28.47  ? 474 HOH A O   1 
HETATM 2232 O O   . HOH D 4 .   ? 26.252 30.176 10.865  1.00 45.71  ? 475 HOH A O   1 
HETATM 2233 O O   . HOH D 4 .   ? 26.908 21.445 -14.619 1.00 33.13  ? 476 HOH A O   1 
HETATM 2234 O O   . HOH D 4 .   ? 9.411  34.767 41.986  1.00 46.69  ? 477 HOH A O   1 
HETATM 2235 O O   . HOH D 4 .   ? 1.318  22.112 29.230  1.00 54.20  ? 478 HOH A O   1 
HETATM 2236 O O   . HOH D 4 .   ? 33.587 20.487 22.966  1.00 58.79  ? 479 HOH A O   1 
HETATM 2237 O O   . HOH D 4 .   ? 12.706 11.383 18.699  1.00 38.55  ? 480 HOH A O   1 
HETATM 2238 O O   . HOH D 4 .   ? 25.447 0.999  1.801   1.00 61.03  ? 481 HOH A O   1 
HETATM 2239 O O   . HOH D 4 .   ? 29.791 4.051  7.745   1.00 45.21  ? 482 HOH A O   1 
HETATM 2240 O O   . HOH D 4 .   ? 14.975 1.551  14.665  1.00 54.27  ? 483 HOH A O   1 
HETATM 2241 O O   . HOH D 4 .   ? 27.508 27.222 9.735   1.00 44.95  ? 484 HOH A O   1 
HETATM 2242 O O   . HOH D 4 .   ? 18.597 20.017 -14.263 1.00 33.14  ? 485 HOH A O   1 
HETATM 2243 O O   . HOH D 4 .   ? 15.752 8.801  19.829  1.00 50.54  ? 486 HOH A O   1 
HETATM 2244 O O   . HOH D 4 .   ? 32.318 26.593 3.727   1.00 54.03  ? 487 HOH A O   1 
HETATM 2245 O O   . HOH D 4 .   ? 20.892 11.354 23.292  1.00 60.22  ? 488 HOH A O   1 
HETATM 2246 O O   . HOH D 4 .   ? 17.286 18.102 -20.356 1.00 54.30  ? 489 HOH A O   1 
HETATM 2247 O O   . HOH D 4 .   ? 21.001 14.371 32.206  1.00 49.17  ? 490 HOH A O   1 
HETATM 2248 O O   . HOH D 4 .   ? 14.634 9.870  17.388  1.00 41.09  ? 491 HOH A O   1 
HETATM 2249 O O   . HOH D 4 .   ? 9.822  2.268  -14.321 1.00 51.23  ? 492 HOH A O   1 
HETATM 2250 O O   . HOH D 4 .   ? 10.783 26.535 -0.045  1.00 49.00  ? 493 HOH A O   1 
HETATM 2251 O O   . HOH D 4 .   ? 33.518 26.040 11.887  1.00 51.81  ? 494 HOH A O   1 
HETATM 2252 O O   . HOH D 4 .   ? 2.104  6.825  1.443   1.00 47.00  ? 495 HOH A O   1 
HETATM 2253 O O   . HOH D 4 .   ? 25.462 22.668 -17.202 1.00 53.33  ? 496 HOH A O   1 
HETATM 2254 O O   . HOH D 4 .   ? 3.441  22.062 -1.125  1.00 54.13  ? 497 HOH A O   1 
HETATM 2255 O O   . HOH D 4 .   ? 16.288 19.537 -16.135 1.00 48.97  ? 498 HOH A O   1 
HETATM 2256 O O   . HOH D 4 .   ? 35.544 10.311 23.985  1.00 52.96  ? 499 HOH A O   1 
HETATM 2257 O O   . HOH D 4 .   ? 16.157 27.768 -4.060  1.00 48.92  ? 500 HOH A O   1 
HETATM 2258 O O   . HOH D 4 .   ? 25.140 16.744 25.151  1.00 46.99  ? 501 HOH A O   1 
HETATM 2259 O O   . HOH D 4 .   ? 30.161 4.813  -1.966  1.00 40.92  ? 502 HOH A O   1 
HETATM 2260 O O   . HOH D 4 .   ? 7.809  17.816 4.601   1.00 42.04  ? 503 HOH A O   1 
HETATM 2261 O O   . HOH D 4 .   ? 13.893 8.204  5.544   1.00 41.49  ? 504 HOH A O   1 
HETATM 2262 O O   . HOH D 4 .   ? 14.983 38.007 8.118   1.00 75.87  ? 505 HOH A O   1 
HETATM 2263 O O   . HOH D 4 .   ? 0.764  14.051 -2.480  1.00 52.72  ? 506 HOH A O   1 
HETATM 2264 O O   . HOH D 4 .   ? 12.012 7.694  7.775   1.00 45.76  ? 507 HOH A O   1 
HETATM 2265 O O   . HOH D 4 .   ? 27.277 16.009 26.004  1.00 58.01  ? 508 HOH A O   1 
HETATM 2266 O O   . HOH D 4 .   ? 34.630 4.459  26.257  1.00 55.82  ? 509 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 0.9020 0.5603 0.6624 0.1225  0.0542  -0.1884 1   MET A N   
2    C CA  . MET A 1   ? 0.8849 0.5366 0.6430 0.1226  0.0501  -0.1693 1   MET A CA  
3    C C   . MET A 1   ? 0.8142 0.5156 0.5955 0.1388  0.0409  -0.1594 1   MET A C   
4    O O   . MET A 1   ? 0.7511 0.5018 0.5534 0.1346  0.0394  -0.1634 1   MET A O   
5    C CB  . MET A 1   ? 0.8773 0.5357 0.6363 0.0921  0.0540  -0.1671 1   MET A CB  
6    C CG  . MET A 1   ? 0.8907 0.5513 0.6503 0.0901  0.0502  -0.1488 1   MET A CG  
7    S SD  . MET A 1   ? 0.9013 0.5523 0.6538 0.0552  0.0581  -0.1491 1   MET A SD  
8    C CE  . MET A 1   ? 0.8511 0.5639 0.6286 0.0391  0.0571  -0.1643 1   MET A CE  
9    N N   . LYS A 2   ? 0.8708 0.5581 0.6461 0.1570  0.0356  -0.1469 2   LYS A N   
10   C CA  . LYS A 2   ? 0.7994 0.5339 0.5967 0.1712  0.0277  -0.1405 2   LYS A CA  
11   C C   . LYS A 2   ? 0.7208 0.4917 0.5348 0.1514  0.0269  -0.1323 2   LYS A C   
12   O O   . LYS A 2   ? 0.7538 0.5067 0.5583 0.1350  0.0290  -0.1250 2   LYS A O   
13   C CB  . LYS A 2   ? 0.7837 0.4972 0.5689 0.1957  0.0213  -0.1308 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.7777 0.4616 0.5486 0.2233  0.0205  -0.1386 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.7727 0.4514 0.5356 0.2534  0.0114  -0.1296 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.8044 0.4688 0.5618 0.2769  0.0096  -0.1341 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.8446 0.5140 0.5961 0.3051  -0.0011 -0.1240 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.6420 0.4628 0.4798 0.1528  0.0252  -0.1342 3   TYR A N   
19   C CA  . TYR A 3   ? 0.5796 0.4331 0.4323 0.1373  0.0255  -0.1269 3   TYR A CA  
20   C C   . TYR A 3   ? 0.5721 0.4673 0.4456 0.1467  0.0236  -0.1263 3   TYR A C   
21   O O   . TYR A 3   ? 0.5424 0.4505 0.4222 0.1619  0.0231  -0.1346 3   TYR A O   
22   C CB  . TYR A 3   ? 0.5666 0.4340 0.4219 0.1194  0.0302  -0.1325 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.5734 0.4725 0.4396 0.1245  0.0326  -0.1412 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.5565 0.4451 0.4160 0.1325  0.0347  -0.1544 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.5326 0.4689 0.4134 0.1213  0.0342  -0.1363 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.5803 0.4995 0.4483 0.1367  0.0379  -0.1630 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.5048 0.4674 0.3917 0.1249  0.0384  -0.1433 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.5590 0.5152 0.4399 0.1324  0.0399  -0.1567 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.5408 0.5247 0.4265 0.1353  0.0450  -0.1640 3   TYR A OH  
30   N N   . MET A 4   ? 0.5425 0.4594 0.4271 0.1364  0.0239  -0.1180 4   MET A N   
31   C CA  . MET A 4   ? 0.5243 0.4799 0.4282 0.1378  0.0260  -0.1186 4   MET A CA  
32   C C   . MET A 4   ? 0.4582 0.4272 0.3674 0.1214  0.0304  -0.1114 4   MET A C   
33   O O   . MET A 4   ? 0.4541 0.4081 0.3551 0.1113  0.0298  -0.1060 4   MET A O   
34   C CB  . MET A 4   ? 0.5242 0.4910 0.4361 0.1492  0.0211  -0.1173 4   MET A CB  
35   C CG  . MET A 4   ? 0.5513 0.5085 0.4593 0.1421  0.0179  -0.1068 4   MET A CG  
36   S SD  . MET A 4   ? 0.5797 0.5674 0.5054 0.1264  0.0239  -0.1028 4   MET A SD  
37   C CE  . MET A 4   ? 0.5681 0.5949 0.5141 0.1354  0.0253  -0.1135 4   MET A CE  
38   N N   . ILE A 5   ? 0.4245 0.4215 0.3466 0.1190  0.0360  -0.1118 5   ILE A N   
39   C CA  . ILE A 5   ? 0.4002 0.4061 0.3241 0.1071  0.0414  -0.1042 5   ILE A CA  
40   C C   . ILE A 5   ? 0.4130 0.4370 0.3505 0.1045  0.0463  -0.1024 5   ILE A C   
41   O O   . ILE A 5   ? 0.3852 0.4285 0.3320 0.1077  0.0509  -0.1097 5   ILE A O   
42   C CB  . ILE A 5   ? 0.4020 0.4174 0.3204 0.1047  0.0471  -0.1062 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.3971 0.3994 0.3039 0.1062  0.0431  -0.1129 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.3898 0.4093 0.3053 0.0968  0.0514  -0.0962 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.4607 0.4765 0.3601 0.1043  0.0474  -0.1163 5   ILE A CD1 
46   N N   . THR A 6   ? 0.3647 0.3842 0.3037 0.0973  0.0465  -0.0948 6   THR A N   
47   C CA  . THR A 6   ? 0.3958 0.4293 0.3459 0.0910  0.0538  -0.0941 6   THR A CA  
48   C C   . THR A 6   ? 0.4545 0.4856 0.3991 0.0838  0.0635  -0.0868 6   THR A C   
49   O O   . THR A 6   ? 0.5262 0.5471 0.4599 0.0841  0.0614  -0.0805 6   THR A O   
50   C CB  A THR A 6   ? 0.4255 0.4550 0.3795 0.0879  0.0497  -0.0912 6   THR A CB  
51   C CB  B THR A 6   ? 0.4259 0.4551 0.3797 0.0879  0.0496  -0.0911 6   THR A CB  
52   O OG1 A THR A 6   ? 0.3889 0.4020 0.3338 0.0832  0.0482  -0.0824 6   THR A OG1 
53   O OG1 B THR A 6   ? 0.4394 0.4531 0.3843 0.0940  0.0394  -0.0897 6   THR A OG1 
54   C CG2 A THR A 6   ? 0.4376 0.4666 0.3915 0.0979  0.0395  -0.0958 6   THR A CG2 
55   C CG2 B THR A 6   ? 0.4118 0.4629 0.3805 0.0871  0.0519  -0.0995 6   THR A CG2 
56   N N   . SER A 7   ? 0.4449 0.4855 0.3959 0.0775  0.0747  -0.0882 7   SER A N   
57   C CA  . SER A 7   ? 0.4447 0.4765 0.3861 0.0721  0.0862  -0.0796 7   SER A CA  
58   C C   . SER A 7   ? 0.4455 0.4723 0.3930 0.0625  0.0951  -0.0781 7   SER A C   
59   O O   . SER A 7   ? 0.4432 0.4840 0.4056 0.0571  0.0963  -0.0879 7   SER A O   
60   C CB  . SER A 7   ? 0.4503 0.4911 0.3868 0.0712  0.0964  -0.0824 7   SER A CB  
61   O OG  . SER A 7   ? 0.5074 0.5349 0.4311 0.0658  0.1101  -0.0727 7   SER A OG  
62   N N   . LYS A 8   ? 0.4163 0.4242 0.3521 0.0614  0.1011  -0.0672 8   LYS A N   
63   C CA  . LYS A 8   ? 0.4899 0.4862 0.4276 0.0516  0.1136  -0.0659 8   LYS A CA  
64   C C   . LYS A 8   ? 0.5195 0.5203 0.4594 0.0405  0.1302  -0.0719 8   LYS A C   
65   O O   . LYS A 8   ? 0.5407 0.5382 0.4879 0.0279  0.1413  -0.0775 8   LYS A O   
66   C CB  . LYS A 8   ? 0.5087 0.4807 0.4295 0.0570  0.1175  -0.0521 8   LYS A CB  
67   C CG  . LYS A 8   ? 0.5369 0.4863 0.4526 0.0486  0.1343  -0.0489 8   LYS A CG  
68   C CD  . LYS A 8   ? 0.6070 0.5309 0.5018 0.0599  0.1378  -0.0339 8   LYS A CD  
69   C CE  . LYS A 8   ? 0.6699 0.5646 0.5590 0.0525  0.1544  -0.0317 8   LYS A CE  
70   N NZ  . LYS A 8   ? 0.6657 0.5710 0.5765 0.0404  0.1522  -0.0451 8   LYS A NZ  
71   N N   . GLY A 9   ? 0.5111 0.5203 0.4447 0.0431  0.1334  -0.0724 9   GLY A N   
72   C CA  . GLY A 9   ? 0.5161 0.5351 0.4536 0.0307  0.1498  -0.0805 9   GLY A CA  
73   C C   . GLY A 9   ? 0.5655 0.5569 0.4801 0.0241  0.1698  -0.0692 9   GLY A C   
74   O O   . GLY A 9   ? 0.6285 0.6249 0.5442 0.0102  0.1870  -0.0759 9   GLY A O   
75   N N   . ASP A 10  ? 0.5541 0.5168 0.4470 0.0341  0.1689  -0.0526 10  ASP A N   
76   C CA  . ASP A 10  ? 0.6354 0.5697 0.4993 0.0341  0.1861  -0.0387 10  ASP A CA  
77   C C   . ASP A 10  ? 0.6718 0.6192 0.5217 0.0442  0.1819  -0.0350 10  ASP A C   
78   O O   . ASP A 10  ? 0.6206 0.5946 0.4829 0.0520  0.1651  -0.0426 10  ASP A O   
79   C CB  . ASP A 10  ? 0.6559 0.5561 0.5006 0.0450  0.1863  -0.0227 10  ASP A CB  
80   C CG  . ASP A 10  ? 0.6651 0.5762 0.5060 0.0651  0.1654  -0.0161 10  ASP A CG  
81   O OD1 . ASP A 10  ? 0.7456 0.6395 0.5611 0.0796  0.1662  -0.0012 10  ASP A OD1 
82   O OD2 . ASP A 10  ? 0.6188 0.5561 0.4807 0.0664  0.1488  -0.0263 10  ASP A OD2 
83   N N   . GLU A 11  ? 0.7358 0.6613 0.5568 0.0437  0.1986  -0.0231 11  GLU A N   
84   C CA  . GLU A 11  ? 0.7409 0.6803 0.5461 0.0513  0.1975  -0.0207 11  GLU A CA  
85   C C   . GLU A 11  ? 0.6963 0.6489 0.4976 0.0713  0.1751  -0.0167 11  GLU A C   
86   O O   . GLU A 11  ? 0.7018 0.6821 0.5115 0.0750  0.1643  -0.0266 11  GLU A O   
87   C CB  . GLU A 11  ? 0.8180 0.7251 0.5859 0.0492  0.2198  -0.0049 11  GLU A CB  
88   C CG  . GLU A 11  ? 0.8646 0.7831 0.6088 0.0587  0.2197  0.0004  11  GLU A CG  
89   C CD  . GLU A 11  ? 0.9439 0.8298 0.6506 0.0523  0.2458  0.0145  11  GLU A CD  
90   O OE1 . GLU A 11  ? 0.9670 0.8286 0.6740 0.0334  0.2669  0.0136  11  GLU A OE1 
91   O OE2 . GLU A 11  ? 0.9816 0.8654 0.6566 0.0653  0.2462  0.0261  11  GLU A OE2 
92   N N   . LYS A 12  ? 0.6854 0.6198 0.4752 0.0837  0.1684  -0.0043 12  LYS A N   
93   C CA  . LYS A 12  ? 0.6599 0.6111 0.4464 0.1007  0.1486  -0.0023 12  LYS A CA  
94   C C   . LYS A 12  ? 0.5789 0.5576 0.3954 0.0974  0.1314  -0.0187 12  LYS A C   
95   O O   . LYS A 12  ? 0.5025 0.5020 0.3189 0.1040  0.1193  -0.0246 12  LYS A O   
96   C CB  . LYS A 12  ? 0.6714 0.6032 0.4456 0.1141  0.1451  0.0110  12  LYS A CB  
97   C CG  . LYS A 12  ? 0.6468 0.6027 0.4204 0.1298  0.1253  0.0103  12  LYS A CG  
98   C CD  . LYS A 12  ? 0.6490 0.5916 0.4098 0.1462  0.1221  0.0227  12  LYS A CD  
99   C CE  . LYS A 12  ? 0.6590 0.6339 0.4166 0.1619  0.1039  0.0203  12  LYS A CE  
100  N NZ  . LYS A 12  ? 0.6860 0.6585 0.4384 0.1790  0.0980  0.0282  12  LYS A NZ  
101  N N   . SER A 13  ? 0.5609 0.5382 0.4010 0.0872  0.1309  -0.0265 13  SER A N   
102  C CA  . SER A 13  ? 0.4880 0.4842 0.3511 0.0862  0.1151  -0.0392 13  SER A CA  
103  C C   . SER A 13  ? 0.4747 0.4905 0.3484 0.0822  0.1145  -0.0525 13  SER A C   
104  O O   . SER A 13  ? 0.4629 0.4914 0.3434 0.0868  0.1017  -0.0608 13  SER A O   
105  C CB  . SER A 13  ? 0.4367 0.4260 0.3177 0.0790  0.1142  -0.0422 13  SER A CB  
106  O OG  . SER A 13  ? 0.4716 0.4437 0.3440 0.0842  0.1143  -0.0315 13  SER A OG  
107  N N   . ASP A 14  ? 0.5163 0.5342 0.3913 0.0732  0.1293  -0.0560 14  ASP A N   
108  C CA  . ASP A 14  ? 0.5310 0.5722 0.4176 0.0712  0.1293  -0.0703 14  ASP A CA  
109  C C   . ASP A 14  ? 0.5338 0.5835 0.4045 0.0799  0.1257  -0.0706 14  ASP A C   
110  O O   . ASP A 14  ? 0.4729 0.5383 0.3530 0.0845  0.1166  -0.0828 14  ASP A O   
111  C CB  . ASP A 14  ? 0.5878 0.6347 0.4798 0.0577  0.1479  -0.0757 14  ASP A CB  
112  C CG  . ASP A 14  ? 0.6193 0.6725 0.5352 0.0483  0.1486  -0.0846 14  ASP A CG  
113  O OD1 . ASP A 14  ? 0.5879 0.6391 0.5140 0.0537  0.1342  -0.0850 14  ASP A OD1 
114  O OD2 . ASP A 14  ? 0.6492 0.7114 0.5731 0.0344  0.1641  -0.0922 14  ASP A OD2 
115  N N   . LEU A 15  ? 0.5817 0.6201 0.4264 0.0833  0.1331  -0.0576 15  LEU A N   
116  C CA  . LEU A 15  ? 0.5922 0.6424 0.4195 0.0915  0.1298  -0.0586 15  LEU A CA  
117  C C   . LEU A 15  ? 0.5267 0.5844 0.3576 0.1002  0.1108  -0.0631 15  LEU A C   
118  O O   . LEU A 15  ? 0.4775 0.5505 0.3100 0.1032  0.1043  -0.0751 15  LEU A O   
119  C CB  . LEU A 15  ? 0.6434 0.6793 0.4380 0.0956  0.1413  -0.0417 15  LEU A CB  
120  C CG  . LEU A 15  ? 0.6960 0.7191 0.4796 0.0842  0.1644  -0.0365 15  LEU A CG  
121  C CD1 . LEU A 15  ? 0.7396 0.7396 0.4837 0.0919  0.1749  -0.0161 15  LEU A CD1 
122  C CD2 . LEU A 15  ? 0.6490 0.6968 0.4412 0.0766  0.1718  -0.0519 15  LEU A CD2 
123  N N   . LEU A 16  ? 0.5071 0.5542 0.3397 0.1032  0.1031  -0.0554 16  LEU A N   
124  C CA  . LEU A 16  ? 0.5209 0.5763 0.3591 0.1074  0.0871  -0.0619 16  LEU A CA  
125  C C   . LEU A 16  ? 0.5058 0.5651 0.3638 0.1029  0.0805  -0.0772 16  LEU A C   
126  O O   . LEU A 16  ? 0.4892 0.5563 0.3463 0.1048  0.0726  -0.0877 16  LEU A O   
127  C CB  . LEU A 16  ? 0.4945 0.5403 0.3350 0.1095  0.0819  -0.0529 16  LEU A CB  
128  C CG  . LEU A 16  ? 0.4894 0.5473 0.3331 0.1120  0.0677  -0.0593 16  LEU A CG  
129  C CD1 . LEU A 16  ? 0.5082 0.5858 0.3342 0.1194  0.0641  -0.0620 16  LEU A CD1 
130  C CD2 . LEU A 16  ? 0.4216 0.4741 0.2692 0.1142  0.0638  -0.0514 16  LEU A CD2 
131  N N   . ARG A 17  ? 0.4758 0.5291 0.3499 0.0978  0.0842  -0.0793 17  ARG A N   
132  C CA  . ARG A 17  ? 0.4174 0.4732 0.3071 0.0980  0.0780  -0.0923 17  ARG A CA  
133  C C   . ARG A 17  ? 0.4090 0.4779 0.2962 0.1017  0.0803  -0.1042 17  ARG A C   
134  O O   . ARG A 17  ? 0.4545 0.5216 0.3431 0.1057  0.0724  -0.1147 17  ARG A O   
135  C CB  . ARG A 17  ? 0.4167 0.4716 0.3229 0.0937  0.0818  -0.0929 17  ARG A CB  
136  C CG  . ARG A 17  ? 0.4335 0.4940 0.3537 0.0984  0.0754  -0.1055 17  ARG A CG  
137  C CD  . ARG A 17  ? 0.4067 0.4736 0.3433 0.0950  0.0777  -0.1072 17  ARG A CD  
138  N NE  . ARG A 17  ? 0.3734 0.4489 0.3214 0.1040  0.0704  -0.1188 17  ARG A NE  
139  C CZ  . ARG A 17  ? 0.5000 0.5964 0.4561 0.1090  0.0744  -0.1308 17  ARG A CZ  
140  N NH1 . ARG A 17  ? 0.4897 0.5996 0.4432 0.1027  0.0869  -0.1324 17  ARG A NH1 
141  N NH2 . ARG A 17  ? 0.5225 0.6264 0.4878 0.1214  0.0664  -0.1409 17  ARG A NH2 
142  N N   . LEU A 18  ? 0.4194 0.4992 0.3013 0.0997  0.0925  -0.1034 18  LEU A N   
143  C CA  . LEU A 18  ? 0.4910 0.5864 0.3708 0.1032  0.0959  -0.1160 18  LEU A CA  
144  C C   . LEU A 18  ? 0.4823 0.5793 0.3461 0.1078  0.0892  -0.1197 18  LEU A C   
145  O O   . LEU A 18  ? 0.4449 0.5475 0.3107 0.1120  0.0857  -0.1342 18  LEU A O   
146  C CB  . LEU A 18  ? 0.4833 0.5904 0.3573 0.0976  0.1126  -0.1137 18  LEU A CB  
147  C CG  . LEU A 18  ? 0.4778 0.5939 0.3711 0.0904  0.1219  -0.1184 18  LEU A CG  
148  C CD1 . LEU A 18  ? 0.4553 0.5836 0.3398 0.0819  0.1412  -0.1185 18  LEU A CD1 
149  C CD2 . LEU A 18  ? 0.4237 0.5537 0.3392 0.0977  0.1132  -0.1351 18  LEU A CD2 
150  N N   . ASN A 19  ? 0.4823 0.5762 0.3301 0.1078  0.0874  -0.1081 19  ASN A N   
151  C CA  . ASN A 19  ? 0.4822 0.5850 0.3160 0.1112  0.0801  -0.1138 19  ASN A CA  
152  C C   . ASN A 19  ? 0.4759 0.5704 0.3197 0.1097  0.0682  -0.1247 19  ASN A C   
153  O O   . ASN A 19  ? 0.5120 0.6123 0.3508 0.1099  0.0643  -0.1387 19  ASN A O   
154  C CB  . ASN A 19  ? 0.5201 0.6263 0.3352 0.1146  0.0798  -0.0990 19  ASN A CB  
155  C CG  . ASN A 19  ? 0.5479 0.6642 0.3400 0.1186  0.0901  -0.0927 19  ASN A CG  
156  O OD1 . ASN A 19  ? 0.5214 0.6479 0.3112 0.1174  0.0964  -0.1028 19  ASN A OD1 
157  N ND2 . ASN A 19  ? 0.6010 0.7138 0.3735 0.1246  0.0924  -0.0758 19  ASN A ND2 
158  N N   . MET A 20  ? 0.4324 0.5116 0.2882 0.1067  0.0635  -0.1190 20  MET A N   
159  C CA  . MET A 20  ? 0.4310 0.4974 0.2925 0.1034  0.0547  -0.1283 20  MET A CA  
160  C C   . MET A 20  ? 0.4517 0.5071 0.3195 0.1068  0.0549  -0.1415 20  MET A C   
161  O O   . MET A 20  ? 0.5117 0.5570 0.3754 0.1053  0.0511  -0.1541 20  MET A O   
162  C CB  . MET A 20  ? 0.4171 0.4698 0.2873 0.0995  0.0507  -0.1186 20  MET A CB  
163  C CG  . MET A 20  ? 0.4679 0.5308 0.3321 0.0982  0.0487  -0.1086 20  MET A CG  
164  S SD  . MET A 20  ? 0.5080 0.5567 0.3831 0.0931  0.0448  -0.1002 20  MET A SD  
165  C CE  . MET A 20  ? 0.4787 0.5214 0.3535 0.0840  0.0376  -0.1138 20  MET A CE  
166  N N   . ILE A 21  ? 0.4489 0.5064 0.3266 0.1116  0.0598  -0.1401 21  ILE A N   
167  C CA  . ILE A 21  ? 0.4427 0.4952 0.3267 0.1195  0.0597  -0.1532 21  ILE A CA  
168  C C   . ILE A 21  ? 0.4603 0.5222 0.3344 0.1219  0.0624  -0.1672 21  ILE A C   
169  O O   . ILE A 21  ? 0.4770 0.5236 0.3483 0.1260  0.0594  -0.1804 21  ILE A O   
170  C CB  . ILE A 21  ? 0.4334 0.4995 0.3316 0.1239  0.0652  -0.1517 21  ILE A CB  
171  C CG1 . ILE A 21  ? 0.4513 0.5070 0.3595 0.1223  0.0610  -0.1419 21  ILE A CG1 
172  C CG2 . ILE A 21  ? 0.4460 0.5173 0.3501 0.1354  0.0659  -0.1675 21  ILE A CG2 
173  C CD1 . ILE A 21  ? 0.4369 0.5116 0.3606 0.1234  0.0667  -0.1422 21  ILE A CD1 
174  N N   . ALA A 22  ? 0.5158 0.6003 0.3818 0.1197  0.0691  -0.1645 22  ALA A N   
175  C CA  . ALA A 22  ? 0.5241 0.6216 0.3785 0.1214  0.0719  -0.1780 22  ALA A CA  
176  C C   . ALA A 22  ? 0.5144 0.6026 0.3590 0.1165  0.0645  -0.1865 22  ALA A C   
177  O O   . ALA A 22  ? 0.5083 0.5912 0.3488 0.1181  0.0642  -0.2040 22  ALA A O   
178  C CB  . ALA A 22  ? 0.4820 0.6033 0.3241 0.1196  0.0806  -0.1699 22  ALA A CB  
179  N N   . GLY A 23  ? 0.5512 0.6382 0.3925 0.1099  0.0592  -0.1763 23  GLY A N   
180  C CA  . GLY A 23  ? 0.5820 0.6649 0.4171 0.1022  0.0529  -0.1869 23  GLY A CA  
181  C C   . GLY A 23  ? 0.5806 0.6300 0.4209 0.0994  0.0506  -0.1972 23  GLY A C   
182  O O   . GLY A 23  ? 0.5624 0.6031 0.3959 0.0940  0.0503  -0.2144 23  GLY A O   
183  N N   . PHE A 24  ? 0.5221 0.5505 0.3723 0.1031  0.0497  -0.1870 24  PHE A N   
184  C CA  . PHE A 24  ? 0.5421 0.5337 0.3923 0.1045  0.0483  -0.1938 24  PHE A CA  
185  C C   . PHE A 24  ? 0.6025 0.5847 0.4497 0.1150  0.0518  -0.2095 24  PHE A C   
186  O O   . PHE A 24  ? 0.6552 0.6039 0.4946 0.1151  0.0521  -0.2204 24  PHE A O   
187  C CB  . PHE A 24  ? 0.4967 0.4741 0.3563 0.1099  0.0460  -0.1792 24  PHE A CB  
188  C CG  . PHE A 24  ? 0.5071 0.4799 0.3677 0.0989  0.0426  -0.1675 24  PHE A CG  
189  C CD1 . PHE A 24  ? 0.4850 0.4697 0.3550 0.1004  0.0418  -0.1521 24  PHE A CD1 
190  C CD2 . PHE A 24  ? 0.5547 0.5122 0.4073 0.0860  0.0413  -0.1739 24  PHE A CD2 
191  C CE1 . PHE A 24  ? 0.5070 0.4887 0.3782 0.0914  0.0391  -0.1427 24  PHE A CE1 
192  C CE2 . PHE A 24  ? 0.5583 0.5161 0.4133 0.0757  0.0390  -0.1648 24  PHE A CE2 
193  C CZ  . PHE A 24  ? 0.5131 0.4832 0.3774 0.0797  0.0374  -0.1489 24  PHE A CZ  
194  N N   . GLY A 25  ? 0.6131 0.6223 0.4648 0.1238  0.0559  -0.2113 25  GLY A N   
195  C CA  . GLY A 25  ? 0.6206 0.6276 0.4709 0.1349  0.0599  -0.2280 25  GLY A CA  
196  C C   . GLY A 25  ? 0.6786 0.6754 0.5164 0.1271  0.0613  -0.2448 25  GLY A C   
197  O O   . GLY A 25  ? 0.6559 0.6355 0.4922 0.1331  0.0641  -0.2553 25  GLY A O   
198  N N   . GLU A 26  ? 0.7401 0.7490 0.5694 0.1132  0.0595  -0.2474 26  GLU A N   
199  C CA  . GLU A 26  ? 0.7317 0.7365 0.5506 0.1018  0.0606  -0.2640 26  GLU A CA  
200  C C   . GLU A 26  ? 0.7432 0.7062 0.5553 0.0917  0.0604  -0.2740 26  GLU A C   
201  O O   . GLU A 26  ? 0.7620 0.7201 0.5657 0.0780  0.0622  -0.2888 26  GLU A O   
202  C CB  . GLU A 26  ? 0.7245 0.7709 0.5383 0.0919  0.0582  -0.2626 26  GLU A CB  
203  C CG  . GLU A 26  ? 0.7067 0.7887 0.5215 0.1004  0.0601  -0.2494 26  GLU A CG  
204  C CD  . GLU A 26  ? 0.7507 0.8405 0.5648 0.1063  0.0658  -0.2564 26  GLU A CD  
205  O OE1 . GLU A 26  ? 0.7451 0.8570 0.5605 0.1124  0.0701  -0.2461 26  GLU A OE1 
206  O OE2 . GLU A 26  ? 0.7500 0.8229 0.5611 0.1040  0.0673  -0.2727 26  GLU A OE2 
207  N N   . TYR A 27  ? 0.6976 0.6285 0.5127 0.0957  0.0586  -0.2623 27  TYR A N   
208  C CA  . TYR A 27  ? 0.7539 0.6375 0.5594 0.0848  0.0604  -0.2668 27  TYR A CA  
209  C C   . TYR A 27  ? 0.8061 0.6435 0.6075 0.1026  0.0616  -0.2618 27  TYR A C   
210  O O   . TYR A 27  ? 0.8043 0.6538 0.6140 0.1228  0.0599  -0.2565 27  TYR A O   
211  C CB  . TYR A 27  ? 0.7270 0.6172 0.5365 0.0693  0.0567  -0.2535 27  TYR A CB  
212  C CG  . TYR A 27  ? 0.6940 0.6315 0.5069 0.0549  0.0541  -0.2587 27  TYR A CG  
213  C CD1 . TYR A 27  ? 0.7219 0.6607 0.5276 0.0355  0.0569  -0.2791 27  TYR A CD1 
214  C CD2 . TYR A 27  ? 0.6280 0.6088 0.4497 0.0615  0.0493  -0.2439 27  TYR A CD2 
215  C CE1 . TYR A 27  ? 0.7304 0.7196 0.5394 0.0252  0.0527  -0.2852 27  TYR A CE1 
216  C CE2 . TYR A 27  ? 0.6216 0.6453 0.4431 0.0532  0.0458  -0.2473 27  TYR A CE2 
217  C CZ  . TYR A 27  ? 0.7179 0.7492 0.5339 0.0362  0.0465  -0.2681 27  TYR A CZ  
218  O OH  . TYR A 27  ? 0.7708 0.8516 0.5869 0.0307  0.0414  -0.2728 27  TYR A OH  
219  N N   . ASP A 28  ? 0.8730 0.6576 0.6599 0.0951  0.0651  -0.2639 28  ASP A N   
220  C CA  . ASP A 28  ? 0.9470 0.6819 0.7241 0.1138  0.0656  -0.2560 28  ASP A CA  
221  C C   . ASP A 28  ? 0.9654 0.7087 0.7512 0.1183  0.0589  -0.2322 28  ASP A C   
222  O O   . ASP A 28  ? 0.9722 0.6824 0.7475 0.1094  0.0596  -0.2225 28  ASP A O   
223  C CB  . ASP A 28  ? 1.0108 0.6794 0.7634 0.1035  0.0740  -0.2659 28  ASP A CB  
224  N N   . MET A 29  ? 0.9422 0.7313 0.7467 0.1308  0.0535  -0.2239 29  MET A N   
225  C CA  . MET A 29  ? 0.8983 0.7038 0.7140 0.1342  0.0476  -0.2041 29  MET A CA  
226  C C   . MET A 29  ? 0.8661 0.6899 0.6934 0.1589  0.0442  -0.2012 29  MET A C   
227  O O   . MET A 29  ? 0.8755 0.7323 0.7132 0.1655  0.0461  -0.2104 29  MET A O   
228  C CB  . MET A 29  ? 0.8652 0.7158 0.6940 0.1179  0.0461  -0.1974 29  MET A CB  
229  C CG  . MET A 29  ? 0.9174 0.7607 0.7388 0.0944  0.0479  -0.2001 29  MET A CG  
230  S SD  . MET A 29  ? 0.9909 0.7846 0.7991 0.0864  0.0487  -0.1898 29  MET A SD  
231  C CE  . MET A 29  ? 0.9821 0.8003 0.7944 0.0582  0.0498  -0.1918 29  MET A CE  
