data_8QG2
# 
_entry.id   8QG2 
# 
_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   8QG2         pdb_00008qg2 10.2210/pdb8qg2/pdb 
WWPDB D_1292132948 ?            ?                   
# 
_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                        8QG2 
_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         Labesse 
_pdbx_contact_author.name_last          Gilles 
_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 0000-0003-1320-8663 
'Labesse, G.' 2 0000-0002-6861-3300 
'Lionne, C.'  3 0000-0002-6348-5311 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a di-adenosine derivative' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gelin, M.'      1 ? 
primary 'Labesse, G.'    2 ? 
primary 'Clement, D.'    3 ? 
primary 'Pochet, S.'     4 ? 
primary 'Lionne, C.'     5 ? 
primary 'Leseigneur, C.' 6 ? 
primary 'Huteau, V.'     7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'NAD kinase 1' 31045.279 1   2.7.1.23 ? ? ? 
2 non-polymer syn 'CITRIC ACID' 192.124   1   ?        ? ? ? 
3 non-polymer syn 
;~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-2-(2-azanyl-2-oxidanylidene-ethyl)benzamide
;
730.687   1   ?        ? ? ? 
4 water       nat water 18.015    101 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ATP-dependent NAD kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 
;~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-2-(2-azanyl-2-oxidanylidene-ethyl)benzamide
;
V2Y 
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 
V2Y non-polymer         . 
;~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-2-(2-azanyl-2-oxidanylidene-ethyl)benzamide
;
? 'C32 H34 N12 O9' 730.687 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ASP 264 264 ?   ?   ?   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        V2Y 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V2Y 
_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 V2Y 1   302 1   V2Y DRG A . 
D 4 HOH 1   401 20  HOH HOH A . 
D 4 HOH 2   402 99  HOH HOH A . 
D 4 HOH 3   403 37  HOH HOH A . 
D 4 HOH 4   404 59  HOH HOH A . 
D 4 HOH 5   405 3   HOH HOH A . 
D 4 HOH 6   406 129 HOH HOH A . 
D 4 HOH 7   407 40  HOH HOH A . 
D 4 HOH 8   408 45  HOH HOH A . 
D 4 HOH 9   409 34  HOH HOH A . 
D 4 HOH 10  410 70  HOH HOH A . 
D 4 HOH 11  411 72  HOH HOH A . 
D 4 HOH 12  412 113 HOH HOH A . 
D 4 HOH 13  413 17  HOH HOH A . 
D 4 HOH 14  414 115 HOH HOH A . 
D 4 HOH 15  415 14  HOH HOH A . 
D 4 HOH 16  416 52  HOH HOH A . 
D 4 HOH 17  417 41  HOH HOH A . 
D 4 HOH 18  418 46  HOH HOH A . 
D 4 HOH 19  419 58  HOH HOH A . 
D 4 HOH 20  420 30  HOH HOH A . 
D 4 HOH 21  421 2   HOH HOH A . 
D 4 HOH 22  422 29  HOH HOH A . 
D 4 HOH 23  423 116 HOH HOH A . 
D 4 HOH 24  424 35  HOH HOH A . 
D 4 HOH 25  425 18  HOH HOH A . 
D 4 HOH 26  426 27  HOH HOH A . 
D 4 HOH 27  427 15  HOH HOH A . 
D 4 HOH 28  428 5   HOH HOH A . 
D 4 HOH 29  429 6   HOH HOH A . 
D 4 HOH 30  430 31  HOH HOH A . 
D 4 HOH 31  431 19  HOH HOH A . 
D 4 HOH 32  432 25  HOH HOH A . 
D 4 HOH 33  433 97  HOH HOH A . 
D 4 HOH 34  434 57  HOH HOH A . 
D 4 HOH 35  435 36  HOH HOH A . 
D 4 HOH 36  436 93  HOH HOH A . 
D 4 HOH 37  437 53  HOH HOH A . 
D 4 HOH 38  438 1   HOH HOH A . 
D 4 HOH 39  439 24  HOH HOH A . 
D 4 HOH 40  440 16  HOH HOH A . 
D 4 HOH 41  441 121 HOH HOH A . 
D 4 HOH 42  442 39  HOH HOH A . 
D 4 HOH 43  443 4   HOH HOH A . 
D 4 HOH 44  444 9   HOH HOH A . 
D 4 HOH 45  445 7   HOH HOH A . 
D 4 HOH 46  446 22  HOH HOH A . 
D 4 HOH 47  447 32  HOH HOH A . 
D 4 HOH 48  448 23  HOH HOH A . 
D 4 HOH 49  449 104 HOH HOH A . 
D 4 HOH 50  450 103 HOH HOH A . 
D 4 HOH 51  451 26  HOH HOH A . 
D 4 HOH 52  452 92  HOH HOH A . 
D 4 HOH 53  453 61  HOH HOH A . 
D 4 HOH 54  454 51  HOH HOH A . 
D 4 HOH 55  455 8   HOH HOH A . 
D 4 HOH 56  456 63  HOH HOH A . 
D 4 HOH 57  457 78  HOH HOH A . 
D 4 HOH 58  458 105 HOH HOH A . 
D 4 HOH 59  459 12  HOH HOH A . 
D 4 HOH 60  460 13  HOH HOH A . 
D 4 HOH 61  461 10  HOH HOH A . 
D 4 HOH 62  462 49  HOH HOH A . 
D 4 HOH 63  463 64  HOH HOH A . 
D 4 HOH 64  464 28  HOH HOH A . 
D 4 HOH 65  465 89  HOH HOH A . 
D 4 HOH 66  466 66  HOH HOH A . 
D 4 HOH 67  467 44  HOH HOH A . 
D 4 HOH 68  468 21  HOH HOH A . 
D 4 HOH 69  469 77  HOH HOH A . 
D 4 HOH 70  470 86  HOH HOH A . 
D 4 HOH 71  471 43  HOH HOH A . 
D 4 HOH 72  472 33  HOH HOH A . 
D 4 HOH 73  473 123 HOH HOH A . 
D 4 HOH 74  474 55  HOH HOH A . 
D 4 HOH 75  475 38  HOH HOH A . 
D 4 HOH 76  476 84  HOH HOH A . 
D 4 HOH 77  477 80  HOH HOH A . 
D 4 HOH 78  478 11  HOH HOH A . 
D 4 HOH 79  479 65  HOH HOH A . 
D 4 HOH 80  480 100 HOH HOH A . 
D 4 HOH 81  481 95  HOH HOH A . 
D 4 HOH 82  482 98  HOH HOH A . 
D 4 HOH 83  483 50  HOH HOH A . 
D 4 HOH 84  484 42  HOH HOH A . 
D 4 HOH 85  485 87  HOH HOH A . 
D 4 HOH 86  486 128 HOH HOH A . 
D 4 HOH 87  487 71  HOH HOH A . 
D 4 HOH 88  488 88  HOH HOH A . 
D 4 HOH 89  489 47  HOH HOH A . 
D 4 HOH 90  490 85  HOH HOH A . 
D 4 HOH 91  491 114 HOH HOH A . 
D 4 HOH 92  492 75  HOH HOH A . 
D 4 HOH 93  493 60  HOH HOH A . 
D 4 HOH 94  494 107 HOH HOH A . 
D 4 HOH 95  495 101 HOH HOH A . 
D 4 HOH 96  496 48  HOH HOH A . 
D 4 HOH 97  497 56  HOH HOH A . 
D 4 HOH 98  498 83  HOH HOH A . 
D 4 HOH 99  499 54  HOH HOH A . 
D 4 HOH 100 500 126 HOH HOH A . 
D 4 HOH 101 501 112 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
6  1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
7  1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
8  1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
9  1 Y 1 A ARG 249 ? CG  ? A ARG 249 CG  
10 1 Y 1 A ARG 249 ? CD  ? A ARG 249 CD  
11 1 Y 1 A ARG 249 ? NE  ? A ARG 249 NE  
12 1 Y 1 A ARG 249 ? CZ  ? A ARG 249 CZ  
13 1 Y 1 A ARG 249 ? NH1 ? A ARG 249 NH1 
14 1 Y 1 A ARG 249 ? NH2 ? A ARG 249 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.13_2998 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .         2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 0.2.14    3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.28      4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QG2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.691 
_cell.length_a_esd                 ? 
_cell.length_b                     75.017 
_cell.length_b_esd                 ? 
_cell.length_c                     118.304 
_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                         8QG2 
_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                   8QG2 
_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          45.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-02-16 
_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   0.96863 
_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        0.96863 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          28.800 
_reflns.entry_id                                       8QG2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.830 
_reflns.d_resolution_low                               48.105 
_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                                     24799 
_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                           99.300 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.700 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.500 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.059 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
1.830 1.890  ? ? 6773 ? ? ? 2346 ? ? ? ? ? ? ? ? ? ? ? 2.900 ? ? 1.600  0.809 0.453 ? 1 1 0.760 ? ? 98.000 ? 0.665 ? ? ? ? ? ? ? ? 
? 
7.090 48.100 ? ? 2128 ? ? ? 481  ? ? ? ? ? ? ? ? ? ? ? 4.400 ? ? 46.300 0.028 0.013 ? 2 1 0.999 ? ? 98.300 ? 0.025 ? ? ? ? ? ? ? ? 
? 
# 
_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                                97.790 
_refine.B_iso_mean                               39.4835 
_refine.B_iso_min                                18.710 
_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                                 8QG2 
_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                            1.8300 
_refine.ls_d_res_low                             48.1050 
_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                     24792 
_refine.ls_number_reflns_R_free                  1265 
_refine.ls_number_reflns_R_work                  23527 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.2000 
_refine.ls_percent_reflns_R_free                 5.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1843 
_refine.ls_R_factor_R_free                       0.2133 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1828 
_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                          1.330 
_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               THROUGHOUT 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.5200 
_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                            0.2000 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.8300 
_refine_hist.d_res_low                        48.1050 
_refine_hist.number_atoms_solvent             101 
_refine_hist.number_atoms_total               2256 
_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       263 
_refine_hist.pdbx_B_iso_mean_ligand           33.25 
_refine_hist.pdbx_B_iso_mean_solvent          42.42 
_refine_hist.pdbx_number_atoms_protein        2089 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         66 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' 1.8301 1.9034 . . 155 2495 98.0000  . . . 0.0000 0.2872 . . . . . . . . . . . 0.3294 
'X-RAY DIFFRACTION' 1.9034 1.9900 . . 124 2588 99.0000  . . . 0.0000 0.2267 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 1.9900 2.0949 . . 142 2606 99.0000  . . . 0.0000 0.1943 . . . . . . . . . . . 0.2350 
'X-RAY DIFFRACTION' 2.0949 2.2261 . . 131 2586 99.0000  . . . 0.0000 0.1788 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 2.2261 2.3980 . . 151 2612 100.0000 . . . 0.0000 0.1718 . . . . . . . . . . . 0.2169 
'X-RAY DIFFRACTION' 2.3980 2.6393 . . 151 2598 100.0000 . . . 0.0000 0.1778 . . . . . . . . . . . 0.2373 
'X-RAY DIFFRACTION' 2.6393 3.0212 . . 140 2621 99.0000  . . . 0.0000 0.1859 . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 3.0212 3.8062 . . 128 2652 99.0000  . . . 0.0000 0.1732 . . . . . . . . . . . 0.1924 
'X-RAY DIFFRACTION' 3.8062 48.105 . . 143 2769 99.0000  . . . 0.0000 0.1761 . . . . . . . . . . . 0.1928 
# 
_struct.entry_id                     8QG2 
_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        8QG2 
_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              8QG2 
_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 8QG2 LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QG2 GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QG2 HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QG2 HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QG2 HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QG2 HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QG2 HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QG2 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)' 11130 ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  41120 ? 
# 
_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                ? 
# 
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 62.6910000000 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 62.6910000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLU A 26  ? ASP A 10  GLU A 26  1 ? 17 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 GLU A 56  ? ILE A 62  ? GLU A 56  ILE A 62  5 ? 7  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 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 PHE A 201 ? O PHE A 201 N MET A 179 ? N MET A 179 
AA3 2 3 O THR A 182 ? O THR A 182 N CYS A 153 ? N CYS A 153 
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 PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QG2 
_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 ASN A 122 ? ? -98.54  -67.18  
2 1 ALA A 162 ? ? -106.69 -129.54 
3 1 ASN A 189 ? ? -155.83 -158.66 
4 1 HIS A 204 ? ? 73.92   -8.82   
5 1 ASN A 213 ? ? -130.74 -72.88  
6 1 ASP A 222 ? ? 54.25   -131.65 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 437 ? D HOH . 
2 1 A HOH 499 ? D HOH . 
# 
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 12.5702 23.8566 23.0870 0.4548 ? 0.0950 ? 0.0508 ? 0.4181 ? -0.0664 ? 0.3450 ? 2.4047 ? -0.1864 ? 
-1.3110 ? 0.6727 ? 0.7924 ? 3.0839 ? -0.0089 ? -0.2889 ? 0.2155 ? 0.1361  ? 0.0322  ? 0.0106 ? -0.2666 ? 0.0644  ? 0.0175 ? 
2 'X-RAY DIFFRACTION' ? refined 18.7478 14.7772 -0.9072 0.1883 ? 0.0378 ? 0.0119 ? 0.2403 ? -0.0023 ? 0.2528 ? 1.0199 ? -0.2045 ? 
-0.1667 ? 1.5527 ? 0.2041 ? 2.1070 ? 0.0419  ? 0.0128  ? 0.1285 ? -0.0416 ? -0.0635 ? 0.2482 ? -0.1684 ? -0.3600 ? 0.0273 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 1  ? ? ? A 91  ? ? 
;chain 'A' and (resid 1 through 91 )
;
2 'X-RAY DIFFRACTION' 2 ? ? A 92 ? ? ? A 263 ? ? 
;chain 'A' and (resid 92 through 263 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASP 264 ? A ASP 264 
2 1 Y 1 A LEU 265 ? A LEU 265 
3 1 Y 1 A GLU 266 ? A GLU 266 
4 1 Y 1 A HIS 267 ? A HIS 267 
5 1 Y 1 A HIS 268 ? A HIS 268 
6 1 Y 1 A HIS 269 ? A HIS 269 
7 1 Y 1 A HIS 270 ? A HIS 270 
8 1 Y 1 A HIS 271 ? A HIS 271 
9 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 
V2Y C1   C Y N 393 
V2Y C2   C Y N 394 
V2Y C3   C Y N 395 
V2Y C4   C Y N 396 
V2Y N1   N Y N 397 
V2Y N2   N Y N 398 
V2Y C5   C N R 399 
V2Y C6   C Y N 400 
V2Y C7   C N R 401 
V2Y C8   C N S 402 
V2Y C9   C N R 403 
V2Y C10  C N N 404 
V2Y C11  C N N 405 
V2Y C12  C N N 406 
V2Y C13  C Y N 407 
V2Y C14  C Y N 408 
V2Y C15  C Y N 409 
V2Y C16  C Y N 410 
V2Y C17  C Y N 411 
V2Y C18  C Y N 412 
V2Y C19  C N N 413 
V2Y C20  C N N 414 
V2Y C21  C N R 415 
V2Y C22  C N R 416 
V2Y C23  C N R 417 
V2Y C24  C N S 418 
V2Y C25  C N N 419 
V2Y C26  C N N 420 
V2Y C27  C N N 421 
V2Y C28  C Y N 422 
V2Y C29  C Y N 423 
V2Y C30  C Y N 424 
V2Y C31  C Y N 425 
V2Y C32  C Y N 426 
V2Y N3   N N N 427 
V2Y N4   N Y N 428 
V2Y N5   N Y N 429 
V2Y N6   N N N 430 
V2Y N7   N N N 431 
V2Y N8   N Y N 432 
V2Y N9   N Y N 433 
V2Y N10  N Y N 434 
V2Y N11  N Y N 435 
V2Y N12  N N N 436 
V2Y O1   O N N 437 
V2Y O2   O N N 438 
V2Y O3   O N N 439 
V2Y O4   O N N 440 
V2Y O5   O N N 441 
V2Y O6   O N N 442 
V2Y O7   O N N 443 
V2Y O8   O N N 444 
V2Y O9   O N N 445 
V2Y H1   H N N 446 
V2Y H2   H N N 447 
V2Y H3   H N N 448 
V2Y H4   H N N 449 
V2Y H5   H N N 450 
V2Y H6   H N N 451 
V2Y H7   H N N 452 
V2Y H8   H N N 453 
V2Y H9   H N N 454 
V2Y H10  H N N 455 
V2Y H11  H N N 456 
V2Y H12  H N N 457 
V2Y H13  H N N 458 
V2Y H14  H N N 459 
V2Y H15  H N N 460 
V2Y H16  H N N 461 
V2Y H17  H N N 462 
V2Y H18  H N N 463 
V2Y H19  H N N 464 
V2Y H20  H N N 465 
V2Y H21  H N N 466 
V2Y H22  H N N 467 
V2Y H23  H N N 468 
V2Y H24  H N N 469 
V2Y H25  H N N 470 
V2Y H26  H N N 471 
V2Y H27  H N N 472 
V2Y H28  H N N 473 
V2Y H29  H N N 474 
V2Y H30  H N N 475 
V2Y H31  H N N 476 
V2Y H32  H N N 477 
V2Y H33  H N N 478 
V2Y H34  H N N 479 
VAL N    N N N 480 
VAL CA   C N S 481 
VAL C    C N N 482 
VAL O    O N N 483 
VAL CB   C N N 484 
VAL CG1  C N N 485 
VAL CG2  C N N 486 
VAL OXT  O N N 487 
VAL H    H N N 488 
VAL H2   H N N 489 
VAL HA   H N N 490 
VAL HB   H N N 491 
VAL HG11 H N N 492 
VAL HG12 H N N 493 
VAL HG13 H N N 494 
VAL HG21 H N N 495 
VAL HG22 H N N 496 
VAL HG23 H N N 497 
VAL HXT  H N N 498 
# 
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 
V2Y N12 C32  sing N N 378 
V2Y N9  C28  doub Y N 379 
V2Y N9  C29  sing Y N 380 
V2Y C32 C29  doub Y N 381 
V2Y C32 N11  sing Y N 382 
V2Y C28 N8   sing Y N 383 
V2Y C29 C30  sing Y N 384 
V2Y C7  O1   sing N N 385 
V2Y C7  C8   sing N N 386 
V2Y C7  C5   sing N N 387 
V2Y N11 C31  doub Y N 388 
V2Y O2  C8   sing N N 389 
V2Y N8  C30  sing Y N 390 
V2Y N8  C5   sing N N 391 
V2Y C30 N10  doub Y N 392 
V2Y C8  C9   sing N N 393 
V2Y C31 N10  sing Y N 394 
V2Y C5  O3   sing N N 395 
V2Y C15 C14  doub Y N 396 
V2Y C15 C16  sing Y N 397 
V2Y C14 C13  sing Y N 398 
V2Y O3  C9   sing N N 399 
V2Y C16 C17  doub Y N 400 
V2Y C9  C10  sing N N 401 
V2Y C13 C12  sing N N 402 
V2Y C13 C18  doub Y N 403 
V2Y C10 O4   sing N N 404 
V2Y C12 C11  sing N N 405 
V2Y C17 C18  sing Y N 406 
V2Y N3  C3   sing N N 407 
V2Y C18 C19  sing N N 408 
V2Y C3  N1   doub Y N 409 
V2Y C3  C2   sing Y N 410 
V2Y O4  C27  sing N N 411 
V2Y N1  C6   sing Y N 412 
V2Y C11 N6   sing N N 413 
V2Y C11 O5   doub N N 414 
V2Y N4  C2   sing Y N 415 
V2Y N4  C4   doub Y N 416 
V2Y C2  C1   doub Y N 417 
V2Y C19 N7   sing N N 418 
V2Y C19 O6   doub N N 419 
V2Y N7  C20  sing N N 420 
V2Y C4  C25  sing N N 421 
V2Y C4  N5   sing Y N 422 
V2Y C6  N2   doub Y N 423 
V2Y C25 C26  trip N N 424 
V2Y C26 C27  sing N N 425 
V2Y C1  N2   sing Y N 426 
V2Y C1  N5   sing Y N 427 
V2Y N5  C22  sing N N 428 
V2Y O7  C22  sing N N 429 
V2Y O7  C21  sing N N 430 
V2Y C20 C21  sing N N 431 
V2Y C22 C23  sing N N 432 
V2Y C21 C24  sing N N 433 
V2Y C23 C24  sing N N 434 
V2Y C23 O8   sing N N 435 
V2Y C24 O9   sing N N 436 
V2Y C5  H1   sing N N 437 
V2Y C6  H2   sing N N 438 
V2Y C7  H3   sing N N 439 
V2Y C8  H4   sing N N 440 
V2Y C9  H5   sing N N 441 
V2Y C10 H6   sing N N 442 
V2Y C10 H7   sing N N 443 
V2Y C12 H8   sing N N 444 
V2Y C12 H9   sing N N 445 
V2Y C14 H10  sing N N 446 
V2Y C15 H11  sing N N 447 
V2Y C16 H12  sing N N 448 
V2Y C17 H13  sing N N 449 
V2Y C20 H14  sing N N 450 
V2Y C20 H15  sing N N 451 
V2Y C21 H16  sing N N 452 
V2Y C22 H17  sing N N 453 
V2Y C23 H18  sing N N 454 
V2Y C24 H19  sing N N 455 
V2Y C27 H20  sing N N 456 
V2Y C27 H21  sing N N 457 
V2Y C28 H22  sing N N 458 
V2Y C31 H23  sing N N 459 
V2Y N3  H24  sing N N 460 
V2Y N3  H25  sing N N 461 
V2Y N6  H26  sing N N 462 
V2Y N6  H27  sing N N 463 
V2Y N7  H28  sing N N 464 
V2Y N12 H29  sing N N 465 
V2Y N12 H30  sing N N 466 
V2Y O1  H31  sing N N 467 
V2Y O2  H32  sing N N 468 
V2Y O8  H33  sing N N 469 
V2Y O9  H34  sing N N 470 
VAL N   CA   sing N N 471 
VAL N   H    sing N N 472 
VAL N   H2   sing N N 473 
VAL CA  C    sing N N 474 
VAL CA  CB   sing N N 475 
VAL CA  HA   sing N N 476 
VAL C   O    doub N N 477 
VAL C   OXT  sing N N 478 
VAL CB  CG1  sing N N 479 
VAL CB  CG2  sing N N 480 
VAL CB  HB   sing N N 481 
VAL CG1 HG11 sing N N 482 
VAL CG1 HG12 sing N N 483 
VAL CG1 HG13 sing N N 484 
VAL CG2 HG21 sing N N 485 
VAL CG2 HG22 sing N N 486 
VAL CG2 HG23 sing N N 487 
VAL OXT HXT  sing N N 488 
# 
_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.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8A9V 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QG2 
_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]   0.015951 
_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]   0.013330 
_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]   0.008453 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_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   ? 11.101 36.629  25.574  1.00 71.37 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.600 36.577  24.206  1.00 69.18 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.508  35.527  24.099  1.00 62.72 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.280  34.777  25.029  1.00 59.93 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.739 36.267  23.244  1.00 71.98 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.839 37.313  23.248  0.77 76.08 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.162 36.950  22.076  0.73 77.68 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 14.982 35.590  22.889  0.91 76.78 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 8.819  35.469  22.961  1.00 59.36 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 7.896  34.360  22.759  1.00 54.37 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.700  33.077  22.565  1.00 46.93 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.747  33.072  21.912  1.00 44.06 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 6.979  34.657  21.571  1.00 55.07 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.009  35.825  21.852  1.00 58.59 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.338  36.300  20.558  0.87 60.96 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.332  37.413  20.804  1.00 64.10 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.166  36.910  21.573  0.97 64.87 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.268  32.004  23.222  1.00 42.96 ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 8.945  30.718  23.083  1.00 39.68 ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.901  29.620  23.123  1.00 38.53 ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.800  29.816  23.635  1.00 40.77 ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 9.983  30.471  24.198  1.00 39.80 ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.341  30.086  25.537  1.00 41.46 ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.879  31.062  26.410  1.00 43.82 ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.194  28.747  25.915  1.00 39.25 ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.273  30.727  27.637  1.00 42.54 ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.585  28.404  27.147  1.00 40.40 ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.133  29.402  27.990  1.00 41.13 ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.536  29.076  29.190  1.00 40.76 ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.263  28.436  22.620  1.00 36.73 ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.422  27.278  22.878  1.00 38.09 ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.312  26.063  23.083  1.00 35.57 ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.497  26.092  22.775  1.00 35.70 ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.398  27.030  21.767  1.00 41.43 ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.004  26.582  20.470  1.00 40.04 ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.237  24.797  20.404  1.00 42.42 ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.530  24.222  20.462  1.00 43.03 ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.740  25.000  23.646  1.00 34.85 ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.489  23.775  23.915  1.00 33.69 ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.661  22.603  23.421  1.00 35.71 ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.499  22.460  23.816  1.00 36.22 ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.818  23.591  25.406  1.00 34.71 ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.512  24.823  25.984  1.00 33.76 ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.697  22.351  25.596  1.00 33.62 ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.961  24.622  27.466  1.00 34.39 ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.248  21.773  22.551  1.00 34.02 ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.596  20.564  22.077  1.00 36.75 ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.223  19.385  22.808  1.00 39.74 ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.405  19.422  23.143  1.00 43.90 ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 7.740  20.431  20.552  1.00 40.05 ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 7.060  19.253  20.103  1.00 44.65 ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 9.199  20.361  20.164  1.00 35.15 ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.420  18.374  23.130  1.00 39.44 ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 7.894  17.227  23.897  1.00 36.96 ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.701  15.940  23.106  1.00 37.02 ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.744  15.814  22.346  1.00 40.67 ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.149  17.109  25.231  1.00 38.29 ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.473  15.882  25.851  1.00 39.62 ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.611  14.973  23.298  1.00 35.58 ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.384  13.641  22.743  1.00 40.46 ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.114  13.011  23.314  1.00 41.32 ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.488  12.170  22.664  1.00 41.59 ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.605  12.760  23.020  1.00 43.24 ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.466  11.282  22.707  1.00 46.22 ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.620 10.515  23.336  1.00 48.59 ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.843 9.174   22.667  0.79 52.60 ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 11.440 9.361   21.329  0.72 53.95 ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.702  13.411  24.513  1.00 41.39 ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.491  12.883  25.095  1.00 41.08 ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.700  11.707  26.013  1.00 44.05 ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.715  11.138  26.501  1.00 45.95 ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.937  11.306  26.254  1.00 44.29 ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.113  10.362  27.324  1.00 47.06 ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.185  11.118  28.648  1.00 47.45 ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.213  12.355  28.704  1.00 43.48 ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.339  9.475   27.086  1.00 51.08 ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.627  10.255  26.983  1.00 52.89 ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.578  11.495  26.963  0.87 52.41 ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.697 9.613   26.900  0.88 55.11 ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.167  10.355  29.733  1.00 49.51 ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.112  10.957  31.053  1.00 51.66 ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.283  11.903  31.285  1.00 49.21 ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.097  13.048  31.711  1.00 49.10 ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.093  9.836   32.075  1.00 58.48 ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 6.947  10.245  33.448  1.00 64.54 ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 6.759  9.028   34.302  0.67 70.55 ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.776  7.908   33.744  1.00 72.73 ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 6.590  9.186   35.517  0.96 73.64 ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.496  11.431  31.010  1.00 48.83 ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.709 12.220  31.211  1.00 48.56 ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.651 13.545  30.460  1.00 44.66 ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.959 14.610  31.016  1.00 41.31 ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.920 11.397  30.761  1.00 51.31 ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.276 12.028  31.029  0.89 53.59 ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.401 11.054  30.704  1.00 56.35 ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.753 11.740  30.816  0.84 58.55 ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 15.849 12.455  32.124  0.90 62.31 ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.262 13.500  29.185  1.00 45.59 ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.286 14.714  28.380  1.00 41.35 ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.184  15.675  28.800  1.00 41.59 ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.385  16.897  28.798  1.00 41.88 ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.176 14.355  26.896  1.00 39.30 ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.224 13.447  26.545  1.00 39.54 ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 8.016  15.151  29.173  1.00 41.58 ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.925  16.042  29.552  1.00 42.34 ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.245  16.777  30.842  1.00 43.25 ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.913  17.962  30.991  1.00 42.18 ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.623  15.259  29.709  1.00 46.18 ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.942  14.990  28.396  1.00 47.39 ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.463  15.427  27.345  1.00 43.62 ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.873  14.345  28.431  0.84 50.34 ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.879  16.079  31.788  1.00 44.03 ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.201  16.685  33.071  1.00 44.83 ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.261  17.763  32.906  1.00 41.97 ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.131  18.859  33.467  1.00 39.60 ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.656  15.599  34.047  0.90 47.45 ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.499  14.639  34.359  0.80 51.34 ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 7.975  13.442  35.191  0.80 52.86 ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 6.325  15.352  35.068  0.80 52.55 ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.299 17.473  32.119  1.00 39.58 ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.305 18.485  31.807  1.00 40.97 ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.673 19.709  31.158  1.00 37.88 ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 10.986 20.845  31.527  1.00 36.55 ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.391 17.906  30.901  1.00 40.50 ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.667 18.756  30.790  1.00 41.81 ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.249 19.082  32.186  1.00 43.17 ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.705 18.057  29.921  1.00 39.55 ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.743  19.499  30.226  1.00 36.70 ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.072  20.635  29.598  1.00 34.90 ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.310  21.472  30.629  1.00 35.52 ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.431  22.703  30.657  1.00 37.80 ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.142  20.144  28.497  1.00 34.02 ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.183  21.210  28.029  1.00 35.98 ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.349  20.715  26.804  1.00 33.47 ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.407  21.725  26.359  1.00 35.10 ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.238  21.953  26.945  1.00 39.06 ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.870  21.241  28.012  1.00 39.01 ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.440  22.898  26.480  1.00 40.48 ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.512  20.835  31.491  1.00 38.08 ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.780  21.618  32.489  1.00 39.48 ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.731  22.364  33.424  1.00 40.02 ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.448  23.497  33.844  1.00 38.39 ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.832  20.734  33.312  1.00 42.37 ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.597  20.190  32.588  1.00 43.02 ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.724  19.386  33.555  1.00 43.46 ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.800  21.337  31.960  1.00 42.51 ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.855  21.739  33.767  1.00 38.71 ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.800  22.405  34.658  1.00 40.80 ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.474 23.582  33.965  1.00 40.61 ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.707 24.622  34.584  1.00 41.62 ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.849 21.425  35.160  1.00 39.50 ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.431 20.743  36.444  1.00 40.70 ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.488  21.174  37.132  1.00 42.40 ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.117 19.665  36.767  1.00 41.25 ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.808 23.439  32.679  1.00 37.60 ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.379 24.580  31.971  1.00 37.49 ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.365 25.704  31.817  1.00 39.42 ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.715 26.884  31.943  1.00 39.74 ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.917 24.141  30.611  1.00 36.37 ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.182 23.328  30.701  1.00 36.42 ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.852 22.993  29.043  0.80 37.14 ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.532 24.598  28.611  0.50 35.71 ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.098  25.371  31.565  1.00 39.03 ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.092  26.421  31.516  1.00 39.62 ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 8.035  27.157  32.850  1.00 39.17 ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.980  28.390  32.896  1.00 40.00 ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.716  25.849  31.145  1.00 41.06 ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.737  25.278  29.733  1.00 39.47 ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.646  26.938  31.339  1.00 41.98 ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.487  24.523  29.379  1.00 39.28 ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.073  26.418  33.959  1.00 39.61 ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 8.035  27.079  35.265  1.00 42.13 ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.233  28.008  35.433  1.00 43.19 ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.089  29.155  35.866  1.00 43.00 ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.980  26.039  36.389  1.00 41.51 ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.422 27.538  35.051  1.00 43.78 ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.607 28.386  35.107  1.00 45.65 ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.509 29.617  34.219  1.00 44.61 ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.950 30.707  34.604  1.00 45.47 ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.947 29.462  33.011  1.00 42.19 ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.757 30.625  32.144  1.00 43.97 ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.774  31.613  32.749  1.00 47.01 ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.890  32.826  32.517  1.00 50.27 ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.275 30.197  30.753  1.00 40.94 ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.368 29.708  29.852  1.00 45.77 ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.514 30.460  29.650  1.00 48.11 ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.237 28.493  29.189  1.00 43.66 ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.516 29.989  28.792  1.00 48.04 ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.231 28.019  28.362  1.00 45.27 ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.366 28.762  28.155  1.00 46.19 ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.798  31.124  33.522  1.00 42.73 ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.880  32.025  34.194  1.00 46.79 ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.558  32.952  35.173  1.00 50.69 ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 8.013  34.012  35.492  1.00 50.85 ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.747  32.589  35.641  1.00 53.37 ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.517 33.455  36.519  1.00 57.17 ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.224 34.589  35.777  1.00 59.06 ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.854 35.424  36.438  1.00 60.63 ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.531 32.611  37.313  1.00 57.59 ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.903 31.447  38.097  1.00 57.99 ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.884  31.939  39.107  0.52 61.76 ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 8.980  31.166  39.524  1.00 62.50 ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 9.991  33.124  39.481  1.00 65.13 ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.120 34.660  34.440  1.00 57.85 ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.709 35.723  33.621  1.00 60.06 ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.617 36.419  32.792  1.00 65.54 ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.422  36.146  32.930  1.00 67.66 ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.829 35.165  32.719  1.00 58.29 ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.973 34.495  33.478  1.00 56.35 ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.918 33.148  33.811  1.00 52.98 ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 15.095 35.214  33.876  1.00 58.37 ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.949 32.531  34.520  1.00 52.77 ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 16.133 34.606  34.583  1.00 58.63 ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 16.054 33.260  34.897  1.00 57.72 ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 17.069 32.643  35.605  1.00 61.32 ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 11.048 37.337  31.925  1.00 70.44 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.176 38.004  30.951  1.00 73.83 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 10.115 37.159  29.673  1.00 72.63 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.684 37.487  28.626  1.00 71.52 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.687 39.414  30.672  0.70 79.30 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.867  40.144  29.630  0.60 82.41 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 8.642  39.905  29.565  0.60 82.74 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 10.455 40.946  28.868  0.60 84.29 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.421  36.028  29.792  1.00 71.05 ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.344  35.039  28.726  1.00 67.63 ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.909  34.557  28.625  1.00 63.10 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.385  33.948  29.562  1.00 63.34 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.291 33.862  28.982  1.00 68.30 ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.772 34.230  29.012  1.00 69.42 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.483 34.596  27.386  1.00 68.91 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 12.083 33.104  26.477  0.78 67.10 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.299  34.820  27.478  1.00 59.14 ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.908  34.507  27.195  1.00 57.59 ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.816  33.226  26.362  1.00 53.22 ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.508  33.094  25.351  1.00 52.97 ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.294  35.696  26.455  0.80 61.36 ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.929  35.506  25.881  0.70 63.56 ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.490  36.732  25.112  0.60 67.07 ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 4.312  37.663  24.957  0.60 68.85 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.327  36.764  24.666  0.60 68.39 ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 4.979  32.280  26.799  1.00 49.35 ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.730  31.060  26.036  1.00 47.85 ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.774  31.378  24.889  1.00 47.88 ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.685  31.917  25.107  1.00 48.04 ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.145  29.953  26.928  1.00 47.05 ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.187  28.584  26.284  1.00 43.42 ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.295  28.235  25.260  1.00 43.39 ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.149  27.646  26.660  1.00 42.45 ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.365  26.988  24.629  1.00 40.93 ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.220  26.392  26.035  1.00 41.59 ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.322  26.074  25.017  1.00 40.13 ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.380  24.823  24.406  1.00 36.75 ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.185  31.059  23.667  1.00 44.79 ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.338  31.307  22.500  1.00 45.87 ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.734  30.269  21.466  1.00 44.36 ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 4.857  30.318  20.956  1.00 45.00 ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.540  32.734  21.981  0.80 46.37 ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.710  33.055  20.739  0.70 46.63 ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.239  32.139  20.033  0.60 43.61 ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.544  34.260  20.467  0.60 48.38 ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 2.859  29.306  21.183  1.00 44.80 ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.199  28.323  20.162  1.00 48.19 ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.664  28.705  18.788  1.00 48.77 ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.573  27.840  17.909  1.00 50.19 ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.732  26.916  20.570  1.00 49.73 ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.218  26.783  20.648  1.00 53.07 ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.507  27.741  20.286  0.83 53.94 ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.743  25.701  21.071  0.83 52.10 ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.310  29.975  18.584  1.00 48.95 ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.916  30.477  17.271  1.00 51.31 ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.033  31.289  16.623  1.00 50.98 ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.449  30.994  15.510  1.00 48.67 ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.607  31.292  17.347  1.00 54.22 ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.243  31.799  15.963  1.00 55.79 ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.499 30.425  17.873  1.00 55.29 ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.553  32.299  17.314  1.00 52.80 ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.704  33.063  16.833  1.00 53.90 ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.845  33.052  17.847  1.00 50.31 ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.269  34.109  18.326  1.00 50.49 ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.310  34.502  16.513  1.00 61.69 ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.262  34.660  15.435  1.00 67.00 ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.921  36.119  15.185  0.72 71.57 ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 2.719  36.477  14.008  1.00 75.63 ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 2.867  36.904  16.161  1.00 71.39 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.393  31.882  18.178  1.00 48.25 ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.596  31.865  19.015  1.00 46.57 ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.807  32.438  18.289  1.00 45.30 ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.917  32.390  17.057  1.00 45.16 ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.797  30.373  19.321  1.00 44.91 ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.168  29.665  18.178  1.00 45.71 ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 5.977  30.517  17.794  1.00 47.37 ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.723  32.991  19.078  1.00 41.21 ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.064 33.326  18.625  1.00 42.12 ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.062 32.243  18.972  1.00 42.02 ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.154 32.206  18.399  1.00 40.06 ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.529 34.643  19.255  1.00 49.11 ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.867 35.876  18.645  0.74 55.20 ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 10.752 37.041  19.620  0.66 60.67 ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 11.731 37.331  20.335  1.00 62.10 ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 9.674  37.669  19.674  0.73 63.60 ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.710 31.387  19.926  1.00 40.91 ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.548 30.308  20.409  1.00 38.41 ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.698 29.054  20.399  1.00 34.87 ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.577 29.057  20.917  1.00 35.04 ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.054 30.607  21.834  1.00 41.23 ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 13.775 31.938  21.825  1.00 43.27 ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 13.984 29.511  22.325  1.00 40.61 ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 14.959 31.920  20.941  0.38 41.45 ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.228 27.981  19.846  1.00 33.80 ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.523 26.713  19.799  1.00 35.42 ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.464 25.686  20.393  1.00 32.20 ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.558 25.468  19.866  1.00 33.66 ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.101 26.327  18.374  1.00 37.14 ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.660 24.890  18.339  1.00 36.50 ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 9.962  27.242  17.866  1.00 36.89 ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.073 25.110  21.523  1.00 32.83 ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.871 24.129  22.236  1.00 32.89 ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.213 22.780  22.039  1.00 31.41 ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.010 22.628  22.267  1.00 31.34 ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 12.954 24.468  23.736  1.00 34.86 ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.481 25.883  23.937  1.00 36.36 ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.808 23.430  24.473  1.00 35.78 ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.305 26.387  25.371  1.00 37.28 ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 