232  N N   . GLU A 30  ? 0.8050 0.6110 0.6305 0.1719  0.0395  -0.1896 30  GLU A N   
233  C CA  . GLU A 30  ? 0.7817 0.6087 0.6193 0.1962  0.0351  -0.1885 30  GLU A CA  
234  C C   . GLU A 30  ? 0.7564 0.6157 0.6099 0.1919  0.0306  -0.1741 30  GLU A C   
235  O O   . GLU A 30  ? 0.7460 0.5847 0.5917 0.1855  0.0276  -0.1616 30  GLU A O   
236  C CB  . GLU A 30  ? 0.8643 0.6472 0.6863 0.2170  0.0323  -0.1868 30  GLU A CB  
237  C CG  . GLU A 30  ? 0.8908 0.7029 0.7291 0.2397  0.0254  -0.1827 30  GLU A CG  
238  C CD  . GLU A 30  ? 0.9464 0.7151 0.7658 0.2596  0.0204  -0.1745 30  GLU A CD  
239  O OE1 . GLU A 30  ? 0.9870 0.7004 0.7824 0.2568  0.0252  -0.1752 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 0.9469 0.7369 0.7741 0.2772  0.0121  -0.1676 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.7011 0.6095 0.5757 0.1937  0.0316  -0.1767 31  TYR A N   
242  C CA  . TYR A 31  ? 0.6383 0.5763 0.5283 0.1892  0.0292  -0.1658 31  TYR A CA  
243  C C   . TYR A 31  ? 0.6071 0.5435 0.4996 0.2102  0.0218  -0.1637 31  TYR A C   
244  O O   . TYR A 31  ? 0.6151 0.5689 0.5157 0.2296  0.0203  -0.1738 31  TYR A O   
245  C CB  . TYR A 31  ? 0.6060 0.5921 0.5148 0.1829  0.0353  -0.1703 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.5985 0.6080 0.5202 0.1721  0.0359  -0.1595 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.5846 0.6152 0.5204 0.1818  0.0324  -0.1600 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.6006 0.6114 0.5198 0.1533  0.0397  -0.1501 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.5629 0.6127 0.5100 0.1699  0.0342  -0.1523 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.5686 0.5950 0.4977 0.1441  0.0415  -0.1408 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.5678 0.6121 0.5107 0.1509  0.0394  -0.1424 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.4905 0.5484 0.4427 0.1397  0.0426  -0.1354 31  TYR A OH  
253  N N   . ASP A 32  ? 0.5881 0.5075 0.4737 0.2069  0.0170  -0.1509 32  ASP A N   
254  C CA  . ASP A 32  ? 0.6313 0.5499 0.5154 0.2280  0.0087  -0.1477 32  ASP A CA  
255  C C   . ASP A 32  ? 0.6268 0.5568 0.5160 0.2154  0.0060  -0.1356 32  ASP A C   
256  O O   . ASP A 32  ? 0.6181 0.5174 0.4926 0.2013  0.0070  -0.1252 32  ASP A O   
257  C CB  . ASP A 32  ? 0.6899 0.5521 0.5451 0.2447  0.0053  -0.1449 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.7130 0.5722 0.5609 0.2712  -0.0046 -0.1397 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.6399 0.5408 0.5053 0.2724  -0.0096 -0.1377 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.7750 0.5902 0.5990 0.2886  -0.0071 -0.1364 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.5912 0.5668 0.5020 0.2190  0.0038  -0.1390 33  ASP A N   
262  C CA  . ASP A 33  ? 0.5941 0.5828 0.5109 0.2073  0.0020  -0.1302 33  ASP A CA  
263  C C   . ASP A 33  ? 0.5871 0.5734 0.4957 0.2266  -0.0085 -0.1265 33  ASP A C   
264  O O   . ASP A 33  ? 0.5683 0.5718 0.4832 0.2192  -0.0109 -0.1220 33  ASP A O   
265  C CB  . ASP A 33  ? 0.5937 0.6311 0.5373 0.1935  0.0086  -0.1366 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.6433 0.7257 0.6068 0.2085  0.0071  -0.1515 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.6784 0.7586 0.6364 0.2337  -0.0014 -0.1564 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.6270 0.7471 0.6112 0.1952  0.0154  -0.1588 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.6057 0.5701 0.4985 0.2525  -0.0148 -0.1285 34  VAL A N   
270  C CA  . VAL A 34  ? 0.6374 0.5893 0.5132 0.2741  -0.0254 -0.1214 34  VAL A CA  
271  C C   . VAL A 34  ? 0.6853 0.5732 0.5263 0.2686  -0.0243 -0.1055 34  VAL A C   
272  O O   . VAL A 34  ? 0.6937 0.5746 0.5241 0.2639  -0.0277 -0.0948 34  VAL A O   
273  C CB  . VAL A 34  ? 0.6950 0.6570 0.5692 0.3098  -0.0331 -0.1310 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.7285 0.6818 0.5827 0.3358  -0.0455 -0.1227 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.6565 0.6868 0.5674 0.3102  -0.0320 -0.1487 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.7235 0.5649 0.5463 0.2667  -0.0183 -0.1052 35  GLU A N   
277  C CA  . GLU A 35  ? 0.8040 0.5828 0.5938 0.2565  -0.0139 -0.0928 35  GLU A CA  
278  C C   . GLU A 35  ? 0.7793 0.5429 0.5718 0.2280  -0.0030 -0.0965 35  GLU A C   
279  O O   . GLU A 35  ? 0.8633 0.5811 0.6354 0.2271  0.0027  -0.0988 35  GLU A O   
280  C CB  . GLU A 35  ? 0.9452 0.6707 0.7013 0.2847  -0.0167 -0.0890 35  GLU A CB  
281  C CG  . GLU A 35  ? 1.0351 0.7752 0.7837 0.3177  -0.0292 -0.0844 35  GLU A CG  
282  C CD  . GLU A 35  ? 1.1558 0.8447 0.8710 0.3470  -0.0318 -0.0795 35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.2116 0.8783 0.8992 0.3647  -0.0385 -0.0659 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.2027 0.8785 0.9206 0.3466  -0.0267 -0.0875 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.7020 0.5024 0.5176 0.2047  0.0003  -0.0977 36  PRO A N   
286  C CA  . PRO A 36  ? 0.6822 0.4714 0.4979 0.1795  0.0089  -0.1004 36  PRO A CA  
287  C C   . PRO A 36  ? 0.7118 0.4541 0.5018 0.1648  0.0133  -0.0916 36  PRO A C   
288  O O   . PRO A 36  ? 0.7417 0.4692 0.5180 0.1677  0.0105  -0.0806 36  PRO A O   
289  C CB  . PRO A 36  ? 0.6010 0.4394 0.4439 0.1637  0.0102  -0.1006 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.6118 0.4710 0.4614 0.1718  0.0040  -0.0944 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.6432 0.4951 0.4841 0.2001  -0.0031 -0.0970 36  PRO A CD  
292  N N   . GLU A 37  ? 0.6826 0.4028 0.4650 0.1481  0.0211  -0.0980 37  GLU A N   
293  C CA  . GLU A 37  ? 0.6749 0.3646 0.4406 0.1253  0.0279  -0.0934 37  GLU A CA  
294  C C   . GLU A 37  ? 0.6420 0.3714 0.4290 0.1022  0.0300  -0.0951 37  GLU A C   
295  O O   . GLU A 37  ? 0.6528 0.3743 0.4334 0.0852  0.0336  -0.0897 37  GLU A O   
296  C CB  . GLU A 37  ? 0.7655 0.4066 0.5090 0.1182  0.0365  -0.1020 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.8575 0.4457 0.5724 0.1422  0.0361  -0.0985 37  GLU A CG  
298  C CD  . GLU A 37  ? 0.9509 0.4936 0.6474 0.1379  0.0454  -0.1109 37  GLU A CD  
299  O OE1 . GLU A 37  ? 0.9500 0.4962 0.6512 0.1107  0.0533  -0.1215 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 1.0122 0.5169 0.6895 0.1626  0.0447  -0.1112 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.5981 0.3697 0.4085 0.1029  0.0283  -0.1022 38  ILE A N   
302  C CA  . ILE A 38  ? 0.5277 0.3378 0.3568 0.0872  0.0295  -0.1029 38  ILE A CA  
303  C C   . ILE A 38  ? 0.4937 0.3427 0.3434 0.0977  0.0253  -0.0989 38  ILE A C   
304  O O   . ILE A 38  ? 0.5254 0.3868 0.3822 0.1118  0.0236  -0.1036 38  ILE A O   
305  C CB  . ILE A 38  ? 0.5357 0.3567 0.3683 0.0772  0.0334  -0.1154 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.5777 0.3603 0.3905 0.0629  0.0395  -0.1229 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.5131 0.3756 0.3624 0.0666  0.0333  -0.1146 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.5592 0.3428 0.3702 0.0413  0.0432  -0.1205 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.4663 0.3345 0.3255 0.0897  0.0250  -0.0917 39  VAL A N   
310  C CA  . VAL A 39  ? 0.4372 0.3389 0.3149 0.0948  0.0239  -0.0890 39  VAL A CA  
311  C C   . VAL A 39  ? 0.4674 0.3922 0.3552 0.0833  0.0275  -0.0882 39  VAL A C   
312  O O   . VAL A 39  ? 0.4638 0.3880 0.3503 0.0726  0.0284  -0.0844 39  VAL A O   
313  C CB  . VAL A 39  ? 0.4506 0.3531 0.3293 0.0988  0.0205  -0.0819 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.4415 0.3771 0.3395 0.0985  0.0220  -0.0815 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.4532 0.3392 0.3215 0.1163  0.0152  -0.0825 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.4507 0.3961 0.3468 0.0867  0.0299  -0.0916 40  ILE A N   
317  C CA  . ILE A 40  ? 0.4318 0.3975 0.3333 0.0807  0.0332  -0.0891 40  ILE A CA  
318  C C   . ILE A 40  ? 0.3941 0.3749 0.3065 0.0832  0.0367  -0.0834 40  ILE A C   
319  O O   . ILE A 40  ? 0.4134 0.4019 0.3318 0.0893  0.0388  -0.0861 40  ILE A O   
320  C CB  . ILE A 40  ? 0.4708 0.4465 0.3687 0.0824  0.0350  -0.0959 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.4685 0.4268 0.3558 0.0780  0.0329  -0.1049 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.4440 0.4401 0.3430 0.0799  0.0374  -0.0914 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.4661 0.4320 0.3494 0.0813  0.0344  -0.1145 40  ILE A CD1 
324  N N   . SER A 41  ? 0.3633 0.3490 0.2784 0.0780  0.0385  -0.0771 41  SER A N   
325  C CA  . SER A 41  ? 0.3990 0.3930 0.3221 0.0781  0.0440  -0.0722 41  SER A CA  
326  C C   . SER A 41  ? 0.4290 0.4311 0.3485 0.0793  0.0493  -0.0675 41  SER A C   
327  O O   . SER A 41  ? 0.4552 0.4605 0.3701 0.0787  0.0470  -0.0655 41  SER A O   
328  C CB  . SER A 41  ? 0.3843 0.3737 0.3109 0.0734  0.0428  -0.0687 41  SER A CB  
329  O OG  . SER A 41  ? 0.4782 0.4730 0.4124 0.0721  0.0492  -0.0664 41  SER A OG  
330  N N   . ILE A 42  ? 0.4027 0.4093 0.3231 0.0813  0.0570  -0.0661 42  ILE A N   
331  C CA  . ILE A 42  ? 0.3817 0.3906 0.2925 0.0847  0.0634  -0.0593 42  ILE A CA  
332  C C   . ILE A 42  ? 0.4149 0.4155 0.3275 0.0822  0.0734  -0.0529 42  ILE A C   
333  O O   . ILE A 42  ? 0.3964 0.3968 0.3140 0.0775  0.0816  -0.0557 42  ILE A O   
334  C CB  . ILE A 42  ? 0.3672 0.3835 0.2709 0.0881  0.0668  -0.0622 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.3695 0.3913 0.2706 0.0898  0.0578  -0.0707 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.4610 0.4766 0.3497 0.0931  0.0742  -0.0526 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.3776 0.4082 0.2717 0.0934  0.0608  -0.0759 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.4010 0.3955 0.3098 0.0847  0.0739  -0.0461 43  GLY A N   
339  C CA  . GLY A 43  ? 0.4475 0.4283 0.3567 0.0821  0.0842  -0.0411 43  GLY A CA  
340  C C   . GLY A 43  ? 0.4807 0.4579 0.3898 0.0860  0.0810  -0.0371 43  GLY A C   
341  O O   . GLY A 43  ? 0.5835 0.5689 0.4859 0.0946  0.0750  -0.0340 43  GLY A O   
342  N N   . GLY A 44  ? 0.4208 0.3898 0.3381 0.0798  0.0851  -0.0391 44  GLY A N   
343  C CA  . GLY A 44  ? 0.4252 0.3930 0.3448 0.0825  0.0826  -0.0378 44  GLY A CA  
344  C C   . GLY A 44  ? 0.3787 0.3559 0.3101 0.0742  0.0745  -0.0456 44  GLY A C   
345  O O   . GLY A 44  ? 0.3583 0.3421 0.2935 0.0697  0.0687  -0.0507 44  GLY A O   
346  N N   . ASP A 45  ? 0.4312 0.4072 0.3661 0.0735  0.0749  -0.0463 45  ASP A N   
347  C CA  . ASP A 45  ? 0.3840 0.3673 0.3261 0.0655  0.0685  -0.0524 45  ASP A CA  
348  C C   . ASP A 45  ? 0.3976 0.3791 0.3457 0.0576  0.0705  -0.0581 45  ASP A C   
349  O O   . ASP A 45  ? 0.3817 0.3693 0.3313 0.0539  0.0631  -0.0619 45  ASP A O   
350  C CB  . ASP A 45  ? 0.3851 0.3704 0.3295 0.0663  0.0698  -0.0531 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.4145 0.4131 0.3566 0.0729  0.0647  -0.0515 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.4014 0.4092 0.3415 0.0707  0.0579  -0.0529 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.4473 0.4487 0.3900 0.0805  0.0678  -0.0504 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.3884 0.3618 0.3388 0.0549  0.0810  -0.0594 46  GLY A N   
355  C CA  . GLY A 46  ? 0.4068 0.3869 0.3656 0.0465  0.0830  -0.0680 46  GLY A CA  
356  C C   . GLY A 46  ? 0.4129 0.4044 0.3732 0.0486  0.0764  -0.0703 46  GLY A C   
357  O O   . GLY A 46  ? 0.3515 0.3556 0.3173 0.0471  0.0699  -0.0770 46  GLY A O   
358  N N   . THR A 47  ? 0.4082 0.3961 0.3622 0.0539  0.0778  -0.0651 47  THR A N   
359  C CA  . THR A 47  ? 0.3441 0.3420 0.2989 0.0574  0.0718  -0.0683 47  THR A CA  
360  C C   . THR A 47  ? 0.3760 0.3751 0.3274 0.0612  0.0591  -0.0684 47  THR A C   
361  O O   . THR A 47  ? 0.3659 0.3714 0.3193 0.0640  0.0529  -0.0735 47  THR A O   
362  C CB  . THR A 47  ? 0.3476 0.3415 0.2938 0.0622  0.0760  -0.0630 47  THR A CB  
363  O OG1 . THR A 47  ? 0.4258 0.4108 0.3694 0.0583  0.0900  -0.0604 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.3488 0.3535 0.2968 0.0653  0.0721  -0.0686 47  THR A CG2 
365  N N   . PHE A 48  ? 0.3255 0.3181 0.2706 0.0617  0.0560  -0.0634 48  PHE A N   
366  C CA  . PHE A 48  ? 0.3519 0.3410 0.2910 0.0616  0.0471  -0.0637 48  PHE A CA  
367  C C   . PHE A 48  ? 0.3432 0.3324 0.2831 0.0593  0.0435  -0.0663 48  PHE A C   
368  O O   . PHE A 48  ? 0.3666 0.3506 0.2996 0.0626  0.0368  -0.0671 48  PHE A O   
369  C CB  . PHE A 48  ? 0.3441 0.3322 0.2789 0.0594  0.0465  -0.0605 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.3586 0.3406 0.2853 0.0557  0.0405  -0.0619 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.3766 0.3566 0.2977 0.0566  0.0381  -0.0641 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.4058 0.3817 0.3281 0.0500  0.0387  -0.0617 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.4124 0.3810 0.3240 0.0506  0.0352  -0.0666 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.4289 0.3926 0.3396 0.0446  0.0360  -0.0623 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.4073 0.3656 0.3128 0.0442  0.0348  -0.0651 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.3799 0.3736 0.3259 0.0547  0.0480  -0.0676 49  LEU A N   
377  C CA  . LEU A 49  ? 0.3849 0.3835 0.3309 0.0527  0.0443  -0.0713 49  LEU A CA  
378  C C   . LEU A 49  ? 0.3721 0.3816 0.3218 0.0582  0.0400  -0.0770 49  LEU A C   
379  O O   . LEU A 49  ? 0.3475 0.3579 0.2897 0.0633  0.0320  -0.0775 49  LEU A O   
380  C CB  . LEU A 49  ? 0.3743 0.3777 0.3278 0.0460  0.0516  -0.0748 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.4880 0.4885 0.4369 0.0417  0.0516  -0.0733 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.5446 0.5377 0.4850 0.0423  0.0486  -0.0672 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.5118 0.5114 0.4684 0.0379  0.0616  -0.0762 49  LEU A CD2 
384  N N   . SER A 50  ? 0.3856 0.4045 0.3455 0.0582  0.0456  -0.0815 50  SER A N   
385  C CA  . SER A 50  ? 0.3660 0.4029 0.3327 0.0639  0.0418  -0.0897 50  SER A CA  
386  C C   . SER A 50  ? 0.3819 0.4107 0.3384 0.0760  0.0328  -0.0867 50  SER A C   
387  O O   . SER A 50  ? 0.4267 0.4649 0.3816 0.0860  0.0248  -0.0908 50  SER A O   
388  C CB  . SER A 50  ? 0.4497 0.4988 0.4292 0.0584  0.0525  -0.0962 50  SER A CB  
389  O OG  . SER A 50  ? 0.5406 0.5924 0.5276 0.0464  0.0625  -0.1006 50  SER A OG  
390  N N   . ALA A 51  ? 0.3537 0.3656 0.3025 0.0762  0.0341  -0.0806 51  ALA A N   
391  C CA  . ALA A 51  ? 0.3776 0.3756 0.3146 0.0854  0.0275  -0.0789 51  ALA A CA  
392  C C   . ALA A 51  ? 0.3878 0.3691 0.3093 0.0890  0.0201  -0.0745 51  ALA A C   
393  O O   . ALA A 51  ? 0.4336 0.4076 0.3457 0.1013  0.0135  -0.0751 51  ALA A O   
394  C CB  . ALA A 51  ? 0.3477 0.3333 0.2792 0.0814  0.0309  -0.0752 51  ALA A CB  
395  N N   . PHE A 52  ? 0.3701 0.3433 0.2864 0.0794  0.0221  -0.0694 52  PHE A N   
396  C CA  . PHE A 52  ? 0.3794 0.3361 0.2781 0.0802  0.0174  -0.0644 52  PHE A CA  
397  C C   . PHE A 52  ? 0.4479 0.4164 0.3445 0.0915  0.0105  -0.0669 52  PHE A C   
398  O O   . PHE A 52  ? 0.4454 0.3970 0.3233 0.1030  0.0041  -0.0629 52  PHE A O   
399  C CB  . PHE A 52  ? 0.3723 0.3284 0.2707 0.0670  0.0221  -0.0614 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.3902 0.3348 0.2712 0.0659  0.0193  -0.0569 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.4710 0.3864 0.3294 0.0646  0.0188  -0.0509 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.3851 0.3465 0.2700 0.0651  0.0183  -0.0593 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.4556 0.3566 0.2931 0.0631  0.0178  -0.0451 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.4592 0.4110 0.3248 0.0647  0.0157  -0.0546 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.4938 0.4145 0.3346 0.0641  0.0156  -0.0464 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.3881 0.3854 0.3023 0.0889  0.0120  -0.0741 53  HIS A N   
407  C CA  . HIS A 53  ? 0.3930 0.4107 0.3073 0.0988  0.0047  -0.0793 53  HIS A CA  
408  C C   . HIS A 53  ? 0.4536 0.4829 0.3711 0.1157  -0.0016 -0.0848 53  HIS A C   
409  O O   . HIS A 53  ? 0.4652 0.5032 0.3736 0.1313  -0.0111 -0.0860 53  HIS A O   
410  C CB  . HIS A 53  ? 0.3676 0.4141 0.3007 0.0878  0.0098  -0.0888 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.3858 0.4236 0.3114 0.0769  0.0129  -0.0847 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.4101 0.4453 0.3180 0.0815  0.0061  -0.0811 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.3676 0.3975 0.2987 0.0635  0.0220  -0.0831 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.4049 0.4336 0.3099 0.0691  0.0118  -0.0790 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.3838 0.4098 0.3036 0.0590  0.0211  -0.0805 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.4329 0.4629 0.3611 0.1150  0.0032  -0.0880 54  GLN A N   
417  C CA  . GLN A 54  ? 0.4134 0.4555 0.3452 0.1319  -0.0020 -0.0945 54  GLN A CA  
418  C C   . GLN A 54  ? 0.5081 0.5175 0.4138 0.1491  -0.0101 -0.0863 54  GLN A C   
419  O O   . GLN A 54  ? 0.5956 0.6143 0.4983 0.1697  -0.0180 -0.0905 54  GLN A O   
420  C CB  . GLN A 54  ? 0.3845 0.4327 0.3307 0.1258  0.0064  -0.0994 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.4254 0.4902 0.3783 0.1419  0.0030  -0.1084 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.4004 0.4731 0.3659 0.1335  0.0131  -0.1134 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.3532 0.4243 0.3242 0.1166  0.0227  -0.1107 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.3893 0.4697 0.3572 0.1470  0.0112  -0.1204 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.5443 0.5151 0.4299 0.1413  -0.0076 -0.0752 55  TYR A N   
426  C CA  . TYR A 55  ? 0.5611 0.4912 0.4182 0.1537  -0.0115 -0.0672 55  TYR A CA  
427  C C   . TYR A 55  ? 0.5850 0.4877 0.4164 0.1496  -0.0124 -0.0559 55  TYR A C   
428  O O   . TYR A 55  ? 0.5977 0.4571 0.4039 0.1480  -0.0095 -0.0479 55  TYR A O   
429  C CB  . TYR A 55  ? 0.5345 0.4390 0.3884 0.1463  -0.0049 -0.0672 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.5706 0.4981 0.4438 0.1533  -0.0041 -0.0776 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.6177 0.5404 0.4847 0.1753  -0.0096 -0.0820 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.5251 0.4782 0.4206 0.1392  0.0028  -0.0830 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.5838 0.5308 0.4690 0.1811  -0.0078 -0.0931 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.5443 0.5180 0.4546 0.1442  0.0052  -0.0923 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.5690 0.5419 0.4755 0.1643  0.0001  -0.0981 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.5125 0.5091 0.4343 0.1689  0.0034  -0.1088 55  TYR A OH  
437  N N   . GLU A 56  ? 0.5832 0.5099 0.4190 0.1468  -0.0151 -0.0562 56  GLU A N   
438  C CA  . GLU A 56  ? 0.6033 0.5052 0.4135 0.1411  -0.0145 -0.0456 56  GLU A CA  
439  C C   . GLU A 56  ? 0.6308 0.5008 0.4055 0.1624  -0.0215 -0.0359 56  GLU A C   
440  O O   . GLU A 56  ? 0.6791 0.5188 0.4255 0.1573  -0.0189 -0.0250 56  GLU A O   
441  C CB  . GLU A 56  ? 0.5552 0.4907 0.3777 0.1319  -0.0149 -0.0495 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.4963 0.4787 0.3395 0.1426  -0.0219 -0.0614 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.5349 0.5434 0.3831 0.1331  -0.0220 -0.0656 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.5873 0.5938 0.4128 0.1438  -0.0293 -0.0604 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.4879 0.5162 0.3599 0.1157  -0.0143 -0.0737 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.6347 0.5093 0.4081 0.1870  -0.0295 -0.0392 57  GLU A N   
447  C CA  . GLU A 57  ? 0.7510 0.5875 0.4864 0.2117  -0.0358 -0.0284 57  GLU A CA  
448  C C   . GLU A 57  ? 0.7680 0.5453 0.4802 0.2109  -0.0283 -0.0219 57  GLU A C   
449  O O   . GLU A 57  ? 0.7973 0.5281 0.4710 0.2284  -0.0300 -0.0106 57  GLU A O   
450  C CB  . GLU A 57  ? 0.8111 0.6820 0.5541 0.2431  -0.0490 -0.0360 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.8939 0.7968 0.6291 0.2572  -0.0599 -0.0352 57  GLU A CG  
452  C CD  . GLU A 57  ? 0.8937 0.8482 0.6612 0.2343  -0.0576 -0.0463 57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.9093 0.8646 0.6626 0.2268  -0.0580 -0.0407 57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.8899 0.8811 0.6949 0.2233  -0.0540 -0.0607 57  GLU A OE2 
455  N N   . ARG A 58  ? 0.6695 0.4460 0.4019 0.1914  -0.0195 -0.0289 58  ARG A N   
456  C CA  . ARG A 58  ? 0.7258 0.4508 0.4391 0.1874  -0.0116 -0.0266 58  ARG A CA  
457  C C   . ARG A 58  ? 0.7246 0.4395 0.4435 0.1541  0.0004  -0.0276 58  ARG A C   
458  O O   . ARG A 58  ? 0.6912 0.3905 0.4139 0.1440  0.0071  -0.0337 58  ARG A O   
459  C CB  . ARG A 58  ? 0.6979 0.4342 0.4282 0.2021  -0.0142 -0.0378 58  ARG A CB  
460  C CG  . ARG A 58  ? 0.7696 0.5062 0.4875 0.2389  -0.0254 -0.0372 58  ARG A CG  
461  C CD  . ARG A 58  ? 0.8052 0.5476 0.5366 0.2542  -0.0263 -0.0490 58  ARG A CD  
462  N NE  . ARG A 58  ? 0.8416 0.5295 0.5542 0.2456  -0.0163 -0.0488 58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.8175 0.5133 0.5494 0.2227  -0.0079 -0.0580 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.7657 0.5162 0.5333 0.2080  -0.0080 -0.0656 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.7888 0.4367 0.5024 0.2147  0.0010  -0.0600 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.7072 0.4334 0.4260 0.1377  0.0031  -0.0228 59  LEU A N   
467  C CA  . LEU A 59  ? 0.6819 0.4072 0.4087 0.1081  0.0137  -0.0252 59  LEU A CA  
468  C C   . LEU A 59  ? 0.7390 0.4097 0.4370 0.0958  0.0241  -0.0221 59  LEU A C   
469  O O   . LEU A 59  ? 0.7734 0.4468 0.4826 0.0738  0.0323  -0.0295 59  LEU A O   
470  C CB  . LEU A 59  ? 0.6354 0.3804 0.3639 0.0960  0.0148  -0.0211 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.6081 0.4073 0.3682 0.1003  0.0082  -0.0274 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.5711 0.3826 0.3274 0.0892  0.0102  -0.0238 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.5600 0.3878 0.3530 0.0900  0.0114  -0.0375 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.7887 0.4093 0.4482 0.1095  0.0246  -0.0118 60  ASP A N   
475  C CA  . ASP A 60  ? 0.9370 0.4971 0.5644 0.0956  0.0374  -0.0090 60  ASP A CA  
476  C C   . ASP A 60  ? 0.9413 0.4875 0.5765 0.0961  0.0404  -0.0204 60  ASP A C   
477  O O   . ASP A 60  ? 1.0055 0.5187 0.6287 0.0744  0.0529  -0.0255 60  ASP A O   
478  C CB  . ASP A 60  ? 1.0928 0.5957 0.6713 0.1135  0.0379  0.0070  60  ASP A CB  
479  C CG  . ASP A 60  ? 1.2616 0.7411 0.8133 0.0929  0.0481  0.0172  60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.2879 0.7688 0.8480 0.0604  0.0605  0.0101  60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.3564 0.8196 0.8784 0.1095  0.0437  0.0314  60  ASP A OD2 
482  N N   . GLU A 61  ? 0.8687 0.4413 0.5237 0.1191  0.0300  -0.0262 61  GLU A N   
483  C CA  . GLU A 61  ? 0.8634 0.4224 0.5229 0.1240  0.0322  -0.0371 61  GLU A CA  
484  C C   . GLU A 61  ? 0.8219 0.4324 0.5212 0.1092  0.0321  -0.0513 61  GLU A C   
485  O O   . GLU A 61  ? 0.8684 0.4742 0.5733 0.1110  0.0342  -0.0620 61  GLU A O   
486  C CB  . GLU A 61  ? 0.8912 0.4461 0.5451 0.1609  0.0218  -0.0358 61  GLU A CB  
487  C CG  . GLU A 61  ? 1.0316 0.5302 0.6406 0.1832  0.0207  -0.0211 61  GLU A CG  