12.989 21.802  21.612  1.00 30.78 ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.481 20.463  21.415  1.00 33.11 ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.095 19.571  22.481  1.00 32.11 ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.303 19.631  22.700  1.00 35.88 ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 12.845 20.004  19.988  1.00 35.88 ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.828 18.618  19.874  1.00 42.07 ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.276 18.745  23.135  1.00 31.43 ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.731 17.849  24.196  1.00 31.54 ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.367 16.421  23.804  1.00 35.08 ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.179 16.067  23.712  1.00 32.46 ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.123 18.199  25.554  1.00 33.73 ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.457 19.649  25.906  1.00 33.81 ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.649 17.211  26.620  1.00 37.62 ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 11.901 20.097  27.249  1.00 33.19 ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.385 15.604  23.573  1.00 34.25 ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.163 14.236  23.154  1.00 35.63 ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.362 13.728  22.408  1.00 37.03 ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.433 13.495  22.990  1.00 37.38 ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.194 13.558  21.098  1.00 31.26 ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.291 13.083  20.310  1.00 31.31 ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.355 13.877  19.021  1.00 30.62 ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.744 14.934  18.895  1.00 30.11 ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.127 13.372  18.077  1.00 30.31 ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.217 14.023  16.776  1.00 30.81 ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 14.888 14.012  16.039  1.00 31.99 ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.620 14.932  15.256  1.00 34.90 ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.293 13.337  15.937  1.00 31.26 ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.704 13.760  16.331  1.00 35.01 ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 18.871 14.850  16.912  1.00 34.07 ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.644 13.004  16.036  1.00 35.46 ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.071 12.964  16.219  1.00 31.96 ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.752 12.954  15.599  1.00 31.89 ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 11.866 14.060  16.121  1.00 32.44 ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.144 14.714  15.354  1.00 30.58 ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 11.905 14.286  17.452  1.00 30.15 ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.177 15.400  18.029  1.00 29.74 ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.653 16.699  17.434  1.00 29.31 ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.845 17.582  17.133  1.00 29.76 ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.367 15.419  19.545  1.00 30.52 ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.278 14.073  20.013  1.00 35.09 ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.298 16.246  20.224  1.00 30.27 ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 12.969 16.844  17.281  1.00 29.13 ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.496 18.096  16.758  1.00 31.25 ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.054 18.300  15.318  1.00 28.80 ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.629 19.397  14.954  1.00 31.11 ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.026 18.148  16.890  1.00 32.07 ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.613 19.466  16.484  1.00 32.18 ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.840 19.743  15.134  1.00 31.03 ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.883 20.439  17.420  1.00 31.15 ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.338 20.955  14.739  1.00 31.55 ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.390 21.649  17.031  1.00 31.60 ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.625 21.915  15.698  1.00 32.13 ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.099 17.243  14.498  1.00 28.72 ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.626 17.365  13.114  1.00 28.76 ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.150 17.746  13.058  1.00 31.98 ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.735 18.527  12.198  1.00 31.76 ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.861 16.059  12.353  1.00 28.81 ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.288 15.714  11.932  0.60 30.10 ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.257 14.298  11.436  0.60 31.54 ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.783 16.630  10.836  0.60 28.58 ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.331 17.223  13.977  1.00 33.01 ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 8.928  17.624  13.946  1.00 34.36 ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.769  19.089  14.334  1.00 32.71 ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 7.917  19.792  13.782  1.00 34.32 ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.095  16.701  14.840  1.00 38.18 ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 7.990  15.439  14.179  1.00 41.04 ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.610  19.579  15.248  1.00 32.17 ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.563  20.992  15.614  1.00 31.09 ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 9.923  21.865  14.426  1.00 31.04 ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.266  22.875  14.157  1.00 34.11 ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.526 21.271  16.774  1.00 30.73 ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 10.991 21.496  13.727  1.00 30.45 ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.409 22.226  12.528  1.00 31.66 ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.275 22.331  11.509  1.00 32.58 ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 9.997  23.412  10.970  1.00 33.52 ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.618 21.517  11.911  1.00 31.19 ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 12.964 21.983  10.532  1.00 33.05 ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.563 23.205  10.324  1.00 34.86 ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.716 21.173  9.450   1.00 29.94 ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.901 23.616  9.031   1.00 33.83 ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 13.030 21.587  8.150   1.00 30.78 ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.633 22.809  7.955   1.00 32.43 ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.609  21.206  11.229  1.00 31.28 ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.547  21.217  10.228  1.00 31.83 ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.282  21.903  10.730  1.00 37.08 ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.530  22.449  9.918   1.00 40.91 ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.252  19.799  9.771   1.00 31.37 ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.311  19.258  8.867   1.00 33.08 ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.456  19.679  7.562   1.00 32.38 ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.323 18.392  9.101   1.00 31.18 ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.488 19.055  7.016   1.00 32.92 ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.044 18.286  7.939   1.00 32.09 ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.013  21.872  12.040  1.00 38.27 ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 5.884  22.642  12.569  1.00 39.74 ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.056  24.125  12.281  1.00 43.27 ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.070  24.831  12.060  1.00 47.38 ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.720  22.403  14.084  0.80 38.09 ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.587  23.196  14.788  0.70 39.44 ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.554  22.948  16.315  0.60 41.09 ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.452  22.313  16.856  0.60 40.26 ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.514  23.454  17.004  0.60 43.62 ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.294  24.619  12.253  1.00 42.22 ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.527  26.051  12.136  1.00 41.47 ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.296  26.414  10.877  1.00 40.61 ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 8.944  27.461  10.826  1.00 40.74 ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.249  26.563  13.377  1.00 40.86 ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.347  26.493  14.580  1.00 41.10 ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.290  27.384  14.724  1.00 42.90 ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.514  25.512  15.533  1.00 38.48 ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.434  27.305  15.805  1.00 43.12 ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.673  25.425  16.623  1.00 41.99 ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.637  26.326  16.759  1.00 43.04 ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.805  26.230  17.845  1.00 42.16 ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.206  25.586  9.838   1.00 41.15 ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.069  25.812  8.684   1.00 43.57 ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.690  27.054  7.894   1.00 45.97 ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.467  27.469  7.028   1.00 47.46 ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.088  24.587  7.765   0.90 42.15 ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.763  24.194  7.174   0.80 43.46 ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.943  23.167  6.068   0.70 45.78 ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 7.519  23.435  4.928   0.60 48.93 ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 8.519  22.099  6.333   0.60 44.42 ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.539  27.664  8.175   1.00 47.17 ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.161  28.894  7.495   1.00 49.64 ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.672  30.151  8.195   1.00 49.21 ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.522  31.247  7.648   1.00 50.11 ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.636  28.953  7.344   1.00 55.05 ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.113  27.847  6.423   1.00 60.83 ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 3.666  28.017  6.037   0.35 67.36 ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 2.895  28.592  6.821   0.86 70.75 ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 3.295  27.575  4.936   0.63 71.11 ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.286  30.027  9.373   1.00 44.83 ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.830  31.169  10.097  1.00 45.63 ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.285 30.924  10.484  1.00 44.36 ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.733 31.314  11.575  1.00 40.55 ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 7.981  31.484  11.331  1.00 48.05 ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.637  32.150  10.985  0.72 52.98 ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.804  32.582  12.216  1.00 56.03 ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.528  33.498  13.098  1.00 58.59 ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.166  33.112  14.204  0.94 58.42 ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.165  31.831  14.557  0.98 57.26 ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.808  33.998  14.957  1.00 58.45 ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.060 30.296  9.582   1.00 39.57 ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.402 29.858  9.955   1.00 39.31 ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.336 31.024  10.205  1.00 42.86 ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.234 30.926  11.049  1.00 44.66 ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.016 28.974  8.873   1.00 38.68 ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.417 27.585  8.757   1.00 37.43 ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.064 26.859  7.570   1.00 34.82 ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.564 26.828  10.074  1.00 35.81 ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.167 32.120  9.478   1.00 44.83 ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 14.083 33.235  9.668   1.00 50.94 ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.837 33.996  10.967  1.00 52.16 ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.659 34.842  11.337  1.00 53.83 ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.974 34.183  8.477   1.00 57.13 ? 60  ASP A CB  1 
ATOM   479  C CG  A ASP A 1 60  ? 15.333 34.731  8.045   0.55 60.10 ? 60  ASP A CG  1 
ATOM   480  C CG  B ASP A 1 60  ? 12.535 34.543  8.174   0.45 57.62 ? 60  ASP A CG  1 
ATOM   481  O OD1 A ASP A 1 60  ? 15.479 35.969  7.972   0.55 62.64 ? 60  ASP A OD1 1 
ATOM   482  O OD1 B ASP A 1 60  ? 11.700 33.614  8.049   0.45 54.78 ? 60  ASP A OD1 1 
ATOM   483  O OD2 A ASP A 1 60  ? 16.262 33.921  7.816   0.55 59.27 ? 60  ASP A OD2 1 
ATOM   484  O OD2 B ASP A 1 60  ? 12.232 35.750  8.097   0.45 61.12 ? 60  ASP A OD2 1 
ATOM   485  N N   . GLU A 1 61  ? 12.741 33.717  11.667  1.00 50.72 ? 61  GLU A N   1 
ATOM   486  C CA  . GLU A 1 61  ? 12.383 34.423  12.890  1.00 53.05 ? 61  GLU A CA  1 
ATOM   487  C C   . GLU A 1 61  ? 12.537 33.563  14.148  1.00 49.53 ? 61  GLU A C   1 
ATOM   488  O O   . GLU A 1 61  ? 12.141 34.001  15.233  1.00 52.12 ? 61  GLU A O   1 
ATOM   489  C CB  . GLU A 1 61  ? 10.949 34.945  12.754  1.00 57.66 ? 61  GLU A CB  1 
ATOM   490  C CG  . GLU A 1 61  ? 10.705 35.621  11.395  1.00 64.09 ? 61  GLU A CG  1 
ATOM   491  C CD  . GLU A 1 61  ? 9.234  35.708  11.015  0.79 67.94 ? 61  GLU A CD  1 
ATOM   492  O OE1 . GLU A 1 61  ? 8.383  35.723  11.935  0.61 68.11 ? 61  GLU A OE1 1 
ATOM   493  O OE2 . GLU A 1 61  ? 8.930  35.756  9.797   0.97 70.03 ? 61  GLU A OE2 1 
ATOM   494  N N   . ILE A 1 62  ? 13.130 32.367  14.043  1.00 44.87 ? 62  ILE A N   1 
ATOM   495  C CA  . ILE A 1 62  ? 13.170 31.387  15.130  1.00 41.73 ? 62  ILE A CA  1 
ATOM   496  C C   . ILE A 1 62  ? 14.594 30.894  15.338  1.00 39.90 ? 62  ILE A C   1 
ATOM   497  O O   . ILE A 1 62  ? 15.305 30.601  14.371  1.00 37.22 ? 62  ILE A O   1 
ATOM   498  C CB  . ILE A 1 62  ? 12.253 30.178  14.839  1.00 38.96 ? 62  ILE A CB  1 
ATOM   499  C CG1 . ILE A 1 62  ? 10.789 30.578  14.888  1.00 39.97 ? 62  ILE A CG1 1 
ATOM   500  C CG2 . ILE A 1 62  ? 12.483 29.042  15.831  1.00 38.43 ? 62  ILE A CG2 1 
ATOM   501  C CD1 . ILE A 1 62  ? 9.878  29.431  14.512  1.00 40.36 ? 62  ILE A CD1 1 
ATOM   502  N N   . ALA A 1 63  ? 14.994 30.758  16.607  1.00 38.80 ? 63  ALA A N   1 
ATOM   503  C CA  . ALA A 1 63  ? 16.199 30.028  16.974  1.00 37.61 ? 63  ALA A CA  1 
ATOM   504  C C   . ALA A 1 63  ? 15.787 28.735  17.668  1.00 36.56 ? 63  ALA A C   1 
ATOM   505  O O   . ALA A 1 63  ? 15.069 28.769  18.680  1.00 36.57 ? 63  ALA A O   1 
ATOM   506  C CB  . ALA A 1 63  ? 17.098 30.868  17.880  1.00 41.12 ? 63  ALA A CB  1 
ATOM   507  N N   . PHE A 1 64  ? 16.235 27.608  17.120  1.00 35.00 ? 64  PHE A N   1 
ATOM   508  C CA  . PHE A 1 64  ? 15.906 26.279  17.619  1.00 34.27 ? 64  PHE A CA  1 
ATOM   509  C C   . PHE A 1 64  ? 16.949 25.781  18.614  1.00 35.93 ? 64  PHE A C   1 
ATOM   510  O O   . PHE A 1 64  ? 18.136 26.098  18.497  1.00 35.15 ? 64  PHE A O   1 
ATOM   511  C CB  . PHE A 1 64  ? 15.827 25.284  16.456  1.00 34.05 ? 64  PHE A CB  1 
ATOM   512  C CG  . PHE A 1 64  ? 14.649 25.468  15.574  1.00 31.41 ? 64  PHE A CG  1 
ATOM   513  C CD1 . PHE A 1 64  ? 13.473 24.808  15.849  1.00 32.12 ? 64  PHE A CD1 1 
ATOM   514  C CD2 . PHE A 1 64  ? 14.726 26.264  14.429  1.00 31.98 ? 64  PHE A CD2 1 
ATOM   515  C CE1 . PHE A 1 64  ? 12.365 24.955  15.024  1.00 32.88 ? 64  PHE A CE1 1 
ATOM   516  C CE2 . PHE A 1 64  ? 13.627 26.418  13.603  1.00 33.98 ? 64  PHE A CE2 1 
ATOM   517  C CZ  . PHE A 1 64  ? 12.437 25.749  13.902  1.00 34.34 ? 64  PHE A CZ  1 
ATOM   518  N N   . ILE A 1 65  ? 16.497 24.963  19.583  1.00 31.96 ? 65  ILE A N   1 
ATOM   519  C CA  . ILE A 1 65  ? 17.368 24.305  20.558  1.00 36.79 ? 65  ILE A CA  1 
ATOM   520  C C   . ILE A 1 65  ? 16.824 22.905  20.817  1.00 33.48 ? 65  ILE A C   1 
ATOM   521  O O   . ILE A 1 65  ? 15.616 22.729  21.005  1.00 34.07 ? 65  ILE A O   1 
ATOM   522  C CB  . ILE A 1 65  ? 17.437 25.088  21.887  1.00 43.62 ? 65  ILE A CB  1 
ATOM   523  C CG1 . ILE A 1 65  ? 18.039 26.448  21.648  1.00 46.91 ? 65  ILE A CG1 1 
ATOM   524  C CG2 . ILE A 1 65  ? 18.249 24.329  22.952  1.00 47.07 ? 65  ILE A CG2 1 
ATOM   525  C CD1 . ILE A 1 65  ? 17.919 27.277  22.834  0.92 48.83 ? 65  ILE A CD1 1 
ATOM   526  N N   . GLY A 1 66  ? 17.711 21.919  20.867  1.00 31.34 ? 66  GLY A N   1 
ATOM   527  C CA  . GLY A 1 66  ? 17.253 20.564  21.090  1.00 32.95 ? 66  GLY A CA  1 
ATOM   528  C C   . GLY A 1 66  ? 17.858 19.985  22.353  1.00 35.34 ? 66  GLY A C   1 
ATOM   529  O O   . GLY A 1 66  ? 19.060 20.136  22.588  1.00 39.16 ? 66  GLY A O   1 
ATOM   530  N N   . ILE A 1 67  ? 17.040 19.352  23.190  1.00 33.83 ? 67  ILE A N   1 
ATOM   531  C CA  . ILE A 1 67  ? 17.512 18.644  24.377  1.00 33.28 ? 67  ILE A CA  1 
ATOM   532  C C   . ILE A 1 67  ? 17.237 17.166  24.159  1.00 35.69 ? 67  ILE A C   1 
ATOM   533  O O   . ILE A 1 67  ? 16.112 16.797  23.791  1.00 35.51 ? 67  ILE A O   1 
ATOM   534  C CB  . ILE A 1 67  ? 16.783 19.144  25.635  1.00 33.16 ? 67  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 67  ? 17.105 20.612  25.858  1.00 35.13 ? 67  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 67  ? 17.095 18.252  26.834  1.00 34.18 ? 67  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 67  ? 16.257 21.217  26.959  1.00 36.23 ? 67  ILE A CD1 1 
ATOM   538  N N   . HIS A 1 68  ? 18.237 16.316  24.391  1.00 33.17 ? 68  HIS A N   1 
ATOM   539  C CA  . HIS A 1 68  ? 18.036 14.881  24.240  1.00 36.78 ? 68  HIS A CA  1 
ATOM   540  C C   . HIS A 1 68  ? 17.792 14.256  25.599  1.00 40.56 ? 68  HIS A C   1 
ATOM   541  O O   . HIS A 1 68  ? 18.641 14.346  26.494  1.00 40.11 ? 68  HIS A O   1 
ATOM   542  C CB  . HIS A 1 68  ? 19.211 14.204  23.532  1.00 39.41 ? 68  HIS A CB  1 
ATOM   543  C CG  . HIS A 1 68  ? 20.509 14.279  24.265  1.00 41.12 ? 68  HIS A CG  1 
ATOM   544  N ND1 . HIS A 1 68  ? 20.914 13.316  25.167  1.00 45.33 ? 68  HIS A ND1 1 
ATOM   545  C CD2 . HIS A 1 68  ? 21.503 15.195  24.222  1.00 42.32 ? 68  HIS A CD2 1 
ATOM   546  C CE1 . HIS A 1 68  ? 22.099 13.640  25.652  1.00 45.52 ? 68  HIS A CE1 1 
ATOM   547  N NE2 . HIS A 1 68  ? 22.484 14.771  25.088  1.00 44.21 ? 68  HIS A NE2 1 
ATOM   548  N N   . THR A 1 69  ? 16.615 13.659  25.764  1.00 42.22 ? 69  THR A N   1 
ATOM   549  C CA  . THR A 1 69  ? 16.361 12.939  26.996  1.00 45.46 ? 69  THR A CA  1 
ATOM   550  C C   . THR A 1 69  ? 16.728 11.466  26.886  1.00 48.79 ? 69  THR A C   1 
ATOM   551  O O   . THR A 1 69  ? 16.793 10.779  27.911  1.00 50.72 ? 69  THR A O   1 
ATOM   552  C CB  . THR A 1 69  ? 14.900 13.131  27.436  1.00 44.68 ? 69  THR A CB  1 
ATOM   553  O OG1 . THR A 1 69  ? 14.008 12.903  26.349  1.00 44.83 ? 69  THR A OG1 1 
ATOM   554  C CG2 . THR A 1 69  ? 14.703 14.551  27.936  1.00 44.92 ? 69  THR A CG2 1 
ATOM   555  N N   . GLY A 1 70  ? 17.006 10.984  25.682  1.00 49.87 ? 70  GLY A N   1 
ATOM   556  C CA  . GLY A 1 70  ? 17.686 9.727   25.465  1.00 50.75 ? 70  GLY A CA  1 
ATOM   557  C C   . GLY A 1 70  ? 19.148 9.953   25.146  1.00 51.72 ? 70  GLY A C   1 
ATOM   558  O O   . GLY A 1 70  ? 19.811 10.809  25.743  1.00 50.67 ? 70  GLY A O   1 
ATOM   559  N N   . HIS A 1 71  ? 19.659 9.195   24.188  1.00 53.15 ? 71  HIS A N   1 
ATOM   560  C CA  . HIS A 1 71  ? 21.057 9.377   23.846  1.00 55.42 ? 71  HIS A CA  1 
ATOM   561  C C   . HIS A 1 71  ? 21.256 10.653  23.032  1.00 49.35 ? 71  HIS A C   1 
ATOM   562  O O   . HIS A 1 71  ? 20.306 11.295  22.582  1.00 48.54 ? 71  HIS A O   1 
ATOM   563  C CB  . HIS A 1 71  ? 21.582 8.149   23.115  1.00 59.91 ? 71  HIS A CB  1 
ATOM   564  C CG  . HIS A 1 71  ? 21.753 6.975   24.025  0.70 64.61 ? 71  HIS A CG  1 
ATOM   565  N ND1 . HIS A 1 71  ? 20.744 6.070   24.269  0.70 65.78 ? 71  HIS A ND1 1 
ATOM   566  C CD2 . HIS A 1 71  ? 22.792 6.601   24.808  0.70 67.07 ? 71  HIS A CD2 1 
ATOM   567  C CE1 . HIS A 1 71  ? 21.167 5.166   25.135  0.70 68.03 ? 71  HIS A CE1 1 
ATOM   568  N NE2 . HIS A 1 71  ? 22.405 5.468   25.482  0.70 68.54 ? 71  HIS A NE2 1 
ATOM   569  N N   . LEU A 1 72  ? 22.523 11.044  22.912  1.00 45.94 ? 72  LEU A N   1 
ATOM   570  C CA  . LEU A 1 72  ? 22.874 12.299  22.270  1.00 44.68 ? 72  LEU A CA  1 
ATOM   571  C C   . LEU A 1 72  ? 22.342 12.314  20.839  1.00 43.49 ? 72  LEU A C   1 
ATOM   572  O O   . LEU A 1 72  ? 22.455 11.322  20.110  1.00 42.37 ? 72  LEU A O   1 
ATOM   573  C CB  . LEU A 1 72  ? 24.400 12.473  22.284  1.00 47.40 ? 72  LEU A CB  1 
ATOM   574  C CG  . LEU A 1 72  ? 25.038 13.546  21.386  1.00 47.38 ? 72  LEU A CG  1 
ATOM   575  C CD1 . LEU A 1 72  ? 24.844 14.921  21.992  1.00 48.31 ? 72  LEU A CD1 1 
ATOM   576  C CD2 . LEU A 1 72  ? 26.518 13.285  21.167  1.00 48.49 ? 72  LEU A CD2 1 
ATOM   577  N N   . GLY A 1 73  ? 21.724 13.426  20.459  1.00 40.44 ? 73  GLY A N   1 
ATOM   578  C CA  . GLY A 1 73  ? 21.225 13.603  19.122  1.00 39.39 ? 73  GLY A CA  1 
ATOM   579  C C   . GLY A 1 73  ? 22.123 14.577  18.404  1.00 41.73 ? 73  GLY A C   1 
ATOM   580  O O   . GLY A 1 73  ? 22.893 15.300  19.044  1.00 44.15 ? 73  GLY A O   1 
ATOM   581  N N   . PHE A 1 74  ? 22.066 14.588  17.079  1.00 35.50 ? 74  PHE A N   1 
ATOM   582  C CA  . PHE A 1 74  ? 22.839 15.574  16.350  1.00 35.43 ? 74  PHE A CA  1 
ATOM   583  C C   . PHE A 1 74  ? 22.173 16.931  16.330  1.00 35.59 ? 74  PHE A C   1 
ATOM   584  O O   . PHE A 1 74  ? 22.848 17.935  16.068  1.00 40.01 ? 74  PHE A O   1 
ATOM   585  C CB  . PHE A 1 74  ? 23.106 15.102  14.909  1.00 30.87 ? 74  PHE A CB  1 
ATOM   586  C CG  . PHE A 1 74  ? 24.371 14.393  14.777  1.00 33.46 ? 74  PHE A CG  1 
ATOM   587  C CD1 . PHE A 1 74  ? 24.449 13.051  15.074  1.00 33.61 ? 74  PHE A CD1 1 
ATOM   588  C CD2 . PHE A 1 74  ? 25.525 15.074  14.441  1.00 34.09 ? 74  PHE A CD2 1 
ATOM   589  C CE1 . PHE A 1 74  ? 25.623 12.397  14.966  1.00 35.52 ? 74  PHE A CE1 1 
ATOM   590  C CE2 . PHE A 1 74  ? 26.698 14.435  14.352  1.00 32.93 ? 74  PHE A CE2 1 
ATOM   591  C CZ  . PHE A 1 74  ? 26.760 13.080  14.606  1.00 38.49 ? 74  PHE A CZ  1 
ATOM   592  N N   . TYR A 1 75  ? 20.863 16.978  16.531  1.00 30.62 ? 75  TYR A N   1 
ATOM   593  C CA  . TYR A 1 75  ? 20.196 18.252  16.713  1.00 29.99 ? 75  TYR A CA  1 
ATOM   594  C C   . TYR A 1 75  ? 19.802 18.468  18.153  1.00 35.02 ? 75  TYR A C   1 
ATOM   595  O O   . TYR A 1 75  ? 19.832 19.601  18.635  1.00 35.37 ? 75  TYR A O   1 
ATOM   596  C CB  . TYR A 1 75  ? 18.944 18.337  15.857  1.00 29.37 ? 75  TYR A CB  1 
ATOM   597  C CG  . TYR A 1 75  ? 19.232 18.131  14.377  1.00 32.76 ? 75  TYR A CG  1 
ATOM   598  C CD1 . TYR A 1 75  ? 20.088 18.979  13.698  1.00 29.35 ? 75  TYR A CD1 1 
ATOM   599  C CD2 . TYR A 1 75  ? 18.669 17.074  13.689  1.00 28.87 ? 75  TYR A CD2 1 
ATOM   600  C CE1 . TYR A 1 75  ? 20.355 18.797  12.314  1.00 29.23 ? 75  TYR A CE1 1 
ATOM   601  C CE2 . TYR A 1 75  ? 18.923 16.868  12.318  1.00 28.77 ? 75  TYR A CE2 1 
ATOM   602  C CZ  . TYR A 1 75  ? 19.774 17.729  11.645  1.00 28.92 ? 75  TYR A CZ  1 
ATOM   603  O OH  . TYR A 1 75  ? 20.028 17.533  10.292  1.00 28.92 ? 75  TYR A OH  1 
ATOM   604  N N   . ALA A 1 76  ? 19.413 17.383  18.807  1.00 34.73 ? 76  ALA A N   1 
ATOM   605  C CA  . ALA A 1 76  ? 19.075 17.370  20.227  1.00 37.12 ? 76  ALA A CA  1 
ATOM   606  C C   . ALA A 1 76  ? 20.371 17.134  20.981  1.00 38.37 ? 76  ALA A C   1 
ATOM   607  O O   . ALA A 1 76  ? 20.668 16.027  21.428  1.00 39.55 ? 76  ALA A O   1 
ATOM   608  C CB  . ALA A 1 76  ? 18.048 16.284  20.513  1.00 35.29 ? 76  ALA A CB  1 
ATOM   609  N N   . ASP A 1 77  ? 21.188 18.186  21.049  1.00 39.23 ? 77  ASP A N   1 
ATOM   610  C CA  . ASP A 1 77  ? 22.565 17.982  21.467  1.00 42.33 ? 77  ASP A CA  1 
ATOM   611  C C   . ASP A 1 77  ? 22.875 18.545  22.850  1.00 46.63 ? 77  ASP A C   1 
ATOM   612  O O   . ASP A 1 77  ? 24.053 18.611  23.215  1.00 49.28 ? 77  ASP A O   1 
ATOM   613  C CB  . ASP A 1 77  ? 23.542 18.529  20.421  1.00 43.96 ? 77  ASP A CB  1 
ATOM   614  C CG  . ASP A 1 77  ? 23.361 20.015  20.139  1.00 48.32 ? 77  ASP A CG  1 
ATOM   615  O OD1 . ASP A 1 77  ? 22.373 20.617  20.604  1.00 49.71 ? 77  ASP A OD1 1 
ATOM   616  O OD2 . ASP A 1 77  ? 24.236 20.580  19.441  1.00 51.78 ? 77  ASP A OD2 1 
ATOM   617  N N   . TRP A 1 78  ? 21.859 18.897  23.652  1.00 45.27 ? 78  TRP A N   1 
ATOM   618  C CA  . TRP A 1 78  ? 22.065 19.356  25.020  1.00 43.49 ? 78  TRP A CA  1 
ATOM   619  C C   . TRP A 1 78  ? 21.414 18.389  26.013  1.00 41.05 ? 78  TRP A C   1 
ATOM   620  O O   . TRP A 1 78  ? 20.390 17.771  25.720  1.00 40.58 ? 78  TRP A O   1 
ATOM   621  C CB  . TRP A 1 78  ? 21.524 20.784  25.226  0.80 46.24 ? 78  TRP A CB  1 
ATOM   622  C CG  . TRP A 1 78  ? 22.092 21.735  24.217  0.70 46.23 ? 78  TRP A CG  1 
ATOM   623  C CD1 . TRP A 1 78  ? 21.391 22.506  23.336  0.60 45.95 ? 78  TRP A CD1 1 
ATOM   624  C CD2 . TRP A 1 78  ? 23.483 21.967  23.930  0.60 48.44 ? 78  TRP A CD2 1 
ATOM   625  N NE1 . TRP A 1 78  ? 22.250 23.220  22.538  0.60 45.02 ? 78  TRP A NE1 1 
ATOM   626  C CE2 . TRP A 1 78  ? 23.539 22.908  22.878  0.60 47.90 ? 78  TRP A CE2 1 
ATOM   627  C CE3 . TRP A 1 78  ? 24.682 21.484  24.468  0.60 49.47 ? 78  TRP A CE3 1 
ATOM   628  C CZ2 . TRP A 1 78  ? 24.747 23.381  22.357  0.60 49.67 ? 78  TRP A CZ2 1 
ATOM   629  C CZ3 . TRP A 1 78  ? 25.884 21.954  23.945  0.60 50.79 ? 78  TRP A CZ3 1 
ATOM   630  C CH2 . TRP A 1 78  ? 25.903 22.890  22.895  0.60 50.66 ? 78  TRP A CH2 1 
ATOM   631  N N   . ARG A 1 79  ? 22.050 18.222  27.181  1.00 41.24 ? 79  ARG A N   1 
ATOM   632  C CA  . ARG A 1 79  ? 21.597 17.256  28.182  1.00 45.86 ? 79  ARG A CA  1 
ATOM   633  C C   . ARG A 1 79  ? 20.495 17.832  29.070  1.00 47.27 ? 79  ARG A C   1 
ATOM   634  O O   . ARG A 1 79  ? 20.496 19.027  29.373  1.00 48.48 ? 79  ARG A O   1 
ATOM   635  C CB  . ARG A 1 79  ? 22.760 16.825  29.078  1.00 49.15 ? 79  ARG A CB  1 
ATOM   636  C CG  . ARG A 1 79  ? 23.847 15.988  28.420  0.99 53.94 ? 79  ARG A CG  1 
ATOM   637  C CD  . ARG A 1 79  ? 25.025 15.754  29.385  1.00 58.38 ? 79  ARG A CD  1 
ATOM   638  N NE  . ARG A 1 79  ? 24.579 15.162  30.650  0.87 64.50 ? 79  ARG A NE  1 
ATOM   639  C CZ  . ARG A 1 79  ? 24.840 15.646  31.864  0.59 68.56 ? 79  ARG A CZ  1 
ATOM   640  N NH1 . ARG A 1 79  ? 25.576 16.743  32.018  1.00 70.24 ? 79  ARG A NH1 1 
ATOM   641  N NH2 . ARG A 1 79  ? 24.364 15.020  32.935  1.00 70.55 ? 79  ARG A NH2 1 
ATOM   642  N N   . PRO A 1 80  ? 19.581 16.983  29.557  1.00 46.65 ? 80  PRO A N   1 
ATOM   643  C CA  . PRO A 1 80  ? 18.556 17.475  30.494  1.00 47.05 ? 80  PRO A CA  1 
ATOM   644  C C   . PRO A 1 80  ? 19.130 18.140  31.725  1.00 52.24 ? 80  PRO A C   1 
ATOM   645  O O   . PRO A 1 80  ? 18.479 19.029  32.297  1.00 50.82 ? 80  PRO A O   1 
ATOM   646  C CB  . PRO A 1 80  ? 17.780 16.205  30.871  1.00 47.08 ? 80  PRO A CB  1 
ATOM   647  C CG  . PRO A 1 80  ? 18.039 15.249  29.764  1.00 45.19 ? 80  PRO A CG  1 
ATOM   648  C CD  . PRO A 1 80  ? 19.417 15.554  29.255  1.00 45.74 ? 80  PRO A CD  1 
ATOM   649  N N   . ALA A 1 81  ? 20.323 17.723  32.171  1.00 53.96 ? 81  ALA A N   1 
ATOM   650  C CA  . ALA A 1 81  ? 20.886 18.309  33.377  1.00 57.52 ? 81  ALA A CA  1 
ATOM   651  C C   . ALA A 1 81  ? 21.224 19.770  33.174  1.00 56.38 ? 81  ALA A C   1 
ATOM   652  O O   . ALA A 1 81  ? 21.360 20.497  34.152  1.00 57.18 ? 81  ALA A O   1 
ATOM   653  C CB  . ALA A 1 81  ? 22.140 17.548  33.825  1.00 58.51 ? 81  ALA A CB  1 
ATOM   654  N N   . GLU A 1 82  ? 21.344 20.228  31.935  1.00 55.28 ? 82  GLU A N   1 
ATOM   655  C CA  . GLU A 1 82  ? 21.702 21.614  31.678  1.00 56.74 ? 82  GLU A CA  1 
ATOM   656  C C   . GLU A 1 82  ? 20.485 22.492  31.380  1.00 52.69 ? 82  GLU A C   1 
ATOM   657  O O   . GLU A 1 82  ? 20.640 23.615  30.878  1.00 49.78 ? 82  GLU A O   1 
ATOM   658  C CB  . GLU A 1 82  ? 22.737 21.667  30.560  1.00 61.53 ? 82  GLU A CB  1 
ATOM   659  C CG  . GLU A 1 82  ? 24.022 20.938  30.957  0.39 65.67 ? 82  GLU A CG  1 
ATOM   660  C CD  . GLU A 1 82  ? 24.722 20.325  29.781  0.87 67.79 ? 82  GLU A CD  1 
ATOM   661  O OE1 . GLU A 1 82  ? 24.193 20.468  28.663  1.00 68.93 ? 82  GLU A OE1 1 
ATOM   662  O OE2 . GLU A 1 82  ? 25.790 19.701  29.964  0.83 70.58 ? 82  GLU A OE2 1 
ATOM   663  N N   . ALA A 1 83  ? 19.280 22.023  31.742  1.00 50.02 ? 83  ALA A N   1 
ATOM   664  C CA  . ALA A 1 83  ? 18.059 22.731  31.361  1.00 50.10 ? 83  ALA A CA  1 
ATOM   665  C C   . ALA A 1 83  ? 17.939 24.059  32.091  1.00 51.87 ? 83  ALA A C   1 
ATOM   666  O O   . ALA A 1 83  ? 17.532 25.067  31.494  1.00 50.30 ? 83  ALA A O   1 
ATOM   667  C CB  . ALA A 1 83  ? 16.832 21.866  31.638  1.00 50.86 ? 83  ALA A CB  1 
ATOM   668  N N   . ASP A 1 84  ? 18.283 24.082  33.380  1.00 53.84 ? 84  ASP A N   1 
ATOM   669  C CA  . ASP A 1 84  ? 18.222 25.338  34.118  1.00 57.06 ? 84  ASP A CA  1 
ATOM   670  C C   . ASP A 1 84  ? 19.196 26.351  33.525  1.00 57.72 ? 84  ASP A C   1 
ATOM   671  O O   . ASP A 1 84  ? 18.854 27.528  33.354  1.00 56.22 ? 84  ASP A O   1 
ATOM   672  C CB  . ASP A 1 84  ? 18.499 25.095  35.604  0.80 58.91 ? 84  ASP A CB  1 
ATOM   673  C CG  . ASP A 1 84  ? 17.406 24.269  36.279  0.70 59.75 ? 84  ASP A CG  1 
ATOM   674  O OD1 . ASP A 1 84  ? 16.258 24.266  35.781  0.70 59.18 ? 84  ASP A OD1 1 
ATOM   675  O OD2 . ASP A 1 84  ? 17.687 23.627  37.313  0.70 61.29 ? 84  ASP A OD2 1 
ATOM   676  N N   . LYS A 1 85  ? 20.403 25.907  33.168  1.00 57.67 ? 85  LYS A N   1 
ATOM   677  C CA  . LYS A 1 85  ? 21.351 26.833  32.561  1.00 58.96 ? 85  LYS A CA  1 
ATOM   678  C C   . LYS A 1 85  ? 20.829 27.325  31.219  1.00 57.75 ? 85  LYS A C   1 
ATOM   679  O O   . LYS A 1 85  ? 20.976 28.507  30.879  1.00 58.20 ? 85  LYS A O   1 
ATOM   680  C CB  . LYS A 1 85  ? 22.723 26.169  32.422  1.00 61.70 ? 85  LYS A CB  1 
ATOM   681  N N   . LEU A 1 86  ? 20.181 26.432  30.459  1.00 54.37 ? 86  LEU A N   1 
ATOM   682  C CA  . LEU A 1 86  ? 19.537 26.807  29.204  1.00 53.40 ? 86  LEU A CA  1 
ATOM   683  C C   . LEU A 1 86  ? 18.482 27.882  29.420  1.00 51.85 ? 86  LEU A C   1 
ATOM   684  O O   . LEU A 1 86  ? 18.425 28.873  28.686  1.00 50.63 ? 86  LEU A O   1 
ATOM   685  C CB  . LEU A 1 86  ? 18.909 25.570  28.565  1.00 53.35 ? 86  LEU A CB  1 
ATOM   686  C CG  . LEU A 1 86  ? 19.075 25.403  27.062  1.00 55.79 ? 86  LEU A CG  1 
ATOM   687  C CD1 . LEU A 1 86  ? 20.410 25.947  26.617  1.00 58.88 ? 86  LEU A CD1 1 
ATOM   688  C CD2 . LEU A 1 86  ? 18.981 23.936  26.716  1.00 54.40 ? 86  LEU A CD2 1 
ATOM   689  N N   . VAL A 1 87  ? 17.617 27.686  30.416  1.00 49.90 ? 87  VAL A N   1 
ATOM   690  C CA  . VAL A 1 87  ? 16.604 28.689  30.719  1.00 52.34 ? 87  VAL A CA  1 
ATOM   691  C C   . VAL A 1 87  ? 17.259 30.033  31.005  1.00 55.57 ? 87  VAL A C   1 
ATOM   692  O O   . VAL A 1 87  ? 16.930 31.048  30.378  1.00 54.68 ? 87  VAL A O   1 
ATOM   693  C CB  . VAL A 1 87  ? 15.730 28.214  31.894  1.00 52.39 ? 87  VAL A CB  1 
ATOM   694  C CG1 . VAL A 1 87  ? 14.991 29.392  32.522  1.00 51.57 ? 87  VAL A CG1 1 
ATOM   695  C CG2 . VAL A 1 87  ? 14.769 27.133  31.404  1.00 48.14 ? 87  VAL A CG2 1 
ATOM   696  N N   . LYS A 1 88  ? 18.225 30.047  31.934  1.00 60.16 ? 88  LYS A N   1 
ATOM   697  C CA  . LYS A 1 88  ? 18.907 31.286  32.303  1.00 66.57 ? 88  LYS A CA  1 
ATOM   698  C C   . LYS A 1 88  ? 19.469 31.992  31.070  1.00 67.85 ? 88  LYS A C   1 
ATOM   699  O O   . LYS A 1 88  ? 19.299 33.204  30.899  1.00 70.05 ? 88  LYS A O   1 
ATOM   700  C CB  . LYS A 1 88  ? 20.018 30.995  33.329  0.71 70.45 ? 88  LYS A CB  1 
ATOM   701  C CG  . LYS A 1 88  ? 19.533 30.495  34.716  0.96 73.72 ? 88  LYS A CG  1 
ATOM   702  C CD  . LYS A 1 88  ? 20.671 30.374  35.757  1.00 76.08 ? 88  LYS A CD  1 
ATOM   703  C CE  . LYS A 1 88  ? 20.143 30.179  37.196  0.96 78.21 ? 88  LYS A CE  1 
ATOM   704  N NZ  . LYS A 1 88  ? 19.528 28.836  37.470  1.00 76.92 ? 88  LYS A NZ  1 
ATOM   705  N N   . LEU A 1 89  ? 20.096 31.249  30.167  1.00 66.93 ? 89  LEU A N   1 
ATOM   706  C CA  . LEU A 1 89  ? 20.798 31.935  29.089  1.00 66.30 ? 89  LEU A CA  1 
ATOM   707  C C   . LEU A 1 89  ? 19.867 32.359  27.956  1.00 63.69 ? 89  LEU A C   1 
ATOM   708  O O   . LEU A 1 89  ? 20.087 33.416  27.360  1.00 64.40 ? 89  LEU A O   1 
ATOM   709  C CB  . LEU A 1 89  ? 21.953 31.066  28.595  1.00 68.30 ? 89  LEU A CB  1 
ATOM   710  C CG  . LEU A 1 89  ? 22.988 30.882  29.720  1.00 70.94 ? 89  LEU A CG  1 
ATOM   711  C CD1 . LEU A 1 89  ? 24.155 29.987  29.288  1.00 70.77 ? 89  LEU A CD1 1 
ATOM   712  C CD2 . LEU A 1 89  ? 23.491 32.232  30.221  1.00 72.27 ? 89  LEU A CD2 1 
ATOM   713  N N   . LEU A 1 90  ? 18.810 31.590  27.670  1.00 60.87 ? 90  LEU A N   1 
ATOM   714  C CA  . LEU A 1 90  ? 17.838 32.015  26.662  1.00 61.70 ? 90  LEU A CA  1 
ATOM   715  C C   . LEU A 1 90  ? 17.045 33.232  27.111  1.00 67.44 ? 90  LEU A C   1 
ATOM   716  O O   . LEU A 1 90  ? 16.715 34.100  26.292  1.00 69.24 ? 90  LEU A O   1 
ATOM   717  C CB  . LEU A 1 90  ? 16.864 30.887  26.346  1.00 58.02 ? 90  LEU A CB  1 
ATOM   718  C CG  . LEU A 1 90  ? 17.361 29.806  25.419  0.54 55.17 ? 90  LEU A CG  1 
ATOM   719  C CD1 . LEU A 1 90  ? 16.514 28.573  25.677  1.00 53.32 ? 90  LEU A CD1 1 
ATOM   720  C CD2 . LEU A 1 90  ? 17.243 30.334  23.994  1.00 54.88 ? 90  LEU A CD2 1 
ATOM   721  N N   . ALA A 1 91  ? 16.678 33.282  28.390  0.84 70.89 ? 91  ALA A N   1 
ATOM   722  C CA  . ALA A 1 91  ? 15.849 34.381  28.871  1.00 75.24 ? 91  ALA A CA  1 
ATOM   723  C C   . ALA A 1 91  ? 16.571 35.712  28.716  1.00 79.06 ? 91  ALA A C   1 
ATOM   724  O O   . ALA A 1 91  ? 15.991 36.694  28.234  1.00 80.11 ? 91  ALA A O   1 
ATOM   725  C CB  . ALA A 1 91  ? 15.458 34.138  30.329  1.00 75.53 ? 91  ALA A CB  1 
ATOM   726  N N   . LYS A 1 92  ? 17.845 35.753  29.105  1.00 83.43 ? 92  LYS A N   1 
ATOM   727  C CA  . LYS A 1 92  ? 18.669 36.940  28.937  1.00 85.30 ? 92  LYS A CA  1 
ATOM   728  C C   . LYS A 1 92  ? 18.991 37.228  27.474  1.00 81.37 ? 92  LYS A C   1 
ATOM   729  O O   . LYS A 1 92  ? 19.367 38.361  27.148  1.00 83.23 ? 92  LYS A O   1 
ATOM   730  C CB  . LYS A 1 92  ? 19.947 36.768  29.760  1.00 89.29 ? 92  LYS A CB  1 
ATOM   731  C CG  . LYS A 1 92  ? 20.958 37.880  29.635  0.88 93.96 ? 92  LYS A CG  1 
ATOM   732  C CD  . LYS A 1 92  ? 22.340 37.285  29.481  0.81 94.83 ? 92  LYS A CD  1 
ATOM   733  C CE  . LYS A 1 92  ? 23.400 38.360  29.417  1.00 97.53 ? 92  LYS A CE  1 
ATOM   734  N NZ  . LYS A 1 92  ? 24.750 37.786  29.647  1.00 97.79 ? 92  LYS A NZ  1 
ATOM   735  N N   . GLY A 1 93  ? 18.832 36.250  26.587  0.50 73.61 ? 93  GLY A N   1 
ATOM   736  C CA  . GLY A 1 93  ? 19.098 36.489  25.185  0.50 67.93 ? 93  GLY A CA  1 
ATOM   737  C C   . GLY A 1 93  ? 20.552 36.842  24.933  0.50 62.49 ? 93  GLY A C   1 
ATOM   738  O O   . GLY A 1 93  ? 21.469 36.383  25.623  0.50 60.74 ? 93  GLY A O   1 
ATOM   739  N N   . GLU A 1 94  ? 20.762 37.670  23.913  0.20 60.83 ? 94  GLU A N   1 
ATOM   740  C CA  . GLU A 1 94  ? 22.084 38.158  23.531  0.20 60.19 ? 94  GLU A CA  1 
ATOM   741  C C   . GLU A 1 94  ? 23.030 37.024  23.136  0.20 61.33 ? 94  GLU A C   1 
ATOM   742  O O   . GLU A 1 94  ? 24.254 37.198  23.144  0.20 61.17 ? 94  GLU A O   1 
ATOM   743  C CB  . GLU A 1 94  ? 22.694 39.008  24.653  0.20 58.98 ? 94  GLU A CB  1 
ATOM   744  C CG  . GLU A 1 94  ? 21.737 40.065  25.206  0.20 58.22 ? 94  GLU A CG  1 
ATOM   745  C CD  . GLU A 1 94  ? 22.354 40.894  26.311  0.20 58.56 ? 94  GLU A CD  1 
ATOM   746  O OE1 . GLU A 1 94  ? 23.280 40.398  26.983  0.20 57.68 ? 94  GLU A OE1 1 
ATOM   747  O OE2 . GLU A 1 94  ? 21.916 42.048  26.503  0.20 59.81 ? 94  GLU A OE2 1 
ATOM   748  N N   . TYR A 1 95  ? 22.480 35.868  22.776  1.00 64.38 ? 95  TYR A N   1 
ATOM   749  C CA  . TYR A 1 95  ? 23.241 34.701  22.356  1.00 65.43 ? 95  TYR A CA  1 
ATOM   750  C C   . TYR A 1 95  ? 23.496 34.750  20.852  1.00 65.79 ? 95  TYR A C   1 
ATOM   751  O O   . TYR A 1 95  ? 22.787 35.420  20.094  1.00 68.19 ? 95  TYR A O   1 
ATOM   752  C CB  . TYR A 1 95  ? 22.482 33.415  22.712  1.00 66.14 ? 95  TYR A CB  1 
ATOM   753  C CG  . TYR A 1 95  ? 21.036 33.497  22.284  1.00 66.48 ? 95  TYR A CG  1 
ATOM   754  C CD1 . TYR A 1 95  ? 20.685 33.350  20.949  1.00 65.67 ? 95  TYR A CD1 1 
ATOM   755  C CD2 . TYR A 1 95  ? 20.030 33.771  23.201  1.00 68.45 ? 95  TYR A CD2 1 
ATOM   756  C CE1 . TYR A 1 95  ? 19.389 33.458  20.533  1.00 66.30 ? 95  TYR A CE1 1 
ATOM   757  C CE2 . TYR A 1 95  ? 18.719 33.877  22.794  1.00 69.82 ? 95  TYR A CE2 1 
ATOM   758  C CZ  . TYR A 1 95  ? 18.410 33.718  21.451  1.00 68.84 ? 95  TYR A CZ  1 
ATOM   759  O OH  . TYR A 1 95  ? 17.121 33.828  21.018  1.00 70.00 ? 95  TYR A OH  1 
ATOM   760  N N   . GLN A 1 96  ? 24.500 33.997  20.417  1.00 63.08 ? 96  GLN A N   1 
ATOM   761  C CA  . GLN A 1 96  ? 24.795 33.909  18.997  1.00 60.58 ? 96  GLN A CA  1 
ATOM   762  C C   . GLN A 1 96  ? 23.937 32.832  18.339  1.00 57.08 ? 96  GLN A C   1 
ATOM   763  O O   . GLN A 1 96  ? 23.484 31.883  18.991  1.00 57.04 ? 96  GLN A O   1 
ATOM   764  C CB  . GLN A 1 96  ? 26.281 33.614  18.779  1.00 62.37 ? 96  GLN A CB  1 
ATOM   765  C CG  . GLN A 1 96  ? 27.226 34.699  19.308  1.00 67.30 ? 96  GLN A CG  1 
ATOM   766  C CD  . GLN A 1 96  ? 28.680 34.276  19.235  0.54 69.24 ? 96  GLN A CD  1 
ATOM   767  O OE1 . GLN A 1 96  ? 28.993 33.086  19.298  0.79 68.04 ? 96  GLN A OE1 1 
ATOM   768  N NE2 . GLN A 1 96  ? 29.576 35.248  19.092  0.99 72.37 ? 96  GLN A NE2 1 
ATOM   769  N N   . LYS A 1 97  ? 23.701 33.003  17.040  1.00 53.61 ? 97  LYS A N   1 
ATOM   770  C CA  . LYS A 1 97  ? 22.958 32.064  16.214  1.00 49.88 ? 97  LYS A CA  1 
ATOM   771  C C   . LYS A 1 97  ? 23.931 31.357  15.278  1.00 45.47 ? 97  LYS A C   1 
ATOM   772  O O   . LYS A 1 97  ? 24.943 31.929  14.877  1.00 44.37 ? 97  LYS A O   1 
ATOM   773  C CB  . LYS A 1 97  ? 21.854 32.781  15.407  1.00 51.36 ? 97  LYS A CB  1 
ATOM   774  C CG  . LYS A 1 97  ? 20.748 33.451  16.281  1.00 54.65 ? 97  LYS A CG  1 
ATOM   775  C CD  . LYS A 1 97  ? 19.828 34.437  15.510  0.80 56.80 ? 97  LYS A CD  1 
ATOM   776  C CE  . LYS A 1 97  ? 19.035 33.758  14.372  0.70 56.81 ? 97  LYS A CE  1 
ATOM   777  N NZ  . LYS A 1 97  ? 18.064 34.662  13.634  0.70 58.21 ? 97  LYS A NZ  1 
ATOM   778  N N   . VAL A 1 98  ? 23.645 30.088  14.989  1.00 41.69 ? 98  VAL A N   1 
ATOM   779  C CA  . VAL A 1 98  ? 24.365 29.284  14.005  1.00 42.08 ? 98  VAL A CA  1 
ATOM   780  C C   . VAL A 1 98  ? 23.350 28.810  12.977  1.00 40.13 ? 98  VAL A C   1 
ATOM   781  O O   . VAL A 1 98  ? 22.239 28.419  13.339  1.00 39.79 ? 98  VAL A O   1 
ATOM   782  C CB  . VAL A 1 98  ? 25.080 28.087  14.677  1.00 44.09 ? 98  VAL A CB  1 
ATOM   783  C CG1 . VAL A 1 98  ? 25.542 27.063  13.662  1.00 43.18 ? 98  VAL A CG1 1 
ATOM   784  C CG2 . VAL A 1 98  ? 26.262 28.579  15.490  1.00 47.38 ? 98  VAL A CG2 1 
ATOM   785  N N   . SER A 1 99  ? 23.720 28.853  11.696  1.00 37.63 ? 99  SER A N   1 
ATOM   786  C CA  . SER A 1 99  ? 22.806 28.542  10.601  1.00 36.86 ? 99  SER A CA  1 
ATOM   787  C C   . SER A 1 99  ? 23.310 27.340  9.821   1.00 32.43 ? 99  SER A C   1 
ATOM   788  O O   . SER A 1 99  ? 24.496 27.268  9.483   1.00 30.07 ? 99  SER A O   1 
ATOM   789  C CB  . SER A 1 99  ? 22.650 29.739  9.660   1.00 42.26 ? 99  SER A CB  1 
ATOM   790  O OG  . SER A 1 99  ? 21.949 30.772  10.316  1.00 45.14 ? 99  SER A OG  1 
ATOM   791  N N   . TYR A 1 100 ? 22.406 26.395  9.526   1.00 33.19 ? 100 TYR A N   1 
ATOM   792  C CA  . TYR A 1 100 ? 22.690 25.225  8.688   1.00 30.24 ? 100 TYR A CA  1 
ATOM   793  C C   . TYR A 1 100 ? 21.898 25.297  7.378   1.00 29.69 ? 100 TYR A C   1 
ATOM   794  O O   . TYR A 1 100 ? 20.787 25.832  7.380   1.00 27.59 ? 100 TYR A O   1 
ATOM   795  C CB  . TYR A 1 100 ? 22.315 23.924  9.403   1.00 31.67 ? 100 TYR A CB  1 
ATOM   796  C CG  . TYR A 1 100 ? 23.263 23.440  10.481  1.00 34.04 ? 100 TYR A CG  1 
ATOM   797  C CD1 . TYR A 1 100 ? 24.396 24.162  10.829  1.00 36.69 ? 100 TYR A CD1 1 
ATOM   798  C CD2 . TYR A 1 100 ? 23.028 22.227  11.123  1.00 35.01 ? 100 TYR A CD2 1 
ATOM   799  C CE1 . TYR A 1 100 ? 25.264 23.696  11.831  1.00 37.44 ? 100 TYR A CE1 1 
ATOM   800  C CE2 . TYR A 1 100 ? 23.872 21.753  12.125  1.00 36.30 ? 100 TYR A CE2 1 
ATOM   801  C CZ  . TYR A 1 100 ? 24.991 22.482  12.465  1.00 37.95 ? 100 TYR A CZ  1 
ATOM   802  O OH  . TYR A 1 100 ? 25.827 22.001  13.445  1.00 40.05 ? 100 TYR A OH  1 
ATOM   803  N N   . PRO A 1 101 ? 22.454 24.818  6.259   1.00 30.08 ? 101 PRO A N   1 
ATOM   804  C CA  . PRO A 1 101 ? 21.726 24.867  4.982   1.00 29.55 ? 101 PRO A CA  1 
ATOM   805  C C   . PRO A 1 101 ? 20.595 23.850  4.934   1.00 29.61 ? 101 PRO A C   1 
ATOM   806  O O   . PRO A 1 101 ? 20.606 22.842  5.647   1.00 27.12 ? 101 PRO A O   1 
ATOM   807  C CB  . PRO A 1 101 ? 22.798 24.519  3.939   1.00 30.43 ? 101 PRO A CB  1 
ATOM   808  C CG  . PRO A 1 101 ? 24.136 24.641  4.626   1.00 27.84 ? 101 PRO A CG  1 
ATOM   809  C CD  . PRO A 1 101 ? 23.819 24.302  6.093   1.00 27.89 ? 101 PRO A CD  1 
ATOM   810  N N   . LEU A 1 102 ? 19.636 24.086  4.024   1.00 25.63 ? 102 LEU A N   1 
ATOM   811  C CA  . LEU A 1 102 ? 18.443 23.250  3.908   1.00 26.37 ? 102 LEU A CA  1 
ATOM   812  C C   . LEU A 1 102 ? 18.305 22.773  2.462   1.00 27.84 ? 102 LEU A C   1 
ATOM   813  O O   . LEU A 1 102 ? 18.964 23.284  1.568   1.00 26.66 ? 102 LEU A O   1 
ATOM   814  C CB  . LEU A 1 102 ? 17.181 23.997  4.312   1.00 26.09 ? 102 LEU A CB  1 
ATOM   815  C CG  . LEU A 1 102 ? 17.206 24.443  5.792   1.00 25.31 ? 102 LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 102 ? 16.012 25.304  6.019   1.00 27.21 ? 102 LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 102 ? 17.221 23.219  6.720   1.00 28.93 ? 102 LEU A CD2 1 
ATOM   818  N N   . LEU A 1 103 ? 17.483 21.759  2.248   1.00 29.05 ? 103 LEU A N   1 
ATOM   819  C CA  . LEU A 1 103 ? 17.291 21.218  0.900   1.00 28.31 ? 103 LEU A CA  1 
ATOM   820  C C   . LEU A 1 103 ? 15.900 21.579  0.404   1.00 29.05 ? 103 LEU A C   1 
ATOM   821  O O   . LEU A 1 103 ? 14.912 21.310  1.089   1.00 30.45 ? 103 LEU A O   1 
ATOM   822  C CB  . LEU A 1 103 ? 17.455 19.696  0.895   1.00 26.40 ? 103 LEU A CB  1 
ATOM   823  C CG  . LEU A 1 103 ? 17.140 19.005  -0.441  1.00 27.39 ? 103 LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 103 ? 18.192 19.343  -1.507  1.00 23.31 ? 103 LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 103 ? 17.041 17.494  -0.228  1.00 28.14 ? 103 LEU A CD2 1 
ATOM   826  N N   . LYS A 1 104 ? 15.807 22.140  -0.807  1.00 29.79 ? 104 LYS A N   1 
ATOM   827  C CA  . LYS A 1 104 ? 14.515 22.414  -1.422  1.00 28.97 ? 104 LYS A CA  1 
ATOM   828  C C   . LYS A 1 104 ? 14.173 21.301  -2.409  1.00 31.06 ? 104 LYS A C   1 
ATOM   829  O O   . LYS A 1 104 ? 15.001 20.928  -3.257  1.00 28.60 ? 104 LYS A O   1 
ATOM   830  C CB  . LYS A 1 104 ? 14.505 23.769  -2.127  0.80 25.33 ? 104 LYS A CB  1 
ATOM   831  C CG  . LYS A 1 104 ? 13.188 24.047  -2.835  0.70 26.96 ? 104 LYS A CG  1 
ATOM   832  C CD  . LYS A 1 104 ? 13.225 25.407  -3.508  0.70 30.55 ? 104 LYS A CD  1 
ATOM   833  C CE  . LYS A 1 104 ? 11.869 25.757  -4.050  0.60 35.38 ? 104 LYS A CE  1 
ATOM   834  N NZ  . LYS A 1 104 ? 11.915 27.125  -4.624  0.60 39.82 ? 104 LYS A NZ  1 
ATOM   835  N N   . THR A 1 105 ? 12.992 20.722  -2.247  1.00 31.49 ? 105 THR A N   1 
ATOM   836  C CA  . THR A 1 105 ? 12.514 19.672  -3.138  1.00 31.95 ? 105 THR A CA  1 
ATOM   837  C C   . THR A 1 105 ? 11.273 20.187  -3.841  1.00 31.41 ? 105 THR A C   1 
ATOM   838  O O   . THR A 1 105 ? 10.339 20.651  -3.186  1.00 35.41 ? 105 THR A O   1 
ATOM   839  C CB  . THR A 1 105 ? 12.195 18.390  -2.374  1.00 35.83 ? 105 THR A CB  1 
ATOM   840  O OG1 . THR A 1 105 ? 13.382 17.929  -1.710  1.00 35.18 ? 105 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 105 ? 11.693 17.306  -3.317  1.00 36.08 ? 105 THR A CG2 1 
ATOM   842  N N   . THR A 1 106 ? 11.268 20.134  -5.175  1.00 32.41 ? 106 THR A N   1 
ATOM   843  C CA  . THR A 1 106 ? 10.077 20.504  -5.931  1.00 33.51 ? 106 THR A CA  1 
ATOM   844  C C   . THR A 1 106 ? 9.543  19.285  -6.665  1.00 34.52 ? 106 THR A C   1 
ATOM   845  O O   . THR A 1 106 ? 10.294 18.604  -7.360  1.00 35.21 ? 106 THR A O   1 
ATOM   846  C CB  . THR A 1 106 ? 10.378 21.622  -6.920  1.00 34.84 ? 106 THR A CB  1 
ATOM   847  O OG1 . THR A 1 106 ? 10.862 22.764  -6.195  1.00 36.84 ? 106 THR A OG1 1 
ATOM   848  C CG2 . THR A 1 106 ? 9.090  22.013  -7.655  1.00 34.59 ? 106 THR A CG2 1 
ATOM   849  N N   . VAL A 1 107 ? 8.250  19.022  -6.522  1.00 36.43 ? 107 VAL A N   1 
ATOM   850  C CA  . VAL A 1 107 ? 7.586  17.918  -7.211  1.00 38.40 ? 107 VAL A CA  1 
ATOM   851  C C   . VAL A 1 107 ? 6.583  18.505  -8.197  1.00 39.51 ? 107 VAL A C   1 
ATOM   852  O O   . VAL A 1 107 ? 5.617  19.165  -7.796  1.00 39.04 ? 107 VAL A O   1 
ATOM   853  C CB  . VAL A 1 107 ? 6.885  16.962  -6.231  1.00 39.73 ? 107 VAL A CB  1 
ATOM   854  C CG1 . VAL A 1 107 ? 6.355  15.748  -6.973  1.00 38.38 ? 107 VAL A CG1 1 
ATOM   855  C CG2 . VAL A 1 107 ? 7.847  16.509  -5.115  1.00 38.95 ? 107 VAL A CG2 1 
ATOM   856  N N   . LYS A 1 108 ? 6.794  18.247  -9.481  1.00 37.82 ? 108 LYS A N   1 
ATOM   857  C CA  . LYS A 1 108 ? 5.881  18.693  -10.517 1.00 40.83 ? 108 LYS A CA  1 
ATOM   858  C C   . LYS A 1 108 ? 5.057  17.510  -11.007 1.00 43.74 ? 108 LYS A C   1 
ATOM   859  O O   . LYS A 1 108 ? 5.568  16.390  -11.119 1.00 42.75 ? 108 LYS A O   1 
ATOM   860  C CB  . LYS A 1 108 ? 6.649  19.345  -11.670 0.80 41.93 ? 108 LYS A CB  1 
ATOM   861  C CG  . LYS A 1 108 ? 7.539  20.505  -11.211 0.70 41.61 ? 108 LYS A CG  1 
ATOM   862  C CD  . LYS A 1 108 ? 8.258  21.185  -12.371 0.60 43.53 ? 108 LYS A CD  1 
ATOM   863  C CE  . LYS A 1 108 ? 7.913  22.664  -12.419 0.50 45.78 ? 108 LYS A CE  1 
ATOM   864  N NZ  . LYS A 1 108 ? 8.074  23.260  -13.766 0.50 48.23 ? 108 LYS A NZ  1 
ATOM   865  N N   . TYR A 1 109 ? 3.786  17.773  -11.298 1.00 46.22 ? 109 TYR A N   1 
ATOM   866  C CA  . TYR A 1 109 ? 2.805  16.780  -11.723 1.00 51.80 ? 109 TYR A CA  1 
ATOM   867  C C   . TYR A 1 109 ? 2.310  17.045  -13.139 1.00 57.43 ? 109 TYR A C   1 
ATOM   868  O O   . TYR A 1 109 ? 2.554  18.102  -13.731 1.00 60.04 ? 109 TYR A O   1 
ATOM   869  C CB  . TYR A 1 109 ? 1.593  16.779  -10.787 1.00 52.28 ? 109 TYR A CB  1 
ATOM   870  C CG  . TYR A 1 109 ? 1.981  16.570  -9.341  1.00 51.57 ? 109 TYR A CG  1 
ATOM   871  C CD1 . TYR A 1 109 ? 2.183  15.298  -8.847  1.00 49.83 ? 109 TYR A CD1 1 
ATOM   872  C CD2 . TYR A 1 109 ? 2.144  17.647  -8.481  1.00 52.78 ? 109 TYR A CD2 1 
ATOM   873  C CE1 . TYR A 1 109 ? 2.525  15.095  -7.536  1.00 52.05 ? 109 TYR A CE1 1 
ATOM   874  C CE2 . TYR A 1 109 ? 2.497  17.462  -7.170  1.00 53.45 ? 109 TYR A CE2 1 
ATOM   875  C CZ  . TYR A 1 109 ? 2.688  16.177  -6.698  1.00 53.98 ? 109 TYR A CZ  1 
ATOM   876  O OH  . TYR A 1 109 ? 3.042  15.958  -5.385  1.00 52.72 ? 109 TYR A OH  1 
ATOM   877  N N   . GLY A 1 110 ? 1.583  16.063  -13.664 0.50 56.06 ? 110 GLY A N   1 
ATOM   878  C CA  . GLY A 1 110 ? 0.735  16.297  -14.807 0.50 55.35 ? 110 GLY A CA  1 
ATOM   879  C C   . GLY A 1 110 ? -0.398 17.235  -14.452 0.50 55.54 ? 110 GLY A C   1 
ATOM   880  O O   . GLY A 1 110 ? -0.609 17.621  -13.301 0.50 54.45 ? 110 GLY A O   1 
ATOM   881  N N   . ILE A 1 111 ? -1.162 17.603  -15.473 0.50 56.08 ? 111 ILE A N   1 
ATOM   882  C CA  . ILE A 1 111 ? -2.105 18.692  -15.308 0.50 58.17 ? 111 ILE A CA  1 
ATOM   883  C C   . ILE A 1 111 ? -3.227 18.274  -14.365 0.50 60.73 ? 111 ILE A C   1 
ATOM   884  O O   . ILE A 1 111 ? -3.697 17.128  -14.387 0.50 61.92 ? 111 ILE A O   1 
ATOM   885  C CB  . ILE A 1 111 ? -2.624 19.132  -16.685 0.50 61.23 ? 111 ILE A CB  1 
ATOM   886  C CG1 . ILE A 1 111 ? -1.622 20.105  -17.333 0.50 60.62 ? 111 ILE A CG1 1 
ATOM   887  C CG2 . ILE A 1 111 ? -4.022 19.689  -16.578 0.50 63.49 ? 111 ILE A CG2 1 
ATOM   888  C CD1 . ILE A 1 111 ? -0.590 20.701  -16.353 0.50 57.60 ? 111 ILE A CD1 1 
ATOM   889  N N   . GLY A 1 112 ? -3.648 19.206  -13.506 0.50 60.67 ? 112 GLY A N   1 
ATOM   890  C CA  . GLY A 1 112 ? -4.631 18.957  -12.473 0.50 62.05 ? 112 GLY A CA  1 
ATOM   891  C C   . GLY A 1 112 ? -4.043 19.033  -11.081 0.50 59.89 ? 112 GLY A C   1 
ATOM   892  O O   . GLY A 1 112 ? -4.751 19.396  -10.134 0.50 59.23 ? 112 GLY A O   1 
ATOM   893  N N   . LYS A 1 113 ? -2.763 18.701  -10.944 0.50 59.89 ? 113 LYS A N   1 
ATOM   894  C CA  . LYS A 1 113 ? -2.013 18.895  -9.713  0.50 60.84 ? 113 LYS A CA  1 
ATOM   895  C C   . LYS A 1 113 ? -0.971 19.987  -9.933  0.50 62.16 ? 113 LYS A C   1 
ATOM   896  O O   . LYS A 1 113 ? -0.138 19.887  -10.838 0.50 59.79 ? 113 LYS A O   1 
ATOM   897  C CB  . LYS A 1 113 ? -1.339 17.598  -9.268  0.50 58.42 ? 113 LYS A CB  1 
ATOM   898  C CG  . LYS A 1 113 ? -2.269 16.532  -8.730  0.50 59.19 ? 113 LYS A CG  1 
ATOM   899  C CD  . LYS A 1 113 ? -2.114 15.238  -9.515  0.50 59.02 ? 113 LYS A CD  1 
ATOM   900  C CE  . LYS A 1 113 ? -2.443 14.015  -8.671  0.50 58.46 ? 113 LYS A CE  1 
ATOM   901  N NZ  . LYS A 1 113 ? -1.254 13.493  -7.924  0.50 54.62 ? 113 LYS A NZ  1 
ATOM   902  N N   . LYS A 1 114 ? -1.037 21.032  -9.120  1.00 67.90 ? 114 LYS A N   1 
ATOM   903  C CA  . LYS A 1 114 ? -0.009 22.063  -9.087  1.00 69.89 ? 114 LYS A CA  1 
ATOM   904  C C   . LYS A 1 114 ? 1.259  21.539  -8.403  1.00 68.43 ? 114 LYS A C   1 
ATOM   905  O O   . LYS A 1 114 ? 1.198  20.657  -7.538  1.00 68.24 ? 114 LYS A O   1 
ATOM   906  C CB  . LYS A 1 114 ? -0.554 23.287  -8.348  1.00 74.37 ? 114 LYS A CB  1 
ATOM   907  C CG  . LYS A 1 114 ? 0.461  24.348  -7.970  0.80 76.13 ? 114 LYS A CG  1 
ATOM   908  C CD  . LYS A 1 114 ? 0.247  24.788  -6.530  0.70 77.60 ? 114 LYS A CD  1 
ATOM   909  C CE  . LYS A 1 114 ? 0.445  26.284  -6.380  0.70 78.64 ? 114 LYS A CE  1 
ATOM   910  N NZ  . LYS A 1 114 ? 0.510  26.682  -4.950  0.70 78.16 ? 114 LYS A NZ  1 
ATOM   911  N N   . GLU A 1 115 ? 2.414  22.087  -8.799  1.00 61.52 ? 115 GLU A N   1 
ATOM   912  C CA  . GLU A 1 115 ? 3.676  21.687  -8.187  1.00 57.30 ? 115 GLU A CA  1 
ATOM   913  C C   . GLU A 1 115 ? 3.665  21.963  -6.684  1.00 53.31 ? 115 GLU A C   1 
ATOM   914  O O   . GLU A 1 115 ? 2.934  22.822  -6.186  1.00 53.32 ? 115 GLU A O   1 
ATOM   915  C CB  . GLU A 1 115 ? 4.857  22.404  -8.850  1.00 58.07 ? 115 GLU A CB  1 
ATOM   916  C CG  . GLU A 1 115 ? 5.324  23.675  -8.158  1.00 60.70 ? 115 GLU A CG  1 
ATOM   917  C CD  . GLU A 1 115 ? 6.507  24.333  -8.873  1.00 63.52 ? 115 GLU A CD  1 
ATOM   918  O OE1 . GLU A 1 115 ? 7.191  25.192  -8.257  0.86 64.42 ? 115 GLU A OE1 1 
ATOM   919  O OE2 . GLU A 1 115 ? 6.751  23.996  -10.056 1.00 63.96 ? 115 GLU A OE2 1 
ATOM   920  N N   . ALA A 1 116 ? 4.479  21.208  -5.957  1.00 48.39 ? 116 ALA A N   1 
ATOM   921  C CA  . ALA A 1 116 ? 4.579  21.319  -4.509  1.00 45.94 ? 116 ALA A CA  1 
ATOM   922  C C   . ALA A 1 116 ? 6.043  21.423  -4.143  1.00 41.61 ? 116 ALA A C   1 
ATOM   923  O O   . ALA A 1 116 ? 6.882  20.750  -4.748  1.00 36.52 ? 116 ALA A O   1 
ATOM   924  C CB  . ALA A 1 116 ? 3.969  20.111  -3.808  1.00 47.09 ? 116 ALA A CB  1 
ATOM   925  N N   . THR A 1 117 ? 6.355  22.257  -3.157  1.00 41.98 ? 117 THR A N   1 
ATOM   926  C CA  . THR A 1 117 ? 7.713  22.349  -2.651  1.00 41.50 ? 117 THR A CA  1 
ATOM   927  C C   . THR A 1 117 ? 7.755  21.936  -1.184  1.00 40.48 ? 117 THR A C   1 
ATOM   928  O O   . THR A 1 117 ? 6.781  22.116  -0.449  1.00 38.43 ? 117 THR A O   1 
ATOM   929  C CB  . THR A 1 117 ? 8.272  23.759  -2.831  1.00 45.40 ? 117 THR A CB  1 
ATOM   930  O OG1 . THR A 1 117 ? 7.464  24.682  -2.093  1.00 48.73 ? 117 THR A OG1 1 
ATOM   931  C CG2 . THR A 1 117 ? 8.217  24.147  -4.307  1.00 45.25 ? 117 THR A CG2 1 
ATOM   932  N N   . TYR A 1 118 ? 8.891  21.352  -0.787  1.00 38.83 ? 118 TYR A N   1 
ATOM   933  C CA  . TYR A 1 118 ? 9.138  20.849  0.565   1.00 35.84 ? 118 TYR A CA  1 
ATOM   934  C C   . TYR A 1 118 ? 10.543 21.236  0.977   1.00 35.36 ? 118 TYR A C   1 
ATOM   935  O O   . TYR A 1 118 ? 11.471 21.199  0.172   1.00 34.61 ? 118 TYR A O   1 
ATOM   936  C CB  . TYR A 1 118 ? 9.047  19.308  0.657   1.00 35.89 ? 118 TYR A CB  1 
ATOM   937  C CG  . TYR A 1 118 ? 7.773  18.738  0.094   1.00 39.66 ? 118 TYR A CG  1 
ATOM   938  C CD1 . TYR A 1 118 ? 6.657  18.563  0.904   1.00 42.83 ? 118 TYR A CD1 1 
ATOM   939  C CD2 . TYR A 1 118 ? 7.677  18.394  -1.243  1.00 42.67 ? 118 TYR A CD2 1 
ATOM   940  C CE1 . TYR A 1 118 ? 5.483  18.068  0.395   1.00 46.47 ? 118 TYR A CE1 1 
ATOM   941  C CE2 . TYR A 1 118 ? 6.490  17.896  -1.770  1.00 44.10 ? 118 TYR A CE2 1 
ATOM   942  C CZ  . TYR A 1 118 ? 5.405  17.727  -0.940  1.00 47.37 ? 118 TYR A CZ  1 
ATOM   943  O OH  . TYR A 1 118 ? 4.224  17.232  -1.446  1.00 52.23 ? 118 TYR A OH  1 
ATOM   944  N N   . LEU A 1 119 ? 10.716 21.530  2.256   1.00 32.14 ? 119 LEU A N   1 
ATOM   945  C CA  . LEU A 1 119 ? 12.029 21.855  2.784   1.00 32.17 ? 119 LEU A CA  1 
ATOM   946  C C   . LEU A 1 119 ? 12.491 20.696  3.650   1.00 30.70 ? 119 LEU A C   1 
ATOM   947  O O   . LEU A 1 119 ? 11.699 20.142  4.423   1.00 33.79 ? 119 LEU A O   1 
ATOM   948  C CB  . LEU A 1 119 ? 11.956 23.148  3.592   1.00 38.90 ? 119 LEU A CB  1 
ATOM   949  C CG  . LEU A 1 119 ? 13.023 24.227  3.654   1.00 41.12 ? 119 LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 119 ? 13.506 24.612  2.293   1.00 39.17 ? 119 LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 119 ? 12.391 25.458  4.345   1.00 43.64 ? 119 LEU A CD2 1 
ATOM   952  N N   . ALA A 1 120 ? 13.749 20.295  3.513   1.00 28.10 ? 120 ALA A N   1 
ATOM   953  C CA  . ALA A 1 120 ? 14.262 19.200  4.317   1.00 29.58 ? 120 ALA A CA  1 
ATOM   954  C C   . ALA A 1 120 ? 15.444 19.663  5.165   1.00 29.91 ? 120 ALA A C   1 
ATOM   955  O O   . ALA A 1 120 ? 16.298 20.425  4.694   1.00 27.71 ? 120 ALA A O   1 
ATOM   956  C CB  . ALA A 1 120 ? 14.665 18.010  3.429   1.00 27.75 ? 120 ALA A CB  1 
ATOM   957  N N   . LEU A 1 121 ? 15.496 19.192  6.424   1.00 28.63 ? 121 LEU A N   1 
ATOM   958  C CA  . LEU A 1 121 ? 16.652 19.389  7.297   1.00 25.15 ? 121 LEU A CA  1 
ATOM   959  C C   . LEU A 1 121 ? 17.619 18.217  7.245   1.00 25.17 ? 121 LEU A C   1 
ATOM   960  O O   . LEU A 1 121 ? 18.836 18.402  7.392   1.00 27.75 ? 121 LEU A O   1 
ATOM   961  C CB  . LEU A 1 121 ? 16.179 19.596  8.751   1.00 26.90 ? 121 LEU A CB  1 
ATOM   962  C CG  . LEU A 1 121 ? 17.268 19.718  9.823   1.00 27.87 ? 121 LEU A CG  1 
ATOM   963  C CD1 . LEU A 1 121 ? 18.207 20.857  9.455   1.00 28.36 ? 121 LEU A CD1 1 
ATOM   964  C CD2 . LEU A 1 121 ? 16.630 19.951  11.211  1.00 25.03 ? 121 LEU A CD2 1 
ATOM   965  N N   . ASN A 1 122 ? 17.105 16.999  7.077   1.00 24.30 ? 122 ASN A N   1 
ATOM   966  C CA  . ASN A 1 122 ? 17.980 15.854  6.893   1.00 20.27 ? 122 ASN A CA  1 
ATOM   967  C C   . ASN A 1 122 ? 18.110 15.504  5.409   1.00 21.94 ? 122 ASN A C   1 
ATOM   968  O O   . ASN A 1 122 ? 19.202 15.571  4.840   1.00 22.96 ? 122 ASN A O   1 
ATOM   969  C CB  . ASN A 1 122 ? 17.460 14.624  7.615   1.00 21.10 ? 122 ASN A CB  1 
ATOM   970  C CG  . ASN A 1 122 ? 17.984 14.513  9.063   1.00 23.31 ? 122 ASN A CG  1 
ATOM   971  O OD1 . ASN A 1 122 ? 18.859 15.275  9.499   1.00 26.41 ? 122 ASN A OD1 1 
ATOM   972  N ND2 . ASN A 1 122 ? 17.463 13.539  9.782   1.00 23.69 ? 122 ASN A ND2 1 
ATOM   973  N N   . GLU A 1 123 ? 17.039 15.045  4.785   1.00 23.43 ? 123 GLU A N   1 
ATOM   974  C CA  . GLU A 1 123 ? 17.178 14.585  3.395   1.00 21.83 ? 123 GLU A CA  1 
ATOM   975  C C   . GLU A 1 123 ? 15.808 14.427  2.762   1.00 22.64 ? 123 GLU A C   1 
ATOM   976  O O   . GLU A 1 123 ? 14.784 14.396  3.432   1.00 22.15 ? 123 GLU A O   1 
ATOM   977  C CB  . GLU A 1 123 ? 17.922 13.244  3.288   1.00 20.53 ? 123 GLU A CB  1 
ATOM   978  C CG  . GLU A 1 123 ? 17.031 12.064  3.712   1.00 21.76 ? 123 GLU A CG  1 
ATOM   979  C CD  . GLU A 1 123 ? 16.926 11.961  5.250   1.00 24.16 ? 123 GLU A CD  1 
ATOM   980  O OE1 . GLU A 1 123 ? 15.797 11.979  5.815   1.00 26.70 ? 123 GLU A OE1 1 
ATOM   981  O OE2 . GLU A 1 123 ? 18.003 11.862  5.878   1.00 26.18 ? 123 GLU A OE2 1 
ATOM   982  N N   . SER A 1 124 ? 15.806 14.289  1.432   1.00 24.49 ? 124 SER A N   1 
ATOM   983  C CA  . SER A 1 124 ? 14.622 13.845  0.704   1.00 26.57 ? 124 SER A CA  1 
ATOM   984  C C   . SER A 1 124 ? 14.998 12.581  -0.051  1.00 26.30 ? 124 SER A C   1 
ATOM   985  O O   . SER A 1 124 ? 16.086 12.514  -0.608  1.00 26.04 ? 124 SER A O   1 
ATOM   986  C CB  . SER A 1 124 ? 14.154 14.918  -0.283  1.00 28.96 ? 124 SER A CB  1 
ATOM   987  O OG  . SER A 1 124 ? 13.020 14.492  -1.019  1.00 29.50 ? 124 SER A OG  1 
ATOM   988  N N   . THR A 1 125 ? 14.141 11.561  -0.049  1.00 25.56 ? 125 THR A N   1 
ATOM   989  C CA  . THR A 1 125 ? 14.462 10.350  -0.802  1.00 25.32 ? 125 THR A CA  1 
ATOM   990  C C   . THR A 1 125 ? 13.327 10.007  -1.753  1.00 25.46 ? 125 THR A C   1 
ATOM   991  O O   . THR A 1 125 ? 12.209 10.487  -1.626  1.00 26.53 ? 125 THR A O   1 
ATOM   992  C CB  . THR A 1 125 ? 14.741 9.134   0.103   1.00 26.51 ? 125 THR A CB  1 
ATOM   993  O OG1 . THR A 1 125 ? 13.505 8.681   0.652   1.00 29.45 ? 125 THR A OG1 1 
ATOM   994  C CG2 . THR A 1 125 ? 15.746 9.494   1.235   1.00 27.74 ? 125 THR A CG2 1 
ATOM   995  N N   . VAL A 1 126 ? 13.642 9.206   -2.759  1.00 27.13 ? 126 VAL A N   1 
ATOM   996  C CA  . VAL A 1 126 ? 12.648 8.767   -3.726  1.00 27.59 ? 126 VAL A CA  1 
ATOM   997  C C   . VAL A 1 126 ? 12.851 7.288   -3.948  1.00 24.80 ? 126 VAL A C   1 
ATOM   998  O O   . VAL A 1 126 ? 13.979 6.845   -4.144  1.00 28.01 ? 126 VAL A O   1 
ATOM   999  C CB  . VAL A 1 126 ? 12.752 9.513   -5.068  1.00 29.07 ? 126 VAL A CB  1 
ATOM   1000 C CG1 . VAL A 1 126 ? 11.509 9.207   -5.921  1.00 28.31 ? 126 VAL A CG1 1 
ATOM   1001 C CG2 . VAL A 1 126 ? 12.871 11.007  -4.866  1.00 32.68 ? 126 VAL A CG2 1 
ATOM   1002 N N   . LYS A 1 127 ? 11.770 6.533   -3.907  1.00 26.86 ? 127 LYS A N   1 
ATOM   1003 C CA  . LYS A 1 127 ? 11.741 5.094   -4.105  1.00 29.30 ? 127 LYS A CA  1 
ATOM   1004 C C   . LYS A 1 127 ? 10.526 4.809   -4.986  1.00 31.19 ? 127 LYS A C   1 
ATOM   1005 O O   . LYS A 1 127 ? 9.664  5.670   -5.175  1.00 32.57 ? 127 LYS A O   1 
ATOM   1006 C CB  . LYS A 1 127 ? 11.679 4.355   -2.752  0.90 29.02 ? 127 LYS A CB  1 
ATOM   1007 C CG  . LYS A 1 127 ? 12.822 4.737   -1.799  0.80 29.72 ? 127 LYS A CG  1 
ATOM   1008 C CD  . LYS A 1 127 ? 12.634 4.098   -0.403  0.80 29.76 ? 127 LYS A CD  1 
ATOM   1009 C CE  . LYS A 1 127 ? 13.753 4.432   0.586   0.70 29.97 ? 127 LYS A CE  1 
ATOM   1010 N NZ  . LYS A 1 127 ? 13.547 3.731   1.892   0.70 28.01 ? 127 LYS A NZ  1 
ATOM   1011 N N   . SER A 1 128 ? 10.467 3.614   -5.565  1.00 32.92 ? 128 SER A N   1 
ATOM   1012 C CA  . SER A 1 128 ? 9.359  3.323   -6.456  1.00 37.49 ? 128 SER A CA  1 
ATOM   1013 C C   . SER A 1 128 ? 8.084  3.080   -5.656  1.00 43.94 ? 128 SER A C   1 
ATOM   1014 O O   . SER A 1 128 ? 8.100  2.954   -4.427  1.00 43.11 ? 128 SER A O   1 
ATOM   1015 C CB  A SER A 1 128 ? 9.638  2.073   -7.278  0.61 38.63 ? 128 SER A CB  1 
ATOM   1016 C CB  B SER A 1 128 ? 9.676  2.126   -7.351  0.39 38.44 ? 128 SER A CB  1 
ATOM   1017 O OG  A SER A 1 128 ? 9.485  0.941   -6.430  0.61 38.42 ? 128 SER A OG  1 
ATOM   1018 O OG  B SER A 1 128 ? 8.729  2.030   -8.399  0.39 40.41 ? 128 SER A OG  1 
ATOM   1019 N N   . SER A 1 129 ? 6.971  3.001   -6.383  1.00 49.03 ? 129 SER A N   1 
ATOM   1020 C CA  . SER A 1 129 ? 5.685  2.620   -5.819  1.00 54.67 ? 129 SER A CA  1 
ATOM   1021 C C   . SER A 1 129 ? 5.453  1.116   -5.881  1.00 56.50 ? 129 SER A C   1 
ATOM   1022 O O   . SER A 1 129 ? 4.308  0.673   -5.953  1.00 57.34 ? 129 SER A O   1 
ATOM   1023 C CB  . SER A 1 129 ? 4.570  3.360   -6.551  1.00 58.48 ? 129 SER A CB  1 
ATOM   1024 O OG  . SER A 1 129 ? 4.663  3.092   -7.947  1.00 61.91 ? 129 SER A OG  1 
ATOM   1025 N N   . GLY A 1 130 ? 6.513  0.319   -5.850  0.97 58.17 ? 130 GLY A N   1 
ATOM   1026 C CA  . GLY A 1 130 ? 6.400  -1.080  -6.197  0.97 60.20 ? 130 GLY A CA  1 
ATOM   1027 C C   . GLY A 1 130 ? 7.135  -1.351  -7.492  0.97 60.32 ? 130 GLY A C   1 
ATOM   1028 O O   . GLY A 1 130 ? 6.909  -0.672  -8.501  0.97 62.21 ? 130 GLY A O   1 
ATOM   1029 N N   . GLY A 1 131 ? 8.048  -2.316  -7.469  1.00 57.32 ? 131 GLY A N   1 
ATOM   1030 C CA  . GLY A 1 131 ? 8.826  -2.638  -8.640  1.00 53.50 ? 131 GLY A CA  1 
ATOM   1031 C C   . GLY A 1 131 ? 10.064 -1.773  -8.760  1.00 48.76 ? 131 GLY A C   1 
ATOM   1032 O O   . GLY A 1 131 ? 10.470 -1.081  -7.815  1.00 46.72 ? 131 GLY A O   1 
ATOM   1033 N N   . PRO A 1 132 ? 10.700 -1.806  -9.934  0.98 44.36 ? 132 PRO A N   1 
ATOM   1034 C CA  . PRO A 1 132 ? 11.972 -1.102  -10.093 0.98 41.08 ? 132 PRO A CA  1 
ATOM   1035 C C   . PRO A 1 132 ? 11.783 0.401   -10.099 0.98 38.60 ? 132 PRO A C   1 
ATOM   1036 O O   . PRO A 1 132 ? 10.815 0.933   -10.646 0.98 42.75 ? 132 PRO A O   1 
ATOM   1037 C CB  . PRO A 1 132 ? 12.495 -1.608  -11.450 0.98 39.39 ? 132 PRO A CB  1 
ATOM   1038 C CG  . PRO A 1 132 ? 11.329 -2.103  -12.144 0.98 42.28 ? 132 PRO A CG  1 
ATOM   1039 C CD  . PRO A 1 132 ? 10.388 -2.633  -11.104 0.98 42.95 ? 132 PRO A CD  1 
ATOM   1040 N N   . PHE A 1 133 ? 12.733 1.079   -9.496  1.00 35.37 ? 133 PHE A N   1 
ATOM   1041 C CA  . PHE A 1 133 ? 12.801 2.527   -9.534  1.00 34.55 ? 133 PHE A CA  1 
ATOM   1042 C C   . PHE A 1 133 ? 13.714 2.906   -10.685 1.00 34.23 ? 133 PHE A C   1 
ATOM   1043 O O   . PHE A 1 133 ? 14.872 2.487   -10.710 1.00 31.63 ? 133 PHE A O   1 
ATOM   1044 C CB  . PHE A 1 133 ? 13.329 3.046   -8.201  1.00 31.39 ? 133 PHE A CB  1 
ATOM   1045 C CG  . PHE A 1 133 ? 13.601 4.508   -8.177  1.00 30.61 ? 133 PHE A CG  1 
ATOM   1046 C CD1 . PHE A 1 133 ? 12.570 5.417   -8.157  1.00 32.36 ? 133 PHE A CD1 1 
ATOM   1047 C CD2 . PHE A 1 133 ? 14.891 4.968   -8.178  1.00 32.03 ? 133 PHE A CD2 1 
ATOM   1048 C CE1 . PHE A 1 133 ? 12.839 6.776   -8.112  1.00 31.20 ? 133 PHE A CE1 1 
ATOM   1049 C CE2 . PHE A 1 133 ? 15.149 6.332   -8.119  1.00 32.42 ? 133 PHE A CE2 1 
ATOM   1050 C CZ  . PHE A 1 133 ? 14.116 7.220   -8.079  1.00 28.37 ? 133 PHE A CZ  1 
ATOM   1051 N N   . VAL A 1 134 ? 13.180 3.634   -11.667 1.00 34.90 ? 134 VAL A N   1 
ATOM   1052 C CA  . VAL A 1 134 ? 13.947 4.063   -12.834 1.00 35.27 ? 134 VAL A CA  1 
ATOM   1053 C C   . VAL A 1 134 ? 13.675 5.544   -13.066 1.00 38.17 ? 134 VAL A C   1 
ATOM   1054 O O   . VAL A 1 134 ? 12.526 5.926   -13.322 1.00 39.24 ? 134 VAL A O   1 
ATOM   1055 C CB  . VAL A 1 134 ? 13.585 3.284   -14.102 1.00 38.58 ? 134 VAL A CB  1 
ATOM   1056 C CG1 . VAL A 1 134 ? 14.596 3.613   -15.221 1.00 38.11 ? 134 VAL A CG1 1 
ATOM   1057 C CG2 . VAL A 1 134 ? 13.512 1.785   -13.851 1.00 40.13 ? 134 VAL A CG2 1 
ATOM   1058 N N   . VAL A 1 135 ? 14.724 6.375   -13.002 1.00 34.39 ? 135 VAL A N   1 
ATOM   1059 C CA  . VAL A 1 135 ? 14.618 7.791   -13.357 1.00 31.08 ? 135 VAL A CA  1 
ATOM   1060 C C   . VAL A 1 135 ? 15.837 8.176   -14.180 1.00 30.80 ? 135 VAL A C   1 
ATOM   1061 O O   . VAL A 1 135 ? 16.913 7.590   -14.033 1.00 28.64 ? 135 VAL A O   1 
ATOM   1062 C CB  . VAL A 1 135 ? 14.517 8.728   -12.118 1.00 30.34 ? 135 VAL A CB  1 
ATOM   1063 C CG1 . VAL A 1 135 ? 13.211 8.525   -11.385 1.00 33.93 ? 135 VAL A CG1 1 
ATOM   1064 C CG2 . VAL A 1 135 ? 15.697 8.545   -11.188 1.00 28.22 ? 135 VAL A CG2 1 
ATOM   1065 N N   . ASP A 1 136 ? 15.660 9.166   -15.067 1.00 33.05 ? 136 ASP A N   1 
ATOM   1066 C CA  . ASP A 1 136 ? 16.794 9.860   -15.659 1.00 29.80 ? 136 ASP A CA  1 
ATOM   1067 C C   . ASP A 1 136 ? 17.246 10.961  -14.706 1.00 29.90 ? 136 ASP A C   1 
ATOM   1068 O O   . ASP A 1 136 ? 16.420 11.719  -14.182 1.00 30.25 ? 136 ASP A O   1 
ATOM   1069 C CB  . ASP A 1 136 ? 16.433 10.454  -17.019 1.00 32.17 ? 136 ASP A CB  1 
ATOM   1070 C CG  . ASP A 1 136 ? 16.347 9.409   -18.099 1.00 33.96 ? 136 ASP A CG  1 
ATOM   1071 O OD1 . ASP A 1 136 ? 17.128 8.440   -18.022 1.00 35.57 ? 136 ASP A OD1 1 
ATOM   1072 O OD2 . ASP A 1 136 ? 15.503 9.543   -19.013 0.69 34.93 ? 136 ASP A OD2 1 
ATOM   1073 N N   . VAL A 1 137 ? 18.546 11.032  -14.461 1.00 27.77 ? 137 VAL A N   1 
ATOM   1074 C CA  . VAL A 1 137 ? 19.135 12.024  -13.568 1.00 26.90 ? 137 VAL A CA  1 
ATOM   1075 C C   . VAL A 1 137 ? 19.727 13.115  -14.442 1.00 29.10 ? 137 VAL A C   1 
ATOM   1076 O O   . VAL A 1 137 ? 20.624 12.842  -15.246 1.00 30.18 ? 137 VAL A O   1 
ATOM   1077 C CB  . VAL A 1 137 ? 20.212 11.398  -12.672 1.00 27.77 ? 137 VAL A CB  1 
ATOM   1078 C CG1 . VAL A 1 137 ? 20.765 12.431  -11.709 1.00 28.67 ? 137 VAL A CG1 1 
ATOM   1079 C CG2 . VAL A 1 137 ? 19.631 10.213  -11.922 1.00 28.63 ? 137 VAL A CG2 1 
ATOM   1080 N N   . VAL A 1 138 ? 19.222 14.338  -14.296 1.00 28.31 ? 138 VAL A N   1 
ATOM   1081 C CA  . VAL A 1 138 ? 19.594 15.476  -15.136 1.00 31.95 ? 138 VAL A CA  1 
ATOM   1082 C C   . VAL A 1 138 ? 20.164 16.557  -14.226 1.00 33.94 ? 138 VAL A C   1 
ATOM   1083 O O   . VAL A 1 138 ? 19.513 16.973  -13.258 1.00 34.47 ? 138 VAL A O   1 
ATOM   1084 C CB  . VAL A 1 138 ? 18.386 15.992  -15.923 1.00 34.27 ? 138 VAL A CB  1 
ATOM   1085 C CG1 . VAL A 1 138 ? 18.748 17.215  -16.751 1.00 33.06 ? 138 VAL A CG1 1 
ATOM   1086 C CG2 . VAL A 1 138 ? 17.816 14.872  -16.796 1.00 32.72 ? 138 VAL A CG2 1 
ATOM   1087 N N   . ILE A 1 139 ? 21.384 16.985  -14.505 1.00 27.97 ? 139 ILE A N   1 
ATOM   1088 C CA  . ILE A 1 139 ? 22.097 17.920  -13.643 1.00 27.89 ? 139 ILE A CA  1 
ATOM   1089 C C   . ILE A 1 139 ? 22.282 19.203  -14.428 1.00 28.62 ? 139 ILE A C   1 
ATOM   1090 O O   . ILE A 1 139 ? 23.005 19.216  -15.432 1.00 29.39 ? 139 ILE A O   1 
ATOM   1091 C CB  . ILE A 1 139 ? 23.457 17.372  -13.190 1.00 29.91 ? 139 ILE A CB  1 
ATOM   1092 C CG1 . ILE A 1 139 ? 23.295 16.049  -12.429 1.00 27.77 ? 139 ILE A CG1 1 
ATOM   1093 C CG2 . ILE A 1 139 ? 24.181 18.423  -12.294 1.00 31.20 ? 139 ILE A CG2 1 
ATOM   1094 C CD1 . ILE A 1 139 ? 24.660 15.342  -12.175 1.00 24.82 ? 139 ILE A CD1 1 
ATOM   1095 N N   . ASN A 1 140 ? 21.647 20.284  -13.984 1.00 28.79 ? 140 ASN A N   1 
ATOM   1096 C CA  . ASN A 1 140 ? 21.717 21.561  -14.711 1.00 29.68 ? 140 ASN A CA  1 
ATOM   1097 C C   . ASN A 1 140 ? 21.386 21.353  -16.179 1.00 32.94 ? 140 ASN A C   1 
ATOM   1098 O O   . ASN A 1 140 ? 22.112 21.809  -17.071 1.00 30.27 ? 140 ASN A O   1 
ATOM   1099 C CB  . ASN A 1 140 ? 23.097 22.210  -14.572 1.00 32.66 ? 140 ASN A CB  1 
ATOM   1100 C CG  . ASN A 1 140 ? 23.446 22.500  -13.121 1.00 32.82 ? 140 ASN A CG  1 
ATOM   1101 O OD1 . ASN A 1 140 ? 22.581 22.919  -12.362 1.00 36.21 ? 140 ASN A OD1 1 
ATOM   1102 N ND2 . ASN A 1 140 ? 24.699 22.259  -12.725 1.00 32.55 ? 140 ASN A ND2 1 
ATOM   1103 N N   . ASP A 1 141 ? 20.310 20.605  -16.425 1.00 32.42 ? 141 ASP A N   1 
ATOM   1104 C CA  . ASP A 1 141 ? 19.773 20.358  -17.785 1.00 35.43 ? 141 ASP A CA  1 
ATOM   1105 C C   . ASP A 1 141 ? 20.605 19.384  -18.612 1.00 38.71 ? 141 ASP A C   1 
ATOM   1106 O O   . ASP A 1 141 ? 20.305 19.198  -19.826 1.00 40.72 ? 141 ASP A O   1 
ATOM   1107 C CB  . ASP A 1 141 ? 19.627 21.653  -18.586 1.00 38.85 ? 141 ASP A CB  1 
ATOM   1108 C CG  . ASP A 1 141 ? 18.731 22.675  -17.899 0.56 40.79 ? 141 ASP A CG  1 
ATOM   1109 O OD1 . ASP A 1 141 ? 17.803 22.262  -17.179 0.77 41.27 ? 141 ASP A OD1 1 
ATOM   1110 O OD2 . ASP A 1 141 ? 18.949 23.891  -18.093 0.27 41.54 ? 141 ASP A OD2 1 
ATOM   1111 N N   . ILE A 1 142 ? 21.621 18.753  -18.038 1.00 38.51 ? 142 ILE A N   1 
ATOM   1112 C CA  . ILE A 1 142 ? 22.482 17.825  -18.755 1.00 42.07 ? 142 ILE A CA  1 
ATOM   1113 C C   . ILE A 1 142 ? 22.148 16.414  -18.296 1.00 32.94 ? 142 ILE A C   1 
ATOM   1114 O O   . ILE A 1 142 ? 22.166 16.128  -17.088 1.00 27.16 ? 142 ILE A O   1 
ATOM   1115 C CB  . ILE A 1 142 ? 23.962 18.140  -18.513 1.00 53.18 ? 142 ILE A CB  1 
ATOM   1116 C CG1 . ILE A 1 142 ? 24.341 19.422  -19.253 1.00 59.73 ? 142 ILE A CG1 1 
ATOM   1117 C CG2 . ILE A 1 142 ? 24.850 16.975  -18.978 1.00 55.30 ? 142 ILE A CG2 1 
ATOM   1118 C CD1 . ILE A 1 142 ? 25.678 19.967  -18.787 1.00 62.17 ? 142 ILE A CD1 1 
ATOM   1119 N N   . HIS A 1 143 ? 21.836 15.535  -19.257 1.00 31.86 ? 143 HIS A N   1 
ATOM   1120 C CA  . HIS A 1 143 ? 21.488 14.160  -18.908 1.00 31.91 ? 143 HIS A CA  1 
ATOM   1121 C C   . HIS A 1 143 ? 22.731 13.479  -18.397 1.00 29.86 ? 143 HIS A C   1 
ATOM   1122 O O   . HIS A 1 143 ? 23.694 13.292  -19.155 1.00 28.29 ? 143 HIS A O   1 
ATOM   1123 C CB  A HIS A 1 143 ? 20.919 13.345  -20.072 0.60 34.19 ? 143 HIS A CB  1 
ATOM   1124 C CB  B HIS A 1 143 ? 20.903 13.455  -20.131 0.40 34.46 ? 143 HIS A CB  1 
ATOM   1125 C CG  A HIS A 1 143 ? 20.700 11.904  -19.697 0.60 37.04 ? 143 HIS A CG  1 
ATOM   1126 C CG  B HIS A 1 143 ? 19.500 13.874  -20.430 0.40 35.29 ? 143 HIS A CG  1 
ATOM   1127 N ND1 A HIS A 1 143 ? 21.718 10.969  -19.675 0.60 38.13 ? 143 HIS A ND1 1 
ATOM   1128 N ND1 B HIS A 1 143 ? 18.436 12.997  -20.399 0.40 36.26 ? 143 HIS A ND1 1 
ATOM   1129 C CD2 A HIS A 1 143 ? 19.609 11.272  -19.201 0.60 39.57 ? 143 HIS A CD2 1 
ATOM   1130 C CD2 B HIS A 1 143 ? 18.973 15.096  -20.681 0.40 35.46 ? 143 HIS A CD2 1 
ATOM   1131 C CE1 A HIS A 1 143 ? 21.245 9.808   -19.257 0.60 37.46 ? 143 HIS A CE1 1 
ATOM   1132 C CE1 B HIS A 1 143 ? 17.321 13.654  -20.670 0.40 36.90 ? 143 HIS A CE1 1 
ATOM   1133 N NE2 A HIS A 1 143 ? 19.971 9.968   -18.949 0.60 38.81 ? 143 HIS A NE2 1 
ATOM   1134 N NE2 B HIS A 1 143 ? 17.619 14.929  -20.843 0.40 36.20 ? 143 HIS A NE2 1 
ATOM   1135 N N   . PHE A 1 144 ? 22.709 13.097  -17.114 1.00 25.55 ? 144 PHE A N   1 
ATOM   1136 C CA  . PHE A 1 144 ? 23.872 12.503  -16.478 1.00 25.45 ? 144 PHE A CA  1 
ATOM   1137 C C   . PHE A 1 144 ? 23.844 10.978  -16.449 1.00 25.74 ? 144 PHE A C   1 
ATOM   1138 O O   . PHE A 1 144 ? 24.860 10.340  -16.712 1.00 28.27 ? 144 PHE A O   1 
ATOM   1139 C CB  . PHE A 1 144 ? 24.005 13.063  -15.049 1.00 24.20 ? 144 PHE A CB  1 
ATOM   1140 C CG  . PHE A 1 144 ? 25.199 12.548  -14.325 1.00 26.49 ? 144 PHE A CG  1 
ATOM   1141 C CD1 . PHE A 1 144 ? 26.482 13.034  -14.635 1.00 24.66 ? 144 PHE A CD1 1 
ATOM   1142 C CD2 . PHE A 1 144 ? 25.057 11.557  -13.379 1.00 26.15 ? 144 PHE A CD2 1 
ATOM   1143 C CE1 . PHE A 1 144 ? 27.580 12.539  -13.980 1.00 25.06 ? 144 PHE A CE1 1 
ATOM   1144 C CE2 . PHE A 1 144 ? 26.150 11.051  -12.697 1.00 28.32 ? 144 PHE A CE2 1 
ATOM   1145 C CZ  . PHE A 1 144 ? 27.428 11.529  -13.016 1.00 27.72 ? 144 PHE A CZ  1 
ATOM   1146 N N   . GLU A 1 145 ? 22.737 10.365  -16.049 1.00 25.91 ? 145 GLU A N   1 
ATOM   1147 C CA  . GLU A 1 145 ? 22.701 8.912   -16.007 1.00 25.23 ? 145 GLU A CA  1 
ATOM   1148 C C   . GLU A 1 145 ? 21.248 8.490   -16.011 1.00 28.37 ? 145 GLU A C   1 
ATOM   1149 O O   . GLU A 1 145 ? 20.361 9.288   -15.704 1.00 28.98 ? 145 GLU A O   1 
ATOM   1150 C CB  . GLU A 1 145 ? 23.441 8.351   -14.776 1.00 25.02 ? 145 GLU A CB  1 
ATOM   1151 C CG  . GLU A 1 145 ? 22.702 8.642   -13.436 1.00 26.05 ? 145 GLU A CG  1 
ATOM   1152 C CD  . GLU A 1 145 ? 23.503 8.236   -12.207 1.00 26.26 ? 145 GLU A CD  1 
ATOM   1153 O OE1 . GLU A 1 145 ? 22.963 8.418   -11.098 0.73 22.48 ? 145 GLU A OE1 1 
ATOM   1154 O OE2 . GLU A 1 145 ? 24.655 7.781   -12.347 0.62 19.82 ? 145 GLU A OE2 1 
ATOM   1155 N N   . ARG A 1 146 ? 21.013 7.230   -16.381 1.00 27.36 ? 146 ARG A N   1 
ATOM   1156 C CA  . ARG A 1 146 ? 19.729 6.584   -16.131 1.00 29.91 ? 146 ARG A CA  1 
ATOM   1157 C C   . ARG A 1 146 ? 19.924 5.638   -14.957 1.00 29.88 ? 146 ARG A C   1 
ATOM   1158 O O   . ARG A 1 146 ? 20.611 4.618   -15.082 1.00 30.47 ? 146 ARG A O   1 
ATOM   1159 C CB  . ARG A 1 146 ? 19.192 5.831   -17.350 1.00 32.45 ? 146 ARG A CB  1 
ATOM   1160 C CG  . ARG A 1 146 ? 17.818 5.207   -17.019 1.00 32.24 ? 146 ARG A CG  1 
ATOM   1161 C CD  . ARG A 1 146 ? 17.079 4.762   -18.300 0.80 32.10 ? 146 ARG A CD  1 
ATOM   1162 N NE  . ARG A 1 146 ? 16.485 5.899   -18.977 0.80 32.81 ? 146 ARG A NE  1 
ATOM   1163 C CZ  . ARG A 1 146 ? 15.801 5.805   -20.119 0.70 35.94 ? 146 ARG A CZ  1 
ATOM   1164 N NH1 . ARG A 1 146 ? 15.626 4.623   -20.701 0.70 34.65 ? 146 ARG A NH1 1 
ATOM   1165 N NH2 . ARG A 1 146 ? 15.282 6.888   -20.677 0.70 36.54 ? 146 ARG A NH2 1 
ATOM   1166 N N   . PHE A 1 147 ? 19.274 5.954   -13.846 1.00 29.45 ? 147 PHE A N   1 
ATOM   1167 C CA  . PHE A 1 147 ? 19.400 5.184   -12.617 1.00 27.76 ? 147 PHE A CA  1 
ATOM   1168 C C   . PHE A 1 147 ? 18.308 4.127   -12.529 1.00 29.71 ? 147 PHE A C   1 
ATOM   1169 O O   . PHE A 1 147 ? 17.128 4.452   -12.636 1.00 29.98 ? 147 PHE A O   1 
ATOM   1170 C CB  . PHE A 1 147 ? 19.297 6.119   -11.419 1.00 27.75 ? 147 PHE A CB  1 
ATOM   1171 C CG  . PHE A 1 147 ? 19.440 5.401   -10.098 1.00 24.10 ? 147 PHE A CG  1 
ATOM   1172 C CD1 . PHE A 1 147 ? 18.336 4.812   -9.491  1.00 26.14 ? 147 PHE A CD1 1 
ATOM   1173 C CD2 . PHE A 1 147 ? 20.683 5.254   -9.525  1.00 26.47 ? 147 PHE A CD2 1 
ATOM   1174 C CE1 . PHE A 1 147 ? 18.472 4.121   -8.271  1.00 25.20 ? 147 PHE A CE1 1 
ATOM   1175 C CE2 . PHE A 1 147 ? 20.822 4.584   -8.297  1.00 24.96 ? 147 PHE A CE2 1 
ATOM   1176 C CZ  . PHE A 1 147 ? 19.696 4.001   -7.710  1.00 23.42 ? 147 PHE A CZ  1 
ATOM   1177 N N   . ARG A 1 148 ? 18.703 2.864   -12.329 1.00 24.35 ? 148 ARG A N   1 
ATOM   1178 C CA  . ARG A 1 148 ? 17.750 1.794   -12.086 1.00 25.33 ? 148 ARG A CA  1 
ATOM   1179 C C   . ARG A 1 148 ? 18.181 1.100   -10.807 1.00 25.36 ? 148 ARG A C   1 
ATOM   1180 O O   . ARG A 1 148 ? 19.334 0.672   -10.690 1.00 26.54 ? 148 ARG A O   1 
ATOM   1181 C CB  . ARG A 1 148 ? 17.687 0.821   -13.249 0.80 27.22 ? 148 ARG A CB  1 
ATOM   1182 C CG  . ARG A 1 148 ? 16.683 -0.287  -13.081 0.80 26.08 ? 148 ARG A CG  1 
ATOM   1183 C CD  . ARG A 1 148 ? 16.703 -1.094  -14.374 0.80 26.50 ? 148 ARG A CD  1 
ATOM   1184 N NE  . ARG A 1 148 ? 15.741 -2.168  -14.313 0.80 31.25 ? 148 ARG A NE  1 
ATOM   1185 C CZ  . ARG A 1 148 ? 14.546 -2.119  -14.876 0.70 34.47 ? 148 ARG A CZ  1 
ATOM   1186 N NH1 . ARG A 1 148 ? 14.181 -1.040  -15.557 0.70 34.42 ? 148 ARG A NH1 1 
ATOM   1187 N NH2 . ARG A 1 148 ? 13.720 -3.150  -14.763 0.70 36.85 ? 148 ARG A NH2 1 
ATOM   1188 N N   . GLY A 1 149 ? 17.289 1.030   -9.829  1.00 25.29 ? 149 GLY A N   1 
ATOM   1189 C CA  . GLY A 1 149 ? 17.747 0.544   -8.521  1.00 23.99 ? 149 GLY A CA  1 
ATOM   1190 C C   . GLY A 1 149 ? 16.613 0.613   -7.524  1.00 23.63 ? 149 GLY A C   1 
ATOM   1191 O O   . GLY A 1 149 ? 15.457 0.545   -7.900  1.00 26.78 ? 149 GLY A O   1 
ATOM   1192 N N   . ASP A 1 150 ? 16.972 0.744   -6.237  1.00 22.91 ? 150 ASP A N   1 
ATOM   1193 C CA  . ASP A 1 150 ? 15.945 0.852   -5.216  1.00 26.40 ? 150 ASP A CA  1 
ATOM   1194 C C   . ASP A 1 150 ? 15.503 2.289   -4.976  1.00 27.29 ? 150 ASP A C   1 
ATOM   1195 O O   . ASP A 1 150 ? 14.368 2.503   -4.550  1.00 29.36 ? 150 ASP A O   1 
ATOM   1196 C CB  . ASP A 1 150 ? 16.448 0.268   -3.880  1.00 26.15 ? 150 ASP A CB  1 
ATOM   1197 C CG  . ASP A 1 150 ? 16.446 -1.243  -3.879  1.00 29.36 ? 150 ASP A CG  1 
ATOM   1198 O OD1 . ASP A 1 150 ? 15.944 -1.808  -4.854  1.00 32.44 ? 150 ASP A OD1 1 
ATOM   1199 O OD2 . ASP A 1 150 ? 16.917 -1.864  -2.911  1.00 31.20 ? 150 ASP A OD2 1 
ATOM   1200 N N   . GLY A 1 151 ? 16.356 3.273   -5.220  1.00 24.45 ? 151 GLY A N   1 
ATOM   1201 C CA  . GLY A 1 151 ? 16.021 4.641   -4.860  1.00 25.25 ? 151 GLY A CA  1 
ATOM   1202 C C   . GLY A 1 151 ? 17.233 5.550   -4.788  1.00 21.83 ? 151 GLY A C   1 
ATOM   1203 O O   . GLY A 1 151 ? 18.366 5.140   -5.009  1.00 23.37 ? 151 GLY A O   1 
ATOM   1204 N N   . LEU A 1 152 ? 16.962 6.820   -4.485  1.00 22.25 ? 152 LEU A N   1 
ATOM   1205 C CA  . LEU A 1 152 ? 18.001 7.843   -4.381  1.00 19.68 ? 152 LEU A CA  1 
ATOM   1206 C C   . LEU A 1 152 ? 17.755 8.695   -3.148  1.00 21.38 ? 152 LEU A C   1 
ATOM   1207 O O   . LEU A 1 152 ? 16.609 8.858   -2.724  1.00 24.86 ? 152 LEU A O   1 
ATOM   1208 C CB  . LEU A 1 152 ? 17.995 8.789   -5.582  1.00 22.28 ? 152 LEU A CB  1 
ATOM   1209 C CG  . LEU A 1 152 ? 18.565 8.140   -6.856  1.00 22.46 ? 152 LEU A CG  1 
ATOM   1210 C CD1 . LEU A 1 152 ? 18.146 9.013   -8.016  1.00 24.55 ? 152 LEU A CD1 1 
ATOM   1211 C CD2 . LEU A 1 152 ? 20.074 8.024   -6.820  1.00 22.53 ? 152 LEU A CD2 1 
ATOM   1212 N N   . CYS A 1 153 ? 18.835 9.230   -2.576  1.00 22.28 ? 153 CYS A N   1 
ATOM   1213 C CA  . CYS A 1 153 ? 18.738 10.036  -1.357  1.00 21.90 ? 153 CYS A CA  1 
ATOM   1214 C C   . CYS A 1 153 ? 19.528 11.315  -1.564  1.00 22.32 ? 153 CYS A C   1 
ATOM   1215 O O   . CYS A 1 153 ? 20.678 11.260  -2.005  1.00 23.08 ? 153 CYS A O   1 
ATOM   1216 C CB  . CYS A 1 153 ? 19.310 9.271   -0.162  1.00 23.24 ? 153 CYS A CB  1 
ATOM   1217 S SG  . CYS A 1 153 ? 19.499 10.248  1.391   1.00 24.30 ? 153 CYS A SG  1 
ATOM   1218 N N   . MET A 1 154 ? 18.905 12.459  -1.289  1.00 22.89 ? 154 MET A N   1 
ATOM   1219 C CA  . MET A 1 154 ? 19.556 13.759  -1.423  1.00 22.69 ? 154 MET A CA  1 
ATOM   1220 C C   . MET A 1 154 ? 19.593 14.400  -0.043  1.00 23.53 ? 154 MET A C   1 
ATOM   1221 O O   . MET A 1 154 ? 18.546 14.734  0.502   1.00 24.85 ? 154 MET A O   1 
ATOM   1222 C CB  . MET A 1 154 ? 18.820 14.681  -2.378  1.00 25.34 ? 154 MET A CB  1 
ATOM   1223 C CG  . MET A 1 154 ? 19.608 15.978  -2.584  1.00 25.21 ? 154 MET A CG  1 
ATOM   1224 S SD  . MET A 1 154 ? 21.139 15.752  -3.549  1.00 23.90 ? 154 MET A SD  1 
ATOM   1225 C CE  . MET A 1 154 ? 20.526 16.008  -5.244  1.00 22.49 ? 154 MET A CE  1 
ATOM   1226 N N   . SER A 1 155 ? 20.797 14.606  0.489   1.00 23.00 ? 155 SER A N   1 
ATOM   1227 C CA  . SER A 1 155 ? 20.987 14.963  1.893   1.00 21.54 ? 155 SER A CA  1 
ATOM   1228 C C   . SER A 1 155 ? 21.507 16.391  1.996   1.00 24.68 ? 155 SER A C   1 
ATOM   1229 O O   . SER A 1 155 ? 22.269 16.860  1.135   1.00 22.35 ? 155 SER A O   1 
ATOM   1230 C CB  . SER A 1 155 ? 21.987 14.004  2.571   1.00 22.91 ? 155 SER A CB  1 
ATOM   1231 O OG  . SER A 1 155 ? 22.236 14.376  3.949   1.00 25.32 ? 155 SER A OG  1 
ATOM   1232 N N   . THR A 1 156 ? 21.077 17.083  3.062   1.00 25.54 ? 156 THR A N   1 
ATOM   1233 C CA  . THR A 1 156 ? 21.718 18.299  3.491   1.00 26.03 ? 156 THR A CA  1 
ATOM   1234 C C   . THR A 1 156 ? 23.059 17.968  4.142   1.00 25.88 ? 156 THR A C   1 
ATOM   1235 O O   . THR A 1 156 ? 23.349 16.805  4.458   1.00 24.52 ? 156 THR A O   1 
ATOM   1236 C CB  . THR A 1 156 ? 20.855 19.027  4.522   1.00 27.60 ? 156 THR A CB  1 
ATOM   1237 O OG1 . THR A 1 156 ? 20.855 18.260  5.738   1.00 24.91 ? 156 THR A OG1 1 
ATOM   1238 C CG2 . THR A 1 156 ? 19.423 19.255  4.023   1.00 27.64 ? 156 THR A CG2 1 
ATOM   1239 N N   . PRO A 1 157 ? 23.874 18.992  4.419   1.00 23.89 ? 157 PRO A N   1 
ATOM   1240 C CA  . PRO A 1 157 ? 25.098 18.755  5.207   1.00 24.70 ? 157 PRO A CA  1 
ATOM   1241 C C   . PRO A 1 157 ? 24.833 18.121  6.566   1.00 24.09 ? 157 PRO A C   1 
ATOM   1242 O O   . PRO A 1 157 ? 25.439 17.091  6.888   1.00 25.75 ? 157 PRO A O   1 
ATOM   1243 C CB  . PRO A 1 157 ? 25.704 20.168  5.323   1.00 25.51 ? 157 PRO A CB  1 
ATOM   1244 C CG  . PRO A 1 157 ? 25.219 20.876  4.072   1.00 25.76 ? 157 PRO A CG  1 
ATOM   1245 C CD  . PRO A 1 157 ? 23.806 20.383  3.900   1.00 23.71 ? 157 PRO A CD  1 
ATOM   1246 N N   . SER A 1 158 ? 23.906 18.672  7.359   1.00 25.40 ? 158 SER A N   1 
ATOM   1247 C CA  . SER A 1 158 ? 23.667 18.068  8.669   1.00 24.09 ? 158 SER A CA  1 
ATOM   1248 C C   . SER A 1 158 ? 22.951 16.737  8.527   1.00 24.71 ? 158 SER A C   1 
ATOM   1249 O O   . SER A 1 158 ? 23.034 15.891  9.421   1.00 25.08 ? 158 SER A O   1 
ATOM   1250 C CB  . SER A 1 158 ? 22.884 19.021  9.568   1.00 25.19 ? 158 SER A CB  1 
ATOM   1251 O OG  . SER A 1 158 ? 21.647 19.401  9.006   1.00 23.30 ? 158 SER A OG  1 
ATOM   1252 N N   . GLY A 1 159 ? 22.285 16.509  7.397   1.00 25.29 ? 159 GLY A N   1 
ATOM   1253 C CA  . GLY A 1 159 ? 21.737 15.187  7.128   1.00 23.72 ? 159 GLY A CA  1 
ATOM   1254 C C   . GLY A 1 159 ? 22.777 14.142  6.791   1.00 24.74 ? 159 GLY A C   1 
ATOM   1255 O O   . GLY A 1 159 ? 22.441 12.944  6.757   1.00 24.27 ? 159 GLY A O   1 
ATOM   1256 N N   . THR A 1 160 ? 24.022 14.544  6.516   1.00 22.35 ? 160 THR A N   1 
ATOM   1257 C CA  . THR A 1 160 ? 24.951 13.536  6.020   1.00 22.80 ? 160 THR A CA  1 
ATOM   1258 C C   . THR A 1 160 ? 25.269 12.480  7.064   1.00 24.59 ? 160 THR A C   1 
ATOM   1259 O O   . THR A 1 160 ? 25.646 11.373  6.689   1.00 24.47 ? 160 THR A O   1 
ATOM   1260 C CB  . THR A 1 160 ? 26.275 14.137  5.470   1.00 25.15 ? 160 THR A CB  1 
ATOM   1261 O OG1 . THR A 1 160 ? 26.955 14.936  6.463   1.00 24.39 ? 160 THR A OG1 1 
ATOM   1262 C CG2 . THR A 1 160 ? 25.984 14.955  4.187   1.00 24.29 ? 160 THR A CG2 1 
ATOM   1263 N N   . THR A 1 161 ? 25.064 12.767  8.366   1.00 25.32 ? 161 THR A N   1 
ATOM   1264 C CA  . THR A 1 161 ? 25.283 11.756  9.390   1.00 24.71 ? 161 THR A CA  1 
ATOM   1265 C C   . THR A 1 161 ? 24.084 10.830  9.581   1.00 27.44 ? 161 THR A C   1 
ATOM   1266 O O   . THR A 1 161 ? 24.145 9.924   10.421  1.00 24.46 ? 161 THR A O   1 
ATOM   1267 C CB  . THR A 1 161 ? 25.640 12.449  10.731  1.00 22.76 ? 161 THR A CB  1 
ATOM   1268 O OG1 . THR A 1 161 ? 24.794 13.592  10.896  1.00 23.45 ? 161 THR A OG1 1 
ATOM   1269 C CG2 . THR A 1 161 ? 27.075 12.979  10.632  1.00 24.96 ? 161 THR A CG2 1 
ATOM   1270 N N   . ALA A 1 162 ? 23.024 10.986  8.800   1.00 24.69 ? 162 ALA A N   1 
ATOM   1271 C CA  . ALA A 1 162 ? 21.798 10.208  8.976   1.00 25.56 ? 162 ALA A CA  1 
ATOM   1272 C C   . ALA A 1 162 ? 21.698 9.176   7.859   1.00 27.33 ? 162 ALA A C   1 
ATOM   1273 O O   . ALA A 1 162 ? 22.663 8.428   7.653   1.00 24.97 ? 162 ALA A O   1 
ATOM   1274 C CB  . ALA A 1 162 ? 20.621 11.169  9.056   1.00 25.06 ? 162 ALA A CB  1 
ATOM   1275 N N   . TYR A 1 163 ? 20.565 9.074   7.148   1.00 23.18 ? 163 TYR A N   1 
ATOM   1276 C CA  . TYR A 1 163 ? 20.405 8.076   6.087   1.00 20.95 ? 163 TYR A CA  1 
ATOM   1277 C C   . TYR A 1 163 ? 21.608 8.064   5.154   1.00 22.80 ? 163 TYR A C   1 
ATOM   1278 O O   . TYR A 1 163 ? 22.127 7.000   4.802   1.00 23.52 ? 163 TYR A O   1 
ATOM   1279 C CB  . TYR A 1 163 ? 19.118 8.398   5.307   1.00 21.89 ? 163 TYR A CB  1 
ATOM   1280 C CG  . TYR A 1 163 ? 18.430 7.252   4.611   1.00 23.43 ? 163 TYR A CG  1 
ATOM   1281 C CD1 . TYR A 1 163 ? 19.025 6.001   4.507   1.00 24.36 ? 163 TYR A CD1 1 
ATOM   1282 C CD2 . TYR A 1 163 ? 17.143 7.425   4.096   1.00 28.40 ? 163 TYR A CD2 1 
ATOM   1283 C CE1 . TYR A 1 163 ? 18.350 4.944   3.855   1.00 27.47 ? 163 TYR A CE1 1 
ATOM   1284 C CE2 . TYR A 1 163 ? 16.465 6.392   3.452   1.00 31.42 ? 163 TYR A CE2 1 
ATOM   1285 C CZ  . TYR A 1 163 ? 17.081 5.168   3.305   1.00 31.46 ? 163 TYR A CZ  1 
ATOM   1286 O OH  . TYR A 1 163 ? 16.381 4.160   2.669   1.00 30.66 ? 163 TYR A OH  1 
ATOM   1287 N N   . ASN A 1 164 ? 22.060 9.251   4.744   1.00 22.06 ? 164 ASN A N   1 
ATOM   1288 C CA  . ASN A 1 164 ? 23.194 9.397   3.833   1.00 20.62 ? 164 ASN A CA  1 
ATOM   1289 C C   . ASN A 1 164 ? 24.383 8.556   4.290   1.00 22.95 ? 164 ASN A C   1 
ATOM   1290 O O   . ASN A 1 164 ? 25.014 7.853   3.494   1.00 22.20 ? 164 ASN A O   1 
ATOM   1291 C CB  . ASN A 1 164 ? 23.576 10.881  3.770   1.00 21.84 ? 164 ASN A CB  1 
ATOM   1292 C CG  . ASN A 1 164 ? 24.897 11.133  3.059   1.00 22.69 ? 164 ASN A CG  1 
ATOM   1293 O OD1 . ASN A 1 164 ? 24.915 11.335  1.846   1.00 21.71 ? 164 ASN A OD1 1 
ATOM   1294 N ND2 . ASN A 1 164 ? 26.003 11.169  3.812   1.00 22.28 ? 164 ASN A ND2 1 
ATOM   1295 N N   . LYS A 1 165 ? 24.671 8.581   5.590   1.00 20.67 ? 165 LYS A N   1 
ATOM   1296 C CA  . LYS A 1 165 ? 25.815 7.831   6.085   1.00 19.17 ? 165 LYS A CA  1 
ATOM   1297 C C   . LYS A 1 165 ? 25.609 6.342   5.870   1.00 20.05 ? 165 LYS A C   1 
ATOM   1298 O O   . LYS A 1 165 ? 26.549 5.617   5.520   1.00 22.01 ? 165 LYS A O   1 
ATOM   1299 C CB  . LYS A 1 165 ? 25.992 8.109   7.575   1.00 20.04 ? 165 LYS A CB  1 
ATOM   1300 C CG  . LYS A 1 165 ? 27.211 7.370   8.190   1.00 22.83 ? 165 LYS A CG  1 
ATOM   1301 C CD  . LYS A 1 165 ? 27.456 7.874   9.595   1.00 24.02 ? 165 LYS A CD  1 
ATOM   1302 C CE  . LYS A 1 165 ? 28.817 7.270   10.028  1.00 28.05 ? 165 LYS A CE  1 
ATOM   1303 N NZ  . LYS A 1 165 ? 28.627 5.806   10.396  1.00 30.31 ? 165 LYS A NZ  1 
ATOM   1304 N N   . SER A 1 166 ? 24.385 5.864   6.089   1.00 19.57 ? 166 SER A N   1 
ATOM   1305 C CA  . SER A 1 166 ? 24.125 4.428   5.942   1.00 21.19 ? 166 SER A CA  1 
ATOM   1306 C C   . SER A 1 166 ? 24.242 3.976   4.499   1.00 23.00 ? 166 SER A C   1 
ATOM   1307 O O   . SER A 1 166 ? 24.424 2.774   4.250   1.00 21.64 ? 166 SER A O   1 
ATOM   1308 C CB  . SER A 1 166 ? 22.725 4.076   6.443   1.00 26.10 ? 166 SER A CB  1 
ATOM   1309 O OG  . SER A 1 166 ? 22.663 4.213   7.856   1.00 33.12 ? 166 SER A OG  1 
ATOM   1310 N N   . LEU A 1 167 ? 24.109 4.905   3.571   1.00 24.23 ? 167 LEU A N   1 
ATOM   1311 C CA  . LEU A 1 167 ? 24.200 4.645   2.140   1.00 21.27 ? 167 LEU A CA  1 
ATOM   1312 C C   . LEU A 1 167 ? 25.606 4.837   1.612   1.00 25.17 ? 167 LEU A C   1 
ATOM   1313 O O   . LEU A 1 167 ? 25.842 4.721   0.396   1.00 24.06 ? 167 LEU A O   1 
ATOM   1314 C CB  . LEU A 1 167 ? 23.247 5.582   1.387   1.00 21.19 ? 167 LEU A CB  1 
ATOM   1315 C CG  . LEU A 1 167 ? 21.776 5.301   1.721   1.00 25.08 ? 167 LEU A CG  1 
ATOM   1316 C CD1 . LEU A 1 167 ? 20.819 6.347   1.145   1.00 24.81 ? 167 LEU A CD1 1 
ATOM   1317 C CD2 . LEU A 1 167 ? 21.363 3.901   1.266   1.00 24.12 ? 167 LEU A CD2 1 
ATOM   1318 N N   . GLY A 1 168 ? 26.571 5.086   2.470   1.00 22.10 ? 168 GLY A N   1 
ATOM   1319 C CA  . GLY A 1 168 ? 27.925 5.249   1.990   1.00 22.25 ? 168 GLY A CA  1 
ATOM   1320 C C   . GLY A 1 168 ? 28.327 6.659   1.679   1.00 23.01 ? 168 GLY A C   1 
ATOM   1321 O O   . GLY A 1 168 ? 29.448 6.868   1.170   1.00 24.19 ? 168 GLY A O   1 
ATOM   1322 N N   . GLY A 1 169 ? 27.492 7.647   2.015   1.00 20.98 ? 169 GLY A N   1 
ATOM   1323 C CA  . GLY A 1 169 ? 27.820 9.015   1.665   1.00 21.17 ? 169 GLY A CA  1 
ATOM   1324 C C   . GLY A 1 169 ? 28.912 9.580   2.562   1.00 24.30 ? 169 GLY A C   1 
ATOM   1325 O O   . GLY A 1 169 ? 29.193 9.031   3.629   1.00 22.94 ? 169 GLY A O   1 
ATOM   1326 N N   . ALA A 1 170 ? 29.521 10.685  2.106   1.00 21.72 ? 170 ALA A N   1 
ATOM   1327 C CA  . ALA A 1 170 ? 30.509 11.389  2.910   1.00 24.18 ? 170 ALA A CA  1 
ATOM   1328 C C   . ALA A 1 170 ? 29.818 12.167  4.032   1.00 21.94 ? 170 ALA A C   1 
ATOM   1329 O O   . ALA A 1 170 ? 28.682 12.621  3.874   1.00 22.09 ? 170 ALA A O   1 
ATOM   1330 C CB  . ALA A 1 170 ? 31.303 12.353  2.031   1.00 25.22 ? 170 ALA A CB  1 
ATOM   1331 N N   . LEU A 1 171 ? 30.514 12.353  5.171   1.00 24.46 ? 171 LEU A N   1 
ATOM   1332 C CA  . LEU A 1 171 ? 30.027 13.292  6.185   1.00 21.48 ? 171 LEU A CA  1 
ATOM   1333 C C   . LEU A 1 171 ? 30.594 14.664  5.859   1.00 22.10 ? 171 LEU A C   1 
ATOM   1334 O O   . LEU A 1 171 ? 31.799 14.792  5.665   1.00 27.14 ? 171 LEU A O   1 
ATOM   1335 C CB  . LEU A 1 171 ? 30.488 12.888  7.583   1.00 20.19 ? 171 LEU A CB  1 
ATOM   1336 C CG  . LEU A 1 171 ? 30.269 11.403  7.864   1.00 22.63 ? 171 LEU A CG  1 
ATOM   1337 C CD1 . LEU A 1 171 ? 30.658 11.141  9.332   1.00 22.29 ? 171 LEU A CD1 1 
ATOM   1338 C CD2 . LEU A 1 171 ? 28.813 10.981  7.623   1.00 25.32 ? 171 LEU A CD2 1 
ATOM   1339 N N   . MET A 1 172 ? 29.748 15.684  5.763   1.00 21.43 ? 172 MET A N   1 
ATOM   1340 C CA  . MET A 1 172 ? 30.216 17.018  5.375   1.00 22.71 ? 172 MET A CA  1 
ATOM   1341 C C   . MET A 1 172 ? 29.949 18.011  6.490   1.00 28.20 ? 172 MET A C   1 
ATOM   1342 O O   . MET A 1 172 ? 28.867 17.997  7.064   1.00 29.11 ? 172 MET A O   1 
ATOM   1343 C CB  . MET A 1 172 ? 29.483 17.520  4.101   1.00 25.23 ? 172 MET A CB  1 
ATOM   1344 C CG  . MET A 1 172 ? 29.222 16.500  3.039   0.85 30.18 ? 172 MET A CG  1 
ATOM   1345 S SD  . MET A 1 172 ? 28.302 17.336  1.691   0.78 31.10 ? 172 MET A SD  1 
ATOM   1346 C CE  . MET A 1 172 ? 29.311 18.774  1.469   0.75 25.09 ? 172 MET A CE  1 
ATOM   1347 N N   . HIS A 1 173 ? 30.927 18.875  6.795   1.00 25.37 ? 173 HIS A N   1 
ATOM   1348 C CA  . HIS A 1 173 ? 30.697 19.903  7.787   1.00 27.61 ? 173 HIS A CA  1 
ATOM   1349 C C   . HIS A 1 173 ? 29.545 20.805  7.365   1.00 30.43 ? 173 HIS A C   1 
ATOM   1350 O O   . HIS A 1 173 ? 29.530 21.279  6.220   1.00 31.50 ? 173 HIS A O   1 
ATOM   1351 C CB  . HIS A 1 173 ? 31.927 20.766  8.002   1.00 27.29 ? 173 HIS A CB  1 
ATOM   1352 C CG  . HIS A 1 173 ? 31.797 21.631  9.211   1.00 29.00 ? 173 HIS A CG  1 
ATOM   1353 N ND1 . HIS A 1 173 ? 31.321 22.922  9.160   1.00 31.15 ? 173 HIS A ND1 1 
ATOM   1354 C CD2 . HIS A 1 173 ? 32.019 21.362  10.514  1.00 29.92 ? 173 HIS A CD2 1 
ATOM   1355 C CE1 . HIS A 1 173 ? 31.284 23.426  10.381  1.00 32.21 ? 173 HIS A CE1 1 
ATOM   1356 N NE2 . HIS A 1 173 ? 31.697 22.496  11.225  1.00 31.78 ? 173 HIS A NE2 1 
ATOM   1357 N N   . PRO A 1 174 ? 28.602 21.118  8.261   1.00 31.05 ? 174 PRO A N   1 
ATOM   1358 C CA  . PRO A 1 174 ? 27.393 21.836  7.837   1.00 31.54 ? 174 PRO A CA  1 
ATOM   1359 C C   . PRO A 1 174 ? 27.602 23.298  7.488   1.00 32.56 ? 174 PRO A C   1 
ATOM   1360 O O   . PRO A 1 174 ? 26.641 23.967  7.100   1.00 38.51 ? 174 PRO A O   1 
ATOM   1361 C CB  . PRO A 1 174 ? 26.444 21.664  9.040   1.00 34.12 ? 174 PRO A CB  1 
ATOM   1362 C CG  . PRO A 1 174 ? 27.303 21.281  10.202  1.00 34.41 ? 174 PRO A CG  1 
ATOM   1363 C CD  . PRO A 1 174 ? 28.515 20.605  9.644   1.00 33.13 ? 174 PRO A CD  1 
ATOM   1364 N N   . SER A 1 175 ? 28.802 23.843  7.581   1.00 31.33 ? 175 SER A N   1 
ATOM   1365 C CA  . SER A 1 175 ? 28.999 25.171  7.040   1.00 32.09 ? 175 SER A CA  1 
ATOM   1366 C C   . SER A 1 175 ? 29.128 25.154  5.520   1.00 34.01 ? 175 SER A C   1 
ATOM   1367 O O   . SER A 1 175 ? 29.153 26.222  4.911   1.00 35.88 ? 175 SER A O   1 
ATOM   1368 C CB  . SER A 1 175 ? 30.243 25.821  7.645   1.00 31.63 ? 175 SER A CB  1 
ATOM   1369 O OG  . SER A 1 175 ? 31.358 25.011  7.334   1.00 34.14 ? 175 SER A OG  1 
ATOM   1370 N N   . ILE A 1 176 ? 29.248 23.975  4.898   1.00 29.59 ? 176 ILE A N   1 
ATOM   1371 C CA  . ILE A 1 176 ? 29.374 23.890  3.446   1.00 28.28 ? 176 ILE A CA  1 
ATOM   1372 C C   . ILE A 1 176 ? 27.980 23.941  2.849   1.00 30.84 ? 176 ILE A C   1 
ATOM   1373 O O   . ILE A 1 176 ? 27.111 23.140  3.209   1.00 29.71 ? 176 ILE A O   1 
ATOM   1374 C CB  . ILE A 1 176 ? 30.087 22.594  3.039   1.00 25.34 ? 176 ILE A CB  1 
ATOM   1375 C CG1 . ILE A 1 176 ? 31.479 22.565  3.678   1.00 29.03 ? 176 ILE A CG1 1 
ATOM   1376 C CG2 . ILE A 1 176 ? 30.180 22.475  1.493   1.00 26.32 ? 176 ILE A CG2 1 
ATOM   1377 C CD1 . ILE A 1 176 ? 32.146 21.210  3.623   1.00 28.21 ? 176 ILE A CD1 1 
ATOM   1378 N N   . GLU A 1 177 ? 27.753 24.880  1.927   1.00 29.59 ? 177 GLU A N   1 
ATOM   1379 C CA  . GLU A 1 177 ? 26.413 25.032  1.371   1.00 29.93 ? 177 GLU A CA  1 
ATOM   1380 C C   . GLU A 1 177 ? 26.312 24.061  0.200   1.00 29.84 ? 177 GLU A C   1 
ATOM   1381 O O   . GLU A 1 177 ? 26.765 24.353  -0.901  1.00 28.83 ? 177 GLU A O   1 
ATOM   1382 C CB  . GLU A 1 177 ? 26.152 26.485  0.980   1.00 33.72 ? 177 GLU A CB  1 
ATOM   1383 C CG  . GLU A 1 177 ? 26.078 27.373  2.254   1.00 35.21 ? 177 GLU A CG  1 
ATOM   1384 C CD  . GLU A 1 177 ? 25.756 28.831  1.997   1.00 42.39 ? 177 GLU A CD  1 
ATOM   1385 O OE1 . GLU A 1 177 ? 25.133 29.465  2.877   0.71 44.42 ? 177 GLU A OE1 1 
ATOM   1386 O OE2 . GLU A 1 177 ? 26.140 29.357  0.936   0.79 44.66 ? 177 GLU A OE2 1 
ATOM   1387 N N   . ALA A 1 178 ? 25.737 22.890  0.445   1.00 26.31 ? 178 ALA A N   1 
ATOM   1388 C CA  . ALA A 1 178 ? 25.785 21.827  -0.554  1.00 23.02 ? 178 ALA A CA  1 
ATOM   1389 C C   . ALA A 1 178 ? 24.678 20.827  -0.274  1.00 25.41 ? 178 ALA A C   1 
ATOM   1390 O O   . ALA A 1 178 ? 24.043 20.848  0.788   1.00 26.48 ? 178 ALA A O   1 
ATOM   1391 C CB  . ALA A 1 178 ? 27.150 21.133  -0.548  1.00 23.50 ? 178 ALA A CB  1 
ATOM   1392 N N   . MET A 1 179 ? 24.473 19.920  -1.235  1.00 23.57 ? 179 MET A N   1 
ATOM   1393 C CA  . MET A 1 179 ? 23.591 18.785  -1.026  1.00 22.00 ? 179 MET A CA  1 
ATOM   1394 C C   . MET A 1 179 ? 24.302 17.580  -1.619  1.00 23.53 ? 179 MET A C   1 
ATOM   1395 O O   . MET A 1 179 ? 25.165 17.722  -2.492  1.00 23.56 ? 179 MET A O   1 
ATOM   1396 C CB  . MET A 1 179 ? 22.210 19.016  -1.658  1.00 23.06 ? 179 MET A CB  1 
ATOM   1397 C CG  . MET A 1 179 ? 22.298 19.125  -3.209  1.00 21.40 ? 179 MET A CG  1 
ATOM   1398 S SD  . MET A 1 179 ? 20.739 19.615  -3.970  1.00 25.63 ? 179 MET A SD  1 
ATOM   1399 C CE  . MET A 1 179 ? 21.310 19.869  -5.645  1.00 22.11 ? 179 MET A CE  1 
ATOM   1400 N N   . GLN A 1 180 ? 23.952 16.385  -1.143  1.00 21.85 ? 180 GLN A N   1 