488  C CD  . GLU A 61  ? 1.0790 0.6032 0.6841 0.1964  0.0107  -0.0095 61  GLU A CD  
489  O OE1 . GLU A 61  ? 1.1316 0.6360 0.7114 0.2282  0.0027  -0.0005 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 1.0567 0.6216 0.6832 0.1766  0.0107  -0.0101 61  GLU A OE2 
491  N N   . ILE A 62  ? 0.7229 0.3800 0.4471 0.0958  0.0304  -0.0515 62  ILE A N   
492  C CA  . ILE A 62  ? 0.7035 0.4113 0.4630 0.0895  0.0284  -0.0616 62  ILE A CA  
493  C C   . ILE A 62  ? 0.6799 0.4042 0.4497 0.0621  0.0353  -0.0656 62  ILE A C   
494  O O   . ILE A 62  ? 0.6637 0.3838 0.4259 0.0500  0.0387  -0.0594 62  ILE A O   
495  C CB  . ILE A 62  ? 0.6797 0.4328 0.4621 0.1039  0.0194  -0.0596 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.6685 0.4196 0.4483 0.1313  0.0122  -0.0611 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.6271 0.4263 0.4405 0.0937  0.0202  -0.0665 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.6220 0.4179 0.4227 0.1435  0.0044  -0.0614 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.5820 0.3284 0.3689 0.0537  0.0372  -0.0766 63  ALA A N   
500  C CA  . ALA A 63  ? 0.5759 0.3547 0.3796 0.0344  0.0405  -0.0817 63  ALA A CA  
501  C C   . ALA A 63  ? 0.5393 0.3646 0.3697 0.0429  0.0352  -0.0834 63  ALA A C   
502  O O   . ALA A 63  ? 0.5657 0.3984 0.4021 0.0536  0.0328  -0.0884 63  ALA A O   
503  C CB  . ALA A 63  ? 0.6320 0.3995 0.4297 0.0159  0.0480  -0.0940 63  ALA A CB  
504  N N   . PHE A 64  ? 0.5163 0.3700 0.3606 0.0378  0.0346  -0.0796 64  PHE A N   
505  C CA  . PHE A 64  ? 0.4462 0.3363 0.3114 0.0451  0.0318  -0.0789 64  PHE A CA  
506  C C   . PHE A 64  ? 0.4707 0.3872 0.3462 0.0368  0.0337  -0.0852 64  PHE A C   
507  O O   . PHE A 64  ? 0.4611 0.3798 0.3340 0.0226  0.0367  -0.0899 64  PHE A O   
508  C CB  . PHE A 64  ? 0.4134 0.3158 0.2858 0.0465  0.0308  -0.0715 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.4680 0.3581 0.3342 0.0582  0.0270  -0.0664 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.4306 0.3393 0.3096 0.0700  0.0242  -0.0670 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.4788 0.3407 0.3249 0.0571  0.0267  -0.0615 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.4345 0.3409 0.3102 0.0816  0.0195  -0.0650 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.5010 0.3561 0.3396 0.0713  0.0214  -0.0568 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.4972 0.3781 0.3524 0.0839  0.0170  -0.0597 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.4193 0.3581 0.3058 0.0460  0.0323  -0.0856 65  ILE A N   
516  C CA  . ILE A 65  ? 0.4024 0.3697 0.2967 0.0440  0.0327  -0.0890 65  ILE A CA  
517  C C   . ILE A 65  ? 0.4265 0.4103 0.3302 0.0547  0.0333  -0.0815 65  ILE A C   
518  O O   . ILE A 65  ? 0.4494 0.4290 0.3544 0.0629  0.0339  -0.0796 65  ILE A O   
519  C CB  . ILE A 65  ? 0.3961 0.3676 0.2858 0.0434  0.0324  -0.0989 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.4797 0.4260 0.3575 0.0313  0.0343  -0.1078 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.3865 0.3920 0.2817 0.0430  0.0313  -0.1025 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.5222 0.4663 0.3942 0.0310  0.0348  -0.1194 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.3661 0.3686 0.2757 0.0547  0.0342  -0.0784 66  GLY A N   
524  C CA  . GLY A 66  ? 0.3906 0.4021 0.3050 0.0643  0.0370  -0.0709 66  GLY A CA  
525  C C   . GLY A 66  ? 0.4231 0.4537 0.3343 0.0716  0.0370  -0.0707 66  GLY A C   
526  O O   . GLY A 66  ? 0.3886 0.4373 0.2995 0.0697  0.0338  -0.0757 66  GLY A O   
527  N N   . ILE A 67  ? 0.4381 0.4669 0.3459 0.0799  0.0409  -0.0654 67  ILE A N   
528  C CA  . ILE A 67  ? 0.3967 0.4394 0.2962 0.0900  0.0422  -0.0613 67  ILE A CA  
529  C C   . ILE A 67  ? 0.4196 0.4529 0.3171 0.0972  0.0495  -0.0499 67  ILE A C   
530  O O   . ILE A 67  ? 0.4617 0.4794 0.3624 0.0939  0.0559  -0.0474 67  ILE A O   
531  C CB  . ILE A 67  ? 0.3789 0.4228 0.2706 0.0926  0.0435  -0.0644 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.3769 0.4254 0.2690 0.0852  0.0376  -0.0773 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.4006 0.4559 0.2789 0.1043  0.0461  -0.0573 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.4266 0.4782 0.3111 0.0882  0.0388  -0.0829 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.4491 0.4919 0.3410 0.1076  0.0492  -0.0443 68  HIS A N   
536  C CA  . HIS A 68  ? 0.5132 0.5391 0.4008 0.1147  0.0577  -0.0336 68  HIS A CA  
537  C C   . HIS A 68  ? 0.5172 0.5333 0.3863 0.1254  0.0654  -0.0236 68  HIS A C   
538  O O   . HIS A 68  ? 0.5596 0.5896 0.4153 0.1384  0.0618  -0.0199 68  HIS A O   
539  C CB  . HIS A 68  ? 0.5967 0.6307 0.4876 0.1223  0.0553  -0.0319 68  HIS A CB  
540  C CG  . HIS A 68  ? 0.6425 0.7061 0.5288 0.1339  0.0470  -0.0342 68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.6509 0.7417 0.5474 0.1253  0.0380  -0.0469 68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.6720 0.7440 0.5442 0.1540  0.0465  -0.0263 68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.6622 0.7831 0.5542 0.1382  0.0318  -0.0490 68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.6792 0.7902 0.5558 0.1578  0.0357  -0.0359 68  HIS A NE2 
545  N N   . THR A 69  ? 0.4858 0.4798 0.3536 0.1189  0.0764  -0.0202 69  THR A N   
546  C CA  . THR A 69  ? 0.5375 0.5117 0.3859 0.1254  0.0891  -0.0090 69  THR A CA  
547  C C   . THR A 69  ? 0.6696 0.6153 0.5174 0.1230  0.1013  -0.0032 69  THR A C   
548  O O   . THR A 69  ? 0.7560 0.6765 0.5873 0.1239  0.1159  0.0055  69  THR A O   
549  C CB  . THR A 69  ? 0.4667 0.4405 0.3135 0.1163  0.0952  -0.0128 69  THR A CB  
550  O OG1 . THR A 69  ? 0.4832 0.4547 0.3498 0.1015  0.0974  -0.0220 69  THR A OG1 
551  C CG2 . THR A 69  ? 0.4296 0.4287 0.2760 0.1186  0.0842  -0.0202 69  THR A CG2 
552  N N   . GLY A 70  ? 0.6350 0.5827 0.4993 0.1183  0.0971  -0.0088 70  GLY A N   
553  C CA  . GLY A 70  ? 0.6101 0.5326 0.4750 0.1154  0.1081  -0.0062 70  GLY A CA  
554  C C   . GLY A 70  ? 0.6255 0.5384 0.4778 0.1339  0.1086  0.0028  70  GLY A C   
555  O O   . GLY A 70  ? 0.6421 0.5572 0.4758 0.1511  0.1067  0.0122  70  GLY A O   
556  N N   . HIS A 71  ? 0.6025 0.5073 0.4642 0.1326  0.1107  -0.0004 71  HIS A N   
557  C CA  . HIS A 71  ? 0.6518 0.5456 0.5018 0.1526  0.1125  0.0073  71  HIS A CA  
558  C C   . HIS A 71  ? 0.6238 0.5534 0.4880 0.1602  0.0974  0.0003  71  HIS A C   
559  O O   . HIS A 71  ? 0.6404 0.5902 0.4966 0.1785  0.0892  0.0042  71  HIS A O   
560  C CB  . HIS A 71  ? 0.7083 0.5646 0.5556 0.1479  0.1283  0.0078  71  HIS A CB  
561  C CG  . HIS A 71  ? 0.7317 0.5534 0.5659 0.1361  0.1459  0.0120  71  HIS A CG  
562  N ND1 . HIS A 71  ? 0.7780 0.5688 0.5824 0.1485  0.1574  0.0268  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 0.7256 0.5411 0.5718 0.1122  0.1548  0.0023  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 0.8065 0.5715 0.6056 0.1302  0.1743  0.0258  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 0.7714 0.5541 0.5975 0.1080  0.1726  0.0098  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.6023 0.5430 0.4871 0.1461  0.0941  -0.0108 72  LEU A N   
567  C CA  . LEU A 72  ? 0.5456 0.5199 0.4435 0.1498  0.0825  -0.0185 72  LEU A CA  
568  C C   . LEU A 72  ? 0.4920 0.4965 0.4005 0.1371  0.0709  -0.0267 72  LEU A C   
569  O O   . LEU A 72  ? 0.4338 0.4686 0.3442 0.1442  0.0616  -0.0302 72  LEU A O   
570  C CB  . LEU A 72  ? 0.5396 0.5091 0.4502 0.1421  0.0864  -0.0259 72  LEU A CB  
571  C CG  . LEU A 72  ? 0.5476 0.5532 0.4711 0.1449  0.0768  -0.0345 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.5779 0.5964 0.4937 0.1716  0.0744  -0.0300 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.5038 0.5082 0.4398 0.1330  0.0803  -0.0432 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.4831 0.4803 0.3986 0.1187  0.0715  -0.0312 73  GLY A N   
575  C CA  . GLY A 73  ? 0.5144 0.5298 0.4356 0.1078  0.0625  -0.0379 73  GLY A CA  
576  C C   . GLY A 73  ? 0.4798 0.5202 0.4110 0.1017  0.0548  -0.0468 73  GLY A C   
577  O O   . GLY A 73  ? 0.4955 0.5593 0.4265 0.1040  0.0481  -0.0509 73  GLY A O   
578  N N   . PHE A 74  ? 0.4722 0.5089 0.4114 0.0919  0.0565  -0.0510 74  PHE A N   
579  C CA  . PHE A 74  ? 0.3717 0.4302 0.3186 0.0839  0.0522  -0.0593 74  PHE A CA  
580  C C   . PHE A 74  ? 0.4004 0.4606 0.3463 0.0687  0.0474  -0.0646 74  PHE A C   
581  O O   . PHE A 74  ? 0.5179 0.5983 0.4667 0.0617  0.0442  -0.0721 74  PHE A O   
582  C CB  . PHE A 74  ? 0.4274 0.4802 0.3801 0.0789  0.0570  -0.0617 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.3548 0.4313 0.3145 0.0713  0.0550  -0.0702 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.3288 0.4302 0.2949 0.0828  0.0549  -0.0740 74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.4428 0.5175 0.4011 0.0533  0.0538  -0.0745 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.4917 0.6216 0.4666 0.0739  0.0543  -0.0844 74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.5709 0.6668 0.5339 0.0431  0.0545  -0.0829 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.5529 0.6792 0.5260 0.0522  0.0550  -0.0889 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.3719 0.4108 0.3132 0.0630  0.0477  -0.0619 75  TYR A N   
590  C CA  . TYR A 75  ? 0.3506 0.3838 0.2872 0.0522  0.0439  -0.0658 75  TYR A CA  
591  C C   . TYR A 75  ? 0.4443 0.4828 0.3766 0.0563  0.0407  -0.0672 75  TYR A C   
592  O O   . TYR A 75  ? 0.4740 0.5037 0.4009 0.0492  0.0385  -0.0711 75  TYR A O   
593  C CB  . TYR A 75  ? 0.3354 0.3469 0.2684 0.0482  0.0443  -0.0633 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.4064 0.4141 0.3399 0.0414  0.0461  -0.0638 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.3866 0.3908 0.3248 0.0444  0.0497  -0.0621 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.3492 0.3570 0.2774 0.0302  0.0456  -0.0670 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.3366 0.3403 0.2742 0.0381  0.0512  -0.0640 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.3592 0.3643 0.2849 0.0238  0.0479  -0.0671 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.3647 0.3694 0.2954 0.0286  0.0499  -0.0658 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.3426 0.3473 0.2699 0.0222  0.0520  -0.0672 75  TYR A OH  
601  N N   . ALA A 76  ? 0.4333 0.4845 0.3655 0.0688  0.0410  -0.0642 76  ALA A N   
602  C CA  . ALA A 76  ? 0.4041 0.4628 0.3302 0.0744  0.0383  -0.0652 76  ALA A CA  
603  C C   . ALA A 76  ? 0.4119 0.4998 0.3400 0.0717  0.0333  -0.0747 76  ALA A C   
604  O O   . ALA A 76  ? 0.4482 0.5575 0.3827 0.0743  0.0324  -0.0775 76  ALA A O   
605  C CB  . ALA A 76  ? 0.3435 0.3992 0.2637 0.0900  0.0420  -0.0557 76  ALA A CB  
606  N N   . ASP A 77  ? 0.5566 0.6478 0.4801 0.0658  0.0304  -0.0820 77  ASP A N   
607  C CA  . ASP A 77  ? 0.5619 0.6844 0.4879 0.0606  0.0263  -0.0946 77  ASP A CA  
608  C C   . ASP A 77  ? 0.5396 0.6807 0.4584 0.0718  0.0224  -0.0962 77  ASP A C   
609  O O   . ASP A 77  ? 0.5046 0.6790 0.4257 0.0693  0.0179  -0.1084 77  ASP A O   
610  C CB  . ASP A 77  ? 0.6215 0.7327 0.5467 0.0394  0.0276  -0.1060 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.6685 0.7654 0.5970 0.0272  0.0317  -0.1051 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.5689 0.6795 0.5050 0.0328  0.0324  -0.1012 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.7653 0.8354 0.6865 0.0131  0.0348  -0.1081 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.4604 0.5836 0.3703 0.0829  0.0245  -0.0857 78  TRP A N   
615  C CA  . TRP A 78  ? 0.5397 0.6773 0.4391 0.0927  0.0220  -0.0866 78  TRP A CA  
616  C C   . TRP A 78  ? 0.5034 0.6322 0.3922 0.1114  0.0257  -0.0706 78  TRP A C   
617  O O   . TRP A 78  ? 0.4531 0.5540 0.3426 0.1118  0.0324  -0.0607 78  TRP A O   
618  C CB  . TRP A 78  ? 0.5595 0.6801 0.4546 0.0830  0.0233  -0.0934 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.5794 0.6998 0.4801 0.0644  0.0219  -0.1084 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.6062 0.7005 0.5111 0.0518  0.0250  -0.1090 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.6160 0.7623 0.5164 0.0554  0.0185  -0.1254 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.6188 0.7150 0.5237 0.0348  0.0252  -0.1239 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.6300 0.7589 0.5338 0.0352  0.0216  -0.1356 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.6456 0.8284 0.5415 0.0620  0.0135  -0.1338 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.6341 0.7785 0.5384 0.0186  0.0216  -0.1552 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.6508 0.8556 0.5494 0.0465  0.0116  -0.1547 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.6648 0.8491 0.5682 0.0236  0.0165  -0.1658 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.5084 0.6618 0.3861 0.1266  0.0219  -0.0688 79  ARG A N   
629  C CA  . ARG A 79  ? 0.5307 0.6714 0.3901 0.1439  0.0269  -0.0536 79  ARG A CA  
630  C C   . ARG A 79  ? 0.5595 0.6904 0.4094 0.1389  0.0302  -0.0553 79  ARG A C   
631  O O   . ARG A 79  ? 0.5426 0.6863 0.3976 0.1277  0.0257  -0.0697 79  ARG A O   
632  C CB  . ARG A 79  ? 0.5242 0.6956 0.3709 0.1654  0.0207  -0.0501 79  ARG A CB  
633  N N   . PRO A 80  ? 0.5550 0.6619 0.3912 0.1457  0.0395  -0.0421 80  PRO A N   
634  C CA  . PRO A 80  ? 0.6086 0.7103 0.4360 0.1415  0.0438  -0.0446 80  PRO A CA  
635  C C   . PRO A 80  ? 0.6694 0.8022 0.4854 0.1468  0.0365  -0.0534 80  PRO A C   
636  O O   . PRO A 80  ? 0.6415 0.7773 0.4584 0.1382  0.0367  -0.0641 80  PRO A O   
637  C CB  . PRO A 80  ? 0.6235 0.6991 0.4338 0.1497  0.0565  -0.0275 80  PRO A CB  
638  C CG  . PRO A 80  ? 0.6059 0.6617 0.4247 0.1502  0.0604  -0.0197 80  PRO A CG  
639  C CD  . PRO A 80  ? 0.5792 0.6599 0.4077 0.1548  0.0485  -0.0259 80  PRO A CD  
640  N N   . ALA A 81  ? 0.6878 0.8466 0.4935 0.1621  0.0296  -0.0505 81  ALA A N   
641  C CA  . ALA A 81  ? 0.7363 0.9312 0.5297 0.1687  0.0218  -0.0598 81  ALA A CA  
642  C C   . ALA A 81  ? 0.6969 0.9146 0.5080 0.1508  0.0144  -0.0836 81  ALA A C   
643  O O   . ALA A 81  ? 0.7056 0.9481 0.5085 0.1501  0.0102  -0.0957 81  ALA A O   
644  C CB  . ALA A 81  ? 0.7869 1.0096 0.5670 0.1915  0.0144  -0.0525 81  ALA A CB  
645  N N   . GLU A 82  ? 0.6160 0.8233 0.4487 0.1356  0.0139  -0.0908 82  GLU A N   
646  C CA  . GLU A 82  ? 0.6115 0.8305 0.4580 0.1163  0.0099  -0.1123 82  GLU A CA  
647  C C   . GLU A 82  ? 0.6265 0.8104 0.4775 0.1022  0.0162  -0.1168 82  GLU A C   
648  O O   . GLU A 82  ? 0.6240 0.8014 0.4849 0.0856  0.0156  -0.1312 82  GLU A O   
649  C CB  . GLU A 82  ? 0.5918 0.8212 0.4556 0.1079  0.0065  -0.1179 82  GLU A CB  
650  C CG  . GLU A 82  ? 0.5777 0.8491 0.4405 0.1233  -0.0010 -0.1171 82  GLU A CG  
651  C CD  . GLU A 82  ? 0.4996 0.7767 0.3800 0.1174  -0.0017 -0.1191 82  GLU A CD  
652  O OE1 . GLU A 82  ? 0.4635 0.7071 0.3474 0.1183  0.0041  -0.1055 82  GLU A OE1 
653  O OE2 . GLU A 82  ? 0.4753 0.7935 0.3665 0.1106  -0.0075 -0.1360 82  GLU A OE2 
654  N N   . ALA A 83  ? 0.5836 0.7446 0.4264 0.1089  0.0231  -0.1054 83  ALA A N   
655  C CA  . ALA A 83  ? 0.6193 0.7508 0.4684 0.0994  0.0284  -0.1094 83  ALA A CA  
656  C C   . ALA A 83  ? 0.6098 0.7470 0.4562 0.0913  0.0268  -0.1284 83  ALA A C   
657  O O   . ALA A 83  ? 0.5759 0.6923 0.4299 0.0801  0.0275  -0.1382 83  ALA A O   
658  C CB  . ALA A 83  ? 0.6688 0.7834 0.5114 0.1075  0.0369  -0.0958 83  ALA A CB  
659  N N   . ASP A 84  ? 0.6499 0.8129 0.4831 0.0976  0.0251  -0.1339 84  ASP A N   
660  C CA  . ASP A 84  ? 0.6437 0.8125 0.4738 0.0894  0.0245  -0.1542 84  ASP A CA  
661  C C   . ASP A 84  ? 0.6480 0.8251 0.4866 0.0738  0.0198  -0.1721 84  ASP A C   
662  O O   . ASP A 84  ? 0.6487 0.8074 0.4892 0.0616  0.0224  -0.1879 84  ASP A O   
663  C CB  . ASP A 84  ? 0.7174 0.9163 0.5297 0.0993  0.0236  -0.1570 84  ASP A CB  
664  C CG  . ASP A 84  ? 0.7457 0.9327 0.5469 0.1108  0.0316  -0.1413 84  ASP A CG  
665  O OD1 . ASP A 84  ? 0.7553 0.9605 0.5388 0.1235  0.0319  -0.1302 84  ASP A OD1 
666  O OD2 . ASP A 84  ? 0.7137 0.8736 0.5228 0.1075  0.0382  -0.1402 84  ASP A OD2 
667  N N   . LYS A 85  ? 0.6210 0.8240 0.4644 0.0739  0.0142  -0.1704 85  LYS A N   
668  C CA  . LYS A 85  ? 0.6451 0.8576 0.4990 0.0558  0.0119  -0.1876 85  LYS A CA  
669  C C   . LYS A 85  ? 0.6501 0.8172 0.5124 0.0428  0.0176  -0.1856 85  LYS A C   
670  O O   . LYS A 85  ? 0.6771 0.8300 0.5411 0.0246  0.0207  -0.2021 85  LYS A O   
671  C CB  . LYS A 85  ? 0.6478 0.9009 0.5073 0.0616  0.0051  -0.1847 85  LYS A CB  
672  C CG  . LYS A 85  ? 0.6945 0.9685 0.5670 0.0416  0.0034  -0.2042 85  LYS A CG  
673  C CD  . LYS A 85  ? 0.7360 1.0700 0.6122 0.0519  -0.0057 -0.2083 85  LYS A CD  
674  C CE  . LYS A 85  ? 0.7702 1.1467 0.6351 0.0586  -0.0119 -0.2222 85  LYS A CE  
675  N NZ  . LYS A 85  ? 0.7828 1.2172 0.6454 0.0791  -0.0225 -0.2201 85  LYS A NZ  
676  N N   . LEU A 86  ? 0.5967 0.7389 0.4618 0.0521  0.0199  -0.1656 86  LEU A N   
677  C CA  . LEU A 86  ? 0.5653 0.6668 0.4355 0.0435  0.0242  -0.1616 86  LEU A CA  
678  C C   . LEU A 86  ? 0.6123 0.6797 0.4761 0.0422  0.0285  -0.1680 86  LEU A C   
679  O O   . LEU A 86  ? 0.6268 0.6619 0.4890 0.0311  0.0318  -0.1741 86  LEU A O   
680  C CB  . LEU A 86  ? 0.5795 0.6711 0.4548 0.0545  0.0248  -0.1409 86  LEU A CB  
681  C CG  . LEU A 86  ? 0.5767 0.6335 0.4566 0.0484  0.0276  -0.1347 86  LEU A CG  
682  C CD1 . LEU A 86  ? 0.6052 0.6617 0.4880 0.0313  0.0279  -0.1438 86  LEU A CD1 
683  C CD2 . LEU A 86  ? 0.5368 0.5921 0.4222 0.0588  0.0283  -0.1172 86  LEU A CD2 
684  N N   . VAL A 87  ? 0.5520 0.6239 0.4107 0.0546  0.0294  -0.1657 87  VAL A N   
685  C CA  . VAL A 87  ? 0.5924 0.6393 0.4457 0.0558  0.0332  -0.1751 87  VAL A CA  
686  C C   . VAL A 87  ? 0.6610 0.7006 0.5086 0.0407  0.0345  -0.1966 87  VAL A C   
687  O O   . VAL A 87  ? 0.6829 0.6832 0.5263 0.0344  0.0385  -0.2028 87  VAL A O   
688  C CB  . VAL A 87  ? 0.5111 0.5759 0.3593 0.0689  0.0347  -0.1736 87  VAL A CB  
689  C CG1 . VAL A 87  ? 0.4896 0.5378 0.3321 0.0695  0.0383  -0.1895 87  VAL A CG1 
690  C CG2 . VAL A 87  ? 0.4749 0.5367 0.3282 0.0803  0.0371  -0.1547 87  VAL A CG2 
691  N N   . LYS A 88  ? 0.6793 0.7564 0.5250 0.0348  0.0316  -0.2086 88  LYS A N   
692  C CA  . LYS A 88  ? 0.6720 0.7490 0.5131 0.0175  0.0339  -0.2331 88  LYS A CA  
693  C C   . LYS A 88  ? 0.7163 0.7686 0.5603 -0.0019 0.0375  -0.2379 88  LYS A C   
694  O O   . LYS A 88  ? 0.7807 0.7995 0.6170 -0.0160 0.0443  -0.2532 88  LYS A O   
695  C CB  . LYS A 88  ? 0.6149 0.7476 0.4549 0.0162  0.0285  -0.2451 88  LYS A CB  
696  C CG  . LYS A 88  ? 0.5949 0.7368 0.4309 -0.0027 0.0310  -0.2745 88  LYS A CG  
697  C CD  . LYS A 88  ? 0.5965 0.8026 0.4337 -0.0019 0.0231  -0.2841 88  LYS A CD  
698  C CE  . LYS A 88  ? 0.6386 0.8553 0.4800 -0.0230 0.0249  -0.3073 88  LYS A CE  
699  N NZ  . LYS A 88  ? 0.6856 0.8946 0.5179 -0.0184 0.0270  -0.3148 88  LYS A NZ  
700  N N   . LEU A 89  ? 0.6681 0.7339 0.5212 -0.0032 0.0346  -0.2254 89  LEU A N   
701  C CA  . LEU A 89  ? 0.6673 0.7126 0.5222 -0.0233 0.0395  -0.2301 89  LEU A CA  
702  C C   . LEU A 89  ? 0.6884 0.6722 0.5345 -0.0219 0.0454  -0.2194 89  LEU A C   
703  O O   . LEU A 89  ? 0.6936 0.6402 0.5301 -0.0393 0.0533  -0.2290 89  LEU A O   
704  C CB  . LEU A 89  ? 0.6356 0.7157 0.5030 -0.0235 0.0349  -0.2207 89  LEU A CB  
705  C CG  . LEU A 89  ? 0.6649 0.8079 0.5407 -0.0273 0.0291  -0.2344 89  LEU A CG  
706  C CD1 . LEU A 89  ? 0.6404 0.8105 0.5289 -0.0286 0.0263  -0.2273 89  LEU A CD1 
707  C CD2 . LEU A 89  ? 0.7248 0.8769 0.5980 -0.0510 0.0336  -0.2637 89  LEU A CD2 
708  N N   . LEU A 90  ? 0.6916 0.6641 0.5392 -0.0013 0.0422  -0.2001 90  LEU A N   
709  C CA  . LEU A 90  ? 0.7272 0.6483 0.5662 0.0051  0.0455  -0.1902 90  LEU A CA  
710  C C   . LEU A 90  ? 0.8284 0.7121 0.6534 0.0051  0.0508  -0.2035 90  LEU A C   
711  O O   . LEU A 90  ? 0.9199 0.7540 0.7308 -0.0010 0.0570  -0.2045 90  LEU A O   
712  C CB  . LEU A 90  ? 0.7139 0.6420 0.5603 0.0266  0.0407  -0.1717 90  LEU A CB  
713  C CG  . LEU A 90  ? 0.7477 0.6715 0.5997 0.0284  0.0391  -0.1548 90  LEU A CG  
714  C CD1 . LEU A 90  ? 0.7281 0.6612 0.5877 0.0474  0.0359  -0.1417 90  LEU A CD1 
715  C CD2 . LEU A 90  ? 0.7876 0.6642 0.6266 0.0210  0.0433  -0.1528 90  LEU A CD2 
716  N N   . ALA A 91  ? 1.2470 0.9915 0.7658 -0.0907 0.1672  -0.3385 91  ALA A N   
717  C CA  . ALA A 91  ? 1.3019 1.0034 0.7945 -0.0906 0.1793  -0.3635 91  ALA A CA  
718  C C   . ALA A 91  ? 1.3124 0.9947 0.7930 -0.1174 0.1614  -0.3791 91  ALA A C   
719  O O   . ALA A 91  ? 1.2870 0.9969 0.7638 -0.1357 0.1387  -0.3733 91  ALA A O   
720  C CB  . ALA A 91  ? 1.3528 1.0594 0.8043 -0.0818 0.1880  -0.3737 91  ALA A CB  
721  N N   . LYS A 92  ? 1.3771 1.0129 0.8558 -0.1195 0.1719  -0.3971 92  LYS A N   
722  C CA  . LYS A 92  ? 1.4553 1.0682 0.9312 -0.1447 0.1574  -0.4112 92  LYS A CA  
723  C C   . LYS A 92  ? 1.4158 1.0399 0.9345 -0.1525 0.1470  -0.3927 92  LYS A C   
724  O O   . LYS A 92  ? 1.4629 1.0619 0.9916 -0.1686 0.1412  -0.4007 92  LYS A O   
725  C CB  . LYS A 92  ? 1.5122 1.1423 0.9507 -0.1668 0.1350  -0.4239 92  LYS A CB  
726  N N   . GLY A 93  ? 1.3387 0.9998 0.8822 -0.1413 0.1449  -0.3683 93  GLY A N   
727  C CA  . GLY A 93  ? 1.2523 0.9239 0.8365 -0.1420 0.1396  -0.3491 93  GLY A CA  
728  C C   . GLY A 93  ? 1.2590 0.9236 0.8545 -0.1665 0.1227  -0.3515 93  GLY A C   
729  O O   . GLY A 93  ? 1.2402 0.9283 0.8223 -0.1872 0.1017  -0.3536 93  GLY A O   
730  N N   . GLU A 94  ? 1.3146 0.9485 0.9374 -0.1633 0.1320  -0.3491 94  GLU A N   
731  C CA  . GLU A 94  ? 1.3967 1.0212 1.0380 -0.1840 0.1195  -0.3482 94  GLU A CA  
732  C C   . GLU A 94  ? 1.3914 1.0628 1.0468 -0.1967 0.0974  -0.3300 94  GLU A C   
733  O O   . GLU A 94  ? 1.4256 1.1017 1.0893 -0.2190 0.0812  -0.3304 94  GLU A O   
734  C CB  . GLU A 94  ? 1.4978 1.0932 1.1159 -0.2057 0.1135  -0.3729 94  GLU A CB  
735  C CG  . GLU A 94  ? 1.5543 1.0927 1.1738 -0.1974 0.1353  -0.3872 94  GLU A CG  
736  C CD  . GLU A 94  ? 1.5911 1.1087 1.1759 -0.1854 0.1505  -0.4062 94  GLU A CD  
737  O OE1 . GLU A 94  ? 1.6419 1.1602 1.1922 -0.2010 0.1398  -0.4254 94  GLU A OE1 
738  O OE2 . GLU A 94  ? 1.5777 1.0795 1.1701 -0.1598 0.1730  -0.4014 94  GLU A OE2 
739  N N   . TYR A 95  ? 1.3330 1.0400 0.9933 -0.1823 0.0973  -0.3134 95  TYR A N   
740  C CA  . TYR A 95  ? 1.2497 0.9994 0.9280 -0.1883 0.0810  -0.2926 95  TYR A CA  
741  C C   . TYR A 95  ? 1.1771 0.9148 0.8898 -0.1896 0.0815  -0.2809 95  TYR A C   
742  O O   . TYR A 95  ? 1.2306 0.9273 0.9548 -0.1831 0.0960  -0.2867 95  TYR A O   
743  C CB  . TYR A 95  ? 1.2095 0.9900 0.8888 -0.1683 0.0863  -0.2782 95  TYR A CB  
744  C CG  . TYR A 95  ? 1.2019 0.9571 0.8911 -0.1426 0.1098  -0.2788 95  TYR A CG  
745  C CD1 . TYR A 95  ? 1.1481 0.8952 0.8688 -0.1296 0.1174  -0.2659 95  TYR A CD1 
746  C CD2 . TYR A 95  ? 1.2719 1.0117 0.9395 -0.1306 0.1244  -0.2915 95  TYR A CD2 
747  C CE1 . TYR A 95  ? 1.1574 0.8853 0.8906 -0.1049 0.1376  -0.2642 95  TYR A CE1 
748  C CE2 . TYR A 95  ? 1.2842 1.0047 0.9650 -0.1064 0.1456  -0.2898 95  TYR A CE2 