ATOM   1401 C CA  . GLN A 1 180 ? 24.713 15.193  -1.511  1.00 20.93 ? 180 GLN A CA  1 
ATOM   1402 C C   . GLN A 1 180 ? 23.771 14.095  -1.955  1.00 19.79 ? 180 GLN A C   1 
ATOM   1403 O O   . GLN A 1 180 ? 22.844 13.767  -1.222  1.00 22.02 ? 180 GLN A O   1 
ATOM   1404 C CB  . GLN A 1 180 ? 25.580 14.679  -0.330  1.00 21.42 ? 180 GLN A CB  1 
ATOM   1405 C CG  . GLN A 1 180 ? 26.348 13.410  -0.692  1.00 18.71 ? 180 GLN A CG  1 
ATOM   1406 C CD  . GLN A 1 180 ? 27.406 12.981  0.320   1.00 22.19 ? 180 GLN A CD  1 
ATOM   1407 O OE1 . GLN A 1 180 ? 28.178 12.036  0.077   1.00 23.86 ? 180 GLN A OE1 1 
ATOM   1408 N NE2 . GLN A 1 180 ? 27.447 13.663  1.461   1.00 22.04 ? 180 GLN A NE2 1 
ATOM   1409 N N   . LEU A 1 181 ? 24.008 13.520  -3.147  1.00 21.25 ? 181 LEU A N   1 
ATOM   1410 C CA  . LEU A 1 181 ? 23.148 12.482  -3.699  1.00 21.33 ? 181 LEU A CA  1 
ATOM   1411 C C   . LEU A 1 181 ? 23.791 11.116  -3.506  1.00 22.93 ? 181 LEU A C   1 
ATOM   1412 O O   . LEU A 1 181 ? 24.888 10.879  -4.008  1.00 22.40 ? 181 LEU A O   1 
ATOM   1413 C CB  . LEU A 1 181 ? 22.918 12.755  -5.204  1.00 21.57 ? 181 LEU A CB  1 
ATOM   1414 C CG  . LEU A 1 181 ? 21.964 11.819  -5.930  1.00 23.77 ? 181 LEU A CG  1 
ATOM   1415 C CD1 . LEU A 1 181 ? 20.503 12.033  -5.439  1.00 22.70 ? 181 LEU A CD1 1 
ATOM   1416 C CD2 . LEU A 1 181 ? 22.088 11.979  -7.479  1.00 21.75 ? 181 LEU A CD2 1 
ATOM   1417 N N   . THR A 1 182 ? 23.080 10.184  -2.877  1.00 20.90 ? 182 THR A N   1 
ATOM   1418 C CA  . THR A 1 182 ? 23.585 8.825   -2.769  1.00 20.30 ? 182 THR A CA  1 
ATOM   1419 C C   . THR A 1 182 ? 22.625 7.844   -3.425  1.00 23.63 ? 182 THR A C   1 
ATOM   1420 O O   . THR A 1 182 ? 21.406 8.044   -3.422  1.00 23.48 ? 182 THR A O   1 
ATOM   1421 C CB  . THR A 1 182 ? 23.808 8.410   -1.307  1.00 21.99 ? 182 THR A CB  1 
ATOM   1422 O OG1 . THR A 1 182 ? 22.645 8.714   -0.550  1.00 21.68 ? 182 THR A OG1 1 
ATOM   1423 C CG2 . THR A 1 182 ? 25.003 9.169   -0.741  1.00 20.74 ? 182 THR A CG2 1 
ATOM   1424 N N   . GLU A 1 183 ? 23.187 6.751   -3.932  1.00 23.18 ? 183 GLU A N   1 
ATOM   1425 C CA  . GLU A 1 183 ? 22.399 5.660   -4.515  1.00 22.89 ? 183 GLU A CA  1 
ATOM   1426 C C   . GLU A 1 183 ? 21.886 4.665   -3.486  1.00 25.35 ? 183 GLU A C   1 
ATOM   1427 O O   . GLU A 1 183 ? 22.529 4.407   -2.465  1.00 22.74 ? 183 GLU A O   1 
ATOM   1428 C CB  . GLU A 1 183 ? 23.263 4.880   -5.510  1.00 27.13 ? 183 GLU A CB  1 
ATOM   1429 C CG  . GLU A 1 183 ? 23.833 5.752   -6.612  1.00 25.47 ? 183 GLU A CG  1 
ATOM   1430 C CD  . GLU A 1 183 ? 24.596 4.962   -7.663  1.00 28.26 ? 183 GLU A CD  1 
ATOM   1431 O OE1 . GLU A 1 183 ? 24.876 3.759   -7.413  1.00 28.30 ? 183 GLU A OE1 1 
ATOM   1432 O OE2 . GLU A 1 183 ? 24.940 5.578   -8.726  1.00 26.89 ? 183 GLU A OE2 1 
ATOM   1433 N N   . MET A 1 184 ? 20.747 4.029   -3.798  1.00 23.82 ? 184 MET A N   1 
ATOM   1434 C CA  . MET A 1 184 ? 20.314 2.847   -3.061  1.00 24.55 ? 184 MET A CA  1 
ATOM   1435 C C   . MET A 1 184 ? 20.294 1.706   -4.062  1.00 25.57 ? 184 MET A C   1 
ATOM   1436 O O   . MET A 1 184 ? 19.381 1.642   -4.894  1.00 25.13 ? 184 MET A O   1 
ATOM   1437 C CB  . MET A 1 184 ? 18.930 3.019   -2.425  1.00 24.73 ? 184 MET A CB  1 
ATOM   1438 C CG  . MET A 1 184 ? 18.729 4.278   -1.636  1.00 28.63 ? 184 MET A CG  1 
ATOM   1439 S SD  . MET A 1 184 ? 17.059 4.271   -0.949  1.00 34.61 ? 184 MET A SD  1 
ATOM   1440 C CE  . MET A 1 184 ? 17.101 5.941   -0.325  1.00 28.80 ? 184 MET A CE  1 
ATOM   1441 N N   . ALA A 1 185 ? 21.292 0.821   -3.999  1.00 23.30 ? 185 ALA A N   1 
ATOM   1442 C CA  . ALA A 1 185 ? 21.252 -0.459  -4.728  1.00 22.61 ? 185 ALA A CA  1 
ATOM   1443 C C   . ALA A 1 185 ? 20.993 -0.271  -6.232  1.00 22.92 ? 185 ALA A C   1 
ATOM   1444 O O   . ALA A 1 185 ? 20.038 -0.776  -6.808  1.00 23.68 ? 185 ALA A O   1 
ATOM   1445 C CB  . ALA A 1 185 ? 20.217 -1.405  -4.111  1.00 24.88 ? 185 ALA A CB  1 
ATOM   1446 N N   . SER A 1 186 ? 21.877 0.444   -6.884  1.00 21.73 ? 186 SER A N   1 
ATOM   1447 C CA  A SER A 1 186 ? 21.772 0.536   -8.337  0.71 22.96 ? 186 SER A CA  1 
ATOM   1448 C CA  B SER A 1 186 ? 21.788 0.547   -8.333  0.29 23.40 ? 186 SER A CA  1 
ATOM   1449 C C   . SER A 1 186 ? 22.220 -0.766  -8.978  1.00 25.48 ? 186 SER A C   1 
ATOM   1450 O O   . SER A 1 186 ? 23.166 -1.409  -8.523  1.00 26.13 ? 186 SER A O   1 
ATOM   1451 C CB  A SER A 1 186 ? 22.646 1.645   -8.863  0.71 23.68 ? 186 SER A CB  1 
ATOM   1452 C CB  B SER A 1 186 ? 22.656 1.703   -8.823  0.29 23.60 ? 186 SER A CB  1 
ATOM   1453 O OG  A SER A 1 186 ? 23.959 1.295   -8.508  0.71 25.22 ? 186 SER A OG  1 
ATOM   1454 O OG  B SER A 1 186 ? 23.111 1.522   -10.142 0.29 23.37 ? 186 SER A OG  1 
ATOM   1455 N N   . ILE A 1 187 ? 21.542 -1.157  -10.066 1.00 26.01 ? 187 ILE A N   1 
ATOM   1456 C CA  . ILE A 1 187 ? 22.028 -2.295  -10.834 1.00 27.67 ? 187 ILE A CA  1 
ATOM   1457 C C   . ILE A 1 187 ? 23.131 -1.786  -11.761 1.00 31.49 ? 187 ILE A C   1 
ATOM   1458 O O   . ILE A 1 187 ? 23.038 -0.683  -12.308 1.00 32.54 ? 187 ILE A O   1 
ATOM   1459 C CB  . ILE A 1 187 ? 20.879 -2.969  -11.612 1.00 29.31 ? 187 ILE A CB  1 
ATOM   1460 C CG1 . ILE A 1 187 ? 21.368 -4.270  -12.250 1.00 27.10 ? 187 ILE A CG1 1 
ATOM   1461 C CG2 . ILE A 1 187 ? 20.249 -2.019  -12.653 1.00 33.63 ? 187 ILE A CG2 1 
ATOM   1462 C CD1 . ILE A 1 187 ? 20.314 -5.064  -13.021 0.75 26.02 ? 187 ILE A CD1 1 
ATOM   1463 N N   . ASN A 1 188 ? 24.202 -2.542  -11.919 1.00 28.93 ? 188 ASN A N   1 
ATOM   1464 C CA  . ASN A 1 188 ? 25.169 -2.146  -12.954 1.00 36.24 ? 188 ASN A CA  1 
ATOM   1465 C C   . ASN A 1 188 ? 25.556 -3.378  -13.737 1.00 36.35 ? 188 ASN A C   1 
ATOM   1466 O O   . ASN A 1 188 ? 26.050 -4.345  -13.153 1.00 35.15 ? 188 ASN A O   1 
ATOM   1467 C CB  . ASN A 1 188 ? 26.418 -1.474  -12.369 1.00 39.98 ? 188 ASN A CB  1 
ATOM   1468 C CG  . ASN A 1 188 ? 26.217 0.014   -12.077 1.00 39.52 ? 188 ASN A CG  1 
ATOM   1469 O OD1 . ASN A 1 188 ? 26.643 0.880   -12.851 1.00 38.20 ? 188 ASN A OD1 1 
ATOM   1470 N ND2 . ASN A 1 188 ? 25.605 0.315   -10.939 1.00 36.90 ? 188 ASN A ND2 1 
ATOM   1471 N N   . ASN A 1 189 ? 25.322 -3.357  -15.046 1.00 36.73 ? 189 ASN A N   1 
ATOM   1472 C CA  . ASN A 1 189 ? 25.745 -4.472  -15.865 1.00 38.00 ? 189 ASN A CA  1 
ATOM   1473 C C   . ASN A 1 189 ? 25.914 -3.951  -17.285 0.25 35.64 ? 189 ASN A C   1 
ATOM   1474 O O   . ASN A 1 189 ? 26.057 -2.743  -17.509 0.57 29.13 ? 189 ASN A O   1 
ATOM   1475 C CB  . ASN A 1 189 ? 24.758 -5.651  -15.742 1.00 40.42 ? 189 ASN A CB  1 
ATOM   1476 C CG  . ASN A 1 189 ? 23.336 -5.285  -16.159 1.00 44.24 ? 189 ASN A CG  1 
ATOM   1477 O OD1 . ASN A 1 189 ? 23.115 -4.269  -16.823 1.00 47.21 ? 189 ASN A OD1 1 
ATOM   1478 N ND2 . ASN A 1 189 ? 22.371 -6.137  -15.803 1.00 42.17 ? 189 ASN A ND2 1 
ATOM   1479 N N   . ARG A 1 190 ? 25.867 -4.852  -18.251 1.00 44.04 ? 190 ARG A N   1 
ATOM   1480 C CA  . ARG A 1 190 ? 26.135 -4.464  -19.631 1.00 47.64 ? 190 ARG A CA  1 
ATOM   1481 C C   . ARG A 1 190 ? 25.124 -3.441  -20.131 1.00 46.75 ? 190 ARG A C   1 
ATOM   1482 O O   . ARG A 1 190 ? 25.443 -2.625  -21.002 1.00 48.75 ? 190 ARG A O   1 
ATOM   1483 C CB  . ARG A 1 190 ? 26.117 -5.710  -20.516 1.00 52.55 ? 190 ARG A CB  1 
ATOM   1484 C CG  . ARG A 1 190 ? 27.103 -5.750  -21.657 0.90 58.26 ? 190 ARG A CG  1 
ATOM   1485 C CD  . ARG A 1 190 ? 26.716 -6.879  -22.613 0.80 63.37 ? 190 ARG A CD  1 
ATOM   1486 N NE  . ARG A 1 190 ? 26.756 -8.200  -21.978 0.70 66.61 ? 190 ARG A NE  1 
ATOM   1487 C CZ  . ARG A 1 190 ? 25.712 -8.810  -21.414 0.60 69.12 ? 190 ARG A CZ  1 
ATOM   1488 N NH1 . ARG A 1 190 ? 25.859 -10.006 -20.864 0.60 70.09 ? 190 ARG A NH1 1 
ATOM   1489 N NH2 . ARG A 1 190 ? 24.520 -8.225  -21.387 0.60 69.95 ? 190 ARG A NH2 1 
ATOM   1490 N N   . VAL A 1 191 ? 23.907 -3.472  -19.600 1.00 42.26 ? 191 VAL A N   1 
ATOM   1491 C CA  . VAL A 1 191 ? 22.841 -2.599  -20.078 1.00 46.66 ? 191 VAL A CA  1 
ATOM   1492 C C   . VAL A 1 191 ? 22.753 -1.317  -19.265 1.00 43.77 ? 191 VAL A C   1 
ATOM   1493 O O   . VAL A 1 191 ? 22.491 -0.247  -19.825 1.00 38.82 ? 191 VAL A O   1 
ATOM   1494 C CB  . VAL A 1 191 ? 21.501 -3.364  -20.069 1.00 52.62 ? 191 VAL A CB  1 
ATOM   1495 C CG1 . VAL A 1 191 ? 20.369 -2.442  -20.504 1.00 52.59 ? 191 VAL A CG1 1 
ATOM   1496 C CG2 . VAL A 1 191 ? 21.580 -4.577  -20.998 1.00 56.28 ? 191 VAL A CG2 1 
ATOM   1497 N N   . TYR A 1 192 ? 22.945 -1.413  -17.939 1.00 43.59 ? 192 TYR A N   1 
ATOM   1498 C CA  . TYR A 1 192 ? 22.696 -0.319  -17.015 1.00 40.93 ? 192 TYR A CA  1 
ATOM   1499 C C   . TYR A 1 192 ? 24.006 0.185   -16.397 1.00 41.13 ? 192 TYR A C   1 
ATOM   1500 O O   . TYR A 1 192 ? 24.869 -0.622  -16.033 1.00 43.86 ? 192 TYR A O   1 
ATOM   1501 C CB  . TYR A 1 192 ? 21.730 -0.782  -15.909 1.00 41.40 ? 192 TYR A CB  1 
ATOM   1502 C CG  . TYR A 1 192 ? 20.440 -1.418  -16.417 1.00 42.80 ? 192 TYR A CG  1 
ATOM   1503 C CD1 . TYR A 1 192 ? 19.489 -0.661  -17.096 1.00 44.29 ? 192 TYR A CD1 1 
ATOM   1504 C CD2 . TYR A 1 192 ? 20.171 -2.773  -16.197 1.00 43.72 ? 192 TYR A CD2 1 
ATOM   1505 C CE1 . TYR A 1 192 ? 18.300 -1.235  -17.576 1.00 44.59 ? 192 TYR A CE1 1 
ATOM   1506 C CE2 . TYR A 1 192 ? 18.987 -3.358  -16.650 1.00 47.21 ? 192 TYR A CE2 1 
ATOM   1507 C CZ  . TYR A 1 192 ? 18.057 -2.585  -17.350 1.00 48.13 ? 192 TYR A CZ  1 
ATOM   1508 O OH  . TYR A 1 192 ? 16.889 -3.178  -17.800 1.00 51.73 ? 192 TYR A OH  1 
ATOM   1509 N N   . ARG A 1 193 ? 24.132 1.519   -16.234 1.00 37.10 ? 193 ARG A N   1 
ATOM   1510 C CA  . ARG A 1 193 ? 25.370 2.125   -15.729 1.00 33.69 ? 193 ARG A CA  1 
ATOM   1511 C C   . ARG A 1 193 ? 25.084 3.371   -14.901 1.00 29.67 ? 193 ARG A C   1 
ATOM   1512 O O   . ARG A 1 193 ? 24.500 4.334   -15.421 1.00 30.68 ? 193 ARG A O   1 
ATOM   1513 C CB  . ARG A 1 193 ? 26.294 2.512   -16.880 1.00 35.60 ? 193 ARG A CB  1 
ATOM   1514 C CG  . ARG A 1 193 ? 27.608 3.160   -16.439 0.66 41.11 ? 193 ARG A CG  1 
ATOM   1515 C CD  . ARG A 1 193 ? 28.838 2.229   -16.622 0.67 47.18 ? 193 ARG A CD  1 
ATOM   1516 N NE  . ARG A 1 193 ? 28.857 1.119   -15.666 0.38 52.57 ? 193 ARG A NE  1 
ATOM   1517 C CZ  . ARG A 1 193 ? 29.613 1.059   -14.569 0.56 56.18 ? 193 ARG A CZ  1 
ATOM   1518 N NH1 . ARG A 1 193 ? 30.442 2.049   -14.253 0.86 57.31 ? 193 ARG A NH1 1 
ATOM   1519 N NH2 . ARG A 1 193 ? 29.541 -0.005  -13.779 0.64 58.26 ? 193 ARG A NH2 1 
ATOM   1520 N N   . THR A 1 194 ? 25.556 3.410   -13.650 1.00 24.94 ? 194 THR A N   1 
ATOM   1521 C CA  . THR A 1 194 ? 25.447 4.640   -12.882 1.00 26.18 ? 194 THR A CA  1 
ATOM   1522 C C   . THR A 1 194 ? 26.826 4.988   -12.340 1.00 27.22 ? 194 THR A C   1 
ATOM   1523 O O   . THR A 1 194 ? 27.774 4.209   -12.463 1.00 24.64 ? 194 THR A O   1 
ATOM   1524 C CB  . THR A 1 194 ? 24.428 4.517   -11.733 1.00 28.67 ? 194 THR A CB  1 
ATOM   1525 O OG1 . THR A 1 194 ? 24.899 3.546   -10.805 1.00 29.21 ? 194 THR A OG1 1 
ATOM   1526 C CG2 . THR A 1 194 ? 23.061 4.087   -12.301 1.00 29.49 ? 194 THR A CG2 1 
ATOM   1527 N N   . ILE A 1 195 ? 26.939 6.189   -11.770 1.00 25.78 ? 195 ILE A N   1 
ATOM   1528 C CA  . ILE A 1 195 ? 28.233 6.639   -11.287 1.00 24.90 ? 195 ILE A CA  1 
ATOM   1529 C C   . ILE A 1 195 ? 28.663 5.853   -10.037 1.00 25.97 ? 195 ILE A C   1 
ATOM   1530 O O   . ILE A 1 195 ? 29.858 5.604   -9.842  1.00 29.15 ? 195 ILE A O   1 
ATOM   1531 C CB  . ILE A 1 195 ? 28.188 8.157   -11.029 1.00 25.10 ? 195 ILE A CB  1 
ATOM   1532 C CG1 . ILE A 1 195 ? 29.602 8.680   -10.715 1.00 24.58 ? 195 ILE A CG1 1 
ATOM   1533 C CG2 . ILE A 1 195 ? 27.246 8.495   -9.847  1.00 24.68 ? 195 ILE A CG2 1 
ATOM   1534 C CD1 . ILE A 1 195 ? 30.597 8.606   -11.917 1.00 26.85 ? 195 ILE A CD1 1 
ATOM   1535 N N   . GLY A 1 196 ? 27.720 5.401   -9.207  1.00 24.11 ? 196 GLY A N   1 
ATOM   1536 C CA  . GLY A 1 196 ? 28.079 4.668   -7.993  1.00 23.08 ? 196 GLY A CA  1 
ATOM   1537 C C   . GLY A 1 196 ? 28.409 5.592   -6.840  1.00 26.05 ? 196 GLY A C   1 
ATOM   1538 O O   . GLY A 1 196 ? 27.756 5.570   -5.780  1.00 27.00 ? 196 GLY A O   1 
ATOM   1539 N N   . SER A 1 197 ? 29.398 6.451   -7.059  1.00 25.73 ? 197 SER A N   1 
ATOM   1540 C CA  . SER A 1 197 ? 29.902 7.342   -6.023  1.00 24.66 ? 197 SER A CA  1 
ATOM   1541 C C   . SER A 1 197 ? 28.830 8.330   -5.585  1.00 22.44 ? 197 SER A C   1 
ATOM   1542 O O   . SER A 1 197 ? 28.010 8.750   -6.393  1.00 21.48 ? 197 SER A O   1 
ATOM   1543 C CB  . SER A 1 197 ? 31.105 8.135   -6.550  1.00 24.10 ? 197 SER A CB  1 
ATOM   1544 O OG  . SER A 1 197 ? 32.021 7.253   -7.149  1.00 23.70 ? 197 SER A OG  1 
ATOM   1545 N N   . PRO A 1 198 ? 28.847 8.757   -4.315  1.00 22.33 ? 198 PRO A N   1 
ATOM   1546 C CA  . PRO A 1 198 ? 28.027 9.898   -3.912  1.00 21.94 ? 198 PRO A CA  1 
ATOM   1547 C C   . PRO A 1 198 ? 28.451 11.130  -4.689  1.00 21.78 ? 198 PRO A C   1 
ATOM   1548 O O   . PRO A 1 198 ? 29.614 11.256  -5.090  1.00 21.84 ? 198 PRO A O   1 
ATOM   1549 C CB  . PRO A 1 198 ? 28.337 10.047  -2.402  1.00 22.19 ? 198 PRO A CB  1 
ATOM   1550 C CG  . PRO A 1 198 ? 28.911 8.669   -1.980  1.00 22.18 ? 198 PRO A CG  1 
ATOM   1551 C CD  . PRO A 1 198 ? 29.695 8.263   -3.223  1.00 21.33 ? 198 PRO A CD  1 
ATOM   1552 N N   . LEU A 1 199 ? 27.501 12.047  -4.919  1.00 20.79 ? 199 LEU A N   1 
ATOM   1553 C CA  . LEU A 1 199 ? 27.787 13.265  -5.672  1.00 20.42 ? 199 LEU A CA  1 
ATOM   1554 C C   . LEU A 1 199 ? 27.450 14.455  -4.790  1.00 22.07 ? 199 LEU A C   1 
ATOM   1555 O O   . LEU A 1 199 ? 26.394 14.475  -4.162  1.00 24.59 ? 199 LEU A O   1 
ATOM   1556 C CB  . LEU A 1 199 ? 26.964 13.358  -6.994  1.00 19.63 ? 199 LEU A CB  1 
ATOM   1557 C CG  . LEU A 1 199 ? 27.094 12.228  -7.965  1.00 20.62 ? 199 LEU A CG  1 
ATOM   1558 C CD1 . LEU A 1 199 ? 26.303 12.615  -9.279  1.00 20.37 ? 199 LEU A CD1 1 
ATOM   1559 C CD2 . LEU A 1 199 ? 28.586 12.055  -8.296  1.00 22.02 ? 199 LEU A CD2 1 
ATOM   1560 N N   . VAL A 1 200 ? 28.342 15.440  -4.738  1.00 21.48 ? 200 VAL A N   1 
ATOM   1561 C CA  . VAL A 1 200 ? 28.170 16.595  -3.864  1.00 20.65 ? 200 VAL A CA  1 
ATOM   1562 C C   . VAL A 1 200 ? 28.035 17.835  -4.738  1.00 22.52 ? 200 VAL A C   1 
ATOM   1563 O O   . VAL A 1 200 ? 28.901 18.104  -5.593  1.00 23.95 ? 200 VAL A O   1 
ATOM   1564 C CB  . VAL A 1 200 ? 29.318 16.746  -2.856  1.00 21.64 ? 200 VAL A CB  1 
ATOM   1565 C CG1 . VAL A 1 200 ? 29.194 18.085  -2.097  1.00 23.67 ? 200 VAL A CG1 1 
ATOM   1566 C CG2 . VAL A 1 200 ? 29.228 15.617  -1.838  1.00 22.24 ? 200 VAL A CG2 1 
ATOM   1567 N N   . PHE A 1 201 ? 26.932 18.561  -4.554  1.00 24.18 ? 201 PHE A N   1 
ATOM   1568 C CA  . PHE A 1 201 ? 26.519 19.652  -5.430  1.00 25.73 ? 201 PHE A CA  1 
ATOM   1569 C C   . PHE A 1 201 ? 26.535 20.956  -4.652  1.00 24.96 ? 201 PHE A C   1 
ATOM   1570 O O   . PHE A 1 201 ? 26.067 20.974  -3.513  1.00 26.25 ? 201 PHE A O   1 
ATOM   1571 C CB  . PHE A 1 201 ? 25.099 19.427  -5.972  1.00 24.44 ? 201 PHE A CB  1 
ATOM   1572 C CG  . PHE A 1 201 ? 24.947 18.181  -6.776  1.00 24.02 ? 201 PHE A CG  1 
ATOM   1573 C CD1 . PHE A 1 201 ? 25.239 18.198  -8.137  1.00 25.21 ? 201 PHE A CD1 1 
ATOM   1574 C CD2 . PHE A 1 201 ? 24.498 17.007  -6.182  1.00 21.63 ? 201 PHE A CD2 1 
ATOM   1575 C CE1 . PHE A 1 201 ? 25.124 17.036  -8.898  1.00 25.95 ? 201 PHE A CE1 1 
ATOM   1576 C CE2 . PHE A 1 201 ? 24.377 15.855  -6.914  1.00 22.89 ? 201 PHE A CE2 1 
ATOM   1577 C CZ  . PHE A 1 201 ? 24.675 15.874  -8.309  1.00 23.23 ? 201 PHE A CZ  1 
ATOM   1578 N N   . PRO A 1 202 ? 26.993 22.071  -5.249  1.00 25.99 ? 202 PRO A N   1 
ATOM   1579 C CA  . PRO A 1 202 ? 26.980 23.359  -4.559  1.00 26.95 ? 202 PRO A CA  1 
ATOM   1580 C C   . PRO A 1 202 ? 25.646 24.060  -4.748  1.00 28.94 ? 202 PRO A C   1 
ATOM   1581 O O   . PRO A 1 202 ? 24.755 23.561  -5.421  1.00 27.52 ? 202 PRO A O   1 
ATOM   1582 C CB  . PRO A 1 202 ? 28.093 24.143  -5.255  1.00 28.50 ? 202 PRO A CB  1 
ATOM   1583 C CG  . PRO A 1 202 ? 27.907 23.717  -6.722  1.00 28.93 ? 202 PRO A CG  1 
ATOM   1584 C CD  . PRO A 1 202 ? 27.554 22.200  -6.611  1.00 25.03 ? 202 PRO A CD  1 
ATOM   1585 N N   . LYS A 1 203 ? 25.516 25.229  -4.119  1.00 28.79 ? 203 LYS A N   1 
ATOM   1586 C CA  . LYS A 1 203 ? 24.322 26.041  -4.306  1.00 32.35 ? 203 LYS A CA  1 
ATOM   1587 C C   . LYS A 1 203 ? 24.142 26.360  -5.781  1.00 34.23 ? 203 LYS A C   1 
ATOM   1588 O O   . LYS A 1 203 ? 25.115 26.436  -6.522  1.00 34.90 ? 203 LYS A O   1 
ATOM   1589 C CB  A LYS A 1 203 ? 24.394 27.332  -3.476  0.50 35.02 ? 203 LYS A CB  1 
ATOM   1590 C CB  B LYS A 1 203 ? 24.437 27.369  -3.566  0.50 35.00 ? 203 LYS A CB  1 
ATOM   1591 C CG  A LYS A 1 203 ? 23.069 27.655  -2.765  0.50 35.69 ? 203 LYS A CG  1 
ATOM   1592 C CG  B LYS A 1 203 ? 24.549 27.287  -2.084  0.50 33.94 ? 203 LYS A CG  1 
ATOM   1593 C CD  A LYS A 1 203 ? 23.060 29.025  -2.087  0.50 38.41 ? 203 LYS A CD  1 
ATOM   1594 C CD  B LYS A 1 203 ? 24.393 28.701  -1.542  0.50 35.81 ? 203 LYS A CD  1 
ATOM   1595 C CE  A LYS A 1 203 ? 21.803 29.201  -1.234  0.50 41.02 ? 203 LYS A CE  1 
ATOM   1596 C CE  B LYS A 1 203 ? 25.329 29.677  -2.242  0.50 36.46 ? 203 LYS A CE  1 
ATOM   1597 N NZ  A LYS A 1 203 ? 21.974 30.275  -0.213  0.50 45.20 ? 203 LYS A NZ  1 
ATOM   1598 N NZ  B LYS A 1 203 ? 25.117 31.096  -1.807  0.50 40.93 ? 203 LYS A NZ  1 
ATOM   1599 N N   . HIS A 1 204 ? 22.877 26.533  -6.189  1.00 36.14 ? 204 HIS A N   1 
ATOM   1600 C CA  . HIS A 1 204 ? 22.462 26.885  -7.552  1.00 37.72 ? 204 HIS A CA  1 
ATOM   1601 C C   . HIS A 1 204 ? 22.573 25.751  -8.562  1.00 36.22 ? 204 HIS A C   1 
ATOM   1602 O O   . HIS A 1 204 ? 22.108 25.893  -9.692  1.00 41.28 ? 204 HIS A O   1 
ATOM   1603 C CB  . HIS A 1 204 ? 23.243 28.095  -8.075  1.00 41.69 ? 204 HIS A CB  1 
ATOM   1604 C CG  . HIS A 1 204 ? 23.278 29.247  -7.123  1.00 44.15 ? 204 HIS A CG  1 
ATOM   1605 N ND1 . HIS A 1 204 ? 22.147 29.943  -6.759  1.00 46.89 ? 204 HIS A ND1 1 
ATOM   1606 C CD2 . HIS A 1 204 ? 24.308 29.837  -6.469  1.00 45.19 ? 204 HIS A CD2 1 
ATOM   1607 C CE1 . HIS A 1 204 ? 22.477 30.916  -5.927  1.00 46.34 ? 204 HIS A CE1 1 
ATOM   1608 N NE2 . HIS A 1 204 ? 23.782 30.870  -5.732  1.00 45.89 ? 204 HIS A NE2 1 
ATOM   1609 N N   . HIS A 1 205 ? 23.180 24.623  -8.213  1.00 31.38 ? 205 HIS A N   1 
ATOM   1610 C CA  . HIS A 1 205 ? 23.049 23.466  -9.071  1.00 25.25 ? 205 HIS A CA  1 
ATOM   1611 C C   . HIS A 1 205 ? 21.682 22.829  -8.865  1.00 28.31 ? 205 HIS A C   1 
ATOM   1612 O O   . HIS A 1 205 ? 21.201 22.702  -7.741  1.00 29.36 ? 205 HIS A O   1 
ATOM   1613 C CB  . HIS A 1 205 ? 24.163 22.450  -8.809  1.00 27.35 ? 205 HIS A CB  1 
ATOM   1614 C CG  . HIS A 1 205 ? 25.468 22.819  -9.456  1.00 28.59 ? 205 HIS A CG  1 
ATOM   1615 N ND1 . HIS A 1 205 ? 26.410 21.885  -9.824  1.00 28.78 ? 205 HIS A ND1 1 
ATOM   1616 C CD2 . HIS A 1 205 ? 25.979 24.029  -9.790  1.00 30.94 ? 205 HIS A CD2 1 
ATOM   1617 C CE1 . HIS A 1 205 ? 27.448 22.509  -10.360 1.00 31.63 ? 205 HIS A CE1 1 
ATOM   1618 N NE2 . HIS A 1 205 ? 27.206 23.811  -10.359 1.00 32.90 ? 205 HIS A NE2 1 
ATOM   1619 N N   . VAL A 1 206 ? 21.055 22.396  -9.953  1.00 27.94 ? 206 VAL A N   1 
ATOM   1620 C CA  . VAL A 1 206 ? 19.746 21.777  -9.871  1.00 29.83 ? 206 VAL A CA  1 
ATOM   1621 C C   . VAL A 1 206 ? 19.856 20.357  -10.390 1.00 29.40 ? 206 VAL A C   1 
ATOM   1622 O O   . VAL A 1 206 ? 20.313 20.133  -11.521 1.00 31.64 ? 206 VAL A O   1 
ATOM   1623 C CB  . VAL A 1 206 ? 18.696 22.562  -10.673 1.00 33.67 ? 206 VAL A CB  1 
ATOM   1624 C CG1 . VAL A 1 206 ? 17.328 21.901  -10.550 1.00 36.30 ? 206 VAL A CG1 1 
ATOM   1625 C CG2 . VAL A 1 206 ? 18.634 23.997  -10.211 1.00 32.64 ? 206 VAL A CG2 1 
ATOM   1626 N N   . VAL A 1 207 ? 19.380 19.409  -9.599  1.00 26.85 ? 207 VAL A N   1 
ATOM   1627 C CA  . VAL A 1 207 ? 19.336 18.008  -9.977  1.00 27.04 ? 207 VAL A CA  1 
ATOM   1628 C C   . VAL A 1 207 ? 17.887 17.657  -10.184 1.00 29.00 ? 207 VAL A C   1 
ATOM   1629 O O   . VAL A 1 207 ? 17.070 17.802  -9.262  1.00 29.78 ? 207 VAL A O   1 
ATOM   1630 C CB  . VAL A 1 207 ? 19.950 17.104  -8.901  1.00 28.19 ? 207 VAL A CB  1 
ATOM   1631 C CG1 . VAL A 1 207 ? 19.815 15.640  -9.348  1.00 29.84 ? 207 VAL A CG1 1 
ATOM   1632 C CG2 . VAL A 1 207 ? 21.403 17.478  -8.667  1.00 27.74 ? 207 VAL A CG2 1 
ATOM   1633 N N   . SER A 1 208 ? 17.563 17.187  -11.385 1.00 25.62 ? 208 SER A N   1 
ATOM   1634 C CA  . SER A 1 208 ? 16.204 16.885  -11.786 1.00 30.23 ? 208 SER A CA  1 
ATOM   1635 C C   . SER A 1 208 ? 16.101 15.385  -12.033 1.00 33.88 ? 208 SER A C   1 
ATOM   1636 O O   . SER A 1 208 ? 16.896 14.826  -12.791 1.00 34.88 ? 208 SER A O   1 
ATOM   1637 C CB  . SER A 1 208 ? 15.851 17.665  -13.068 1.00 33.22 ? 208 SER A CB  1 
ATOM   1638 O OG  . SER A 1 208 ? 14.683 17.142  -13.666 1.00 38.86 ? 208 SER A OG  1 
ATOM   1639 N N   . LEU A 1 209 ? 15.139 14.736  -11.385 1.00 29.84 ? 209 LEU A N   1 
ATOM   1640 C CA  . LEU A 1 209 ? 14.835 13.326  -11.602 1.00 29.20 ? 209 LEU A CA  1 
ATOM   1641 C C   . LEU A 1 209 ? 13.586 13.246  -12.461 1.00 34.11 ? 209 LEU A C   1 
ATOM   1642 O O   . LEU A 1 209 ? 12.549 13.793  -12.083 1.00 38.13 ? 209 LEU A O   1 
ATOM   1643 C CB  . LEU A 1 209 ? 14.595 12.587  -10.281 1.00 29.21 ? 209 LEU A CB  1 
ATOM   1644 C CG  . LEU A 1 209 ? 15.694 12.692  -9.245  1.00 30.11 ? 209 LEU A CG  1 
ATOM   1645 C CD1 . LEU A 1 209 ? 15.356 11.831  -8.023  1.00 35.02 ? 209 LEU A CD1 1 
ATOM   1646 C CD2 . LEU A 1 209 ? 17.032 12.298  -9.839  1.00 27.42 ? 209 LEU A CD2 1 
ATOM   1647 N N   . GLN A 1 210 ? 13.678 12.544  -13.594 1.00 31.82 ? 210 GLN A N   1 
ATOM   1648 C CA  . GLN A 1 210 ? 12.604 12.463  -14.554 1.00 35.41 ? 210 GLN A CA  1 
ATOM   1649 C C   . GLN A 1 210 ? 12.212 11.006  -14.796 1.00 37.46 ? 210 GLN A C   1 
ATOM   1650 O O   . GLN A 1 210 ? 13.072 10.173  -15.112 1.00 35.86 ? 210 GLN A O   1 
ATOM   1651 C CB  . GLN A 1 210 ? 13.032 13.169  -15.875 0.90 36.79 ? 210 GLN A CB  1 
ATOM   1652 C CG  . GLN A 1 210 ? 13.439 14.634  -15.589 0.80 36.78 ? 210 GLN A CG  1 
ATOM   1653 C CD  . GLN A 1 210 ? 14.015 15.388  -16.784 0.70 38.34 ? 210 GLN A CD  1 
ATOM   1654 O OE1 . GLN A 1 210 ? 14.007 14.901  -17.912 0.70 35.74 ? 210 GLN A OE1 1 
ATOM   1655 N NE2 . GLN A 1 210 ? 14.538 16.585  -16.525 0.70 39.23 ? 210 GLN A NE2 1 
ATOM   1656 N N   . PRO A 1 211 ? 10.935 10.668  -14.666 1.00 42.28 ? 211 PRO A N   1 
ATOM   1657 C CA  . PRO A 1 211 ? 10.500 9.274   -14.826 1.00 44.48 ? 211 PRO A CA  1 
ATOM   1658 C C   . PRO A 1 211 ? 10.667 8.765   -16.245 1.00 44.23 ? 211 PRO A C   1 
ATOM   1659 O O   . PRO A 1 211 ? 10.648 9.525   -17.213 1.00 44.16 ? 211 PRO A O   1 
ATOM   1660 C CB  . PRO A 1 211 ? 9.014  9.329   -14.447 1.00 48.39 ? 211 PRO A CB  1 
ATOM   1661 C CG  . PRO A 1 211 ? 8.931  10.554  -13.530 1.00 49.11 ? 211 PRO A CG  1 
ATOM   1662 C CD  . PRO A 1 211 ? 9.832  11.538  -14.237 1.00 47.37 ? 211 PRO A CD  1 
ATOM   1663 N N   . VAL A 1 212 ? 10.829 7.452   -16.355 1.00 43.74 ? 212 VAL A N   1 
ATOM   1664 C CA  . VAL A 1 212 ? 11.054 6.785   -17.630 1.00 46.88 ? 212 VAL A CA  1 
ATOM   1665 C C   . VAL A 1 212 ? 9.816  6.021   -18.075 1.00 51.23 ? 212 VAL A C   1 
ATOM   1666 O O   . VAL A 1 212 ? 9.381  6.142   -19.220 1.00 56.81 ? 212 VAL A O   1 
ATOM   1667 C CB  . VAL A 1 212 ? 12.289 5.857   -17.562 1.00 43.93 ? 212 VAL A CB  1 
ATOM   1668 C CG1 . VAL A 1 212 ? 12.497 5.124   -18.878 1.00 44.83 ? 212 VAL A CG1 1 
ATOM   1669 C CG2 . VAL A 1 212 ? 13.535 6.659   -17.200 1.00 42.70 ? 212 VAL A CG2 1 
ATOM   1670 N N   . ASN A 1 213 ? 9.228  5.234   -17.177 1.00 51.32 ? 213 ASN A N   1 
ATOM   1671 C CA  . ASN A 1 213 ? 7.974  4.551   -17.476 1.00 56.50 ? 213 ASN A CA  1 
ATOM   1672 C C   . ASN A 1 213 ? 6.961  4.765   -16.357 1.00 54.01 ? 213 ASN A C   1 
ATOM   1673 O O   . ASN A 1 213 ? 5.991  5.502   -16.534 1.00 54.31 ? 213 ASN A O   1 
ATOM   1674 C CB  . ASN A 1 213 ? 8.206  3.054   -17.708 1.00 62.31 ? 213 ASN A CB  1 
ATOM   1675 C CG  . ASN A 1 213 ? 8.732  2.749   -19.101 1.00 67.72 ? 213 ASN A CG  1 
ATOM   1676 O OD1 . ASN A 1 213 ? 8.331  3.374   -20.094 1.00 70.97 ? 213 ASN A OD1 1 
ATOM   1677 N ND2 . ASN A 1 213 ? 9.634  1.775   -19.184 0.54 67.84 ? 213 ASN A ND2 1 
ATOM   1678 N N   . ASP A 1 214 ? 7.168  4.117   -15.215 1.00 51.51 ? 214 ASP A N   1 
ATOM   1679 C CA  . ASP A 1 214 ? 6.275  4.302   -14.077 1.00 52.69 ? 214 ASP A CA  1 
ATOM   1680 C C   . ASP A 1 214 ? 6.372  5.739   -13.588 1.00 52.26 ? 214 ASP A C   1 
ATOM   1681 O O   . ASP A 1 214 ? 7.454  6.324   -13.553 1.00 54.68 ? 214 ASP A O   1 
ATOM   1682 C CB  . ASP A 1 214 ? 6.643  3.324   -12.959 0.80 52.48 ? 214 ASP A CB  1 
ATOM   1683 C CG  . ASP A 1 214 ? 5.651  3.337   -11.800 0.60 55.15 ? 214 ASP A CG  1 
ATOM   1684 O OD1 . ASP A 1 214 ? 4.704  4.150   -11.800 0.60 56.64 ? 214 ASP A OD1 1 
ATOM   1685 O OD2 . ASP A 1 214 ? 5.830  2.517   -10.872 0.60 55.54 ? 214 ASP A OD2 1 
ATOM   1686 N N   . LYS A 1 215 ? 5.238  6.317   -13.208 1.00 50.41 ? 215 LYS A N   1 
ATOM   1687 C CA  . LYS A 1 215 ? 5.224  7.712   -12.789 1.00 50.86 ? 215 LYS A CA  1 
ATOM   1688 C C   . LYS A 1 215 ? 4.804  7.900   -11.334 1.00 49.79 ? 215 LYS A C   1 
ATOM   1689 O O   . LYS A 1 215 ? 4.620  9.042   -10.903 1.00 50.94 ? 215 LYS A O   1 
ATOM   1690 C CB  . LYS A 1 215 ? 4.309  8.529   -13.699 0.90 52.66 ? 215 LYS A CB  1 
ATOM   1691 C CG  . LYS A 1 215 ? 4.610  8.342   -15.170 0.70 54.52 ? 215 LYS A CG  1 
ATOM   1692 C CD  . LYS A 1 215 ? 3.644  9.132   -16.036 0.60 57.28 ? 215 LYS A CD  1 
ATOM   1693 C CE  . LYS A 1 215 ? 4.027  9.020   -17.511 0.60 59.43 ? 215 LYS A CE  1 
ATOM   1694 N NZ  . LYS A 1 215 ? 2.965  9.540   -18.423 0.50 62.95 ? 215 LYS A NZ  1 
ATOM   1695 N N   . ASP A 1 216 ? 4.615  6.826   -10.580 1.00 46.12 ? 216 ASP A N   1 
ATOM   1696 C CA  . ASP A 1 216 ? 4.261  6.920   -9.172  1.00 44.84 ? 216 ASP A CA  1 
ATOM   1697 C C   . ASP A 1 216 ? 5.505  6.642   -8.333  1.00 42.49 ? 216 ASP A C   1 
ATOM   1698 O O   . ASP A 1 216 ? 6.260  5.702   -8.615  1.00 43.00 ? 216 ASP A O   1 
ATOM   1699 C CB  . ASP A 1 216 ? 3.151  5.934   -8.816  1.00 45.59 ? 216 ASP A CB  1 
ATOM   1700 C CG  . ASP A 1 216 ? 1.849  6.208   -9.555  1.00 50.99 ? 216 ASP A CG  1 
ATOM   1701 O OD1 . ASP A 1 216 ? 1.739  7.231   -10.279 1.00 51.35 ? 216 ASP A OD1 1 
ATOM   1702 O OD2 . ASP A 1 216 ? 0.916  5.390   -9.391  1.00 51.92 ? 216 ASP A OD2 1 
ATOM   1703 N N   . PHE A 1 217 ? 5.738  7.472   -7.316  1.00 39.67 ? 217 PHE A N   1 
ATOM   1704 C CA  . PHE A 1 217 ? 6.938  7.336   -6.497  1.00 36.24 ? 217 PHE A CA  1 
ATOM   1705 C C   . PHE A 1 217 ? 6.591  7.608   -5.048  1.00 35.92 ? 217 PHE A C   1 
ATOM   1706 O O   . PHE A 1 217 ? 5.726  8.432   -4.753  1.00 39.93 ? 217 PHE A O   1 
ATOM   1707 C CB  . PHE A 1 217 ? 8.066  8.305   -6.903  1.00 35.62 ? 217 PHE A CB  1 
ATOM   1708 C CG  . PHE A 1 217 ? 8.446  8.206   -8.353  1.00 37.66 ? 217 PHE A CG  1 
ATOM   1709 C CD1 . PHE A 1 217 ? 9.494  7.384   -8.746  1.00 37.54 ? 217 PHE A CD1 1 
ATOM   1710 C CD2 . PHE A 1 217 ? 7.741  8.903   -9.315  1.00 40.58 ? 217 PHE A CD2 1 
ATOM   1711 C CE1 . PHE A 1 217 ? 9.860  7.277   -10.094 1.00 38.55 ? 217 PHE A CE1 1 
ATOM   1712 C CE2 . PHE A 1 217 ? 8.088  8.791   -10.675 1.00 41.78 ? 217 PHE A CE2 1 
ATOM   1713 C CZ  . PHE A 1 217 ? 9.146  7.975   -11.051 1.00 40.67 ? 217 PHE A CZ  1 
ATOM   1714 N N   . GLN A 1 218 ? 7.303  6.931   -4.156  1.00 34.41 ? 218 GLN A N   1 
ATOM   1715 C CA  . GLN A 1 218 ? 7.235  7.207   -2.730  1.00 32.49 ? 218 GLN A CA  1 
ATOM   1716 C C   . GLN A 1 218 ? 8.299  8.255   -2.433  1.00 30.71 ? 218 GLN A C   1 
ATOM   1717 O O   . GLN A 1 218 ? 9.500  8.000   -2.597  1.00 30.27 ? 218 GLN A O   1 
ATOM   1718 C CB  . GLN A 1 218 ? 7.459  5.917   -1.945  0.80 34.69 ? 218 GLN A CB  1 
ATOM   1719 C CG  . GLN A 1 218 ? 7.106  6.009   -0.463  0.70 37.54 ? 218 GLN A CG  1 
ATOM   1720 C CD  . GLN A 1 218 ? 5.611  6.009   -0.210  0.60 40.64 ? 218 GLN A CD  1 
ATOM   1721 O OE1 . GLN A 1 218 ? 4.827  5.493   -1.012  0.60 43.77 ? 218 GLN A OE1 1 
ATOM   1722 N NE2 . GLN A 1 218 ? 5.205  6.593   0.903   0.60 41.86 ? 218 GLN A NE2 1 
ATOM   1723 N N   . ILE A 1 219 ? 7.880  9.461   -2.062  1.00 30.27 ? 219 ILE A N   1 
ATOM   1724 C CA  . ILE A 1 219 ? 8.824  10.546  -1.806  1.00 28.82 ? 219 ILE A CA  1 
ATOM   1725 C C   . ILE A 1 219 ? 8.833  10.840  -0.311  1.00 29.96 ? 219 ILE A C   1 
ATOM   1726 O O   . ILE A 1 219 ? 7.769  11.035  0.289   1.00 31.79 ? 219 ILE A O   1 
ATOM   1727 C CB  . ILE A 1 219 ? 8.477  11.811  -2.602  1.00 34.69 ? 219 ILE A CB  1 
ATOM   1728 C CG1 . ILE A 1 219 ? 8.546  11.519  -4.109  1.00 35.51 ? 219 ILE A CG1 1 
ATOM   1729 C CG2 . ILE A 1 219 ? 9.457  12.909  -2.252  1.00 36.04 ? 219 ILE A CG2 1 
ATOM   1730 C CD1 . ILE A 1 219 ? 8.064  12.681  -4.938  1.00 39.62 ? 219 ILE A CD1 1 
ATOM   1731 N N   . SER A 1 220 ? 10.026 10.882  0.285   1.00 31.22 ? 220 SER A N   1 
ATOM   1732 C CA  . SER A 1 220 ? 10.143 11.200  1.705   1.00 33.14 ? 220 SER A CA  1 
ATOM   1733 C C   . SER A 1 220 ? 10.831 12.546  1.868   1.00 34.18 ? 220 SER A C   1 
ATOM   1734 O O   . SER A 1 220 ? 11.668 12.937  1.053   1.00 35.40 ? 220 SER A O   1 
ATOM   1735 C CB  . SER A 1 220 ? 10.942 10.147  2.447   1.00 33.25 ? 220 SER A CB  1 
ATOM   1736 O OG  . SER A 1 220 ? 12.330 10.410  2.205   1.00 35.34 ? 220 SER A OG  1 
ATOM   1737 N N   . VAL A 1 221 ? 10.446 13.279  2.901   1.00 31.60 ? 221 VAL A N   1 
ATOM   1738 C CA  . VAL A 1 221 ? 11.158 14.481  3.307   1.00 29.76 ? 221 VAL A CA  1 
ATOM   1739 C C   . VAL A 1 221 ? 11.318 14.334  4.808   1.00 31.83 ? 221 VAL A C   1 
ATOM   1740 O O   . VAL A 1 221 ? 10.317 14.348  5.530   1.00 29.08 ? 221 VAL A O   1 
ATOM   1741 C CB  . VAL A 1 221 ? 10.388 15.759  2.957   1.00 34.68 ? 221 VAL A CB  1 
ATOM   1742 C CG1 . VAL A 1 221 ? 11.016 16.993  3.650   1.00 31.76 ? 221 VAL A CG1 1 
ATOM   1743 C CG2 . VAL A 1 221 ? 10.340 15.936  1.438   1.00 36.62 ? 221 VAL A CG2 1 
ATOM   1744 N N   . ASP A 1 222 ? 12.545 14.118  5.266   1.00 31.85 ? 222 ASP A N   1 
ATOM   1745 C CA  . ASP A 1 222 ? 12.804 13.893  6.695   1.00 31.62 ? 222 ASP A CA  1 
ATOM   1746 C C   . ASP A 1 222 ? 11.903 12.742  7.136   1.00 34.37 ? 222 ASP A C   1 
ATOM   1747 O O   . ASP A 1 222 ? 11.807 11.715  6.447   1.00 31.90 ? 222 ASP A O   1 
ATOM   1748 C CB  . ASP A 1 222 ? 12.610 15.199  7.466   1.00 30.12 ? 222 ASP A CB  1 
ATOM   1749 C CG  . ASP A 1 222 ? 13.630 16.246  7.106   1.00 26.98 ? 222 ASP A CG  1 
ATOM   1750 O OD1 . ASP A 1 222 ? 14.706 15.860  6.652   1.00 27.81 ? 222 ASP A OD1 1 
ATOM   1751 O OD2 . ASP A 1 222 ? 13.369 17.466  7.283   1.00 28.59 ? 222 ASP A OD2 1 
ATOM   1752 N N   . HIS A 1 223 ? 11.178 12.872  8.239   1.00 35.42 ? 223 HIS A N   1 
ATOM   1753 C CA  . HIS A 1 223 ? 10.441 11.704  8.682   1.00 44.17 ? 223 HIS A CA  1 
ATOM   1754 C C   . HIS A 1 223 ? 9.193  11.374  7.842   1.00 49.62 ? 223 HIS A C   1 
ATOM   1755 O O   . HIS A 1 223 ? 8.639  10.283  8.000   1.00 55.23 ? 223 HIS A O   1 
ATOM   1756 C CB  . HIS A 1 223 ? 10.059 11.891  10.146  0.80 47.72 ? 223 HIS A CB  1 
ATOM   1757 C CG  . HIS A 1 223 ? 9.404  10.692  10.731  0.70 54.18 ? 223 HIS A CG  1 
ATOM   1758 N ND1 . HIS A 1 223 ? 8.063  10.425  10.553  0.70 57.69 ? 223 HIS A ND1 1 
ATOM   1759 C CD2 . HIS A 1 223 ? 9.906  9.664   11.451  0.70 55.25 ? 223 HIS A CD2 1 
ATOM   1760 C CE1 . HIS A 1 223 ? 7.760  9.296   11.166  0.70 58.00 ? 223 HIS A CE1 1 
ATOM   1761 N NE2 . HIS A 1 223 ? 8.860  8.813   11.716  0.70 56.49 ? 223 HIS A NE2 1 
ATOM   1762 N N   . LEU A 1 224 ? 8.753  12.245  6.939   1.00 46.29 ? 224 LEU A N   1 
ATOM   1763 C CA  . LEU A 1 224 ? 7.451  12.130  6.282   1.00 43.72 ? 224 LEU A CA  1 
ATOM   1764 C C   . LEU A 1 224 ? 7.576  11.413  4.935   1.00 42.96 ? 224 LEU A C   1 
ATOM   1765 O O   . LEU A 1 224 ? 8.444  11.758  4.137   1.00 42.46 ? 224 LEU A O   1 
ATOM   1766 C CB  . LEU A 1 224 ? 6.874  13.527  6.073   0.90 46.44 ? 224 LEU A CB  1 
ATOM   1767 C CG  . LEU A 1 224 ? 5.695  13.645  5.110   0.80 50.40 ? 224 LEU A CG  1 
ATOM   1768 C CD1 . LEU A 1 224 ? 4.455  13.175  5.813   0.80 52.73 ? 224 LEU A CD1 1 
ATOM   1769 C CD2 . LEU A 1 224 ? 5.529  15.067  4.574   0.80 51.05 ? 224 LEU A CD2 1 
ATOM   1770 N N   . SER A 1 225 ? 6.697  10.443  4.663   1.00 42.48 ? 225 SER A N   1 
ATOM   1771 C CA  . SER A 1 225 ? 6.760  9.685   3.410   1.00 43.66 ? 225 SER A CA  1 
ATOM   1772 C C   . SER A 1 225 ? 5.381  9.574   2.772   1.00 46.30 ? 225 SER A C   1 
ATOM   1773 O O   . SER A 1 225 ? 4.453  9.027   3.377   1.00 49.42 ? 225 SER A O   1 
ATOM   1774 C CB  . SER A 1 225 ? 7.341  8.290   3.635   1.00 45.55 ? 225 SER A CB  1 
ATOM   1775 O OG  . SER A 1 225 ? 7.470  7.612   2.394   1.00 48.41 ? 225 SER A OG  1 
ATOM   1776 N N   . ILE A 1 226 ? 5.264  10.047  1.533   1.00 45.29 ? 226 ILE A N   1 
ATOM   1777 C CA  . ILE A 1 226 ? 3.989  10.132  0.831   1.00 46.38 ? 226 ILE A CA  1 
ATOM   1778 C C   . ILE A 1 226 ? 4.138  9.527   -0.560  1.00 45.39 ? 226 ILE A C   1 
ATOM   1779 O O   . ILE A 1 226 ? 5.166  9.711   -1.220  1.00 44.08 ? 226 ILE A O   1 
ATOM   1780 C CB  . ILE A 1 226 ? 3.508  11.597  0.745   0.70 47.42 ? 226 ILE A CB  1 
ATOM   1781 C CG1 . ILE A 1 226 ? 3.406  12.198  2.153   0.60 48.52 ? 226 ILE A CG1 1 
ATOM   1782 C CG2 . ILE A 1 226 ? 2.163  11.680  0.051   0.60 49.08 ? 226 ILE A CG2 1 
ATOM   1783 C CD1 . ILE A 1 226 ? 3.098  13.682  2.179   0.60 49.08 ? 226 ILE A CD1 1 
ATOM   1784 N N   . LEU A 1 227 ? 3.112  8.800   -1.008  1.00 45.21 ? 227 LEU A N   1 
ATOM   1785 C CA  . LEU A 1 227 ? 3.092  8.280   -2.367  1.00 45.41 ? 227 LEU A CA  1 
ATOM   1786 C C   . LEU A 1 227 ? 2.563  9.362   -3.290  1.00 47.82 ? 227 LEU A C   1 
ATOM   1787 O O   . LEU A 1 227 ? 1.432  9.820   -3.121  1.00 51.77 ? 227 LEU A O   1 
ATOM   1788 C CB  . LEU A 1 227 ? 2.224  7.032   -2.476  1.00 48.37 ? 227 LEU A CB  1 
ATOM   1789 C CG  . LEU A 1 227 ? 1.901  6.665   -3.934  1.00 50.23 ? 227 LEU A CG  1 
ATOM   1790 C CD1 . LEU A 1 227 ? 3.162  6.254   -4.682  1.00 47.99 ? 227 LEU A CD1 1 
ATOM   1791 C CD2 . LEU A 1 227 ? 0.857  5.574   -4.009  1.00 52.64 ? 227 LEU A CD2 1 
ATOM   1792 N N   . HIS A 1 228 ? 3.383  9.782   -4.242  1.00 47.73 ? 228 HIS A N   1 
ATOM   1793 C CA  . HIS A 1 228 ? 3.051  10.843  -5.178  1.00 49.98 ? 228 HIS A CA  1 
ATOM   1794 C C   . HIS A 1 228 ? 2.725  10.217  -6.527  1.00 49.17 ? 228 HIS A C   1 
ATOM   1795 O O   . HIS A 1 228 ? 3.414  9.294   -6.976  1.00 46.83 ? 228 HIS A O   1 
ATOM   1796 C CB  . HIS A 1 228 ? 4.212  11.840  -5.309  1.00 51.94 ? 228 HIS A CB  1 
ATOM   1797 C CG  . HIS A 1 228 ? 4.405  12.719  -4.109  1.00 55.22 ? 228 HIS A CG  1 
ATOM   1798 N ND1 . HIS A 1 228 ? 4.128  14.071  -4.122  1.00 56.39 ? 228 HIS A ND1 1 
ATOM   1799 C CD2 . HIS A 1 228 ? 4.849  12.439  -2.858  1.00 55.18 ? 228 HIS A CD2 1 
ATOM   1800 C CE1 . HIS A 1 228 ? 4.390  14.584  -2.932  1.00 56.27 ? 228 HIS A CE1 1 
ATOM   1801 N NE2 . HIS A 1 228 ? 4.823  13.615  -2.146  1.00 55.17 ? 228 HIS A NE2 1 
ATOM   1802 N N   . ARG A 1 229 ? 1.676  10.722  -7.171  1.00 50.86 ? 229 ARG A N   1 
ATOM   1803 C CA  . ARG A 1 229 ? 1.107  10.116  -8.363  1.00 52.52 ? 229 ARG A CA  1 
ATOM   1804 C C   . ARG A 1 229 ? 1.220  11.068  -9.546  1.00 52.13 ? 229 ARG A C   1 
ATOM   1805 O O   . ARG A 1 229 ? 1.105  12.284  -9.386  1.00 52.59 ? 229 ARG A O   1 
ATOM   1806 C CB  . ARG A 1 229 ? -0.369 9.773   -8.122  1.00 60.74 ? 229 ARG A CB  1 
ATOM   1807 C CG  . ARG A 1 229 ? -0.808 8.441   -8.682  1.00 66.96 ? 229 ARG A CG  1 
ATOM   1808 C CD  . ARG A 1 229 ? -0.671 7.336   -7.631  1.00 69.04 ? 229 ARG A CD  1 
ATOM   1809 N NE  . ARG A 1 229 ? -1.802 7.321   -6.709  0.78 72.34 ? 229 ARG A NE  1 
ATOM   1810 C CZ  . ARG A 1 229 ? -2.255 6.232   -6.095  0.88 75.30 ? 229 ARG A CZ  1 
ATOM   1811 N NH1 . ARG A 1 229 ? -1.688 5.051   -6.315  1.00 76.34 ? 229 ARG A NH1 1 
ATOM   1812 N NH2 . ARG A 1 229 ? -3.281 6.323   -5.262  0.89 77.20 ? 229 ARG A NH2 1 
ATOM   1813 N N   . ASP A 1 230 ? 1.403  10.504  -10.745 1.00 52.40 ? 230 ASP A N   1 
ATOM   1814 C CA  . ASP A 1 230 ? 1.511  11.282  -11.982 1.00 53.91 ? 230 ASP A CA  1 
ATOM   1815 C C   . ASP A 1 230 ? 2.603  12.342  -11.866 1.00 51.70 ? 230 ASP A C   1 
ATOM   1816 O O   . ASP A 1 230 ? 2.419  13.508  -12.219 1.00 51.34 ? 230 ASP A O   1 
ATOM   1817 C CB  . ASP A 1 230 ? 0.171  11.919  -12.355 1.00 59.22 ? 230 ASP A CB  1 
ATOM   1818 C CG  . ASP A 1 230 ? 0.189  12.548  -13.739 1.00 63.39 ? 230 ASP A CG  1 
ATOM   1819 O OD1 . ASP A 1 230 ? 0.931  12.056  -14.619 1.00 64.81 ? 230 ASP A OD1 1 
ATOM   1820 O OD2 . ASP A 1 230 ? -0.521 13.554  -13.932 1.00 66.69 ? 230 ASP A OD2 1 
ATOM   1821 N N   . VAL A 1 231 ? 3.748  11.925  -11.339 1.00 48.66 ? 231 VAL A N   1 
ATOM   1822 C CA  . VAL A 1 231 ? 4.891  12.814  -11.164 1.00 45.39 ? 231 VAL A CA  1 
ATOM   1823 C C   . VAL A 1 231 ? 5.594  12.991  -12.500 1.00 45.87 ? 231 VAL A C   1 
ATOM   1824 O O   . VAL A 1 231 ? 5.831  12.021  -13.227 1.00 50.98 ? 231 VAL A O   1 
ATOM   1825 C CB  . VAL A 1 231 ? 5.849  12.256  -10.105 1.00 45.50 ? 231 VAL A CB  1 
ATOM   1826 C CG1 . VAL A 1 231 ? 7.139  13.061  -10.102 1.00 43.28 ? 231 VAL A CG1 1 
ATOM   1827 C CG2 . VAL A 1 231 ? 5.178  12.281  -8.742  1.00 45.96 ? 231 VAL A CG2 1 
ATOM   1828 N N   . GLN A 1 232 ? 5.902  14.239  -12.842 1.00 44.30 ? 232 GLN A N   1 
ATOM   1829 C CA  . GLN A 1 232 ? 6.639  14.570  -14.051 1.00 44.12 ? 232 GLN A CA  1 
ATOM   1830 C C   . GLN A 1 232 ? 8.094  14.891  -13.767 1.00 43.32 ? 232 GLN A C   1 
ATOM   1831 O O   . GLN A 1 232 ? 8.952  14.679  -14.635 1.00 41.63 ? 232 GLN A O   1 
ATOM   1832 C CB  . GLN A 1 232 ? 5.988  15.770  -14.750 1.00 44.54 ? 232 GLN A CB  1 
ATOM   1833 N N   . GLU A 1 233 ? 8.397  15.351  -12.559 1.00 41.58 ? 233 GLU A N   1 
ATOM   1834 C CA  . GLU A 1 233 ? 9.752  15.797  -12.274 1.00 39.97 ? 233 GLU A CA  1 
ATOM   1835 C C   . GLU A 1 233 ? 9.894  15.991  -10.785 1.00 39.66 ? 233 GLU A C   1 
ATOM   1836 O O   . GLU A 1 233 ? 8.956  16.444  -10.134 1.00 41.69 ? 233 GLU A O   1 
ATOM   1837 C CB  . GLU A 1 233 ? 10.056 17.117  -12.998 1.00 42.50 ? 233 GLU A CB  1 
ATOM   1838 C CG  . GLU A 1 233 ? 11.519 17.511  -12.990 0.80 43.01 ? 233 GLU A CG  1 
ATOM   1839 C CD  . GLU A 1 233 ? 11.739 18.877  -13.600 0.70 44.84 ? 233 GLU A CD  1 
ATOM   1840 O OE1 . GLU A 1 233 ? 10.769 19.645  -13.687 0.70 45.22 ? 233 GLU A OE1 1 
ATOM   1841 O OE2 . GLU A 1 233 ? 12.878 19.179  -13.995 0.70 44.90 ? 233 GLU A OE2 1 
ATOM   1842 N N   . ILE A 1 234 ? 11.069 15.655  -10.260 1.00 36.16 ? 234 ILE A N   1 
ATOM   1843 C CA  . ILE A 1 234 ? 11.475 15.962  -8.892  1.00 34.81 ? 234 ILE A CA  1 
ATOM   1844 C C   . ILE A 1 234 ? 12.757 16.769  -8.992  1.00 34.48 ? 234 ILE A C   1 
ATOM   1845 O O   . ILE A 1 234 ? 13.728 16.301  -9.597  1.00 37.90 ? 234 ILE A O   1 
ATOM   1846 C CB  . ILE A 1 234 ? 11.703 14.690  -8.062  1.00 37.37 ? 234 ILE A CB  1 
ATOM   1847 C CG1 . ILE A 1 234 ? 10.482 13.775  -8.117  1.00 41.37 ? 234 ILE A CG1 1 
ATOM   1848 C CG2 . ILE A 1 234 ? 12.015 15.061  -6.604  1.00 34.43 ? 234 ILE A CG2 1 
ATOM   1849 C CD1 . ILE A 1 234 ? 10.732 12.405  -7.543  1.00 41.27 ? 234 ILE A CD1 1 
ATOM   1850 N N   . ARG A 1 235 ? 12.768 17.987  -8.435  1.00 31.34 ? 235 ARG A N   1 
ATOM   1851 C CA  . ARG A 1 235 ? 13.926 18.872  -8.548  1.00 30.39 ? 235 ARG A CA  1 
ATOM   1852 C C   . ARG A 1 235 ? 14.505 19.137  -7.169  1.00 29.17 ? 235 ARG A C   1 
ATOM   1853 O O   . ARG A 1 235 ? 13.771 19.536  -6.264  1.00 29.35 ? 235 ARG A O   1 
ATOM   1854 C CB  . ARG A 1 235 ? 13.570 20.223  -9.188  0.80 30.09 ? 235 ARG A CB  1 
ATOM   1855 C CG  . ARG A 1 235 ? 13.071 20.156  -10.609 0.70 33.96 ? 235 ARG A CG  1 
ATOM   1856 C CD  . ARG A 1 235 ? 12.592 21.529  -11.087 0.60 36.43 ? 235 ARG A CD  1 
ATOM   1857 N NE  . ARG A 1 235 ? 13.654 22.442  -11.506 0.50 39.61 ? 235 ARG A NE  1 
ATOM   1858 C CZ  . ARG A 1 235 ? 14.282 22.381  -12.680 0.50 40.77 ? 235 ARG A CZ  1 
ATOM   1859 N NH1 . ARG A 1 235 ? 15.229 23.264  -12.989 0.50 40.88 ? 235 ARG A NH1 1 
ATOM   1860 N NH2 . ARG A 1 235 ? 13.978 21.423  -13.541 0.50 40.93 ? 235 ARG A NH2 1 
ATOM   1861 N N   . TYR A 1 236 ? 15.810 18.971  -7.048  1.00 27.20 ? 236 TYR A N   1 
ATOM   1862 C CA  . TYR A 1 236 ? 16.557 19.242  -5.819  1.00 30.33 ? 236 TYR A CA  1 
ATOM   1863 C C   . TYR A 1 236 ? 17.488 20.423  -6.013  1.00 31.47 ? 236 TYR A C   1 
ATOM   1864 O O   . TYR A 1 236 ? 18.164 20.516  -7.039  1.00 27.88 ? 236 TYR A O   1 
ATOM   1865 C CB  . TYR A 1 236 ? 17.394 18.035  -5.418  1.00 30.05 ? 236 TYR A CB  1 
ATOM   1866 C CG  . TYR A 1 236 ? 16.572 16.858  -5.020  1.00 30.08 ? 236 TYR A CG  1 
ATOM   1867 C CD1 . TYR A 1 236 ? 15.694 16.947  -3.955  1.00 30.57 ? 236 TYR A CD1 1 
ATOM   1868 C CD2 . TYR A 1 236 ? 16.643 15.661  -5.709  1.00 32.66 ? 236 TYR A CD2 1 
ATOM   1869 C CE1 . TYR A 1 236 ? 14.920 15.880  -3.578  1.00 33.85 ? 236 TYR A CE1 1 
ATOM   1870 C CE2 . TYR A 1 236 ? 15.853 14.560  -5.307  1.00 34.96 ? 236 TYR A CE2 1 
ATOM   1871 C CZ  . TYR A 1 236 ? 15.009 14.697  -4.241  1.00 36.83 ? 236 TYR A CZ  1 
ATOM   1872 O OH  . TYR A 1 236 ? 14.207 13.670  -3.803  1.00 44.33 ? 236 TYR A OH  1 
ATOM   1873 N N   . GLU A 1 237 ? 17.536 21.312  -5.018  1.00 30.38 ? 237 GLU A N   1 
ATOM   1874 C CA  . GLU A 1 237 ? 18.530 22.377  -4.989  1.00 29.22 ? 237 GLU A CA  1 
ATOM   1875 C C   . GLU A 1 237 ? 18.708 22.832  -3.551  1.00 28.79 ? 237 GLU A C   1 
ATOM   1876 O O   . GLU A 1 237 ? 17.809 22.696  -2.712  1.00 26.03 ? 237 GLU A O   1 
ATOM   1877 C CB  . GLU A 1 237 ? 18.141 23.574  -5.869  1.00 32.62 ? 237 GLU A CB  1 
ATOM   1878 C CG  . GLU A 1 237 ? 16.846 24.142  -5.507  1.00 35.37 ? 237 GLU A CG  1 
ATOM   1879 C CD  . GLU A 1 237 ? 16.178 24.809  -6.671  0.40 39.51 ? 237 GLU A CD  1 
ATOM   1880 O OE1 . GLU A 1 237 ? 16.772 25.781  -7.170  1.00 41.59 ? 237 GLU A OE1 1 
ATOM   1881 O OE2 . GLU A 1 237 ? 15.088 24.348  -7.089  0.81 40.43 ? 237 GLU A OE2 1 
ATOM   1882 N N   . VAL A 1 238 ? 19.879 23.390  -3.281  1.00 28.36 ? 238 VAL A N   1 
ATOM   1883 C CA  . VAL A 1 238 ? 20.117 23.917  -1.941  1.00 28.59 ? 238 VAL A CA  1 
ATOM   1884 C C   . VAL A 1 238 ? 19.170 25.080  -1.727  1.00 32.18 ? 238 VAL A C   1 
ATOM   1885 O O   . VAL A 1 238 ? 19.037 25.952  -2.597  1.00 30.70 ? 238 VAL A O   1 
ATOM   1886 C CB  . VAL A 1 238 ? 21.584 24.336  -1.774  1.00 26.87 ? 238 VAL A CB  1 
ATOM   1887 C CG1 . VAL A 1 238 ? 21.826 25.015  -0.353  1.00 26.55 ? 238 VAL A CG1 1 
ATOM   1888 C CG2 . VAL A 1 238 ? 22.459 23.136  -1.942  1.00 27.25 ? 238 VAL A CG2 1 
ATOM   1889 N N   . SER A 1 239 ? 18.509 25.113  -0.562  1.00 28.19 ? 239 SER A N   1 
ATOM   1890 C CA  . SER A 1 239 ? 17.503 26.137  -0.361  1.00 28.31 ? 239 SER A CA  1 
ATOM   1891 C C   . SER A 1 239 ? 18.182 27.478  -0.123  1.00 29.92 ? 239 SER A C   1 
ATOM   1892 O O   . SER A 1 239 ? 19.345 27.542  0.280   1.00 31.53 ? 239 SER A O   1 
ATOM   1893 C CB  . SER A 1 239 ? 16.589 25.760  0.819   1.00 29.42 ? 239 SER A CB  1 
ATOM   1894 O OG  . SER A 1 239 ? 15.655 26.786  1.139   1.00 35.10 ? 239 SER A OG  1 
ATOM   1895 N N   . ALA A 1 240 ? 17.453 28.562  -0.409  1.00 32.39 ? 240 ALA A N   1 
ATOM   1896 C CA  . ALA A 1 240 ? 17.873 29.870  0.081   1.00 36.42 ? 240 ALA A CA  1 
ATOM   1897 C C   . ALA A 1 240 ? 17.592 30.044  1.573   1.00 37.96 ? 240 ALA A C   1 
ATOM   1898 O O   . ALA A 1 240 ? 18.162 30.944  2.199   1.00 40.98 ? 240 ALA A O   1 
ATOM   1899 C CB  . ALA A 1 240 ? 17.151 30.985  -0.666  1.00 37.19 ? 240 ALA A CB  1 
ATOM   1900 N N   . LYS A 1 241 ? 16.696 29.237  2.129   1.00 34.09 ? 241 LYS A N   1 
ATOM   1901 C CA  . LYS A 1 241 ? 16.341 29.354  3.538   1.00 34.13 ? 241 LYS A CA  1 
ATOM   1902 C C   . LYS A 1 241 ? 17.342 28.580  4.383   1.00 34.33 ? 241 LYS A C   1 
ATOM   1903 O O   . LYS A 1 241 ? 17.999 27.656  3.902   1.00 32.12 ? 241 LYS A O   1 
ATOM   1904 C CB  . LYS A 1 241 ? 14.911 28.842  3.764   0.80 34.58 ? 241 LYS A CB  1 
ATOM   1905 C CG  . LYS A 1 241 ? 13.841 29.511  2.863   0.70 36.58 ? 241 LYS A CG  1 
ATOM   1906 C CD  . LYS A 1 241 ? 12.503 28.776  2.948   0.60 37.19 ? 241 LYS A CD  1 
ATOM   1907 C CE  . LYS A 1 241 ? 11.427 29.383  2.060   0.50 39.43 ? 241 LYS A CE  1 
ATOM   1908 N NZ  . LYS A 1 241 ? 10.119 28.662  2.206   0.50 40.63 ? 241 LYS A NZ  1 
ATOM   1909 N N   . LYS A 1 242 ? 17.479 28.995  5.650   1.00 34.26 ? 242 LYS A N   1 
ATOM   1910 C CA  . LYS A 1 242 ? 18.409 28.360  6.565   1.00 34.83 ? 242 LYS A CA  1 
ATOM   1911 C C   . LYS A 1 242 ? 17.704 28.167  7.898   1.00 34.16 ? 242 LYS A C   1 
ATOM   1912 O O   . LYS A 1 242 ? 16.831 28.954  8.271   1.00 33.84 ? 242 LYS A O   1 
ATOM   1913 C CB  . LYS A 1 242 ? 19.692 29.187  6.744   0.70 34.81 ? 242 LYS A CB  1 
ATOM   1914 C CG  . LYS A 1 242 ? 20.522 29.308  5.442   0.60 36.55 ? 242 LYS A CG  1 
ATOM   1915 C CD  . LYS A 1 242 ? 21.802 30.086  5.666   0.50 38.86 ? 242 LYS A CD  1 
ATOM   1916 C CE  . LYS A 1 242 ? 22.926 29.149  6.086   0.50 40.63 ? 242 LYS A CE  1 
ATOM   1917 N NZ  . LYS A 1 242 ? 23.653 28.597  4.914   0.50 41.22 ? 242 LYS A NZ  1 
ATOM   1918 N N   . ILE A 1 243 ? 18.070 27.097  8.599   1.00 32.74 ? 243 ILE A N   1 
ATOM   1919 C CA  . ILE A 1 243 ? 17.626 26.917  9.974   1.00 32.18 ? 243 ILE A CA  1 
ATOM   1920 C C   . ILE A 1 243 ? 18.671 27.531  10.887  1.00 32.53 ? 243 ILE A C   1 
ATOM   1921 O O   . ILE A 1 243 ? 19.880 27.414  10.646  1.00 33.44 ? 243 ILE A O   1 
ATOM   1922 C CB  . ILE A 1 243 ? 17.379 25.436  10.306  1.00 29.49 ? 243 ILE A CB  1 
ATOM   1923 C CG1 . ILE A 1 243 ? 16.847 25.299  11.751  1.00 31.38 ? 243 ILE A CG1 1 
ATOM   1924 C CG2 . ILE A 1 243 ? 18.644 24.644  10.198  1.00 29.35 ? 243 ILE A CG2 1 
ATOM   1925 C CD1 . ILE A 1 243 ? 16.751 23.852  12.194  1.00 31.08 ? 243 ILE A CD1 1 
ATOM   1926 N N   . HIS A 1 244 ? 18.195 28.217  11.916  1.00 34.39 ? 244 HIS A N   1 
ATOM   1927 C CA  . HIS A 1 244 ? 19.031 28.937  12.871  1.00 34.93 ? 244 HIS A CA  1 
ATOM   1928 C C   . HIS A 1 244 ? 18.961 28.231  14.209  1.00 34.36 ? 244 HIS A C   1 
ATOM   1929 O O   . HIS A 1 244 ? 17.860 27.962  14.704  1.00 34.37 ? 244 HIS A O   1 
ATOM   1930 C CB  . HIS A 1 244 ? 18.566 30.386  13.009  1.00 39.01 ? 244 HIS A CB  1 
ATOM   1931 C CG  . HIS A 1 244 ? 18.502 31.106  11.698  1.00 42.98 ? 244 HIS A CG  1 
ATOM   1932 N ND1 . HIS A 1 244 ? 19.633 31.438  10.979  1.00 43.24 ? 244 HIS A ND1 1 
ATOM   1933 C CD2 . HIS A 1 244 ? 17.447 31.506  10.947  1.00 44.92 ? 244 HIS A CD2 1 
ATOM   1934 C CE1 . HIS A 1 244 ? 19.278 32.033  9.853   1.00 44.15 ? 244 HIS A CE1 1 
ATOM   1935 N NE2 . HIS A 1 244 ? 17.959 32.083  9.805   1.00 44.46 ? 244 HIS A NE2 1 
ATOM   1936 N N   . PHE A 1 245 ? 20.127 27.937  14.787  1.00 34.05 ? 245 PHE A N   1 
ATOM   1937 C CA  . PHE A 1 245 ? 20.228 27.391  16.142  1.00 37.79 ? 245 PHE A CA  1 
ATOM   1938 C C   . PHE A 1 245 ? 20.691 28.450  17.135  1.00 39.17 ? 245 PHE A C   1 
ATOM   1939 O O   . PHE A 1 245 ? 21.551 29.280  16.829  1.00 40.23 ? 245 PHE A O   1 
ATOM   1940 C CB  . PHE A 1 245 ? 21.213 26.226  16.182  1.00 38.31 ? 245 PHE A CB  1 
ATOM   1941 C CG  . PHE A 1 245 ? 20.804 25.056  15.360  1.00 37.13 ? 245 PHE A CG  1 
ATOM   1942 C CD1 . PHE A 1 245 ? 21.086 25.011  13.988  1.00 36.53 ? 245 PHE A CD1 1 
ATOM   1943 C CD2 . PHE A 1 245 ? 20.159 23.981  15.948  1.00 38.10 ? 245 PHE A CD2 1 
ATOM   1944 C CE1 . PHE A 1 245 ? 20.733 23.930  13.231  1.00 36.17 ? 245 PHE A CE1 1 
ATOM   1945 C CE2 . PHE A 1 245 ? 19.797 22.880  15.180  1.00 37.65 ? 245 PHE A CE2 1 
ATOM   1946 C CZ  . PHE A 1 245 ? 20.080 22.859  13.808  1.00 34.82 ? 245 PHE A CZ  1 
ATOM   1947 N N   . ALA A 1 246 ? 20.142 28.414  18.337  1.00 41.09 ? 246 ALA A N   1 
ATOM   1948 C CA  . ALA A 1 246 ? 20.790 29.123  19.424  1.00 42.72 ? 246 ALA A CA  1 
ATOM   1949 C C   . ALA A 1 246 ? 21.957 28.261  19.887  1.00 47.59 ? 246 ALA A C   1 
ATOM   1950 O O   . ALA A 1 246 ? 21.810 27.046  20.026  1.00 50.24 ? 246 ALA A O   1 
ATOM   1951 C CB  . ALA A 1 246 ? 19.790 29.366  20.543  1.00 45.45 ? 246 ALA A CB  1 
ATOM   1952 N N   . ARG A 1 247 ? 23.137 28.851  20.062  1.00 51.16 ? 247 ARG A N   1 
ATOM   1953 C CA  . ARG A 1 247 ? 24.232 28.113  20.683  1.00 54.85 ? 247 ARG A CA  1 
ATOM   1954 C C   . ARG A 1 247 ? 24.684 28.871  21.924  1.00 60.32 ? 247 ARG A C   1 
ATOM   1955 O O   . ARG A 1 247 ? 24.799 30.100  21.909  1.00 60.74 ? 247 ARG A O   1 
ATOM   1956 C CB  . ARG A 1 247 ? 25.413 27.872  19.723  0.70 53.87 ? 247 ARG A CB  1 
ATOM   1957 C CG  . ARG A 1 247 ? 25.116 27.010  18.454  0.60 51.75 ? 247 ARG A CG  1 
ATOM   1958 C CD  . ARG A 1 247 ? 24.835 25.487  18.663  0.50 50.29 ? 247 ARG A CD  1 
ATOM   1959 N NE  . ARG A 1 247 ? 24.611 24.819  17.369  0.50 50.53 ? 247 ARG A NE  1 
ATOM   1960 C CZ  . ARG A 1 247 ? 24.141 23.583  17.193  0.50 47.60 ? 247 ARG A CZ  1 
ATOM   1961 N NH1 . ARG A 1 247 ? 23.832 22.815  18.223  0.50 47.38 ? 247 ARG A NH1 1 
ATOM   1962 N NH2 . ARG A 1 247 ? 23.991 23.110  15.971  0.50 47.24 ? 247 ARG A NH2 1 
ATOM   1963 N N   . PHE A 1 248 ? 24.899 28.146  23.013  1.00 67.85 ? 248 PHE A N   1 
ATOM   1964 C CA  . PHE A 1 248 ? 25.368 28.787  24.230  1.00 72.04 ? 248 PHE A CA  1 
ATOM   1965 C C   . PHE A 1 248 ? 26.761 28.330  24.633  1.00 71.38 ? 248 PHE A C   1 
ATOM   1966 O O   . PHE A 1 248 ? 27.326 28.886  25.581  1.00 72.92 ? 248 PHE A O   1 
ATOM   1967 C CB  . PHE A 1 248 ? 24.357 28.591  25.373  1.00 78.89 ? 248 PHE A CB  1 
ATOM   1968 C CG  . PHE A 1 248 ? 24.235 27.177  25.885  1.00 84.59 ? 248 PHE A CG  1 
ATOM   1969 C CD1 . PHE A 1 248 ? 23.723 26.160  25.087  1.00 84.44 ? 248 PHE A CD1 1 
ATOM   1970 C CD2 . PHE A 1 248 ? 24.564 26.883  27.206  1.00 87.64 ? 248 PHE A CD2 1 
ATOM   1971 C CE1 . PHE A 1 248 ? 23.591 24.869  25.589  1.00 85.14 ? 248 PHE A CE1 1 
ATOM   1972 C CE2 . PHE A 1 248 ? 24.431 25.597  27.709  1.00 87.73 ? 248 PHE A CE2 1 
ATOM   1973 C CZ  . PHE A 1 248 ? 23.946 24.591  26.900  1.00 86.37 ? 248 PHE A CZ  1 
ATOM   1974 N N   . ARG A 1 249 ? 27.351 27.381  23.907  1.00 61.04 ? 249 ARG A N   1 
ATOM   1975 C CA  . ARG A 1 249 ? 28.734 26.979  24.118  1.00 57.77 ? 249 ARG A CA  1 
ATOM   1976 C C   . ARG A 1 249 ? 29.239 26.342  22.830  1.00 52.85 ? 249 ARG A C   1 
ATOM   1977 O O   . ARG A 1 249 ? 28.485 26.148  21.872  1.00 48.64 ? 249 ARG A O   1 
ATOM   1978 C CB  . ARG A 1 249 ? 28.864 26.025  25.317  1.00 59.58 ? 249 ARG A CB  1 
ATOM   1979 N N   . SER A 1 250 ? 30.532 26.033  22.812  1.00 51.73 ? 250 SER A N   1 
ATOM   1980 C CA  . SER A 1 250 ? 31.114 25.302  21.697  1.00 49.07 ? 250 SER A CA  1 
ATOM   1981 C C   . SER A 1 250 ? 30.793 23.826  21.858  1.00 44.13 ? 250 SER A C   1 
ATOM   1982 O O   . SER A 1 250 ? 31.130 23.209  22.879  1.00 44.01 ? 250 SER A O   1 
ATOM   1983 C CB  . SER A 1 250 ? 32.625 25.512  21.639  1.00 51.93 ? 250 SER A CB  1 
ATOM   1984 O OG  . SER A 1 250 ? 33.167 24.844  20.506  0.92 50.48 ? 250 SER A OG  1 
ATOM   1985 N N   . PHE A 1 251 ? 30.118 23.268  20.866  1.00 43.92 ? 251 PHE A N   1 
ATOM   1986 C CA  . PHE A 1 251 ? 29.990 21.825  20.715  1.00 40.77 ? 251 PHE A CA  1 
ATOM   1987 C C   . PHE A 1 251 ? 30.231 21.567  19.237  1.00 37.43 ? 251 PHE A C   1 
ATOM   1988 O O   . PHE A 1 251 ? 29.286 21.504  18.440  1.00 38.87 ? 251 PHE A O   1 
ATOM   1989 C CB  . PHE A 1 251 ? 28.615 21.330  21.151  1.00 42.90 ? 251 PHE A CB  1 
ATOM   1990 C CG  . PHE A 1 251 ? 28.528 19.845  21.317  1.00 44.80 ? 251 PHE A CG  1 
ATOM   1991 C CD1 . PHE A 1 251 ? 29.622 19.038  21.053  1.00 43.95 ? 251 PHE A CD1 1 
ATOM   1992 C CD2 . PHE A 1 251 ? 27.357 19.254  21.762  1.00 45.54 ? 251 PHE A CD2 1 
ATOM   1993 C CE1 . PHE A 1 251 ? 29.566 17.666  21.220  1.00 42.85 ? 251 PHE A CE1 1 
ATOM   1994 C CE2 . PHE A 1 251 ? 27.278 17.876  21.918  1.00 45.76 ? 251 PHE A CE2 1 
ATOM   1995 C CZ  . PHE A 1 251 ? 28.395 17.079  21.642  1.00 44.95 ? 251 PHE A CZ  1 
ATOM   1996 N N   . PRO A 1 252 ? 31.496 21.439  18.830  1.00 33.12 ? 252 PRO A N   1 
ATOM   1997 C CA  . PRO A 1 252 ? 31.813 21.358  17.398  1.00 32.33 ? 252 PRO A CA  1 
ATOM   1998 C C   . PRO A 1 252 ? 31.190 20.148  16.719  1.00 31.07 ? 252 PRO A C   1 
ATOM   1999 O O   . PRO A 1 252 ? 31.130 19.057  17.277  1.00 30.15 ? 252 PRO A O   1 
ATOM   2000 C CB  . PRO A 1 252 ? 33.346 21.280  17.380  1.00 32.04 ? 252 PRO A CB  1 
ATOM   2001 C CG  . PRO A 1 252 ? 33.789 21.932  18.649  1.00 33.19 ? 252 PRO A CG  1 
ATOM   2002 C CD  . PRO A 1 252 ? 32.698 21.629  19.678  1.00 33.33 ? 252 PRO A CD  1 
ATOM   2003 N N   . PHE A 1 253 ? 30.760 20.348  15.467  1.00 28.71 ? 253 PHE A N   1 
ATOM   2004 C CA  . PHE A 1 253 ? 30.223 19.260  14.659  1.00 26.82 ? 253 PHE A CA  1 
ATOM   2005 C C   . PHE A 1 253 ? 31.113 18.026  14.706  1.00 26.96 ? 253 PHE A C   1 
ATOM   2006 O O   . PHE A 1 253 ? 30.627 16.910  14.878  1.00 26.20 ? 253 PHE A O   1 
ATOM   2007 C CB  . PHE A 1 253 ? 30.065 19.740  13.212  1.00 28.02 ? 253 PHE A CB  1 
ATOM   2008 C CG  . PHE A 1 253 ? 29.537 18.722  12.283  1.00 25.80 ? 253 PHE A CG  1 
ATOM   2009 C CD1 . PHE A 1 253 ? 28.192 18.414  12.259  1.00 29.41 ? 253 PHE A CD1 1 
ATOM   2010 C CD2 . PHE A 1 253 ? 30.388 18.085  11.399  1.00 26.75 ? 253 PHE A CD2 1 
ATOM   2011 C CE1 . PHE A 1 253 ? 27.684 17.481  11.345  1.00 30.74 ? 253 PHE A CE1 1 
ATOM   2012 C CE2 . PHE A 1 253 ? 29.907 17.166  10.457  1.00 29.02 ? 253 PHE A CE2 1 
ATOM   2013 C CZ  . PHE A 1 253 ? 28.542 16.860  10.441  1.00 31.59 ? 253 PHE A CZ  1 
ATOM   2014 N N   . TRP A 1 254 ? 32.426 18.201  14.530  1.00 28.04 ? 254 TRP A N   1 
ATOM   2015 C CA  . TRP A 1 254 ? 33.262 17.007  14.440  1.00 30.20 ? 254 TRP A CA  1 
ATOM   2016 C C   . TRP A 1 254 ? 33.359 16.327  15.789  1.00 27.30 ? 254 TRP A C   1 
ATOM   2017 O O   . TRP A 1 254 ? 33.557 15.111  15.861  1.00 26.32 ? 254 TRP A O   1 
ATOM   2018 C CB  . TRP A 1 254 ? 34.669 17.333  13.920  1.00 31.55 ? 254 TRP A CB  1 
ATOM   2019 C CG  . TRP A 1 254 ? 34.699 17.834  12.474  1.00 27.41 ? 254 TRP A CG  1 
ATOM   2020 C CD1 . TRP A 1 254 ? 35.192 19.034  12.043  1.00 28.13 ? 254 TRP A CD1 1 
ATOM   2021 C CD2 . TRP A 1 254 ? 34.216 17.150  11.304  1.00 29.53 ? 254 TRP A CD2 1 
ATOM   2022 N NE1 . TRP A 1 254 ? 35.035 19.148  10.659  1.00 25.47 ? 254 TRP A NE1 1 
ATOM   2023 C CE2 . TRP A 1 254 ? 34.442 18.001  10.191  1.00 26.94 ? 254 TRP A CE2 1 
ATOM   2024 C CE3 . TRP A 1 254 ? 33.612 15.909  11.085  1.00 30.18 ? 254 TRP A CE3 1 
ATOM   2025 C CZ2 . TRP A 1 254 ? 34.089 17.643  8.896   1.00 29.82 ? 254 TRP A CZ2 1 
ATOM   2026 C CZ3 . TRP A 1 254 ? 33.256 15.560  9.791   1.00 29.24 ? 254 TRP A CZ3 1 
ATOM   2027 C CH2 . TRP A 1 254 ? 33.500 16.425  8.713   1.00 29.72 ? 254 TRP A CH2 1 
ATOM   2028 N N   . ARG A 1 255 ? 33.197 17.092  16.869  1.00 26.97 ? 255 ARG A N   1 
ATOM   2029 C CA  . ARG A 1 255 ? 33.115 16.439  18.167  1.00 27.09 ? 255 ARG A CA  1 
ATOM   2030 C C   . ARG A 1 255 ? 31.794 15.700  18.348  1.00 29.29 ? 255 ARG A C   1 
ATOM   2031 O O   . ARG A 1 255 ? 31.772 14.603  18.930  1.00 29.34 ? 255 ARG A O   1 
ATOM   2032 C CB  . ARG A 1 255 ? 33.315 17.447  19.292  0.90 27.62 ? 255 ARG A CB  1 
ATOM   2033 C CG  . ARG A 1 255 ? 33.244 16.742  20.608  0.80 30.48 ? 255 ARG A CG  1 
ATOM   2034 C CD  . ARG A 1 255 ? 33.470 17.663  21.724  0.70 35.06 ? 255 ARG A CD  1 
ATOM   2035 N NE  . ARG A 1 255 ? 34.783 18.281  21.720  0.60 36.58 ? 255 ARG A NE  1 
ATOM   2036 C CZ  . ARG A 1 255 ? 35.927 17.641  21.945  0.50 38.99 ? 255 ARG A CZ  1 
ATOM   2037 N NH1 . ARG A 1 255 ? 35.949 16.330  22.142  0.50 40.19 ? 255 ARG A NH1 1 
ATOM   2038 N NH2 . ARG A 1 255 ? 37.061 18.322  21.983  0.50 38.33 ? 255 ARG A NH2 1 
ATOM   2039 N N   . ARG A 1 256 ? 30.686 16.263  17.831  1.00 28.72 ? 256 ARG A N   1 
ATOM   2040 C CA  . ARG A 1 256 ? 29.415 15.537  17.830  1.00 31.63 ? 256 ARG A CA  1 
ATOM   2041 C C   . ARG A 1 256 ? 29.522 14.253  17.019  1.00 30.07 ? 256 ARG A C   1 
ATOM   2042 O O   . ARG A 1 256 ? 29.006 13.207  17.427  1.00 29.14 ? 256 ARG A O   1 
ATOM   2043 C CB  . ARG A 1 256 ? 28.270 16.400  17.278  0.90 33.69 ? 256 ARG A CB  1 
ATOM   2044 C CG  . ARG A 1 256 ? 27.863 17.549  18.151  0.80 38.05 ? 256 ARG A CG  1 
ATOM   2045 C CD  . ARG A 1 256 ? 26.382 17.929  17.947  0.80 36.47 ? 256 ARG A CD  1 
ATOM   2046 N NE  . ARG A 1 256 ? 26.114 18.418  16.601  0.70 30.12 ? 256 ARG A NE  1 
ATOM   2047 C CZ  . ARG A 1 256 ? 26.552 19.580  16.138  0.70 34.23 ? 256 ARG A CZ  1 
ATOM   2048 N NH1 . ARG A 1 256 ? 27.333 20.345  16.878  0.70 38.57 ? 256 ARG A NH1 1 
ATOM   2049 N NH2 . ARG A 1 256 ? 26.236 19.960  14.916  0.70 35.32 ? 256 ARG A NH2 1 
ATOM   2050 N N   . VAL A 1 257 ? 30.175 14.315  15.848  1.00 26.94 ? 257 VAL A N   1 
ATOM   2051 C CA  . VAL A 1 257 ? 30.407 13.097  15.089  1.00 24.97 ? 257 VAL A CA  1 
ATOM   2052 C C   . VAL A 1 257 ? 31.190 12.095  15.911  1.00 26.16 ? 257 VAL A C   1 
ATOM   2053 O O   . VAL A 1 257 ? 30.830 10.910  15.986  1.00 27.82 ? 257 VAL A O   1 
ATOM   2054 C CB  . VAL A 1 257 ? 31.129 13.438  13.772  1.00 25.35 ? 257 VAL A CB  1 
ATOM   2055 C CG1 . VAL A 1 257 ? 31.624 12.178  13.053  1.00 25.28 ? 257 VAL A CG1 1 
ATOM   2056 C CG2 . VAL A 1 257 ? 30.214 14.264  12.891  1.00 24.34 ? 257 VAL A CG2 1 
ATOM   2057 N N   . HIS A 1 258 ? 32.286 12.552  16.534  1.00 27.29 ? 258 HIS A N   1 
ATOM   2058 C CA  . HIS A 1 258 ? 33.096 11.655  17.349  1.00 27.97 ? 258 HIS A CA  1 
ATOM   2059 C C   . HIS A 1 258 ? 32.261 11.060  18.470  1.00 30.51 ? 258 HIS A C   1 
ATOM   2060 O O   . HIS A 1 258 ? 32.317 9.856   18.750  1.00 32.25 ? 258 HIS A O   1 
ATOM   2061 C CB  . HIS A 1 258 ? 34.268 12.423  17.953  1.00 27.23 ? 258 HIS A CB  1 
ATOM   2062 C CG  . HIS A 1 258 ? 35.055 11.647  18.968  1.00 26.40 ? 258 HIS A CG  1 
ATOM   2063 N ND1 . HIS A 1 258 ? 34.768 11.678  20.328  1.00 29.49 ? 258 HIS A ND1 1 
ATOM   2064 C CD2 . HIS A 1 258 ? 36.140 10.847  18.834  1.00 25.40 ? 258 HIS A CD2 1 
ATOM   2065 C CE1 . HIS A 1 258 ? 35.626 10.909  20.977  1.00 27.49 ? 258 HIS A CE1 1 
ATOM   2066 N NE2 . HIS A 1 258 ? 36.469 10.396  20.096  1.00 31.49 ? 258 HIS A NE2 1 
ATOM   2067 N N   . ASP A 1 259 ? 31.510 11.905  19.146  1.00 30.16 ? 259 ASP A N   1 
ATOM   2068 C CA  . ASP A 1 259 ? 30.772 11.425  20.304  1.00 31.47 ? 259 ASP A CA  1 
ATOM   2069 C C   . ASP A 1 259 ? 29.708 10.412  19.905  1.00 34.63 ? 259 ASP A C   1 
ATOM   2070 O O   . ASP A 1 259 ? 29.402 9.500   20.680  1.00 36.42 ? 259 ASP A O   1 
ATOM   2071 C CB  . ASP A 1 259 ? 30.176 12.619  21.022  1.00 31.96 ? 259 ASP A CB  1 
ATOM   2072 C CG  . ASP A 1 259 ? 31.199 13.342  21.878  1.00 38.07 ? 259 ASP A CG  1 
ATOM   2073 O OD1 . ASP A 1 259 ? 32.366 12.871  21.987  1.00 36.72 ? 259 ASP A OD1 1 
ATOM   2074 O OD2 . ASP A 1 259 ? 30.829 14.373  22.470  1.00 40.09 ? 259 ASP A OD2 1 
ATOM   2075 N N   . SER A 1 260 ? 29.154 10.536  18.698  1.00 32.12 ? 260 SER A N   1 
ATOM   2076 C CA  . SER A 1 260 ? 28.059 9.664   18.284  1.00 34.27 ? 260 SER A CA  1 
ATOM   2077 C C   . SER A 1 260 ? 28.515 8.362   17.654  1.00 33.30 ? 260 SER A C   1 
ATOM   2078 O O   . SER A 1 260 ? 27.811 7.349   17.775  1.00 35.08 ? 260 SER A O   1 
ATOM   2079 C CB  . SER A 1 260 ? 27.150 10.357  17.264  1.00 34.87 ? 260 SER A CB  1 
ATOM   2080 O OG  . SER A 1 260 ? 26.692 11.627  17.696  1.00 36.91 ? 260 SER A OG  1 
ATOM   2081 N N   . PHE A 1 261 ? 29.649 8.362   16.936  1.00 27.76 ? 261 PHE A N   1 
ATOM   2082 C CA  . PHE A 1 261 ? 30.027 7.189   16.155  1.00 28.25 ? 261 PHE A CA  1 
ATOM   2083 C C   . PHE A 1 261 ? 31.311 6.523   16.622  1.00 31.93 ? 261 PHE A C   1 
ATOM   2084 O O   . PHE A 1 261 ? 31.521 5.349   16.304  1.00 32.79 ? 261 PHE A O   1 
ATOM   2085 C CB  . PHE A 1 261 ? 30.175 7.555   14.655  1.00 27.10 ? 261 PHE A CB  1 
ATOM   2086 C CG  . PHE A 1 261 ? 28.885 8.038   14.026  1.00 26.86 ? 261 PHE A CG  1 
ATOM   2087 C CD1 . PHE A 1 261 ? 27.837 7.141   13.761  1.00 26.52 ? 261 PHE A CD1 1 
ATOM   2088 C CD2 . PHE A 1 261 ? 28.710 9.381   13.728  1.00 25.71 ? 261 PHE A CD2 1 
ATOM   2089 C CE1 . PHE A 1 261 ? 26.637 7.571   13.207  1.00 26.01 ? 261 PHE A CE1 1 
ATOM   2090 C CE2 . PHE A 1 261 ? 27.518 9.837   13.187  1.00 25.65 ? 261 PHE A CE2 1 
ATOM   2091 C CZ  . PHE A 1 261 ? 26.474 8.918   12.903  1.00 26.31 ? 261 PHE A CZ  1 
ATOM   2092 N N   . ILE A 1 262 ? 32.173 7.228   17.361  1.00 29.25 ? 262 ILE A N   1 
ATOM   2093 C CA  . ILE A 1 262 ? 33.478 6.700   17.727  1.00 29.27 ? 262 ILE A CA  1 
ATOM   2094 C C   . ILE A 1 262 ? 33.489 6.246   19.185  1.00 34.57 ? 262 ILE A C   1 
ATOM   2095 O O   . ILE A 1 262 ? 33.779 5.098   19.483  1.00 38.37 ? 262 ILE A O   1 
ATOM   2096 C CB  . ILE A 1 262 ? 34.589 7.749   17.486  1.00 28.59 ? 262 ILE A CB  1 
ATOM   2097 C CG1 . ILE A 1 262 ? 34.628 8.132   15.980  1.00 31.25 ? 262 ILE A CG1 1 
ATOM   2098 C CG2 . ILE A 1 262 ? 35.934 7.216   17.929  1.00 29.52 ? 262 ILE A CG2 1 
ATOM   2099 C CD1 . ILE A 1 262 ? 34.848 6.954   15.052  1.00 32.88 ? 262 ILE A CD1 1 
ATOM   2100 N N   . GLU A 1 263 ? 33.151 7.124   20.092  1.00 35.96 ? 263 GLU A N   1 
ATOM   2101 C CA  . GLU A 1 263 ? 33.304 6.706   21.456  1.00 47.37 ? 263 GLU A CA  1 
ATOM   2102 C C   . GLU A 1 263 ? 32.276 7.378   22.311  1.00 53.53 ? 263 GLU A C   1 
ATOM   2103 O O   . GLU A 1 263 ? 32.451 8.539   22.636  1.00 58.47 ? 263 GLU A O   1 
ATOM   2104 C CB  . GLU A 1 263 ? 34.735 7.027   21.950  1.00 53.16 ? 263 GLU A CB  1 
ATOM   2105 C CG  . GLU A 1 263 ? 35.064 6.640   23.363  0.70 58.02 ? 263 GLU A CG  1 
ATOM   2106 C CD  . GLU A 1 263 ? 35.135 5.145   23.554  0.60 59.93 ? 263 GLU A CD  1 
ATOM   2107 O OE1 . GLU A 1 263 ? 35.209 4.395   22.562  0.60 60.30 ? 263 GLU A OE1 1 
ATOM   2108 O OE2 . GLU A 1 263 ? 35.113 4.717   24.720  0.60 62.84 ? 263 GLU A OE2 1 
HETATM 2109 C C1  . CIT B 2 .   ? 31.651 23.854  14.324  0.93 46.30 ? 301 CIT A C1  1 
HETATM 2110 O O1  . CIT B 2 .   ? 31.421 22.654  14.082  0.93 44.20 ? 301 CIT A O1  1 
HETATM 2111 O O2  . CIT B 2 .   ? 32.839 24.192  14.530  0.93 46.40 ? 301 CIT A O2  1 
HETATM 2112 C C2  . CIT B 2 .   ? 30.564 24.904  14.377  0.93 47.64 ? 301 CIT A C2  1 
HETATM 2113 C C3  . CIT B 2 .   ? 29.406 24.519  15.300  0.93 50.61 ? 301 CIT A C3  1 
HETATM 2114 O O7  . CIT B 2 .   ? 29.909 24.033  16.580  0.93 49.29 ? 301 CIT A O7  1 
HETATM 2115 C C4  . CIT B 2 .   ? 28.477 25.707  15.541  0.93 55.42 ? 301 CIT A C4  1 
HETATM 2116 C C5  . CIT B 2 .   ? 28.975 26.639  16.632  0.93 59.55 ? 301 CIT A C5  1 
HETATM 2117 O O3  . CIT B 2 .   ? 29.264 27.818  16.333  0.93 61.36 ? 301 CIT A O3  1 
HETATM 2118 O O4  . CIT B 2 .   ? 29.095 26.272  17.831  0.93 59.90 ? 301 CIT A O4  1 
HETATM 2119 C C6  . CIT B 2 .   ? 28.585 23.409  14.660  0.93 48.61 ? 301 CIT A C6  1 
HETATM 2120 O O5  . CIT B 2 .   ? 28.005 23.610  13.569  0.93 48.66 ? 301 CIT A O5  1 
HETATM 2121 O O6  . CIT B 2 .   ? 28.485 22.289  15.211  0.93 48.73 ? 301 CIT A O6  1 
HETATM 2122 C C1  . V2Y C 3 .   ? 20.533 11.226  13.051  1.00 24.11 ? 302 V2Y A C1  1 
HETATM 2123 C C2  . V2Y C 3 .   ? 20.289 12.398  12.364  1.00 26.20 ? 302 V2Y A C2  1 
HETATM 2124 C C3  . V2Y C 3 .   ? 21.371 13.136  11.882  1.00 27.09 ? 302 V2Y A C3  1 
HETATM 2125 C C4  . V2Y C 3 .   ? 18.415 11.514  12.844  1.00 25.49 ? 302 V2Y A C4  1 
HETATM 2126 N N1  . V2Y C 3 .   ? 22.587 12.691  12.180  1.00 26.16 ? 302 V2Y A N1  1 
HETATM 2127 N N2  . V2Y C 3 .   ? 21.773 10.833  13.309  1.00 23.55 ? 302 V2Y A N2  1 
HETATM 2128 C C5  . V2Y C 3 .   ? 16.785 8.414   8.980   1.00 26.42 ? 302 V2Y A C5  1 
HETATM 2129 C C6  . V2Y C 3 .   ? 22.771 11.575  12.873  1.00 25.72 ? 302 V2Y A C6  1 
HETATM 2130 C C7  . V2Y C 3 .   ? 16.608 9.567   7.968   1.00 27.09 ? 302 V2Y A C7  1 
HETATM 2131 C C8  . V2Y C 3 .   ? 15.356 10.278  8.520   1.00 27.99 ? 302 V2Y A C8  1 
HETATM 2132 C C9  . V2Y C 3 .   ? 15.348 9.879   9.996   1.00 27.62 ? 302 V2Y A C9  1 
HETATM 2133 C C10 . V2Y C 3 .   ? 14.009 10.052  10.698  1.00 26.70 ? 302 V2Y A C10 1 
HETATM 2134 C C11 . V2Y C 3 .   ? 13.078 6.048   12.192  1.00 41.20 ? 302 V2Y A C11 1 
HETATM 2135 C C12 . V2Y C 3 .   ? 13.701 6.125   10.772  1.00 35.76 ? 302 V2Y A C12 1 
HETATM 2136 C C13 . V2Y C 3 .   ? 14.742 4.998   10.550  1.00 35.74 ? 302 V2Y A C13 1 
HETATM 2137 C C14 . V2Y C 3 .   ? 14.452 4.151   9.474   1.00 36.28 ? 302 V2Y A C14 1 
HETATM 2138 C C15 . V2Y C 3 .   ? 15.253 3.052   9.163   1.00 33.46 ? 302 V2Y A C15 1 
HETATM 2139 C C16 . V2Y C 3 .   ? 16.364 2.771   9.948   1.00 31.46 ? 302 V2Y A C16 1 
HETATM 2140 C C17 . V2Y C 3 .   ? 16.627 3.582   11.054  1.00 35.00 ? 302 V2Y A C17 1 
HETATM 2141 C C18 . V2Y C 3 .   ? 15.780 4.640   11.427  1.00 33.58 ? 302 V2Y A C18 1 
HETATM 2142 C C19 . V2Y C 3 .   ? 16.281 5.471   12.616  1.00 33.75 ? 302 V2Y A C19 1 
HETATM 2143 C C20 . V2Y C 3 .   ? 16.484 7.613   13.819  1.00 27.46 ? 302 V2Y A C20 1 
HETATM 2144 C C21 . V2Y C 3 .   ? 17.880 7.394   14.378  1.00 30.32 ? 302 V2Y A C21 1 
HETATM 2145 C C22 . V2Y C 3 .   ? 19.164 9.409   14.193  1.00 27.85 ? 302 V2Y A C22 1 
HETATM 2146 C C23 . V2Y C 3 .   ? 18.243 9.535   15.412  1.00 29.10 ? 302 V2Y A C23 1 
HETATM 2147 C C24 . V2Y C 3 .   ? 18.241 8.067   15.736  1.00 29.87 ? 302 V2Y A C24 1 
HETATM 2148 C C25 . V2Y C 3 .   ? 17.026 11.368  12.883  1.00 27.36 ? 302 V2Y A C25 1 
HETATM 2149 C C26 . V2Y C 3 .   ? 15.851 11.200  12.955  1.00 30.78 ? 302 V2Y A C26 1 
HETATM 2150 C C27 . V2Y C 3 .   ? 14.455 10.830  13.112  1.00 31.17 ? 302 V2Y A C27 1 
HETATM 2151 C C28 . V2Y C 3 .   ? 15.920 6.664   7.540   1.00 25.56 ? 302 V2Y A C28 1 
HETATM 2152 C C29 . V2Y C 3 .   ? 17.541 5.237   7.610   1.00 25.82 ? 302 V2Y A C29 1 
HETATM 2153 C C30 . V2Y C 3 .   ? 17.889 6.304   8.422   1.00 25.90 ? 302 V2Y A C30 1 
HETATM 2154 C C31 . V2Y C 3 .   ? 19.890 5.303   8.924   1.00 25.80 ? 302 V2Y A C31 1 
HETATM 2155 C C32 . V2Y C 3 .   ? 18.442 4.195   7.490   1.00 27.21 ? 302 V2Y A C32 1 
HETATM 2156 N N3  . V2Y C 3 .   ? 21.184 14.258  11.140  1.00 26.89 ? 302 V2Y A N3  1 
HETATM 2157 N N4  . V2Y C 3 .   ? 18.968 12.554  12.226  1.00 26.65 ? 302 V2Y A N4  1 
HETATM 2158 N N5  . V2Y C 3 .   ? 19.368 10.703  13.384  1.00 26.22 ? 302 V2Y A N5  1 
HETATM 2159 N N6  . V2Y C 3 .   ? 12.302 7.071   12.543  1.00 45.64 ? 302 V2Y A N6  1 
HETATM 2160 N N7  . V2Y C 3 .   ? 16.023 6.780   12.679  1.00 32.14 ? 302 V2Y A N7  1 
HETATM 2161 N N8  . V2Y C 3 .   ? 16.885 7.151   8.357   1.00 25.55 ? 302 V2Y A N8  1 
HETATM 2162 N N9  . V2Y C 3 .   ? 16.315 5.466   7.095   1.00 25.86 ? 302 V2Y A N9  1 
HETATM 2163 N N10 . V2Y C 3 .   ? 19.061 6.335   9.070   1.00 25.49 ? 302 V2Y A N10 1 
HETATM 2164 N N11 . V2Y C 3 .   ? 19.599 4.262   8.165   1.00 23.62 ? 302 V2Y A N11 1 
HETATM 2165 N N12 . V2Y C 3 .   ? 18.141 3.143   6.709   1.00 24.86 ? 302 V2Y A N12 1 
HETATM 2166 O O1  . V2Y C 3 .   ? 17.754 10.423  7.992   1.00 27.83 ? 302 V2Y A O1  1 
HETATM 2167 O O2  . V2Y C 3 .   ? 15.387 11.676  8.336   1.00 26.74 ? 302 V2Y A O2  1 
HETATM 2168 O O3  . V2Y C 3 .   ? 15.757 8.511   9.945   1.00 26.80 ? 302 V2Y A O3  1 
HETATM 2169 O O4  . V2Y C 3 .   ? 14.045 9.782   12.113  1.00 31.51 ? 302 V2Y A O4  1 
HETATM 2170 O O5  . V2Y C 3 .   ? 13.352 5.133   12.956  1.00 38.34 ? 302 V2Y A O5  1 
HETATM 2171 O O6  . V2Y C 3 .   ? 16.540 4.850   13.650  1.00 30.89 ? 302 V2Y A O6  1 
HETATM 2172 O O7  . V2Y C 3 .   ? 18.437 8.435   13.413  1.00 28.61 ? 302 V2Y A O7  1 
HETATM 2173 O O8  . V2Y C 3 .   ? 18.954 10.169  16.512  1.00 30.66 ? 302 V2Y A O8  1 
HETATM 2174 O O9  . V2Y C 3 .   ? 19.445 7.606   16.304  1.00 32.46 ? 302 V2Y A O9  1 
HETATM 2175 O O   . HOH D 4 .   ? 23.985 8.079   -8.896  1.00 24.68 ? 401 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 34.582 14.424  22.959  1.00 53.50 ? 402 HOH A O   1 
HETATM 2177 O O   . HOH D 4 .   ? 8.236  18.171  18.201  1.00 51.06 ? 403 HOH A O   1 
HETATM 2178 O O   . HOH D 4 .   ? 32.165 15.662  24.125  1.00 41.90 ? 404 HOH A O   1 
HETATM 2179 O O   . HOH D 4 .   ? 8.243  31.799  41.815  1.00 27.08 ? 405 HOH A O   1 
HETATM 2180 O O   . HOH D 4 .   ? 24.473 16.333  24.988  1.00 53.41 ? 406 HOH A O   1 
HETATM 2181 O O   . HOH D 4 .   ? 2.715  20.015  -10.784 1.00 51.29 ? 407 HOH A O   1 
HETATM 2182 O O   . HOH D 4 .   ? 7.845  4.069   -9.779  1.00 47.85 ? 408 HOH A O   1 
HETATM 2183 O O   . HOH D 4 .   ? 10.160 5.671   -14.273 1.00 38.93 ? 409 HOH A O   1 
HETATM 2184 O O   . HOH D 4 .   ? 16.963 11.441  22.862  1.00 43.33 ? 410 HOH A O   1 
HETATM 2185 O O   . HOH D 4 .   ? 8.875  16.268  6.437   1.00 42.56 ? 411 HOH A O   1 
HETATM 2186 O O   . HOH D 4 .   ? 13.511 1.159   1.886   1.00 59.69 ? 412 HOH A O   1 
HETATM 2187 O O   . HOH D 4 .   ? 14.742 17.087  20.747  1.00 34.97 ? 413 HOH A O   1 
HETATM 2188 O O   . HOH D 4 .   ? 37.504 14.361  21.393  1.00 46.33 ? 414 HOH A O   1 
HETATM 2189 O O   . HOH D 4 .   ? 22.680 11.283  0.479   1.00 21.28 ? 415 HOH A O   1 
HETATM 2190 O O   . HOH D 4 .   ? 33.352 20.926  13.647  1.00 33.99 ? 416 HOH A O   1 
HETATM 2191 O O   . HOH D 4 .   ? 24.363 16.390  11.636  1.00 29.58 ? 417 HOH A O   1 
HETATM 2192 O O   . HOH D 4 .   ? 15.707 31.033  7.114   1.00 45.52 ? 418 HOH A O   1 
HETATM 2193 O O   . HOH D 4 .   ? 13.313 19.059  0.668   1.00 39.12 ? 419 HOH A O   1 
HETATM 2194 O O   . HOH D 4 .   ? 12.021 1.373   -4.939  1.00 37.49 ? 420 HOH A O   1 
HETATM 2195 O O   . HOH D 4 .   ? 21.992 23.387  -5.319  1.00 31.15 ? 421 HOH A O   1 
HETATM 2196 O O   . HOH D 4 .   ? 13.525 11.071  4.475   1.00 27.24 ? 422 HOH A O   1 
HETATM 2197 O O   . HOH D 4 .   ? 31.914 26.747  24.958  1.00 60.36 ? 423 HOH A O   1 
HETATM 2198 O O   . HOH D 4 .   ? 25.013 3.552   -1.843  1.00 40.27 ? 424 HOH A O   1 
HETATM 2199 O O   . HOH D 4 .   ? 13.646 22.404  -5.984  1.00 35.69 ? 425 HOH A O   1 
HETATM 2200 O O   . HOH D 4 .   ? 13.514 26.946  -0.457  1.00 42.26 ? 426 HOH A O   1 
HETATM 2201 O O   . HOH D 4 .   ? 15.424 28.782  12.138  1.00 32.45 ? 427 HOH A O   1 
HETATM 2202 O O   . HOH D 4 .   ? 27.927 26.129  -2.545  1.00 39.73 ? 428 HOH A O   1 
HETATM 2203 O O   . HOH D 4 .   ? 31.697 5.254   -11.769 1.00 31.91 ? 429 HOH A O   1 
HETATM 2204 O O   . HOH D 4 .   ? 9.771  6.419   1.634   1.00 39.68 ? 430 HOH A O   1 
HETATM 2205 O O   . HOH D 4 .   ? 20.176 26.604  2.694   1.00 33.52 ? 431 HOH A O   1 
HETATM 2206 O O   . HOH D 4 .   ? 22.366 21.107  7.033   1.00 26.90 ? 432 HOH A O   1 
HETATM 2207 O O   . HOH D 4 .   ? 6.416  31.128  30.554  1.00 47.91 ? 433 HOH A O   1 
HETATM 2208 O O   . HOH D 4 .   ? 22.877 -8.110  -14.012 1.00 38.14 ? 434 HOH A O   1 
HETATM 2209 O O   . HOH D 4 .   ? 17.423 10.910  18.625  1.00 37.87 ? 435 HOH A O   1 
HETATM 2210 O O   . HOH D 4 .   ? 2.518  24.191  22.533  1.00 45.78 ? 436 HOH A O   1 
HETATM 2211 O O   . HOH D 4 .   ? 31.346 5.311   0.000   0.50 36.64 ? 437 HOH A O   1 
HETATM 2212 O O   . HOH D 4 .   ? 29.173 6.609   4.881   1.00 22.93 ? 438 HOH A O   1 
HETATM 2213 O O   . HOH D 4 .   ? 24.002 5.428   9.902   1.00 31.44 ? 439 HOH A O   1 
HETATM 2214 O O   . HOH D 4 .   ? 11.093 7.454   -0.442  1.00 28.31 ? 440 HOH A O   1 
HETATM 2215 O O   . HOH D 4 .   ? 10.452 25.336  -7.047  1.00 51.77 ? 441 HOH A O   1 
HETATM 2216 O O   . HOH D 4 .   ? 12.855 10.261  -18.676 1.00 46.31 ? 442 HOH A O   1 
HETATM 2217 O O   . HOH D 4 .   ? 20.131 22.179  19.547  1.00 42.97 ? 443 HOH A O   1 
HETATM 2218 O O   . HOH D 4 .   ? 20.547 26.909  -4.723  1.00 34.35 ? 444 HOH A O   1 
HETATM 2219 O O   . HOH D 4 .   ? 22.979 7.523   11.203  1.00 28.30 ? 445 HOH A O   1 
HETATM 2220 O O   . HOH D 4 .   ? 20.645 11.713  5.001   1.00 25.06 ? 446 HOH A O   1 
HETATM 2221 O O   . HOH D 4 .   ? 8.443  20.665  3.940   1.00 45.97 ? 447 HOH A O   1 
HETATM 2222 O O   . HOH D 4 .   ? 25.243 9.226   -6.556  1.00 24.66 ? 448 HOH A O   1 
HETATM 2223 O O   . HOH D 4 .   ? 4.876  24.514  34.379  1.00 44.89 ? 449 HOH A O   1 
HETATM 2224 O O   . HOH D 4 .   ? 26.152 30.148  11.086  1.00 52.28 ? 450 HOH A O   1 
HETATM 2225 O O   . HOH D 4 .   ? 26.750 21.536  -14.539 1.00 39.60 ? 451 HOH A O   1 
HETATM 2226 O O   . HOH D 4 .   ? 4.782  18.858  29.243  1.00 40.91 ? 452 HOH A O   1 
HETATM 2227 O O   . HOH D 4 .   ? 21.436 15.121  31.995  1.00 46.84 ? 453 HOH A O   1 
HETATM 2228 O O   . HOH D 4 .   ? 20.182 8.094   10.992  1.00 28.07 ? 454 HOH A O   1 
HETATM 2229 O O   . HOH D 4 .   ? 29.887 26.604  1.203   1.00 39.90 ? 455 HOH A O   1 
HETATM 2230 O O   . HOH D 4 .   ? 27.352 5.888   -1.706  1.00 32.48 ? 456 HOH A O   1 
HETATM 2231 O O   . HOH D 4 .   ? 12.538 14.684  33.379  1.00 49.32 ? 457 HOH A O   1 
HETATM 2232 O O   . HOH D 4 .   ? 16.481 1.910   -20.673 1.00 50.94 ? 458 HOH A O   1 
HETATM 2233 O O   . HOH D 4 .   ? 21.248 1.485   -12.801 1.00 32.43 ? 459 HOH A O   1 
HETATM 2234 O O   . HOH D 4 .   ? 26.035 6.651   -3.767  1.00 23.39 ? 460 HOH A O   1 
HETATM 2235 O O   . HOH D 4 .   ? 27.322 26.910  9.672   1.00 44.15 ? 461 HOH A O   1 
HETATM 2236 O O   . HOH D 4 .   ? 14.393 4.171   5.398   1.00 32.18 ? 462 HOH A O   1 
HETATM 2237 O O   . HOH D 4 .   ? 10.145 13.542  12.890  1.00 45.94 ? 463 HOH A O   1 
HETATM 2238 O O   . HOH D 4 .   ? 23.498 0.577   -2.119  1.00 42.08 ? 464 HOH A O   1 
HETATM 2239 O O   . HOH D 4 .   ? 18.179 22.750  -14.336 1.00 49.15 ? 465 HOH A O   1 
HETATM 2240 O O   . HOH D 4 .   ? 24.154 18.617  13.389  1.00 45.81 ? 466 HOH A O   1 
HETATM 2241 O O   . HOH D 4 .   ? 27.405 27.212  -8.155  1.00 62.33 ? 467 HOH A O   1 
HETATM 2242 O O   . HOH D 4 .   ? 21.192 21.190  1.356   1.00 31.22 ? 468 HOH A O   1 
HETATM 2243 O O   . HOH D 4 .   ? 29.975 4.514   8.136   1.00 43.07 ? 469 HOH A O   1 
HETATM 2244 O O   . HOH D 4 .   ? 4.536  18.976  23.277  1.00 55.89 ? 470 HOH A O   1 
HETATM 2245 O O   . HOH D 4 .   ? 18.457 19.921  -14.219 1.00 45.23 ? 471 HOH A O   1 
HETATM 2246 O O   . HOH D 4 .   ? 26.982 3.238   -4.098  1.00 40.93 ? 472 HOH A O   1 
HETATM 2247 O O   . HOH D 4 .   ? 28.572 2.080   -10.540 1.00 41.54 ? 473 HOH A O   1 
HETATM 2248 O O   . HOH D 4 .   ? 10.083 15.128  9.845   1.00 36.68 ? 474 HOH A O   1 
HETATM 2249 O O   . HOH D 4 .   ? 10.166 3.658   -11.729 1.00 39.71 ? 475 HOH A O   1 
HETATM 2250 O O   . HOH D 4 .   ? 9.537  2.613   -14.136 1.00 66.58 ? 476 HOH A O   1 
HETATM 2251 O O   . HOH D 4 .   ? 5.991  21.911  2.459   1.00 58.17 ? 477 HOH A O   1 
HETATM 2252 O O   . HOH D 4 .   ? 24.366 1.458   -5.495  1.00 29.69 ? 478 HOH A O   1 
HETATM 2253 O O   . HOH D 4 .   ? 12.156 -3.390  -6.810  1.00 44.43 ? 479 HOH A O   1 
HETATM 2254 O O   . HOH D 4 .   ? 20.298 24.671  -13.379 1.00 57.26 ? 480 HOH A O   1 
HETATM 2255 O O   . HOH D 4 .   ? 3.149  16.489  25.626  1.00 53.25 ? 481 HOH A O   1 
HETATM 2256 O O   . HOH D 4 .   ? 11.100 26.820  -0.109  1.00 56.90 ? 482 HOH A O   1 
HETATM 2257 O O   . HOH D 4 .   ? 14.670 9.919   16.655  1.00 39.15 ? 483 HOH A O   1 
HETATM 2258 O O   . HOH D 4 .   ? 12.726 11.529  18.712  1.00 38.69 ? 484 HOH A O   1 
HETATM 2259 O O   . HOH D 4 .   ? 0.439  28.695  23.311  1.00 54.54 ? 485 HOH A O   1 
HETATM 2260 O O   . HOH D 4 .   ? 31.370 2.838   -9.379  1.00 70.77 ? 486 HOH A O   1 
HETATM 2261 O O   . HOH D 4 .   ? 29.108 25.895  -11.881 1.00 57.04 ? 487 HOH A O   1 
HETATM 2262 O O   . HOH D 4 .   ? 12.688 31.348  5.924   1.00 49.69 ? 488 HOH A O   1 
HETATM 2263 O O   . HOH D 4 .   ? 12.907 6.167   4.372   1.00 41.67 ? 489 HOH A O   1 
HETATM 2264 O O   . HOH D 4 .   ? 7.796  18.210  4.651   1.00 52.49 ? 490 HOH A O   1 
HETATM 2265 O O   . HOH D 4 .   ? 14.622 1.555   -0.875  1.00 50.13 ? 491 HOH A O   1 
HETATM 2266 O O   . HOH D 4 .   ? 16.328 28.043  -4.037  1.00 53.22 ? 492 HOH A O   1 
HETATM 2267 O O   . HOH D 4 .   ? 10.487 6.514   4.370   1.00 57.04 ? 493 HOH A O   1 
HETATM 2268 O O   . HOH D 4 .   ? 35.842 10.124  23.842  1.00 45.19 ? 494 HOH A O   1 
HETATM 2269 O O   . HOH D 4 .   ? 29.843 4.724   -2.047  1.00 46.74 ? 495 HOH A O   1 
HETATM 2270 O O   . HOH D 4 .   ? 13.688 8.358   5.636   1.00 43.65 ? 496 HOH A O   1 
HETATM 2271 O O   . HOH D 4 .   ? 31.112 4.785   4.088   1.00 32.70 ? 497 HOH A O   1 
HETATM 2272 O O   . HOH D 4 .   ? 11.930 7.931   7.882   1.00 42.03 ? 498 HOH A O   1 
HETATM 2273 O O   . HOH D 4 .   ? 21.332 0.000   0.000   0.50 51.90 ? 499 HOH A O   1 
HETATM 2274 O O   . HOH D 4 .   ? 0.250  14.308  -2.610  1.00 57.46 ? 500 HOH A O   1 
HETATM 2275 O O   . HOH D 4 .   ? 10.932 -5.799  -8.463  1.00 43.97 ? 501 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 1.0527 0.7716 0.8875 0.0937  0.1175  -0.1548 1   MET A N   
2    C CA  . MET A 1   ? 1.0302 0.7341 0.8642 0.1081  0.1171  -0.1341 1   MET A CA  
3    C C   . MET A 1   ? 0.9347 0.6726 0.7757 0.1250  0.1069  -0.1226 1   MET A C   
4    O O   . MET A 1   ? 0.8871 0.6570 0.7328 0.1234  0.1008  -0.1290 1   MET A O   
5    C CB  . MET A 1   ? 1.0652 0.7689 0.9010 0.0939  0.1148  -0.1262 1   MET A CB  
6    C CG  . MET A 1   ? 1.1302 0.8009 0.9596 0.0745  0.1266  -0.1382 1   MET A CG  
7    S SD  . MET A 1   ? 1.1486 0.8225 0.9805 0.0575  0.1247  -0.1293 1   MET A SD  
8    C CE  . MET A 1   ? 1.1133 0.8465 0.9575 0.0447  0.1100  -0.1381 1   MET A CE  
9    N N   . LYS A 2   ? 0.8941 0.6265 0.7349 0.1409  0.1059  -0.1058 2   LYS A N   
10   C CA  . LYS A 2   ? 0.8156 0.5855 0.6648 0.1526  0.0966  -0.0969 2   LYS A CA  
11   C C   . LYS A 2   ? 0.7089 0.5086 0.5656 0.1382  0.0874  -0.0931 2   LYS A C   
12   O O   . LYS A 2   ? 0.6757 0.4666 0.5318 0.1266  0.0872  -0.0895 2   LYS A O   
13   C CB  . LYS A 2   ? 0.8277 0.5897 0.6750 0.1732  0.0977  -0.0817 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.8831 0.6198 0.7231 0.1929  0.1066  -0.0844 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.9190 0.6433 0.7538 0.2147  0.1088  -0.0673 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.9693 0.6698 0.7965 0.2386  0.1177  -0.0684 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.9632 0.7019 0.7998 0.2498  0.1128  -0.0761 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.6452 0.4789 0.5084 0.1383  0.0812  -0.0951 3   TYR A N   
19   C CA  . TYR A 3   ? 0.5929 0.4524 0.4624 0.1275  0.0739  -0.0907 3   TYR A CA  
20   C C   . TYR A 3   ? 0.5664 0.4551 0.4426 0.1354  0.0701  -0.0858 3   TYR A C   
21   O O   . TYR A 3   ? 0.5926 0.4876 0.4688 0.1458  0.0724  -0.0895 3   TYR A O   
22   C CB  . TYR A 3   ? 0.5918 0.4607 0.4596 0.1129  0.0723  -0.1015 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.6067 0.4954 0.4733 0.1160  0.0719  -0.1091 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.6421 0.5195 0.5034 0.1195  0.0775  -0.1212 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.5682 0.4850 0.4381 0.1154  0.0673  -0.1042 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.6198 0.5173 0.4793 0.1222  0.0775  -0.1285 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.5782 0.5121 0.4449 0.1180  0.0683  -0.1100 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.5917 0.5177 0.4535 0.1213  0.0729  -0.1221 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.5820 0.5267 0.4401 0.1236  0.0742  -0.1280 3   TYR A OH  
30   N N   . MET A 4   ? 0.5355 0.4424 0.4175 0.1294  0.0654  -0.0787 4   MET A N   
31   C CA  . MET A 4   ? 0.5420 0.4753 0.4297 0.1320  0.0641  -0.0768 4   MET A CA  
32   C C   . MET A 4   ? 0.5054 0.4511 0.3950 0.1212  0.0611  -0.0740 4   MET A C   
33   O O   . MET A 4   ? 0.5098 0.4484 0.3984 0.1135  0.0588  -0.0726 4   MET A O   
34   C CB  . MET A 4   ? 0.5784 0.5231 0.4727 0.1413  0.0639  -0.0702 4   MET A CB  
35   C CG  . MET A 4   ? 0.5593 0.5047 0.4574 0.1370  0.0609  -0.0619 4   MET A CG  
36   S SD  . MET A 4   ? 0.5793 0.5475 0.4850 0.1264  0.0596  -0.0597 4   MET A SD  
37   C CE  . MET A 4   ? 0.5760 0.5705 0.4886 0.1331  0.0628  -0.0629 4   MET A CE  
38   N N   . ILE A 5   ? 0.4896 0.4534 0.3810 0.1209  0.0624  -0.0734 5   ILE A N   
39   C CA  . ILE A 5   ? 0.4720 0.4447 0.3633 0.1136  0.0614  -0.0691 5   ILE A CA  
40   C C   . ILE A 5   ? 0.4911 0.4766 0.3889 0.1135  0.0647  -0.0645 5   ILE A C   
41   O O   . ILE A 5   ? 0.4939 0.4895 0.3929 0.1167  0.0688  -0.0675 5   ILE A O   
42   C CB  . ILE A 5   ? 0.4859 0.4644 0.3686 0.1119  0.0622  -0.0730 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.4788 0.4483 0.3557 0.1102  0.0602  -0.0819 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.4704 0.4560 0.3510 0.1079  0.0613  -0.0660 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.4856 0.4677 0.3533 0.1083  0.0599  -0.0869 5   ILE A CD1 
46   N N   . THR A 6   ? 0.4680 0.4542 0.3705 0.1087  0.0638  -0.0588 6   THR A N   
47   C CA  . THR A 6   ? 0.4969 0.4936 0.4057 0.1057  0.0687  -0.0564 6   THR A CA  
48   C C   . THR A 6   ? 0.5373 0.5316 0.4410 0.1016  0.0723  -0.0519 6   THR A C   
49   O O   . THR A 6   ? 0.5936 0.5821 0.4922 0.1016  0.0685  -0.0490 6   THR A O   
50   C CB  . THR A 6   ? 0.5351 0.5342 0.4524 0.1038  0.0666  -0.0542 6   THR A CB  
51   O OG1 . THR A 6   ? 0.5871 0.5981 0.5113 0.0988  0.0726  -0.0551 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.4769 0.4661 0.3928 0.1002  0.0625  -0.0500 6   THR A CG2 
53   N N   . SER A 7   ? 0.5317 0.5311 0.4357 0.0987  0.0805  -0.0514 7   SER A N   
54   C CA  . SER A 7   ? 0.5051 0.4980 0.4013 0.0969  0.0865  -0.0450 7   SER A CA  
55   C C   . SER A 7   ? 0.5050 0.4944 0.4073 0.0904  0.0947  -0.0429 7   SER A C   
56   O O   . SER A 7   ? 0.5448 0.5437 0.4567 0.0853  0.0984  -0.0490 7   SER A O   
57   C CB  . SER A 7   ? 0.5239 0.5203 0.4108 0.0982  0.0926  -0.0457 7   SER A CB  
58   O OG  . SER A 7   ? 0.5467 0.5343 0.4245 0.0973  0.1008  -0.0372 7   SER A OG  
59   N N   . LYS A 8   ? 0.4927 0.4700 0.3892 0.0911  0.0983  -0.0350 8   LYS A N   
60   C CA  . LYS A 8   ? 0.5563 0.5248 0.4564 0.0845  0.1096  -0.0335 8   LYS A CA  
61   C C   . LYS A 8   ? 0.5678 0.5364 0.4656 0.0778  0.1227  -0.0362 8   LYS A C   
62   O O   . LYS A 8   ? 0.5694 0.5365 0.4744 0.0680  0.1331  -0.0411 8   LYS A O   
63   C CB  . LYS A 8   ? 0.5995 0.5522 0.4913 0.0901  0.1121  -0.0232 8   LYS A CB  
64   C CG  . LYS A 8   ? 0.6432 0.5784 0.5347 0.0850  0.1270  -0.0201 8   LYS A CG  
65   C CD  . LYS A 8   ? 0.6828 0.6017 0.5617 0.0960  0.1298  -0.0070 8   LYS A CD  
66   C CE  . LYS A 8   ? 0.7400 0.6378 0.6208 0.0931  0.1429  -0.0045 8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.7497 0.6553 0.6448 0.0904  0.1355  -0.0112 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.5708 0.5428 0.4589 0.0815  0.1233  -0.0348 9   GLY A N   
69   C CA  . GLY A 9   ? 0.5669 0.5413 0.4525 0.0743  0.1362  -0.0380 9   GLY A CA  
70   C C   . GLY A 9   ? 0.6166 0.5702 0.4869 0.0741  0.1499  -0.0271 9   GLY A C   
71   O O   . GLY A 9   ? 0.6424 0.5945 0.5092 0.0660  0.1636  -0.0290 9   GLY A O   
72   N N   . ASP A 10  ? 0.6281 0.5662 0.4884 0.0833  0.1475  -0.0154 10  ASP A N   
73   C CA  . ASP A 10  ? 0.6756 0.5952 0.5173 0.0877  0.1597  -0.0024 10  ASP A CA  
74   C C   . ASP A 10  ? 0.6808 0.6132 0.5089 0.0967  0.1530  0.0013  10  ASP A C   
75   O O   . ASP A 10  ? 0.6219 0.5743 0.4557 0.0993  0.1392  -0.0069 10  ASP A O   
76   C CB  . ASP A 10  ? 0.7357 0.6343 0.5708 0.0963  0.1620  0.0096  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.7538 0.6655 0.5902 0.1084  0.1440  0.0118  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.7385 0.6713 0.5817 0.1080  0.1306  0.0031  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.7876 0.6881 0.6183 0.1182  0.1444  0.0216  10  ASP A OD2 
80   N N   . GLU A 11  ? 0.7175 0.6373 0.5264 0.1012  0.1644  0.0135  11  GLU A N   
81   C CA  . GLU A 11  ? 0.7446 0.6790 0.5391 0.1086  0.1602  0.0164  11  GLU A CA  
82   C C   . GLU A 11  ? 0.7083 0.6601 0.5014 0.1206  0.1417  0.0160  11  GLU A C   
83   O O   . GLU A 11  ? 0.6993 0.6716 0.4946 0.1209  0.1318  0.0063  11  GLU A O   
84   C CB  . GLU A 11  ? 0.8450 0.7605 0.6164 0.1136  0.1762  0.0330  11  GLU A CB  
85   C CG  . GLU A 11  ? 0.9225 0.8529 0.6767 0.1203  0.1751  0.0371  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.0141 0.9214 0.7448 0.1236  0.1944  0.0548  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.0523 0.9290 0.7819 0.1201  0.2087  0.0625  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.0556 0.9739 0.7683 0.1295  0.1964  0.0607  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.7071 0.6514 0.4969 0.1301  0.1379  0.0254  12  LYS A N   
90   C CA  . LYS A 12  ? 0.6974 0.6613 0.4864 0.1401  0.1216  0.0241  12  LYS A CA  
91   C C   . LYS A 12  ? 0.6370 0.6155 0.4444 0.1322  0.1086  0.0074  12  LYS A C   
92   O O   . LYS A 12  ? 0.5886 0.5864 0.3945 0.1343  0.0983  -0.0002 12  LYS A O   
93   C CB  . LYS A 12  ? 0.7361 0.6904 0.5230 0.1502  0.1210  0.0352  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.7573 0.7361 0.5426 0.1610  0.1057  0.0344  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.7962 0.7672 0.5775 0.1739  0.1071  0.0469  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.8129 0.8150 0.5967 0.1823  0.0912  0.0427  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.8555 0.8855 0.6265 0.1871  0.0845  0.0400  12  LYS A NZ  
98   N N   . SER A 13  ? 0.6463 0.6155 0.4704 0.1232  0.1099  0.0013  13  SER A N   
99   C CA  . SER A 13  ? 0.5841 0.5638 0.4234 0.1181  0.0986  -0.0115 13  SER A CA  
100  C C   . SER A 13  ? 0.5831 0.5726 0.4244 0.1139  0.0979  -0.0219 13  SER A C   
101  O O   . SER A 13  ? 0.5822 0.5812 0.4276 0.1142  0.0884  -0.0309 13  SER A O   
102  C CB  . SER A 13  ? 0.5561 0.5263 0.4107 0.1112  0.1003  -0.0140 13  SER A CB  
103  O OG  . SER A 13  ? 0.5630 0.5237 0.4156 0.1162  0.1017  -0.0050 13  SER A OG  
104  N N   . ASP A 14  ? 0.5849 0.5716 0.4233 0.1097  0.1091  -0.0215 14  ASP A N   
105  C CA  . ASP A 14  ? 0.5894 0.5883 0.4309 0.1070  0.1088  -0.0321 14  ASP A CA  
106  C C   . ASP A 14  ? 0.6013 0.6117 0.4302 0.1132  0.1038  -0.0341 14  ASP A C   
107  O O   . ASP A 14  ? 0.5833 0.6031 0.4164 0.1136  0.0980  -0.0453 14  ASP A O   
108  C CB  . ASP A 14  ? 0.6383 0.6362 0.4799 0.0997  0.1230  -0.0324 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.6482 0.6458 0.5067 0.0913  0.1264  -0.0386 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.5970 0.5943 0.4661 0.0924  0.1174  -0.0412 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.6839 0.6842 0.5447 0.0830  0.1386  -0.0416 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.6168 0.6270 0.4293 0.1190  0.1068  -0.0234 15  LEU A N   
113  C CA  . LEU A 15  ? 0.6260 0.6524 0.4251 0.1248  0.1023  -0.0258 15  LEU A CA  
114  C C   . LEU A 15  ? 0.5848 0.6212 0.3886 0.1269  0.0887  -0.0344 15  LEU A C   
115  O O   . LEU A 15  ? 0.5510 0.5994 0.3541 0.1261  0.0840  -0.0466 15  LEU A O   
116  C CB  . LEU A 15  ? 0.6662 0.6918 0.4449 0.1326  0.1090  -0.0101 15  LEU A CB  
117  C CG  . LEU A 15  ? 0.7218 0.7352 0.4936 0.1280  0.1255  -0.0030 15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.7515 0.7559 0.5009 0.1370  0.1348  0.0163  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.7325 0.7604 0.5038 0.1231  0.1285  -0.0143 15  LEU A CD2 
120  N N   . LEU A 16  ? 0.5545 0.5857 0.3638 0.1283  0.0835  -0.0296 16  LEU A N   
121  C CA  . LEU A 16  ? 0.5669 0.6070 0.3827 0.1271  0.0722  -0.0391 16  LEU A CA  
122  C C   . LEU A 16  ? 0.5256 0.5595 0.3541 0.1202  0.0696  -0.0527 16  LEU A C   
123  O O   . LEU A 16  ? 0.5064 0.5477 0.3348 0.1183  0.0643  -0.0646 16  LEU A O   
124  C CB  . LEU A 16  ? 0.5606 0.5960 0.3822 0.1288  0.0685  -0.0319 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.5710 0.6212 0.3965 0.1275  0.0579  -0.0405 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.5840 0.6602 0.3959 0.1323  0.0538  -0.0447 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.5410 0.5895 0.3722 0.1301  0.0552  -0.0329 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.5116 0.5326 0.3503 0.1170  0.0742  -0.0515 17  ARG A N   
129  C CA  . ARG A 17  ? 0.4869 0.5029 0.3361 0.1143  0.0722  -0.0621 17  ARG A CA  
130  C C   . ARG A 17  ? 0.4941 0.5177 0.3377 0.1160  0.0740  -0.0721 17  ARG A C   
131  O O   . ARG A 17  ? 0.5231 0.5441 0.3688 0.1157  0.0703  -0.0829 17  ARG A O   
132  C CB  . ARG A 17  ? 0.4746 0.4834 0.3347 0.1121  0.0769  -0.0590 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.4968 0.5050 0.3651 0.1134  0.0763  -0.0681 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.4609 0.4696 0.3411 0.1116  0.0795  -0.0658 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.4782 0.4902 0.3651 0.1165  0.0786  -0.0731 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.5245 0.5479 0.4116 0.1198  0.0831  -0.0792 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.5236 0.5550 0.4038 0.1167  0.0895  -0.0788 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.5392 0.5663 0.4324 0.1272  0.0819  -0.0850 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.5265 0.5579 0.3624 0.1175  0.0811  -0.0692 18  LEU A N   
140  C CA  . LEU A 18  ? 0.5428 0.5839 0.3735 0.1193  0.0832  -0.0797 18  LEU A CA  
141  C C   . LEU A 18  ? 0.5496 0.6000 0.3710 0.1200  0.0776  -0.0875 18  LEU A C   
142  O O   . LEU A 18  ? 0.5282 0.5805 0.3499 0.1200  0.0769  -0.1012 18  LEU A O   
143  C CB  . LEU A 18  ? 0.5791 0.6291 0.4017 0.1195  0.0928  -0.0747 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.5847 0.6323 0.4175 0.1163  0.1005  -0.0732 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.5904 0.6473 0.4135 0.1141  0.1118  -0.0698 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.5733 0.6226 0.4191 0.1189  0.0977  -0.0852 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.5333 0.5913 0.3464 0.1209  0.0742  -0.0800 19  ASN A N   
148  C CA  . ASN A 19  ? 0.5570 0.6315 0.3619 0.1206  0.0685  -0.0893 19  ASN A CA  
149  C C   . ASN A 19  ? 0.5539 0.6200 0.3690 0.1147  0.0627  -0.1017 19  ASN A C   
150  O O   . ASN A 19  ? 0.5654 0.6383 0.3779 0.1112  0.0613  -0.1172 19  ASN A O   
151  C CB  . ASN A 19  ? 0.5391 0.6290 0.3328 0.1254  0.0658  -0.0776 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.5550 0.6602 0.3312 0.1316  0.0713  -0.0706 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.5764 0.6862 0.3486 0.1305  0.0759  -0.0783 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.5633 0.6760 0.3280 0.1393  0.0716  -0.0551 19  ASN A ND2 
155  N N   . MET A 20  ? 0.5174 0.5677 0.3434 0.1126  0.0606  -0.0958 20  MET A N   
156  C CA  . MET A 20  ? 0.5173 0.5557 0.3515 0.1063  0.0573  -0.1064 20  MET A CA  
157  C C   . MET A 20  ? 0.5459 0.5676 0.3842 0.1065  0.0615  -0.1167 20  MET A C   
158  O O   . MET A 20  ? 0.5524 0.5665 0.3909 0.1016  0.0618  -0.1305 20  MET A O   
159  C CB  . MET A 20  ? 0.5038 0.5305 0.3475 0.1045  0.0547  -0.0968 20  MET A CB  
160  C CG  . MET A 20  ? 0.5001 0.5428 0.3410 0.1045  0.0499  -0.0903 20  MET A CG  
161  S SD  . MET A 20  ? 0.5095 0.5387 0.3628 0.1012  0.0474  -0.0823 20  MET A SD  
162  C CE  . MET A 20  ? 0.4927 0.5129 0.3512 0.0903  0.0455  -0.0980 20  MET A CE  
163  N N   . ILE A 21  ? 0.5417 0.5582 0.3831 0.1123  0.0659  -0.1111 21  ILE A N   
164  C CA  . ILE A 21  ? 0.5520 0.5569 0.3966 0.1161  0.0700  -0.1207 21  ILE A CA  
165  C C   . ILE A 21  ? 0.5461 0.5602 0.3820 0.1153  0.0722  -0.1355 21  ILE A C   
166  O O   . ILE A 21  ? 0.5611 0.5610 0.3978 0.1147  0.0745  -0.1485 21  ILE A O   
167  C CB  . ILE A 21  ? 0.5676 0.5750 0.4175 0.1226  0.0742  -0.1138 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.5469 0.5464 0.4063 0.1225  0.0725  -0.1026 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.5805 0.5823 0.4324 0.1296  0.0785  -0.1247 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.5394 0.5482 0.4047 0.1260  0.0769  -0.0974 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.5472 0.5842 0.3736 0.1154  0.0724  -0.1338 22  ALA A N   
172  C CA  . ALA A 22  ? 0.5775 0.6283 0.3948 0.1144  0.0743  -0.1488 22  ALA A CA  
173  C C   . ALA A 22  ? 0.5917 0.6413 0.4078 0.1060  0.0711  -0.1629 22  ALA A C   
174  O O   . ALA A 22  ? 0.5919 0.6346 0.4071 0.1032  0.0748  -0.1805 22  ALA A O   
175  C CB  . ALA A 22  ? 0.5650 0.6426 0.3698 0.1166  0.0751  -0.1419 22  ALA A CB  
176  N N   . GLY A 23  ? 0.5969 0.6528 0.4137 0.1012  0.0653  -0.1567 23  GLY A N   
177  C CA  . GLY A 23  ? 0.6196 0.6776 0.4372 0.0908  0.0629  -0.1713 23  GLY A CA  
178  C C   . GLY A 23  ? 0.6152 0.6387 0.4409 0.0858  0.0674  -0.1805 23  GLY A C   
179  O O   . GLY A 23  ? 0.6284 0.6466 0.4527 0.0767  0.0708  -0.1995 23  GLY A O   
180  N N   . PHE A 24  ? 0.5901 0.5894 0.4234 0.0914  0.0684  -0.1673 24  PHE A N   
181  C CA  . PHE A 24  ? 0.6227 0.5871 0.4611 0.0901  0.0737  -0.1727 24  PHE A CA  
182  C C   . PHE A 24  ? 0.6666 0.6177 0.5019 0.0954  0.0812  -0.1858 24  PHE A C   
183  O O   . PHE A 24  ? 0.7173 0.6402 0.5525 0.0919  0.0879  -0.1972 24  PHE A O   
184  C CB  . PHE A 24  ? 0.5873 0.5350 0.4332 0.0974  0.0726  -0.1551 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.6469 0.5951 0.4971 0.0903  0.0678  -0.1463 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.6795 0.6186 0.5298 0.0779  0.0687  -0.1559 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.6154 0.5735 0.4701 0.0950  0.0634  -0.1297 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.6758 0.6185 0.5309 0.0715  0.0645  -0.1482 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.6338 0.5935 0.4929 0.0894  0.0593  -0.1224 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.6474 0.6007 0.5069 0.0783  0.0594  -0.1311 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.6073 0.5766 0.4396 0.1040  0.0817  -0.1845 25  GLY A N   
192  C CA  . GLY A 25  ? 0.6623 0.6236 0.4918 0.1098  0.0890  -0.1984 25  GLY A CA  
193  C C   . GLY A 25  ? 0.7133 0.6763 0.5366 0.0991  0.0928  -0.2209 25  GLY A C   
194  O O   . GLY A 25  ? 0.7220 0.6663 0.5438 0.1019  0.1009  -0.2355 25  GLY A O   
195  N N   . GLU A 26  ? 0.7406 0.7270 0.5604 0.0871  0.0876  -0.2253 26  GLU A N   
196  C CA  . GLU A 26  ? 0.7877 0.7816 0.6026 0.0740  0.0909  -0.2494 26  GLU A CA  