749  C CZ  . TYR A 95  ? 1.2370 0.9532 0.9519 -0.0935 0.1514  -0.2755 95  TYR A CZ  
750  O OH  . TYR A 95  ? 1.2647 0.9663 0.9957 -0.0683 0.1711  -0.2715 95  TYR A OH  
751  N N   . GLN A 96  ? 1.0553 0.8281 0.7849 -0.1964 0.0670  -0.2628 96  GLN A N   
752  C CA  . GLN A 96  ? 0.9809 0.7462 0.7423 -0.1943 0.0685  -0.2485 96  GLN A CA  
753  C C   . GLN A 96  ? 0.9359 0.7193 0.7091 -0.1724 0.0754  -0.2328 96  GLN A C   
754  O O   . GLN A 96  ? 0.9563 0.7723 0.7179 -0.1660 0.0717  -0.2278 96  GLN A O   
755  C CB  . GLN A 96  ? 0.9327 0.7235 0.7078 -0.2176 0.0477  -0.2383 96  GLN A CB  
756  C CG  . GLN A 96  ? 0.9860 0.7530 0.7620 -0.2390 0.0421  -0.2515 96  GLN A CG  
757  C CD  . GLN A 96  ? 0.9366 0.7389 0.7270 -0.2617 0.0195  -0.2402 96  GLN A CD  
758  O OE1 . GLN A 96  ? 0.8751 0.7216 0.6705 -0.2611 0.0077  -0.2227 96  GLN A OE1 
759  N NE2 . GLN A 96  ? 0.9565 0.7404 0.7559 -0.2811 0.0137  -0.2489 96  GLN A NE2 
760  N N   . LYS A 97  ? 0.8652 0.6263 0.6623 -0.1600 0.0859  -0.2243 97  LYS A N   
761  C CA  . LYS A 97  ? 0.7886 0.5645 0.5996 -0.1393 0.0915  -0.2099 97  LYS A CA  
762  C C   . LYS A 97  ? 0.7245 0.5279 0.5628 -0.1413 0.0762  -0.1831 97  LYS A C   
763  O O   . LYS A 97  ? 0.7560 0.5440 0.6069 -0.1548 0.0725  -0.1803 97  LYS A O   
764  C CB  . LYS A 97  ? 0.8015 0.5431 0.6267 -0.1133 0.1127  -0.2095 97  LYS A CB  
765  C CG  . LYS A 97  ? 0.8585 0.5895 0.6684 -0.1010 0.1258  -0.2223 97  LYS A CG  
766  C CD  . LYS A 97  ? 0.8609 0.5631 0.6894 -0.0745 0.1454  -0.2180 97  LYS A CD  
767  C CE  . LYS A 97  ? 0.8858 0.5456 0.7072 -0.0781 0.1565  -0.2319 97  LYS A CE  
768  N NZ  . LYS A 97  ? 0.8915 0.5271 0.7331 -0.0509 0.1754  -0.2241 97  LYS A NZ  
769  N N   . VAL A 98  ? 0.6470 0.4905 0.4943 -0.1286 0.0684  -0.1637 98  VAL A N   
770  C CA  . VAL A 98  ? 0.6409 0.5077 0.5135 -0.1236 0.0580  -0.1371 98  VAL A CA  
771  C C   . VAL A 98  ? 0.5470 0.4191 0.4358 -0.0945 0.0648  -0.1224 98  VAL A C   
772  O O   . VAL A 98  ? 0.5274 0.4050 0.4097 -0.0818 0.0717  -0.1284 98  VAL A O   
773  C CB  . VAL A 98  ? 0.6445 0.5557 0.5132 -0.1375 0.0404  -0.1262 98  VAL A CB  
774  C CG1 . VAL A 98  ? 0.6742 0.5856 0.5247 -0.1667 0.0313  -0.1424 98  VAL A CG1 
775  C CG2 . VAL A 98  ? 0.6828 0.6226 0.5422 -0.1256 0.0400  -0.1227 98  VAL A CG2 
776  N N   . SER A 99  ? 0.5204 0.3916 0.4304 -0.0844 0.0629  -0.1028 99  SER A N   
777  C CA  . SER A 99  ? 0.5303 0.4061 0.4549 -0.0578 0.0668  -0.0888 99  SER A CA  
778  C C   . SER A 99  ? 0.4808 0.3890 0.4146 -0.0536 0.0545  -0.0675 99  SER A C   
779  O O   . SER A 99  ? 0.4767 0.3905 0.4159 -0.0642 0.0479  -0.0565 99  SER A O   
780  C CB  . SER A 99  ? 0.6090 0.4501 0.5468 -0.0445 0.0780  -0.0842 99  SER A CB  
781  O OG  . SER A 99  ? 0.7133 0.5200 0.6426 -0.0476 0.0918  -0.1043 99  SER A OG  
782  N N   . TYR A 100 ? 0.4635 0.3926 0.4002 -0.0385 0.0525  -0.0620 100 TYR A N   
783  C CA  . TYR A 100 ? 0.3929 0.3465 0.3371 -0.0307 0.0433  -0.0436 100 TYR A CA  
784  C C   . TYR A 100 ? 0.3893 0.3359 0.3449 -0.0073 0.0457  -0.0340 100 TYR A C   
785  O O   . TYR A 100 ? 0.3533 0.2895 0.3130 0.0048  0.0528  -0.0416 100 TYR A O   
786  C CB  . TYR A 100 ? 0.3705 0.3537 0.3094 -0.0330 0.0380  -0.0443 100 TYR A CB  
787  C CG  . TYR A 100 ? 0.4280 0.4283 0.3551 -0.0536 0.0323  -0.0468 100 TYR A CG  
788  C CD1 . TYR A 100 ? 0.4836 0.4758 0.4065 -0.0709 0.0296  -0.0494 100 TYR A CD1 
789  C CD2 . TYR A 100 ? 0.4309 0.4570 0.3524 -0.0557 0.0291  -0.0451 100 TYR A CD2 
790  C CE1 . TYR A 100 ? 0.4779 0.4908 0.3902 -0.0898 0.0218  -0.0508 100 TYR A CE1 
791  C CE2 . TYR A 100 ? 0.4300 0.4748 0.3398 -0.0725 0.0234  -0.0448 100 TYR A CE2 
792  C CZ  . TYR A 100 ? 0.4769 0.5169 0.3818 -0.0894 0.0186  -0.0477 100 TYR A CZ  
793  O OH  . TYR A 100 ? 0.5794 0.6427 0.4730 -0.1063 0.0104  -0.0466 100 TYR A OH  
794  N N   . PRO A 101 ? 0.3942 0.3476 0.3543 0.0003  0.0400  -0.0170 101 PRO A N   
795  C CA  . PRO A 101 ? 0.3682 0.3168 0.3347 0.0226  0.0402  -0.0080 101 PRO A CA  
796  C C   . PRO A 101 ? 0.3594 0.3292 0.3286 0.0323  0.0347  -0.0109 101 PRO A C   
797  O O   . PRO A 101 ? 0.3485 0.3375 0.3149 0.0230  0.0306  -0.0147 101 PRO A O   
798  C CB  . PRO A 101 ? 0.3816 0.3315 0.3469 0.0256  0.0363  0.0102  101 PRO A CB  
799  C CG  . PRO A 101 ? 0.3619 0.3148 0.3261 0.0038  0.0359  0.0112  101 PRO A CG  
800  C CD  . PRO A 101 ? 0.3714 0.3367 0.3303 -0.0103 0.0339  -0.0046 101 PRO A CD  
801  N N   . LEU A 102 ? 0.3407 0.3078 0.3169 0.0513  0.0344  -0.0074 102 LEU A N   
802  C CA  . LEU A 102 ? 0.3314 0.3192 0.3150 0.0606  0.0280  -0.0101 102 LEU A CA  
803  C C   . LEU A 102 ? 0.3139 0.3065 0.2957 0.0762  0.0190  0.0019  102 LEU A C   
804  O O   . LEU A 102 ? 0.3250 0.3029 0.3005 0.0841  0.0204  0.0130  102 LEU A O   
805  C CB  . LEU A 102 ? 0.2991 0.2851 0.2954 0.0688  0.0353  -0.0196 102 LEU A CB  
806  C CG  . LEU A 102 ? 0.2937 0.2716 0.2866 0.0550  0.0463  -0.0338 102 LEU A CG  
807  C CD1 . LEU A 102 ? 0.3219 0.2915 0.3267 0.0671  0.0571  -0.0409 102 LEU A CD1 
808  C CD2 . LEU A 102 ? 0.3301 0.3302 0.3195 0.0415  0.0427  -0.0394 102 LEU A CD2 
809  N N   . LEU A 103 ? 0.3105 0.3238 0.2971 0.0800  0.0099  -0.0005 103 LEU A N   
810  C CA  . LEU A 103 ? 0.3009 0.3206 0.2820 0.0931  -0.0010 0.0072  103 LEU A CA  
811  C C   . LEU A 103 ? 0.3300 0.3613 0.3258 0.1079  -0.0064 0.0052  103 LEU A C   
812  O O   . LEU A 103 ? 0.3050 0.3517 0.3182 0.1044  -0.0059 -0.0039 103 LEU A O   
813  C CB  . LEU A 103 ? 0.3066 0.3398 0.2820 0.0845  -0.0087 0.0051  103 LEU A CB  
814  C CG  . LEU A 103 ? 0.3171 0.3574 0.2851 0.0960  -0.0213 0.0077  103 LEU A CG  
815  C CD1 . LEU A 103 ? 0.3004 0.3246 0.2473 0.1063  -0.0210 0.0204  103 LEU A CD1 
816  C CD2 . LEU A 103 ? 0.3144 0.3657 0.2820 0.0851  -0.0263 0.0015  103 LEU A CD2 
817  N N   . LYS A 104 ? 0.3346 0.3612 0.3245 0.1253  -0.0111 0.0153  104 LYS A N   
818  C CA  . LYS A 104 ? 0.2916 0.3343 0.2959 0.1411  -0.0188 0.0163  104 LYS A CA  
819  C C   . LYS A 104 ? 0.3599 0.4203 0.3554 0.1453  -0.0367 0.0164  104 LYS A C   
820  O O   . LYS A 104 ? 0.3540 0.4041 0.3253 0.1485  -0.0406 0.0231  104 LYS A O   
821  C CB  . LYS A 104 ? 0.3256 0.3528 0.3297 0.1596  -0.0121 0.0286  104 LYS A CB  
822  C CG  . LYS A 104 ? 0.3830 0.4302 0.4023 0.1778  -0.0211 0.0333  104 LYS A CG  
823  C CD  . LYS A 104 ? 0.4571 0.4850 0.4718 0.1879  -0.0131 0.0469  104 LYS A CD  
824  C CE  . LYS A 104 ? 0.5140 0.5614 0.5454 0.1994  -0.0205 0.0519  104 LYS A CE  
825  N NZ  . LYS A 104 ? 0.6156 0.6459 0.6391 0.2098  -0.0141 0.0664  104 LYS A NZ  
826  N N   . THR A 105 ? 0.3789 0.4653 0.3941 0.1444  -0.0468 0.0084  105 THR A N   
827  C CA  . THR A 105 ? 0.3594 0.4638 0.3690 0.1462  -0.0658 0.0052  105 THR A CA  
828  C C   . THR A 105 ? 0.3461 0.4699 0.3715 0.1585  -0.0753 0.0092  105 THR A C   
829  O O   . THR A 105 ? 0.3638 0.5043 0.4197 0.1617  -0.0719 0.0077  105 THR A O   
830  C CB  . THR A 105 ? 0.3515 0.4700 0.3737 0.1275  -0.0698 -0.0081 105 THR A CB  
831  O OG1 . THR A 105 ? 0.3619 0.4619 0.3709 0.1135  -0.0580 -0.0096 105 THR A OG1 
832  C CG2 . THR A 105 ? 0.3497 0.4810 0.3631 0.1268  -0.0894 -0.0138 105 THR A CG2 
833  N N   . THR A 106 ? 0.3310 0.4519 0.3360 0.1630  -0.0849 0.0145  106 THR A N   
834  C CA  . THR A 106 ? 0.3463 0.4867 0.3638 0.1716  -0.0954 0.0193  106 THR A CA  
835  C C   . THR A 106 ? 0.3907 0.5484 0.4018 0.1639  -0.1150 0.0101  106 THR A C   
836  O O   . THR A 106 ? 0.4061 0.5487 0.3862 0.1599  -0.1185 0.0066  106 THR A O   
837  C CB  . THR A 106 ? 0.3770 0.5008 0.3772 0.1852  -0.0894 0.0343  106 THR A CB  
838  O OG1 . THR A 106 ? 0.4158 0.5206 0.4241 0.1901  -0.0706 0.0412  106 THR A OG1 
839  C CG2 . THR A 106 ? 0.3583 0.5056 0.3729 0.1951  -0.1015 0.0408  106 THR A CG2 
840  N N   . VAL A 107 ? 0.3794 0.5678 0.4210 0.1611  -0.1267 0.0060  107 VAL A N   
841  C CA  . VAL A 107 ? 0.3500 0.5568 0.3908 0.1513  -0.1466 -0.0038 107 VAL A CA  
842  C C   . VAL A 107 ? 0.3853 0.6135 0.4352 0.1613  -0.1593 0.0055  107 VAL A C   
843  O O   . VAL A 107 ? 0.3689 0.6186 0.4543 0.1670  -0.1580 0.0124  107 VAL A O   
844  C CB  . VAL A 107 ? 0.3298 0.5572 0.4032 0.1351  -0.1505 -0.0169 107 VAL A CB  
845  C CG1 . VAL A 107 ? 0.3175 0.5599 0.3898 0.1222  -0.1708 -0.0280 107 VAL A CG1 
846  C CG2 . VAL A 107 ? 0.3084 0.5164 0.3751 0.1266  -0.1366 -0.0240 107 VAL A CG2 
847  N N   . LYS A 108 ? 0.3978 0.6206 0.4161 0.1643  -0.1708 0.0063  108 LYS A N   
848  C CA  . LYS A 108 ? 0.4306 0.6751 0.4528 0.1735  -0.1856 0.0152  108 LYS A CA  
849  C C   . LYS A 108 ? 0.4857 0.7536 0.5114 0.1595  -0.2090 0.0026  108 LYS A C   
850  O O   . LYS A 108 ? 0.4674 0.7216 0.4710 0.1468  -0.2130 -0.0121 108 LYS A O   
851  C CB  . LYS A 108 ? 0.4950 0.7183 0.4784 0.1879  -0.1815 0.0263  108 LYS A CB  
852  C CG  . LYS A 108 ? 0.5161 0.7142 0.4966 0.1994  -0.1582 0.0389  108 LYS A CG  
853  C CD  . LYS A 108 ? 0.5933 0.7741 0.5411 0.2132  -0.1536 0.0514  108 LYS A CD  
854  C CE  . LYS A 108 ? 0.6042 0.7620 0.5553 0.2230  -0.1310 0.0647  108 LYS A CE  
855  N NZ  . LYS A 108 ? 0.6308 0.7766 0.5579 0.2374  -0.1260 0.0794  108 LYS A NZ  
856  N N   . TYR A 109 ? 0.4399 0.7418 0.4940 0.1619  -0.2241 0.0090  109 TYR A N   
857  C CA  . TYR A 109 ? 0.5972 0.9272 0.6641 0.1466  -0.2476 -0.0015 109 TYR A CA  
858  C C   . TYR A 109 ? 0.6923 1.0358 0.7393 0.1546  -0.2672 0.0056  109 TYR A C   
859  O O   . TYR A 109 ? 0.7185 1.0577 0.7546 0.1738  -0.2623 0.0219  109 TYR A O   
860  C CB  . TYR A 109 ? 0.5054 0.8709 0.6305 0.1396  -0.2509 0.0006  109 TYR A CB  
861  C CG  . TYR A 109 ? 0.4381 0.7932 0.5847 0.1331  -0.2306 -0.0051 109 TYR A CG  
862  C CD1 . TYR A 109 ? 0.3824 0.7353 0.5345 0.1123  -0.2319 -0.0221 109 TYR A CD1 
863  C CD2 . TYR A 109 ? 0.4014 0.7472 0.5615 0.1475  -0.2096 0.0063  109 TYR A CD2 
864  C CE1 . TYR A 109 ? 0.4176 0.7625 0.5883 0.1067  -0.2138 -0.0265 109 TYR A CE1 
865  C CE2 . TYR A 109 ? 0.3414 0.6786 0.5183 0.1415  -0.1917 0.0005  109 TYR A CE2 
866  C CZ  . TYR A 109 ? 0.4219 0.7600 0.6040 0.1213  -0.1942 -0.0154 109 TYR A CZ  
867  O OH  . TYR A 109 ? 0.3742 0.7048 0.5723 0.1151  -0.1763 -0.0206 109 TYR A OH  
868  N N   . GLY A 110 ? 0.7539 1.1134 0.7959 0.1388  -0.2893 -0.0071 110 GLY A N   
869  C CA  . GLY A 110 ? 0.8273 1.2104 0.8607 0.1435  -0.3125 -0.0005 110 GLY A CA  
870  C C   . GLY A 110 ? 0.8638 1.2863 0.9479 0.1512  -0.3207 0.0160  110 GLY A C   
871  O O   . GLY A 110 ? 0.8078 1.2429 0.9374 0.1487  -0.3104 0.0190  110 GLY A O   
872  N N   . ILE A 111 ? 0.9509 1.3927 1.0265 0.1617  -0.3390 0.0273  111 ILE A N   
873  C CA  . ILE A 111 ? 0.9405 1.4203 1.0614 0.1724  -0.3498 0.0451  111 ILE A CA  
874  C C   . ILE A 111 ? 0.8564 1.3237 0.9962 0.1947  -0.3241 0.0623  111 ILE A C   
875  O O   . ILE A 111 ? 0.8010 1.2794 0.9875 0.1945  -0.3128 0.0654  111 ILE A O   
876  C CB  . ILE A 111 ? 0.9825 1.5005 1.1577 0.1524  -0.3651 0.0387  111 ILE A CB  
877  C CG1 . ILE A 111 ? 1.0277 1.5531 1.1811 0.1276  -0.3892 0.0196  111 ILE A CG1 
878  C CG2 . ILE A 111 ? 1.0107 1.5697 1.2339 0.1645  -0.3792 0.0572  111 ILE A CG2 
879  C CD1 . ILE A 111 ? 1.0186 1.5797 1.2245 0.1043  -0.4032 0.0125  111 ILE A CD1 
880  N N   . GLU A 115 ? 0.3985 0.7078 0.5563 0.2103  -0.1684 0.0556  115 GLU A N   
881  C CA  . GLU A 115 ? 0.3844 0.6586 0.5192 0.2059  -0.1493 0.0489  115 GLU A CA  
882  C C   . GLU A 115 ? 0.4254 0.7036 0.5923 0.1990  -0.1351 0.0417  115 GLU A C   
883  O O   . GLU A 115 ? 0.4353 0.7261 0.6370 0.2075  -0.1266 0.0482  115 GLU A O   
884  C CB  . GLU A 115 ? 0.4399 0.6827 0.5531 0.2213  -0.1325 0.0616  115 GLU A CB  
885  C CG  . GLU A 115 ? 0.4539 0.6650 0.5223 0.2181  -0.1274 0.0592  115 GLU A CG  
886  C CD  . GLU A 115 ? 0.4945 0.6758 0.5483 0.2312  -0.1091 0.0726  115 GLU A CD  
887  O OE1 . GLU A 115 ? 0.4832 0.6508 0.5542 0.2340  -0.0913 0.0744  115 GLU A OE1 
888  O OE2 . GLU A 115 ? 0.5325 0.7038 0.5580 0.2383  -0.1119 0.0808  115 GLU A OE2 
889  N N   . ALA A 116 ? 0.3868 0.6529 0.5411 0.1847  -0.1310 0.0283  116 ALA A N   
890  C CA  . ALA A 116 ? 0.3702 0.6338 0.5460 0.1791  -0.1140 0.0214  116 ALA A CA  
891  C C   . ALA A 116 ? 0.3799 0.6069 0.5228 0.1778  -0.0997 0.0181  116 ALA A C   
892  O O   . ALA A 116 ? 0.3656 0.5776 0.4752 0.1719  -0.1068 0.0142  116 ALA A O   
893  C CB  . ALA A 116 ? 0.3871 0.6754 0.5854 0.1608  -0.1227 0.0083  116 ALA A CB  
894  N N   . THR A 117 ? 0.3618 0.5738 0.5141 0.1830  -0.0789 0.0195  117 THR A N   
895  C CA  . THR A 117 ? 0.3733 0.5531 0.4995 0.1802  -0.0650 0.0163  117 THR A CA  
896  C C   . THR A 117 ? 0.3459 0.5303 0.4886 0.1706  -0.0530 0.0043  117 THR A C   
897  O O   . THR A 117 ? 0.2903 0.4935 0.4653 0.1715  -0.0458 0.0020  117 THR A O   
898  C CB  . THR A 117 ? 0.4363 0.5866 0.5521 0.1934  -0.0491 0.0276  117 THR A CB  
899  O OG1 . THR A 117 ? 0.4827 0.6385 0.6290 0.2017  -0.0359 0.0295  117 THR A OG1 
900  C CG2 . THR A 117 ? 0.4312 0.5765 0.5283 0.2027  -0.0590 0.0402  117 THR A CG2 
901  N N   . TYR A 118 ? 0.3216 0.4838 0.4391 0.1565  -0.0481 -0.0020 118 TYR A N   
902  C CA  . TYR A 118 ? 0.3112 0.4677 0.4328 0.1381  -0.0351 -0.0122 118 TYR A CA  
903  C C   . TYR A 118 ? 0.3330 0.4545 0.4257 0.1318  -0.0220 -0.0116 118 TYR A C   
904  O O   . TYR A 118 ? 0.3518 0.4566 0.4200 0.1353  -0.0268 -0.0052 118 TYR A O   
905  C CB  . TYR A 118 ? 0.2269 0.3988 0.3505 0.1210  -0.0461 -0.0205 118 TYR A CB  
906  C CG  . TYR A 118 ? 0.2335 0.4408 0.3859 0.1240  -0.0623 -0.0220 118 TYR A CG  
907  C CD1 . TYR A 118 ? 0.2634 0.4961 0.4533 0.1205  -0.0566 -0.0252 118 TYR A CD1 
908  C CD2 . TYR A 118 ? 0.2474 0.4642 0.3897 0.1306  -0.0835 -0.0198 118 TYR A CD2 
909  C CE1 . TYR A 118 ? 0.2872 0.5564 0.5092 0.1219  -0.0723 -0.0257 118 TYR A CE1 
910  C CE2 . TYR A 118 ? 0.2916 0.5398 0.4593 0.1291  -0.0994 -0.0213 118 TYR A CE2 
911  C CZ  . TYR A 118 ? 0.3033 0.5778 0.5125 0.1239  -0.0941 -0.0236 118 TYR A CZ  
912  O OH  . TYR A 118 ? 0.3598 0.6631 0.5953 0.1188  -0.1087 -0.0228 118 TYR A OH  
913  N N   . LEU A 119 ? 0.2754 0.3876 0.3711 0.1218  -0.0059 -0.0184 119 LEU A N   
914  C CA  . LEU A 119 ? 0.3019 0.3859 0.3733 0.1112  0.0049  -0.0202 119 LEU A CA  
915  C C   . LEU A 119 ? 0.2916 0.3817 0.3569 0.0916  0.0055  -0.0271 119 LEU A C   
916  O O   . LEU A 119 ? 0.2793 0.3878 0.3620 0.0859  0.0084  -0.0331 119 LEU A O   
917  C CB  . LEU A 119 ? 0.3111 0.3767 0.3861 0.1153  0.0230  -0.0235 119 LEU A CB  
918  C CG  . LEU A 119 ? 0.3493 0.3808 0.4037 0.1121  0.0332  -0.0225 119 LEU A CG  
919  C CD1 . LEU A 119 ? 0.3189 0.3392 0.3631 0.1234  0.0258  -0.0094 119 LEU A CD1 
920  C CD2 . LEU A 119 ? 0.3819 0.3965 0.4447 0.1193  0.0508  -0.0278 119 LEU A CD2 
921  N N   . ALA A 120 ? 0.2874 0.3636 0.3299 0.0823  0.0038  -0.0244 120 ALA A N   
922  C CA  . ALA A 120 ? 0.2749 0.3572 0.3111 0.0657  0.0046  -0.0277 120 ALA A CA  
923  C C   . ALA A 120 ? 0.3037 0.3691 0.3220 0.0545  0.0140  -0.0282 120 ALA A C   
924  O O   . ALA A 120 ? 0.2615 0.3088 0.2675 0.0571  0.0149  -0.0230 120 ALA A O   
925  C CB  . ALA A 120 ? 0.3182 0.4050 0.3462 0.0643  -0.0078 -0.0232 120 ALA A CB  
926  N N   . LEU A 121 ? 0.2412 0.3140 0.2589 0.0418  0.0209  -0.0338 121 LEU A N   
927  C CA  . LEU A 121 ? 0.2676 0.3309 0.2674 0.0286  0.0265  -0.0345 121 LEU A CA  
928  C C   . LEU A 121 ? 0.2823 0.3526 0.2728 0.0199  0.0206  -0.0263 121 LEU A C   
929  O O   . LEU A 121 ? 0.2998 0.3628 0.2770 0.0124  0.0206  -0.0214 121 LEU A O   
930  C CB  . LEU A 121 ? 0.2388 0.3069 0.2383 0.0210  0.0376  -0.0445 121 LEU A CB  
931  C CG  . LEU A 121 ? 0.2754 0.3404 0.2547 0.0053  0.0417  -0.0472 121 LEU A CG  
932  C CD1 . LEU A 121 ? 0.2581 0.3022 0.2251 0.0017  0.0405  -0.0469 121 LEU A CD1 
933  C CD2 . LEU A 121 ? 0.2516 0.3202 0.2265 0.0009  0.0540  -0.0587 121 LEU A CD2 
934  N N   . ASN A 122 ? 0.2609 0.3453 0.2603 0.0204  0.0162  -0.0242 122 ASN A N   
935  C CA  . ASN A 122 ? 0.2398 0.3278 0.2317 0.0148  0.0126  -0.0155 122 ASN A CA  
936  C C   . ASN A 122 ? 0.2421 0.3231 0.2316 0.0247  0.0038  -0.0105 122 ASN A C   
937  O O   . ASN A 122 ? 0.2645 0.3353 0.2410 0.0266  0.0025  -0.0022 122 ASN A O   
938  C CB  . ASN A 122 ? 0.2176 0.3210 0.2190 0.0081  0.0158  -0.0163 122 ASN A CB  
939  C CG  . ASN A 122 ? 0.2616 0.3722 0.2542 -0.0033 0.0239  -0.0145 122 ASN A CG  
940  O OD1 . ASN A 122 ? 0.2799 0.3851 0.2588 -0.0081 0.0253  -0.0143 122 ASN A OD1 
941  N ND2 . ASN A 122 ? 0.2233 0.3468 0.2236 -0.0081 0.0288  -0.0127 122 ASN A ND2 
942  N N   . GLU A 123 ? 0.1910 0.2758 0.2813 0.0432  0.0288  -0.0300 123 GLU A N   
943  C CA  . GLU A 123 ? 0.1915 0.2758 0.2887 0.0406  0.0213  -0.0238 123 GLU A CA  
944  C C   . GLU A 123 ? 0.2203 0.3274 0.3365 0.0424  0.0216  -0.0236 123 GLU A C   
945  O O   . GLU A 123 ? 0.1939 0.3206 0.3197 0.0433  0.0289  -0.0273 123 GLU A O   
946  C CB  . GLU A 123 ? 0.2112 0.2879 0.2977 0.0302  0.0193  -0.0183 123 GLU A CB  
947  C CG  . GLU A 123 ? 0.2155 0.3042 0.3034 0.0212  0.0245  -0.0165 123 GLU A CG  
948  C CD  . GLU A 123 ? 0.2686 0.3595 0.3465 0.0190  0.0333  -0.0187 123 GLU A CD  
949  O OE1 . GLU A 123 ? 0.2443 0.3544 0.3314 0.0179  0.0413  -0.0212 123 GLU A OE1 
950  O OE2 . GLU A 123 ? 0.2353 0.3106 0.2961 0.0186  0.0323  -0.0182 123 GLU A OE2 
951  N N   . SER A 124 ? 0.2201 0.3266 0.3415 0.0428  0.0134  -0.0195 124 SER A N   
952  C CA  . SER A 124 ? 0.2127 0.3413 0.3506 0.0415  0.0103  -0.0186 124 SER A CA  
953  C C   . SER A 124 ? 0.1961 0.3188 0.3267 0.0302  0.0054  -0.0144 124 SER A C   
954  O O   . SER A 124 ? 0.2253 0.3287 0.3428 0.0303  0.0010  -0.0114 124 SER A O   
955  C CB  . SER A 124 ? 0.2694 0.4018 0.4177 0.0544  0.0031  -0.0181 124 SER A CB  
956  O OG  . SER A 124 ? 0.2293 0.3863 0.3942 0.0532  -0.0018 -0.0175 124 SER A OG  
957  N N   . THR A 125 ? 0.1858 0.3244 0.3244 0.0201  0.0067  -0.0146 125 THR A N   
958  C CA  . THR A 125 ? 0.1768 0.3058 0.3067 0.0097  0.0014  -0.0123 125 THR A CA  
959  C C   . THR A 125 ? 0.1983 0.3485 0.3437 0.0056  -0.0056 -0.0135 125 THR A C   
960  O O   . THR A 125 ? 0.1844 0.3619 0.3505 0.0084  -0.0045 -0.0157 125 THR A O   
961  C CB  . THR A 125 ? 0.2122 0.3308 0.3308 -0.0027 0.0075  -0.0109 125 THR A CB  
962  O OG1 . THR A 125 ? 0.2324 0.3731 0.3651 -0.0126 0.0127  -0.0119 125 THR A OG1 
963  C CG2 . THR A 125 ? 0.2081 0.3117 0.3130 0.0016  0.0139  -0.0100 125 THR A CG2 
964  N N   . VAL A 126 ? 0.2367 0.3754 0.3720 -0.0002 -0.0132 -0.0128 126 VAL A N   
965  C CA  . VAL A 126 ? 0.2348 0.3909 0.3807 -0.0062 -0.0223 -0.0149 126 VAL A CA  
966  C C   . VAL A 126 ? 0.2016 0.3424 0.3351 -0.0218 -0.0237 -0.0163 126 VAL A C   
967  O O   . VAL A 126 ? 0.2011 0.3137 0.3131 -0.0212 -0.0235 -0.0154 126 VAL A O   
968  C CB  . VAL A 126 ? 0.2292 0.3832 0.3704 0.0044  -0.0330 -0.0138 126 VAL A CB  
969  C CG1 . VAL A 126 ? 0.1831 0.3640 0.3403 0.0005  -0.0436 -0.0164 126 VAL A CG1 
970  C CG2 . VAL A 126 ? 0.3015 0.4539 0.4450 0.0203  -0.0311 -0.0109 126 VAL A CG2 
971  N N   . LYS A 127 ? 0.1799 0.3394 0.3275 -0.0356 -0.0252 -0.0188 127 LYS A N   
972  C CA  . LYS A 127 ? 0.2500 0.3944 0.3870 -0.0523 -0.0289 -0.0212 127 LYS A CA  
973  C C   . LYS A 127 ? 0.2512 0.4227 0.4058 -0.0610 -0.0399 -0.0257 127 LYS A C   
974  O O   . LYS A 127 ? 0.2204 0.4254 0.3978 -0.0536 -0.0433 -0.0260 127 LYS A O   
975  C CB  . LYS A 127 ? 0.3180 0.4531 0.4522 -0.0661 -0.0181 -0.0187 127 LYS A CB  
976  C CG  . LYS A 127 ? 0.3627 0.4743 0.4797 -0.0568 -0.0088 -0.0141 127 LYS A CG  
977  C CD  . LYS A 127 ? 0.3618 0.4698 0.4765 -0.0687 0.0024  -0.0099 127 LYS A CD  
978  C CE  . LYS A 127 ? 0.4015 0.4844 0.4958 -0.0592 0.0086  -0.0056 127 LYS A CE  
979  N NZ  . LYS A 127 ? 0.3548 0.4364 0.4439 -0.0674 0.0198  -0.0005 127 LYS A NZ  
980  N N   . SER A 128 ? 0.2727 0.4294 0.4165 -0.0764 -0.0465 -0.0298 128 SER A N   
981  C CA  . SER A 128 ? 0.3330 0.5173 0.4939 -0.0867 -0.0585 -0.0350 128 SER A CA  
982  C C   . SER A 128 ? 0.3868 0.6008 0.5748 -0.1043 -0.0526 -0.0347 128 SER A C   
983  O O   . SER A 128 ? 0.3789 0.5857 0.5666 -0.1103 -0.0389 -0.0304 128 SER A O   
984  C CB  . SER A 128 ? 0.4495 0.6070 0.5877 -0.0974 -0.0694 -0.0415 128 SER A CB  
985  O OG  . SER A 128 ? 0.4968 0.6325 0.6276 -0.1174 -0.0644 -0.0427 128 SER A OG  
986  N N   . SER A 129 ? 0.4153 0.6653 0.6272 -0.1131 -0.0632 -0.0392 129 SER A N   
987  C CA  . SER A 129 ? 0.5035 0.7877 0.7450 -0.1321 -0.0583 -0.0394 129 SER A CA  
988  C C   . SER A 129 ? 0.5848 0.8455 0.8150 -0.1574 -0.0626 -0.0428 129 SER A C   
989  O O   . SER A 129 ? 0.6447 0.9240 0.8919 -0.1672 -0.0701 -0.0456 129 SER A O   
990  C CB  . SER A 129 ? 0.5316 0.8568 0.8021 -0.1200 -0.0659 -0.0395 129 SER A CB  
991  O OG  . SER A 129 ? 0.5833 0.9060 0.8454 -0.1169 -0.0847 -0.0442 129 SER A OG  
992  N N   . GLY A 130 ? 0.6323 0.8465 0.8317 -0.1657 -0.0584 -0.0424 130 GLY A N   
993  C CA  . GLY A 130 ? 0.7036 0.8878 0.8884 -0.1887 -0.0629 -0.0463 130 GLY A CA  
994  C C   . GLY A 130 ? 0.7326 0.8747 0.8834 -0.1863 -0.0750 -0.0537 130 GLY A C   
995  O O   . GLY A 130 ? 0.7779 0.8706 0.8990 -0.1889 -0.0703 -0.0529 130 GLY A O   
996  N N   . GLY A 131 ? 0.6852 0.8442 0.8378 -0.1778 -0.0902 -0.0604 131 GLY A N   
997  C CA  . GLY A 131 ? 0.6564 0.7779 0.7751 -0.1731 -0.1010 -0.0682 131 GLY A CA  
998  C C   . GLY A 131 ? 0.5984 0.6854 0.6891 -0.1494 -0.0929 -0.0643 131 GLY A C   
999  O O   . GLY A 131 ? 0.5383 0.6246 0.6334 -0.1387 -0.0793 -0.0555 131 GLY A O   
1000 N N   . PRO A 132 ? 0.5479 0.6070 0.6090 -0.1411 -0.1009 -0.0713 132 PRO A N   
1001 C CA  . PRO A 132 ? 0.4870 0.5193 0.5244 -0.1187 -0.0931 -0.0678 132 PRO A CA  
1002 C C   . PRO A 132 ? 0.4039 0.4672 0.4560 -0.0987 -0.0905 -0.0602 132 PRO A C   
1003 O O   . PRO A 132 ? 0.3845 0.4814 0.4523 -0.0966 -0.1003 -0.0608 132 PRO A O   
1004 C CB  . PRO A 132 ? 0.5069 0.5105 0.5120 -0.1164 -0.1030 -0.0787 132 PRO A CB  
1005 C CG  . PRO A 132 ? 0.5642 0.5668 0.5711 -0.1408 -0.1151 -0.0885 132 PRO A CG  
1006 C CD  . PRO A 132 ? 0.5978 0.6491 0.6448 -0.1527 -0.1172 -0.0834 132 PRO A CD  
1007 N N   . PHE A 133 ? 0.3504 0.4007 0.3965 -0.0839 -0.0784 -0.0531 133 PHE A N   
1008 C CA  . PHE A 133 ? 0.3646 0.4354 0.4204 -0.0655 -0.0751 -0.0460 133 PHE A CA  
1009 C C   . PHE A 133 ? 0.3667 0.4215 0.3974 -0.0509 -0.0781 -0.0473 133 PHE A C   
1010 O O   . PHE A 133 ? 0.3366 0.3618 0.3462 -0.0456 -0.0717 -0.0484 133 PHE A O   
1011 C CB  . PHE A 133 ? 0.2939 0.3607 0.3567 -0.0592 -0.0609 -0.0382 133 PHE A CB  
1012 C CG  . PHE A 133 ? 0.2750 0.3586 0.3472 -0.0421 -0.0574 -0.0318 133 PHE A CG  
1013 C CD1 . PHE A 133 ? 0.2741 0.3918 0.3707 -0.0391 -0.0608 -0.0297 133 PHE A CD1 
1014 C CD2 . PHE A 133 ? 0.3003 0.3652 0.3575 -0.0289 -0.0509 -0.0281 133 PHE A CD2 
1015 C CE1 . PHE A 133 ? 0.2803 0.4072 0.3831 -0.0232 -0.0580 -0.0241 133 PHE A CE1 
1016 C CE2 . PHE A 133 ? 0.2997 0.3762 0.3645 -0.0156 -0.0480 -0.0224 133 PHE A CE2 
1017 C CZ  . PHE A 133 ? 0.2606 0.3651 0.3465 -0.0126 -0.0516 -0.0204 133 PHE A CZ  
1018 N N   . VAL A 134 ? 0.3414 0.4168 0.3745 -0.0437 -0.0874 -0.0466 134 VAL A N   
1019 C CA  . VAL A 134 ? 0.3525 0.4165 0.3611 -0.0306 -0.0897 -0.0461 134 VAL A CA  
1020 C C   . VAL A 134 ? 0.3510 0.4389 0.3720 -0.0179 -0.0923 -0.0374 134 VAL A C   
1021 O O   . VAL A 134 ? 0.3490 0.4632 0.3854 -0.0197 -0.1034 -0.0374 134 VAL A O   
1022 C CB  . VAL A 134 ? 0.4175 0.4729 0.4034 -0.0367 -0.1023 -0.0560 134 VAL A CB  
1023 C CG1 . VAL A 134 ? 0.4405 0.4801 0.3964 -0.0231 -0.1002 -0.0554 134 VAL A CG1 
1024 C CG2 . VAL A 134 ? 0.4746 0.5072 0.4520 -0.0526 -0.1031 -0.0661 134 VAL A CG2 
1025 N N   . VAL A 135 ? 0.2940 0.3726 0.3083 -0.0052 -0.0830 -0.0301 135 VAL A N   
1026 C CA  . VAL A 135 ? 0.3050 0.3973 0.3247 0.0072  -0.0856 -0.0212 135 VAL A CA  
1027 C C   . VAL A 135 ? 0.3286 0.4028 0.3223 0.0164  -0.0808 -0.0168 135 VAL A C   
1028 O O   . VAL A 135 ? 0.3390 0.3945 0.3199 0.0163  -0.0710 -0.0189 135 VAL A O   
1029 C CB  . VAL A 135 ? 0.2757 0.3788 0.3206 0.0121  -0.0777 -0.0151 135 VAL A CB  
1030 C CG1 . VAL A 135 ? 0.2863 0.4139 0.3585 0.0043  -0.0813 -0.0185 135 VAL A CG1 
1031 C CG2 . VAL A 135 ? 0.2649 0.3488 0.3053 0.0121  -0.0638 -0.0141 135 VAL A CG2 
1032 N N   . ASP A 136 ? 0.3246 0.4055 0.3111 0.0250  -0.0875 -0.0099 136 ASP A N   
1033 C CA  . ASP A 136 ? 0.3129 0.3798 0.2787 0.0333  -0.0809 -0.0021 136 ASP A CA  
1034 C C   . ASP A 136 ? 0.3224 0.3883 0.3048 0.0392  -0.0719 0.0067  136 ASP A C   
1035 O O   . ASP A 136 ? 0.3309 0.4091 0.3334 0.0430  -0.0763 0.0101  136 ASP A O   
1036 C CB  . ASP A 136 ? 0.3429 0.4131 0.2886 0.0391  -0.0921 0.0031  136 ASP A CB  
1037 C CG  . ASP A 136 ? 0.4055 0.4698 0.3240 0.0342  -0.0984 -0.0061 136 ASP A CG  
1038 O OD1 . ASP A 136 ? 0.4528 0.5270 0.3615 0.0347  -0.1134 -0.0068 136 ASP A OD1 
1039 O OD2 . ASP A 136 ? 0.4152 0.4645 0.3213 0.0305  -0.0889 -0.0132 136 ASP A OD2 
1040 N N   . VAL A 137 ? 0.2962 0.3482 0.2706 0.0401  -0.0596 0.0093  137 VAL A N   
1041 C CA  . VAL A 137 ? 0.2801 0.3285 0.2676 0.0434  -0.0513 0.0161  137 VAL A CA  
1042 C C   . VAL A 137 ? 0.3331 0.3732 0.3051 0.0487  -0.0501 0.0271  137 VAL A C   
1043 O O   . VAL A 137 ? 0.3321 0.3651 0.2836 0.0478  -0.0446 0.0287  137 VAL A O   
1044 C CB  . VAL A 137 ? 0.2579 0.2993 0.2492 0.0395  -0.0398 0.0122  137 VAL A CB  
1045 C CG1 . VAL A 137 ? 0.2535 0.2926 0.2592 0.0413  -0.0332 0.0175  137 VAL A CG1 
1046 C CG2 . VAL A 137 ? 0.2711 0.3154 0.2710 0.0334  -0.0413 0.0028  137 VAL A CG2 
1047 N N   . VAL A 138 ? 0.2915 0.3315 0.2722 0.0546  -0.0545 0.0347  138 VAL A N   
1048 C CA  . VAL A 138 ? 0.3601 0.3883 0.3243 0.0594  -0.0551 0.0471  138 VAL A CA  
1049 C C   . VAL A 138 ? 0.4113 0.4278 0.3870 0.0599  -0.0475 0.0528  138 VAL A C   
1050 O O   . VAL A 138 ? 0.3747 0.3937 0.3702 0.0637  -0.0499 0.0505  138 VAL A O   
1051 C CB  . VAL A 138 ? 0.3508 0.3840 0.3102 0.0676  -0.0698 0.0522  138 VAL A CB  
1052 C CG1 . VAL A 138 ? 0.4040 0.4199 0.3433 0.0729  -0.0706 0.0670  138 VAL A CG1 
1053 C CG2 . VAL A 138 ? 0.3304 0.3758 0.2774 0.0651  -0.0791 0.0449  138 VAL A CG2 
1054 N N   . ILE A 139 ? 0.3569 0.3616 0.3204 0.0554  -0.0380 0.0594  139 ILE A N   
1055 C CA  . ILE A 139 ? 0.3056 0.2983 0.2789 0.0525  -0.0309 0.0638  139 ILE A CA  
1056 C C   . ILE A 139 ? 0.3525 0.3265 0.3091 0.0543  -0.0321 0.0783  139 ILE A C   
1057 O O   . ILE A 139 ? 0.3669 0.3374 0.3026 0.0503  -0.0275 0.0857  139 ILE A O   
1058 C CB  . ILE A 139 ? 0.3177 0.3142 0.2949 0.0437  -0.0188 0.0599  139 ILE A CB  
1059 C CG1 . ILE A 139 ? 0.3035 0.3140 0.2933 0.0429  -0.0183 0.0471  139 ILE A CG1 
1060 C CG2 . ILE A 139 ? 0.3485 0.3338 0.3368 0.0391  -0.0137 0.0634  139 ILE A CG2 
1061 C CD1 . ILE A 139 ? 0.2684 0.2844 0.2610 0.0373  -0.0080 0.0433  139 ILE A CD1 
1062 N N   . ASN A 140 ? 0.3042 0.2647 0.2683 0.0607  -0.0377 0.0824  140 ASN A N   
1063 C CA  . ASN A 140 ? 0.3568 0.2932 0.3038 0.0636  -0.0404 0.0973  140 ASN A CA  
1064 C C   . ASN A 140 ? 0.4183 0.3563 0.3394 0.0672  -0.0464 0.1059  140 ASN A C   
1065 O O   . ASN A 140 ? 0.4103 0.3344 0.3084 0.0620  -0.0414 0.1182  140 ASN A O   
1066 C CB  . ASN A 140 ? 0.3769 0.2965 0.3198 0.0513  -0.0289 0.1039  140 ASN A CB  
1067 C CG  . ASN A 140 ? 0.4210 0.3393 0.3870 0.0473  -0.0247 0.0943  140 ASN A CG  
1068 O OD1 . ASN A 140 ? 0.4111 0.3258 0.3901 0.0563  -0.0309 0.0885  140 ASN A OD1 
1069 N ND2 . ASN A 140 ? 0.4265 0.3501 0.3978 0.0345  -0.0143 0.0920  140 ASN A ND2 
1070 N N   . ASP A 141 ? 0.4380 0.3946 0.3623 0.0749  -0.0569 0.0990  141 ASP A N   
1071 C CA  . ASP A 141 ? 0.4795 0.4408 0.3798 0.0797  -0.0665 0.1044  141 ASP A CA  
1072 C C   . ASP A 141 ? 0.4820 0.4505 0.3614 0.0706  -0.0582 0.1021  141 ASP A C   
1073 O O   . ASP A 141 ? 0.5719 0.5418 0.4254 0.0733  -0.0647 0.1064  141 ASP A O   
1074 C CB  . ASP A 141 ? 0.5228 0.4605 0.4015 0.0874  -0.0734 0.1221  141 ASP A CB  
1075 C CG  . ASP A 141 ? 0.5726 0.4990 0.4696 0.0994  -0.0815 0.1245  141 ASP A CG  
1076 O OD1 . ASP A 141 ? 0.5187 0.4647 0.4423 0.1061  -0.0874 0.1127  141 ASP A OD1 
1077 O OD2 . ASP A 141 ? 0.6217 0.5186 0.5057 0.1022  -0.0812 0.1383  141 ASP A OD2 
1078 N N   . ILE A 142 ? 0.4526 0.4263 0.3416 0.0611  -0.0445 0.0948  142 ILE A N   
1079 C CA  . ILE A 142 ? 0.5086 0.4904 0.3807 0.0549  -0.0352 0.0908  142 ILE A CA  
1080 C C   . ILE A 142 ? 0.4012 0.4001 0.2860 0.0548  -0.0378 0.0737  142 ILE A C   
1081 O O   . ILE A 142 ? 0.3771 0.3814 0.2881 0.0531  -0.0359 0.0656  142 ILE A O   
1082 C CB  . ILE A 142 ? 0.6179 0.5958 0.4933 0.0454  -0.0183 0.0949  142 ILE A CB  
1083 C CG1 . ILE A 142 ? 0.7233 0.6845 0.5744 0.0421  -0.0137 0.1128  142 ILE A CG1 
1084 C CG2 . ILE A 142 ? 0.6354 0.6290 0.5094 0.0416  -0.0079 0.0840  142 ILE A CG2 
1085 C CD1 . ILE A 142 ? 0.7866 0.7468 0.6433 0.0304  0.0027  0.1179  142 ILE A CD1 
1086 N N   . HIS A 143 ? 0.3835 0.3886 0.2477 0.0560  -0.0426 0.0682  143 HIS A N   
1087 C CA  . HIS A 143 ? 0.3863 0.4025 0.2602 0.0544  -0.0456 0.0520  143 HIS A CA  
1088 C C   . HIS A 143 ? 0.3976 0.4150 0.2775 0.0499  -0.0307 0.0450  143 HIS A C   
1089 O O   . HIS A 143 ? 0.3822 0.3985 0.2423 0.0491  -0.0210 0.0457  143 HIS A O   
1090 C CB  A HIS A 143 ? 0.4198 0.4396 0.2687 0.0558  -0.0555 0.0458  143 HIS A CB  
1091 C CB  B HIS A 143 ? 0.4192 0.4386 0.2672 0.0561  -0.0559 0.0469  143 HIS A CB  
1092 C CG  A HIS A 143 ? 0.4564 0.4818 0.3126 0.0519  -0.0569 0.0290  143 HIS A CG  
1093 C CG  B HIS A 143 ? 0.3915 0.4167 0.2419 0.0610  -0.0741 0.0501  143 HIS A CG  
1094 N ND1 A HIS A 143 ? 0.4584 0.4795 0.3039 0.0499  -0.0456 0.0204  143 HIS A ND1 
1095 N ND1 B HIS A 143 ? 0.4292 0.4667 0.2856 0.0596  -0.0873 0.0387  143 HIS A ND1 
1096 C CD2 A HIS A 143 ? 0.4627 0.4963 0.3377 0.0492  -0.0673 0.0198  143 HIS A CD2 
1097 C CD2 B HIS A 143 ? 0.3921 0.4133 0.2420 0.0677  -0.0817 0.0635  143 HIS A CD2 
1098 C CE1 A HIS A 143 ? 0.4529 0.4745 0.3069 0.0466  -0.0501 0.0069  143 HIS A CE1 
1099 C CE1 B HIS A 143 ? 0.4164 0.4620 0.2777 0.0657  -0.1025 0.0447  143 HIS A CE1 
1100 N NE2 A HIS A 143 ? 0.4340 0.4637 0.3060 0.0446  -0.0629 0.0066  143 HIS A NE2 
1101 N NE2 B HIS A 143 ? 0.4059 0.4405 0.2626 0.0721  -0.0996 0.0599  143 HIS A NE2 
1102 N N   . PHE A 144 ? 0.3017 0.3229 0.2082 0.0479  -0.0290 0.0381  144 PHE A N   
1103 C CA  . PHE A 144 ? 0.3295 0.3523 0.2447 0.0453  -0.0164 0.0332  144 PHE A CA  
1104 C C   . PHE A 144 ? 0.3424 0.3661 0.2539 0.0455  -0.0164 0.0195  144 PHE A C   
1105 O O   . PHE A 144 ? 0.3420 0.3658 0.2445 0.0470  -0.0066 0.0155  144 PHE A O   
1106 C CB  . PHE A 144 ? 0.3200 0.3435 0.2628 0.0432  -0.0141 0.0348  144 PHE A CB  
1107 C CG  . PHE A 144 ? 0.2986 0.3260 0.2520 0.0411  -0.0034 0.0305  144 PHE A CG  
1108 C CD1 . PHE A 144 ? 0.2559 0.2866 0.2063 0.0390  0.0075  0.0366  144 PHE A CD1 
1109 C CD2 . PHE A 144 ? 0.2721 0.3011 0.2386 0.0411  -0.0045 0.0212  144 PHE A CD2 
1110 C CE1 . PHE A 144 ? 0.2889 0.3281 0.2521 0.0383  0.0162  0.0325  144 PHE A CE1 
1111 C CE2 . PHE A 144 ? 0.2691 0.3019 0.2449 0.0412  0.0036  0.0179  144 PHE A CE2 
1112 C CZ  . PHE A 144 ? 0.2884 0.3281 0.2640 0.0406  0.0134  0.0231  144 PHE A CZ  
1113 N N   . GLU A 145 ? 0.2953 0.3193 0.2140 0.0440  -0.0268 0.0120  145 GLU A N   
1114 C CA  . GLU A 145 ? 0.3211 0.3404 0.2354 0.0425  -0.0273 -0.0007 145 GLU A CA  
1115 C C   . GLU A 145 ? 0.3146 0.3363 0.2333 0.0380  -0.0410 -0.0062 145 GLU A C   
1116 O O   . GLU A 145 ? 0.3292 0.3601 0.2626 0.0375  -0.0481 -0.0007 145 GLU A O   
1117 C CB  . GLU A 145 ? 0.2787 0.2960 0.2109 0.0421  -0.0191 -0.0039 145 GLU A CB  
1118 C CG  . GLU A 145 ? 0.2756 0.2969 0.2323 0.0381  -0.0236 -0.0025 145 GLU A CG  
1119 C CD  . GLU A 145 ? 0.3391 0.3580 0.3100 0.0379  -0.0165 -0.0041 145 GLU A CD  
1120 O OE1 . GLU A 145 ? 0.2789 0.3010 0.2669 0.0347  -0.0186 -0.0030 145 GLU A OE1 
1121 O OE2 . GLU A 145 ? 0.3363 0.3516 0.3011 0.0418  -0.0091 -0.0065 145 GLU A OE2 
1122 N N   . ARG A 146 ? 0.3091 0.3228 0.2157 0.0348  -0.0447 -0.0177 146 ARG A N   
1123 C CA  . ARG A 146 ? 0.3291 0.3458 0.2445 0.0269  -0.0565 -0.0246 146 ARG A CA  
1124 C C   . ARG A 146 ? 0.3249 0.3328 0.2543 0.0222  -0.0512 -0.0299 146 ARG A C   
1125 O O   . ARG A 146 ? 0.3751 0.3665 0.2912 0.0238  -0.0455 -0.0367 146 ARG A O   
1126 C CB  . ARG A 146 ? 0.3895 0.4002 0.2794 0.0239  -0.0664 -0.0341 146 ARG A CB  
1127 C CG  . ARG A 146 ? 0.3653 0.3806 0.2667 0.0125  -0.0790 -0.0420 146 ARG A CG  
1128 C CD  . ARG A 146 ? 0.3800 0.3951 0.2577 0.0090  -0.0927 -0.0500 146 ARG A CD  
1129 N NE  . ARG A 146 ? 0.3521 0.3859 0.2288 0.0141  -0.1021 -0.0410 146 ARG A NE  
1130 C CZ  . ARG A 146 ? 0.3950 0.4343 0.2531 0.0122  -0.1169 -0.0454 146 ARG A CZ  
1131 N NH1 . ARG A 146 ? 0.3941 0.4208 0.2329 0.0040  -0.1234 -0.0599 146 ARG A NH1 
1132 N NH2 . ARG A 146 ? 0.3708 0.4262 0.2277 0.0188  -0.1261 -0.0354 146 ARG A NH2 
1133 N N   . PHE A 147 ? 0.2993 0.3175 0.2540 0.0178  -0.0525 -0.0263 147 PHE A N   
1134 C CA  . PHE A 147 ? 0.2962 0.3060 0.2625 0.0132  -0.0469 -0.0288 147 PHE A CA  
1135 C C   . PHE A 147 ? 0.3399 0.3450 0.3074 0.0010  -0.0545 -0.0369 147 PHE A C   
1136 O O   . PHE A 147 ? 0.3440 0.3664 0.3241 -0.0057 -0.0632 -0.0371 147 PHE A O   
1137 C CB  . PHE A 147 ? 0.2901 0.3124 0.2802 0.0142  -0.0423 -0.0210 147 PHE A CB  
1138 C CG  . PHE A 147 ? 0.2579 0.2714 0.2561 0.0098  -0.0366 -0.0224 147 PHE A CG  
1139 C CD1 . PHE A 147 ? 0.2928 0.3099 0.3021 -0.0009 -0.0399 -0.0250 147 PHE A CD1 
1140 C CD2 . PHE A 147 ? 0.2857 0.2880 0.2793 0.0159  -0.0282 -0.0207 147 PHE A CD2 
1141 C CE1 . PHE A 147 ? 0.2708 0.2768 0.2832 -0.0057 -0.0342 -0.0246 147 PHE A CE1 
1142 C CE2 . PHE A 147 ? 0.2697 0.2619 0.2674 0.0127  -0.0244 -0.0210 147 PHE A CE2 
1143 C CZ  . PHE A 147 ? 0.2828 0.2749 0.2877 0.0020  -0.0272 -0.0224 147 PHE A CZ  
1144 N N   . ARG A 148 ? 0.3378 0.3197 0.2930 -0.0019 -0.0514 -0.0435 148 ARG A N   
1145 C CA  . ARG A 148 ? 0.3391 0.3096 0.2941 -0.0158 -0.0571 -0.0506 148 ARG A CA  
1146 C C   . ARG A 148 ? 0.3011 0.2559 0.2616 -0.0179 -0.0490 -0.0480 148 ARG A C   
1147 O O   . ARG A 148 ? 0.3541 0.2922 0.3038 -0.0077 -0.0419 -0.0475 148 ARG A O   
1148 C CB  . ARG A 148 ? 0.3929 0.3406 0.3207 -0.0179 -0.0628 -0.0623 148 ARG A CB  
1149 C CG  . ARG A 148 ? 0.4924 0.4539 0.4121 -0.0203 -0.0740 -0.0664 148 ARG A CG  
1150 C CD  . ARG A 148 ? 0.5528 0.4885 0.4438 -0.0248 -0.0803 -0.0802 148 ARG A CD  
1151 N NE  . ARG A 148 ? 0.6192 0.5679 0.4967 -0.0252 -0.0917 -0.0844 148 ARG A NE  
1152 C CZ  . ARG A 148 ? 0.6122 0.5684 0.4750 -0.0120 -0.0891 -0.0806 148 ARG A CZ  
1153 N NH1 . ARG A 148 ? 0.5623 0.5169 0.4256 0.0011  -0.0752 -0.0731 148 ARG A NH1 
1154 N NH2 . ARG A 148 ? 0.6583 0.6246 0.5054 -0.0127 -0.1008 -0.0838 148 ARG A NH2 
1155 N N   . GLY A 149 ? 0.3193 0.2809 0.2962 -0.0306 -0.0500 -0.0458 149 GLY A N   
1156 C CA  . GLY A 149 ? 0.3094 0.2572 0.2897 -0.0324 -0.0421 -0.0410 149 GLY A CA  
1157 C C   . GLY A 149 ? 0.3209 0.2872 0.3226 -0.0458 -0.0413 -0.0367 149 GLY A C   
1158 O O   . GLY A 149 ? 0.3039 0.2875 0.3167 -0.0573 -0.0480 -0.0399 149 GLY A O   
1159 N N   . ASP A 150 ? 0.2410 0.2056 0.2485 -0.0441 -0.0328 -0.0296 150 ASP A N   
1160 C CA  . ASP A 150 ? 0.3093 0.2922 0.3353 -0.0564 -0.0295 -0.0254 150 ASP A CA  
1161 C C   . ASP A 150 ? 0.3017 0.3206 0.3497 -0.0499 -0.0282 -0.0225 150 ASP A C   
1162 O O   . ASP A 150 ? 0.3135 0.3572 0.3808 -0.0594 -0.0283 -0.0223 150 ASP A O   
1163 C CB  . ASP A 150 ? 0.2936 0.2585 0.3127 -0.0581 -0.0210 -0.0189 150 ASP A CB  
1164 C CG  . ASP A 150 ? 0.3581 0.2880 0.3592 -0.0696 -0.0223 -0.0202 150 ASP A CG  
1165 O OD1 . ASP A 150 ? 0.3958 0.3150 0.3904 -0.0774 -0.0296 -0.0277 150 ASP A OD1 
1166 O OD2 . ASP A 150 ? 0.3637 0.2741 0.3551 -0.0707 -0.0165 -0.0138 150 ASP A OD2 
1167 N N   . GLY A 151 ? 0.2652 0.2874 0.3114 -0.0342 -0.0267 -0.0204 151 GLY A N   
1168 C CA  . GLY A 151 ? 0.2529 0.3018 0.3170 -0.0268 -0.0251 -0.0174 151 GLY A CA  
1169 C C   . GLY A 151 ? 0.2117 0.2543 0.2698 -0.0127 -0.0212 -0.0139 151 GLY A C   
1170 O O   . GLY A 151 ? 0.2611 0.2840 0.3038 -0.0079 -0.0199 -0.0138 151 GLY A O   
1171 N N   . LEU A 152 ? 0.1975 0.2581 0.2693 -0.0059 -0.0196 -0.0116 152 LEU A N   
1172 C CA  . LEU A 152 ? 0.1794 0.2357 0.2481 0.0053  -0.0168 -0.0085 152 LEU A CA  
1173 C C   . LEU A 152 ? 0.2214 0.2877 0.3015 0.0079  -0.0110 -0.0071 152 LEU A C   
1174 O O   . LEU A 152 ? 0.2122 0.2955 0.3059 0.0046  -0.0096 -0.0085 152 LEU A O   
1175 C CB  . LEU A 152 ? 0.2069 0.2684 0.2750 0.0127  -0.0226 -0.0073 152 LEU A CB  
1176 C CG  . LEU A 152 ? 0.2206 0.2708 0.2722 0.0129  -0.0270 -0.0087 152 LEU A CG  
1177 C CD1 . LEU A 152 ? 0.2373 0.2971 0.2886 0.0178  -0.0342 -0.0070 152 LEU A CD1 
1178 C CD2 . LEU A 152 ? 0.1836 0.2194 0.2234 0.0182  -0.0216 -0.0069 152 LEU A CD2 
1179 N N   . CYS A 153 ? 0.2247 0.2821 0.2994 0.0139  -0.0076 -0.0053 153 CYS A N   
1180 C CA  . CYS A 153 ? 0.2269 0.2889 0.3070 0.0164  -0.0023 -0.0056 153 CYS A CA  
1181 C C   . CYS A 153 ? 0.2125 0.2697 0.2922 0.0246  -0.0033 -0.0045 153 CYS A C   
1182 O O   . CYS A 153 ? 0.1968 0.2436 0.2682 0.0257  -0.0043 -0.0024 153 CYS A O   
1183 C CB  . CYS A 153 ? 0.1850 0.2369 0.2550 0.0120  0.0023  -0.0048 153 CYS A CB  
1184 S SG  . CYS A 153 ? 0.2108 0.2656 0.2808 0.0154  0.0082  -0.0064 153 CYS A SG  
1185 N N   . MET A 154 ? 0.1797 0.2444 0.2690 0.0301  -0.0027 -0.0059 154 MET A N   
1186 C CA  . MET A 154 ? 0.2236 0.2791 0.3114 0.0365  -0.0036 -0.0049 154 MET A CA  
1187 C C   . MET A 154 ? 0.2162 0.2697 0.3043 0.0381  0.0013  -0.0093 154 MET A C   
1188 O O   . MET A 154 ? 0.1845 0.2486 0.2806 0.0415  0.0044  -0.0130 154 MET A O   
1189 C CB  . MET A 154 ? 0.1637 0.2226 0.2585 0.0438  -0.0083 -0.0030 154 MET A CB  
1190 C CG  . MET A 154 ? 0.2026 0.2452 0.2922 0.0483  -0.0097 -0.0001 154 MET A CG  
1191 S SD  . MET A 154 ? 0.2414 0.2729 0.3185 0.0423  -0.0103 0.0057  154 MET A SD  
1192 C CE  . MET A 154 ? 0.2342 0.2659 0.3076 0.0469  -0.0166 0.0122  154 MET A CE  
1193 N N   . SER A 155 ? 0.2236 0.2653 0.3030 0.0361  0.0017  -0.0093 155 SER A N   
1194 C CA  . SER A 155 ? 0.2203 0.2588 0.2948 0.0358  0.0052  -0.0142 155 SER A CA  
1195 C C   . SER A 155 ? 0.2482 0.2738 0.3213 0.0391  0.0034  -0.0168 155 SER A C   
1196 O O   . SER A 155 ? 0.2471 0.2644 0.3202 0.0380  -0.0002 -0.0127 155 SER A O   
1197 C CB  . SER A 155 ? 0.2449 0.2806 0.3094 0.0300  0.0052  -0.0128 155 SER A CB  
1198 O OG  . SER A 155 ? 0.3128 0.3454 0.3693 0.0296  0.0072  -0.0174 155 SER A OG  
1199 N N   . THR A 156 ? 0.2160 0.2391 0.2870 0.0429  0.0065  -0.0237 156 THR A N   
1200 C CA  . THR A 156 ? 0.2429 0.2490 0.3081 0.0438  0.0046  -0.0285 156 THR A CA  
1201 C C   . THR A 156 ? 0.2306 0.2332 0.2866 0.0355  0.0021  -0.0292 156 THR A C   
1202 O O   . THR A 156 ? 0.2427 0.2549 0.2953 0.0318  0.0026  -0.0264 156 THR A O   
1203 C CB  . THR A 156 ? 0.2889 0.2929 0.3517 0.0514  0.0093  -0.0379 156 THR A CB  
1204 O OG1 . THR A 156 ? 0.2582 0.2710 0.3118 0.0479  0.0139  -0.0419 156 THR A OG1 
1205 C CG2 . THR A 156 ? 0.2576 0.2727 0.3331 0.0616  0.0122  -0.0380 156 THR A CG2 
1206 N N   . PRO A 157 ? 0.2690 0.2570 0.3206 0.0324  -0.0015 -0.0329 157 PRO A N   
1207 C CA  . PRO A 157 ? 0.2505 0.2393 0.2948 0.0247  -0.0054 -0.0351 157 PRO A CA  
1208 C C   . PRO A 157 ? 0.2266 0.2217 0.2589 0.0258  -0.0031 -0.0402 157 PRO A C   
1209 O O   . PRO A 157 ? 0.2425 0.2469 0.2708 0.0225  -0.0051 -0.0364 157 PRO A O   
1210 C CB  . PRO A 157 ? 0.2786 0.2489 0.3205 0.0205  -0.0096 -0.0403 157 PRO A CB  
1211 C CG  . PRO A 157 ? 0.3131 0.2727 0.3627 0.0240  -0.0086 -0.0353 157 PRO A CG  
1212 C CD  . PRO A 157 ? 0.2793 0.2487 0.3330 0.0345  -0.0036 -0.0338 157 PRO A CD  
1213 N N   . SER A 158 ? 0.2841 0.2740 0.3091 0.0312  0.0015  -0.0486 158 SER A N   
1214 C CA  . SER A 158 ? 0.2746 0.2710 0.2849 0.0314  0.0052  -0.0526 158 SER A CA  
1215 C C   . SER A 158 ? 0.2572 0.2690 0.2706 0.0318  0.0108  -0.0450 158 SER A C   
1216 O O   . SER A 158 ? 0.2792 0.2956 0.2794 0.0291  0.0124  -0.0434 158 SER A O   
1217 C CB  . SER A 158 ? 0.3237 0.3122 0.3242 0.0379  0.0105  -0.0645 158 SER A CB  
1218 O OG  . SER A 158 ? 0.2978 0.2905 0.3104 0.0469  0.0175  -0.0653 158 SER A OG  
1219 N N   . GLY A 159 ? 0.2292 0.2472 0.2581 0.0340  0.0127  -0.0395 159 GLY A N   
1220 C CA  . GLY A 159 ? 0.2527 0.2827 0.2849 0.0316  0.0163  -0.0325 159 GLY A CA  
1221 C C   . GLY A 159 ? 0.2296 0.2580 0.2593 0.0266  0.0107  -0.0250 159 GLY A C   
1222 O O   . GLY A 159 ? 0.2649 0.2976 0.2927 0.0238  0.0130  -0.0196 159 GLY A O   
1223 N N   . THR A 160 ? 0.2255 0.2479 0.2559 0.0254  0.0038  -0.0246 160 THR A N   
1224 C CA  . THR A 160 ? 0.2281 0.2524 0.2592 0.0233  -0.0006 -0.0179 160 THR A CA  
1225 C C   . THR A 160 ? 0.2487 0.2727 0.2654 0.0223  -0.0016 -0.0155 160 THR A C   
1226 O O   . THR A 160 ? 0.2494 0.2729 0.2651 0.0228  -0.0038 -0.0095 160 THR A O   
1227 C CB  . THR A 160 ? 0.2346 0.2584 0.2726 0.0216  -0.0068 -0.0178 160 THR A CB  
1228 O OG1 . THR A 160 ? 0.2604 0.2809 0.2917 0.0190  -0.0109 -0.0237 160 THR A OG1 
1229 C CG2 . THR A 160 ? 0.3218 0.3429 0.3711 0.0221  -0.0056 -0.0169 160 THR A CG2 
1230 N N   . THR A 161 ? 0.2138 0.2359 0.2169 0.0218  -0.0001 -0.0198 161 THR A N   
1231 C CA  . THR A 161 ? 0.2580 0.2778 0.2432 0.0209  -0.0013 -0.0159 161 THR A CA  
1232 C C   . THR A 161 ? 0.3148 0.3340 0.2936 0.0187  0.0072  -0.0111 161 THR A C   
1233 O O   . THR A 161 ? 0.3249 0.3387 0.2857 0.0171  0.0075  -0.0061 161 THR A O   
1234 C CB  . THR A 161 ? 0.3121 0.3299 0.2808 0.0206  -0.0038 -0.0225 161 THR A CB  
1235 O OG1 . THR A 161 ? 0.3081 0.3256 0.2786 0.0214  0.0026  -0.0312 161 THR A OG1 
1236 C CG2 . THR A 161 ? 0.3222 0.3416 0.2944 0.0201  -0.0152 -0.0249 161 THR A CG2 
1237 N N   . ALA A 162 ? 0.2739 0.2986 0.2667 0.0178  0.0134  -0.0120 162 ALA A N   
1238 C CA  . ALA A 162 ? 0.2852 0.3139 0.2761 0.0131  0.0221  -0.0087 162 ALA A CA  
1239 C C   . ALA A 162 ? 0.2940 0.3193 0.2933 0.0101  0.0201  -0.0025 162 ALA A C   
1240 O O   . ALA A 162 ? 0.2491 0.2636 0.2419 0.0115  0.0138  0.0022  162 ALA A O   
1241 C CB  . ALA A 162 ? 0.2967 0.3384 0.2981 0.0147  0.0301  -0.0157 162 ALA A CB  
1242 N N   . TYR A 163 ? 0.2419 0.2765 0.2551 0.0067  0.0247  -0.0030 163 TYR A N   
1243 C CA  . TYR A 163 ? 0.2023 0.2320 0.2209 0.0026  0.0220  0.0012  163 TYR A CA  
1244 C C   . TYR A 163 ? 0.2046 0.2259 0.2251 0.0085  0.0138  0.0017  163 TYR A C   
1245 O O   . TYR A 163 ? 0.2257 0.2345 0.2393 0.0079  0.0105  0.0056  163 TYR A O   
1246 C CB  . TYR A 163 ? 0.2260 0.2724 0.2633 -0.0003 0.0254  -0.0017 163 TYR A CB  
1247 C CG  . TYR A 163 ? 0.2334 0.2782 0.2744 -0.0093 0.0249  0.0014  163 TYR A CG  
1248 C CD1 . TYR A 163 ? 0.2343 0.2582 0.2611 -0.0131 0.0216  0.0062  163 TYR A CD1 
1249 C CD2 . TYR A 163 ? 0.2998 0.3640 0.3588 -0.0136 0.0270  -0.0012 163 TYR A CD2 
1250 C CE1 . TYR A 163 ? 0.3067 0.3249 0.3349 -0.0226 0.0205  0.0078  163 TYR A CE1 
1251 C CE2 . TYR A 163 ? 0.3312 0.3945 0.3939 -0.0241 0.0252  0.0005  163 TYR A CE2 
1252 C CZ  . TYR A 163 ? 0.3389 0.3771 0.3851 -0.0292 0.0220  0.0046  163 TYR A CZ  
1253 O OH  . TYR A 163 ? 0.3216 0.3546 0.3693 -0.0406 0.0197  0.0050  163 TYR A OH  
1254 N N   . ASN A 164 ? 0.1954 0.2225 0.2247 0.0143  0.0111  -0.0024 164 ASN A N   
1255 C CA  . ASN A 164 ? 0.2257 0.2493 0.2587 0.0188  0.0052  -0.0017 164 ASN A CA  
1256 C C   . ASN A 164 ? 0.2455 0.2602 0.2674 0.0210  0.0013  0.0017  164 ASN A C   
1257 O O   . ASN A 164 ? 0.2377 0.2481 0.2603 0.0242  -0.0017 0.0036  164 ASN A O   
1258 C CB  . ASN A 164 ? 0.1932 0.2216 0.2335 0.0221  0.0038  -0.0057 164 ASN A CB  
1259 C CG  . ASN A 164 ? 0.2492 0.2768 0.2932 0.0245  -0.0009 -0.0043 164 ASN A CG  
1260 O OD1 . ASN A 164 ? 0.2513 0.2804 0.3022 0.0255  -0.0014 -0.0031 164 ASN A OD1 
1261 N ND2 . ASN A 164 ? 0.2067 0.2341 0.2460 0.0251  -0.0043 -0.0045 164 ASN A ND2 
1262 N N   . LYS A 165 ? 0.2061 0.2186 0.2167 0.0209  0.0010  0.0023  165 LYS A N   
1263 C CA  . LYS A 165 ? 0.1747 0.1804 0.1751 0.0250  -0.0046 0.0061  165 LYS A CA  
1264 C C   . LYS A 165 ? 0.2481 0.2391 0.2389 0.0249  -0.0043 0.0118  165 LYS A C   
1265 O O   . LYS A 165 ? 0.2257 0.2107 0.2153 0.0315  -0.0090 0.0140  165 LYS A O   
1266 C CB  . LYS A 165 ? 0.2257 0.2314 0.2121 0.0244  -0.0058 0.0057  165 LYS A CB  
1267 C CG  . LYS A 165 ? 0.2495 0.2514 0.2259 0.0301  -0.0141 0.0098  165 LYS A CG  
1268 C CD  . LYS A 165 ? 0.2453 0.2479 0.2055 0.0292  -0.0168 0.0088  165 LYS A CD  
1269 C CE  . LYS A 165 ? 0.3272 0.3313 0.2814 0.0362  -0.0279 0.0122  165 LYS A CE  
1270 N NZ  . LYS A 165 ? 0.3697 0.3589 0.3129 0.0418  -0.0298 0.0213  165 LYS A NZ  
1271 N N   . SER A 166 ? 0.2538 0.2388 0.2385 0.0174  0.0014  0.0137  166 SER A N   
1272 C CA  . SER A 166 ? 0.2644 0.2308 0.2384 0.0144  0.0018  0.0190  166 SER A CA  
1273 C C   . SER A 166 ? 0.2463 0.2084 0.2290 0.0166  -0.0003 0.0165  166 SER A C   
1274 O O   . SER A 166 ? 0.2698 0.2121 0.2422 0.0179  -0.0024 0.0194  166 SER A O   
1275 C CB  . SER A 166 ? 0.2676 0.2327 0.2370 0.0025  0.0094  0.0212  166 SER A CB  
1276 O OG  . SER A 166 ? 0.3485 0.3149 0.3043 0.0009  0.0126  0.0241  166 SER A OG  
1277 N N   . LEU A 167 ? 0.2552 0.2328 0.2539 0.0171  0.0002  0.0112  167 LEU A N   
1278 C CA  . LEU A 167 ? 0.2486 0.2243 0.2532 0.0194  -0.0016 0.0083  167 LEU A CA  
1279 C C   . LEU A 167 ? 0.2879 0.2670 0.2956 0.0300  -0.0050 0.0073  167 LEU A C   
1280 O O   . LEU A 167 ? 0.2575 0.2377 0.2690 0.0330  -0.0053 0.0046  167 LEU A O   
1281 C CB  . LEU A 167 ? 0.2303 0.2211 0.2484 0.0148  0.0002  0.0045  167 LEU A CB  
1282 C CG  . LEU A 167 ? 0.2424 0.2363 0.2627 0.0042  0.0037  0.0046  167 LEU A CG  
1283 C CD1 . LEU A 167 ? 0.2273 0.2405 0.2638 0.0029  0.0041  0.0009  167 LEU A CD1 
1284 C CD2 . LEU A 167 ? 0.2260 0.2021 0.2367 -0.0027 0.0027  0.0057  167 LEU A CD2 
1285 N N   . GLY A 168 ? 0.2615 0.2446 0.2679 0.0354  -0.0074 0.0094  168 GLY A N   
1286 C CA  . GLY A 168 ? 0.2365 0.2281 0.2495 0.0446  -0.0103 0.0086  168 GLY A CA  
1287 C C   . GLY A 168 ? 0.2842 0.2954 0.3119 0.0431  -0.0096 0.0061  168 GLY A C   
1288 O O   . GLY A 168 ? 0.3050 0.3273 0.3412 0.0485  -0.0106 0.0057  168 GLY A O   