197  C C   . GLU A 26  ? 0.8222 0.7808 0.6411 0.0625  0.0973  -0.2604 26  GLU A C   
198  O O   . GLU A 26  ? 0.8423 0.8033 0.6582 0.0488  0.1025  -0.2837 26  GLU A O   
199  C CB  . GLU A 26  ? 0.7797 0.8192 0.5891 0.0669  0.0825  -0.2501 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.7767 0.8481 0.5788 0.0781  0.0781  -0.2372 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.8246 0.9011 0.6208 0.0828  0.0845  -0.2503 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.8310 0.9212 0.6227 0.0930  0.0845  -0.2389 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 0.8711 0.9368 0.6670 0.0752  0.0909  -0.2733 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.8155 0.7420 0.6404 0.0668  0.0983  -0.2454 27  TYR A N   
205  C CA  . TYR A 27  ? 0.8560 0.7432 0.6828 0.0570  0.1063  -0.2522 27  TYR A CA  
206  C C   . TYR A 27  ? 0.9401 0.7826 0.7675 0.0721  0.1144  -0.2437 27  TYR A C   
207  O O   . TYR A 27  ? 0.9656 0.8122 0.7932 0.0890  0.1136  -0.2362 27  TYR A O   
208  C CB  . TYR A 27  ? 0.8299 0.7234 0.6615 0.0476  0.0999  -0.2410 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.7897 0.7302 0.6210 0.0354  0.0916  -0.2487 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.7348 0.7128 0.5655 0.0444  0.0808  -0.2342 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.8130 0.7610 0.6439 0.0155  0.0955  -0.2710 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.7181 0.7402 0.5467 0.0374  0.0733  -0.2393 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.7996 0.7977 0.6304 0.0066  0.0871  -0.2785 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.7763 0.8114 0.6054 0.0194  0.0756  -0.2613 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.8057 0.8914 0.6327 0.0146  0.0672  -0.2666 27  TYR A OH  
216  N N   . ASP A 28  ? 1.0161 0.8172 0.8430 0.0662  0.1230  -0.2450 28  ASP A N   
217  C CA  . ASP A 28  ? 1.0742 0.8311 0.8997 0.0822  0.1308  -0.2333 28  ASP A CA  
218  C C   . ASP A 28  ? 1.0561 0.8169 0.8866 0.0904  0.1223  -0.2076 28  ASP A C   
219  O O   . ASP A 28  ? 1.0508 0.7858 0.8807 0.0857  0.1256  -0.1995 28  ASP A O   
220  C CB  . ASP A 28  ? 1.1622 0.8689 0.9819 0.0719  0.1464  -0.2464 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.2192 0.8773 1.0346 0.0909  0.1554  -0.2318 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.2209 0.8852 1.0375 0.1138  0.1523  -0.2212 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 1.2589 0.8747 1.0692 0.0832  0.1660  -0.2306 28  ASP A OD2 
224  N N   . MET A 29  ? 1.0231 0.8182 0.8581 0.1017  0.1122  -0.1956 29  MET A N   
225  C CA  . MET A 29  ? 0.9739 0.7810 0.8147 0.1076  0.1037  -0.1742 29  MET A CA  
226  C C   . MET A 29  ? 0.9112 0.7310 0.7552 0.1273  0.1012  -0.1640 29  MET A C   
227  O O   . MET A 29  ? 0.9044 0.7532 0.7492 0.1298  0.0981  -0.1682 29  MET A O   
228  C CB  . MET A 29  ? 0.9691 0.8126 0.8135 0.0952  0.0937  -0.1714 29  MET A CB  
229  C CG  . MET A 29  ? 0.9846 0.8252 0.8279 0.0754  0.0948  -0.1818 29  MET A CG  
230  S SD  . MET A 29  ? 0.9878 0.7973 0.8330 0.0698  0.0978  -0.1701 29  MET A SD  
231  C CE  . MET A 29  ? 0.9543 0.7884 0.8068 0.0813  0.0865  -0.1465 29  MET A CE  
232  N N   . GLU A 30  ? 0.8669 0.6680 0.7123 0.1409  0.1029  -0.1507 30  GLU A N   
233  C CA  . GLU A 30  ? 0.8415 0.6560 0.6909 0.1605  0.1013  -0.1420 30  GLU A CA  
234  C C   . GLU A 30  ? 0.7745 0.6161 0.6316 0.1607  0.0924  -0.1264 30  GLU A C   
235  O O   . GLU A 30  ? 0.7743 0.6063 0.6321 0.1557  0.0901  -0.1167 30  GLU A O   
236  C CB  . GLU A 30  ? 0.9027 0.6812 0.7476 0.1777  0.1096  -0.1379 30  GLU A CB  
237  C CG  . GLU A 30  ? 0.9240 0.7177 0.7734 0.2003  0.1078  -0.1276 30  GLU A CG  
238  C CD  . GLU A 30  ? 0.9834 0.7392 0.8256 0.2194  0.1162  -0.1214 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.0231 0.7364 0.8563 0.2125  0.1245  -0.1240 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 0.9949 0.7638 0.8398 0.2416  0.1154  -0.1141 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.7125 0.5875 0.5750 0.1651  0.0885  -0.1252 31  TYR A N   
242  C CA  . TYR A 31  ? 0.6827 0.5825 0.5529 0.1650  0.0824  -0.1128 31  TYR A CA  
243  C C   . TYR A 31  ? 0.6823 0.5806 0.5563 0.1819  0.0830  -0.1039 31  TYR A C   
244  O O   . TYR A 31  ? 0.6830 0.5847 0.5575 0.1971  0.0866  -0.1076 31  TYR A O   
245  C CB  . TYR A 31  ? 0.6604 0.5936 0.5339 0.1620  0.0808  -0.1154 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.6053 0.5592 0.4855 0.1563  0.0765  -0.1049 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.5977 0.5649 0.4860 0.1645  0.0758  -0.0981 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.5913 0.5521 0.4696 0.1432  0.0736  -0.1023 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.5587 0.5431 0.4534 0.1573  0.0733  -0.0908 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.5740 0.5485 0.4578 0.1382  0.0715  -0.0930 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.5491 0.5342 0.4415 0.1441  0.0719  -0.0882 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.5000 0.4980 0.3982 0.1374  0.0713  -0.0817 31  TYR A OH  
253  N N   . ASP A 32  ? 0.6430 0.5392 0.5195 0.1803  0.0795  -0.0924 32  ASP A N   
254  C CA  . ASP A 32  ? 0.6544 0.5549 0.5336 0.1969  0.0792  -0.0830 32  ASP A CA  
255  C C   . ASP A 32  ? 0.6275 0.5452 0.5128 0.1887  0.0735  -0.0735 32  ASP A C   
256  O O   . ASP A 32  ? 0.6425 0.5426 0.5245 0.1786  0.0724  -0.0688 32  ASP A O   
257  C CB  . ASP A 32  ? 0.6772 0.5382 0.5465 0.2080  0.0849  -0.0793 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.6789 0.5448 0.5482 0.2286  0.0845  -0.0672 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.6263 0.5268 0.5040 0.2302  0.0786  -0.0615 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.7147 0.5490 0.5744 0.2437  0.0909  -0.0634 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.6181 0.5712 0.5127 0.1912  0.0708  -0.0724 33  ASP A N   
262  C CA  . ASP A 33  ? 0.6538 0.6227 0.5545 0.1831  0.0666  -0.0653 33  ASP A CA  
263  C C   . ASP A 33  ? 0.6582 0.6351 0.5598 0.1973  0.0650  -0.0568 33  ASP A C   
264  O O   . ASP A 33  ? 0.6659 0.6666 0.5746 0.1930  0.0619  -0.0534 33  ASP A O   
265  C CB  . ASP A 33  ? 0.6596 0.6605 0.5694 0.1732  0.0663  -0.0700 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.6890 0.7215 0.6061 0.1839  0.0682  -0.0752 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.7001 0.7336 0.6157 0.2017  0.0683  -0.0742 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.6664 0.7229 0.5902 0.1745  0.0704  -0.0804 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.6696 0.6270 0.5634 0.2149  0.0678  -0.0532 34  VAL A N   
270  C CA  . VAL A 34  ? 0.6993 0.6603 0.5900 0.2315  0.0667  -0.0422 34  VAL A CA  
271  C C   . VAL A 34  ? 0.7128 0.6328 0.5915 0.2294  0.0692  -0.0323 34  VAL A C   
272  O O   . VAL A 34  ? 0.6818 0.6075 0.5599 0.2267  0.0664  -0.0235 34  VAL A O   
273  C CB  . VAL A 34  ? 0.7334 0.7042 0.6226 0.2572  0.0690  -0.0424 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.7531 0.7299 0.6368 0.2770  0.0675  -0.0289 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.7271 0.7443 0.6295 0.2570  0.0670  -0.0530 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.7528 0.6316 0.6217 0.2288  0.0754  -0.0350 35  GLU A N   
277  C CA  . GLU A 35  ? 0.7844 0.6217 0.6420 0.2219  0.0802  -0.0283 35  GLU A CA  
278  C C   . GLU A 35  ? 0.7458 0.5629 0.6029 0.1996  0.0825  -0.0395 35  GLU A C   
279  O O   . GLU A 35  ? 0.7638 0.5431 0.6115 0.1981  0.0905  -0.0438 35  GLU A O   
280  C CB  . GLU A 35  ? 0.8999 0.7006 0.7434 0.2429  0.0887  -0.0205 35  GLU A CB  
281  C CG  . GLU A 35  ? 0.9612 0.7819 0.8023 0.2687  0.0866  -0.0073 35  GLU A CG  
282  C CD  . GLU A 35  ? 1.0387 0.8174 0.8632 0.2922  0.0967  0.0022  35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.0940 0.8705 0.9091 0.3090  0.0975  0.0187  35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.0485 0.7956 0.8682 0.2945  0.1046  -0.0066 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.7083 0.5502 0.5748 0.1822  0.0763  -0.0447 36  PRO A N   
286  C CA  . PRO A 36  ? 0.6921 0.5202 0.5573 0.1625  0.0776  -0.0540 36  PRO A CA  
287  C C   . PRO A 36  ? 0.6874 0.4877 0.5460 0.1519  0.0812  -0.0494 36  PRO A C   
288  O O   . PRO A 36  ? 0.6864 0.4861 0.5433 0.1553  0.0805  -0.0376 36  PRO A O   
289  C CB  . PRO A 36  ? 0.6557 0.5191 0.5316 0.1513  0.0702  -0.0566 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.6560 0.5429 0.5380 0.1587  0.0663  -0.0471 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.6796 0.5627 0.5575 0.1797  0.0691  -0.0428 36  PRO A CD  
292  N N   . GLU A 37  ? 0.6439 0.4236 0.4984 0.1378  0.0859  -0.0600 37  GLU A N   
293  C CA  . GLU A 37  ? 0.6626 0.4241 0.5136 0.1212  0.0893  -0.0602 37  GLU A CA  
294  C C   . GLU A 37  ? 0.6487 0.4390 0.5086 0.1042  0.0819  -0.0659 37  GLU A C   
295  O O   . GLU A 37  ? 0.6249 0.4122 0.4851 0.0912  0.0824  -0.0646 37  GLU A O   
296  C CB  . GLU A 37  ? 0.7672 0.4901 0.6087 0.1138  0.1005  -0.0711 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.8621 0.5438 0.6913 0.1297  0.1113  -0.0625 37  GLU A CG  
298  C CD  . GLU A 37  ? 0.9456 0.5928 0.7669 0.1291  0.1227  -0.0762 37  GLU A CD  
299  O OE1 . GLU A 37  ? 0.9662 0.6057 0.7877 0.1082  0.1271  -0.0918 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 0.9903 0.6204 0.8058 0.1500  0.1277  -0.0725 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.6234 0.4412 0.4897 0.1051  0.0760  -0.0720 38  ILE A N   
302  C CA  . ILE A 38  ? 0.5803 0.4257 0.4534 0.0934  0.0695  -0.0761 38  ILE A CA  
303  C C   . ILE A 38  ? 0.5240 0.3969 0.4039 0.1021  0.0637  -0.0699 38  ILE A C   
304  O O   . ILE A 38  ? 0.5247 0.4024 0.4043 0.1124  0.0645  -0.0713 38  ILE A O   
305  C CB  . ILE A 38  ? 0.6158 0.4644 0.4864 0.0845  0.0707  -0.0913 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.6537 0.4726 0.5178 0.0741  0.0790  -0.1003 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.5961 0.4751 0.4718 0.0755  0.0639  -0.0939 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.6309 0.4474 0.4967 0.0611  0.0794  -0.0974 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.5023 0.3934 0.3885 0.0972  0.0590  -0.0644 39  VAL A N   
310  C CA  . VAL A 39  ? 0.5130 0.4272 0.4056 0.1023  0.0558  -0.0598 39  VAL A CA  
311  C C   . VAL A 39  ? 0.4660 0.3963 0.3612 0.0941  0.0525  -0.0617 39  VAL A C   
312  O O   . VAL A 39  ? 0.4831 0.4154 0.3806 0.0867  0.0506  -0.0603 39  VAL A O   
313  C CB  . VAL A 39  ? 0.5313 0.4511 0.4286 0.1067  0.0548  -0.0507 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.5129 0.4562 0.4179 0.1066  0.0531  -0.0489 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.5324 0.4429 0.4263 0.1198  0.0575  -0.0473 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.4706 0.4126 0.3644 0.0965  0.0524  -0.0648 40  ILE A N   
317  C CA  . ILE A 40  ? 0.4664 0.4235 0.3599 0.0927  0.0501  -0.0648 40  ILE A CA  
318  C C   . ILE A 40  ? 0.4428 0.4103 0.3403 0.0965  0.0516  -0.0577 40  ILE A C   
319  O O   . ILE A 40  ? 0.4411 0.4108 0.3388 0.1012  0.0548  -0.0578 40  ILE A O   
320  C CB  . ILE A 40  ? 0.4921 0.4544 0.3781 0.0927  0.0503  -0.0727 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.5164 0.4662 0.3989 0.0869  0.0511  -0.0830 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.4983 0.4792 0.3818 0.0920  0.0476  -0.0705 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.5287 0.4837 0.4040 0.0870  0.0524  -0.0937 40  ILE A CD1 
324  N N   . SER A 41  ? 0.4316 0.4054 0.3324 0.0939  0.0504  -0.0528 41  SER A N   
325  C CA  . SER A 41  ? 0.4583 0.4376 0.3623 0.0957  0.0542  -0.0472 41  SER A CA  
326  C C   . SER A 41  ? 0.4457 0.4311 0.3434 0.0980  0.0551  -0.0441 41  SER A C   
327  O O   . SER A 41  ? 0.4922 0.4831 0.3880 0.0975  0.0510  -0.0443 41  SER A O   
328  C CB  . SER A 41  ? 0.4904 0.4700 0.4028 0.0924  0.0538  -0.0439 41  SER A CB  
329  O OG  . SER A 41  ? 0.5669 0.5497 0.4819 0.0923  0.0581  -0.0399 41  SER A OG  
330  N N   . ILE A 42  ? 0.4381 0.4241 0.3320 0.1008  0.0610  -0.0410 42  ILE A N   
331  C CA  . ILE A 42  ? 0.4415 0.4307 0.3261 0.1055  0.0636  -0.0352 42  ILE A CA  
332  C C   . ILE A 42  ? 0.4883 0.4699 0.3745 0.1055  0.0723  -0.0281 42  ILE A C   
333  O O   . ILE A 42  ? 0.4557 0.4337 0.3440 0.1022  0.0796  -0.0293 42  ILE A O   
334  C CB  . ILE A 42  ? 0.4711 0.4650 0.3456 0.1085  0.0653  -0.0375 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.4708 0.4697 0.3442 0.1069  0.0585  -0.0472 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.5230 0.5213 0.3852 0.1153  0.0684  -0.0289 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.4639 0.4695 0.3277 0.1095  0.0599  -0.0520 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.4786 0.4583 0.3642 0.1089  0.0726  -0.0220 43  GLY A N   
339  C CA  . GLY A 43  ? 0.4998 0.4675 0.3866 0.1087  0.0826  -0.0161 43  GLY A CA  
340  C C   . GLY A 43  ? 0.5161 0.4834 0.4076 0.1116  0.0803  -0.0130 43  GLY A C   
341  O O   . GLY A 43  ? 0.5209 0.4937 0.4056 0.1206  0.0771  -0.0074 43  GLY A O   
342  N N   . GLY A 44  ? 0.4400 0.4045 0.3432 0.1046  0.0818  -0.0174 44  GLY A N   
343  C CA  . GLY A 44  ? 0.4386 0.4039 0.3473 0.1067  0.0802  -0.0158 44  GLY A CA  
344  C C   . GLY A 44  ? 0.4232 0.3969 0.3435 0.0984  0.0740  -0.0233 44  GLY A C   
345  O O   . GLY A 44  ? 0.4144 0.3930 0.3364 0.0940  0.0695  -0.0280 44  GLY A O   
346  N N   . ASP A 45  ? 0.4164 0.3916 0.3437 0.0978  0.0744  -0.0238 45  ASP A N   
347  C CA  . ASP A 45  ? 0.4167 0.4004 0.3536 0.0902  0.0696  -0.0297 45  ASP A CA  
348  C C   . ASP A 45  ? 0.4300 0.4133 0.3722 0.0828  0.0741  -0.0346 45  ASP A C   
349  O O   . ASP A 45  ? 0.4628 0.4545 0.4089 0.0787  0.0689  -0.0379 45  ASP A O   
350  C CB  . ASP A 45  ? 0.4192 0.4062 0.3623 0.0911  0.0705  -0.0298 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.4634 0.4620 0.4047 0.0965  0.0628  -0.0280 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.4506 0.4560 0.3878 0.0952  0.0559  -0.0293 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.4669 0.4692 0.4113 0.1016  0.0643  -0.0267 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.4324 0.4073 0.3746 0.0810  0.0845  -0.0353 46  GLY A N   
355  C CA  . GLY A 46  ? 0.4273 0.4088 0.3756 0.0731  0.0889  -0.0424 46  GLY A CA  
356  C C   . GLY A 46  ? 0.4330 0.4215 0.3781 0.0745  0.0838  -0.0433 46  GLY A C   
357  O O   . GLY A 46  ? 0.4033 0.4051 0.3536 0.0719  0.0807  -0.0480 46  GLY A O   
358  N N   . THR A 47  ? 0.4096 0.3906 0.3453 0.0800  0.0832  -0.0387 47  THR A N   
359  C CA  . THR A 47  ? 0.4038 0.3902 0.3360 0.0824  0.0786  -0.0403 47  THR A CA  
360  C C   . THR A 47  ? 0.3964 0.3874 0.3299 0.0840  0.0688  -0.0409 47  THR A C   
361  O O   . THR A 47  ? 0.3996 0.3965 0.3345 0.0852  0.0663  -0.0437 47  THR A O   
362  C CB  . THR A 47  ? 0.4197 0.3989 0.3408 0.0878  0.0792  -0.0359 47  THR A CB  
363  O OG1 . THR A 47  ? 0.4821 0.4516 0.3995 0.0874  0.0896  -0.0320 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.4159 0.4002 0.3340 0.0892  0.0785  -0.0396 47  THR A CG2 
365  N N   . PHE A 48  ? 0.3954 0.3835 0.3278 0.0846  0.0641  -0.0382 48  PHE A N   
366  C CA  . PHE A 48  ? 0.4220 0.4110 0.3543 0.0839  0.0571  -0.0389 48  PHE A CA  
367  C C   . PHE A 48  ? 0.3867 0.3823 0.3254 0.0812  0.0568  -0.0400 48  PHE A C   
368  O O   . PHE A 48  ? 0.4168 0.4117 0.3534 0.0833  0.0539  -0.0398 48  PHE A O   
369  C CB  . PHE A 48  ? 0.4328 0.4220 0.3639 0.0831  0.0531  -0.0376 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.4352 0.4226 0.3650 0.0796  0.0482  -0.0394 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.4185 0.4076 0.3527 0.0756  0.0475  -0.0386 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.4257 0.4087 0.3491 0.0795  0.0457  -0.0423 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.4282 0.4112 0.3592 0.0717  0.0454  -0.0390 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.4342 0.4108 0.3557 0.0744  0.0439  -0.0448 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.4404 0.4152 0.3651 0.0705  0.0442  -0.0424 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.3812 0.3834 0.3267 0.0775  0.0606  -0.0413 49  LEU A N   
377  C CA  . LEU A 49  ? 0.3757 0.3901 0.3270 0.0749  0.0604  -0.0435 49  LEU A CA  
378  C C   . LEU A 49  ? 0.4130 0.4373 0.3649 0.0778  0.0614  -0.0462 49  LEU A C   
379  O O   . LEU A 49  ? 0.4070 0.4408 0.3588 0.0809  0.0581  -0.0452 49  LEU A O   
380  C CB  . LEU A 49  ? 0.3715 0.3925 0.3305 0.0692  0.0658  -0.0472 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.3882 0.4064 0.3490 0.0675  0.0645  -0.0456 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.4033 0.4238 0.3712 0.0632  0.0725  -0.0507 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.3664 0.3924 0.3273 0.0657  0.0590  -0.0441 49  LEU A CD2 
384  N N   . SER A 50  ? 0.4261 0.4501 0.3780 0.0779  0.0663  -0.0491 50  SER A N   
385  C CA  . SER A 50  ? 0.4377 0.4763 0.3915 0.0811  0.0671  -0.0530 50  SER A CA  
386  C C   . SER A 50  ? 0.4215 0.4534 0.3680 0.0905  0.0613  -0.0490 50  SER A C   
387  O O   . SER A 50  ? 0.4375 0.4819 0.3846 0.0970  0.0592  -0.0494 50  SER A O   
388  C CB  . SER A 50  ? 0.4849 0.5254 0.4405 0.0771  0.0754  -0.0579 50  SER A CB  
389  O OG  . SER A 50  ? 0.5161 0.5638 0.4794 0.0676  0.0829  -0.0637 50  SER A OG  
390  N N   . ALA A 51  ? 0.4234 0.4363 0.3627 0.0918  0.0590  -0.0455 51  ALA A N   
391  C CA  . ALA A 51  ? 0.4157 0.4177 0.3477 0.0988  0.0554  -0.0435 51  ALA A CA  
392  C C   . ALA A 51  ? 0.4168 0.4156 0.3469 0.1013  0.0522  -0.0390 51  ALA A C   
393  O O   . ALA A 51  ? 0.4578 0.4544 0.3837 0.1102  0.0514  -0.0367 51  ALA A O   
394  C CB  . ALA A 51  ? 0.4188 0.4048 0.3441 0.0968  0.0542  -0.0435 51  ALA A CB  
395  N N   . PHE A 52  ? 0.4092 0.4068 0.3412 0.0945  0.0511  -0.0369 52  PHE A N   
396  C CA  . PHE A 52  ? 0.4261 0.4214 0.3553 0.0953  0.0492  -0.0317 52  PHE A CA  
397  C C   . PHE A 52  ? 0.4310 0.4449 0.3619 0.1028  0.0490  -0.0301 52  PHE A C   
398  O O   . PHE A 52  ? 0.4473 0.4554 0.3708 0.1114  0.0482  -0.0239 52  PHE A O   
399  C CB  . PHE A 52  ? 0.4177 0.4163 0.3511 0.0860  0.0488  -0.0317 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.4408 0.4429 0.3721 0.0853  0.0480  -0.0268 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.4728 0.4567 0.3951 0.0854  0.0480  -0.0214 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.3922 0.4156 0.3300 0.0834  0.0484  -0.0283 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.4603 0.4464 0.3787 0.0846  0.0485  -0.0153 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.4017 0.4315 0.3363 0.0831  0.0476  -0.0233 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.4325 0.4430 0.3568 0.0842  0.0478  -0.0158 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.4038 0.4410 0.3438 0.0998  0.0507  -0.0358 53  HIS A N   
407  C CA  . HIS A 53  ? 0.4008 0.4647 0.3439 0.1058  0.0501  -0.0368 53  HIS A CA  
408  C C   . HIS A 53  ? 0.4657 0.5366 0.4066 0.1180  0.0498  -0.0372 53  HIS A C   
409  O O   . HIS A 53  ? 0.5088 0.5978 0.4478 0.1289  0.0478  -0.0342 53  HIS A O   
410  C CB  . HIS A 53  ? 0.3831 0.4711 0.3376 0.0960  0.0535  -0.0460 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.4039 0.4923 0.3608 0.0876  0.0536  -0.0457 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.3912 0.4934 0.3456 0.0903  0.0508  -0.0417 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.3826 0.4591 0.3430 0.0782  0.0563  -0.0480 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.3976 0.4980 0.3552 0.0811  0.0519  -0.0432 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.3912 0.4755 0.3527 0.0744  0.0551  -0.0469 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.4846 0.5443 0.4253 0.1178  0.0519  -0.0409 54  GLN A N   
417  C CA  . GLN A 54  ? 0.5023 0.5672 0.4405 0.1305  0.0518  -0.0416 54  GLN A CA  
418  C C   . GLN A 54  ? 0.5575 0.6024 0.4842 0.1437  0.0497  -0.0322 54  GLN A C   
419  O O   . GLN A 54  ? 0.6068 0.6624 0.5309 0.1589  0.0491  -0.0301 54  GLN A O   
420  C CB  . GLN A 54  ? 0.4850 0.5390 0.4232 0.1269  0.0549  -0.0470 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.5014 0.5600 0.4373 0.1397  0.0556  -0.0494 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.5263 0.5741 0.4607 0.1349  0.0590  -0.0546 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.5208 0.5552 0.4538 0.1241  0.0601  -0.0545 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.5558 0.6117 0.4898 0.1442  0.0606  -0.0589 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.5563 0.5721 0.4757 0.1385  0.0495  -0.0267 55  TYR A N   
426  C CA  . TYR A 55  ? 0.5600 0.5484 0.4671 0.1483  0.0506  -0.0187 55  TYR A CA  
427  C C   . TYR A 55  ? 0.5537 0.5348 0.4545 0.1470  0.0504  -0.0094 55  TYR A C   
428  O O   . TYR A 55  ? 0.5694 0.5193 0.4592 0.1482  0.0535  -0.0031 55  TYR A O   
429  C CB  . TYR A 55  ? 0.5642 0.5221 0.4663 0.1421  0.0529  -0.0223 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.5644 0.5281 0.4693 0.1470  0.0539  -0.0298 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.5892 0.5510 0.4897 0.1635  0.0556  -0.0287 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.5262 0.4985 0.4372 0.1366  0.0538  -0.0373 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.5882 0.5586 0.4917 0.1678  0.0568  -0.0365 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.5680 0.5470 0.4804 0.1403  0.0555  -0.0437 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.5823 0.5614 0.4917 0.1551  0.0569  -0.0442 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.5675 0.5557 0.4788 0.1584  0.0590  -0.0515 55  TYR A OH  
437  N N   . GLU A 56  ? 0.5489 0.5585 0.4560 0.1440  0.0480  -0.0092 56  GLU A N   
438  C CA  . GLU A 56  ? 0.5832 0.5877 0.4845 0.1404  0.0481  -0.0012 56  GLU A CA  
439  C C   . GLU A 56  ? 0.6220 0.6158 0.5090 0.1569  0.0498  0.0119  56  GLU A C   
440  O O   . GLU A 56  ? 0.6477 0.6295 0.5261 0.1542  0.0517  0.0206  56  GLU A O   
441  C CB  . GLU A 56  ? 0.5503 0.5893 0.4619 0.1325  0.0457  -0.0058 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.5520 0.6303 0.4691 0.1421  0.0436  -0.0089 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.5683 0.6779 0.4933 0.1329  0.0426  -0.0140 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.6016 0.7354 0.5223 0.1417  0.0407  -0.0089 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.5475 0.6578 0.4822 0.1177  0.0442  -0.0228 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.6373 0.6344 0.5205 0.1748  0.0500  0.0142  57  GLU A N   
447  C CA  . GLU A 57  ? 0.6788 0.6613 0.5460 0.1944  0.0527  0.0286  57  GLU A CA  
448  C C   . GLU A 57  ? 0.6953 0.6250 0.5495 0.1966  0.0600  0.0336  57  GLU A C   
449  O O   . GLU A 57  ? 0.7198 0.6263 0.5579 0.2121  0.0651  0.0472  57  GLU A O   
450  C CB  . GLU A 57  ? 0.7352 0.7516 0.6047 0.2159  0.0497  0.0289  57  GLU A CB  
451  C CG  . GLU A 57  ? 0.7863 0.8578 0.6671 0.2135  0.0439  0.0235  57  GLU A CG  
452  C CD  . GLU A 57  ? 0.8551 0.9674 0.7369 0.2358  0.0407  0.0244  57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.9005 1.0063 0.7812 0.2498  0.0420  0.0234  57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.8877 1.0423 0.7717 0.2397  0.0369  0.0250  57  GLU A OE2 
455  N N   . ARG A 58  ? 0.6446 0.5546 0.5041 0.1816  0.0616  0.0230  58  ARG A N   
456  C CA  . ARG A 58  ? 0.6742 0.5367 0.5227 0.1798  0.0693  0.0236  58  ARG A CA  
457  C C   . ARG A 58  ? 0.6622 0.5092 0.5139 0.1554  0.0709  0.0164  58  ARG A C   
458  O O   . ARG A 58  ? 0.6216 0.4463 0.4730 0.1467  0.0743  0.0074  58  ARG A O   
459  C CB  . ARG A 58  ? 0.7059 0.5631 0.5568 0.1889  0.0703  0.0153  58  ARG A CB  
460  C CG  . ARG A 58  ? 0.7687 0.6316 0.6128 0.2166  0.0713  0.0236  58  ARG A CG  
461  C CD  . ARG A 58  ? 0.8092 0.6649 0.6549 0.2267  0.0735  0.0149  58  ARG A CD  
462  N NE  . ARG A 58  ? 0.8602 0.6683 0.6977 0.2185  0.0819  0.0100  58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.8567 0.6616 0.7014 0.1993  0.0813  -0.0040 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.8251 0.6667 0.6838 0.1880  0.0735  -0.0119 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.8727 0.6383 0.7098 0.1913  0.0893  -0.0104 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.5956 0.4573 0.4505 0.1442  0.0685  0.0193  59  LEU A N   
467  C CA  . LEU A 59  ? 0.5915 0.4495 0.4525 0.1224  0.0684  0.0109  59  LEU A CA  
468  C C   . LEU A 59  ? 0.6539 0.4709 0.5038 0.1129  0.0775  0.0110  59  LEU A C   
469  O O   . LEU A 59  ? 0.6765 0.4887 0.5315 0.0970  0.0781  -0.0003 59  LEU A O   
470  C CB  . LEU A 59  ? 0.5733 0.4562 0.4401 0.1138  0.0648  0.0135  59  LEU A CB  
471  C CG  . LEU A 59  ? 0.5393 0.4625 0.4203 0.1153  0.0574  0.0081  59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.4981 0.4420 0.3830 0.1072  0.0557  0.0103  59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.5135 0.4422 0.4051 0.1074  0.0548  -0.0041 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.6936 0.4819 0.5278 0.1220  0.0854  0.0233  60  ASP A N   
475  C CA  . ASP A 60  ? 0.7890 0.5345 0.6120 0.1101  0.0969  0.0224  60  ASP A CA  
476  C C   . ASP A 60  ? 0.8145 0.5325 0.6348 0.1107  0.1024  0.0122  60  ASP A C   
477  O O   . ASP A 60  ? 0.8490 0.5338 0.6626 0.0964  0.1125  0.0061  60  ASP A O   
478  C CB  . ASP A 60  ? 0.8830 0.6005 0.6871 0.1202  0.1062  0.0405  60  ASP A CB  
479  C CG  A ASP A 60  ? 0.9319 0.6234 0.7284 0.0991  0.1164  0.0410  60  ASP A CG  
480  C CG  B ASP A 60  ? 0.8919 0.6097 0.6878 0.1492  0.1052  0.0527  60  ASP A CG  
481  O OD1 A ASP A 60  ? 0.9856 0.6293 0.7652 0.0994  0.1306  0.0470  60  ASP A OD1 
482  O OD1 B ASP A 60  ? 0.8379 0.5985 0.6448 0.1599  0.0941  0.0517  60  ASP A OD1 
483  O OD2 A ASP A 60  ? 0.9089 0.6269 0.7164 0.0817  0.1114  0.0344  60  ASP A OD2 
484  O OD2 B ASP A 60  ? 0.9560 0.6318 0.7346 0.1614  0.1164  0.0622  60  ASP A OD2 
485  N N   . GLU A 61  ? 0.7895 0.5222 0.6154 0.1252  0.0968  0.0086  61  GLU A N   
486  C CA  . GLU A 61  ? 0.8276 0.5373 0.6509 0.1279  0.1018  -0.0016 61  GLU A CA  
487  C C   . GLU A 61  ? 0.7690 0.5062 0.6066 0.1174  0.0941  -0.0180 61  GLU A C   
488  O O   . GLU A 61  ? 0.8057 0.5321 0.6425 0.1202  0.0968  -0.0277 61  GLU A O   
489  C CB  . GLU A 61  ? 0.8906 0.5934 0.7067 0.1554  0.1033  0.0076  61  GLU A CB  
490  C CG  . GLU A 61  ? 0.9835 0.6672 0.7842 0.1707  0.1093  0.0275  61  GLU A CG  
491  C CD  . GLU A 61  ? 1.0281 0.7278 0.8256 0.2008  0.1059  0.0381  61  GLU A CD  
492  O OE1 . GLU A 61  ? 1.0258 0.7331 0.8289 0.2110  0.1038  0.0296  61  GLU A OE1 
493  O OE2 . GLU A 61  ? 1.0542 0.7627 0.8437 0.2146  0.1051  0.0543  61  GLU A OE2 
494  N N   . ILE A 62  ? 0.6947 0.4661 0.5442 0.1060  0.0854  -0.0212 62  ILE A N   
495  C CA  . ILE A 62  ? 0.6414 0.4413 0.5028 0.1002  0.0779  -0.0328 62  ILE A CA  
496  C C   . ILE A 62  ? 0.6125 0.4238 0.4799 0.0801  0.0758  -0.0406 62  ILE A C   
497  O O   . ILE A 62  ? 0.5760 0.3933 0.4449 0.0731  0.0752  -0.0350 62  ILE A O   
498  C CB  . ILE A 62  ? 0.5915 0.4267 0.4622 0.1107  0.0695  -0.0281 62  ILE A CB  
499  C CG1 . ILE A 62  ? 0.6057 0.4398 0.4731 0.1305  0.0705  -0.0242 62  ILE A CG1 
500  C CG2 . ILE A 62  ? 0.5727 0.4337 0.4536 0.1030  0.0636  -0.0375 62  ILE A CG2 
501  C CD1 . ILE A 62  ? 0.5950 0.4664 0.4722 0.1380  0.0638  -0.0217 62  ILE A CD1 
502  N N   . ALA A 63  ? 0.5948 0.4137 0.4657 0.0720  0.0744  -0.0536 63  ALA A N   
503  C CA  . ALA A 63  ? 0.5696 0.4115 0.4480 0.0576  0.0699  -0.0613 63  ALA A CA  
504  C C   . ALA A 63  ? 0.5434 0.4159 0.4297 0.0639  0.0617  -0.0622 63  ALA A C   
505  O O   . ALA A 63  ? 0.5436 0.4176 0.4284 0.0702  0.0614  -0.0670 63  ALA A O   
506  C CB  . ALA A 63  ? 0.6185 0.4500 0.4938 0.0429  0.0750  -0.0761 63  ALA A CB  
507  N N   . PHE A 64  ? 0.5138 0.4085 0.4076 0.0622  0.0566  -0.0575 64  PHE A N   
508  C CA  . PHE A 64  ? 0.4944 0.4133 0.3945 0.0678  0.0512  -0.0565 64  PHE A CA  
509  C C   . PHE A 64  ? 0.5087 0.4454 0.4110 0.0612  0.0481  -0.0641 64  PHE A C   
510  O O   . PHE A 64  ? 0.4971 0.4378 0.4006 0.0507  0.0481  -0.0693 64  PHE A O   
511  C CB  . PHE A 64  ? 0.4853 0.4167 0.3920 0.0702  0.0491  -0.0481 64  PHE A CB  
512  C CG  . PHE A 64  ? 0.4539 0.3799 0.3595 0.0792  0.0506  -0.0409 64  PHE A CG  
513  C CD1 . PHE A 64  ? 0.4583 0.3953 0.3669 0.0879  0.0498  -0.0400 64  PHE A CD1 
514  C CD2 . PHE A 64  ? 0.4669 0.3800 0.3681 0.0793  0.0532  -0.0349 64  PHE A CD2 
515  C CE1 . PHE A 64  ? 0.4668 0.4067 0.3756 0.0968  0.0507  -0.0350 64  PHE A CE1 
516  C CE2 . PHE A 64  ? 0.4926 0.4065 0.3919 0.0902  0.0539  -0.0277 64  PHE A CE2 
517  C CZ  . PHE A 64  ? 0.4901 0.4203 0.3942 0.0992  0.0520  -0.0285 64  PHE A CZ  
518  N N   . ILE A 65  ? 0.4539 0.4041 0.3564 0.0678  0.0457  -0.0644 65  ILE A N   
519  C CA  . ILE A 65  ? 0.5080 0.4790 0.4107 0.0662  0.0422  -0.0687 65  ILE A CA  
520  C C   . ILE A 65  ? 0.4620 0.4438 0.3662 0.0755  0.0413  -0.0610 65  ILE A C   
521  O O   . ILE A 65  ? 0.4721 0.4476 0.3746 0.0816  0.0437  -0.0581 65  ILE A O   
522  C CB  . ILE A 65  ? 0.5962 0.5688 0.4923 0.0637  0.0426  -0.0795 65  ILE A CB  
523  C CG1 . ILE A 65  ? 0.6430 0.6017 0.5376 0.0520  0.0461  -0.0891 65  ILE A CG1 
524  C CG2 . ILE A 65  ? 0.6310 0.6315 0.5258 0.0653  0.0383  -0.0826 65  ILE A CG2 
525  C CD1 . ILE A 65  ? 0.6701 0.6267 0.5585 0.0489  0.0483  -0.1014 65  ILE A CD1 
526  N N   . GLY A 66  ? 0.4286 0.4266 0.3356 0.0768  0.0389  -0.0582 66  GLY A N   
527  C CA  . GLY A 66  ? 0.4477 0.4498 0.3545 0.0853  0.0406  -0.0503 66  GLY A CA  
528  C C   . GLY A 66  ? 0.4748 0.4929 0.3751 0.0914  0.0388  -0.0497 66  GLY A C   
529  O O   . GLY A 66  ? 0.5175 0.5524 0.4182 0.0898  0.0346  -0.0538 66  GLY A O   
530  N N   . ILE A 67  ? 0.4588 0.4745 0.3523 0.0985  0.0422  -0.0449 67  ILE A N   
531  C CA  . ILE A 67  ? 0.4500 0.4799 0.3344 0.1073  0.0417  -0.0408 67  ILE A CA  
532  C C   . ILE A 67  ? 0.4839 0.5052 0.3671 0.1150  0.0480  -0.0290 67  ILE A C   
533  O O   . ILE A 67  ? 0.4862 0.4917 0.3712 0.1131  0.0544  -0.0264 67  ILE A O   
534  C CB  . ILE A 67  ? 0.4510 0.4833 0.3256 0.1089  0.0426  -0.0445 67  ILE A CB  
535  C CG1 . ILE A 67  ? 0.4739 0.5116 0.3495 0.1004  0.0383  -0.0581 67  ILE A CG1 
536  C CG2 . ILE A 67  ? 0.4634 0.5096 0.3259 0.1200  0.0435  -0.0370 67  ILE A CG2 
537  C CD1 . ILE A 67  ? 0.4906 0.5281 0.3580 0.1011  0.0402  -0.0640 67  ILE A CD1 
538  N N   . HIS A 68  ? 0.4493 0.4813 0.3295 0.1240  0.0471  -0.0227 68  HIS A N   
539  C CA  . HIS A 68  ? 0.5006 0.5190 0.3779 0.1323  0.0554  -0.0112 68  HIS A CA  
540  C C   . HIS A 68  ? 0.5535 0.5726 0.4149 0.1435  0.0598  -0.0021 68  HIS A C   
541  O O   . HIS A 68  ? 0.5435 0.5839 0.3965 0.1527  0.0544  -0.0004 68  HIS A O   
542  C CB  . HIS A 68  ? 0.5297 0.5545 0.4130 0.1379  0.0541  -0.0079 68  HIS A CB  
543  C CG  . HIS A 68  ? 0.5439 0.5963 0.4222 0.1479  0.0468  -0.0073 68  HIS A CG  
544  N ND1 . HIS A 68  ? 0.5996 0.6574 0.4654 0.1653  0.0496  0.0042  68  HIS A ND1 
545  C CD2 . HIS A 68  ? 0.5485 0.6271 0.4325 0.1431  0.0374  -0.0174 68  HIS A CD2 
546  C CE1 . HIS A 68  ? 0.5912 0.6823 0.4559 0.1722  0.0407  0.0010  68  HIS A CE1 
547  N NE2 . HIS A 68  ? 0.5662 0.6710 0.4427 0.1574  0.0335  -0.0133 68  HIS A NE2 
548  N N   . THR A 69  ? 0.5829 0.5815 0.4396 0.1422  0.0700  0.0029  69  THR A N   
549  C CA  . THR A 69  ? 0.6308 0.6259 0.4704 0.1528  0.0768  0.0137  69  THR A CA  
550  C C   . THR A 69  ? 0.6811 0.6588 0.5140 0.1641  0.0868  0.0277  69  THR A C   
551  O O   . THR A 69  ? 0.7122 0.6867 0.5281 0.1768  0.0928  0.0401  69  THR A O   
552  C CB  . THR A 69  ? 0.6259 0.6101 0.4618 0.1449  0.0839  0.0113  69  THR A CB  
553  O OG1 . THR A 69  ? 0.6294 0.5966 0.4775 0.1338  0.0904  0.0069  69  THR A OG1 
554  C CG2 . THR A 69  ? 0.6224 0.6248 0.4595 0.1395  0.0745  -0.0005 69  THR A CG2 
555  N N   . GLY A 70  ? 0.6945 0.6609 0.5395 0.1608  0.0894  0.0263  70  GLY A N   
556  C CA  . GLY A 70  ? 0.7116 0.6642 0.5523 0.1733  0.0972  0.0374  70  GLY A CA  
557  C C   . GLY A 70  ? 0.7139 0.6907 0.5605 0.1823  0.0860  0.0359  70  GLY A C   
558  O O   . GLY A 70  ? 0.6911 0.6980 0.5359 0.1855  0.0740  0.0317  70  GLY A O   
559  N N   . HIS A 71  ? 0.7331 0.6990 0.5875 0.1853  0.0906  0.0373  71  HIS A N   
560  C CA  . HIS A 71  ? 0.7508 0.7429 0.6121 0.1937  0.0805  0.0349  71  HIS A CA  
561  C C   . HIS A 71  ? 0.6616 0.6741 0.5392 0.1767  0.0688  0.0191  71  HIS A C   
562  O O   . HIS A 71  ? 0.6525 0.6555 0.5362 0.1606  0.0692  0.0113  71  HIS A O   
563  C CB  . HIS A 71  ? 0.8126 0.7870 0.6766 0.2039  0.0898  0.0412  71  HIS A CB  
564  C CG  . HIS A 71  ? 0.8841 0.8414 0.7295 0.2260  0.1005  0.0590  71  HIS A CG  
565  N ND1 . HIS A 71  ? 0.9158 0.8332 0.7503 0.2252  0.1176  0.0677  71  HIS A ND1 
566  C CD2 . HIS A 71  ? 0.9129 0.8887 0.7468 0.2500  0.0969  0.0702  71  HIS A CD2 
567  C CE1 . HIS A 71  ? 0.9541 0.8607 0.7700 0.2482  0.1254  0.0852  71  HIS A CE1 
568  N NE2 . HIS A 71  ? 0.9488 0.8919 0.7637 0.2651  0.1123  0.0876  71  HIS A NE2 
569  N N   . LEU A 72  ? 0.6067 0.6492 0.4898 0.1814  0.0589  0.0147  72  LEU A N   
570  C CA  . LEU A 72  ? 0.5799 0.6421 0.4758 0.1656  0.0491  0.0005  72  LEU A CA  
571  C C   . LEU A 72  ? 0.5670 0.6100 0.4756 0.1515  0.0533  -0.0050 72  LEU A C   
572  O O   . LEU A 72  ? 0.5558 0.5855 0.4685 0.1558  0.0604  -0.0013 72  LEU A O   
573  C CB  . LEU A 72  ? 0.6005 0.6990 0.5013 0.1728  0.0404  -0.0036 72  LEU A CB  
574  C CG  . LEU A 72  ? 0.5892 0.7066 0.5044 0.1562  0.0331  -0.0179 72  LEU A CG  
575  C CD1 . LEU A 72  ? 0.5977 0.7271 0.5109 0.1431  0.0268  -0.0281 72  LEU A CD1 
576  C CD2 . LEU A 72  ? 0.5897 0.7407 0.5118 0.1648  0.0280  -0.0208 72  LEU A CD2 
577  N N   . GLY A 73  ? 0.5273 0.5684 0.4408 0.1356  0.0497  -0.0136 73  GLY A N   
578  C CA  . GLY A 73  ? 0.5145 0.5437 0.4386 0.1231  0.0522  -0.0186 73  GLY A CA  
579  C C   . GLY A 73  ? 0.5349 0.5828 0.4677 0.1140  0.0446  -0.0272 73  GLY A C   
580  O O   . GLY A 73  ? 0.5596 0.6275 0.4904 0.1137  0.0379  -0.0315 73  GLY A O   
581  N N   . PHE A 74  ? 0.4546 0.4978 0.3966 0.1056  0.0464  -0.0304 74  PHE A N   
582  C CA  . PHE A 74  ? 0.4465 0.5044 0.3951 0.0952  0.0409  -0.0377 74  PHE A CA  
583  C C   . PHE A 74  ? 0.4523 0.5020 0.3980 0.0840  0.0387  -0.0417 74  PHE A C   
584  O O   . PHE A 74  ? 0.5045 0.5634 0.4523 0.0748  0.0353  -0.0476 74  PHE A O   
585  C CB  . PHE A 74  ? 0.3856 0.4438 0.3436 0.0910  0.0440  -0.0392 74  PHE A CB  
586  C CG  . PHE A 74  ? 0.4106 0.4869 0.3739 0.0985  0.0433  -0.0399 74  PHE A CG  
587  C CD1 . PHE A 74  ? 0.4148 0.4852 0.3768 0.1128  0.0486  -0.0341 74  PHE A CD1 
588  C CD2 . PHE A 74  ? 0.4088 0.5087 0.3778 0.0921  0.0382  -0.0465 74  PHE A CD2 
589  C CE1 . PHE A 74  ? 0.4317 0.5195 0.3983 0.1228  0.0482  -0.0342 74  PHE A CE1 
590  C CE2 . PHE A 74  ? 0.3849 0.5066 0.3597 0.1003  0.0372  -0.0480 74  PHE A CE2 
591  C CZ  . PHE A 74  ? 0.4574 0.5737 0.4312 0.1172  0.0417  -0.0415 74  PHE A CZ  
592  N N   . TYR A 75  ? 0.3966 0.4289 0.3380 0.0843  0.0419  -0.0389 75  TYR A N   
593  C CA  . TYR A 75  ? 0.3929 0.4165 0.3301 0.0777  0.0402  -0.0419 75  TYR A CA  
594  C C   . TYR A 75  ? 0.4598 0.4823 0.3885 0.0826  0.0393  -0.0422 75  TYR A C   
595  O O   . TYR A 75  ? 0.4657 0.4876 0.3907 0.0776  0.0370  -0.0477 75  TYR A O   
596  C CB  . TYR A 75  ? 0.3891 0.3992 0.3278 0.0753  0.0438  -0.0399 75  TYR A CB  
597  C CG  . TYR A 75  ? 0.4284 0.4422 0.3742 0.0704  0.0449  -0.0399 75  TYR A CG  
598  C CD1 . TYR A 75  ? 0.3831 0.4016 0.3304 0.0629  0.0425  -0.0423 75  TYR A CD1 
599  C CD2 . TYR A 75  ? 0.3775 0.3909 0.3283 0.0721  0.0494  -0.0387 75  TYR A CD2 
600  C CE1 . TYR A 75  ? 0.3780 0.4019 0.3307 0.0583  0.0438  -0.0420 75  TYR A CE1 
601  C CE2 . TYR A 75  ? 0.3719 0.3920 0.3291 0.0673  0.0505  -0.0401 75  TYR A CE2 
602  C CZ  . TYR A 75  ? 0.3716 0.3977 0.3294 0.0612  0.0473  -0.0410 75  TYR A CZ  
603  O OH  . TYR A 75  ? 0.3672 0.4018 0.3300 0.0565  0.0487  -0.0421 75  TYR A OH  
604  N N   . ALA A 76  ? 0.4580 0.4784 0.3831 0.0919  0.0426  -0.0365 76  ALA A N   
605  C CA  . ALA A 76  ? 0.4910 0.5127 0.4065 0.0982  0.0426  -0.0351 76  ALA A CA  
606  C C   . ALA A 76  ? 0.5009 0.5438 0.4133 0.1046  0.0381  -0.0353 76  ALA A C   
607  O O   . ALA A 76  ? 0.5159 0.5625 0.4242 0.1162  0.0405  -0.0278 76  ALA A O   
608  C CB  . ALA A 76  ? 0.4737 0.4820 0.3852 0.1043  0.0501  -0.0280 76  ALA A CB  
609  N N   . ASP A 77  ? 0.5060 0.5640 0.4206 0.0971  0.0325  -0.0444 77  ASP A N   
610  C CA  . ASP A 77  ? 0.5355 0.6218 0.4509 0.1015  0.0277  -0.0471 77  ASP A CA  
611  C C   . ASP A 77  ? 0.5859 0.6925 0.4932 0.1032  0.0234  -0.0533 77  ASP A C   
612  O O   . ASP A 77  ? 0.6087 0.7462 0.5175 0.1048  0.0184  -0.0589 77  ASP A O   
613  C CB  . ASP A 77  ? 0.5491 0.6462 0.4750 0.0906  0.0253  -0.0546 77  ASP A CB  
614  C CG  . ASP A 77  ? 0.6070 0.6948 0.5339 0.0742  0.0254  -0.0644 77  ASP A CG  
615  O OD1 . ASP A 77  ? 0.6325 0.7029 0.5532 0.0723  0.0273  -0.0652 77  ASP A OD1 
616  O OD2 . ASP A 77  ? 0.6456 0.7428 0.5791 0.0634  0.0247  -0.0714 77  ASP A OD2 
617  N N   . TRP A 78  ? 0.5756 0.6700 0.4745 0.1034  0.0254  -0.0532 78  TRP A N   
618  C CA  . TRP A 78  ? 0.5492 0.6642 0.4392 0.1055  0.0220  -0.0595 78  TRP A CA  
619  C C   . TRP A 78  ? 0.5232 0.6358 0.4009 0.1206  0.0248  -0.0477 78  TRP A C   
620  O O   . TRP A 78  ? 0.5265 0.6131 0.4025 0.1238  0.0312  -0.0384 78  TRP A O   
621  C CB  . TRP A 78  ? 0.5876 0.6921 0.4771 0.0917  0.0227  -0.0723 78  TRP A CB  
622  C CG  . TRP A 78  ? 0.5860 0.6856 0.4850 0.0765  0.0227  -0.0819 78  TRP A CG  
623  C CD1 . TRP A 78  ? 0.5911 0.6612 0.4934 0.0675  0.0270  -0.0830 78  TRP A CD1 
624  C CD2 . TRP A 78  ? 0.6031 0.7285 0.5090 0.0692  0.0192  -0.0905 78  TRP A CD2 
625  N NE1 . TRP A 78  ? 0.5765 0.6484 0.4855 0.0547  0.0273  -0.0906 78  TRP A NE1 
626  C CE2 . TRP A 78  ? 0.6005 0.7067 0.5127 0.0540  0.0228  -0.0964 78  TRP A CE2 
627  C CE3 . TRP A 78  ? 0.6024 0.7677 0.5095 0.0747  0.0137  -0.0939 78  TRP A CE3 
628  C CZ2 . TRP A 78  ? 0.6146 0.7382 0.5343 0.0415  0.0221  -0.1063 78  TRP A CZ2 
629  C CZ3 . TRP A 78  ? 0.6086 0.7960 0.5250 0.0630  0.0119  -0.1051 78  TRP A CZ3 
630  C CH2 . TRP A 78  ? 0.6122 0.7776 0.5349 0.0453  0.0166  -0.1115 78  TRP A CH2 
631  N N   . ARG A 79  ? 0.5187 0.6609 0.3872 0.1299  0.0208  -0.0482 79  ARG A N   
632  C CA  . ARG A 79  ? 0.5822 0.7243 0.4360 0.1460  0.0241  -0.0349 79  ARG A CA  
633  C C   . ARG A 79  ? 0.6060 0.7394 0.4508 0.1419  0.0269  -0.0386 79  ARG A C   
634  O O   . ARG A 79  ? 0.6174 0.7601 0.4644 0.1304  0.0235  -0.0538 79  ARG A O   
635  C CB  . ARG A 79  ? 0.6132 0.7953 0.4590 0.1607  0.0183  -0.0324 79  ARG A CB  
636  C CG  . ARG A 79  ? 0.6677 0.8622 0.5196 0.1714  0.0164  -0.0257 79  ARG A CG  
637  C CD  . ARG A 79  ? 0.7102 0.9535 0.5543 0.1870  0.0090  -0.0255 79  ARG A CD  
638  N NE  . ARG A 79  ? 0.7933 1.0403 0.6172 0.2038  0.0116  -0.0127 79  ARG A NE  
639  C CZ  . ARG A 79  ? 0.8358 1.1199 0.6493 0.2072  0.0058  -0.0193 79  ARG A CZ  
640  N NH1 . ARG A 79  ? 0.8415 1.1635 0.6638 0.1937  -0.0025 -0.0407 79  ARG A NH1 
641  N NH2 . ARG A 79  ? 0.8678 1.1516 0.6612 0.2233  0.0096  -0.0051 79  ARG A NH2 
642  N N   . PRO A 80  ? 0.6075 0.7237 0.4414 0.1511  0.0341  -0.0255 80  PRO A N   
643  C CA  . PRO A 80  ? 0.6168 0.7294 0.4415 0.1482  0.0370  -0.0292 80  PRO A CA  
644  C C   . PRO A 80  ? 0.6738 0.8217 0.4894 0.1500  0.0306  -0.0389 80  PRO A C   
645  O O   . PRO A 80  ? 0.6565 0.8049 0.4696 0.1420  0.0311  -0.0500 80  PRO A O   
646  C CB  . PRO A 80  ? 0.6274 0.7213 0.4401 0.1594  0.0468  -0.0115 80  PRO A CB  
647  C CG  . PRO A 80  ? 0.6073 0.6821 0.4277 0.1625  0.0509  -0.0018 80  PRO A CG  
648  C CD  . PRO A 80  ? 0.6037 0.7010 0.4333 0.1631  0.0417  -0.0079 80  PRO A CD  
649  N N   . ALA A 81  ? 0.6865 0.8669 0.4970 0.1609  0.0248  -0.0359 81  ALA A N   
650  C CA  . ALA A 81  ? 0.7210 0.9422 0.5224 0.1627  0.0184  -0.0465 81  ALA A CA  
651  C C   . ALA A 81  ? 0.6986 0.9314 0.5121 0.1431  0.0137  -0.0709 81  ALA A C   
652  O O   . ALA A 81  ? 0.7017 0.9614 0.5092 0.1388  0.0107  -0.0848 81  ALA A O   
653  C CB  . ALA A 81  ? 0.7231 0.9827 0.5173 0.1804  0.0126  -0.0385 81  ALA A CB  
654  N N   . GLU A 82  ? 0.6865 0.8983 0.5158 0.1305  0.0142  -0.0766 82  GLU A N   
655  C CA  . GLU A 82  ? 0.7000 0.9165 0.5393 0.1112  0.0122  -0.0986 82  GLU A CA  
656  C C   . GLU A 82  ? 0.6606 0.8390 0.5025 0.1001  0.0185  -0.1046 82  GLU A C   
657  O O   . GLU A 82  ? 0.6244 0.7921 0.4748 0.0845  0.0198  -0.1194 82  GLU A O   
658  C CB  . GLU A 82  ? 0.7545 0.9758 0.6076 0.1045  0.0094  -0.1017 82  GLU A CB  
659  C CG  . GLU A 82  ? 0.7923 1.0593 0.6437 0.1165  0.0025  -0.0990 82  GLU A CG  
660  C CD  . GLU A 82  ? 0.8167 1.0801 0.6791 0.1191  0.0016  -0.0914 82  GLU A CD  
661  O OE1 . GLU A 82  ? 0.8408 1.0667 0.7116 0.1107  0.0062  -0.0883 82  GLU A OE1 
662  O OE2 . GLU A 82  ? 0.8397 1.1398 0.7023 0.1307  -0.0037 -0.0886 82  GLU A OE2 
663  N N   . ALA A 83  ? 0.6359 0.7949 0.4699 0.1082  0.0234  -0.0938 83  ALA A N   
664  C CA  . ALA A 83  ? 0.6469 0.7722 0.4845 0.1010  0.0292  -0.0977 83  ALA A CA  
665  C C   . ALA A 83  ? 0.6682 0.7991 0.5036 0.0908  0.0300  -0.1180 83  ALA A C   
666  O O   . ALA A 83  ? 0.6546 0.7599 0.4967 0.0809  0.0338  -0.1271 83  ALA A O   
667  C CB  . ALA A 83  ? 0.6641 0.7739 0.4944 0.1113  0.0348  -0.0833 83  ALA A CB  
668  N N   . ASP A 84  ? 0.6857 0.8493 0.5107 0.0936  0.0273  -0.1252 84  ASP A N   
669  C CA  . ASP A 84  ? 0.7247 0.8956 0.5478 0.0825  0.0290  -0.1474 84  ASP A CA  
670  C C   . ASP A 84  ? 0.7293 0.9007 0.5629 0.0658  0.0284  -0.1649 84  ASP A C   
671  O O   . ASP A 84  ? 0.7170 0.8648 0.5541 0.0538  0.0343  -0.1797 84  ASP A O   
672  C CB  . ASP A 84  ? 0.7387 0.9516 0.5482 0.0887  0.0256  -0.1525 84  ASP A CB  
673  C CG  . ASP A 84  ? 0.7551 0.9631 0.5521 0.1027  0.0290  -0.1369 84  ASP A CG  
674  O OD1 . ASP A 84  ? 0.7584 0.9315 0.5587 0.1034  0.0350  -0.1301 84  ASP A OD1 
675  O OD2 . ASP A 84  ? 0.7682 1.0089 0.5515 0.1131  0.0262  -0.1313 84  ASP A OD2 
676  N N   . LYS A 85  ? 0.7189 0.9149 0.5574 0.0650  0.0228  -0.1631 85  LYS A N   
677  C CA  . LYS A 85  ? 0.7313 0.9287 0.5801 0.0469  0.0236  -0.1800 85  LYS A CA  
678  C C   . LYS A 85  ? 0.7297 0.8776 0.5868 0.0403  0.0299  -0.1749 85  LYS A C   
679  O O   . LYS A 85  ? 0.7406 0.8690 0.6019 0.0243  0.0360  -0.1902 85  LYS A O   
680  C CB  . LYS A 85  ? 0.7509 0.9893 0.6041 0.0490  0.0161  -0.1785 85  LYS A CB  
681  N N   . LEU A 86  ? 0.6935 0.8201 0.5520 0.0526  0.0295  -0.1534 86  LEU A N   
682  C CA  . LEU A 86  ? 0.6934 0.7775 0.5583 0.0495  0.0348  -0.1466 86  LEU A CA  
683  C C   . LEU A 86  ? 0.6850 0.7389 0.5463 0.0463  0.0420  -0.1550 86  LEU A C   
684  O O   . LEU A 86  ? 0.6781 0.7026 0.5429 0.0370  0.0480  -0.1609 86  LEU A O   
685  C CB  . LEU A 86  ? 0.6956 0.7696 0.5617 0.0636  0.0333  -0.1247 86  LEU A CB  
686  C CG  . LEU A 86  ? 0.7301 0.7844 0.6054 0.0611  0.0342  -0.1157 86  LEU A CG  
687  C CD1 . LEU A 86  ? 0.7632 0.8294 0.6446 0.0477  0.0330  -0.1262 86  LEU A CD1 
688  C CD2 . LEU A 86  ? 0.7099 0.7706 0.5863 0.0735  0.0316  -0.0983 86  LEU A CD2 
689  N N   . VAL A 87  ? 0.6609 0.7207 0.5146 0.0551  0.0425  -0.1547 87  VAL A N   
690  C CA  . VAL A 87  ? 0.7012 0.7358 0.5517 0.0540  0.0495  -0.1639 87  VAL A CA  
691  C C   . VAL A 87  ? 0.7436 0.7735 0.5942 0.0377  0.0545  -0.1867 87  VAL A C   
692  O O   . VAL A 87  ? 0.7441 0.7372 0.5964 0.0322  0.0623  -0.1916 87  VAL A O   
693  C CB  . VAL A 87  ? 0.6996 0.7497 0.5414 0.0646  0.0490  -0.1622 87  VAL A CB  
694  C CG1 . VAL A 87  ? 0.6955 0.7303 0.5335 0.0614  0.0560  -0.1785 87  VAL A CG1 
695  C CG2 . VAL A 87  ? 0.6485 0.6894 0.4911 0.0777  0.0487  -0.1414 87  VAL A CG2 
696  N N   . LYS A 88  ? 0.7901 0.8575 0.6382 0.0298  0.0509  -0.2010 88  LYS A N   
697  C CA  . LYS A 88  ? 0.8710 0.9389 0.7196 0.0111  0.0569  -0.2266 88  LYS A CA  
698  C C   . LYS A 88  ? 0.8949 0.9321 0.7509 -0.0023 0.0629  -0.2287 88  LYS A C   
699  O O   . LYS A 88  ? 0.9345 0.9376 0.7896 -0.0133 0.0738  -0.2420 88  LYS A O   
700  C CB  . LYS A 88  ? 0.9020 1.0261 0.7487 0.0049  0.0502  -0.2407 88  LYS A CB  
701  C CG  . LYS A 88  ? 0.9361 1.0928 0.7723 0.0164  0.0459  -0.2417 88  LYS A CG  
702  C CD  . LYS A 88  ? 0.9470 1.1638 0.7800 0.0104  0.0395  -0.2580 88  LYS A CD  
703  C CE  . LYS A 88  ? 0.9683 1.2148 0.7886 0.0193  0.0376  -0.2631 88  LYS A CE  
704  N NZ  . LYS A 88  ? 0.9520 1.2072 0.7633 0.0421  0.0319  -0.2360 88  LYS A NZ  
705  N N   . LEU A 89  ? 0.8785 0.9239 0.7408 -0.0007 0.0574  -0.2149 89  LEU A N   
706  C CA  . LEU A 89  ? 0.8760 0.8988 0.7442 -0.0159 0.0636  -0.2189 89  LEU A CA  
707  C C   . LEU A 89  ? 0.8610 0.8306 0.7283 -0.0099 0.0707  -0.2046 89  LEU A C   
708  O O   . LEU A 89  ? 0.8812 0.8175 0.7481 -0.0227 0.0811  -0.2121 89  LEU A O   
709  C CB  . LEU A 89  ? 0.8874 0.9445 0.7631 -0.0180 0.0556  -0.2129 89  LEU A CB  
710  C CG  . LEU A 89  ? 0.9020 1.0152 0.7781 -0.0248 0.0496  -0.2304 89  LEU A CG  
711  C CD1 . LEU A 89  ? 0.8843 1.0365 0.7681 -0.0237 0.0412  -0.2246 89  LEU A CD1 
712  C CD2 . LEU A 89  ? 0.9193 1.0314 0.7954 -0.0482 0.0590  -0.2596 89  LEU A CD2 
713  N N   . LEU A 90  ? 0.8284 0.7897 0.6946 0.0092  0.0664  -0.1849 90  LEU A N   
714  C CA  . LEU A 90  ? 0.8539 0.7717 0.7189 0.0171  0.0724  -0.1724 90  LEU A CA  
715  C C   . LEU A 90  ? 0.9396 0.8246 0.7980 0.0173  0.0827  -0.1834 90  LEU A C   
716  O O   . LEU A 90  ? 0.9771 0.8210 0.8327 0.0173  0.0917  -0.1800 90  LEU A O   
717  C CB  . LEU A 90  ? 0.8047 0.7284 0.6712 0.0359  0.0658  -0.1524 90  LEU A CB  
718  C CG  . LEU A 90  ? 0.7618 0.6997 0.6347 0.0384  0.0593  -0.1375 90  LEU A CG  
719  C CD1 . LEU A 90  ? 0.7330 0.6865 0.6063 0.0537  0.0537  -0.1245 90  LEU A CD1 
720  C CD2 . LEU A 90  ? 0.7682 0.6743 0.6427 0.0369  0.0643  -0.1289 90  LEU A CD2 
721  N N   . ALA A 91  ? 0.9790 0.8809 0.8336 0.0196  0.0819  -0.1953 91  ALA A N   
722  C CA  . ALA A 91  ? 1.0461 0.9180 0.8946 0.0218  0.0919  -0.2065 91  ALA A CA  
723  C C   . ALA A 91  ? 1.1052 0.9472 0.9514 0.0031  0.1045  -0.2242 91  ALA A C   
724  O O   . ALA A 91  ? 1.1358 0.9309 0.9771 0.0065  0.1159  -0.2236 91  ALA A O   
725  C CB  . ALA A 91  ? 1.0412 0.9428 0.8860 0.0256  0.0887  -0.2179 91  ALA A CB  
726  N N   . LYS A 92  ? 1.2817 0.9559 0.9323 0.1329  0.1273  -0.2398 92  LYS A N   
727  C CA  . LYS A 92  ? 1.3202 0.9598 0.9612 0.1265  0.1176  -0.2479 92  LYS A CA  
728  C C   . LYS A 92  ? 1.2667 0.8970 0.9280 0.1242  0.1118  -0.2399 92  LYS A C   
729  O O   . LYS A 92  ? 1.3012 0.9022 0.9589 0.1223  0.1070  -0.2448 92  LYS A O   
730  C CB  . LYS A 92  ? 1.3816 1.0114 0.9997 0.1097  0.1058  -0.2553 92  LYS A CB  