1289 N N   . GLY A 169 ? 0.2288 0.2442 0.2600 0.0361  -0.0077 0.0046  169 GLY A N   
1290 C CA  . GLY A 169 ? 0.2189 0.2464 0.2614 0.0341  -0.0075 0.0027  169 GLY A CA  
1291 C C   . GLY A 169 ? 0.2725 0.3086 0.3182 0.0347  -0.0116 0.0022  169 GLY A C   
1292 O O   . GLY A 169 ? 0.2324 0.2660 0.2699 0.0370  -0.0152 0.0032  169 GLY A O   
1293 N N   . ALA A 170 ? 0.1886 0.2342 0.2453 0.0318  -0.0118 0.0009  170 ALA A N   
1294 C CA  . ALA A 170 ? 0.2360 0.2911 0.2982 0.0291  -0.0166 -0.0009 170 ALA A CA  
1295 C C   . ALA A 170 ? 0.2421 0.2897 0.2969 0.0244  -0.0178 -0.0051 170 ALA A C   
1296 O O   . ALA A 170 ? 0.2297 0.2688 0.2814 0.0231  -0.0136 -0.0066 170 ALA A O   
1297 C CB  . ALA A 170 ? 0.2274 0.2934 0.3038 0.0248  -0.0154 -0.0004 170 ALA A CB  
1298 N N   . LEU A 171 ? 0.2178 0.2700 0.2693 0.0230  -0.0239 -0.0076 171 LEU A N   
1299 C CA  . LEU A 171 ? 0.2036 0.2485 0.2461 0.0186  -0.0252 -0.0136 171 LEU A CA  
1300 C C   . LEU A 171 ? 0.2199 0.2659 0.2728 0.0114  -0.0271 -0.0176 171 LEU A C   
1301 O O   . LEU A 171 ? 0.3022 0.3609 0.3661 0.0078  -0.0320 -0.0169 171 LEU A O   
1302 C CB  . LEU A 171 ? 0.1973 0.2443 0.2265 0.0199  -0.0319 -0.0149 171 LEU A CB  
1303 C CG  . LEU A 171 ? 0.2590 0.3023 0.2760 0.0266  -0.0315 -0.0087 171 LEU A CG  
1304 C CD1 . LEU A 171 ? 0.2935 0.3361 0.2925 0.0277  -0.0385 -0.0092 171 LEU A CD1 
1305 C CD2 . LEU A 171 ? 0.2969 0.3287 0.3075 0.0266  -0.0221 -0.0069 171 LEU A CD2 
1306 N N   . MET A 172 ? 0.2247 0.2577 0.2754 0.0093  -0.0234 -0.0216 172 MET A N   
1307 C CA  . MET A 172 ? 0.2502 0.2780 0.3087 0.0018  -0.0253 -0.0242 172 MET A CA  
1308 C C   . MET A 172 ? 0.2918 0.3045 0.3393 -0.0011 -0.0276 -0.0338 172 MET A C   
1309 O O   . MET A 172 ? 0.3163 0.3197 0.3532 0.0048  -0.0232 -0.0377 172 MET A O   
1310 C CB  . MET A 172 ? 0.2868 0.3086 0.3535 0.0022  -0.0196 -0.0189 172 MET A CB  
1311 C CG  . MET A 172 ? 0.3601 0.3734 0.4220 0.0097  -0.0141 -0.0181 172 MET A CG  
1312 S SD  . MET A 172 ? 0.3558 0.3685 0.4260 0.0108  -0.0103 -0.0094 172 MET A SD  
1313 C CE  . MET A 172 ? 0.3038 0.3066 0.3788 0.0005  -0.0127 -0.0090 172 MET A CE  
1314 N N   . HIS A 173 ? 0.2867 0.2981 0.3375 -0.0106 -0.0341 -0.0383 173 HIS A N   
1315 C CA  . HIS A 173 ? 0.2938 0.2873 0.3322 -0.0144 -0.0374 -0.0493 173 HIS A CA  
1316 C C   . HIS A 173 ? 0.3549 0.3254 0.3903 -0.0100 -0.0310 -0.0515 173 HIS A C   
1317 O O   . HIS A 173 ? 0.3763 0.3417 0.4222 -0.0114 -0.0281 -0.0446 173 HIS A O   
1318 C CB  . HIS A 173 ? 0.3009 0.2954 0.3456 -0.0282 -0.0463 -0.0534 173 HIS A CB  
1319 C CG  . HIS A 173 ? 0.3350 0.3114 0.3631 -0.0325 -0.0519 -0.0669 173 HIS A CG  
1320 N ND1 . HIS A 173 ? 0.3805 0.3277 0.4021 -0.0349 -0.0502 -0.0738 173 HIS A ND1 
1321 C CD2 . HIS A 173 ? 0.3631 0.3443 0.3764 -0.0333 -0.0594 -0.0752 173 HIS A CD2 
1322 C CE1 . HIS A 173 ? 0.4082 0.3425 0.4122 -0.0376 -0.0560 -0.0873 173 HIS A CE1 
1323 N NE2 . HIS A 173 ? 0.3667 0.3223 0.3648 -0.0372 -0.0617 -0.0883 173 HIS A NE2 
1324 N N   . PRO A 174 ? 0.3504 0.3070 0.3707 -0.0039 -0.0288 -0.0610 174 PRO A N   
1325 C CA  . PRO A 174 ? 0.3460 0.2844 0.3649 0.0047  -0.0223 -0.0632 174 PRO A CA  
1326 C C   . PRO A 174 ? 0.4337 0.3449 0.4525 -0.0005 -0.0255 -0.0672 174 PRO A C   
1327 O O   . PRO A 174 ? 0.5021 0.3959 0.5201 0.0084  -0.0213 -0.0680 174 PRO A O   
1328 C CB  . PRO A 174 ? 0.4239 0.3612 0.4268 0.0135  -0.0179 -0.0731 174 PRO A CB  
1329 C CG  . PRO A 174 ? 0.4352 0.3792 0.4253 0.0063  -0.0247 -0.0786 174 PRO A CG  
1330 C CD  . PRO A 174 ? 0.3617 0.3240 0.3652 -0.0015 -0.0305 -0.0683 174 PRO A CD  
1331 N N   . SER A 175 ? 0.4146 0.3213 0.4348 -0.0149 -0.0331 -0.0691 175 SER A N   
1332 C CA  . SER A 175 ? 0.4374 0.3169 0.4593 -0.0232 -0.0356 -0.0694 175 SER A CA  
1333 C C   . SER A 175 ? 0.4431 0.3255 0.4791 -0.0249 -0.0319 -0.0543 175 SER A C   
1334 O O   . SER A 175 ? 0.4591 0.3161 0.4948 -0.0307 -0.0326 -0.0514 175 SER A O   
1335 C CB  . SER A 175 ? 0.4737 0.3513 0.4951 -0.0413 -0.0450 -0.0757 175 SER A CB  
1336 O OG  . SER A 175 ? 0.4677 0.3782 0.5052 -0.0493 -0.0473 -0.0666 175 SER A OG  
1337 N N   . ILE A 176 ? 0.3777 0.2878 0.4235 -0.0202 -0.0281 -0.0447 176 ILE A N   
1338 C CA  . ILE A 176 ? 0.3922 0.3068 0.4480 -0.0211 -0.0243 -0.0313 176 ILE A CA  
1339 C C   . ILE A 176 ? 0.3789 0.2844 0.4310 -0.0056 -0.0196 -0.0284 176 ILE A C   
1340 O O   . ILE A 176 ? 0.3822 0.3014 0.4332 0.0052  -0.0169 -0.0312 176 ILE A O   
1341 C CB  . ILE A 176 ? 0.3145 0.2624 0.3815 -0.0236 -0.0232 -0.0241 176 ILE A CB  
1342 C CG1 . ILE A 176 ? 0.3497 0.3117 0.4233 -0.0370 -0.0291 -0.0277 176 ILE A CG1 
1343 C CG2 . ILE A 176 ? 0.3160 0.2680 0.3900 -0.0244 -0.0184 -0.0112 176 ILE A CG2 
1344 C CD1 . ILE A 176 ? 0.3705 0.3660 0.4546 -0.0354 -0.0289 -0.0229 176 ILE A CD1 
1345 N N   . GLU A 177 ? 0.3580 0.2409 0.4084 -0.0048 -0.0191 -0.0222 177 GLU A N   
1346 C CA  . GLU A 177 ? 0.3633 0.2387 0.4116 0.0112  -0.0167 -0.0193 177 GLU A CA  
1347 C C   . GLU A 177 ? 0.3814 0.2790 0.4365 0.0131  -0.0141 -0.0076 177 GLU A C   
1348 O O   . GLU A 177 ? 0.3958 0.2866 0.4504 0.0083  -0.0138 0.0031  177 GLU A O   
1349 C CB  . GLU A 177 ? 0.3688 0.2069 0.4094 0.0134  -0.0188 -0.0177 177 GLU A CB  
1350 C CG  . GLU A 177 ? 0.3835 0.1946 0.4147 0.0117  -0.0216 -0.0313 177 GLU A CG  
1351 C CD  . GLU A 177 ? 0.4832 0.2526 0.5051 0.0185  -0.0236 -0.0302 177 GLU A CD  
1352 O OE1 . GLU A 177 ? 0.5476 0.3077 0.5661 0.0370  -0.0225 -0.0368 177 GLU A OE1 
1353 O OE2 . GLU A 177 ? 0.5197 0.2660 0.5379 0.0059  -0.0258 -0.0217 177 GLU A OE2 
1354 N N   . ALA A 178 ? 0.3334 0.2558 0.3926 0.0194  -0.0120 -0.0099 178 ALA A N   
1355 C CA  . ALA A 178 ? 0.2848 0.2278 0.3487 0.0198  -0.0101 -0.0014 178 ALA A CA  
1356 C C   . ALA A 178 ? 0.2968 0.2569 0.3632 0.0295  -0.0085 -0.0049 178 ALA A C   
1357 O O   . ALA A 178 ? 0.2911 0.2518 0.3566 0.0343  -0.0074 -0.0133 178 ALA A O   
1358 C CB  . ALA A 178 ? 0.2906 0.2495 0.3586 0.0086  -0.0095 0.0007  178 ALA A CB  
1359 N N   . MET A 179 ? 0.2376 0.2115 0.3063 0.0312  -0.0078 0.0015  179 MET A N   
1360 C CA  . MET A 179 ? 0.2189 0.2100 0.2906 0.0360  -0.0064 -0.0009 179 MET A CA  
1361 C C   . MET A 179 ? 0.2441 0.2478 0.3151 0.0311  -0.0056 0.0030  179 MET A C   
1362 O O   . MET A 179 ? 0.2121 0.2142 0.2814 0.0271  -0.0055 0.0089  179 MET A O   
1363 C CB  . MET A 179 ? 0.2232 0.2168 0.2986 0.0454  -0.0080 0.0010  179 MET A CB  
1364 C CG  . MET A 179 ? 0.2542 0.2425 0.3257 0.0461  -0.0112 0.0104  179 MET A CG  
1365 S SD  . MET A 179 ? 0.2619 0.2550 0.3379 0.0586  -0.0161 0.0127  179 MET A SD  
1366 C CE  . MET A 179 ? 0.2581 0.2421 0.3221 0.0567  -0.0198 0.0249  179 MET A CE  
1367 N N   . GLN A 180 ? 0.2290 0.2440 0.3004 0.0315  -0.0043 0.0000  180 GLN A N   
1368 C CA  . GLN A 180 ? 0.2394 0.2620 0.3084 0.0286  -0.0038 0.0025  180 GLN A CA  
1369 C C   . GLN A 180 ? 0.2281 0.2571 0.2961 0.0307  -0.0039 0.0024  180 GLN A C   
1370 O O   . GLN A 180 ? 0.2135 0.2465 0.2836 0.0312  -0.0029 -0.0010 180 GLN A O   
1371 C CB  . GLN A 180 ? 0.1914 0.2170 0.2589 0.0256  -0.0035 -0.0005 180 GLN A CB  
1372 C CG  . GLN A 180 ? 0.1740 0.2060 0.2393 0.0258  -0.0032 0.0017  180 GLN A CG  
1373 C CD  . GLN A 180 ? 0.2090 0.2449 0.2735 0.0249  -0.0048 0.0002  180 GLN A CD  
1374 O OE1 . GLN A 180 ? 0.2073 0.2476 0.2707 0.0274  -0.0050 0.0017  180 GLN A OE1 
1375 N NE2 . GLN A 180 ? 0.1813 0.2150 0.2453 0.0224  -0.0066 -0.0033 180 GLN A NE2 
1376 N N   . LEU A 181 ? 0.2036 0.2342 0.2679 0.0307  -0.0046 0.0056  181 LEU A N   
1377 C CA  . LEU A 181 ? 0.1789 0.2132 0.2407 0.0310  -0.0061 0.0046  181 LEU A CA  
1378 C C   . LEU A 181 ? 0.2246 0.2569 0.2800 0.0294  -0.0048 0.0031  181 LEU A C   
1379 O O   . LEU A 181 ? 0.2538 0.2853 0.3054 0.0308  -0.0034 0.0046  181 LEU A O   
1380 C CB  . LEU A 181 ? 0.2128 0.2472 0.2703 0.0331  -0.0090 0.0081  181 LEU A CB  
1381 C CG  . LEU A 181 ? 0.2419 0.2801 0.2954 0.0322  -0.0126 0.0059  181 LEU A CG  
1382 C CD1 . LEU A 181 ? 0.2163 0.2637 0.2808 0.0323  -0.0156 0.0037  181 LEU A CD1 
1383 C CD2 . LEU A 181 ? 0.2045 0.2411 0.2471 0.0344  -0.0153 0.0095  181 LEU A CD2 
1384 N N   . THR A 182 ? 0.1994 0.2309 0.2538 0.0267  -0.0047 0.0006  182 THR A N   
1385 C CA  . THR A 182 ? 0.1766 0.2003 0.2225 0.0261  -0.0043 -0.0003 182 THR A CA  
1386 C C   . THR A 182 ? 0.2233 0.2432 0.2647 0.0221  -0.0065 -0.0026 182 THR A C   
1387 O O   . THR A 182 ? 0.2584 0.2860 0.3066 0.0182  -0.0080 -0.0035 182 THR A O   
1388 C CB  . THR A 182 ? 0.2378 0.2578 0.2817 0.0246  -0.0026 -0.0001 182 THR A CB  
1389 O OG1 . THR A 182 ? 0.2520 0.2772 0.3006 0.0203  -0.0010 -0.0010 182 THR A OG1 
1390 C CG2 . THR A 182 ? 0.2022 0.2255 0.2485 0.0279  -0.0024 0.0009  182 THR A CG2 
1391 N N   . GLU A 183 ? 0.2106 0.2191 0.2413 0.0235  -0.0070 -0.0041 183 GLU A N   
1392 C CA  . GLU A 183 ? 0.2451 0.2446 0.2682 0.0184  -0.0100 -0.0077 183 GLU A CA  
1393 C C   . GLU A 183 ? 0.2808 0.2689 0.3003 0.0117  -0.0091 -0.0074 183 GLU A C   
1394 O O   . GLU A 183 ? 0.2315 0.2117 0.2469 0.0147  -0.0068 -0.0047 183 GLU A O   
1395 C CB  . GLU A 183 ? 0.3166 0.3046 0.3263 0.0242  -0.0104 -0.0109 183 GLU A CB  
1396 C CG  . GLU A 183 ? 0.2952 0.2936 0.3049 0.0305  -0.0091 -0.0098 183 GLU A CG  
1397 C CD  . GLU A 183 ? 0.3499 0.3394 0.3450 0.0368  -0.0077 -0.0141 183 GLU A CD  
1398 O OE1 . GLU A 183 ? 0.3820 0.3554 0.3680 0.0393  -0.0075 -0.0180 183 GLU A OE1 
1399 O OE2 . GLU A 183 ? 0.3491 0.3464 0.3401 0.0399  -0.0063 -0.0134 183 GLU A OE2 
1400 N N   . MET A 184 ? 0.2263 0.2133 0.2465 0.0019  -0.0116 -0.0098 184 MET A N   
1401 C CA  . MET A 184 ? 0.2813 0.2523 0.2944 -0.0074 -0.0107 -0.0092 184 MET A CA  
1402 C C   . MET A 184 ? 0.3213 0.2709 0.3201 -0.0103 -0.0150 -0.0144 184 MET A C   
1403 O O   . MET A 184 ? 0.3865 0.3420 0.3878 -0.0175 -0.0198 -0.0190 184 MET A O   
1404 C CB  . MET A 184 ? 0.2659 0.2529 0.2922 -0.0195 -0.0091 -0.0081 184 MET A CB  
1405 C CG  . MET A 184 ? 0.2608 0.2701 0.3012 -0.0155 -0.0048 -0.0055 184 MET A CG  
1406 S SD  . MET A 184 ? 0.3650 0.3967 0.4224 -0.0290 -0.0023 -0.0060 184 MET A SD  
1407 C CE  . MET A 184 ? 0.3500 0.4062 0.4229 -0.0180 0.0011  -0.0060 184 MET A CE  
1408 N N   . ALA A 185 ? 0.2661 0.1907 0.2494 -0.0039 -0.0143 -0.0143 185 ALA A N   
1409 C CA  . ALA A 185 ? 0.3029 0.1990 0.2688 -0.0059 -0.0177 -0.0200 185 ALA A CA  
1410 C C   . ALA A 185 ? 0.3744 0.2760 0.3369 -0.0046 -0.0222 -0.0281 185 ALA A C   
1411 O O   . ALA A 185 ? 0.3583 0.2549 0.3176 -0.0163 -0.0274 -0.0334 185 ALA A O   
1412 C CB  . ALA A 185 ? 0.3199 0.1996 0.2818 -0.0231 -0.0189 -0.0190 185 ALA A CB  
1413 N N   . SER A 186 ? 0.3583 0.2715 0.3211 0.0087  -0.0202 -0.0288 186 SER A N   
1414 C CA  . SER A 186 ? 0.4080 0.3248 0.3627 0.0106  -0.0238 -0.0356 186 SER A CA  
1415 C C   . SER A 186 ? 0.4285 0.3151 0.3605 0.0142  -0.0253 -0.0445 186 SER A C   
1416 O O   . SER A 186 ? 0.4220 0.2877 0.3457 0.0223  -0.0221 -0.0444 186 SER A O   
1417 C CB  . SER A 186 ? 0.4407 0.3778 0.4002 0.0221  -0.0198 -0.0326 186 SER A CB  
1418 O OG  . SER A 186 ? 0.5139 0.4466 0.4725 0.0338  -0.0138 -0.0303 186 SER A OG  
1419 N N   . ILE A 187 ? 0.4253 0.3086 0.3459 0.0093  -0.0311 -0.0527 187 ILE A N   
1420 C CA  . ILE A 187 ? 0.4611 0.3153 0.3566 0.0141  -0.0327 -0.0638 187 ILE A CA  
1421 C C   . ILE A 187 ? 0.4830 0.3466 0.3699 0.0311  -0.0267 -0.0660 187 ILE A C   
1422 O O   . ILE A 187 ? 0.4391 0.3285 0.3316 0.0323  -0.0262 -0.0626 187 ILE A O   
1423 C CB  . ILE A 187 ? 0.5020 0.3491 0.3873 -0.0005 -0.0427 -0.0728 187 ILE A CB  
1424 C CG1 . ILE A 187 ? 0.6220 0.4830 0.5279 -0.0187 -0.0472 -0.0671 187 ILE A CG1 
1425 C CG2 . ILE A 187 ? 0.5096 0.3151 0.3676 0.0000  -0.0453 -0.0853 187 ILE A CG2 
1426 C CD1 . ILE A 187 ? 0.6539 0.4915 0.5512 -0.0357 -0.0543 -0.0742 187 ILE A CD1 
1427 N N   . ASN A 188 ? 0.4581 0.3005 0.3309 0.0446  -0.0217 -0.0714 188 ASN A N   
1428 C CA  . ASN A 188 ? 0.5113 0.3641 0.3754 0.0607  -0.0143 -0.0749 188 ASN A CA  
1429 C C   . ASN A 188 ? 0.5005 0.3199 0.3379 0.0702  -0.0137 -0.0886 188 ASN A C   
1430 O O   . ASN A 188 ? 0.5528 0.3470 0.3867 0.0775  -0.0125 -0.0902 188 ASN A O   
1431 C CB  . ASN A 188 ? 0.5290 0.4032 0.4123 0.0724  -0.0056 -0.0654 188 ASN A CB  
1432 C CG  . ASN A 188 ? 0.5403 0.4483 0.4434 0.0660  -0.0046 -0.0548 188 ASN A CG  
1433 O OD1 . ASN A 188 ? 0.5934 0.5203 0.4947 0.0701  0.0001  -0.0535 188 ASN A OD1 
1434 N ND2 . ASN A 188 ? 0.5242 0.4379 0.4442 0.0558  -0.0084 -0.0472 188 ASN A ND2 
1435 N N   . ASN A 189 ? 0.5095 0.3259 0.3258 0.0701  -0.0155 -0.0987 189 ASN A N   
1436 C CA  . ASN A 189 ? 0.5501 0.3357 0.3375 0.0811  -0.0137 -0.1140 189 ASN A CA  
1437 C C   . ASN A 189 ? 0.5807 0.3846 0.3516 0.0887  -0.0085 -0.1196 189 ASN A C   
1438 O O   . ASN A 189 ? 0.6146 0.4534 0.3989 0.0881  -0.0041 -0.1093 189 ASN A O   
1439 C CB  . ASN A 189 ? 0.6409 0.3876 0.4106 0.0668  -0.0253 -0.1242 189 ASN A CB  
1440 C CG  . ASN A 189 ? 0.6777 0.4386 0.4495 0.0457  -0.0365 -0.1239 189 ASN A CG  
1441 O OD1 . ASN A 189 ? 0.6349 0.4234 0.4050 0.0460  -0.0365 -0.1224 189 ASN A OD1 
1442 N ND2 . ASN A 189 ? 0.6709 0.4139 0.4469 0.0271  -0.0460 -0.1245 189 ASN A ND2 
1443 N N   . ARG A 190 ? 0.6738 0.4515 0.4131 0.0957  -0.0085 -0.1359 190 ARG A N   
1444 C CA  . ARG A 190 ? 0.7743 0.5673 0.4929 0.1020  -0.0030 -0.1418 190 ARG A CA  
1445 C C   . ARG A 190 ? 0.7616 0.5770 0.4795 0.0865  -0.0117 -0.1357 190 ARG A C   
1446 O O   . ARG A 190 ? 0.8045 0.6463 0.5175 0.0909  -0.0052 -0.1304 190 ARG A O   
1447 C CB  . ARG A 190 ? 0.8247 0.5909 0.5205 0.1033  -0.0040 -0.1561 190 ARG A CB  
1448 C CG  . ARG A 190 ? 0.8621 0.6420 0.5356 0.1087  0.0022  -0.1626 190 ARG A CG  
1449 C CD  . ARG A 190 ? 0.9015 0.6537 0.5484 0.0993  -0.0073 -0.1777 190 ARG A CD  
1450 N NE  . ARG A 190 ? 0.9110 0.6266 0.5602 0.0971  -0.0121 -0.1846 190 ARG A NE  
1451 C CZ  . ARG A 190 ? 0.9547 0.6433 0.5915 0.0813  -0.0250 -0.1942 190 ARG A CZ  
1452 N NH1 . ARG A 190 ? 0.9400 0.6368 0.5629 0.0667  -0.0355 -0.1986 190 ARG A NH1 
1453 N NH2 . ARG A 190 ? 1.0065 0.6609 0.6457 0.0794  -0.0278 -0.1984 190 ARG A NH2 
1454 N N   . VAL A 191 ? 0.7030 0.5101 0.4280 0.0680  -0.0261 -0.1348 191 VAL A N   
1455 C CA  . VAL A 191 ? 0.6754 0.5017 0.3991 0.0539  -0.0374 -0.1311 191 VAL A CA  
1456 C C   . VAL A 191 ? 0.6128 0.4719 0.3711 0.0475  -0.0378 -0.1124 191 VAL A C   
1457 O O   . VAL A 191 ? 0.6120 0.4950 0.3705 0.0450  -0.0409 -0.1050 191 VAL A O   
1458 C CB  . VAL A 191 ? 0.7333 0.5347 0.4451 0.0370  -0.0537 -0.1431 191 VAL A CB  
1459 C CG1 . VAL A 191 ? 0.7800 0.6061 0.4967 0.0226  -0.0675 -0.1386 191 VAL A CG1 
1460 C CG2 . VAL A 191 ? 0.7734 0.5428 0.4488 0.0427  -0.0535 -0.1620 191 VAL A CG2 
1461 N N   . TYR A 192 ? 0.5338 0.3931 0.3196 0.0457  -0.0348 -0.1045 192 TYR A N   
1462 C CA  . TYR A 192 ? 0.4908 0.3774 0.3079 0.0394  -0.0356 -0.0890 192 TYR A CA  
1463 C C   . TYR A 192 ? 0.5206 0.4196 0.3551 0.0511  -0.0224 -0.0793 192 TYR A C   
1464 O O   . TYR A 192 ? 0.5275 0.4107 0.3627 0.0590  -0.0165 -0.0825 192 TYR A O   
1465 C CB  . TYR A 192 ? 0.5363 0.4157 0.3712 0.0243  -0.0443 -0.0879 192 TYR A CB  
1466 C CG  . TYR A 192 ? 0.5908 0.4582 0.4125 0.0098  -0.0581 -0.0986 192 TYR A CG  
1467 C CD1 . TYR A 192 ? 0.6271 0.4668 0.4464 -0.0012 -0.0628 -0.1058 192 TYR A CD1 
1468 C CD2 . TYR A 192 ? 0.6493 0.5329 0.4609 0.0060  -0.0672 -0.1006 192 TYR A CD2 
1469 C CE1 . TYR A 192 ? 0.7159 0.5457 0.5253 -0.0174 -0.0761 -0.1160 192 TYR A CE1 
1470 C CE2 . TYR A 192 ? 0.7151 0.5910 0.5163 -0.0085 -0.0819 -0.1111 192 TYR A CE2 
1471 C CZ  . TYR A 192 ? 0.7365 0.5862 0.5379 -0.0211 -0.0861 -0.1192 192 TYR A CZ  
1472 O OH  . TYR A 192 ? 0.7968 0.6396 0.5896 -0.0381 -0.1011 -0.1301 192 TYR A OH  
1473 N N   . ARG A 193 ? 0.4693 0.3957 0.3181 0.0519  -0.0190 -0.0673 193 ARG A N   
1474 C CA  . ARG A 193 ? 0.4880 0.4295 0.3535 0.0606  -0.0074 -0.0583 193 ARG A CA  
1475 C C   . ARG A 193 ? 0.4493 0.4111 0.3397 0.0537  -0.0094 -0.0453 193 ARG A C   
1476 O O   . ARG A 193 ? 0.4357 0.4088 0.3245 0.0489  -0.0145 -0.0403 193 ARG A O   
1477 C CB  . ARG A 193 ? 0.5812 0.5334 0.4317 0.0712  0.0032  -0.0586 193 ARG A CB  
1478 N N   . THR A 194 ? 0.3176 0.2828 0.2291 0.0545  -0.0059 -0.0400 194 THR A N   
1479 C CA  . THR A 194 ? 0.3023 0.2852 0.2358 0.0505  -0.0054 -0.0290 194 THR A CA  
1480 C C   . THR A 194 ? 0.2950 0.2892 0.2397 0.0579  0.0045  -0.0240 194 THR A C   
1481 O O   . THR A 194 ? 0.3219 0.3124 0.2607 0.0669  0.0106  -0.0289 194 THR A O   
1482 C CB  . THR A 194 ? 0.3810 0.3603 0.3301 0.0423  -0.0115 -0.0276 194 THR A CB  
1483 O OG1 . THR A 194 ? 0.3803 0.3468 0.3319 0.0455  -0.0086 -0.0300 194 THR A OG1 
1484 C CG2 . THR A 194 ? 0.3804 0.3528 0.3219 0.0334  -0.0213 -0.0331 194 THR A CG2 
1485 N N   . ILE A 195 ? 0.2616 0.2701 0.2233 0.0542  0.0056  -0.0149 195 ILE A N   
1486 C CA  . ILE A 195 ? 0.2819 0.3041 0.2564 0.0583  0.0138  -0.0102 195 ILE A CA  
1487 C C   . ILE A 195 ? 0.2930 0.3113 0.2783 0.0623  0.0136  -0.0127 195 ILE A C   
1488 O O   . ILE A 195 ? 0.3032 0.3317 0.2958 0.0694  0.0194  -0.0125 195 ILE A O   
1489 C CB  . ILE A 195 ? 0.2536 0.2874 0.2406 0.0518  0.0139  -0.0006 195 ILE A CB  
1490 C CG1 . ILE A 195 ? 0.2854 0.3352 0.2854 0.0530  0.0221  0.0039  195 ILE A CG1 
1491 C CG2 . ILE A 195 ? 0.2538 0.2835 0.2536 0.0462  0.0069  0.0009  195 ILE A CG2 
1492 C CD1 . ILE A 195 ? 0.2784 0.3393 0.2690 0.0575  0.0319  0.0043  195 ILE A CD1 
1493 N N   A GLY A 196 ? 0.2804 0.2851 0.2663 0.0579  0.0069  -0.0145 196 GLY A N   
1494 N N   B GLY A 196 ? 0.2822 0.2874 0.2688 0.0579  0.0070  -0.0143 196 GLY A N   
1495 C CA  A GLY A 196 ? 0.2842 0.2811 0.2764 0.0602  0.0054  -0.0149 196 GLY A CA  
1496 C CA  B GLY A 196 ? 0.2823 0.2794 0.2733 0.0623  0.0064  -0.0156 196 GLY A CA  
1497 C C   A GLY A 196 ? 0.2830 0.2932 0.2925 0.0570  0.0053  -0.0085 196 GLY A C   
1498 C C   B GLY A 196 ? 0.2741 0.2868 0.2823 0.0640  0.0084  -0.0101 196 GLY A C   
1499 O O   A GLY A 196 ? 0.2271 0.2313 0.2403 0.0523  0.0017  -0.0071 196 GLY A O   
1500 O O   B GLY A 196 ? 0.3422 0.3516 0.3529 0.0708  0.0079  -0.0107 196 GLY A O   
1501 N N   . SER A 197 ? 0.2897 0.3178 0.3087 0.0582  0.0097  -0.0049 197 SER A N   
1502 C CA  . SER A 197 ? 0.2448 0.2849 0.2793 0.0554  0.0092  -0.0006 197 SER A CA  
1503 C C   . SER A 197 ? 0.2085 0.2462 0.2468 0.0464  0.0058  0.0022  197 SER A C   
1504 O O   . SER A 197 ? 0.2211 0.2562 0.2544 0.0431  0.0051  0.0031  197 SER A O   
1505 C CB  . SER A 197 ? 0.1674 0.2279 0.2122 0.0565  0.0150  0.0023  197 SER A CB  
1506 O OG  . SER A 197 ? 0.2070 0.2733 0.2494 0.0668  0.0196  -0.0011 197 SER A OG  
1507 N N   . PRO A 198 ? 0.1929 0.2321 0.2392 0.0435  0.0032  0.0034  198 PRO A N   
1508 C CA  . PRO A 198 ? 0.2307 0.2699 0.2819 0.0370  0.0015  0.0052  198 PRO A CA  
1509 C C   . PRO A 198 ? 0.2113 0.2572 0.2670 0.0341  0.0040  0.0090  198 PRO A C   
1510 O O   . PRO A 198 ? 0.2117 0.2680 0.2720 0.0346  0.0075  0.0107  198 PRO A O   
1511 C CB  . PRO A 198 ? 0.2427 0.2834 0.2992 0.0357  -0.0008 0.0046  198 PRO A CB  
1512 C CG  . PRO A 198 ? 0.2143 0.2525 0.2662 0.0415  -0.0018 0.0035  198 PRO A CG  
1513 C CD  . PRO A 198 ? 0.2082 0.2498 0.2583 0.0473  0.0014  0.0030  198 PRO A CD  
1514 N N   . LEU A 199 ? 0.1756 0.2162 0.2306 0.0311  0.0024  0.0108  199 LEU A N   
1515 C CA  . LEU A 199 ? 0.1887 0.2292 0.2448 0.0279  0.0040  0.0160  199 LEU A CA  
1516 C C   . LEU A 199 ? 0.2207 0.2548 0.2832 0.0244  0.0015  0.0160  199 LEU A C   
1517 O O   . LEU A 199 ? 0.2574 0.2865 0.3201 0.0265  -0.0014 0.0129  199 LEU A O   
1518 C CB  . LEU A 199 ? 0.1966 0.2324 0.2426 0.0298  0.0029  0.0189  199 LEU A CB  
1519 C CG  . LEU A 199 ? 0.2031 0.2414 0.2384 0.0335  0.0043  0.0166  199 LEU A CG  
1520 C CD1 . LEU A 199 ? 0.2263 0.2604 0.2496 0.0345  0.0015  0.0199  199 LEU A CD1 
1521 C CD2 . LEU A 199 ? 0.2347 0.2825 0.2703 0.0343  0.0112  0.0176  199 LEU A CD2 
1522 N N   . VAL A 200 ? 0.1980 0.2323 0.2655 0.0188  0.0030  0.0189  200 VAL A N   
1523 C CA  . VAL A 200 ? 0.2295 0.2531 0.3004 0.0151  0.0004  0.0176  200 VAL A CA  
1524 C C   . VAL A 200 ? 0.2510 0.2617 0.3177 0.0123  0.0010  0.0245  200 VAL A C   
1525 O O   . VAL A 200 ? 0.2297 0.2436 0.2956 0.0066  0.0048  0.0307  200 VAL A O   
1526 C CB  . VAL A 200 ? 0.2309 0.2611 0.3099 0.0087  -0.0003 0.0145  200 VAL A CB  
1527 C CG1 . VAL A 200 ? 0.2269 0.2418 0.3064 0.0036  -0.0032 0.0121  200 VAL A CG1 
1528 C CG2 . VAL A 200 ? 0.2458 0.2848 0.3256 0.0130  -0.0023 0.0089  200 VAL A CG2 
1529 N N   . PHE A 201 ? 0.2439 0.2402 0.3074 0.0171  -0.0024 0.0240  201 PHE A N   
1530 C CA  . PHE A 201 ? 0.2676 0.2469 0.3246 0.0181  -0.0038 0.0311  201 PHE A CA  
1531 C C   . PHE A 201 ? 0.3251 0.2843 0.3833 0.0152  -0.0057 0.0290  201 PHE A C   
1532 O O   . PHE A 201 ? 0.2983 0.2563 0.3606 0.0181  -0.0074 0.0201  201 PHE A O   
1533 C CB  . PHE A 201 ? 0.2212 0.2003 0.2744 0.0289  -0.0077 0.0316  201 PHE A CB  
1534 C CG  . PHE A 201 ? 0.2566 0.2510 0.3057 0.0307  -0.0072 0.0325  201 PHE A CG  
1535 C CD1 . PHE A 201 ? 0.2335 0.2409 0.2874 0.0328  -0.0075 0.0253  201 PHE A CD1 
1536 C CD2 . PHE A 201 ? 0.2793 0.2725 0.3170 0.0296  -0.0060 0.0406  201 PHE A CD2 
1537 C CE1 . PHE A 201 ? 0.2531 0.2699 0.3014 0.0338  -0.0075 0.0248  201 PHE A CE1 
1538 C CE2 . PHE A 201 ? 0.2741 0.2790 0.3051 0.0316  -0.0057 0.0396  201 PHE A CE2 
1539 C CZ  . PHE A 201 ? 0.2658 0.2813 0.3023 0.0336  -0.0069 0.0312  201 PHE A CZ  
1540 N N   . PRO A 202 ? 0.3417 0.2828 0.3942 0.0091  -0.0052 0.0369  202 PRO A N   
1541 C CA  . PRO A 202 ? 0.3276 0.2427 0.3785 0.0063  -0.0078 0.0345  202 PRO A CA  
1542 C C   . PRO A 202 ? 0.3631 0.2588 0.4081 0.0202  -0.0122 0.0350  202 PRO A C   
1543 O O   . PRO A 202 ? 0.3268 0.2319 0.3704 0.0308  -0.0140 0.0382  202 PRO A O   
1544 C CB  . PRO A 202 ? 0.3854 0.2887 0.4322 -0.0080 -0.0049 0.0446  202 PRO A CB  
1545 C CG  . PRO A 202 ? 0.3540 0.2679 0.3936 -0.0053 -0.0018 0.0552  202 PRO A CG  
1546 C CD  . PRO A 202 ? 0.3159 0.2578 0.3611 0.0031  -0.0014 0.0486  202 PRO A CD  
1547 N N   . LYS A 203 ? 0.3810 0.2500 0.4233 0.0207  -0.0146 0.0307  203 LYS A N   
1548 C CA  . LYS A 203 ? 0.4640 0.3094 0.5001 0.0351  -0.0188 0.0324  203 LYS A CA  
1549 C C   . LYS A 203 ? 0.4720 0.3092 0.4983 0.0375  -0.0205 0.0477  203 LYS A C   
1550 O O   . LYS A 203 ? 0.4632 0.2977 0.4832 0.0243  -0.0173 0.0575  203 LYS A O   
1551 C CB  . LYS A 203 ? 0.5257 0.3339 0.5553 0.0326  -0.0208 0.0281  203 LYS A CB  
1552 C CG  . LYS A 203 ? 0.5820 0.3904 0.6157 0.0333  -0.0204 0.0120  203 LYS A CG  
1553 C CD  A LYS A 203 ? 0.6096 0.3758 0.6336 0.0385  -0.0235 0.0067  203 LYS A CD  
1554 C CD  B LYS A 203 ? 0.6121 0.3771 0.6355 0.0315  -0.0233 0.0076  203 LYS A CD  
1555 C CE  A LYS A 203 ? 0.6131 0.3709 0.6365 0.0622  -0.0259 0.0065  203 LYS A CE  
1556 C CE  B LYS A 203 ? 0.5894 0.3344 0.6070 0.0103  -0.0234 0.0168  203 LYS A CE  
1557 N NZ  A LYS A 203 ? 0.5848 0.3661 0.6171 0.0747  -0.0232 -0.0080 203 LYS A NZ  
1558 N NZ  B LYS A 203 ? 0.5029 0.2703 0.5288 -0.0084 -0.0217 0.0110  203 LYS A NZ  
1559 N N   . HIS A 204 ? 0.4678 0.3019 0.4924 0.0548  -0.0256 0.0499  204 HIS A N   
1560 C CA  . HIS A 204 ? 0.5027 0.3246 0.5149 0.0616  -0.0301 0.0643  204 HIS A CA  
1561 C C   . HIS A 204 ? 0.5189 0.3696 0.5287 0.0585  -0.0291 0.0705  204 HIS A C   
1562 O O   . HIS A 204 ? 0.5772 0.4233 0.5755 0.0657  -0.0341 0.0812  204 HIS A O   
1563 C CB  . HIS A 204 ? 0.4903 0.2730 0.4860 0.0520  -0.0297 0.0765  204 HIS A CB  
1564 C CG  . HIS A 204 ? 0.5134 0.2611 0.5080 0.0527  -0.0311 0.0698  204 HIS A CG  
1565 N ND1 . HIS A 204 ? 0.5524 0.2819 0.5473 0.0728  -0.0369 0.0648  204 HIS A ND1 
1566 C CD2 . HIS A 204 ? 0.5421 0.2700 0.5353 0.0361  -0.0278 0.0660  204 HIS A CD2 
1567 C CE1 . HIS A 204 ? 0.5542 0.2504 0.5452 0.0692  -0.0366 0.0576  204 HIS A CE1 
1568 N NE2 . HIS A 204 ? 0.5669 0.2611 0.5565 0.0459  -0.0317 0.0583  204 HIS A NE2 
1569 N N   . HIS A 205 ? 0.4262 0.3043 0.4444 0.0492  -0.0236 0.0639  205 HIS A N   
1570 C CA  . HIS A 205 ? 0.3699 0.2738 0.3857 0.0497  -0.0236 0.0663  205 HIS A CA  
1571 C C   . HIS A 205 ? 0.3973 0.3205 0.4233 0.0630  -0.0294 0.0588  205 HIS A C   
1572 O O   . HIS A 205 ? 0.3471 0.2770 0.3868 0.0671  -0.0289 0.0483  205 HIS A O   
1573 C CB  . HIS A 205 ? 0.3070 0.2309 0.3279 0.0371  -0.0159 0.0617  205 HIS A CB  
1574 C CG  . HIS A 205 ? 0.3301 0.2472 0.3419 0.0240  -0.0096 0.0711  205 HIS A CG  
1575 N ND1 . HIS A 205 ? 0.3579 0.2963 0.3701 0.0164  -0.0029 0.0709  205 HIS A ND1 
1576 C CD2 . HIS A 205 ? 0.3908 0.2825 0.3933 0.0167  -0.0081 0.0811  205 HIS A CD2 
1577 C CE1 . HIS A 205 ? 0.3987 0.3299 0.4044 0.0049  0.0033  0.0802  205 HIS A CE1 
1578 N NE2 . HIS A 205 ? 0.3894 0.2914 0.3886 0.0034  0.0002  0.0871  205 HIS A NE2 
1579 N N   . VAL A 206 ? 0.3319 0.2658 0.3507 0.0686  -0.0348 0.0642  206 VAL A N   
1580 C CA  . VAL A 206 ? 0.3559 0.3112 0.3856 0.0792  -0.0416 0.0582  206 VAL A CA  
1581 C C   . VAL A 206 ? 0.3530 0.3315 0.3810 0.0725  -0.0406 0.0546  206 VAL A C   
1582 O O   . VAL A 206 ? 0.3612 0.3379 0.3725 0.0682  -0.0404 0.0613  206 VAL A O   
1583 C CB  . VAL A 206 ? 0.4597 0.4075 0.4833 0.0934  -0.0522 0.0666  206 VAL A CB  
1584 C CG1 . VAL A 206 ? 0.4726 0.4503 0.5095 0.1016  -0.0600 0.0605  206 VAL A CG1 
1585 C CG2 . VAL A 206 ? 0.4711 0.3934 0.4977 0.1032  -0.0537 0.0680  206 VAL A CG2 
1586 N N   . VAL A 207 ? 0.2725 0.2711 0.3158 0.0717  -0.0396 0.0439  207 VAL A N   
1587 C CA  . VAL A 207 ? 0.3038 0.3201 0.3455 0.0655  -0.0395 0.0391  207 VAL A CA  
1588 C C   . VAL A 207 ? 0.2999 0.3356 0.3518 0.0720  -0.0485 0.0355  207 VAL A C   
1589 O O   . VAL A 207 ? 0.2916 0.3380 0.3619 0.0765  -0.0487 0.0299  207 VAL A O   
1590 C CB  . VAL A 207 ? 0.3299 0.3516 0.3794 0.0572  -0.0313 0.0309  207 VAL A CB  
1591 C CG1 . VAL A 207 ? 0.3474 0.3823 0.3941 0.0520  -0.0319 0.0258  207 VAL A CG1 
1592 C CG2 . VAL A 207 ? 0.3145 0.3223 0.3571 0.0509  -0.0239 0.0344  207 VAL A CG2 
1593 N N   . SER A 208 ? 0.2369 0.2789 0.2771 0.0721  -0.0558 0.0383  208 SER A N   
1594 C CA  . SER A 208 ? 0.2566 0.3195 0.3061 0.0770  -0.0670 0.0354  208 SER A CA  
1595 C C   . SER A 208 ? 0.3441 0.4201 0.3912 0.0665  -0.0680 0.0276  208 SER A C   
1596 O O   . SER A 208 ? 0.3414 0.4076 0.3681 0.0610  -0.0658 0.0283  208 SER A O   
1597 C CB  . SER A 208 ? 0.3320 0.3897 0.3670 0.0865  -0.0781 0.0454  208 SER A CB  
1598 O OG  . SER A 208 ? 0.3823 0.4635 0.4239 0.0893  -0.0907 0.0422  208 SER A OG  
1599 N N   . LEU A 209 ? 0.3077 0.4049 0.3748 0.0636  -0.0707 0.0198  209 LEU A N   
1600 C CA  . LEU A 209 ? 0.2822 0.3895 0.3474 0.0525  -0.0735 0.0121  209 LEU A CA  
1601 C C   . LEU A 209 ? 0.2808 0.4087 0.3506 0.0549  -0.0885 0.0113  209 LEU A C   
1602 O O   . LEU A 209 ? 0.2961 0.4441 0.3878 0.0622  -0.0939 0.0119  209 LEU A O   
1603 C CB  . LEU A 209 ? 0.2396 0.3555 0.3226 0.0438  -0.0659 0.0046  209 LEU A CB  
1604 C CG  . LEU A 209 ? 0.2716 0.3711 0.3528 0.0424  -0.0528 0.0050  209 LEU A CG  
1605 C CD1 . LEU A 209 ? 0.2871 0.3946 0.3814 0.0334  -0.0465 -0.0012 209 LEU A CD1 
1606 C CD2 . LEU A 209 ? 0.2449 0.3231 0.3030 0.0401  -0.0484 0.0071  209 LEU A CD2 
1607 N N   . GLN A 210 ? 0.2676 0.3921 0.3172 0.0495  -0.0956 0.0092  210 GLN A N   
1608 C CA  . GLN A 210 ? 0.3063 0.4501 0.3567 0.0512  -0.1121 0.0082  210 GLN A CA  
1609 C C   . GLN A 210 ? 0.3419 0.4932 0.3901 0.0362  -0.1171 -0.0028 210 GLN A C   
1610 O O   . GLN A 210 ? 0.3806 0.5112 0.4055 0.0292  -0.1121 -0.0069 210 GLN A O   
1611 C CB  . GLN A 210 ? 0.3733 0.5035 0.3946 0.0603  -0.1192 0.0172  210 GLN A CB  
1612 C CG  . GLN A 210 ? 0.4214 0.5407 0.4450 0.0741  -0.1156 0.0290  210 GLN A CG  
1613 C CD  . GLN A 210 ? 0.4285 0.5266 0.4198 0.0804  -0.1177 0.0403  210 GLN A CD  
1614 O OE1 . GLN A 210 ? 0.3916 0.4896 0.3591 0.0783  -0.1260 0.0403  210 GLN A OE1 
1615 N NE2 . GLN A 210 ? 0.4682 0.5470 0.4568 0.0873  -0.1099 0.0501  210 GLN A NE2 
1616 N N   . PRO A 211 ? 0.3628 0.5430 0.4353 0.0306  -0.1265 -0.0084 211 PRO A N   
1617 C CA  . PRO A 211 ? 0.3770 0.5612 0.4483 0.0130  -0.1309 -0.0193 211 PRO A CA  
1618 C C   . PRO A 211 ? 0.3808 0.5544 0.4206 0.0105  -0.1429 -0.0230 211 PRO A C   
1619 O O   . PRO A 211 ? 0.3662 0.5438 0.3928 0.0215  -0.1533 -0.0169 211 PRO A O   
1620 C CB  . PRO A 211 ? 0.4343 0.6581 0.5422 0.0083  -0.1391 -0.0226 211 PRO A CB  
1621 C CG  . PRO A 211 ? 0.4459 0.6873 0.5663 0.0276  -0.1455 -0.0138 211 PRO A CG  
1622 C CD  . PRO A 211 ? 0.3955 0.6068 0.4986 0.0401  -0.1334 -0.0051 211 PRO A CD  
1623 N N   . VAL A 212 ? 0.3751 0.5329 0.4005 -0.0037 -0.1414 -0.0330 212 VAL A N   
1624 C CA  . VAL A 212 ? 0.3778 0.5220 0.3700 -0.0075 -0.1516 -0.0398 212 VAL A CA  
1625 C C   . VAL A 212 ? 0.4248 0.5902 0.4268 -0.0221 -0.1688 -0.0501 212 VAL A C   
1626 O O   . VAL A 212 ? 0.3981 0.5734 0.3854 -0.0202 -0.1854 -0.0521 212 VAL A O   
1627 C CB  . VAL A 212 ? 0.3551 0.4630 0.3206 -0.0112 -0.1384 -0.0454 212 VAL A CB  
1628 C CG1 . VAL A 212 ? 0.4111 0.5033 0.3403 -0.0149 -0.1475 -0.0550 212 VAL A CG1 
1629 C CG2 . VAL A 212 ? 0.3226 0.4161 0.2807 0.0025  -0.1231 -0.0350 212 VAL A CG2 
1630 N N   . ASN A 213 ? 0.4473 0.6209 0.4742 -0.0377 -0.1656 -0.0562 213 ASN A N   
1631 C CA  . ASN A 213 ? 0.5380 0.7353 0.5806 -0.0552 -0.1810 -0.0658 213 ASN A CA  
1632 C C   . ASN A 213 ? 0.5471 0.7832 0.6370 -0.0602 -0.1792 -0.0624 213 ASN A C   
1633 O O   . ASN A 213 ? 0.5770 0.8403 0.6867 -0.0512 -0.1865 -0.0548 213 ASN A O   
1634 C CB  . ASN A 213 ? 0.5966 0.7631 0.6195 -0.0743 -0.1795 -0.0785 213 ASN A CB  
1635 C CG  . ASN A 213 ? 0.6708 0.8127 0.6505 -0.0730 -0.1895 -0.0870 213 ASN A CG  
1636 O OD1 . ASN A 213 ? 0.7039 0.8614 0.6781 -0.0792 -0.2068 -0.0919 213 ASN A OD1 
1637 N ND2 . ASN A 213 ? 0.7066 0.8103 0.6547 -0.0645 -0.1766 -0.0875 213 ASN A ND2 
1638 N N   . ASP A 214 ? 0.5145 0.7430 0.6188 -0.0732 -0.1655 -0.0641 214 ASP A N   
1639 C CA  . ASP A 214 ? 0.5238 0.7878 0.6707 -0.0776 -0.1598 -0.0603 214 ASP A CA  
1640 C C   . ASP A 214 ? 0.4270 0.7065 0.5885 -0.0544 -0.1527 -0.0497 214 ASP A C   
1641 O O   . ASP A 214 ? 0.4298 0.6805 0.5695 -0.0402 -0.1434 -0.0440 214 ASP A O   
1642 C CB  . ASP A 214 ? 0.5717 0.8192 0.7238 -0.0951 -0.1447 -0.0626 214 ASP A CB  
1643 C CG  . ASP A 214 ? 0.6238 0.9050 0.8165 -0.1008 -0.1360 -0.0582 214 ASP A CG  
1644 O OD1 . ASP A 214 ? 0.6632 0.9763 0.8805 -0.0928 -0.1424 -0.0545 214 ASP A OD1 
1645 O OD2 . ASP A 214 ? 0.6689 0.9407 0.8662 -0.1121 -0.1216 -0.0573 214 ASP A OD2 
1646 N N   . LYS A 215 ? 0.4068 0.7175 0.6004 -0.0493 -0.1533 -0.0441 215 LYS A N   
1647 C CA  . LYS A 215 ? 0.3712 0.6926 0.5776 -0.0269 -0.1471 -0.0348 215 LYS A CA  
1648 C C   . LYS A 215 ? 0.3211 0.6601 0.5580 -0.0280 -0.1311 -0.0329 215 LYS A C   
1649 O O   . LYS A 215 ? 0.2929 0.6414 0.5430 -0.0101 -0.1257 -0.0266 215 LYS A O   
1650 C CB  . LYS A 215 ? 0.3859 0.7252 0.5989 -0.0144 -0.1618 -0.0293 215 LYS A CB  
1651 C CG  . LYS A 215 ? 0.4492 0.7698 0.6272 -0.0109 -0.1767 -0.0292 215 LYS A CG  
1652 C CD  . LYS A 215 ? 0.5456 0.8839 0.7296 0.0011  -0.1917 -0.0223 215 LYS A CD  
1653 C CE  . LYS A 215 ? 0.5727 0.9086 0.7609 0.0250  -0.1861 -0.0110 215 LYS A CE  
1654 N NZ  . LYS A 215 ? 0.6337 0.9906 0.8352 0.0364  -0.1997 -0.0043 215 LYS A NZ  
1655 N N   . ASP A 216 ? 0.3041 0.6446 0.5497 -0.0485 -0.1229 -0.0379 216 ASP A N   
1656 C CA  . ASP A 216 ? 0.2579 0.6131 0.5274 -0.0511 -0.1061 -0.0358 216 ASP A CA  
1657 C C   . ASP A 216 ? 0.2548 0.5842 0.5074 -0.0543 -0.0919 -0.0362 216 ASP A C   
1658 O O   . ASP A 216 ? 0.2979 0.5974 0.5262 -0.0672 -0.0927 -0.0396 216 ASP A O   
1659 C CB  . ASP A 216 ? 0.2189 0.5938 0.5100 -0.0727 -0.1053 -0.0392 216 ASP A CB  
1660 C CG  . ASP A 216 ? 0.2930 0.6977 0.6051 -0.0705 -0.1199 -0.0395 216 ASP A CG  
1661 O OD1 . ASP A 216 ? 0.3355 0.7456 0.6454 -0.0510 -0.1299 -0.0359 216 ASP A OD1 
1662 O OD2 . ASP A 216 ? 0.3402 0.7623 0.6708 -0.0887 -0.1216 -0.0429 216 ASP A OD2 
1663 N N   . PHE A 217 ? 0.2958 0.5286 0.4793 -0.0142 -0.0998 -0.0877 217 PHE A N   
1664 C CA  . PHE A 217 ? 0.2489 0.4501 0.4167 -0.0170 -0.0852 -0.0822 217 PHE A CA  
1665 C C   . PHE A 217 ? 0.2928 0.5032 0.4812 -0.0234 -0.0711 -0.0760 217 PHE A C   
1666 O O   . PHE A 217 ? 0.2271 0.4656 0.4361 -0.0176 -0.0692 -0.0732 217 PHE A O   
1667 C CB  . PHE A 217 ? 0.2860 0.4681 0.4270 0.0002  -0.0802 -0.0753 217 PHE A CB  
1668 C CG  . PHE A 217 ? 0.2978 0.4728 0.4157 0.0086  -0.0920 -0.0796 217 PHE A CG  
1669 C CD1 . PHE A 217 ? 0.2809 0.4293 0.3757 0.0054  -0.0922 -0.0839 217 PHE A CD1 
1670 C CD2 . PHE A 217 ? 0.3247 0.5204 0.4429 0.0209  -0.1029 -0.0796 217 PHE A CD2 
1671 C CE1 . PHE A 217 ? 0.2911 0.4344 0.3625 0.0142  -0.1021 -0.0885 217 PHE A CE1 
1672 C CE2 . PHE A 217 ? 0.3320 0.5220 0.4258 0.0293  -0.1136 -0.0833 217 PHE A CE2 
1673 C CZ  . PHE A 217 ? 0.3390 0.5033 0.4091 0.0258  -0.1127 -0.0880 217 PHE A CZ  
1674 N N   . GLN A 218 ? 0.2319 0.4181 0.4126 -0.0334 -0.0609 -0.0736 218 GLN A N   
1675 C CA  . GLN A 218 ? 0.2456 0.4348 0.4378 -0.0378 -0.0459 -0.0669 218 GLN A CA  
1676 C C   . GLN A 218 ? 0.2871 0.4566 0.4589 -0.0237 -0.0363 -0.0603 218 GLN A C   
1677 O O   . GLN A 218 ? 0.2674 0.4084 0.4165 -0.0229 -0.0347 -0.0597 218 GLN A O   
1678 C CB  . GLN A 218 ? 0.3328 0.5062 0.5267 -0.0567 -0.0413 -0.0672 218 GLN A CB  
1679 C CG  . GLN A 218 ? 0.3349 0.5180 0.5433 -0.0637 -0.0265 -0.0602 218 GLN A CG  
1680 C CD  . GLN A 218 ? 0.3601 0.5819 0.6018 -0.0729 -0.0275 -0.0613 218 GLN A CD  
1681 O OE1 . GLN A 218 ? 0.3477 0.5832 0.6026 -0.0812 -0.0400 -0.0678 218 GLN A OE1 
1682 N NE2 . GLN A 218 ? 0.3861 0.6278 0.6419 -0.0711 -0.0146 -0.0556 218 GLN A NE2 
1683 N N   . ILE A 219 ? 0.2035 0.3883 0.3836 -0.0119 -0.0309 -0.0561 219 ILE A N   
1684 C CA  . ILE A 219 ? 0.1983 0.3645 0.3609 0.0010  -0.0233 -0.0505 219 ILE A CA  
1685 C C   . ILE A 219 ? 0.1908 0.3577 0.3605 -0.0016 -0.0093 -0.0470 219 ILE A C   
1686 O O   . ILE A 219 ? 0.2306 0.4235 0.4217 -0.0021 -0.0056 -0.0473 219 ILE A O   
1687 C CB  . ILE A 219 ? 0.2792 0.4552 0.4409 0.0185  -0.0287 -0.0484 219 ILE A CB  
1688 C CG1 . ILE A 219 ? 0.2666 0.4434 0.4186 0.0212  -0.0429 -0.0517 219 ILE A CG1 
1689 C CG2 . ILE A 219 ? 0.2885 0.4413 0.4325 0.0291  -0.0207 -0.0424 219 ILE A CG2 
1690 C CD1 . ILE A 219 ? 0.2943 0.4828 0.4452 0.0381  -0.0502 -0.0488 219 ILE A CD1 
1691 N N   . SER A 220 ? 0.1887 0.3295 0.3404 -0.0031 -0.0019 -0.0442 220 SER A N   
1692 C CA  . SER A 220 ? 0.2534 0.3922 0.4066 -0.0044 0.0107  -0.0413 220 SER A CA  
1693 C C   . SER A 220 ? 0.3240 0.4494 0.4647 0.0096  0.0147  -0.0390 220 SER A C   
1694 O O   . SER A 220 ? 0.3443 0.4520 0.4692 0.0151  0.0102  -0.0376 220 SER A O   
1695 C CB  . SER A 220 ? 0.2413 0.3605 0.3835 -0.0167 0.0155  -0.0400 220 SER A CB  
1696 O OG  . SER A 220 ? 0.3316 0.4247 0.4518 -0.0111 0.0152  -0.0386 220 SER A OG  
1697 N N   . VAL A 221 ? 0.2374 0.3717 0.3853 0.0152  0.0231  -0.0387 221 VAL A N   
1698 C CA  . VAL A 221 ? 0.2181 0.3356 0.3536 0.0261  0.0277  -0.0375 221 VAL A CA  
1699 C C   . VAL A 221 ? 0.2674 0.3830 0.4008 0.0215  0.0387  -0.0381 221 VAL A C   
1700 O O   . VAL A 221 ? 0.2517 0.3892 0.3993 0.0218  0.0448  -0.0396 221 VAL A O   
1701 C CB  . VAL A 221 ? 0.2981 0.4264 0.4422 0.0417  0.0257  -0.0382 221 VAL A CB  
1702 C CG1 . VAL A 221 ? 0.3300 0.4370 0.4613 0.0511  0.0309  -0.0380 221 VAL A CG1 
1703 C CG2 . VAL A 221 ? 0.3368 0.4667 0.4802 0.0475  0.0142  -0.0364 221 VAL A CG2 
1704 N N   . ASP A 222 ? 0.2281 0.3203 0.3437 0.0174  0.0413  -0.0368 222 ASP A N   
1705 C CA  . ASP A 222 ? 0.2795 0.3689 0.3894 0.0129  0.0506  -0.0370 222 ASP A CA  
1706 C C   . ASP A 222 ? 0.2939 0.4018 0.4160 0.0014  0.0544  -0.0353 222 ASP A C   
1707 O O   . ASP A 222 ? 0.2867 0.3934 0.4115 -0.0082 0.0487  -0.0338 222 ASP A O   
1708 C CB  . ASP A 222 ? 0.2278 0.3190 0.3373 0.0248  0.0564  -0.0404 222 ASP A CB  
1709 C CG  . ASP A 222 ? 0.2217 0.2890 0.3179 0.0328  0.0525  -0.0412 222 ASP A CG  
1710 O OD1 . ASP A 222 ? 0.2749 0.3253 0.3601 0.0274  0.0483  -0.0386 222 ASP A OD1 
1711 O OD2 . ASP A 222 ? 0.2974 0.3625 0.3945 0.0442  0.0539  -0.0444 222 ASP A OD2 
1712 N N   . HIS A 223 ? 0.2710 0.3968 0.4012 0.0016  0.0637  -0.0357 223 HIS A N   
1713 C CA  A HIS A 223 ? 0.3810 0.5236 0.5220 -0.0115 0.0692  -0.0322 223 HIS A CA  
1714 C CA  B HIS A 223 ? 0.3811 0.5237 0.5220 -0.0114 0.0692  -0.0322 223 HIS A CA  
1715 C C   . HIS A 223 ? 0.4123 0.5812 0.5777 -0.0162 0.0644  -0.0328 223 HIS A C   
1716 O O   . HIS A 223 ? 0.4869 0.6676 0.6631 -0.0304 0.0669  -0.0295 223 HIS A O   
1717 C CB  A HIS A 223 ? 0.4341 0.5902 0.5745 -0.0087 0.0822  -0.0320 223 HIS A CB  
1718 C CB  B HIS A 223 ? 0.4347 0.5908 0.5750 -0.0087 0.0822  -0.0320 223 HIS A CB  
1719 C CG  A HIS A 223 ? 0.4751 0.6456 0.6226 0.0077  0.0850  -0.0377 223 HIS A CG  
1720 C CG  B HIS A 223 ? 0.4764 0.6462 0.6233 0.0079  0.0851  -0.0378 223 HIS A CG  
1721 N ND1 A HIS A 223 ? 0.4852 0.6352 0.6196 0.0207  0.0812  -0.0421 223 HIS A ND1 
1722 N ND1 B HIS A 223 ? 0.4808 0.6303 0.6155 0.0207  0.0803  -0.0421 223 HIS A ND1 
1723 C CD2 A HIS A 223 ? 0.4909 0.6934 0.6577 0.0138  0.0912  -0.0399 223 HIS A CD2 
1724 C CD2 B HIS A 223 ? 0.4940 0.6949 0.6585 0.0142  0.0923  -0.0400 223 HIS A CD2 
1725 C CE1 A HIS A 223 ? 0.4939 0.6590 0.6374 0.0347  0.0843  -0.0470 223 HIS A CE1 
1726 C CE1 B HIS A 223 ? 0.4960 0.6600 0.6392 0.0347  0.0837  -0.0470 223 HIS A CE1 
1727 N NE2 A HIS A 223 ? 0.4952 0.6938 0.6586 0.0318  0.0906  -0.0461 223 HIS A NE2 
1728 N NE2 B HIS A 223 ? 0.5005 0.6971 0.6618 0.0321  0.0911  -0.0463 223 HIS A NE2 
1729 N N   . LEU A 224 ? 0.2981 0.4763 0.4727 -0.0052 0.0570  -0.0365 224 LEU A N   
1730 C CA  . LEU A 224 ? 0.2389 0.4485 0.4391 -0.0068 0.0524  -0.0380 224 LEU A CA  
1731 C C   . LEU A 224 ? 0.3121 0.5142 0.5123 -0.0118 0.0384  -0.0392 224 LEU A C   
1732 O O   . LEU A 224 ? 0.3327 0.5120 0.5160 -0.0044 0.0317  -0.0398 224 LEU A O   
1733 C CB  . LEU A 224 ? 0.2469 0.4753 0.4578 0.0115  0.0530  -0.0415 224 LEU A CB  
1734 C CG  . LEU A 224 ? 0.2884 0.5544 0.5277 0.0139  0.0475  -0.0436 224 LEU A CG  
1735 C CD1 . LEU A 224 ? 0.2529 0.5508 0.5148 -0.0009 0.0553  -0.0420 224 LEU A CD1 
1736 C CD2 . LEU A 224 ? 0.2751 0.5532 0.5205 0.0357  0.0480  -0.0468 224 LEU A CD2 
1737 N N   . SER A 225 ? 0.2986 0.5211 0.5178 -0.0244 0.0342  -0.0398 225 SER A N   
1738 C CA  . SER A 225 ? 0.3472 0.5633 0.5661 -0.0308 0.0204  -0.0426 225 SER A CA  
1739 C C   . SER A 225 ? 0.3381 0.5915 0.5851 -0.0317 0.0130  -0.0461 225 SER A C   
1740 O O   . SER A 225 ? 0.3485 0.6294 0.6185 -0.0422 0.0185  -0.0452 225 SER A O   
1741 C CB  . SER A 225 ? 0.3726 0.5686 0.5835 -0.0490 0.0204  -0.0409 225 SER A CB  
1742 O OG  . SER A 225 ? 0.4063 0.5946 0.6154 -0.0545 0.0067  -0.0455 225 SER A OG  
1743 N N   . ILE A 226 ? 0.3290 0.5853 0.5745 -0.0208 0.0006  -0.0496 226 ILE A N   
1744 C CA  . ILE A 226 ? 0.3185 0.6119 0.5896 -0.0179 -0.0085 -0.0533 226 ILE A CA  
1745 C C   . ILE A 226 ? 0.3072 0.5946 0.5734 -0.0234 -0.0250 -0.0582 226 ILE A C   
1746 O O   . ILE A 226 ? 0.2459 0.5034 0.4860 -0.0178 -0.0300 -0.0584 226 ILE A O   
1747 C CB  . ILE A 226 ? 0.3689 0.6749 0.6424 0.0052  -0.0090 -0.0529 226 ILE A CB  
1748 C CG1 . ILE A 226 ? 0.4212 0.7246 0.6923 0.0134  0.0067  -0.0498 226 ILE A CG1 
1749 C CG2 . ILE A 226 ? 0.3764 0.7256 0.6792 0.0094  -0.0181 -0.0565 226 ILE A CG2 
1750 C CD1 . ILE A 226 ? 0.4645 0.7400 0.7124 0.0318  0.0073  -0.0479 226 ILE A CD1 
1751 N N   . LEU A 227 ? 0.2079 0.5253 0.4993 -0.0341 -0.0334 -0.0628 227 LEU A N   
1752 C CA  . LEU A 227 ? 0.2717 0.5887 0.5596 -0.0364 -0.0512 -0.0694 227 LEU A CA  
1753 C C   . LEU A 227 ? 0.3065 0.6433 0.5968 -0.0157 -0.0609 -0.0705 227 LEU A C   
1754 O O   . LEU A 227 ? 0.3307 0.7055 0.6479 -0.0101 -0.0614 -0.0708 227 LEU A O   
1755 C CB  . LEU A 227 ? 0.2827 0.6226 0.5969 -0.0579 -0.0581 -0.0748 227 LEU A CB  
1756 C CG  . LEU A 227 ? 0.3049 0.6548 0.6216 -0.0595 -0.0787 -0.0840 227 LEU A CG  
1757 C CD1 . LEU A 227 ? 0.3601 0.6676 0.6422 -0.0592 -0.0856 -0.0876 227 LEU A CD1 
1758 C CD2 . LEU A 227 ? 0.3429 0.7207 0.6917 -0.0821 -0.0851 -0.0894 227 LEU A CD2 
1759 N N   . HIS A 228 ? 0.3118 0.6237 0.5740 -0.0036 -0.0682 -0.0703 228 HIS A N   
1760 C CA  . HIS A 228 ? 0.3593 0.6846 0.6183 0.0159  -0.0791 -0.0700 228 HIS A CA  
1761 C C   . HIS A 228 ? 0.3578 0.6909 0.6141 0.0113  -0.0978 -0.0780 228 HIS A C   
1762 O O   . HIS A 228 ? 0.3521 0.6591 0.5885 0.0020  -0.1014 -0.0819 228 HIS A O   
1763 C CB  . HIS A 228 ? 0.3727 0.6655 0.6008 0.0326  -0.0742 -0.0629 228 HIS A CB  
1764 C CG  . HIS A 228 ? 0.3795 0.6638 0.6086 0.0394  -0.0583 -0.0566 228 HIS A CG  
1765 N ND1 . HIS A 228 ? 0.3904 0.6806 0.6210 0.0590  -0.0568 -0.0520 228 HIS A ND1 
1766 C CD2 . HIS A 228 ? 0.3999 0.6690 0.6272 0.0298  -0.0440 -0.0548 228 HIS A CD2 
1767 C CE1 . HIS A 228 ? 0.4063 0.6849 0.6361 0.0609  -0.0423 -0.0489 228 HIS A CE1 
1768 N NE2 . HIS A 228 ? 0.3821 0.6492 0.6097 0.0433  -0.0344 -0.0503 228 HIS A NE2 
1769 N N   . ARG A 229 ? 0.3396 0.7089 0.6152 0.0191  -0.1102 -0.0811 229 ARG A N   
1770 C CA  . ARG A 229 ? 0.3385 0.7201 0.6127 0.0161  -0.1300 -0.0899 229 ARG A CA  
1771 C C   . ARG A 229 ? 0.3369 0.7171 0.5897 0.0394  -0.1405 -0.0866 229 ARG A C   
1772 O O   . ARG A 229 ? 0.3426 0.7267 0.5951 0.0578  -0.1353 -0.0782 229 ARG A O   
1773 C CB  . ARG A 229 ? 0.3389 0.7674 0.6535 0.0049  -0.1391 -0.0970 229 ARG A CB  
1774 C CG  . ARG A 229 ? 0.3171 0.7477 0.6527 -0.0215 -0.1310 -0.1001 229 ARG A CG  
1775 C CD  . ARG A 229 ? 0.3022 0.7807 0.6782 -0.0337 -0.1407 -0.1064 229 ARG A CD  
1776 N NE  . ARG A 229 ? 0.3584 0.8405 0.7564 -0.0576 -0.1285 -0.1044 229 ARG A NE  
1777 C CZ  . ARG A 229 ? 0.4598 0.9229 0.8562 -0.0813 -0.1320 -0.1093 229 ARG A CZ  
1778 N NH1 . ARG A 229 ? 0.5017 0.9412 0.8754 -0.0836 -0.1475 -0.1184 229 ARG A NH1 
1779 N NH2 . ARG A 229 ? 0.5064 0.9717 0.9215 -0.1019 -0.1197 -0.1045 229 ARG A NH2 
1780 N N   . ASP A 230 ? 0.3712 0.7443 0.6045 0.0388  -0.1556 -0.0933 230 ASP A N   
1781 C CA  . ASP A 230 ? 0.3970 0.7714 0.6079 0.0596  -0.1678 -0.0904 230 ASP A CA  
1782 C C   . ASP A 230 ? 0.4193 0.7605 0.6007 0.0754  -0.1552 -0.0774 230 ASP A C   
1783 O O   . ASP A 230 ? 0.4312 0.7777 0.6071 0.0952  -0.1572 -0.0688 230 ASP A O   
1784 C CB  . ASP A 230 ? 0.3382 0.7570 0.5754 0.0717  -0.1798 -0.0908 230 ASP A CB  
1785 C CG  . ASP A 230 ? 0.3462 0.7692 0.5600 0.0907  -0.1964 -0.0894 230 ASP A CG  
1786 O OD1 . ASP A 230 ? 0.3641 0.7667 0.5479 0.0887  -0.2036 -0.0938 230 ASP A OD1 
1787 O OD2 . ASP A 230 ? 0.3699 0.8084 0.5905 0.1066  -0.1985 -0.0818 230 ASP A OD2 
1788 N N   . VAL A 231 ? 0.3668 0.6732 0.5299 0.0663  -0.1426 -0.0756 231 VAL A N   
1789 C CA  . VAL A 231 ? 0.2906 0.5660 0.4288 0.0775  -0.1299 -0.0638 231 VAL A CA  
1790 C C   . VAL A 231 ? 0.3683 0.6292 0.4717 0.0892  -0.1380 -0.0609 231 VAL A C   
1791 O O   . VAL A 231 ? 0.3790 0.6359 0.4681 0.0825  -0.1466 -0.0697 231 VAL A O   
1792 C CB  . VAL A 231 ? 0.3240 0.5717 0.4577 0.0636  -0.1139 -0.0633 231 VAL A CB  
1793 C CG1 . VAL A 231 ? 0.3217 0.5377 0.4263 0.0728  -0.1043 -0.0534 231 VAL A CG1 
1794 C CG2 . VAL A 231 ? 0.3323 0.5916 0.4946 0.0573  -0.1026 -0.0620 231 VAL A CG2 
1795 N N   . GLN A 232 ? 0.3481 0.6004 0.4368 0.1070  -0.1352 -0.0484 232 GLN A N   
1796 C CA  . GLN A 232 ? 0.3850 0.6207 0.4382 0.1183  -0.1390 -0.0417 232 GLN A CA  
1797 C C   . GLN A 232 ? 0.4250 0.6260 0.4564 0.1158  -0.1229 -0.0334 232 GLN A C   
1798 O O   . GLN A 232 ? 0.4759 0.6629 0.4789 0.1176  -0.1234 -0.0319 232 GLN A O   
1799 C CB  . GLN A 232 ? 0.3907 0.6365 0.4392 0.1393  -0.1464 -0.0310 232 GLN A CB  
1800 N N   . GLU A 233 ? 0.3807 0.5697 0.4255 0.1117  -0.1088 -0.0285 233 GLU A N   
1801 C CA  . GLU A 233 ? 0.3810 0.5395 0.4078 0.1102  -0.0945 -0.0198 233 GLU A CA  
1802 C C   . GLU A 233 ? 0.3878 0.5390 0.4346 0.1020  -0.0817 -0.0201 233 GLU A C   
1803 O O   . GLU A 233 ? 0.3487 0.5147 0.4180 0.1056  -0.0820 -0.0207 233 GLU A O   
1804 C CB  . GLU A 233 ? 0.4641 0.6099 0.4712 0.1262  -0.0936 -0.0047 233 GLU A CB  
1805 C CG  . GLU A 233 ? 0.4938 0.6107 0.4808 0.1237  -0.0803 0.0050  233 GLU A CG  
1806 C CD  . GLU A 233 ? 0.5097 0.6124 0.4808 0.1376  -0.0788 0.0214  233 GLU A CD  
1807 O OE1 . GLU A 233 ? 0.5398 0.6523 0.5180 0.1502  -0.0868 0.0252  233 GLU A OE1 
1808 O OE2 . GLU A 233 ? 0.5585 0.6404 0.5107 0.1358  -0.0697 0.0311  233 GLU A OE2 
1809 N N   . ILE A 234 ? 0.3306 0.4609 0.3687 0.0921  -0.0707 -0.0199 234 ILE A N   
1810 C CA  . ILE A 234 ? 0.3131 0.4313 0.3625 0.0864  -0.0578 -0.0180 234 ILE A CA  
1811 C C   . ILE A 234 ? 0.3592 0.4514 0.3887 0.0898  -0.0489 -0.0074 234 ILE A C   
1812 O O   . ILE A 234 ? 0.4181 0.5006 0.4283 0.0873  -0.0478 -0.0059 234 ILE A O   
1813 C CB  . ILE A 234 ? 0.3505 0.4683 0.4098 0.0703  -0.0531 -0.0272 234 ILE A CB  
1814 C CG1 . ILE A 234 ? 0.3772 0.5206 0.4572 0.0641  -0.0621 -0.0370 234 ILE A CG1 
1815 C CG2 . ILE A 234 ? 0.3126 0.4188 0.3807 0.0661  -0.0403 -0.0247 234 ILE A CG2 
1816 C CD1 . ILE A 234 ? 0.4018 0.5414 0.4819 0.0490  -0.0630 -0.0460 234 ILE A CD1 
1817 N N   . ARG A 235 ? 0.3019 0.3838 0.3365 0.0955  -0.0427 -0.0006 235 ARG A N   
1818 C CA  . ARG A 235 ? 0.3289 0.3864 0.3474 0.0989  -0.0356 0.0106  235 ARG A CA  
1819 C C   . ARG A 235 ? 0.3101 0.3525 0.3365 0.0911  -0.0245 0.0094  235 ARG A C   
1820 O O   . ARG A 235 ? 0.2944 0.3413 0.3373 0.0928  -0.0226 0.0054  235 ARG A O   
1821 C CB  . ARG A 235 ? 0.4307 0.4845 0.4452 0.1142  -0.0404 0.0205  235 ARG A CB  
1822 C CG  . ARG A 235 ? 0.5294 0.5596 0.5228 0.1176  -0.0361 0.0342  235 ARG A CG  
1823 C CD  . ARG A 235 ? 0.5773 0.6120 0.5557 0.1313  -0.0455 0.0434  235 ARG A CD  
1824 N NE  . ARG A 235 ? 0.6066 0.6477 0.5962 0.1455  -0.0528 0.0450  235 ARG A NE  
1825 C CZ  . ARG A 235 ? 0.6764 0.6981 0.6698 0.1527  -0.0491 0.0518  235 ARG A CZ  
1826 N NH1 . ARG A 235 ? 0.6784 0.7082 0.6820 0.1681  -0.0565 0.0522  235 ARG A NH1 
1827 N NH2 . ARG A 235 ? 0.6732 0.6676 0.6609 0.1450  -0.0385 0.0571  235 ARG A NH2 
1828 N N   . TYR A 236 ? 0.2721 0.2988 0.2867 0.0833  -0.0173 0.0125  236 TYR A N   