731  C CG  . LYS A 92  ? 1.4546 1.0517 1.0638 0.0990  0.0945  -0.2640 92  LYS A CG  
732  C CD  . LYS A 92  ? 1.4652 1.0650 1.0727 0.0800  0.0800  -0.2626 92  LYS A CD  
733  C CE  . LYS A 92  ? 1.5115 1.0821 1.1120 0.0669  0.0686  -0.2717 92  LYS A CE  
734  N NZ  . LYS A 92  ? 1.5141 1.0917 1.1097 0.0481  0.0540  -0.2735 92  LYS A NZ  
735  N N   . GLY A 93  ? 1.1540 0.8074 0.8356 0.1243  0.1125  -0.2276 93  GLY A N   
736  C CA  . GLY A 93  ? 1.0786 0.7239 0.7786 0.1228  0.1075  -0.2194 93  GLY A CA  
737  C C   . GLY A 93  ? 1.0204 0.6423 0.7118 0.1046  0.0941  -0.2225 93  GLY A C   
738  O O   . GLY A 93  ? 1.0023 0.6258 0.6798 0.0911  0.0867  -0.2273 93  GLY A O   
739  N N   . GLU A 94  ? 1.0033 0.6043 0.7038 0.1040  0.0908  -0.2194 94  GLU A N   
740  C CA  . GLU A 94  ? 1.0043 0.5823 0.7004 0.0862  0.0793  -0.2216 94  GLU A CA  
741  C C   . GLU A 94  ? 1.0106 0.6059 0.7138 0.0713  0.0715  -0.2155 94  GLU A C   
742  O O   . GLU A 94  ? 1.0140 0.5980 0.7123 0.0536  0.0610  -0.2193 94  GLU A O   
743  C CB  . GLU A 94  ? 1.0040 0.5597 0.6774 0.0778  0.0745  -0.2362 94  GLU A CB  
744  C CG  . GLU A 94  ? 1.0033 0.5421 0.6666 0.0931  0.0830  -0.2437 94  GLU A CG  
745  C CD  . GLU A 94  ? 1.0231 0.5389 0.6630 0.0847  0.0782  -0.2586 94  GLU A CD  
746  O OE1 . GLU A 94  ? 1.0130 0.5357 0.6428 0.0702  0.0697  -0.2640 94  GLU A OE1 
747  O OE2 . GLU A 94  ? 1.0501 0.5410 0.6815 0.0928  0.0824  -0.2652 94  GLU A OE2 
748  N N   . TYR A 95  ? 1.0357 0.6591 0.7515 0.0779  0.0763  -0.2061 95  TYR A N   
749  C CA  . TYR A 95  ? 1.0408 0.6816 0.7637 0.0661  0.0703  -0.1995 95  TYR A CA  
750  C C   . TYR A 95  ? 1.0365 0.6793 0.7840 0.0623  0.0669  -0.1872 95  TYR A C   
751  O O   . TYR A 95  ? 1.0696 0.6984 0.8231 0.0742  0.0728  -0.1840 95  TYR A O   
752  C CB  . TYR A 95  ? 1.0344 0.7127 0.7659 0.0737  0.0764  -0.1922 95  TYR A CB  
753  C CG  . TYR A 95  ? 1.0319 0.7188 0.7754 0.0933  0.0890  -0.1874 95  TYR A CG  
754  C CD1 . TYR A 95  ? 1.0088 0.7074 0.7789 0.0973  0.0890  -0.1751 95  TYR A CD1 
755  C CD2 . TYR A 95  ? 1.0585 0.7491 0.7931 0.1063  0.0988  -0.1935 95  TYR A CD2 
756  C CE1 . TYR A 95  ? 1.0093 0.7178 0.7918 0.1153  0.0989  -0.1712 95  TYR A CE1 
757  C CE2 . TYR A 95  ? 1.0654 0.7703 0.8170 0.1232  0.1089  -0.1886 95  TYR A CE2 
758  C CZ  . TYR A 95  ? 1.0429 0.7555 0.8172 0.1282  0.1088  -0.1780 95  TYR A CZ  
759  O OH  . TYR A 95  ? 1.0456 0.7753 0.8386 0.1447  0.1169  -0.1732 95  TYR A OH  
760  N N   . GLN A 96  ? 0.9910 0.6529 0.7528 0.0466  0.0574  -0.1799 96  GLN A N   
761  C CA  . GLN A 96  ? 0.9499 0.6172 0.7347 0.0422  0.0544  -0.1676 96  GLN A CA  
762  C C   . GLN A 96  ? 0.8869 0.5882 0.6937 0.0521  0.0589  -0.1543 96  GLN A C   
763  O O   . GLN A 96  ? 0.8779 0.6040 0.6853 0.0560  0.0617  -0.1532 96  GLN A O   
764  C CB  . GLN A 96  ? 0.9684 0.6417 0.7597 0.0213  0.0429  -0.1662 96  GLN A CB  
765  C CG  . GLN A 96  ? 1.0477 0.6888 0.8207 0.0081  0.0372  -0.1794 96  GLN A CG  
766  C CD  . GLN A 96  ? 1.0644 0.7197 0.8467 -0.0125 0.0255  -0.1788 96  GLN A CD  
767  O OE1 . GLN A 96  ? 1.0340 0.7229 0.8285 -0.0153 0.0211  -0.1722 96  GLN A OE1 
768  N NE2 . GLN A 96  ? 1.1142 0.7441 0.8914 -0.0269 0.0208  -0.1857 96  GLN A NE2 
769  N N   . LYS A 97  ? 0.8377 0.5383 0.6611 0.0558  0.0598  -0.1444 97  LYS A N   
770  C CA  . LYS A 97  ? 0.7730 0.5037 0.6184 0.0635  0.0624  -0.1318 97  LYS A CA  
771  C C   . LYS A 97  ? 0.7067 0.4525 0.5685 0.0497  0.0546  -0.1218 97  LYS A C   
772  O O   . LYS A 97  ? 0.6993 0.4274 0.5589 0.0380  0.0493  -0.1226 97  LYS A O   
773  C CB  . LYS A 97  ? 0.7935 0.5136 0.6445 0.0807  0.0689  -0.1281 97  LYS A CB  
774  C CG  . LYS A 97  ? 0.8436 0.5521 0.6809 0.0979  0.0782  -0.1377 97  LYS A CG  
775  C CD  . LYS A 97  ? 0.8763 0.5664 0.7156 0.1158  0.0832  -0.1356 97  LYS A CD  
776  C CE  . LYS A 97  ? 0.8581 0.5776 0.7228 0.1247  0.0835  -0.1225 97  LYS A CE  
777  N NZ  . LYS A 97  ? 0.8796 0.5850 0.7469 0.1446  0.0874  -0.1200 97  LYS A NZ  
778  N N   . VAL A 98  ? 0.6427 0.4212 0.5203 0.0505  0.0543  -0.1130 98  VAL A N   
779  C CA  . VAL A 98  ? 0.6363 0.4319 0.5307 0.0408  0.0484  -0.1027 98  VAL A CA  
780  C C   . VAL A 98  ? 0.6005 0.4127 0.5116 0.0515  0.0520  -0.0925 98  VAL A C   
781  O O   . VAL A 98  ? 0.5903 0.4172 0.5045 0.0623  0.0578  -0.0926 98  VAL A O   
782  C CB  . VAL A 98  ? 0.6538 0.4720 0.5492 0.0308  0.0434  -0.1022 98  VAL A CB  
783  C CG1 . VAL A 98  ? 0.6291 0.4687 0.5428 0.0249  0.0392  -0.0910 98  VAL A CG1 
784  C CG2 . VAL A 98  ? 0.7050 0.5089 0.5864 0.0186  0.0370  -0.1116 98  VAL A CG2 
785  N N   . SER A 99  ? 0.5657 0.3765 0.4875 0.0483  0.0488  -0.0841 99  SER A N   
786  C CA  . SER A 99  ? 0.5470 0.3705 0.4829 0.0584  0.0507  -0.0750 99  SER A CA  
787  C C   . SER A 99  ? 0.4785 0.3252 0.4285 0.0502  0.0462  -0.0659 99  SER A C   
788  O O   . SER A 99  ? 0.4499 0.2924 0.4002 0.0380  0.0416  -0.0640 99  SER A O   
789  C CB  . SER A 99  ? 0.6254 0.4228 0.5577 0.0649  0.0515  -0.0724 99  SER A CB  
790  O OG  . SER A 99  ? 0.6728 0.4497 0.5928 0.0764  0.0565  -0.0804 99  SER A OG  
791  N N   . TYR A 100 ? 0.4759 0.3473 0.4381 0.0566  0.0478  -0.0607 100 TYR A N   
792  C CA  . TYR A 100 ? 0.4274 0.3193 0.4023 0.0508  0.0440  -0.0522 100 TYR A CA  
793  C C   . TYR A 100 ? 0.4154 0.3120 0.4005 0.0596  0.0437  -0.0448 100 TYR A C   
794  O O   . TYR A 100 ? 0.3886 0.2845 0.3753 0.0722  0.0471  -0.0463 100 TYR A O   
795  C CB  . TYR A 100 ? 0.4358 0.3522 0.4154 0.0490  0.0454  -0.0521 100 TYR A CB  
796  C CG  . TYR A 100 ? 0.4686 0.3857 0.4390 0.0392  0.0434  -0.0563 100 TYR A CG  
797  C CD1 . TYR A 100 ? 0.5114 0.4110 0.4719 0.0317  0.0397  -0.0611 100 TYR A CD1 
798  C CD2 . TYR A 100 ? 0.4744 0.4099 0.4459 0.0371  0.0446  -0.0550 100 TYR A CD2 
799  C CE1 . TYR A 100 ? 0.5225 0.4253 0.4749 0.0235  0.0363  -0.0652 100 TYR A CE1 
800  C CE2 . TYR A 100 ? 0.4942 0.4300 0.4552 0.0298  0.0420  -0.0582 100 TYR A CE2 
801  C CZ  . TYR A 100 ? 0.5231 0.4439 0.4751 0.0235  0.0372  -0.0633 100 TYR A CZ  
802  O OH  . TYR A 100 ? 0.5520 0.4754 0.4942 0.0170  0.0331  -0.0666 100 TYR A OH  
803  N N   . PRO A 101 ? 0.4169 0.3179 0.4081 0.0541  0.0396  -0.0373 101 PRO A N   
804  C CA  . PRO A 101 ? 0.4065 0.3115 0.4049 0.0626  0.0382  -0.0304 101 PRO A CA  
805  C C   . PRO A 101 ? 0.3937 0.3265 0.4049 0.0680  0.0386  -0.0288 101 PRO A C   
806  O O   . PRO A 101 ? 0.3556 0.3046 0.3704 0.0621  0.0397  -0.0306 101 PRO A O   
807  C CB  . PRO A 101 ? 0.4184 0.3207 0.4172 0.0532  0.0344  -0.0239 101 PRO A CB  
808  C CG  . PRO A 101 ? 0.3908 0.2836 0.3833 0.0407  0.0340  -0.0278 101 PRO A CG  
809  C CD  . PRO A 101 ? 0.3892 0.2907 0.3799 0.0407  0.0360  -0.0353 101 PRO A CD  
810  N N   . LEU A 102 ? 0.3393 0.2774 0.3571 0.0788  0.0372  -0.0249 102 LEU A N   
811  C CA  . LEU A 102 ? 0.3345 0.3005 0.3669 0.0840  0.0372  -0.0241 102 LEU A CA  
812  C C   . LEU A 102 ? 0.3484 0.3227 0.3869 0.0847  0.0311  -0.0168 102 LEU A C   
813  O O   . LEU A 102 ? 0.3419 0.2989 0.3722 0.0842  0.0280  -0.0123 102 LEU A O   
814  C CB  . LEU A 102 ? 0.3280 0.2984 0.3651 0.0988  0.0410  -0.0281 102 LEU A CB  
815  C CG  . LEU A 102 ? 0.3233 0.2858 0.3525 0.0992  0.0479  -0.0363 102 LEU A CG  
816  C CD1 . LEU A 102 ? 0.3453 0.3098 0.3785 0.1158  0.0519  -0.0400 102 LEU A CD1 
817  C CD2 . LEU A 102 ? 0.3612 0.3435 0.3945 0.0892  0.0512  -0.0385 102 LEU A CD2 
818  N N   . LEU A 103 ? 0.3505 0.3509 0.4023 0.0845  0.0296  -0.0159 103 LEU A N   
819  C CA  . LEU A 103 ? 0.3364 0.3460 0.3931 0.0847  0.0230  -0.0102 103 LEU A CA  
820  C C   . LEU A 103 ? 0.3369 0.3620 0.4049 0.0984  0.0203  -0.0100 103 LEU A C   
821  O O   . LEU A 103 ? 0.3433 0.3894 0.4243 0.1017  0.0235  -0.0142 103 LEU A O   
822  C CB  . LEU A 103 ? 0.3043 0.3313 0.3673 0.0729  0.0219  -0.0095 103 LEU A CB  
823  C CG  . LEU A 103 ? 0.3116 0.3497 0.3794 0.0725  0.0150  -0.0051 103 LEU A CG  
824  C CD1 . LEU A 103 ? 0.2710 0.2890 0.3255 0.0711  0.0115  0.0002  103 LEU A CD1 
825  C CD2 . LEU A 103 ? 0.3130 0.3683 0.3878 0.0615  0.0151  -0.0062 103 LEU A CD2 
826  N N   . LYS A 104 ? 0.3507 0.3673 0.4140 0.1064  0.0143  -0.0049 104 LYS A N   
827  C CA  . LYS A 104 ? 0.3310 0.3645 0.4053 0.1203  0.0095  -0.0041 104 LYS A CA  
828  C C   . LYS A 104 ? 0.3475 0.4023 0.4301 0.1152  0.0021  -0.0014 104 LYS A C   
829  O O   . LYS A 104 ? 0.3238 0.3673 0.3956 0.1082  -0.0016 0.0030  104 LYS A O   
830  C CB  . LYS A 104 ? 0.2969 0.3067 0.3587 0.1345  0.0067  0.0001  104 LYS A CB  
831  C CG  . LYS A 104 ? 0.3078 0.3362 0.3805 0.1508  0.0000  0.0014  104 LYS A CG  
832  C CD  . LYS A 104 ? 0.3679 0.3682 0.4247 0.1660  -0.0026 0.0065  104 LYS A CD  
833  C CE  . LYS A 104 ? 0.4187 0.4387 0.4870 0.1850  -0.0094 0.0073  104 LYS A CE  
834  N NZ  . LYS A 104 ? 0.4916 0.4799 0.5415 0.2012  -0.0114 0.0127  104 LYS A NZ  
835  N N   . THR A 105 ? 0.3362 0.4223 0.4381 0.1175  0.0006  -0.0048 105 THR A N   
836  C CA  . THR A 105 ? 0.3315 0.4396 0.4428 0.1123  -0.0071 -0.0038 105 THR A CA  
837  C C   . THR A 105 ? 0.3144 0.4415 0.4375 0.1278  -0.0147 -0.0035 105 THR A C   
838  O O   . THR A 105 ? 0.3547 0.4982 0.4923 0.1375  -0.0115 -0.0073 105 THR A O   
839  C CB  . THR A 105 ? 0.3685 0.4992 0.4939 0.0987  -0.0029 -0.0083 105 THR A CB  
840  O OG1 . THR A 105 ? 0.3705 0.4827 0.4835 0.0862  0.0033  -0.0082 105 THR A OG1 
841  C CG2 . THR A 105 ? 0.3617 0.5130 0.4960 0.0921  -0.0112 -0.0081 105 THR A CG2 
842  N N   . THR A 106 ? 0.3300 0.4552 0.4462 0.1313  -0.0248 0.0010  106 THR A N   
843  C CA  . THR A 106 ? 0.3332 0.4794 0.4605 0.1461  -0.0343 0.0015  106 THR A CA  
844  C C   . THR A 106 ? 0.3331 0.5066 0.4719 0.1371  -0.0431 -0.0004 106 THR A C   
845  O O   . THR A 106 ? 0.3505 0.5119 0.4756 0.1266  -0.0463 0.0020  106 THR A O   
846  C CB  . THR A 106 ? 0.3657 0.4856 0.4727 0.1607  -0.0402 0.0085  106 THR A CB  
847  O OG1 . THR A 106 ? 0.4039 0.4961 0.4998 0.1678  -0.0316 0.0095  106 THR A OG1 
848  C CG2 . THR A 106 ? 0.3507 0.4941 0.4694 0.1783  -0.0512 0.0090  106 THR A CG2 
849  N N   . VAL A 107 ? 0.3365 0.5469 0.5006 0.1411  -0.0467 -0.0052 107 VAL A N   
850  C CA  . VAL A 107 ? 0.3473 0.5866 0.5250 0.1323  -0.0561 -0.0082 107 VAL A CA  
851  C C   . VAL A 107 ? 0.3524 0.6111 0.5377 0.1497  -0.0695 -0.0071 107 VAL A C   
852  O O   . VAL A 107 ? 0.3331 0.6134 0.5370 0.1638  -0.0694 -0.0094 107 VAL A O   
853  C CB  . VAL A 107 ? 0.3452 0.6157 0.5486 0.1191  -0.0495 -0.0152 107 VAL A CB  
854  C CG1 . VAL A 107 ? 0.3163 0.6111 0.5307 0.1065  -0.0589 -0.0187 107 VAL A CG1 
855  C CG2 . VAL A 107 ? 0.3454 0.5952 0.5394 0.1049  -0.0358 -0.0157 107 VAL A CG2 
856  N N   . LYS A 108 ? 0.3381 0.5901 0.5088 0.1496  -0.0812 -0.0040 108 LYS A N   
857  C CA  . LYS A 108 ? 0.3687 0.6390 0.5438 0.1656  -0.0961 -0.0027 108 LYS A CA  
858  C C   . LYS A 108 ? 0.3866 0.6940 0.5811 0.1542  -0.1064 -0.0091 108 LYS A C   
859  O O   . LYS A 108 ? 0.3776 0.6800 0.5665 0.1348  -0.1051 -0.0116 108 LYS A O   
860  C CB  . LYS A 108 ? 0.4053 0.6406 0.5472 0.1752  -0.1027 0.0058  108 LYS A CB  
861  C CG  . LYS A 108 ? 0.4212 0.6168 0.5429 0.1837  -0.0921 0.0120  108 LYS A CG  
862  C CD  . LYS A 108 ? 0.4683 0.6289 0.5569 0.1926  -0.0974 0.0212  108 LYS A CD  
863  C CE  . LYS A 108 ? 0.5043 0.6498 0.5853 0.2159  -0.0985 0.0267  108 LYS A CE  
864  N NZ  . LYS A 108 ? 0.5517 0.6755 0.6052 0.2287  -0.1086 0.0354  108 LYS A NZ  
865  N N   . TYR A 109 ? 0.3982 0.7425 0.6155 0.1665  -0.1168 -0.0122 109 TYR A N   
866  C CA  . TYR A 109 ? 0.4486 0.8315 0.6881 0.1554  -0.1268 -0.0190 109 TYR A CA  
867  C C   . TYR A 109 ? 0.5237 0.9071 0.7513 0.1644  -0.1434 -0.0161 109 TYR A C   
868  O O   . TYR A 109 ? 0.5723 0.9308 0.7780 0.1817  -0.1469 -0.0085 109 TYR A O   
869  C CB  . TYR A 109 ? 0.4316 0.8491 0.7056 0.1534  -0.1199 -0.0243 109 TYR A CB  
870  C CG  . TYR A 109 ? 0.4192 0.8364 0.7037 0.1450  -0.1025 -0.0272 109 TYR A CG  
871  C CD1 . TYR A 109 ? 0.3906 0.8182 0.6846 0.1222  -0.0968 -0.0325 109 TYR A CD1 
872  C CD2 . TYR A 109 ? 0.4405 0.8425 0.7222 0.1590  -0.0912 -0.0243 109 TYR A CD2 
873  C CE1 . TYR A 109 ? 0.4200 0.8398 0.7177 0.1125  -0.0795 -0.0336 109 TYR A CE1 
874  C CE2 . TYR A 109 ? 0.4471 0.8479 0.7359 0.1516  -0.0755 -0.0271 109 TYR A CE2 
875  C CZ  . TYR A 109 ? 0.4497 0.8567 0.7446 0.1272  -0.0691 -0.0310 109 TYR A CZ  
876  O OH  . TYR A 109 ? 0.4361 0.8347 0.7323 0.1174  -0.0525 -0.0324 109 TYR A OH  
877  N N   . GLY A 110 ? 0.4923 0.9036 0.7341 0.1514  -0.1532 -0.0222 110 GLY A N   
878  C CA  . GLY A 110 ? 0.4798 0.9031 0.7202 0.1596  -0.1686 -0.0213 110 GLY A CA  
879  C C   . GLY A 110 ? 0.4683 0.9118 0.7300 0.1748  -0.1677 -0.0203 110 GLY A C   
880  O O   . GLY A 110 ? 0.4465 0.8969 0.7256 0.1776  -0.1548 -0.0213 110 GLY A O   
881  N N   . ILE A 111 ? 0.4725 0.9260 0.7323 0.1852  -0.1819 -0.0185 111 ILE A N   
882  C CA  . ILE A 111 ? 0.4903 0.9562 0.7637 0.2041  -0.1823 -0.0159 111 ILE A CA  
883  C C   . ILE A 111 ? 0.4946 1.0033 0.8097 0.1963  -0.1765 -0.0234 111 ILE A C   
884  O O   . ILE A 111 ? 0.4940 1.0304 0.8284 0.1775  -0.1800 -0.0304 111 ILE A O   
885  C CB  . ILE A 111 ? 0.5334 0.9999 0.7933 0.2170  -0.1998 -0.0121 111 ILE A CB  
886  C CG1 . ILE A 111 ? 0.5551 0.9741 0.7739 0.2321  -0.2001 -0.0020 111 ILE A CG1 
887  C CG2 . ILE A 111 ? 0.5414 1.0415 0.8295 0.2293  -0.2043 -0.0137 111 ILE A CG2 
888  C CD1 . ILE A 111 ? 0.5320 0.9181 0.7386 0.2353  -0.1832 0.0020  111 ILE A CD1 
889  N N   . GLY A 112 ? 0.4884 1.0004 0.8163 0.2101  -0.1666 -0.0220 112 GLY A N   
890  C CA  . GLY A 112 ? 0.4813 1.0299 0.8464 0.2046  -0.1577 -0.0281 112 GLY A CA  
891  C C   . GLY A 112 ? 0.4573 0.9933 0.8250 0.2001  -0.1381 -0.0291 112 GLY A C   
892  O O   . GLY A 112 ? 0.4352 0.9898 0.8255 0.2048  -0.1280 -0.0316 112 GLY A O   
893  N N   . LYS A 113 ? 0.4753 0.9805 0.8197 0.1914  -0.1328 -0.0274 113 LYS A N   
894  C CA  . LYS A 113 ? 0.4950 0.9815 0.8352 0.1892  -0.1153 -0.0273 113 LYS A CA  
895  C C   . LYS A 113 ? 0.5379 0.9790 0.8447 0.2053  -0.1139 -0.0198 113 LYS A C   
896  O O   . LYS A 113 ? 0.5248 0.9413 0.8055 0.2046  -0.1219 -0.0155 113 LYS A O   
897  C CB  . LYS A 113 ? 0.4634 0.9511 0.8051 0.1651  -0.1091 -0.0315 113 LYS A CB  
898  C CG  . LYS A 113 ? 0.4495 0.9763 0.8233 0.1464  -0.1052 -0.0388 113 LYS A CG  
899  C CD  . LYS A 113 ? 0.4455 0.9794 0.8174 0.1264  -0.1153 -0.0422 113 LYS A CD  
900  C CE  . LYS A 113 ? 0.4238 0.9795 0.8177 0.1020  -0.1054 -0.0486 113 LYS A CE  
901  N NZ  . LYS A 113 ? 0.3882 0.9198 0.7674 0.0898  -0.0933 -0.0485 113 LYS A NZ  
902  N N   . LYS A 114 ? 0.6148 1.0438 0.9213 0.2192  -0.1034 -0.0182 114 LYS A N   
903  C CA  . LYS A 114 ? 0.6656 1.0488 0.9413 0.2317  -0.0988 -0.0118 114 LYS A CA  
904  C C   . LYS A 114 ? 0.6585 1.0200 0.9216 0.2183  -0.0883 -0.0125 114 LYS A C   
905  O O   . LYS A 114 ? 0.6434 1.0251 0.9245 0.2031  -0.0797 -0.0183 114 LYS A O   
906  C CB  . LYS A 114 ? 0.7223 1.1003 1.0032 0.2493  -0.0905 -0.0115 114 LYS A CB  
907  C CG  . LYS A 114 ? 0.7698 1.1005 1.0223 0.2594  -0.0820 -0.0068 114 LYS A CG  
908  C CD  . LYS A 114 ? 0.7840 1.1161 1.0482 0.2622  -0.0662 -0.0116 114 LYS A CD  
909  C CE  . LYS A 114 ? 0.8161 1.1118 1.0602 0.2812  -0.0622 -0.0077 114 LYS A CE  
910  N NZ  . LYS A 114 ? 0.8108 1.0997 1.0593 0.2821  -0.0461 -0.0128 114 LYS A NZ  
911  N N   . GLU A 115 ? 0.5954 0.9152 0.8269 0.2238  -0.0885 -0.0061 115 GLU A N   
912  C CA  . GLU A 115 ? 0.5538 0.8513 0.7722 0.2131  -0.0790 -0.0062 115 GLU A CA  
913  C C   . GLU A 115 ? 0.4992 0.7975 0.7287 0.2125  -0.0629 -0.0107 115 GLU A C   
914  O O   . GLU A 115 ? 0.4955 0.7972 0.7332 0.2246  -0.0583 -0.0118 115 GLU A O   
915  C CB  . GLU A 115 ? 0.5910 0.8418 0.7737 0.2205  -0.0810 0.0021  115 GLU A CB  
916  C CG  . GLU A 115 ? 0.6410 0.8570 0.8085 0.2321  -0.0704 0.0050  115 GLU A CG  
917  C CD  . GLU A 115 ? 0.7043 0.8729 0.8362 0.2364  -0.0718 0.0137  115 GLU A CD  
918  O OE1 . GLU A 115 ? 0.7321 0.8671 0.8487 0.2405  -0.0620 0.0157  115 GLU A OE1 
919  O OE2 . GLU A 115 ? 0.7160 0.8800 0.8343 0.2346  -0.0822 0.0185  115 GLU A OE2 
920  N N   . ALA A 116 ? 0.4400 0.7317 0.6668 0.1961  -0.0537 -0.0131 116 ALA A N   
921  C CA  . ALA A 116 ? 0.4076 0.6971 0.6407 0.1919  -0.0379 -0.0174 116 ALA A CA  
922  C C   . ALA A 116 ? 0.3774 0.6218 0.5816 0.1814  -0.0300 -0.0140 116 ALA A C   
923  O O   . ALA A 116 ? 0.3230 0.5520 0.5125 0.1677  -0.0339 -0.0108 116 ALA A O   
924  C CB  . ALA A 116 ? 0.4013 0.7277 0.6603 0.1747  -0.0322 -0.0240 116 ALA A CB  
925  N N   . THR A 117 ? 0.3916 0.6157 0.5878 0.1878  -0.0192 -0.0153 117 THR A N   
926  C CA  . THR A 117 ? 0.4064 0.5920 0.5785 0.1767  -0.0115 -0.0135 117 THR A CA  
927  C C   . THR A 117 ? 0.3888 0.5813 0.5682 0.1664  0.0017  -0.0195 117 THR A C   
928  O O   . THR A 117 ? 0.3484 0.5653 0.5463 0.1741  0.0075  -0.0246 117 THR A O   
929  C CB  . THR A 117 ? 0.4762 0.6231 0.6257 0.1913  -0.0110 -0.0095 117 THR A CB  
930  O OG1 . THR A 117 ? 0.5135 0.6663 0.6719 0.2086  -0.0054 -0.0136 117 THR A OG1 
931  C CG2 . THR A 117 ? 0.4805 0.6189 0.6198 0.2018  -0.0237 -0.0024 117 THR A CG2 
932  N N   . TYR A 118 ? 0.3796 0.5516 0.5442 0.1494  0.0063  -0.0186 118 TYR A N   
933  C CA  . TYR A 118 ? 0.3409 0.5143 0.5066 0.1378  0.0179  -0.0232 118 TYR A CA  
934  C C   . TYR A 118 ? 0.3561 0.4909 0.4966 0.1317  0.0218  -0.0216 118 TYR A C   
935  O O   . TYR A 118 ? 0.3583 0.4724 0.4843 0.1268  0.0161  -0.0167 118 TYR A O   
936  C CB  . TYR A 118 ? 0.3307 0.5257 0.5071 0.1190  0.0183  -0.0241 118 TYR A CB  
937  C CG  . TYR A 118 ? 0.3570 0.5911 0.5589 0.1202  0.0128  -0.0258 118 TYR A CG  
938  C CD1 . TYR A 118 ? 0.3789 0.6451 0.6034 0.1217  0.0202  -0.0310 118 TYR A CD1 
939  C CD2 . TYR A 118 ? 0.3926 0.6326 0.5959 0.1197  0.0002  -0.0226 118 TYR A CD2 
940  C CE1 . TYR A 118 ? 0.4033 0.7084 0.6539 0.1219  0.0149  -0.0331 118 TYR A CE1 
941  C CE2 . TYR A 118 ? 0.3901 0.6677 0.6176 0.1204  -0.0063 -0.0251 118 TYR A CE2 
942  C CZ  . TYR A 118 ? 0.4122 0.7232 0.6645 0.1209  0.0009  -0.0304 118 TYR A CZ  
943  O OH  . TYR A 118 ? 0.4512 0.8029 0.7304 0.1204  -0.0056 -0.0335 118 TYR A OH  
944  N N   . LEU A 119 ? 0.3194 0.4464 0.4553 0.1308  0.0318  -0.0261 119 LEU A N   
945  C CA  . LEU A 119 ? 0.3383 0.4321 0.4521 0.1237  0.0352  -0.0259 119 LEU A CA  
946  C C   . LEU A 119 ? 0.3178 0.4179 0.4307 0.1069  0.0405  -0.0276 119 LEU A C   
947  O O   . LEU A 119 ? 0.3453 0.4682 0.4704 0.1047  0.0469  -0.0312 119 LEU A O   
948  C CB  . LEU A 119 ? 0.4326 0.5081 0.5374 0.1360  0.0416  -0.0304 119 LEU A CB  
949  C CG  . LEU A 119 ? 0.4814 0.5174 0.5636 0.1378  0.0417  -0.0300 119 LEU A CG  
950  C CD1 . LEU A 119 ? 0.4648 0.4842 0.5392 0.1402  0.0332  -0.0229 119 LEU A CD1 
951  C CD2 . LEU A 119 ? 0.5177 0.5438 0.5967 0.1543  0.0477  -0.0355 119 LEU A CD2 
952  N N   . ALA A 120 ? 0.2961 0.3770 0.3946 0.0954  0.0382  -0.0247 120 ALA A N   
953  C CA  . ALA A 120 ? 0.3149 0.3989 0.4101 0.0810  0.0423  -0.0256 120 ALA A CA  
954  C C   . ALA A 120 ? 0.3338 0.3921 0.4104 0.0770  0.0454  -0.0275 120 ALA A C   
955  O O   . ALA A 120 ? 0.3171 0.3531 0.3827 0.0786  0.0417  -0.0259 120 ALA A O   
956  C CB  . ALA A 120 ? 0.2892 0.3787 0.3864 0.0700  0.0361  -0.0210 120 ALA A CB  
957  N N   . LEU A 121 ? 0.3180 0.3794 0.3904 0.0711  0.0522  -0.0311 121 LEU A N   
958  C CA  . LEU A 121 ? 0.2867 0.3273 0.3415 0.0653  0.0538  -0.0332 121 LEU A CA  
959  C C   . LEU A 121 ? 0.2892 0.3284 0.3388 0.0524  0.0506  -0.0295 121 LEU A C   
960  O O   . LEU A 121 ? 0.3316 0.3537 0.3691 0.0477  0.0477  -0.0294 121 LEU A O   
961  C CB  . LEU A 121 ? 0.3098 0.3529 0.3594 0.0677  0.0629  -0.0394 121 LEU A CB  
962  C CG  . LEU A 121 ? 0.3348 0.3591 0.3649 0.0616  0.0641  -0.0427 121 LEU A CG  
963  C CD1 . LEU A 121 ? 0.3525 0.3522 0.3728 0.0638  0.0590  -0.0440 121 LEU A CD1 
964  C CD2 . LEU A 121 ? 0.3001 0.3275 0.3235 0.0656  0.0736  -0.0490 121 LEU A CD2 
965  N N   . ASN A 122 ? 0.2694 0.3261 0.3278 0.0465  0.0512  -0.0268 122 ASN A N   
966  C CA  . ASN A 122 ? 0.2213 0.2747 0.2743 0.0360  0.0479  -0.0229 122 ASN A CA  
967  C C   . ASN A 122 ? 0.2394 0.2951 0.2992 0.0349  0.0407  -0.0184 122 ASN A C   
968  O O   . ASN A 122 ? 0.2591 0.3017 0.3118 0.0326  0.0360  -0.0159 122 ASN A O   
969  C CB  . ASN A 122 ? 0.2272 0.2928 0.2817 0.0287  0.0531  -0.0224 122 ASN A CB  
970  C CG  . ASN A 122 ? 0.2635 0.3197 0.3023 0.0258  0.0582  -0.0246 122 ASN A CG  
971  O OD1 . ASN A 122 ? 0.3117 0.3529 0.3390 0.0280  0.0564  -0.0270 122 ASN A OD1 
972  N ND2 . ASN A 122 ? 0.2660 0.3306 0.3036 0.0200  0.0644  -0.0236 122 ASN A ND2 
973  N N   . GLU A 123 ? 0.2479 0.3213 0.3212 0.0357  0.0399  -0.0175 123 GLU A N   
974  C CA  . GLU A 123 ? 0.2259 0.3008 0.3028 0.0339  0.0326  -0.0138 123 GLU A CA  
975  C C   . GLU A 123 ? 0.2234 0.3201 0.3168 0.0371  0.0308  -0.0145 123 GLU A C   
976  O O   . GLU A 123 ? 0.2081 0.3214 0.3122 0.0383  0.0361  -0.0174 123 GLU A O   
977  C CB  . GLU A 123 ? 0.2130 0.2835 0.2835 0.0233  0.0312  -0.0111 123 GLU A CB  
978  C CG  . GLU A 123 ? 0.2212 0.3066 0.2989 0.0158  0.0349  -0.0118 123 GLU A CG  
979  C CD  . GLU A 123 ? 0.2533 0.3385 0.3259 0.0134  0.0434  -0.0138 123 GLU A CD  
980  O OE1 . GLU A 123 ? 0.2769 0.3780 0.3594 0.0138  0.0494  -0.0162 123 GLU A OE1 
981  O OE2 . GLU A 123 ? 0.2889 0.3586 0.3472 0.0114  0.0439  -0.0129 123 GLU A OE2 
982  N N   . SER A 124 ? 0.2457 0.3436 0.3412 0.0381  0.0232  -0.0118 124 SER A N   
983  C CA  . SER A 124 ? 0.2596 0.3796 0.3703 0.0385  0.0191  -0.0126 124 SER A CA  
984  C C   . SER A 124 ? 0.2581 0.3762 0.3649 0.0281  0.0145  -0.0108 124 SER A C   
985  O O   . SER A 124 ? 0.2653 0.3654 0.3587 0.0270  0.0115  -0.0079 124 SER A O   
986  C CB  . SER A 124 ? 0.2877 0.4104 0.4024 0.0513  0.0127  -0.0116 124 SER A CB  
987  O OG  . SER A 124 ? 0.2815 0.4280 0.4115 0.0520  0.0070  -0.0128 124 SER A OG  
988  N N   . THR A 125 ? 0.2392 0.3749 0.3571 0.0200  0.0147  -0.0127 125 THR A N   
989  C CA  . THR A 125 ? 0.2395 0.3705 0.3519 0.0102  0.0101  -0.0118 125 THR A CA  
990  C C   . THR A 125 ? 0.2295 0.3819 0.3560 0.0089  0.0030  -0.0142 125 THR A C   
991  O O   . THR A 125 ? 0.2298 0.4048 0.3736 0.0136  0.0028  -0.0167 125 THR A O   
992  C CB  . THR A 125 ? 0.2583 0.3834 0.3655 -0.0021 0.0167  -0.0119 125 THR A CB  
993  O OG1 . THR A 125 ? 0.2831 0.4297 0.4061 -0.0083 0.0210  -0.0148 125 THR A OG1 
994  C CG2 . THR A 125 ? 0.2839 0.3919 0.3783 -0.0002 0.0233  -0.0102 125 THR A CG2 
995  N N   . VAL A 126 ? 0.2554 0.4009 0.3744 0.0032  -0.0035 -0.0138 126 VAL A N   
996  C CA  . VAL A 126 ? 0.2512 0.4156 0.3814 0.0003  -0.0119 -0.0169 126 VAL A CA  
997  C C   . VAL A 126 ? 0.2207 0.3772 0.3441 -0.0141 -0.0125 -0.0185 126 VAL A C   
998  O O   . VAL A 126 ? 0.2756 0.4081 0.3806 -0.0160 -0.0117 -0.0161 126 VAL A O   
999  C CB  . VAL A 126 ? 0.2728 0.4347 0.3968 0.0113  -0.0221 -0.0152 126 VAL A CB  
1000 C CG1 . VAL A 126 ? 0.2498 0.4372 0.3885 0.0098  -0.0318 -0.0193 126 VAL A CG1 
1001 C CG2 . VAL A 126 ? 0.3198 0.4785 0.4435 0.0261  -0.0207 -0.0123 126 VAL A CG2 
1002 N N   . LYS A 127 ? 0.2352 0.4117 0.3737 -0.0243 -0.0135 -0.0227 127 LYS A N   
1003 C CA  . LYS A 127 ? 0.2700 0.4396 0.4037 -0.0396 -0.0140 -0.0252 127 LYS A CA  
1004 C C   . LYS A 127 ? 0.2799 0.4751 0.4300 -0.0447 -0.0235 -0.0307 127 LYS A C   
1005 O O   . LYS A 127 ? 0.2830 0.5039 0.4507 -0.0364 -0.0278 -0.0321 127 LYS A O   
1006 C CB  . LYS A 127 ? 0.2673 0.4330 0.4024 -0.0507 -0.0022 -0.0246 127 LYS A CB  
1007 C CG  . LYS A 127 ? 0.2885 0.4324 0.4083 -0.0445 0.0060  -0.0196 127 LYS A CG  
1008 C CD  . LYS A 127 ? 0.2895 0.4314 0.4098 -0.0541 0.0175  -0.0186 127 LYS A CD  
1009 C CE  . LYS A 127 ? 0.3045 0.4258 0.4086 -0.0480 0.0242  -0.0143 127 LYS A CE  
1010 N NZ  . LYS A 127 ? 0.2819 0.3994 0.3829 -0.0572 0.0349  -0.0128 127 LYS A NZ  
1011 N N   . SER A 128 ? 0.3064 0.4943 0.4503 -0.0576 -0.0276 -0.0341 128 SER A N   
1012 C CA  . SER A 128 ? 0.3512 0.5635 0.5099 -0.0634 -0.0382 -0.0403 128 SER A CA  
1013 C C   . SER A 128 ? 0.4131 0.6567 0.5996 -0.0739 -0.0332 -0.0439 128 SER A C   
1014 O O   . SER A 128 ? 0.4020 0.6437 0.5924 -0.0785 -0.0206 -0.0415 128 SER A O   
1015 C CB  A SER A 128 ? 0.3770 0.5708 0.5199 -0.0758 -0.0439 -0.0442 128 SER A CB  
1016 C CB  B SER A 128 ? 0.3751 0.5684 0.5171 -0.0747 -0.0445 -0.0440 128 SER A CB  
1017 O OG  A SER A 128 ? 0.3766 0.5627 0.5207 -0.0928 -0.0349 -0.0455 128 SER A OG  
1018 O OG  B SER A 128 ? 0.3889 0.6047 0.5419 -0.0777 -0.0576 -0.0503 128 SER A OG  
1019 N N   . SER A 129 ? 0.4612 0.7347 0.6670 -0.0779 -0.0434 -0.0498 129 SER A N   
1020 C CA  . SER A 129 ? 0.5116 0.8189 0.7466 -0.0906 -0.0398 -0.0546 129 SER A CA  
1021 C C   . SER A 129 ? 0.5383 0.8375 0.7709 -0.1142 -0.0388 -0.0594 129 SER A C   
1022 O O   . SER A 129 ? 0.5308 0.8603 0.7876 -0.1273 -0.0415 -0.0655 129 SER A O   
1023 C CB  . SER A 129 ? 0.5380 0.8860 0.7981 -0.0821 -0.0520 -0.0590 129 SER A CB  
1024 O OG  . SER A 129 ? 0.5871 0.9296 0.8355 -0.0818 -0.0678 -0.0625 129 SER A OG  
1025 N N   . GLY A 130 ? 0.5824 0.8411 0.7868 -0.1199 -0.0349 -0.0569 130 GLY A N   
1026 C CA  . GLY A 130 ? 0.6156 0.8597 0.8119 -0.1399 -0.0367 -0.0619 130 GLY A CA  
1027 C C   . GLY A 130 ? 0.6335 0.8532 0.8052 -0.1354 -0.0487 -0.0640 130 GLY A C   
1028 O O   . GLY A 130 ? 0.6512 0.8863 0.8261 -0.1247 -0.0614 -0.0663 130 GLY A O   
1029 N N   . GLY A 131 ? 0.6174 0.7978 0.7626 -0.1421 -0.0443 -0.0629 131 GLY A N   
1030 C CA  . GLY A 131 ? 0.5862 0.7408 0.7057 -0.1375 -0.0535 -0.0651 131 GLY A CA  
1031 C C   . GLY A 131 ? 0.5385 0.6746 0.6397 -0.1170 -0.0518 -0.0579 131 GLY A C   
1032 O O   . GLY A 131 ? 0.5113 0.6478 0.6160 -0.1081 -0.0426 -0.0511 131 GLY A O   
1033 N N   . PRO A 132 ? 0.4952 0.6145 0.5756 -0.1098 -0.0603 -0.0595 132 PRO A N   
1034 C CA  . PRO A 132 ? 0.4664 0.5661 0.5282 -0.0925 -0.0574 -0.0528 132 PRO A CA  
1035 C C   . PRO A 132 ? 0.4231 0.5456 0.4981 -0.0769 -0.0598 -0.0484 132 PRO A C   
1036 O O   . PRO A 132 ? 0.4614 0.6112 0.5516 -0.0746 -0.0693 -0.0515 132 PRO A O   
1037 C CB  . PRO A 132 ? 0.4601 0.5393 0.4975 -0.0909 -0.0660 -0.0570 132 PRO A CB  
1038 C CG  . PRO A 132 ? 0.4874 0.5845 0.5344 -0.1027 -0.0771 -0.0658 132 PRO A CG  
1039 C CD  . PRO A 132 ? 0.4828 0.5961 0.5529 -0.1189 -0.0714 -0.0679 132 PRO A CD  
1040 N N   . PHE A 133 ? 0.3885 0.4987 0.4567 -0.0658 -0.0516 -0.0412 133 PHE A N   
1041 C CA  . PHE A 133 ? 0.3718 0.4945 0.4464 -0.0501 -0.0528 -0.0364 133 PHE A CA  
1042 C C   . PHE A 133 ? 0.3811 0.4860 0.4335 -0.0392 -0.0579 -0.0342 133 PHE A C   
1043 O O   . PHE A 133 ? 0.3631 0.4421 0.3966 -0.0383 -0.0525 -0.0319 133 PHE A O   
1044 C CB  . PHE A 133 ? 0.3318 0.4501 0.4107 -0.0459 -0.0408 -0.0307 133 PHE A CB  
1045 C CG  . PHE A 133 ? 0.3194 0.4429 0.4007 -0.0303 -0.0406 -0.0258 133 PHE A CG  
1046 C CD1 . PHE A 133 ? 0.3264 0.4765 0.4267 -0.0240 -0.0446 -0.0265 133 PHE A CD1 
1047 C CD2 . PHE A 133 ? 0.3502 0.4519 0.4149 -0.0220 -0.0363 -0.0206 133 PHE A CD2 
1048 C CE1 . PHE A 133 ? 0.3116 0.4620 0.4118 -0.0092 -0.0439 -0.0218 133 PHE A CE1 
1049 C CE2 . PHE A 133 ? 0.3538 0.4578 0.4201 -0.0091 -0.0355 -0.0162 133 PHE A CE2 
1050 C CZ  . PHE A 133 ? 0.2897 0.4159 0.3724 -0.0028 -0.0392 -0.0168 133 PHE A CZ  
1051 N N   . VAL A 134 ? 0.3843 0.5034 0.4384 -0.0310 -0.0683 -0.0350 134 VAL A N   
1052 C CA  . VAL A 134 ? 0.4018 0.5049 0.4334 -0.0205 -0.0730 -0.0324 134 VAL A CA  
1053 C C   . VAL A 134 ? 0.4324 0.5482 0.4698 -0.0056 -0.0766 -0.0273 134 VAL A C   
1054 O O   . VAL A 134 ? 0.4324 0.5732 0.4851 -0.0032 -0.0855 -0.0298 134 VAL A O   
1055 C CB  . VAL A 134 ? 0.4487 0.5497 0.4676 -0.0256 -0.0843 -0.0389 134 VAL A CB  
1056 C CG1 . VAL A 134 ? 0.4594 0.5385 0.4502 -0.0152 -0.0859 -0.0356 134 VAL A CG1 
1057 C CG2 . VAL A 134 ? 0.4725 0.5635 0.4888 -0.0422 -0.0823 -0.0456 134 VAL A CG2 
1058 N N   . VAL A 135 ? 0.3941 0.4928 0.4196 0.0044  -0.0700 -0.0203 135 VAL A N   
1059 C CA  . VAL A 135 ? 0.3511 0.4540 0.3760 0.0189  -0.0729 -0.0148 135 VAL A CA  
1060 C C   . VAL A 135 ? 0.3644 0.4422 0.3636 0.0259  -0.0703 -0.0094 135 VAL A C   
1061 O O   . VAL A 135 ? 0.3470 0.4063 0.3347 0.0212  -0.0626 -0.0089 135 VAL A O   
1062 C CB  . VAL A 135 ? 0.3336 0.4439 0.3754 0.0238  -0.0651 -0.0112 135 VAL A CB  
1063 C CG1 . VAL A 135 ? 0.3609 0.4995 0.4289 0.0190  -0.0671 -0.0160 135 VAL A CG1 
1064 C CG2 . VAL A 135 ? 0.3146 0.4063 0.3512 0.0196  -0.0527 -0.0085 135 VAL A CG2 
1065 N N   . ASP A 136 ? 0.3962 0.4734 0.3860 0.0378  -0.0766 -0.0052 136 ASP A N   
1066 C CA  . ASP A 136 ? 0.3701 0.4243 0.3380 0.0453  -0.0714 0.0018  136 ASP A CA  
1067 C C   . ASP A 136 ? 0.3702 0.4195 0.3465 0.0505  -0.0623 0.0075  136 ASP A C   
1068 O O   . ASP A 136 ? 0.3649 0.4278 0.3566 0.0561  -0.0646 0.0081  136 ASP A O   
1069 C CB  . ASP A 136 ? 0.4066 0.4587 0.3572 0.0556  -0.0815 0.0047  136 ASP A CB  
1070 C CG  . ASP A 136 ? 0.4356 0.4849 0.3699 0.0508  -0.0892 -0.0007 136 ASP A CG  
1071 O OD1 . ASP A 136 ? 0.4626 0.4997 0.3893 0.0421  -0.0828 -0.0038 136 ASP A OD1 
1072 O OD2 . ASP A 136 ? 0.4466 0.5057 0.3750 0.0562  -0.1020 -0.0023 136 ASP A OD2 
1073 N N   . VAL A 137 ? 0.3526 0.3833 0.3192 0.0484  -0.0520 0.0110  137 VAL A N   
1074 C CA  . VAL A 137 ? 0.3419 0.3656 0.3145 0.0513  -0.0431 0.0156  137 VAL A CA  
1075 C C   . VAL A 137 ? 0.3817 0.3881 0.3359 0.0599  -0.0417 0.0230  137 VAL A C   
1076 O O   . VAL A 137 ? 0.4059 0.3985 0.3422 0.0586  -0.0385 0.0253  137 VAL A O   
1077 C CB  . VAL A 137 ? 0.3544 0.3708 0.3299 0.0426  -0.0332 0.0144  137 VAL A CB  
1078 C CG1 . VAL A 137 ? 0.3656 0.3762 0.3476 0.0447  -0.0255 0.0179  137 VAL A CG1 
1079 C CG2 . VAL A 137 ? 0.3565 0.3858 0.3455 0.0338  -0.0345 0.0079  137 VAL A CG2 
1080 N N   . VAL A 138 ? 0.3707 0.3769 0.3282 0.0689  -0.0432 0.0269  138 VAL A N   
1081 C CA  . VAL A 138 ? 0.4291 0.4169 0.3679 0.0779  -0.0425 0.0348  138 VAL A CA  
1082 C C   . VAL A 138 ? 0.4566 0.4326 0.4004 0.0788  -0.0334 0.0384  138 VAL A C   
1083 O O   . VAL A 138 ? 0.4548 0.4400 0.4150 0.0813  -0.0337 0.0359  138 VAL A O   
1084 C CB  . VAL A 138 ? 0.4574 0.4526 0.3922 0.0897  -0.0543 0.0365  138 VAL A CB  
1085 C CG1 . VAL A 138 ? 0.4570 0.4294 0.3696 0.0999  -0.0531 0.0458  138 VAL A CG1 
1086 C CG2 . VAL A 138 ? 0.4350 0.4431 0.3652 0.0872  -0.0644 0.0315  138 VAL A CG2 
1087 N N   . ILE A 139 ? 0.3921 0.3483 0.3222 0.0761  -0.0248 0.0435  139 ILE A N   
1088 C CA  . ILE A 139 ? 0.3939 0.3377 0.3281 0.0739  -0.0159 0.0458  139 ILE A CA  
1089 C C   . ILE A 139 ? 0.4168 0.3383 0.3324 0.0815  -0.0142 0.0543  139 ILE A C   
1090 O O   . ILE A 139 ? 0.4371 0.3454 0.3341 0.0804  -0.0109 0.0594  139 ILE A O   
1091 C CB  . ILE A 139 ? 0.4196 0.3604 0.3563 0.0625  -0.0065 0.0444  139 ILE A CB  
1092 C CG1 . ILE A 139 ? 0.3813 0.3406 0.3332 0.0557  -0.0081 0.0369  139 ILE A CG1 
1093 C CG2 . ILE A 139 ? 0.4384 0.3672 0.3798 0.0593  0.0016  0.0461  139 ILE A CG2 
1094 C CD1 . ILE A 139 ? 0.3446 0.3017 0.2967 0.0467  -0.0003 0.0357  139 ILE A CD1 
1095 N N   . ASN A 140 ? 0.4199 0.3353 0.3387 0.0897  -0.0157 0.0560  140 ASN A N   
1096 C CA  . ASN A 140 ? 0.4461 0.3364 0.3451 0.0983  -0.0145 0.0647  140 ASN A CA  
1097 C C   . ASN A 140 ? 0.4952 0.3824 0.3739 0.1055  -0.0214 0.0698  140 ASN A C   
1098 O O   . ASN A 140 ? 0.4760 0.3416 0.3323 0.1054  -0.0164 0.0773  140 ASN A O   
1099 C CB  . ASN A 140 ? 0.4943 0.3619 0.3846 0.0892  -0.0022 0.0689  140 ASN A CB  
1100 C CG  . ASN A 140 ? 0.4898 0.3592 0.3981 0.0822  0.0035  0.0635  140 ASN A CG  
1101 O OD1 . ASN A 140 ? 0.5278 0.4018 0.4464 0.0889  -0.0001 0.0601  140 ASN A OD1 
1102 N ND2 . ASN A 140 ? 0.4857 0.3531 0.3978 0.0693  0.0121  0.0621  140 ASN A ND2 
1103 N N   . ASP A 141 ? 0.4787 0.3882 0.3649 0.1107  -0.0327 0.0651  141 ASP A N   
1104 C CA  . ASP A 141 ? 0.5227 0.4330 0.3905 0.1187  -0.0425 0.0683  141 ASP A CA  
1105 C C   . ASP A 141 ? 0.5698 0.4778 0.4233 0.1100  -0.0395 0.0680  141 ASP A C   
1106 O O   . ASP A 141 ? 0.6030 0.5080 0.4363 0.1161  -0.0468 0.0708  141 ASP A O   
1107 C CB  . ASP A 141 ? 0.5821 0.4676 0.4263 0.1318  -0.0439 0.0786  141 ASP A CB  
1108 C CG  . ASP A 141 ? 0.6032 0.4884 0.4583 0.1437  -0.0475 0.0793  141 ASP A CG  
1109 O OD1 . ASP A 141 ? 0.5924 0.5040 0.4717 0.1457  -0.0539 0.0717  141 ASP A OD1 
1110 O OD2 . ASP A 141 ? 0.6273 0.4849 0.4660 0.1511  -0.0434 0.0874  141 ASP A OD2 
1111 N N   . ILE A 142 ? 0.5639 0.4732 0.4259 0.0972  -0.0297 0.0644  142 ILE A N   
1112 C CA  . ILE A 142 ? 0.6140 0.5209 0.4635 0.0900  -0.0255 0.0636  142 ILE A CA  
1113 C C   . ILE A 142 ? 0.4854 0.4146 0.3516 0.0832  -0.0301 0.0537  142 ILE A C   
1114 O O   . ILE A 142 ? 0.4010 0.3414 0.2895 0.0771  -0.0273 0.0487  142 ILE A O   
1115 C CB  . ILE A 142 ? 0.7607 0.6529 0.6071 0.0814  -0.0106 0.0672  142 ILE A CB  
1116 C CG1 . ILE A 142 ? 0.8597 0.7262 0.6837 0.0866  -0.0053 0.0778  142 ILE A CG1 
1117 C CG2 . ILE A 142 ? 0.7882 0.6841 0.6288 0.0739  -0.0054 0.0640  142 ILE A CG2 
1118 C CD1 . ILE A 142 ? 0.8938 0.7478 0.7207 0.0768  0.0093  0.0810  142 ILE A CD1 
1119 N N   . HIS A 143 ? 0.4743 0.4083 0.3280 0.0839  -0.0372 0.0508  143 HIS A N   
1120 C CA  . HIS A 143 ? 0.4647 0.4162 0.3315 0.0767  -0.0417 0.0413  143 HIS A CA  
1121 C C   . HIS A 143 ? 0.4388 0.3860 0.3097 0.0670  -0.0301 0.0391  143 HIS A C   
1122 O O   . HIS A 143 ? 0.4291 0.3638 0.2821 0.0660  -0.0234 0.0417  143 HIS A O   
1123 C CB  A HIS A 143 ? 0.4977 0.4529 0.3485 0.0786  -0.0521 0.0375  143 HIS A CB  
1124 C CB  B HIS A 143 ? 0.5019 0.4561 0.3513 0.0795  -0.0523 0.0383  143 HIS A CB  
1125 C CG  A HIS A 143 ? 0.5255 0.4938 0.3879 0.0692  -0.0550 0.0277  143 HIS A CG  
1126 C CG  B HIS A 143 ? 0.5071 0.4740 0.3598 0.0882  -0.0666 0.0379  143 HIS A CG  
1127 N ND1 A HIS A 143 ? 0.5437 0.5043 0.4008 0.0618  -0.0466 0.0247  143 HIS A ND1 
1128 N ND1 B HIS A 143 ? 0.5082 0.4963 0.3733 0.0854  -0.0782 0.0294  143 HIS A ND1 
1129 C CD2 A HIS A 143 ? 0.5449 0.5329 0.4258 0.0655  -0.0640 0.0204  143 HIS A CD2 
1130 C CD2 B HIS A 143 ? 0.5123 0.4750 0.3599 0.0999  -0.0709 0.0447  143 HIS A CD2 
1131 C CE1 A HIS A 143 ? 0.5278 0.4994 0.3962 0.0545  -0.0510 0.0163  143 HIS A CE1 
1132 C CE1 B HIS A 143 ? 0.5113 0.5107 0.3798 0.0953  -0.0897 0.0308  143 HIS A CE1 
1133 N NE2 A HIS A 143 ? 0.5342 0.5228 0.4178 0.0555  -0.0612 0.0136  143 HIS A NE2 
1134 N NE2 B HIS A 143 ? 0.5116 0.4951 0.3689 0.1052  -0.0856 0.0403  143 HIS A NE2 
1135 N N   . PHE A 144 ? 0.3729 0.3312 0.2667 0.0607  -0.0276 0.0345  144 PHE A N   
1136 C CA  . PHE A 144 ? 0.3706 0.3264 0.2702 0.0530  -0.0175 0.0327  144 PHE A CA  
1137 C C   . PHE A 144 ? 0.3716 0.3337 0.2728 0.0471  -0.0197 0.0253  144 PHE A C   
1138 O O   . PHE A 144 ? 0.4087 0.3638 0.3018 0.0445  -0.0130 0.0246  144 PHE A O   
1139 C CB  . PHE A 144 ? 0.3463 0.3069 0.2665 0.0500  -0.0129 0.0327  144 PHE A CB  
1140 C CG  . PHE A 144 ? 0.3732 0.3330 0.3003 0.0431  -0.0039 0.0312  144 PHE A CG  
1141 C CD1 . PHE A 144 ? 0.3561 0.3054 0.2756 0.0420  0.0055  0.0358  144 PHE A CD1 
1142 C CD2 . PHE A 144 ? 0.3612 0.3309 0.3016 0.0378  -0.0047 0.0253  144 PHE A CD2 
1143 C CE1 . PHE A 144 ? 0.3575 0.3096 0.2852 0.0365  0.0127  0.0339  144 PHE A CE1 
1144 C CE2 . PHE A 144 ? 0.3869 0.3562 0.3329 0.0331  0.0024  0.0241  144 PHE A CE2 
1145 C CZ  . PHE A 144 ? 0.3836 0.3454 0.3240 0.0329  0.0107  0.0281  144 PHE A CZ  
1146 N N   . GLU A 145 ? 0.3655 0.3407 0.2783 0.0447  -0.0280 0.0195  145 GLU A N   
1147 C CA  . GLU A 145 ? 0.3561 0.3336 0.2688 0.0380  -0.0297 0.0126  145 GLU A CA  
1148 C C   . GLU A 145 ? 0.3882 0.3802 0.3097 0.0359  -0.0409 0.0072  145 GLU A C   
1149 O O   . GLU A 145 ? 0.3880 0.3916 0.3214 0.0395  -0.0457 0.0086  145 GLU A O   
1150 C CB  . GLU A 145 ? 0.3490 0.3267 0.2747 0.0319  -0.0216 0.0109  145 GLU A CB  
1151 C CG  . GLU A 145 ? 0.3504 0.3411 0.2982 0.0291  -0.0226 0.0098  145 GLU A CG  
1152 C CD  . GLU A 145 ? 0.3504 0.3397 0.3078 0.0244  -0.0148 0.0092  145 GLU A CD  
1153 O OE1 . GLU A 145 ? 0.2944 0.2928 0.2670 0.0219  -0.0147 0.0082  145 GLU A OE1 
1154 O OE2 . GLU A 145 ? 0.2744 0.2546 0.2241 0.0240  -0.0089 0.0099  145 GLU A OE2 
1155 N N   . ARG A 146 ? 0.3776 0.3688 0.2932 0.0300  -0.0450 0.0006  146 ARG A N   
1156 C CA  . ARG A 146 ? 0.4006 0.4070 0.3290 0.0238  -0.0540 -0.0060 146 ARG A CA  
1157 C C   . ARG A 146 ? 0.3961 0.4024 0.3369 0.0144  -0.0479 -0.0095 146 ARG A C   
1158 O O   . ARG A 146 ? 0.4117 0.4044 0.3416 0.0103  -0.0441 -0.0123 146 ARG A O   
1159 C CB  . ARG A 146 ? 0.4384 0.4433 0.3511 0.0220  -0.0640 -0.0118 146 ARG A CB  
1160 C CG  . ARG A 146 ? 0.4236 0.4477 0.3537 0.0136  -0.0734 -0.0190 146 ARG A CG  
1161 C CD  . ARG A 146 ? 0.4253 0.4526 0.3417 0.0129  -0.0866 -0.0249 146 ARG A CD  
1162 N NE  . ARG A 146 ? 0.4312 0.4695 0.3458 0.0238  -0.0952 -0.0208 146 ARG A NE  
1163 C CZ  . ARG A 146 ? 0.4732 0.5168 0.3754 0.0263  -0.1084 -0.0245 146 ARG A CZ  
1164 N NH1 . ARG A 146 ? 0.4622 0.5010 0.3532 0.0173  -0.1142 -0.0333 146 ARG A NH1 
1165 N NH2 . ARG A 146 ? 0.4786 0.5313 0.3784 0.0380  -0.1163 -0.0197 146 ARG A NH2 
1166 N N   . PHE A 147 ? 0.3787 0.3995 0.3409 0.0118  -0.0471 -0.0093 147 PHE A N   
1167 C CA  . PHE A 147 ? 0.3537 0.3742 0.3269 0.0036  -0.0408 -0.0113 147 PHE A CA  
1168 C C   . PHE A 147 ? 0.3728 0.4025 0.3537 -0.0070 -0.0466 -0.0183 147 PHE A C   
1169 O O   . PHE A 147 ? 0.3653 0.4145 0.3592 -0.0078 -0.0538 -0.0205 147 PHE A O   
1170 C CB  . PHE A 147 ? 0.3447 0.3749 0.3350 0.0061  -0.0357 -0.0075 147 PHE A CB  
1171 C CG  . PHE A 147 ? 0.2957 0.3251 0.2949 -0.0016 -0.0290 -0.0088 147 PHE A CG  
1172 C CD1 . PHE A 147 ? 0.3126 0.3551 0.3255 -0.0100 -0.0308 -0.0129 147 PHE A CD1 
1173 C CD2 . PHE A 147 ? 0.3324 0.3480 0.3254 -0.0006 -0.0211 -0.0059 147 PHE A CD2 
1174 C CE1 . PHE A 147 ? 0.3002 0.3392 0.3181 -0.0171 -0.0238 -0.0132 147 PHE A CE1 
1175 C CE2 . PHE A 147 ? 0.3122 0.3256 0.3107 -0.0065 -0.0157 -0.0065 147 PHE A CE2 
1176 C CZ  . PHE A 147 ? 0.2856 0.3092 0.2949 -0.0148 -0.0169 -0.0099 147 PHE A CZ  
1177 N N   . ARG A 148 ? 0.3120 0.3278 0.2852 -0.0150 -0.0433 -0.0217 148 ARG A N   
1178 C CA  . ARG A 148 ? 0.3205 0.3414 0.3007 -0.0275 -0.0468 -0.0281 148 ARG A CA  
1179 C C   . ARG A 148 ? 0.3229 0.3341 0.3066 -0.0336 -0.0373 -0.0268 148 ARG A C   
1180 O O   . ARG A 148 ? 0.3491 0.3403 0.3191 -0.0306 -0.0313 -0.0247 148 ARG A O   
1181 C CB  . ARG A 148 ? 0.3543 0.3630 0.3168 -0.0320 -0.0534 -0.0344 148 ARG A CB  
1182 C CG  . ARG A 148 ? 0.3364 0.3491 0.3055 -0.0468 -0.0575 -0.0418 148 ARG A CG  
1183 C CD  . ARG A 148 ? 0.3535 0.3519 0.3016 -0.0498 -0.0650 -0.0487 148 ARG A CD  
1184 N NE  . ARG A 148 ? 0.4111 0.4117 0.3645 -0.0657 -0.0698 -0.0567 148 ARG A NE  
1185 C CZ  . ARG A 148 ? 0.4414 0.4632 0.4052 -0.0720 -0.0812 -0.0626 148 ARG A CZ  
1186 N NH1 . ARG A 148 ? 0.4328 0.4740 0.4009 -0.0618 -0.0893 -0.0609 148 ARG A NH1 
1187 N NH2 . ARG A 148 ? 0.4690 0.4923 0.4387 -0.0887 -0.0846 -0.0703 148 ARG A NH2 
1188 N N   . GLY A 149 ? 0.3111 0.3369 0.3129 -0.0412 -0.0356 -0.0276 149 GLY A N   
1189 C CA  . GLY A 149 ? 0.2974 0.3134 0.3005 -0.0452 -0.0260 -0.0248 149 GLY A CA  
1190 C C   . GLY A 149 ? 0.2796 0.3151 0.3031 -0.0533 -0.0238 -0.0256 149 GLY A C   
1191 O O   . GLY A 149 ? 0.3093 0.3630 0.3451 -0.0597 -0.0297 -0.0301 149 GLY A O   
1192 N N   . ASP A 150 ? 0.2703 0.3031 0.2973 -0.0528 -0.0150 -0.0214 150 ASP A N   
1193 C CA  . ASP A 150 ? 0.3024 0.3534 0.3473 -0.0597 -0.0109 -0.0217 150 ASP A CA  
1194 C C   . ASP A 150 ? 0.3008 0.3745 0.3617 -0.0504 -0.0114 -0.0201 150 ASP A C   
1195 O O   . ASP A 150 ? 0.3133 0.4094 0.3927 -0.0547 -0.0107 -0.0222 150 ASP A O   
1196 C CB  . ASP A 150 ? 0.3063 0.3424 0.3447 -0.0638 -0.0009 -0.0181 150 ASP A CB  
1197 C CG  . ASP A 150 ? 0.3578 0.3737 0.3841 -0.0757 0.0008  -0.0200 150 ASP A CG  
1198 O OD1 . ASP A 150 ? 0.3971 0.4131 0.4224 -0.0824 -0.0055 -0.0252 150 ASP A OD1 
1199 O OD2 . ASP A 150 ? 0.3900 0.3891 0.4065 -0.0785 0.0082  -0.0166 150 ASP A OD2 
1200 N N   . GLY A 151 ? 0.2687 0.3370 0.3234 -0.0379 -0.0121 -0.0165 151 GLY A N   
1201 C CA  . GLY A 151 ? 0.2693 0.3536 0.3363 -0.0287 -0.0114 -0.0147 151 GLY A CA  
1202 C C   . GLY A 151 ? 0.2340 0.3048 0.2907 -0.0181 -0.0091 -0.0102 151 GLY A C   
1203 O O   . GLY A 151 ? 0.2646 0.3167 0.3066 -0.0173 -0.0078 -0.0084 151 GLY A O   
1204 N N   . LEU A 152 ? 0.2328 0.3139 0.2985 -0.0097 -0.0084 -0.0088 152 LEU A N   
1205 C CA  . LEU A 152 ? 0.2068 0.2763 0.2647 -0.0008 -0.0061 -0.0051 152 LEU A CA  
1206 C C   . LEU A 152 ? 0.2232 0.2992 0.2898 0.0025  -0.0003 -0.0048 152 LEU A C   
1207 O O   . LEU A 152 ? 0.2569 0.3503 0.3374 0.0020  0.0005  -0.0072 152 LEU A O   
1208 C CB  . LEU A 152 ? 0.2407 0.3103 0.2954 0.0083  -0.0123 -0.0034 152 LEU A CB  
1209 C CG  . LEU A 152 ? 0.2516 0.3099 0.2920 0.0071  -0.0170 -0.0031 152 LEU A CG  
1210 C CD1 . LEU A 152 ? 0.2774 0.3399 0.3156 0.0156  -0.0240 -0.0017 152 LEU A CD1 
1211 C CD2 . LEU A 152 ? 0.2633 0.3027 0.2901 0.0078  -0.0121 -0.0001 152 LEU A CD2 
1212 N N   . CYS A 153 ? 0.2418 0.3045 0.3004 0.0058  0.0038  -0.0025 153 CYS A N   
1213 C CA  . CYS A 153 ? 0.2345 0.2998 0.2977 0.0088  0.0093  -0.0030 153 CYS A CA  
1214 C C   . CYS A 153 ? 0.2452 0.3000 0.3029 0.0166  0.0090  -0.0010 153 CYS A C   
1215 O O   . CYS A 153 ? 0.2625 0.3043 0.3102 0.0162  0.0083  0.0013  153 CYS A O   
1216 C CB  . CYS A 153 ? 0.2559 0.3141 0.3132 0.0024  0.0150  -0.0030 153 CYS A CB  
1217 S SG  . CYS A 153 ? 0.2699 0.3266 0.3268 0.0061  0.0215  -0.0041 153 CYS A SG  
1218 N N   . MET A 154 ? 0.2487 0.3085 0.3127 0.0237  0.0098  -0.0020 154 MET A N   
1219 C CA  . MET A 154 ? 0.2524 0.2995 0.3104 0.0305  0.0101  -0.0003 154 MET A CA  
1220 C C   . MET A 154 ? 0.2635 0.3082 0.3223 0.0317  0.0158  -0.0030 154 MET A C   
1221 O O   . MET A 154 ? 0.2736 0.3295 0.3410 0.0356  0.0180  -0.0057 154 MET A O   
1222 C CB  . MET A 154 ? 0.2840 0.3339 0.3449 0.0398  0.0056  0.0011  154 MET A CB  
1223 C CG  . MET A 154 ? 0.2918 0.3230 0.3432 0.0454  0.0067  0.0037  154 MET A CG  
1224 S SD  . MET A 154 ? 0.2853 0.2998 0.3229 0.0405  0.0059  0.0081  154 MET A SD  
1225 C CE  . MET A 154 ? 0.2690 0.2836 0.3018 0.0479  -0.0009 0.0122  154 MET A CE  
1226 N N   . SER A 155 ? 0.2642 0.2955 0.3142 0.0287  0.0180  -0.0027 155 SER A N   
1227 C CA  . SER A 155 ? 0.2475 0.2757 0.2952 0.0278  0.0228  -0.0061 155 SER A CA  
1228 C C   . SER A 155 ? 0.2938 0.3078 0.3362 0.0324  0.0234  -0.0070 155 SER A C   
1229 O O   . SER A 155 ? 0.2693 0.2726 0.3073 0.0326  0.0211  -0.0041 155 SER A O   
1230 C CB  . SER A 155 ? 0.2684 0.2929 0.3093 0.0202  0.0238  -0.0058 155 SER A CB  
1231 O OG  . SER A 155 ? 0.3018 0.3225 0.3378 0.0196  0.0274  -0.0092 155 SER A OG  
1232 N N   . THR A 156 ? 0.3053 0.3180 0.3472 0.0358  0.0273  -0.0112 156 THR A N   
1233 C CA  . THR A 156 ? 0.3195 0.3156 0.3538 0.0376  0.0285  -0.0136 156 THR A CA  
1234 C C   . THR A 156 ? 0.3222 0.3118 0.3493 0.0292  0.0281  -0.0147 156 THR A C   
1235 O O   . THR A 156 ? 0.3022 0.3000 0.3293 0.0239  0.0277  -0.0137 156 THR A O   
1236 C CB  . THR A 156 ? 0.3394 0.3358 0.3737 0.0440  0.0331  -0.0190 156 THR A CB  
1237 O OG1 . THR A 156 ? 0.3036 0.3075 0.3356 0.0390  0.0365  -0.0220 156 THR A OG1 
1238 C CG2 . THR A 156 ? 0.3322 0.3409 0.3770 0.0536  0.0336  -0.0186 156 THR A CG2 
1239 N N   . PRO A 157 ? 0.3042 0.2787 0.3247 0.0279  0.0281  -0.0171 157 PRO A N   
1240 C CA  . PRO A 157 ? 0.3172 0.2888 0.3324 0.0202  0.0269  -0.0194 157 PRO A CA  
1241 C C   . PRO A 157 ? 0.3086 0.2872 0.3195 0.0192  0.0287  -0.0232 157 PRO A C   
1242 O O   . PRO A 157 ? 0.3280 0.3130 0.3374 0.0145  0.0268  -0.0217 157 PRO A O   
1243 C CB  . PRO A 157 ? 0.3353 0.2891 0.3448 0.0191  0.0271  -0.0227 157 PRO A CB  
1244 C CG  . PRO A 157 ? 0.3404 0.2862 0.3520 0.0246  0.0276  -0.0185 157 PRO A CG  
1245 C CD  . PRO A 157 ? 0.3082 0.2668 0.3257 0.0327  0.0286  -0.0172 157 PRO A CD  
1246 N N   . SER A 158 ? 0.3266 0.3037 0.3347 0.0243  0.0327  -0.0276 158 SER A N   
1247 C CA  . SER A 158 ? 0.3103 0.2931 0.3119 0.0231  0.0355  -0.0308 158 SER A CA  
1248 C C   . SER A 158 ? 0.3112 0.3090 0.3185 0.0222  0.0373  -0.0265 158 SER A C   
1249 O O   . SER A 158 ? 0.3169 0.3184 0.3175 0.0190  0.0389  -0.0265 158 SER A O   
1250 C CB  . SER A 158 ? 0.3281 0.3052 0.3239 0.0290  0.0405  -0.0371 158 SER A CB  
1251 O OG  . SER A 158 ? 0.2992 0.2819 0.3043 0.0371  0.0441  -0.0364 158 SER A OG  
1252 N N   . GLY A 159 ? 0.3124 0.3177 0.3307 0.0245  0.0368  -0.0226 159 GLY A N   
1253 C CA  . GLY A 159 ? 0.2865 0.3046 0.3104 0.0214  0.0376  -0.0189 159 GLY A CA  
1254 C C   . GLY A 159 ? 0.3013 0.3172 0.3215 0.0153  0.0335  -0.0150 159 GLY A C   
1255 O O   . GLY A 159 ? 0.2929 0.3151 0.3140 0.0118  0.0344  -0.0123 159 GLY A O   
1256 N N   . THR A 160 ? 0.2751 0.2823 0.2917 0.0139  0.0293  -0.0147 160 THR A N   
1257 C CA  . THR A 160 ? 0.2811 0.2886 0.2966 0.0101  0.0258  -0.0109 160 THR A CA  
1258 C C   . THR A 160 ? 0.3065 0.3146 0.3134 0.0073  0.0263  -0.0104 160 THR A C   
1259 O O   . THR A 160 ? 0.3051 0.3138 0.3108 0.0054  0.0246  -0.0068 160 THR A O   
1260 C CB  . THR A 160 ? 0.3128 0.3142 0.3285 0.0087  0.0221  -0.0105 160 THR A CB  
1261 O OG1 . THR A 160 ? 0.3068 0.3028 0.3171 0.0074  0.0213  -0.0150 160 THR A OG1 
1262 C CG2 . THR A 160 ? 0.3010 0.2993 0.3227 0.0113  0.0219  -0.0088 160 THR A CG2 
1263 N N   . THR A 161 ? 0.3189 0.3253 0.3179 0.0076  0.0288  -0.0138 161 THR A N   
1264 C CA  . THR A 161 ? 0.3153 0.3206 0.3030 0.0057  0.0295  -0.0125 161 THR A CA  
1265 C C   . THR A 161 ? 0.3485 0.3581 0.3359 0.0040  0.0354  -0.0101 161 THR A C   
1266 O O   . THR A 161 ? 0.3156 0.3218 0.2917 0.0020  0.0373  -0.0079 161 THR A O   
1267 C CB  . THR A 161 ? 0.2961 0.2966 0.2722 0.0066  0.0295  -0.0174 161 THR A CB  
1268 O OG1 . THR A 161 ? 0.3038 0.3041 0.2830 0.0093  0.0338  -0.0220 161 THR A OG1 
1269 C CG2 . THR A 161 ? 0.3251 0.3225 0.3009 0.0057  0.0224  -0.0193 161 THR A CG2 
1270 N N   . ALA A 162 ? 0.3072 0.3243 0.3067 0.0043  0.0381  -0.0100 162 ALA A N   
1271 C CA  . ALA A 162 ? 0.3146 0.3392 0.3173 0.0011  0.0441  -0.0086 162 ALA A CA  
1272 C C   . ALA A 162 ? 0.3345 0.3606 0.3432 -0.0027 0.0414  -0.0049 162 ALA A C   
1273 O O   . ALA A 162 ? 0.3100 0.3274 0.3112 -0.0040 0.0376  -0.0020 162 ALA A O   
1274 C CB  . ALA A 162 ? 0.3015 0.3364 0.3143 0.0048  0.0488  -0.0125 162 ALA A CB  
1275 N N   . TYR A 163 ? 0.2740 0.3112 0.2955 -0.0043 0.0431  -0.0052 163 TYR A N   
1276 C CA  . TYR A 163 ? 0.2442 0.2821 0.2699 -0.0088 0.0401  -0.0028 163 TYR A CA  
1277 C C   . TYR A 163 ? 0.2719 0.3006 0.2939 -0.0062 0.0333  -0.0011 163 TYR A C   
1278 O O   . TYR A 163 ? 0.2859 0.3065 0.3013 -0.0091 0.0314  0.0014  163 TYR A O   
1279 C CB  . TYR A 163 ? 0.2451 0.2992 0.2874 -0.0087 0.0402  -0.0048 163 TYR A CB  
1280 C CG  . TYR A 163 ? 0.2611 0.3203 0.3089 -0.0163 0.0394  -0.0039 163 TYR A CG  
1281 C CD1 . TYR A 163 ? 0.2812 0.3268 0.3178 -0.0222 0.0385  -0.0012 163 TYR A CD1 