1829 C CA  . TYR A 236 ? 0.3174 0.3297 0.3371 0.0756  -0.0079 0.0112  236 TYR A CA  
1830 C C   . TYR A 236 ? 0.3559 0.3461 0.3648 0.0772  -0.0030 0.0221  236 TYR A C   
1831 O O   . TYR A 236 ? 0.3411 0.3269 0.3349 0.0779  -0.0029 0.0304  236 TYR A O   
1832 C CB  . TYR A 236 ? 0.3310 0.3449 0.3492 0.0637  -0.0039 0.0048  236 TYR A CB  
1833 C CG  . TYR A 236 ? 0.3212 0.3514 0.3512 0.0590  -0.0074 -0.0055 236 TYR A CG  
1834 C CD1 . TYR A 236 ? 0.3249 0.3621 0.3717 0.0579  -0.0055 -0.0104 236 TYR A CD1 
1835 C CD2 . TYR A 236 ? 0.3641 0.4026 0.3883 0.0554  -0.0124 -0.0104 236 TYR A CD2 
1836 C CE1 . TYR A 236 ? 0.3272 0.3798 0.3859 0.0515  -0.0077 -0.0182 236 TYR A CE1 
1837 C CE2 . TYR A 236 ? 0.3828 0.4333 0.4186 0.0490  -0.0159 -0.0194 236 TYR A CE2 
1838 C CZ  . TYR A 236 ? 0.3905 0.4485 0.4442 0.0463  -0.0132 -0.0224 236 TYR A CZ  
1839 O OH  . TYR A 236 ? 0.5300 0.6007 0.5965 0.0382  -0.0156 -0.0296 236 TYR A OH  
1840 N N   . GLU A 237 ? 0.3356 0.3120 0.3519 0.0770  0.0015  0.0218  237 GLU A N   
1841 C CA  . GLU A 237 ? 0.3130 0.2653 0.3216 0.0758  0.0061  0.0308  237 GLU A CA  
1842 C C   . GLU A 237 ? 0.3065 0.2474 0.3247 0.0709  0.0111  0.0239  237 GLU A C   
1843 O O   . GLU A 237 ? 0.2795 0.2299 0.3090 0.0738  0.0107  0.0148  237 GLU A O   
1844 C CB  A GLU A 237 ? 0.3591 0.2998 0.3612 0.0881  0.0017  0.0414  237 GLU A CB  
1845 C CB  B GLU A 237 ? 0.3594 0.3006 0.3619 0.0883  0.0015  0.0411  237 GLU A CB  
1846 C CG  A GLU A 237 ? 0.3952 0.3448 0.4084 0.1010  -0.0042 0.0366  237 GLU A CG  
1847 C CG  B GLU A 237 ? 0.3982 0.3126 0.3902 0.0855  0.0057  0.0533  237 GLU A CG  
1848 C CD  A GLU A 237 ? 0.4487 0.3963 0.4529 0.1151  -0.0116 0.0471  237 GLU A CD  
1849 C CD  B GLU A 237 ? 0.4627 0.3629 0.4468 0.0987  0.0008  0.0649  237 GLU A CD  
1850 O OE1 A GLU A 237 ? 0.4758 0.3983 0.4695 0.1187  -0.0104 0.0587  237 GLU A OE1 
1851 O OE1 B GLU A 237 ? 0.4732 0.3892 0.4574 0.1105  -0.0066 0.0644  237 GLU A OE1 
1852 O OE2 A GLU A 237 ? 0.4394 0.4102 0.4468 0.1223  -0.0191 0.0442  237 GLU A OE2 
1853 O OE2 B GLU A 237 ? 0.4455 0.3183 0.4234 0.0970  0.0037  0.0747  237 GLU A OE2 
1854 N N   . VAL A 238 ? 0.3282 0.2508 0.3418 0.0629  0.0160  0.0281  238 VAL A N   
1855 C CA  . VAL A 238 ? 0.3777 0.2863 0.3976 0.0592  0.0194  0.0215  238 VAL A CA  
1856 C C   . VAL A 238 ? 0.4262 0.3207 0.4489 0.0714  0.0166  0.0216  238 VAL A C   
1857 O O   . VAL A 238 ? 0.4213 0.3001 0.4371 0.0778  0.0141  0.0319  238 VAL A O   
1858 C CB  . VAL A 238 ? 0.3489 0.2419 0.3646 0.0474  0.0236  0.0260  238 VAL A CB  
1859 C CG1 . VAL A 238 ? 0.3680 0.2455 0.3891 0.0437  0.0254  0.0176  238 VAL A CG1 
1860 C CG2 . VAL A 238 ? 0.3009 0.2110 0.3151 0.0381  0.0263  0.0247  238 VAL A CG2 
1861 N N   . SER A 239 ? 0.3711 0.2715 0.4031 0.0757  0.0173  0.0105  239 SER A N   
1862 C CA  . SER A 239 ? 0.3797 0.2694 0.4153 0.0898  0.0150  0.0086  239 SER A CA  
1863 C C   . SER A 239 ? 0.4156 0.2702 0.4446 0.0888  0.0157  0.0117  239 SER A C   
1864 O O   . SER A 239 ? 0.4637 0.3066 0.4898 0.0758  0.0189  0.0105  239 SER A O   
1865 C CB  . SER A 239 ? 0.3505 0.2567 0.3972 0.0941  0.0174  -0.0046 239 SER A CB  
1866 O OG  . SER A 239 ? 0.4244 0.3203 0.4746 0.1091  0.0161  -0.0080 239 SER A OG  
1867 N N   . ALA A 240 ? 0.4307 0.2679 0.4579 0.1027  0.0120  0.0156  240 ALA A N   
1868 C CA  . ALA A 240 ? 0.4592 0.2596 0.4815 0.1037  0.0119  0.0152  240 ALA A CA  
1869 C C   . ALA A 240 ? 0.5010 0.2991 0.5290 0.1072  0.0143  -0.0012 240 ALA A C   
1870 O O   . ALA A 240 ? 0.5108 0.2789 0.5344 0.1046  0.0142  -0.0053 240 ALA A O   
1871 C CB  . ALA A 240 ? 0.5275 0.3066 0.5445 0.1195  0.0067  0.0249  240 ALA A CB  
1872 N N   . LYS A 241 ? 0.5113 0.3402 0.5484 0.1127  0.0163  -0.0107 241 LYS A N   
1873 C CA  . LYS A 241 ? 0.4837 0.3153 0.5245 0.1166  0.0199  -0.0259 241 LYS A CA  
1874 C C   . LYS A 241 ? 0.4449 0.2824 0.4835 0.0995  0.0242  -0.0318 241 LYS A C   
1875 O O   . LYS A 241 ? 0.4020 0.2546 0.4409 0.0874  0.0250  -0.0262 241 LYS A O   
1876 C CB  . LYS A 241 ? 0.4574 0.3224 0.5101 0.1294  0.0214  -0.0319 241 LYS A CB  
1877 C CG  . LYS A 241 ? 0.4756 0.3390 0.5323 0.1488  0.0163  -0.0270 241 LYS A CG  
1878 C CD  . LYS A 241 ? 0.4818 0.3870 0.5539 0.1580  0.0166  -0.0302 241 LYS A CD  
1879 C CE  . LYS A 241 ? 0.4981 0.4036 0.5750 0.1789  0.0102  -0.0256 241 LYS A CE  
1880 N NZ  . LYS A 241 ? 0.5222 0.4711 0.6176 0.1887  0.0104  -0.0305 241 LYS A NZ  
1881 N N   . LYS A 242 ? 0.4613 0.2866 0.4967 0.0999  0.0262  -0.0439 242 LYS A N   
1882 C CA  . LYS A 242 ? 0.4818 0.3128 0.5139 0.0857  0.0292  -0.0504 242 LYS A CA  
1883 C C   . LYS A 242 ? 0.4481 0.2924 0.4805 0.0932  0.0337  -0.0643 242 LYS A C   
1884 O O   . LYS A 242 ? 0.4543 0.2929 0.4875 0.1086  0.0341  -0.0712 242 LYS A O   
1885 C CB  . LYS A 242 ? 0.5581 0.3577 0.5827 0.0747  0.0262  -0.0507 242 LYS A CB  
1886 C CG  . LYS A 242 ? 0.6248 0.4087 0.6486 0.0678  0.0230  -0.0358 242 LYS A CG  
1887 C CD  . LYS A 242 ? 0.6948 0.4603 0.7155 0.0508  0.0215  -0.0349 242 LYS A CD  
1888 C CE  . LYS A 242 ? 0.6814 0.4727 0.7047 0.0371  0.0240  -0.0327 242 LYS A CE  
1889 N NZ  . LYS A 242 ? 0.6567 0.4363 0.6798 0.0211  0.0222  -0.0340 242 LYS A NZ  
1890 N N   . ILE A 243 ? 0.4248 0.2878 0.4558 0.0833  0.0373  -0.0680 243 ILE A N   
1891 C CA  . ILE A 243 ? 0.4180 0.2918 0.4454 0.0880  0.0424  -0.0804 243 ILE A CA  
1892 C C   . ILE A 243 ? 0.4444 0.2934 0.4599 0.0825  0.0398  -0.0896 243 ILE A C   
1893 O O   . ILE A 243 ? 0.4262 0.2641 0.4390 0.0688  0.0360  -0.0854 243 ILE A O   
1894 C CB  . ILE A 243 ? 0.3687 0.2741 0.3991 0.0806  0.0475  -0.0784 243 ILE A CB  
1895 C CG1 . ILE A 243 ? 0.4184 0.3364 0.4435 0.0861  0.0541  -0.0895 243 ILE A CG1 
1896 C CG2 . ILE A 243 ? 0.3512 0.2540 0.3772 0.0643  0.0451  -0.0729 243 ILE A CG2 
1897 C CD1 . ILE A 243 ? 0.3843 0.3294 0.4108 0.0776  0.0594  -0.0860 243 ILE A CD1 
1898 N N   . HIS A 244 ? 0.4354 0.2771 0.4443 0.0934  0.0416  -0.1028 244 HIS A N   
1899 C CA  . HIS A 244 ? 0.4897 0.3071 0.4861 0.0897  0.0380  -0.1144 244 HIS A CA  
1900 C C   . HIS A 244 ? 0.4729 0.3096 0.4599 0.0896  0.0430  -0.1243 244 HIS A C   
1901 O O   . HIS A 244 ? 0.4417 0.2997 0.4296 0.1011  0.0503  -0.1283 244 HIS A O   
1902 C CB  . HIS A 244 ? 0.5291 0.3161 0.5213 0.1037  0.0348  -0.1235 244 HIS A CB  
1903 C CG  . HIS A 244 ? 0.5544 0.3211 0.5539 0.1059  0.0302  -0.1122 244 HIS A CG  
1904 N ND1 . HIS A 244 ? 0.5499 0.2920 0.5492 0.0917  0.0241  -0.1043 244 HIS A ND1 
1905 C CD2 . HIS A 244 ? 0.5583 0.3274 0.5654 0.1207  0.0309  -0.1066 244 HIS A CD2 
1906 C CE1 . HIS A 244 ? 0.5717 0.2997 0.5759 0.0977  0.0217  -0.0934 244 HIS A CE1 
1907 N NE2 . HIS A 244 ? 0.5697 0.3133 0.5783 0.1158  0.0250  -0.0949 244 HIS A NE2 
1908 N N   . PHE A 245 ? 0.4869 0.3178 0.4654 0.0769  0.0393  -0.1276 245 PHE A N   
1909 C CA  . PHE A 245 ? 0.4857 0.3308 0.4513 0.0766  0.0425  -0.1368 245 PHE A CA  
1910 C C   . PHE A 245 ? 0.5511 0.3711 0.5020 0.0801  0.0371  -0.1538 245 PHE A C   
1911 O O   . PHE A 245 ? 0.5394 0.3313 0.4910 0.0733  0.0287  -0.1561 245 PHE A O   
1912 C CB  . PHE A 245 ? 0.4745 0.3336 0.4398 0.0611  0.0409  -0.1287 245 PHE A CB  
1913 C CG  . PHE A 245 ? 0.4590 0.3415 0.4359 0.0576  0.0457  -0.1142 245 PHE A CG  
1914 C CD1 . PHE A 245 ? 0.4696 0.3778 0.4446 0.0606  0.0536  -0.1122 245 PHE A CD1 
1915 C CD2 . PHE A 245 ? 0.4638 0.3422 0.4527 0.0509  0.0424  -0.1026 245 PHE A CD2 
1916 C CE1 . PHE A 245 ? 0.4701 0.3973 0.4560 0.0561  0.0569  -0.0999 245 PHE A CE1 
1917 C CE2 . PHE A 245 ? 0.4722 0.3708 0.4702 0.0481  0.0457  -0.0911 245 PHE A CE2 
1918 C CZ  . PHE A 245 ? 0.4505 0.3724 0.4475 0.0503  0.0524  -0.0904 245 PHE A CZ  
1919 N N   . ALA A 246 ? 0.5727 0.4028 0.5099 0.0904  0.0421  -0.1658 246 ALA A N   
1920 C CA  . ALA A 246 ? 0.5987 0.4107 0.5186 0.0898  0.0371  -0.1793 246 ALA A CA  
1921 C C   . ALA A 246 ? 0.6538 0.4746 0.5646 0.0776  0.0324  -0.1816 246 ALA A C   
1922 O O   . ALA A 246 ? 0.6962 0.5444 0.6031 0.0774  0.0389  -0.1765 246 ALA A O   
1923 C CB  . ALA A 246 ? 0.6187 0.4411 0.5278 0.1041  0.0456  -0.1870 246 ALA A CB  
1924 N N   . ARG A 247 ? 0.6795 0.4791 0.5884 0.0657  0.0214  -0.1860 247 ARG A N   
1925 C CA  . ARG A 247 ? 0.7161 0.5253 0.6177 0.0545  0.0152  -0.1886 247 ARG A CA  
1926 C C   . ARG A 247 ? 0.7504 0.5456 0.6343 0.0534  0.0084  -0.2023 247 ARG A C   
1927 O O   . ARG A 247 ? 0.7867 0.5551 0.6719 0.0511  0.0029  -0.2078 247 ARG A O   
1928 C CB  . ARG A 247 ? 0.7136 0.5211 0.6322 0.0372  0.0089  -0.1758 247 ARG A CB  
1929 C CG  . ARG A 247 ? 0.7211 0.5464 0.6558 0.0353  0.0163  -0.1564 247 ARG A CG  
1930 C CD  . ARG A 247 ? 0.6934 0.5479 0.6262 0.0313  0.0202  -0.1469 247 ARG A CD  
1931 N NE  . ARG A 247 ? 0.7142 0.5787 0.6635 0.0249  0.0228  -0.1302 247 ARG A NE  
1932 C CZ  . ARG A 247 ? 0.6516 0.5341 0.6055 0.0290  0.0309  -0.1201 247 ARG A CZ  
1933 N NH1 . ARG A 247 ? 0.6023 0.4973 0.5472 0.0384  0.0384  -0.1232 247 ARG A NH1 
1934 N NH2 . ARG A 247 ? 0.6081 0.4969 0.5753 0.0232  0.0315  -0.1071 247 ARG A NH2 
1935 N N   . PHE A 248 ? 0.7702 0.5832 0.6369 0.0550  0.0090  -0.2072 248 PHE A N   
1936 C CA  . PHE A 248 ? 0.7761 0.5806 0.6242 0.0550  0.0028  -0.2206 248 PHE A CA  
1937 C C   . PHE A 248 ? 0.7658 0.5749 0.6099 0.0419  -0.0092 -0.2235 248 PHE A C   
1938 O O   . PHE A 248 ? 0.7939 0.5951 0.6244 0.0397  -0.0169 -0.2351 248 PHE A O   
1939 C CB  . PHE A 248 ? 0.8116 0.6338 0.6403 0.0688  0.0130  -0.2245 248 PHE A CB  
1940 C CG  . PHE A 248 ? 0.8155 0.6343 0.6480 0.0823  0.0235  -0.2250 248 PHE A CG  
1941 C CD1 . PHE A 248 ? 0.8035 0.6386 0.6493 0.0883  0.0341  -0.2135 248 PHE A CD1 
1942 C CD2 . PHE A 248 ? 0.8036 0.6037 0.6274 0.0891  0.0222  -0.2376 248 PHE A CD2 
1943 C CE1 . PHE A 248 ? 0.7721 0.6073 0.6236 0.1011  0.0429  -0.2140 248 PHE A CE1 
1944 C CE2 . PHE A 248 ? 0.7943 0.5928 0.6228 0.1027  0.0313  -0.2384 248 PHE A CE2 
1945 C CZ  . PHE A 248 ? 0.7579 0.5751 0.6009 0.1087  0.0415  -0.2264 248 PHE A CZ  
1946 N N   . ARG A 249 ? 0.6326 0.4558 0.4894 0.0337  -0.0113 -0.2139 249 ARG A N   
1947 C CA  . ARG A 249 ? 0.6422 0.4751 0.4990 0.0221  -0.0226 -0.2153 249 ARG A CA  
1948 C C   . ARG A 249 ? 0.6074 0.4505 0.4883 0.0117  -0.0216 -0.1986 249 ARG A C   
1949 O O   . ARG A 249 ? 0.5652 0.4103 0.4577 0.0148  -0.0117 -0.1860 249 ARG A O   
1950 C CB  . ARG A 249 ? 0.6432 0.4984 0.4770 0.0289  -0.0212 -0.2168 249 ARG A CB  
1951 C CG  . ARG A 249 ? 0.6010 0.4771 0.4327 0.0369  -0.0076 -0.2034 249 ARG A CG  
1952 C CD  . ARG A 249 ? 0.6321 0.5267 0.4374 0.0450  -0.0044 -0.2044 249 ARG A CD  
1953 N NE  . ARG A 249 ? 0.6593 0.5722 0.4667 0.0486  0.0093  -0.1867 249 ARG A NE  
1954 C CZ  . ARG A 249 ? 0.7056 0.6348 0.4918 0.0559  0.0167  -0.1826 249 ARG A CZ  
1955 N NH1 . ARG A 249 ? 0.6868 0.6303 0.4785 0.0565  0.0288  -0.1657 249 ARG A NH1 
1956 N NH2 . ARG A 249 ? 0.6933 0.6241 0.4537 0.0611  0.0121  -0.1935 249 ARG A NH2 
1957 N N   . SER A 250 ? 0.6595 0.5113 0.5485 -0.0008 -0.0316 -0.1967 250 SER A N   
1958 C CA  . SER A 250 ? 0.6201 0.4847 0.5312 -0.0105 -0.0301 -0.1792 250 SER A CA  
1959 C C   . SER A 250 ? 0.5757 0.4650 0.4809 -0.0045 -0.0227 -0.1663 250 SER A C   
1960 O O   . SER A 250 ? 0.5728 0.4755 0.4618 -0.0010 -0.0263 -0.1695 250 SER A O   
1961 C CB  . SER A 250 ? 0.6775 0.5457 0.6016 -0.0255 -0.0431 -0.1821 250 SER A CB  
1962 O OG  . SER A 250 ? 0.6259 0.5112 0.5696 -0.0328 -0.0406 -0.1656 250 SER A OG  
1963 N N   . PHE A 251 ? 0.5551 0.4488 0.4722 -0.0030 -0.0128 -0.1518 251 PHE A N   
1964 C CA  . PHE A 251 ? 0.5402 0.4537 0.4564 -0.0002 -0.0067 -0.1380 251 PHE A CA  
1965 C C   . PHE A 251 ? 0.5038 0.4192 0.4423 -0.0068 -0.0039 -0.1248 251 PHE A C   
1966 O O   . PHE A 251 ? 0.4894 0.4013 0.4341 -0.0032 0.0045  -0.1178 251 PHE A O   
1967 C CB  . PHE A 251 ? 0.5880 0.5053 0.4901 0.0112  0.0045  -0.1359 251 PHE A CB  
1968 C CG  . PHE A 251 ? 0.6234 0.5578 0.5217 0.0130  0.0101  -0.1225 251 PHE A CG  
1969 C CD1 . PHE A 251 ? 0.6206 0.5651 0.5219 0.0081  0.0039  -0.1158 251 PHE A CD1 
1970 C CD2 . PHE A 251 ? 0.6676 0.6075 0.5600 0.0198  0.0215  -0.1166 251 PHE A CD2 
1971 C CE1 . PHE A 251 ? 0.6074 0.5627 0.5038 0.0105  0.0084  -0.1037 251 PHE A CE1 
1972 C CE2 . PHE A 251 ? 0.6685 0.6204 0.5575 0.0199  0.0263  -0.1040 251 PHE A CE2 
1973 C CZ  . PHE A 251 ? 0.6418 0.5990 0.5316 0.0156  0.0195  -0.0977 251 PHE A CZ  
1974 N N   . PRO A 252 ? 0.4499 0.3723 0.4010 -0.0162 -0.0111 -0.1218 252 PRO A N   
1975 C CA  . PRO A 252 ? 0.4336 0.3579 0.4049 -0.0226 -0.0084 -0.1104 252 PRO A CA  
1976 C C   . PRO A 252 ? 0.4216 0.3565 0.3939 -0.0171 0.0000  -0.0976 252 PRO A C   
1977 O O   . PRO A 252 ? 0.4055 0.3512 0.3671 -0.0119 0.0012  -0.0948 252 PRO A O   
1978 C CB  . PRO A 252 ? 0.4317 0.3687 0.4142 -0.0323 -0.0175 -0.1106 252 PRO A CB  
1979 C CG  . PRO A 252 ? 0.4156 0.3488 0.3871 -0.0338 -0.0271 -0.1254 252 PRO A CG  
1980 C CD  . PRO A 252 ? 0.4529 0.3832 0.4011 -0.0215 -0.0226 -0.1298 252 PRO A CD  
1981 N N   . PHE A 253 ? 0.4186 0.3490 0.4034 -0.0187 0.0050  -0.0896 253 PHE A N   
1982 C CA  . PHE A 253 ? 0.3892 0.3281 0.3762 -0.0145 0.0118  -0.0787 253 PHE A CA  
1983 C C   . PHE A 253 ? 0.3384 0.2934 0.3249 -0.0147 0.0095  -0.0732 253 PHE A C   
1984 O O   . PHE A 253 ? 0.3051 0.2651 0.2835 -0.0093 0.0131  -0.0688 253 PHE A O   
1985 C CB  . PHE A 253 ? 0.3610 0.2946 0.3616 -0.0173 0.0149  -0.0714 253 PHE A CB  
1986 C CG  . PHE A 253 ? 0.3526 0.2941 0.3554 -0.0133 0.0205  -0.0618 253 PHE A CG  
1987 C CD1 . PHE A 253 ? 0.3779 0.3168 0.3767 -0.0068 0.0259  -0.0609 253 PHE A CD1 
1988 C CD2 . PHE A 253 ? 0.3629 0.3155 0.3728 -0.0160 0.0200  -0.0545 253 PHE A CD2 
1989 C CE1 . PHE A 253 ? 0.4153 0.3613 0.4171 -0.0045 0.0297  -0.0532 253 PHE A CE1 
1990 C CE2 . PHE A 253 ? 0.3494 0.3071 0.3600 -0.0121 0.0241  -0.0474 253 PHE A CE2 
1991 C CZ  . PHE A 253 ? 0.3663 0.3199 0.3730 -0.0072 0.0283  -0.0470 253 PHE A CZ  
1992 N N   . TRP A 254 ? 0.3358 0.2993 0.3316 -0.0209 0.0034  -0.0734 254 TRP A N   
1993 C CA  . TRP A 254 ? 0.3159 0.2955 0.3123 -0.0187 0.0011  -0.0683 254 TRP A CA  
1994 C C   . TRP A 254 ? 0.3141 0.2974 0.2938 -0.0132 -0.0028 -0.0723 254 TRP A C   
1995 O O   . TRP A 254 ? 0.3208 0.3109 0.2946 -0.0076 -0.0024 -0.0664 254 TRP A O   
1996 C CB  . TRP A 254 ? 0.3314 0.3241 0.3441 -0.0261 -0.0041 -0.0677 254 TRP A CB  
1997 C CG  . TRP A 254 ? 0.3123 0.3038 0.3396 -0.0311 0.0010  -0.0608 254 TRP A CG  
1998 C CD1 . TRP A 254 ? 0.3097 0.2979 0.3500 -0.0412 -0.0003 -0.0613 254 TRP A CD1 
1999 C CD2 . TRP A 254 ? 0.2951 0.2876 0.3236 -0.0265 0.0078  -0.0520 254 TRP A CD2 
2000 N NE1 . TRP A 254 ? 0.2966 0.2845 0.3448 -0.0423 0.0062  -0.0520 254 TRP A NE1 
2001 C CE2 . TRP A 254 ? 0.2797 0.2710 0.3205 -0.0330 0.0108  -0.0471 254 TRP A CE2 
2002 C CE3 . TRP A 254 ? 0.2896 0.2829 0.3095 -0.0182 0.0112  -0.0479 254 TRP A CE3 
2003 C CZ2 . TRP A 254 ? 0.3084 0.3013 0.3514 -0.0299 0.0168  -0.0389 254 TRP A CZ2 
2004 C CZ3 . TRP A 254 ? 0.3118 0.3056 0.3354 -0.0160 0.0164  -0.0411 254 TRP A CZ3 
2005 C CH2 . TRP A 254 ? 0.3163 0.3107 0.3505 -0.0211 0.0190  -0.0370 254 TRP A CH2 
2006 N N   . ARG A 255 ? 0.3235 0.3010 0.2937 -0.0139 -0.0069 -0.0822 255 ARG A N   
2007 C CA  . ARG A 255 ? 0.3286 0.3088 0.2788 -0.0073 -0.0092 -0.0850 255 ARG A CA  
2008 C C   . ARG A 255 ? 0.3503 0.3239 0.2884 -0.0010 0.0005  -0.0794 255 ARG A C   
2009 O O   . ARG A 255 ? 0.3545 0.3319 0.2800 0.0042  0.0016  -0.0737 255 ARG A O   
2010 C CB  . ARG A 255 ? 0.3080 0.2833 0.2486 -0.0088 -0.0158 -0.0985 255 ARG A CB  
2011 C CG  . ARG A 255 ? 0.4402 0.4161 0.3558 -0.0007 -0.0156 -0.1014 255 ARG A CG  
2012 C CD  . ARG A 255 ? 0.4760 0.4641 0.3831 0.0005  -0.0271 -0.1054 255 ARG A CD  
2013 N NE  . ARG A 255 ? 0.4137 0.4013 0.3256 -0.0060 -0.0374 -0.1191 255 ARG A NE  
2014 C CZ  . ARG A 255 ? 0.4060 0.4079 0.3246 -0.0098 -0.0495 -0.1231 255 ARG A CZ  
2015 N NH1 . ARG A 255 ? 0.3637 0.3818 0.2845 -0.0057 -0.0524 -0.1142 255 ARG A NH1 
2016 N NH2 . ARG A 255 ? 0.4123 0.4123 0.3362 -0.0177 -0.0591 -0.1365 255 ARG A NH2 
2017 N N   . ARG A 256 ? 0.3499 0.3140 0.2927 -0.0015 0.0073  -0.0804 256 ARG A N   
2018 C CA  A ARG A 256 ? 0.4068 0.3688 0.3437 0.0030  0.0168  -0.0746 256 ARG A CA  
2019 C CA  B ARG A 256 ? 0.4069 0.3688 0.3438 0.0030  0.0168  -0.0746 256 ARG A CA  
2020 C C   . ARG A 256 ? 0.3888 0.3554 0.3301 0.0032  0.0191  -0.0632 256 ARG A C   
2021 O O   . ARG A 256 ? 0.3516 0.3188 0.2823 0.0062  0.0233  -0.0575 256 ARG A O   
2022 C CB  A ARG A 256 ? 0.4428 0.3966 0.3889 0.0029  0.0221  -0.0773 256 ARG A CB  
2023 C CB  B ARG A 256 ? 0.4428 0.3965 0.3888 0.0028  0.0220  -0.0774 256 ARG A CB  
2024 C CG  A ARG A 256 ? 0.4593 0.4146 0.4019 0.0074  0.0316  -0.0734 256 ARG A CG  
2025 C CG  B ARG A 256 ? 0.4544 0.4099 0.4004 0.0065  0.0314  -0.0718 256 ARG A CG  
2026 C CD  A ARG A 256 ? 0.4373 0.3869 0.3924 0.0085  0.0354  -0.0747 256 ARG A CD  
2027 C CD  B ARG A 256 ? 0.4384 0.3873 0.3955 0.0078  0.0346  -0.0745 256 ARG A CD  
2028 N NE  A ARG A 256 ? 0.4388 0.3780 0.3917 0.0105  0.0329  -0.0857 256 ARG A NE  
2029 N NE  B ARG A 256 ? 0.4473 0.3897 0.3963 0.0126  0.0356  -0.0853 256 ARG A NE  
2030 C CZ  A ARG A 256 ? 0.4658 0.4036 0.4073 0.0171  0.0365  -0.0938 256 ARG A CZ  
2031 C CZ  B ARG A 256 ? 0.4841 0.4143 0.4345 0.0114  0.0300  -0.0941 256 ARG A CZ  
2032 N NH1 A ARG A 256 ? 0.4149 0.3640 0.3475 0.0212  0.0438  -0.0907 256 ARG A NH1 
2033 N NH1 B ARG A 256 ? 0.5005 0.4234 0.4413 0.0175  0.0310  -0.1052 256 ARG A NH1 
2034 N NH2 A ARG A 256 ? 0.4908 0.4157 0.4297 0.0195  0.0332  -0.1052 256 ARG A NH2 
2035 N NH2 B ARG A 256 ? 0.4330 0.3579 0.3942 0.0041  0.0237  -0.0923 256 ARG A NH2 
2036 N N   . VAL A 257 ? 0.3359 0.3051 0.2919 0.0000  0.0164  -0.0598 257 VAL A N   
2037 C CA  . VAL A 257 ? 0.3074 0.2799 0.2666 0.0014  0.0174  -0.0511 257 VAL A CA  
2038 C C   . VAL A 257 ? 0.3063 0.2830 0.2539 0.0054  0.0126  -0.0487 257 VAL A C   
2039 O O   . VAL A 257 ? 0.3061 0.2793 0.2464 0.0086  0.0148  -0.0417 257 VAL A O   
2040 C CB  . VAL A 257 ? 0.2779 0.2546 0.2535 -0.0016 0.0158  -0.0491 257 VAL A CB  
2041 C CG1 . VAL A 257 ? 0.2626 0.2429 0.2392 0.0019  0.0157  -0.0423 257 VAL A CG1 
2042 C CG2 . VAL A 257 ? 0.2680 0.2386 0.2528 -0.0042 0.0206  -0.0492 257 VAL A CG2 
2043 N N   . HIS A 258 ? 0.2967 0.2806 0.2431 0.0052  0.0049  -0.0542 258 HIS A N   
2044 C CA  . HIS A 258 ? 0.3412 0.3304 0.2759 0.0107  -0.0011 -0.0519 258 HIS A CA  
2045 C C   . HIS A 258 ? 0.3222 0.3038 0.2354 0.0147  0.0027  -0.0487 258 HIS A C   
2046 O O   . HIS A 258 ? 0.3596 0.3377 0.2627 0.0194  0.0029  -0.0405 258 HIS A O   
2047 C CB  . HIS A 258 ? 0.3216 0.3219 0.2586 0.0093  -0.0108 -0.0599 258 HIS A CB  
2048 C CG  . HIS A 258 ? 0.3137 0.3205 0.2359 0.0163  -0.0183 -0.0585 258 HIS A CG  
2049 N ND1 . HIS A 258 ? 0.3932 0.3961 0.2934 0.0198  -0.0196 -0.0610 258 HIS A ND1 
2050 C CD2 . HIS A 258 ? 0.3117 0.3294 0.2371 0.0218  -0.0250 -0.0548 258 HIS A CD2 
2051 C CE1 . HIS A 258 ? 0.3413 0.3513 0.2307 0.0268  -0.0273 -0.0580 258 HIS A CE1 
2052 N NE2 . HIS A 258 ? 0.4090 0.4279 0.3141 0.0286  -0.0311 -0.0544 258 HIS A NE2 
2053 N N   . ASP A 259 ? 0.3747 0.3532 0.2803 0.0133  0.0062  -0.0548 259 ASP A N   
2054 C CA  . ASP A 259 ? 0.3848 0.3597 0.2690 0.0171  0.0109  -0.0520 259 ASP A CA  
2055 C C   . ASP A 259 ? 0.4449 0.4132 0.3284 0.0164  0.0203  -0.0413 259 ASP A C   
2056 O O   . ASP A 259 ? 0.4871 0.4522 0.3538 0.0189  0.0234  -0.0338 259 ASP A O   
2057 C CB  . ASP A 259 ? 0.3913 0.3657 0.2690 0.0168  0.0136  -0.0624 259 ASP A CB  
2058 C CG  . ASP A 259 ? 0.4563 0.4352 0.3273 0.0176  0.0030  -0.0735 259 ASP A CG  
2059 O OD1 . ASP A 259 ? 0.4407 0.4263 0.3113 0.0189  -0.0062 -0.0720 259 ASP A OD1 
2060 O OD2 . ASP A 259 ? 0.5072 0.4831 0.3738 0.0175  0.0032  -0.0845 259 ASP A OD2 
2061 N N   . SER A 260 ? 0.4176 0.3839 0.3189 0.0124  0.0243  -0.0401 260 SER A N   
2062 C CA  . SER A 260 ? 0.4382 0.3996 0.3419 0.0101  0.0322  -0.0318 260 SER A CA  
2063 C C   . SER A 260 ? 0.4623 0.4173 0.3678 0.0108  0.0291  -0.0236 260 SER A C   
2064 O O   . SER A 260 ? 0.4743 0.4220 0.3749 0.0089  0.0338  -0.0155 260 SER A O   
2065 C CB  . SER A 260 ? 0.4892 0.4522 0.4103 0.0065  0.0369  -0.0352 260 SER A CB  
2066 O OG  . SER A 260 ? 0.5134 0.4798 0.4326 0.0075  0.0404  -0.0428 260 SER A OG  
2067 N N   . PHE A 261 ? 0.3881 0.3457 0.3008 0.0133  0.0215  -0.0256 261 PHE A N   
2068 C CA  . PHE A 261 ? 0.3784 0.3297 0.2933 0.0160  0.0188  -0.0197 261 PHE A CA  
2069 C C   . PHE A 261 ? 0.4203 0.3728 0.3263 0.0235  0.0106  -0.0177 261 PHE A C   
2070 O O   . PHE A 261 ? 0.3927 0.3352 0.2940 0.0278  0.0088  -0.0114 261 PHE A O   
2071 C CB  . PHE A 261 ? 0.3197 0.2749 0.2532 0.0143  0.0184  -0.0228 261 PHE A CB  
2072 C CG  . PHE A 261 ? 0.3403 0.2939 0.2828 0.0085  0.0251  -0.0236 261 PHE A CG  
2073 C CD1 . PHE A 261 ? 0.3438 0.3039 0.2949 0.0057  0.0269  -0.0295 261 PHE A CD1 
2074 C CD2 . PHE A 261 ? 0.3561 0.3010 0.2984 0.0061  0.0287  -0.0185 261 PHE A CD2 
2075 C CE1 . PHE A 261 ? 0.3933 0.3531 0.3526 0.0025  0.0323  -0.0299 261 PHE A CE1 
2076 C CE2 . PHE A 261 ? 0.3693 0.3163 0.3214 0.0013  0.0338  -0.0196 261 PHE A CE2 
2077 C CZ  . PHE A 261 ? 0.3449 0.3002 0.3054 0.0004  0.0355  -0.0250 261 PHE A CZ  
2078 N N   . ILE A 262 ? 0.3190 0.2827 0.2226 0.0257  0.0048  -0.0233 262 ILE A N   
2079 C CA  . ILE A 262 ? 0.3558 0.3251 0.2545 0.0338  -0.0043 -0.0221 262 ILE A CA  
2080 C C   . ILE A 262 ? 0.4419 0.4062 0.3168 0.0384  -0.0066 -0.0176 262 ILE A C   
2081 O O   . ILE A 262 ? 0.5066 0.4613 0.3693 0.0453  -0.0091 -0.0092 262 ILE A O   
2082 C CB  . ILE A 262 ? 0.3553 0.3436 0.2690 0.0329  -0.0111 -0.0308 262 ILE A CB  
2083 C CG1 . ILE A 262 ? 0.3881 0.3809 0.3231 0.0284  -0.0076 -0.0329 262 ILE A CG1 
2084 C CG2 . ILE A 262 ? 0.3936 0.3922 0.3049 0.0422  -0.0211 -0.0297 262 ILE A CG2 
2085 C CD1 . ILE A 262 ? 0.3850 0.3754 0.3243 0.0348  -0.0079 -0.0279 262 ILE A CD1 
2086 N N   . GLU A 263 ? 0.4364 0.4059 0.3030 0.0355  -0.0056 -0.0231 263 GLU A N   
2087 C CA  . GLU A 263 ? 0.6272 0.5934 0.4681 0.0402  -0.0068 -0.0189 263 GLU A CA  
2088 C C   . GLU A 263 ? 0.7136 0.6863 0.5479 0.0365  -0.0044 -0.0283 263 GLU A C   
2089 O O   . GLU A 263 ? 0.7191 0.6994 0.5686 0.0320  -0.0062 -0.0390 263 GLU A O   
2090 C CB  . GLU A 263 ? 0.7002 0.6732 0.5320 0.0498  -0.0190 -0.0177 263 GLU A CB  
2091 N N   . ASP A 264 ? 0.8446 0.8131 0.6548 0.0390  -0.0001 -0.0239 264 ASP A N   
2092 C CA  . ASP A 264 ? 0.9632 0.9376 0.7630 0.0380  0.0025  -0.0336 264 ASP A CA  
2093 C C   . ASP A 264 ? 1.0243 0.9976 0.7920 0.0442  0.0037  -0.0277 264 ASP A C   
2094 O O   . ASP A 264 ? 1.0620 1.0429 0.8146 0.0496  -0.0055 -0.0345 264 ASP A O   
2095 C CB  . ASP A 264 ? 1.0164 0.9881 0.8280 0.0315  0.0146  -0.0360 264 ASP A CB  
2096 C CG  . ASP A 264 ? 1.0899 1.0670 0.8948 0.0319  0.0162  -0.0493 264 ASP A CG  
2097 O OD1 . ASP A 264 ? 1.1063 1.0886 0.9005 0.0355  0.0066  -0.0585 264 ASP A OD1 
2098 O OD2 . ASP A 264 ? 1.1042 1.0806 0.9149 0.0294  0.0265  -0.0513 264 ASP A OD2 
# 