1282 C CD2 . TYR A 163 ? 0.3124 0.3902 0.3766 -0.0175 0.0394  -0.0064 163 TYR A CD2 
1283 C CE1 . TYR A 163 ? 0.3184 0.3663 0.3589 -0.0304 0.0377  -0.0013 163 TYR A CE1 
1284 C CE2 . TYR A 163 ? 0.3466 0.4305 0.4169 -0.0261 0.0379  -0.0066 163 TYR A CE2 
1285 C CZ  . TYR A 163 ? 0.3566 0.4242 0.4144 -0.0330 0.0371  -0.0043 163 TYR A CZ  
1286 O OH  . TYR A 163 ? 0.3437 0.4150 0.4064 -0.0425 0.0356  -0.0055 163 TYR A OH  
1287 N N   . ASN A 164 ? 0.2614 0.2901 0.2868 -0.0006 0.0304  -0.0025 164 ASN A N   
1288 C CA  . ASN A 164 ? 0.2461 0.2680 0.2694 0.0016  0.0254  -0.0009 164 ASN A CA  
1289 C C   . ASN A 164 ? 0.2821 0.2951 0.2949 0.0002  0.0243  0.0011  164 ASN A C   
1290 O O   . ASN A 164 ? 0.2747 0.2833 0.2853 0.0001  0.0217  0.0031  164 ASN A O   
1291 C CB  . ASN A 164 ? 0.2611 0.2816 0.2870 0.0063  0.0244  -0.0027 164 ASN A CB  
1292 C CG  . ASN A 164 ? 0.2749 0.2888 0.2983 0.0072  0.0209  -0.0011 164 ASN A CG  
1293 O OD1 . ASN A 164 ? 0.2616 0.2751 0.2880 0.0086  0.0189  0.0006  164 ASN A OD1 
1294 N ND2 . ASN A 164 ? 0.2728 0.2827 0.2910 0.0063  0.0203  -0.0017 164 ASN A ND2 
1295 N N   . LYS A 165 ? 0.2564 0.2668 0.2620 0.0001  0.0261  0.0004  165 LYS A N   
1296 C CA  . LYS A 165 ? 0.2433 0.2464 0.2387 0.0006  0.0239  0.0024  165 LYS A CA  
1297 C C   . LYS A 165 ? 0.2585 0.2554 0.2478 -0.0020 0.0249  0.0057  165 LYS A C   
1298 O O   . LYS A 165 ? 0.2872 0.2777 0.2714 0.0000  0.0219  0.0079  165 LYS A O   
1299 C CB  . LYS A 165 ? 0.2579 0.2592 0.2442 0.0012  0.0253  0.0009  165 LYS A CB  
1300 C CG  . LYS A 165 ? 0.2991 0.2941 0.2741 0.0032  0.0215  0.0031  165 LYS A CG  
1301 C CD  . LYS A 165 ? 0.3177 0.3118 0.2830 0.0043  0.0212  0.0007  165 LYS A CD  
1302 C CE  . LYS A 165 ? 0.3727 0.3637 0.3293 0.0079  0.0151  0.0027  165 LYS A CE  
1303 N NZ  . LYS A 165 ? 0.4092 0.3901 0.3524 0.0085  0.0170  0.0080  165 LYS A NZ  
1304 N N   . SER A 166 ? 0.2518 0.2501 0.2416 -0.0067 0.0293  0.0059  166 SER A N   
1305 C CA  . SER A 166 ? 0.2778 0.2670 0.2603 -0.0111 0.0308  0.0088  166 SER A CA  
1306 C C   . SER A 166 ? 0.2999 0.2872 0.2868 -0.0114 0.0273  0.0088  166 SER A C   
1307 O O   . SER A 166 ? 0.2895 0.2650 0.2677 -0.0134 0.0272  0.0108  166 SER A O   
1308 C CB  . SER A 166 ? 0.3380 0.3313 0.3225 -0.0182 0.0371  0.0086  166 SER A CB  
1309 O OG  . SER A 166 ? 0.4306 0.4220 0.4059 -0.0180 0.0416  0.0093  166 SER A OG  
1310 N N   . LEU A 167 ? 0.3086 0.3053 0.3067 -0.0093 0.0248  0.0066  167 LEU A N   
1311 C CA  . LEU A 167 ? 0.2706 0.2662 0.2713 -0.0089 0.0213  0.0062  167 LEU A CA  
1312 C C   . LEU A 167 ? 0.3226 0.3137 0.3201 -0.0029 0.0185  0.0073  167 LEU A C   
1313 O O   . LEU A 167 ? 0.3089 0.2985 0.3068 -0.0015 0.0163  0.0071  167 LEU A O   
1314 C CB  . LEU A 167 ? 0.2614 0.2694 0.2743 -0.0088 0.0200  0.0040  167 LEU A CB  
1315 C CG  . LEU A 167 ? 0.3053 0.3224 0.3252 -0.0149 0.0227  0.0023  167 LEU A CG  
1316 C CD1 . LEU A 167 ? 0.2924 0.3247 0.3258 -0.0124 0.0209  0.0001  167 LEU A CD1 
1317 C CD2 . LEU A 167 ? 0.2968 0.3074 0.3123 -0.0221 0.0224  0.0023  167 LEU A CD2 
1318 N N   . GLY A 168 ? 0.2854 0.2751 0.2794 0.0004  0.0184  0.0082  168 GLY A N   
1319 C CA  . GLY A 168 ? 0.2874 0.2767 0.2813 0.0053  0.0161  0.0089  168 GLY A CA  
1320 C C   . GLY A 168 ? 0.2914 0.2888 0.2941 0.0068  0.0153  0.0076  168 GLY A C   
1321 O O   . GLY A 168 ? 0.3052 0.3041 0.3098 0.0096  0.0143  0.0081  168 GLY A O   
1322 N N   . GLY A 169 ? 0.2624 0.2644 0.2702 0.0051  0.0163  0.0059  169 GLY A N   
1323 C CA  . GLY A 169 ? 0.2616 0.2670 0.2757 0.0064  0.0159  0.0048  169 GLY A CA  
1324 C C   . GLY A 169 ? 0.3008 0.3074 0.3149 0.0067  0.0150  0.0036  169 GLY A C   
1325 O O   . GLY A 169 ? 0.2856 0.2917 0.2944 0.0067  0.0143  0.0032  169 GLY A O   
1326 N N   . ALA A 170 ? 0.2661 0.2738 0.2853 0.0064  0.0149  0.0029  170 ALA A N   
1327 C CA  . ALA A 170 ? 0.2960 0.3059 0.3170 0.0049  0.0135  0.0005  170 ALA A CA  
1328 C C   . ALA A 170 ? 0.2693 0.2767 0.2876 0.0039  0.0139  -0.0030 170 ALA A C   
1329 O O   . ALA A 170 ? 0.2720 0.2768 0.2907 0.0049  0.0162  -0.0035 170 ALA A O   
1330 C CB  . ALA A 170 ? 0.3070 0.3172 0.3342 0.0030  0.0143  0.0009  170 ALA A CB  
1331 N N   . LEU A 171 ? 0.3017 0.3107 0.3171 0.0026  0.0115  -0.0060 171 LEU A N   
1332 C CA  . LEU A 171 ? 0.2666 0.2716 0.2780 0.0017  0.0122  -0.0105 171 LEU A CA  
1333 C C   . LEU A 171 ? 0.2741 0.2753 0.2903 -0.0014 0.0118  -0.0133 171 LEU A C   
1334 O O   . LEU A 171 ? 0.3349 0.3404 0.3560 -0.0047 0.0093  -0.0136 171 LEU A O   
1335 C CB  . LEU A 171 ? 0.2525 0.2592 0.2554 0.0015  0.0092  -0.0130 171 LEU A CB  
1336 C CG  . LEU A 171 ? 0.2853 0.2931 0.2815 0.0041  0.0093  -0.0090 171 LEU A CG  
1337 C CD1 . LEU A 171 ? 0.2851 0.2923 0.2694 0.0049  0.0062  -0.0110 171 LEU A CD1 
1338 C CD2 . LEU A 171 ? 0.3207 0.3257 0.3156 0.0047  0.0146  -0.0069 171 LEU A CD2 
1339 N N   . MET A 172 ? 0.2685 0.2617 0.2840 -0.0005 0.0147  -0.0152 172 MET A N   
1340 C CA  . MET A 172 ? 0.2867 0.2715 0.3046 -0.0036 0.0152  -0.0172 172 MET A CA  
1341 C C   . MET A 172 ? 0.3615 0.3374 0.3726 -0.0043 0.0153  -0.0237 172 MET A C   
1342 O O   . MET A 172 ? 0.3753 0.3494 0.3814 0.0004  0.0177  -0.0254 172 MET A O   
1343 C CB  . MET A 172 ? 0.3200 0.2982 0.3404 -0.0004 0.0183  -0.0132 172 MET A CB  
1344 C CG  . MET A 172 ? 0.3793 0.3645 0.4030 0.0022  0.0185  -0.0076 172 MET A CG  
1345 S SD  . MET A 172 ? 0.3940 0.3701 0.4176 0.0070  0.0207  -0.0039 172 MET A SD  
1346 C CE  . MET A 172 ? 0.3230 0.2852 0.3450 0.0018  0.0223  -0.0046 172 MET A CE  
1347 N N   . HIS A 173 ? 0.3274 0.2982 0.3385 -0.0105 0.0132  -0.0279 173 HIS A N   
1348 C CA  . HIS A 173 ? 0.3625 0.3215 0.3652 -0.0115 0.0133  -0.0352 173 HIS A CA  
1349 C C   . HIS A 173 ? 0.4039 0.3487 0.4035 -0.0058 0.0183  -0.0350 173 HIS A C   
1350 O O   . HIS A 173 ? 0.4182 0.3565 0.4221 -0.0055 0.0202  -0.0307 173 HIS A O   
1351 C CB  . HIS A 173 ? 0.3595 0.3137 0.3636 -0.0208 0.0101  -0.0400 173 HIS A CB  
1352 C CG  . HIS A 173 ? 0.3888 0.3312 0.3817 -0.0224 0.0088  -0.0489 173 HIS A CG  
1353 N ND1 . HIS A 173 ? 0.4251 0.3468 0.4118 -0.0222 0.0123  -0.0527 173 HIS A ND1 
1354 C CD2 . HIS A 173 ? 0.4019 0.3487 0.3863 -0.0232 0.0046  -0.0549 173 HIS A CD2 
1355 C CE1 . HIS A 173 ? 0.4451 0.3587 0.4202 -0.0233 0.0105  -0.0614 173 HIS A CE1 
1356 N NE2 . HIS A 173 ? 0.4351 0.3642 0.4083 -0.0240 0.0057  -0.0629 173 HIS A NE2 
1357 N N   . PRO A 174 ? 0.4163 0.3557 0.4078 -0.0004 0.0206  -0.0397 174 PRO A N   
1358 C CA  . PRO A 174 ? 0.4261 0.3556 0.4165 0.0078  0.0253  -0.0391 174 PRO A CA  
1359 C C   . PRO A 174 ? 0.4478 0.3555 0.4339 0.0068  0.0265  -0.0416 174 PRO A C   
1360 O O   . PRO A 174 ? 0.5271 0.4248 0.5114 0.0152  0.0299  -0.0408 174 PRO A O   
1361 C CB  . PRO A 174 ? 0.4602 0.3928 0.4435 0.0136  0.0283  -0.0440 174 PRO A CB  
1362 C CG  . PRO A 174 ? 0.4654 0.4012 0.4409 0.0073  0.0247  -0.0488 174 PRO A CG  
1363 C CD  . PRO A 174 ? 0.4436 0.3887 0.4266 -0.0000 0.0195  -0.0445 174 PRO A CD  
1364 N N   . SER A 175 ? 0.4355 0.3350 0.4200 -0.0030 0.0239  -0.0445 175 SER A N   
1365 C CA  . SER A 175 ? 0.4542 0.3306 0.4345 -0.0052 0.0259  -0.0452 175 SER A CA  
1366 C C   . SER A 175 ? 0.4766 0.3520 0.4635 -0.0051 0.0274  -0.0360 175 SER A C   
1367 O O   . SER A 175 ? 0.5092 0.3633 0.4909 -0.0055 0.0300  -0.0345 175 SER A O   
1368 C CB  . SER A 175 ? 0.4524 0.3200 0.4294 -0.0179 0.0229  -0.0520 175 SER A CB  
1369 O OG  . SER A 175 ? 0.4742 0.3607 0.4621 -0.0265 0.0193  -0.0488 175 SER A OG  
1370 N N   . ILE A 176 ? 0.4110 0.3066 0.4069 -0.0047 0.0261  -0.0298 176 ILE A N   
1371 C CA  . ILE A 176 ? 0.3932 0.2882 0.3932 -0.0043 0.0276  -0.0213 176 ILE A CA  
1372 C C   . ILE A 176 ? 0.4273 0.3195 0.4251 0.0083  0.0291  -0.0174 176 ILE A C   
1373 O O   . ILE A 176 ? 0.4069 0.3138 0.4081 0.0148  0.0283  -0.0179 176 ILE A O   
1374 C CB  . ILE A 176 ? 0.3456 0.2623 0.3548 -0.0084 0.0255  -0.0174 176 ILE A CB  
1375 C CG1 . ILE A 176 ? 0.3890 0.3118 0.4024 -0.0196 0.0232  -0.0217 176 ILE A CG1 
1376 C CG2 . ILE A 176 ? 0.3578 0.2733 0.3688 -0.0072 0.0277  -0.0090 176 ILE A CG2 
1377 C CD1 . ILE A 176 ? 0.3682 0.3136 0.3900 -0.0212 0.0205  -0.0195 176 ILE A CD1 
1378 N N   . GLU A 177 ? 0.4195 0.2931 0.4116 0.0119  0.0313  -0.0131 177 GLU A N   
1379 C CA  . GLU A 177 ? 0.4251 0.2968 0.4154 0.0253  0.0315  -0.0097 177 GLU A CA  
1380 C C   . GLU A 177 ? 0.4172 0.3040 0.4128 0.0269  0.0296  -0.0023 177 GLU A C   
1381 O O   . GLU A 177 ? 0.4089 0.2863 0.4002 0.0251  0.0306  0.0039  177 GLU A O   
1382 C CB  . GLU A 177 ? 0.4864 0.3292 0.4655 0.0305  0.0340  -0.0084 177 GLU A CB  
1383 C CG  . GLU A 177 ? 0.5126 0.3399 0.4852 0.0304  0.0358  -0.0175 177 GLU A CG  
1384 C CD  . GLU A 177 ? 0.6188 0.4135 0.5784 0.0367  0.0386  -0.0172 177 GLU A CD  
1385 O OE1 . GLU A 177 ? 0.6500 0.4340 0.6039 0.0438  0.0401  -0.0241 177 GLU A OE1 
1386 O OE2 . GLU A 177 ? 0.6552 0.4332 0.6086 0.0348  0.0398  -0.0102 177 GLU A OE2 
1387 N N   . ALA A 178 ? 0.3625 0.2714 0.3659 0.0295  0.0274  -0.0030 178 ALA A N   
1388 C CA  . ALA A 178 ? 0.3148 0.2376 0.3224 0.0290  0.0253  0.0024  178 ALA A CA  
1389 C C   . ALA A 178 ? 0.3361 0.2785 0.3509 0.0343  0.0232  0.0010  178 ALA A C   
1390 O O   . ALA A 178 ? 0.3470 0.2945 0.3646 0.0369  0.0242  -0.0040 178 ALA A O   
1391 C CB  . ALA A 178 ? 0.3178 0.2471 0.3280 0.0182  0.0256  0.0028  178 ALA A CB  
1392 N N   . MET A 179 ? 0.3083 0.2615 0.3257 0.0350  0.0207  0.0052  179 MET A N   
1393 C CA  . MET A 179 ? 0.2797 0.2517 0.3046 0.0365  0.0187  0.0038  179 MET A CA  
1394 C C   . MET A 179 ? 0.2967 0.2757 0.3216 0.0303  0.0172  0.0064  179 MET A C   
1395 O O   . MET A 179 ? 0.3014 0.2727 0.3211 0.0280  0.0175  0.0100  179 MET A O   
1396 C CB  . MET A 179 ? 0.2899 0.2681 0.3182 0.0463  0.0159  0.0052  179 MET A CB  
1397 C CG  . MET A 179 ? 0.2728 0.2453 0.2950 0.0494  0.0125  0.0112  179 MET A CG  
1398 S SD  . MET A 179 ? 0.3232 0.3022 0.3483 0.0628  0.0074  0.0129  179 MET A SD  
1399 C CE  . MET A 179 ? 0.2882 0.2530 0.2990 0.0645  0.0044  0.0205  179 MET A CE  
1400 N N   . GLN A 180 ? 0.2694 0.2618 0.2991 0.0276  0.0165  0.0044  180 GLN A N   
1401 C CA  . GLN A 180 ? 0.2569 0.2531 0.2851 0.0222  0.0157  0.0060  180 GLN A CA  
1402 C C   . GLN A 180 ? 0.2378 0.2449 0.2691 0.0226  0.0130  0.0061  180 GLN A C   
1403 O O   . GLN A 180 ? 0.2612 0.2774 0.2982 0.0226  0.0136  0.0034  180 GLN A O   
1404 C CB  . GLN A 180 ? 0.2627 0.2603 0.2908 0.0168  0.0174  0.0035  180 GLN A CB  
1405 C CG  . GLN A 180 ? 0.2280 0.2287 0.2541 0.0133  0.0166  0.0052  180 GLN A CG  
1406 C CD  . GLN A 180 ? 0.2721 0.2736 0.2973 0.0097  0.0172  0.0036  180 GLN A CD  
1407 O OE1 . GLN A 180 ? 0.2933 0.2966 0.3169 0.0084  0.0166  0.0050  180 GLN A OE1 
1408 N NE2 . GLN A 180 ? 0.2707 0.2709 0.2959 0.0089  0.0180  0.0004  180 GLN A NE2 
1409 N N   . LEU A 181 ? 0.2580 0.2641 0.2851 0.0223  0.0107  0.0088  181 LEU A N   
1410 C CA  . LEU A 181 ? 0.2557 0.2704 0.2844 0.0215  0.0073  0.0081  181 LEU A CA  
1411 C C   . LEU A 181 ? 0.2773 0.2912 0.3027 0.0157  0.0082  0.0075  181 LEU A C   
1412 O O   . LEU A 181 ? 0.2750 0.2820 0.2940 0.0151  0.0091  0.0092  181 LEU A O   
1413 C CB  . LEU A 181 ? 0.2615 0.2734 0.2846 0.0258  0.0032  0.0109  181 LEU A CB  
1414 C CG  . LEU A 181 ? 0.2860 0.3070 0.3102 0.0249  -0.0020 0.0093  181 LEU A CG  
1415 C CD1 . LEU A 181 ? 0.2632 0.2992 0.2999 0.0270  -0.0043 0.0066  181 LEU A CD1 
1416 C CD2 . LEU A 181 ? 0.2660 0.2810 0.2793 0.0289  -0.0061 0.0122  181 LEU A CD2 
1417 N N   . THR A 182 ? 0.2481 0.2687 0.2772 0.0119  0.0082  0.0051  182 THR A N   
1418 C CA  . THR A 182 ? 0.2438 0.2602 0.2674 0.0072  0.0088  0.0049  182 THR A CA  
1419 C C   . THR A 182 ? 0.2845 0.3049 0.3084 0.0036  0.0057  0.0032  182 THR A C   
1420 O O   . THR A 182 ? 0.2761 0.3075 0.3085 0.0029  0.0039  0.0014  182 THR A O   
1421 C CB  . THR A 182 ? 0.2653 0.2812 0.2891 0.0041  0.0125  0.0041  182 THR A CB  
1422 O OG1 . THR A 182 ? 0.2557 0.2807 0.2871 0.0030  0.0140  0.0022  182 THR A OG1 
1423 C CG2 . THR A 182 ? 0.2516 0.2630 0.2735 0.0065  0.0142  0.0050  182 THR A CG2 
1424 N N   . GLU A 183 ? 0.2846 0.2964 0.2996 0.0013  0.0051  0.0032  183 GLU A N   
1425 C CA  . GLU A 183 ? 0.2816 0.2935 0.2945 -0.0039 0.0021  0.0007  183 GLU A CA  
1426 C C   . GLU A 183 ? 0.3124 0.3238 0.3269 -0.0112 0.0049  -0.0007 183 GLU A C   
1427 O O   . GLU A 183 ? 0.2826 0.2877 0.2937 -0.0115 0.0091  0.0010  183 GLU A O   
1428 C CB  . GLU A 183 ? 0.3439 0.3431 0.3437 -0.0028 0.0009  0.0007  183 GLU A CB  
1429 C CG  . GLU A 183 ? 0.3248 0.3227 0.3201 0.0037  -0.0005 0.0026  183 GLU A CG  
1430 C CD  . GLU A 183 ? 0.3687 0.3550 0.3501 0.0053  -0.0007 0.0020  183 GLU A CD  
1431 O OE1 . GLU A 183 ? 0.3742 0.3515 0.3495 0.0024  0.0006  0.0003  183 GLU A OE1 
1432 O OE2 . GLU A 183 ? 0.3539 0.3386 0.3292 0.0099  -0.0015 0.0036  183 GLU A OE2 
1433 N N   . MET A 184 ? 0.2895 0.3070 0.3083 -0.0179 0.0024  -0.0037 184 MET A N   
1434 C CA  . MET A 184 ? 0.3011 0.3136 0.3181 -0.0270 0.0056  -0.0048 184 MET A CA  
1435 C C   . MET A 184 ? 0.3212 0.3223 0.3283 -0.0319 0.0019  -0.0074 184 MET A C   
1436 O O   . MET A 184 ? 0.3106 0.3211 0.3231 -0.0357 -0.0034 -0.0110 184 MET A O   
1437 C CB  . MET A 184 ? 0.2924 0.3227 0.3245 -0.0332 0.0072  -0.0066 184 MET A CB  
1438 C CG  . MET A 184 ? 0.3340 0.3773 0.3764 -0.0272 0.0102  -0.0054 184 MET A CG  
1439 S SD  . MET A 184 ? 0.3961 0.4621 0.4568 -0.0346 0.0134  -0.0083 184 MET A SD  
1440 C CE  . MET A 184 ? 0.3166 0.3927 0.3849 -0.0231 0.0158  -0.0072 184 MET A CE  
1441 N N   . ALA A 185 ? 0.3039 0.2850 0.2963 -0.0310 0.0041  -0.0062 185 ALA A N   
1442 C CA  . ALA A 185 ? 0.3047 0.2698 0.2848 -0.0364 0.0021  -0.0093 185 ALA A CA  
1443 C C   . ALA A 185 ? 0.3080 0.2769 0.2860 -0.0349 -0.0048 -0.0131 185 ALA A C   
1444 O O   . ALA A 185 ? 0.3160 0.2881 0.2955 -0.0429 -0.0093 -0.0177 185 ALA A O   
1445 C CB  . ALA A 185 ? 0.3333 0.2963 0.3159 -0.0493 0.0042  -0.0113 185 ALA A CB  
1446 N N   . SER A 186 ? 0.2947 0.2630 0.2681 -0.0249 -0.0056 -0.0112 186 SER A N   
1447 C CA  A SER A 186 ? 0.3128 0.2807 0.2790 -0.0226 -0.0115 -0.0141 186 SER A CA  
1448 C CA  B SER A 186 ? 0.3184 0.2862 0.2846 -0.0224 -0.0114 -0.0141 186 SER A CA  
1449 C C   . SER A 186 ? 0.3579 0.3043 0.3060 -0.0246 -0.0117 -0.0177 186 SER A C   
1450 O O   . SER A 186 ? 0.3743 0.3051 0.3134 -0.0217 -0.0065 -0.0160 186 SER A O   
1451 C CB  A SER A 186 ? 0.3216 0.2924 0.2858 -0.0119 -0.0106 -0.0104 186 SER A CB  
1452 C CB  B SER A 186 ? 0.3201 0.2915 0.2850 -0.0117 -0.0105 -0.0102 186 SER A CB  
1453 O OG  A SER A 186 ? 0.3479 0.3061 0.3043 -0.0072 -0.0048 -0.0080 186 SER A OG  
1454 O OG  B SER A 186 ? 0.3251 0.2876 0.2754 -0.0076 -0.0129 -0.0118 186 SER A OG  
1455 N N   . ILE A 187 ? 0.3671 0.3124 0.3088 -0.0289 -0.0182 -0.0231 187 ILE A N   
1456 C CA  . ILE A 187 ? 0.4024 0.3251 0.3238 -0.0294 -0.0186 -0.0274 187 ILE A CA  
1457 C C   . ILE A 187 ? 0.4562 0.3742 0.3659 -0.0173 -0.0171 -0.0255 187 ILE A C   
1458 O O   . ILE A 187 ? 0.4635 0.3953 0.3775 -0.0123 -0.0197 -0.0233 187 ILE A O   
1459 C CB  . ILE A 187 ? 0.4245 0.3467 0.3422 -0.0399 -0.0266 -0.0350 187 ILE A CB  
1460 C CG1 . ILE A 187 ? 0.4136 0.3077 0.3083 -0.0415 -0.0261 -0.0404 187 ILE A CG1 
1461 C CG2 . ILE A 187 ? 0.4718 0.4125 0.3933 -0.0368 -0.0350 -0.0365 187 ILE A CG2 
1462 C CD1 . ILE A 187 ? 0.4036 0.2934 0.2919 -0.0535 -0.0344 -0.0493 187 ILE A CD1 
1463 N N   . ASN A 188 ? 0.4352 0.3339 0.3299 -0.0120 -0.0121 -0.0259 188 ASN A N   
1464 C CA  . ASN A 188 ? 0.5330 0.4282 0.4158 -0.0016 -0.0099 -0.0251 188 ASN A CA  
1465 C C   . ASN A 188 ? 0.5495 0.4213 0.4102 -0.0003 -0.0093 -0.0310 188 ASN A C   
1466 O O   . ASN A 188 ? 0.5417 0.3972 0.3967 0.0003  -0.0050 -0.0316 188 ASN A O   
1467 C CB  . ASN A 188 ? 0.5762 0.4769 0.4660 0.0075  -0.0023 -0.0185 188 ASN A CB  
1468 C CG  . ASN A 188 ? 0.5580 0.4794 0.4641 0.0086  -0.0029 -0.0133 188 ASN A CG  
1469 O OD1 . ASN A 188 ? 0.5406 0.4670 0.4437 0.0143  -0.0018 -0.0109 188 ASN A OD1 
1470 N ND2 . ASN A 188 ? 0.5163 0.4477 0.4380 0.0035  -0.0037 -0.0115 188 ASN A ND2 
1471 N N   . ASN A 189 ? 0.5603 0.4287 0.4065 0.0007  -0.0137 -0.0353 189 ASN A N   
1472 C CA  . ASN A 189 ? 0.5923 0.4369 0.4149 0.0031  -0.0126 -0.0418 189 ASN A CA  
1473 C C   . ASN A 189 ? 0.5670 0.4130 0.3743 0.0092  -0.0146 -0.0434 189 ASN A C   
1474 O O   . ASN A 189 ? 0.4764 0.3392 0.2913 0.0139  -0.0140 -0.0377 189 ASN A O   
1475 C CB  . ASN A 189 ? 0.6298 0.4597 0.4463 -0.0093 -0.0184 -0.0492 189 ASN A CB  
1476 C CG  . ASN A 189 ? 0.6707 0.5159 0.4944 -0.0200 -0.0292 -0.0531 189 ASN A CG  
1477 O OD1 . ASN A 189 ? 0.7017 0.5637 0.5282 -0.0159 -0.0334 -0.0511 189 ASN A OD1 
1478 N ND2 . ASN A 189 ? 0.6455 0.4848 0.4718 -0.0335 -0.0338 -0.0585 189 ASN A ND2 
1479 N N   . ARG A 190 ? 0.6876 0.5143 0.4716 0.0089  -0.0169 -0.0513 190 ARG A N   
1480 C CA  . ARG A 190 ? 0.7403 0.5650 0.5049 0.0158  -0.0177 -0.0531 190 ARG A CA  
1481 C C   . ARG A 190 ? 0.7207 0.5645 0.4910 0.0122  -0.0274 -0.0515 190 ARG A C   
1482 O O   . ARG A 190 ? 0.7477 0.5964 0.5082 0.0196  -0.0264 -0.0483 190 ARG A O   
1483 C CB  . ARG A 190 ? 0.8205 0.6189 0.5571 0.0150  -0.0197 -0.0634 190 ARG A CB  
1484 C CG  . ARG A 190 ? 0.9050 0.6916 0.6170 0.0270  -0.0130 -0.0651 190 ARG A CG  
1485 C CD  . ARG A 190 ? 0.9877 0.7492 0.6707 0.0238  -0.0184 -0.0770 190 ARG A CD  
1486 N NE  . ARG A 190 ? 1.0376 0.7762 0.7169 0.0194  -0.0167 -0.0828 190 ARG A NE  
1487 C CZ  . ARG A 190 ? 1.0685 0.8025 0.7552 0.0051  -0.0248 -0.0872 190 ARG A CZ  
1488 N NH1 . ARG A 190 ? 1.0914 0.8003 0.7715 0.0019  -0.0216 -0.0915 190 ARG A NH1 
1489 N NH2 . ARG A 190 ? 1.0675 0.8218 0.7684 -0.0059 -0.0356 -0.0872 190 ARG A NH2 
1490 N N   . VAL A 191 ? 0.6550 0.5099 0.4408 0.0013  -0.0363 -0.0536 191 VAL A N   
1491 C CA  . VAL A 191 ? 0.7023 0.5765 0.4943 -0.0014 -0.0470 -0.0531 191 VAL A CA  
1492 C C   . VAL A 191 ? 0.6499 0.5464 0.4666 0.0015  -0.0449 -0.0437 191 VAL A C   
1493 O O   . VAL A 191 ? 0.5833 0.4917 0.3998 0.0068  -0.0489 -0.0395 191 VAL A O   
1494 C CB  . VAL A 191 ? 0.7756 0.6522 0.5716 -0.0150 -0.0586 -0.0619 191 VAL A CB  
1495 C CG1 . VAL A 191 ? 0.7638 0.6647 0.5697 -0.0163 -0.0706 -0.0614 191 VAL A CG1 
1496 C CG2 . VAL A 191 ? 0.8395 0.6912 0.6076 -0.0181 -0.0616 -0.0723 191 VAL A CG2 
1497 N N   . TYR A 192 ? 0.6399 0.5402 0.4760 -0.0017 -0.0388 -0.0403 192 TYR A N   
1498 C CA  . TYR A 192 ? 0.5916 0.5119 0.4515 -0.0009 -0.0375 -0.0332 192 TYR A CA  
1499 C C   . TYR A 192 ? 0.5934 0.5115 0.4578 0.0068  -0.0260 -0.0259 192 TYR A C   
1500 O O   . TYR A 192 ? 0.6342 0.5389 0.4933 0.0081  -0.0191 -0.0268 192 TYR A O   
1501 C CB  . TYR A 192 ? 0.5882 0.5174 0.4676 -0.0119 -0.0404 -0.0356 192 TYR A CB  
1502 C CG  . TYR A 192 ? 0.6048 0.5381 0.4832 -0.0222 -0.0514 -0.0438 192 TYR A CG  
1503 C CD1 . TYR A 192 ? 0.6160 0.5678 0.4990 -0.0213 -0.0616 -0.0447 192 TYR A CD1 
1504 C CD2 . TYR A 192 ? 0.6231 0.5418 0.4961 -0.0329 -0.0518 -0.0507 192 TYR A CD2 
1505 C CE1 . TYR A 192 ? 0.6168 0.5762 0.5011 -0.0312 -0.0730 -0.0529 192 TYR A CE1 
1506 C CE2 . TYR A 192 ? 0.6655 0.5891 0.5392 -0.0444 -0.0621 -0.0589 192 TYR A CE2 
1507 C CZ  . TYR A 192 ? 0.6675 0.6134 0.5478 -0.0436 -0.0731 -0.0603 192 TYR A CZ  
1508 O OH  . TYR A 192 ? 0.7096 0.6634 0.5925 -0.0555 -0.0843 -0.0693 192 TYR A OH  
1509 N N   . ARG A 193 ? 0.5345 0.4659 0.4093 0.0119  -0.0244 -0.0190 193 ARG A N   
1510 C CA  . ARG A 193 ? 0.4896 0.4209 0.3695 0.0180  -0.0143 -0.0126 193 ARG A CA  
1511 C C   . ARG A 193 ? 0.4272 0.3738 0.3264 0.0183  -0.0140 -0.0069 193 ARG A C   
1512 O O   . ARG A 193 ? 0.4375 0.3914 0.3369 0.0208  -0.0186 -0.0044 193 ARG A O   
1513 C CB  . ARG A 193 ? 0.5222 0.4461 0.3845 0.0258  -0.0094 -0.0102 193 ARG A CB  
1514 C CG  . ARG A 193 ? 0.5887 0.5151 0.4580 0.0307  0.0013  -0.0040 193 ARG A CG  
1515 C CD  . ARG A 193 ? 0.6723 0.5881 0.5320 0.0350  0.0096  -0.0061 193 ARG A CD  
1516 N NE  . ARG A 193 ? 0.7403 0.6511 0.6062 0.0321  0.0094  -0.0099 193 ARG A NE  
1517 C CZ  . ARG A 193 ? 0.7799 0.6951 0.6595 0.0334  0.0146  -0.0073 193 ARG A CZ  
1518 N NH1 . ARG A 193 ? 0.7867 0.7132 0.6775 0.0363  0.0203  -0.0018 193 ARG A NH1 
1519 N NH2 . ARG A 193 ? 0.8084 0.7159 0.6894 0.0313  0.0138  -0.0103 193 ARG A NH2 
1520 N N   . THR A 194 ? 0.3613 0.3114 0.2748 0.0169  -0.0086 -0.0047 194 THR A N   
1521 C CA  . THR A 194 ? 0.3679 0.3297 0.2971 0.0178  -0.0073 0.0002  194 THR A CA  
1522 C C   . THR A 194 ? 0.3804 0.3406 0.3133 0.0211  0.0015  0.0041  194 THR A C   
1523 O O   . THR A 194 ? 0.3525 0.3051 0.2785 0.0230  0.0061  0.0030  194 THR A O   
1524 C CB  . THR A 194 ? 0.3907 0.3624 0.3361 0.0118  -0.0106 -0.0016 194 THR A CB  
1525 O OG1 . THR A 194 ? 0.3989 0.3647 0.3464 0.0084  -0.0065 -0.0030 194 THR A OG1 
1526 C CG2 . THR A 194 ? 0.3997 0.3765 0.3441 0.0074  -0.0195 -0.0063 194 THR A CG2 
1527 N N   . ILE A 195 ? 0.3560 0.3237 0.3000 0.0220  0.0034  0.0083  195 ILE A N   
1528 C CA  . ILE A 195 ? 0.3428 0.3113 0.2919 0.0238  0.0108  0.0115  195 ILE A CA  
1529 C C   . ILE A 195 ? 0.3531 0.3231 0.3106 0.0216  0.0127  0.0097  195 ILE A C   
1530 O O   . ILE A 195 ? 0.3932 0.3628 0.3514 0.0240  0.0178  0.0105  195 ILE A O   
1531 C CB  . ILE A 195 ? 0.3411 0.3143 0.2981 0.0243  0.0119  0.0157  195 ILE A CB  
1532 C CG1 . ILE A 195 ? 0.3326 0.3069 0.2944 0.0245  0.0196  0.0186  195 ILE A CG1 
1533 C CG2 . ILE A 195 ? 0.3290 0.3094 0.2992 0.0215  0.0083  0.0145  195 ILE A CG2 
1534 C CD1 . ILE A 195 ? 0.3668 0.3362 0.3170 0.0274  0.0255  0.0207  195 ILE A CD1 
1535 N N   . GLY A 196 ? 0.3268 0.2990 0.2901 0.0175  0.0088  0.0073  196 GLY A N   
1536 C CA  . GLY A 196 ? 0.3125 0.2839 0.2807 0.0158  0.0106  0.0065  196 GLY A CA  
1537 C C   . GLY A 196 ? 0.3433 0.3229 0.3236 0.0154  0.0125  0.0087  196 GLY A C   
1538 O O   . GLY A 196 ? 0.3521 0.3350 0.3386 0.0122  0.0112  0.0080  196 GLY A O   
1539 N N   . SER A 197 ? 0.3373 0.3201 0.3203 0.0181  0.0159  0.0111  197 SER A N   
1540 C CA  . SER A 197 ? 0.3181 0.3075 0.3114 0.0171  0.0175  0.0123  197 SER A CA  
1541 C C   . SER A 197 ? 0.2871 0.2795 0.2860 0.0149  0.0152  0.0123  197 SER A C   
1542 O O   . SER A 197 ? 0.2762 0.2675 0.2723 0.0157  0.0131  0.0128  197 SER A O   
1543 C CB  . SER A 197 ? 0.3093 0.3015 0.3048 0.0186  0.0219  0.0146  197 SER A CB  
1544 O OG  . SER A 197 ? 0.3064 0.2974 0.2968 0.0220  0.0248  0.0145  197 SER A OG  
1545 N N   . PRO A 198 ? 0.2820 0.2784 0.2881 0.0131  0.0154  0.0116  198 PRO A N   
1546 C CA  . PRO A 198 ? 0.2746 0.2732 0.2859 0.0126  0.0146  0.0113  198 PRO A CA  
1547 C C   . PRO A 198 ? 0.2738 0.2691 0.2845 0.0140  0.0163  0.0138  198 PRO A C   
1548 O O   . PRO A 198 ? 0.2754 0.2695 0.2851 0.0135  0.0193  0.0153  198 PRO A O   
1549 C CB  . PRO A 198 ? 0.2752 0.2767 0.2913 0.0107  0.0154  0.0096  198 PRO A CB  
1550 C CG  . PRO A 198 ? 0.2765 0.2774 0.2889 0.0104  0.0153  0.0092  198 PRO A CG  
1551 C CD  . PRO A 198 ? 0.2678 0.2663 0.2763 0.0127  0.0163  0.0108  198 PRO A CD  
1552 N N   . LEU A 199 ? 0.2617 0.2553 0.2729 0.0159  0.0148  0.0144  199 LEU A N   
1553 C CA  . LEU A 199 ? 0.2606 0.2469 0.2683 0.0177  0.0165  0.0176  199 LEU A CA  
1554 C C   . LEU A 199 ? 0.2810 0.2644 0.2933 0.0179  0.0170  0.0164  199 LEU A C   
1555 O O   . LEU A 199 ? 0.3100 0.2978 0.3264 0.0200  0.0148  0.0141  199 LEU A O   
1556 C CB  . LEU A 199 ? 0.2543 0.2373 0.2541 0.0222  0.0135  0.0201  199 LEU A CB  
1557 C CG  . LEU A 199 ? 0.2691 0.2528 0.2614 0.0224  0.0123  0.0202  199 LEU A CG  
1558 C CD1 . LEU A 199 ? 0.2708 0.2502 0.2532 0.0274  0.0084  0.0228  199 LEU A CD1 
1559 C CD2 . LEU A 199 ? 0.2891 0.2696 0.2780 0.0204  0.0179  0.0219  199 LEU A CD2 
1560 N N   . VAL A 200 ? 0.2761 0.2521 0.2879 0.0155  0.0205  0.0178  200 VAL A N   
1561 C CA  . VAL A 200 ? 0.2668 0.2366 0.2810 0.0151  0.0213  0.0158  200 VAL A CA  
1562 C C   . VAL A 200 ? 0.2977 0.2531 0.3048 0.0179  0.0230  0.0199  200 VAL A C   
1563 O O   . VAL A 200 ? 0.3197 0.2686 0.3218 0.0150  0.0263  0.0238  200 VAL A O   
1564 C CB  . VAL A 200 ? 0.2771 0.2487 0.2963 0.0085  0.0233  0.0127  200 VAL A CB  
1565 C CG1 . VAL A 200 ? 0.3065 0.2676 0.3253 0.0074  0.0244  0.0101  200 VAL A CG1 
1566 C CG2 . VAL A 200 ? 0.2794 0.2626 0.3029 0.0078  0.0210  0.0092  200 VAL A CG2 
1567 N N   . PHE A 201 ? 0.3209 0.2710 0.3267 0.0241  0.0210  0.0193  201 PHE A N   
1568 C CA  . PHE A 201 ? 0.3487 0.2837 0.3455 0.0298  0.0213  0.0239  201 PHE A CA  
1569 C C   . PHE A 201 ? 0.3441 0.2645 0.3396 0.0300  0.0237  0.0219  201 PHE A C   
1570 O O   . PHE A 201 ? 0.3566 0.2823 0.3583 0.0310  0.0229  0.0164  201 PHE A O   
1571 C CB  . PHE A 201 ? 0.3303 0.2717 0.3265 0.0395  0.0159  0.0249  201 PHE A CB  
1572 C CG  . PHE A 201 ? 0.3212 0.2748 0.3169 0.0391  0.0126  0.0259  201 PHE A CG  
1573 C CD1 . PHE A 201 ? 0.3426 0.2888 0.3266 0.0409  0.0122  0.0312  201 PHE A CD1 
1574 C CD2 . PHE A 201 ? 0.2822 0.2525 0.2871 0.0369  0.0102  0.0214  201 PHE A CD2 
1575 C CE1 . PHE A 201 ? 0.3497 0.3052 0.3310 0.0405  0.0091  0.0312  201 PHE A CE1 
1576 C CE2 . PHE A 201 ? 0.2961 0.2745 0.2991 0.0357  0.0072  0.0216  201 PHE A CE2 
1577 C CZ  . PHE A 201 ? 0.3069 0.2780 0.2979 0.0378  0.0063  0.0261  201 PHE A CZ  
1578 N N   . PRO A 202 ? 0.3673 0.2672 0.3530 0.0294  0.0270  0.0261  202 PRO A N   
1579 C CA  . PRO A 202 ? 0.3867 0.2682 0.3689 0.0295  0.0294  0.0239  202 PRO A CA  
1580 C C   . PRO A 202 ? 0.4167 0.2893 0.3935 0.0429  0.0267  0.0252  202 PRO A C   
1581 O O   . PRO A 202 ? 0.3952 0.2781 0.3724 0.0514  0.0223  0.0278  202 PRO A O   
1582 C CB  . PRO A 202 ? 0.4157 0.2783 0.3890 0.0217  0.0348  0.0288  202 PRO A CB  
1583 C CG  . PRO A 202 ? 0.4235 0.2871 0.3887 0.0267  0.0341  0.0365  202 PRO A CG  
1584 C CD  . PRO A 202 ? 0.3616 0.2523 0.3371 0.0282  0.0295  0.0334  202 PRO A CD  
1585 N N   . LYS A 203 ? 0.4229 0.2764 0.3948 0.0451  0.0289  0.0227  203 LYS A N   
1586 C CA  . LYS A 203 ? 0.4737 0.3160 0.4396 0.0597  0.0269  0.0241  203 LYS A CA  
1587 C C   . LYS A 203 ? 0.5056 0.3358 0.4590 0.0663  0.0255  0.0335  203 LYS A C   
1588 O O   . LYS A 203 ? 0.5203 0.3400 0.4656 0.0581  0.0289  0.0387  203 LYS A O   
1589 C CB  A LYS A 203 ? 0.5181 0.3355 0.4770 0.0605  0.0306  0.0200  203 LYS A CB  
1590 C CB  B LYS A 203 ? 0.5187 0.3346 0.4767 0.0603  0.0307  0.0207  203 LYS A CB  
1591 C CG  A LYS A 203 ? 0.5240 0.3453 0.4866 0.0747  0.0288  0.0151  203 LYS A CG  
1592 C CG  B LYS A 203 ? 0.5004 0.3232 0.4661 0.0554  0.0321  0.0110  203 LYS A CG  
1593 C CD  A LYS A 203 ? 0.5719 0.3636 0.5240 0.0780  0.0326  0.0112  203 LYS A CD  
1594 C CD  B LYS A 203 ? 0.5377 0.3307 0.4923 0.0597  0.0352  0.0077  203 LYS A CD  
1595 C CE  A LYS A 203 ? 0.6002 0.4005 0.5580 0.0920  0.0319  0.0049  203 LYS A CE  
1596 C CE  B LYS A 203 ? 0.5609 0.3229 0.5015 0.0522  0.0390  0.0129  203 LYS A CE  
1597 N NZ  A LYS A 203 ? 0.6645 0.4396 0.6132 0.0920  0.0363  -0.0022 203 LYS A NZ  
1598 N NZ  B LYS A 203 ? 0.6334 0.3611 0.5604 0.0570  0.0420  0.0100  203 LYS A NZ  
1599 N N   . HIS A 204 ? 0.5292 0.3627 0.4813 0.0817  0.0204  0.0355  204 HIS A N   
1600 C CA  . HIS A 204 ? 0.5574 0.3800 0.4959 0.0916  0.0171  0.0442  204 HIS A CA  
1601 C C   . HIS A 204 ? 0.5321 0.3730 0.4711 0.0888  0.0132  0.0479  204 HIS A C   
1602 O O   . HIS A 204 ? 0.6017 0.4376 0.5293 0.0979  0.0089  0.0545  204 HIS A O   
1603 C CB  . HIS A 204 ? 0.6265 0.4122 0.5452 0.0891  0.0228  0.0508  204 HIS A CB  
1604 C CG  . HIS A 204 ? 0.6668 0.4290 0.5819 0.0900  0.0271  0.0467  204 HIS A CG  
1605 N ND1 . HIS A 204 ? 0.7041 0.4595 0.6180 0.1062  0.0242  0.0448  204 HIS A ND1 
1606 C CD2 . HIS A 204 ? 0.6870 0.4307 0.5992 0.0769  0.0338  0.0436  204 HIS A CD2 
1607 C CE1 . HIS A 204 ? 0.7072 0.4381 0.6154 0.1034  0.0295  0.0405  204 HIS A CE1 
1608 N NE2 . HIS A 204 ? 0.7044 0.4278 0.6115 0.0849  0.0349  0.0396  204 HIS A NE2 
1609 N N   . HIS A 205 ? 0.4605 0.3211 0.4107 0.0771  0.0144  0.0438  205 HIS A N   
1610 C CA  . HIS A 205 ? 0.3764 0.2553 0.3277 0.0764  0.0100  0.0456  205 HIS A CA  
1611 C C   . HIS A 205 ? 0.4029 0.3060 0.3668 0.0850  0.0022  0.0414  205 HIS A C   
1612 O O   . HIS A 205 ? 0.4075 0.3227 0.3854 0.0851  0.0026  0.0350  205 HIS A O   
1613 C CB  . HIS A 205 ? 0.3971 0.2870 0.3550 0.0623  0.0139  0.0428  205 HIS A CB  
1614 C CG  . HIS A 205 ? 0.4224 0.2953 0.3686 0.0541  0.0207  0.0481  205 HIS A CG  
1615 N ND1 . HIS A 205 ? 0.4212 0.3036 0.3688 0.0453  0.0236  0.0482  205 HIS A ND1 
1616 C CD2 . HIS A 205 ? 0.4652 0.3121 0.3984 0.0532  0.0260  0.0534  205 HIS A CD2 
1617 C CE1 . HIS A 205 ? 0.4660 0.3320 0.4037 0.0392  0.0307  0.0533  205 HIS A CE1 
1618 N NE2 . HIS A 205 ? 0.4928 0.3362 0.4211 0.0430  0.0324  0.0567  205 HIS A NE2 
1619 N N   . VAL A 206 ? 0.3970 0.3083 0.3560 0.0916  -0.0047 0.0446  206 VAL A N   
1620 C CA  . VAL A 206 ? 0.4081 0.3448 0.3804 0.0985  -0.0126 0.0405  206 VAL A CA  
1621 C C   . VAL A 206 ? 0.3959 0.3502 0.3711 0.0907  -0.0161 0.0386  206 VAL A C   
1622 O O   . VAL A 206 ? 0.4318 0.3781 0.3922 0.0899  -0.0176 0.0432  206 VAL A O   
1623 C CB  . VAL A 206 ? 0.4602 0.3935 0.4254 0.1150  -0.0201 0.0449  206 VAL A CB  
1624 C CG1 . VAL A 206 ? 0.4771 0.4419 0.4603 0.1211  -0.0286 0.0397  206 VAL A CG1 
1625 C CG2 . VAL A 206 ? 0.4568 0.3675 0.4160 0.1237  -0.0161 0.0471  206 VAL A CG2 
1626 N N   . VAL A 207 ? 0.3503 0.3270 0.3429 0.0856  -0.0172 0.0319  207 VAL A N   
1627 C CA  . VAL A 207 ? 0.3462 0.3387 0.3423 0.0781  -0.0208 0.0290  207 VAL A CA  
1628 C C   . VAL A 207 ? 0.3597 0.3749 0.3674 0.0843  -0.0297 0.0258  207 VAL A C   
1629 O O   . VAL A 207 ? 0.3592 0.3890 0.3834 0.0869  -0.0293 0.0217  207 VAL A O   
1630 C CB  . VAL A 207 ? 0.3555 0.3544 0.3614 0.0662  -0.0148 0.0241  207 VAL A CB  
1631 C CG1 . VAL A 207 ? 0.3714 0.3833 0.3790 0.0593  -0.0187 0.0211  207 VAL A CG1 
1632 C CG2 . VAL A 207 ? 0.3588 0.3392 0.3560 0.0602  -0.0069 0.0267  207 VAL A CG2 
1633 N N   . SER A 208 ? 0.3181 0.3378 0.3176 0.0865  -0.0376 0.0271  208 SER A N   
1634 C CA  . SER A 208 ? 0.3654 0.4080 0.3752 0.0923  -0.0481 0.0241  208 SER A CA  
1635 C C   . SER A 208 ? 0.4054 0.4623 0.4195 0.0808  -0.0516 0.0188  208 SER A C   
1636 O O   . SER A 208 ? 0.4277 0.4721 0.4256 0.0757  -0.0512 0.0202  208 SER A O   
1637 C CB  . SER A 208 ? 0.4113 0.4458 0.4051 0.1054  -0.0564 0.0300  208 SER A CB  
1638 O OG  . SER A 208 ? 0.4720 0.5305 0.4739 0.1092  -0.0684 0.0264  208 SER A OG  
1639 N N   . LEU A 209 ? 0.3392 0.4206 0.3741 0.0765  -0.0540 0.0125  209 LEU A N   
1640 C CA  . LEU A 209 ? 0.3249 0.4199 0.3648 0.0652  -0.0580 0.0069  209 LEU A CA  
1641 C C   . LEU A 209 ? 0.3777 0.4941 0.4241 0.0707  -0.0711 0.0044  209 LEU A C   
1642 O O   . LEU A 209 ? 0.4160 0.5526 0.4802 0.0780  -0.0743 0.0029  209 LEU A O   
1643 C CB  . LEU A 209 ? 0.3144 0.4223 0.3730 0.0545  -0.0513 0.0018  209 LEU A CB  
1644 C CG  . LEU A 209 ? 0.3328 0.4237 0.3876 0.0500  -0.0396 0.0035  209 LEU A CG  
1645 C CD1 . LEU A 209 ? 0.3857 0.4891 0.4558 0.0395  -0.0341 -0.0013 209 LEU A CD1 
1646 C CD2 . LEU A 209 ? 0.3129 0.3813 0.3476 0.0458  -0.0369 0.0064  209 LEU A CD2 
1647 N N   . GLN A 210 ? 0.3544 0.4677 0.3868 0.0674  -0.0787 0.0032  210 GLN A N   
1648 C CA  . GLN A 210 ? 0.3929 0.5250 0.4277 0.0725  -0.0929 0.0006  210 GLN A CA  
1649 C C   . GLN A 210 ? 0.4128 0.5578 0.4528 0.0581  -0.0982 -0.0075 210 GLN A C   
1650 O O   . GLN A 210 ? 0.4040 0.5308 0.4276 0.0492  -0.0949 -0.0085 210 GLN A O   
1651 C CB  . GLN A 210 ? 0.4259 0.5387 0.4332 0.0842  -0.0989 0.0071  210 GLN A CB  
1652 C CG  . GLN A 210 ? 0.4334 0.5295 0.4345 0.0972  -0.0925 0.0154  210 GLN A CG  
1653 C CD  . GLN A 210 ? 0.4713 0.5429 0.4426 0.1075  -0.0952 0.0235  210 GLN A CD  
1654 O OE1 . GLN A 210 ? 0.4449 0.5141 0.3991 0.1073  -0.1032 0.0231  210 GLN A OE1 
1655 N NE2 . GLN A 210 ? 0.4920 0.5434 0.4552 0.1159  -0.0878 0.0309  210 GLN A NE2 
1656 N N   . PRO A 211 ? 0.4559 0.6319 0.5186 0.0553  -0.1063 -0.0136 211 PRO A N   
1657 C CA  . PRO A 211 ? 0.4776 0.6656 0.5467 0.0393  -0.1110 -0.0220 211 PRO A CA  
1658 C C   . PRO A 211 ? 0.4856 0.6636 0.5314 0.0385  -0.1220 -0.0241 211 PRO A C   
1659 O O   . PRO A 211 ? 0.4913 0.6649 0.5217 0.0518  -0.1302 -0.0200 211 PRO A O   
1660 C CB  . PRO A 211 ? 0.5035 0.7308 0.6043 0.0389  -0.1178 -0.0273 211 PRO A CB  
1661 C CG  . PRO A 211 ? 0.5071 0.7384 0.6203 0.0517  -0.1098 -0.0219 211 PRO A CG  
1662 C CD  . PRO A 211 ? 0.5037 0.7063 0.5897 0.0659  -0.1100 -0.0136 211 PRO A CD  
1663 N N   . VAL A 212 ? 0.4827 0.6553 0.5238 0.0230  -0.1219 -0.0307 212 VAL A N   
1664 C CA  . VAL A 212 ? 0.5348 0.6949 0.5516 0.0202  -0.1310 -0.0343 212 VAL A CA  
1665 C C   . VAL A 212 ? 0.5764 0.7632 0.6069 0.0107  -0.1451 -0.0442 212 VAL A C   
1666 O O   . VAL A 212 ? 0.6487 0.8419 0.6677 0.0164  -0.1594 -0.0464 212 VAL A O   
1667 C CB  . VAL A 212 ? 0.5146 0.6436 0.5111 0.0109  -0.1206 -0.0349 212 VAL A CB  
1668 C CG1 . VAL A 212 ? 0.5395 0.6545 0.5094 0.0082  -0.1293 -0.0398 212 VAL A CG1 
1669 C CG2 . VAL A 212 ? 0.5107 0.6167 0.4952 0.0201  -0.1077 -0.0255 212 VAL A CG2 
1670 N N   . ASN A 213 ? 0.5639 0.7671 0.6187 -0.0043 -0.1415 -0.0502 213 ASN A N   
1671 C CA  . ASN A 213 ? 0.6135 0.8464 0.6868 -0.0154 -0.1541 -0.0600 213 ASN A CA  
1672 C C   . ASN A 213 ? 0.5577 0.8250 0.6694 -0.0194 -0.1504 -0.0614 213 ASN A C   
1673 O O   . ASN A 213 ? 0.5446 0.8436 0.6755 -0.0099 -0.1599 -0.0618 213 ASN A O   
1674 C CB  . ASN A 213 ? 0.6966 0.9129 0.7578 -0.0347 -0.1540 -0.0683 213 ASN A CB  
1675 C CG  . ASN A 213 ? 0.7841 0.9779 0.8109 -0.0313 -0.1634 -0.0707 213 ASN A CG  
1676 O OD1 . ASN A 213 ? 0.8244 1.0290 0.8433 -0.0199 -0.1770 -0.0705 213 ASN A OD1 
1677 N ND2 . ASN A 213 ? 0.8037 0.9654 0.8084 -0.0404 -0.1561 -0.0731 213 ASN A ND2 
1678 N N   . ASP A 214 ? 0.5245 0.7860 0.6467 -0.0327 -0.1366 -0.0621 214 ASP A N   
1679 C CA  . ASP A 214 ? 0.5178 0.8100 0.6744 -0.0370 -0.1305 -0.0630 214 ASP A CA  
1680 C C   . ASP A 214 ? 0.5081 0.8060 0.6715 -0.0171 -0.1254 -0.0548 214 ASP A C   
1681 O O   . ASP A 214 ? 0.5556 0.8244 0.6976 -0.0067 -0.1187 -0.0475 214 ASP A O   
1682 C CB  . ASP A 214 ? 0.5190 0.7966 0.6784 -0.0543 -0.1154 -0.0639 214 ASP A CB  
1683 C CG  . ASP A 214 ? 0.5307 0.8404 0.7246 -0.0618 -0.1081 -0.0657 214 ASP A CG  
1684 O OD1 . ASP A 214 ? 0.5299 0.8746 0.7477 -0.0524 -0.1138 -0.0664 214 ASP A OD1 
1685 O OD2 . ASP A 214 ? 0.5383 0.8375 0.7344 -0.0766 -0.0960 -0.0662 214 ASP A OD2 
1686 N N   . LYS A 215 ? 0.4621 0.7977 0.6558 -0.0119 -0.1285 -0.0565 215 LYS A N   
1687 C CA  . LYS A 215 ? 0.4640 0.8047 0.6637 0.0082  -0.1246 -0.0496 215 LYS A CA  
1688 C C   . LYS A 215 ? 0.4363 0.7939 0.6617 0.0054  -0.1107 -0.0494 215 LYS A C   
1689 O O   . LYS A 215 ? 0.4454 0.8109 0.6793 0.0218  -0.1073 -0.0453 215 LYS A O   
1690 C CB  . LYS A 215 ? 0.4745 0.8427 0.6837 0.0243  -0.1409 -0.0503 215 LYS A CB  
1691 C CG  . LYS A 215 ? 0.5117 0.8655 0.6943 0.0273  -0.1557 -0.0509 215 LYS A CG  
1692 C CD  . LYS A 215 ? 0.5341 0.9165 0.7256 0.0440  -0.1730 -0.0513 215 LYS A CD  
1693 C CE  . LYS A 215 ? 0.5782 0.9421 0.7377 0.0486  -0.1873 -0.0509 215 LYS A CE  
1694 N NZ  . LYS A 215 ? 0.6094 1.0046 0.7777 0.0621  -0.2071 -0.0530 215 LYS A NZ  
1695 N N   . ASP A 216 ? 0.3843 0.7468 0.6211 -0.0145 -0.1023 -0.0539 216 ASP A N   
1696 C CA  . ASP A 216 ? 0.3567 0.7328 0.6144 -0.0184 -0.0876 -0.0535 216 ASP A CA  
1697 C C   . ASP A 216 ? 0.3471 0.6845 0.5827 -0.0234 -0.0729 -0.0484 216 ASP A C   
1698 O O   . ASP A 216 ? 0.3693 0.6799 0.5846 -0.0349 -0.0724 -0.0487 216 ASP A O   
1699 C CB  . ASP A 216 ? 0.3457 0.7548 0.6316 -0.0379 -0.0869 -0.0612 216 ASP A CB  
1700 C CG  . ASP A 216 ? 0.3902 0.8443 0.7031 -0.0334 -0.1018 -0.0671 216 ASP A CG  
1701 O OD1 . ASP A 216 ? 0.3935 0.8541 0.7035 -0.0130 -0.1126 -0.0646 216 ASP A OD1 
1702 O OD2 . ASP A 216 ? 0.3838 0.8676 0.7214 -0.0507 -0.1027 -0.0743 216 ASP A OD2 
1703 N N   . PHE A 217 ? 0.3115 0.6455 0.5502 -0.0137 -0.0616 -0.0440 217 PHE A N   
1704 C CA  . PHE A 217 ? 0.2865 0.5858 0.5045 -0.0164 -0.0490 -0.0391 217 PHE A CA  
1705 C C   . PHE A 217 ? 0.2737 0.5843 0.5067 -0.0171 -0.0350 -0.0386 217 PHE A C   
1706 O O   . PHE A 217 ? 0.3086 0.6463 0.5623 -0.0069 -0.0344 -0.0399 217 PHE A O   
1707 C CB  . PHE A 217 ? 0.2964 0.5665 0.4903 -0.0005 -0.0504 -0.0328 217 PHE A CB  
1708 C CG  . PHE A 217 ? 0.3323 0.5902 0.5085 0.0028  -0.0631 -0.0324 217 PHE A CG  
1709 C CD1 . PHE A 217 ? 0.3485 0.5768 0.5011 -0.0055 -0.0622 -0.0314 217 PHE A CD1 
1710 C CD2 . PHE A 217 ? 0.3611 0.6372 0.5436 0.0149  -0.0756 -0.0330 217 PHE A CD2 
1711 C CE1 . PHE A 217 ? 0.3714 0.5877 0.5056 -0.0022 -0.0729 -0.0313 217 PHE A CE1 
1712 C CE2 . PHE A 217 ? 0.3869 0.6505 0.5499 0.0180  -0.0873 -0.0325 217 PHE A CE2 
1713 C CZ  . PHE A 217 ? 0.3909 0.6246 0.5297 0.0090  -0.0853 -0.0319 217 PHE A CZ  
1714 N N   . GLN A 218 ? 0.2660 0.5545 0.4868 -0.0278 -0.0237 -0.0367 218 GLN A N   
1715 C CA  . GLN A 218 ? 0.2389 0.5298 0.4657 -0.0277 -0.0095 -0.0352 218 GLN A CA  
1716 C C   . GLN A 218 ? 0.2312 0.4965 0.4392 -0.0128 -0.0063 -0.0302 218 GLN A C   
1717 O O   . GLN A 218 ? 0.2438 0.4780 0.4284 -0.0141 -0.0064 -0.0268 218 GLN A O   
1718 C CB  . GLN A 218 ? 0.2730 0.5515 0.4935 -0.0466 0.0002  -0.0353 218 GLN A CB  
1719 C CG  . GLN A 218 ? 0.3035 0.5904 0.5325 -0.0495 0.0152  -0.0346 218 GLN A CG  
1720 C CD  . GLN A 218 ? 0.3181 0.6470 0.5791 -0.0541 0.0181  -0.0394 218 GLN A CD  
1721 O OE1 . GLN A 218 ? 0.3450 0.6957 0.6222 -0.0623 0.0098  -0.0438 218 GLN A OE1 
1722 N NE2 . GLN A 218 ? 0.3259 0.6679 0.5967 -0.0489 0.0299  -0.0392 218 GLN A NE2 
1723 N N   . ILE A 219 ? 0.2179 0.4961 0.4361 0.0019  -0.0041 -0.0300 219 ILE A N   
1724 C CA  . ILE A 219 ? 0.2135 0.4672 0.4145 0.0155  -0.0016 -0.0259 219 ILE A CA  
1725 C C   . ILE A 219 ? 0.2278 0.4803 0.4303 0.0158  0.0121  -0.0262 219 ILE A C   
1726 O O   . ILE A 219 ? 0.2353 0.5147 0.4581 0.0175  0.0176  -0.0295 219 ILE A O   
1727 C CB  . ILE A 219 ? 0.2840 0.5448 0.4892 0.0339  -0.0101 -0.0251 219 ILE A CB  
1728 C CG1 . ILE A 219 ? 0.2970 0.5561 0.4960 0.0340  -0.0240 -0.0244 219 ILE A CG1 
1729 C CG2 . ILE A 219 ? 0.3166 0.5494 0.5035 0.0455  -0.0061 -0.0213 219 ILE A CG2 
1730 C CD1 . ILE A 219 ? 0.3449 0.6126 0.5477 0.0524  -0.0333 -0.0231 219 ILE A CD1 
1731 N N   . SER A 220 ? 0.2607 0.4836 0.4419 0.0146  0.0175  -0.0231 220 SER A N   
1732 C CA  . SER A 220 ? 0.2876 0.5061 0.4656 0.0156  0.0295  -0.0236 220 SER A CA  
1733 C C   . SER A 220 ? 0.3109 0.5110 0.4768 0.0300  0.0295  -0.0223 220 SER A C   
1734 O O   . SER A 220 ? 0.3368 0.5181 0.4900 0.0346  0.0224  -0.0194 220 SER A O   
1735 C CB  . SER A 220 ? 0.3004 0.5000 0.4628 0.0021  0.0358  -0.0216 220 SER A CB  
1736 O OG  . SER A 220 ? 0.3439 0.5142 0.4849 0.0056  0.0322  -0.0183 220 SER A OG  
1737 N N   . VAL A 221 ? 0.2751 0.4806 0.4450 0.0370  0.0381  -0.0247 221 VAL A N   
1738 C CA  . VAL A 221 ? 0.2637 0.4476 0.4193 0.0482  0.0399  -0.0244 221 VAL A CA  
1739 C C   . VAL A 221 ? 0.2939 0.4730 0.4423 0.0438  0.0516  -0.0264 221 VAL A C   
1740 O O   . VAL A 221 ? 0.2479 0.4477 0.4094 0.0451  0.0596  -0.0297 221 VAL A O   
1741 C CB  . VAL A 221 ? 0.3191 0.5133 0.4854 0.0654  0.0375  -0.0262 221 VAL A CB  
1742 C CG1 . VAL A 221 ? 0.2952 0.4654 0.4461 0.0757  0.0421  -0.0273 221 VAL A CG1 
1743 C CG2 . VAL A 221 ? 0.3425 0.5376 0.5111 0.0707  0.0250  -0.0233 221 VAL A CG2 
1744 N N   . ASP A 222 ? 0.3094 0.4633 0.4376 0.0381  0.0526  -0.0244 222 ASP A N   
1745 C CA  . ASP A 222 ? 0.3124 0.4593 0.4296 0.0335  0.0624  -0.0259 222 ASP A CA  
1746 C C   . ASP A 222 ? 0.3368 0.5041 0.4650 0.0228  0.0692  -0.0260 222 ASP A C   
1747 O O   . ASP A 222 ? 0.3019 0.4747 0.4354 0.0131  0.0650  -0.0237 222 ASP A O   
1748 C CB  . ASP A 222 ? 0.2959 0.4388 0.4098 0.0457  0.0678  -0.0302 222 ASP A CB  
1749 C CG  . ASP A 222 ? 0.2689 0.3869 0.3691 0.0530  0.0618  -0.0299 222 ASP A CG  
1750 O OD1 . ASP A 222 ? 0.2882 0.3906 0.3779 0.0466  0.0559  -0.0264 222 ASP A OD1 
1751 O OD2 . ASP A 222 ? 0.2912 0.4045 0.3909 0.0650  0.0634  -0.0332 222 ASP A OD2 
1752 N N   . HIS A 223 ? 0.3450 0.5241 0.4769 0.0238  0.0803  -0.0290 223 HIS A N   
1753 C CA  . HIS A 223 ? 0.4475 0.6431 0.5876 0.0112  0.0879  -0.0283 223 HIS A CA  
1754 C C   . HIS A 223 ? 0.4966 0.7240 0.6647 0.0086  0.0857  -0.0297 223 HIS A C   
1755 O O   . HIS A 223 ? 0.5609 0.8009 0.7369 -0.0049 0.0905  -0.0289 223 HIS A O   
1756 C CB  . HIS A 223 ? 0.4934 0.6922 0.6275 0.0120  0.1019  -0.0307 223 HIS A CB  
1757 C CG  . HIS A 223 ? 0.5696 0.7811 0.7081 -0.0022 0.1117  -0.0290 223 HIS A CG  
1758 N ND1 . HIS A 223 ? 0.5942 0.8387 0.7591 -0.0060 0.1172  -0.0312 223 HIS A ND1 
1759 C CD2 . HIS A 223 ? 0.5947 0.7899 0.7147 -0.0142 0.1170  -0.0250 223 HIS A CD2 
1760 C CE1 . HIS A 223 ? 0.5981 0.8453 0.7604 -0.0210 0.1264  -0.0286 223 HIS A CE1 
1761 N NE2 . HIS A 223 ? 0.5989 0.8149 0.7327 -0.0257 0.1265  -0.0245 223 HIS A NE2 
1762 N N   . LEU A 224 ? 0.4454 0.6853 0.6280 0.0206  0.0780  -0.0317 224 LEU A N   
1763 C CA  . LEU A 224 ? 0.3915 0.6667 0.6029 0.0211  0.0758  -0.0343 224 LEU A CA  
1764 C C   . LEU A 224 ? 0.3801 0.6564 0.5959 0.0137  0.0629  -0.0322 224 LEU A C   
1765 O O   . LEU A 224 ? 0.3853 0.6405 0.5877 0.0190  0.0532  -0.0298 224 LEU A O   
1766 C CB  . LEU A 224 ? 0.4179 0.7055 0.6410 0.0408  0.0739  -0.0375 224 LEU A CB  
1767 C CG  . LEU A 224 ? 0.4469 0.7695 0.6988 0.0462  0.0667  -0.0398 224 LEU A CG  
1768 C CD1 . LEU A 224 ? 0.4561 0.8149 0.7323 0.0401  0.0778  -0.0435 224 LEU A CD1 
1769 C CD2 . LEU A 224 ? 0.4544 0.7763 0.7090 0.0681  0.0601  -0.0408 224 LEU A CD2 
1770 N N   . SER A 225 ? 0.3596 0.6604 0.5939 0.0012  0.0632  -0.0336 225 SER A N   
1771 C CA  . SER A 225 ? 0.3734 0.6749 0.6105 -0.0070 0.0511  -0.0329 225 SER A CA  
1772 C C   . SER A 225 ? 0.3830 0.7250 0.6513 -0.0082 0.0465  -0.0372 225 SER A C   
1773 O O   . SER A 225 ? 0.4079 0.7753 0.6946 -0.0184 0.0554  -0.0398 225 SER A O   
1774 C CB  . SER A 225 ? 0.4087 0.6909 0.6310 -0.0257 0.0541  -0.0303 225 SER A CB  
1775 O OG  . SER A 225 ? 0.4460 0.7254 0.6681 -0.0324 0.0422  -0.0304 225 SER A OG  
1776 N N   . ILE A 226 ? 0.3663 0.7146 0.6400 0.0012  0.0324  -0.0377 226 ILE A N   
1777 C CA  . ILE A 226 ? 0.3568 0.7452 0.6601 0.0038  0.0251  -0.0421 226 ILE A CA  
1778 C C   . ILE A 226 ? 0.3464 0.7318 0.6464 -0.0023 0.0097  -0.0422 226 ILE A C   
1779 O O   . ILE A 226 ? 0.3480 0.7027 0.6242 0.0025  0.0024  -0.0386 226 ILE A O   
1780 C CB  . ILE A 226 ? 0.3617 0.7645 0.6756 0.0273  0.0227  -0.0430 226 ILE A CB  
1781 C CG1 . ILE A 226 ? 0.3756 0.7782 0.6897 0.0337  0.0386  -0.0438 226 ILE A CG1 
1782 C CG2 . ILE A 226 ? 0.3568 0.8047 0.7032 0.0316  0.0143  -0.0476 226 ILE A CG2 
1783 C CD1 . ILE A 226 ? 0.3794 0.7872 0.6981 0.0580  0.0377  -0.0447 226 ILE A CD1 
1784 N N   . LEU A 227 ? 0.3255 0.7433 0.6491 -0.0135 0.0049  -0.0468 227 LEU A N   
1785 C CA  . LEU A 227 ? 0.3283 0.7471 0.6501 -0.0185 -0.0110 -0.0485 227 LEU A CA  
1786 C C   . LEU A 227 ? 0.3484 0.7872 0.6812 0.0016  -0.0242 -0.0493 227 LEU A C   
1787 O O   . LEU A 227 ? 0.3760 0.8536 0.7376 0.0087  -0.0242 -0.0529 227 LEU A O   
1788 C CB  . LEU A 227 ? 0.3506 0.7947 0.6923 -0.0404 -0.0116 -0.0539 227 LEU A CB  
1789 C CG  . LEU A 227 ? 0.3693 0.8243 0.7148 -0.0433 -0.0301 -0.0577 227 LEU A CG  
1790 C CD1 . LEU A 227 ? 0.3672 0.7783 0.6777 -0.0453 -0.0366 -0.0544 227 LEU A CD1 
1791 C CD2 . LEU A 227 ? 0.3809 0.8674 0.7516 -0.0648 -0.0312 -0.0645 227 LEU A CD2 
1792 N N   . HIS A 228 ? 0.3640 0.7761 0.6735 0.0115  -0.0347 -0.0457 228 HIS A N   
1793 C CA  . HIS A 228 ? 0.3881 0.8104 0.7005 0.0319  -0.0475 -0.0448 228 HIS A CA  
1794 C C   . HIS A 228 ? 0.3740 0.8071 0.6873 0.0260  -0.0642 -0.0477 228 HIS A C   
1795 O O   . HIS A 228 ? 0.3582 0.7682 0.6528 0.0120  -0.0668 -0.0477 228 HIS A O   
1796 C CB  . HIS A 228 ? 0.4360 0.8185 0.7189 0.0473  -0.0467 -0.0380 228 HIS A CB  
1797 C CG  . HIS A 228 ? 0.4805 0.8547 0.7630 0.0571  -0.0331 -0.0361 228 HIS A CG  
1798 N ND1 . HIS A 228 ? 0.4936 0.8704 0.7786 0.0791  -0.0346 -0.0344 228 HIS A ND1 
1799 C CD2 . HIS A 228 ? 0.4858 0.8474 0.7634 0.0484  -0.0182 -0.0358 228 HIS A CD2 
1800 C CE1 . HIS A 228 ? 0.4966 0.8628 0.7787 0.0828  -0.0209 -0.0340 228 HIS A CE1 
1801 N NE2 . HIS A 228 ? 0.4869 0.8447 0.7646 0.0644  -0.0111 -0.0348 228 HIS A NE2 
1802 N N   . ARG A 229 ? 0.3766 0.8448 0.7112 0.0374  -0.0760 -0.0507 229 ARG A N   
1803 C CA  . ARG A 229 ? 0.3887 0.8768 0.7300 0.0312  -0.0930 -0.0553 229 ARG A CA  
1804 C C   . ARG A 229 ? 0.3911 0.8721 0.7176 0.0526  -0.1084 -0.0516 229 ARG A C   
1805 O O   . ARG A 229 ? 0.3973 0.8768 0.7238 0.0737  -0.1071 -0.0471 229 ARG A O   
1806 C CB  . ARG A 229 ? 0.4689 0.9962 0.8429 0.0235  -0.0930 -0.0601 229 ARG A CB  
1807 C CG  . ARG A 229 ? 0.5422 1.0797 0.9223 0.0006  -0.1003 -0.0660 229 ARG A CG  
1808 C CD  . ARG A 229 ? 0.5676 1.1018 0.9537 -0.0234 -0.0849 -0.0687 229 ARG A CD  
1809 N NE  . ARG A 229 ? 0.5909 1.1524 1.0052 -0.0278 -0.0742 -0.0697 229 ARG A NE  
1810 C CZ  . ARG A 229 ? 0.6221 1.1907 1.0482 -0.0505 -0.0650 -0.0727 229 ARG A CZ  
1811 N NH1 . ARG A 229 ? 0.6468 1.1952 1.0584 -0.0711 -0.0656 -0.0752 229 ARG A NH1 
1812 N NH2 . ARG A 229 ? 0.6293 1.2234 1.0806 -0.0524 -0.0548 -0.0729 229 ARG A NH2 
1813 N N   . ASP A 230 ? 0.4021 0.8755 0.7134 0.0470  -0.1226 -0.0531 230 ASP A N   
1814 C CA  . ASP A 230 ? 0.4299 0.8951 0.7233 0.0658  -0.1381 -0.0493 230 ASP A CA  
1815 C C   . ASP A 230 ? 0.4254 0.8489 0.6900 0.0820  -0.1307 -0.0397 230 ASP A C   
1816 O O   . ASP A 230 ? 0.4222 0.8454 0.6829 0.1041  -0.1362 -0.0350 230 ASP A O   
1817 C CB  . ASP A 230 ? 0.4821 0.9739 0.7942 0.0775  -0.1461 -0.0489 230 ASP A CB  
1818 C CG  . ASP A 230 ? 0.5460 1.0261 0.8363 0.0935  -0.1625 -0.0446 230 ASP A CG  
1819 O OD1 . ASP A 230 ? 0.5793 1.0392 0.8441 0.0885  -0.1708 -0.0447 230 ASP A OD1 
1820 O OD2 . ASP A 230 ? 0.5826 1.0718 0.8793 0.1116  -0.1664 -0.0408 230 ASP A OD2 
1821 N N   . VAL A 231 ? 0.4054 0.7933 0.6500 0.0707  -0.1179 -0.0370 231 VAL A N   
1822 C CA  . VAL A 231 ? 0.3862 0.7342 0.6043 0.0820  -0.1098 -0.0287 231 VAL A CA  
1823 C C   . VAL A 231 ? 0.4115 0.7329 0.5983 0.0883  -0.1202 -0.0241 231 VAL A C   
1824 O O   . VAL A 231 ? 0.4817 0.7978 0.6573 0.0759  -0.1266 -0.0271 231 VAL A O   
1825 C CB  . VAL A 231 ? 0.3984 0.7220 0.6083 0.0674  -0.0934 -0.0280 231 VAL A CB  
1826 C CG1 . VAL A 231 ? 0.3936 0.6760 0.5749 0.0764  -0.0870 -0.0202 231 VAL A CG1 
1827 C CG2 . VAL A 231 ? 0.3875 0.7343 0.6243 0.0641  -0.0818 -0.0313 231 VAL A CG2 
1828 N N   . GLN A 232 ? 0.4027 0.7063 0.5742 0.1078  -0.1217 -0.0169 232 GLN A N   
1829 C CA  . GLN A 232 ? 0.4210 0.6957 0.5598 0.1152  -0.1291 -0.0108 232 GLN A CA  
1830 C C   . GLN A 232 ? 0.4336 0.6656 0.5467 0.1132  -0.1162 -0.0043 232 GLN A C   
1831 O O   . GLN A 232 ? 0.4296 0.6363 0.5157 0.1107  -0.1183 -0.0009 232 GLN A O   
1832 C CB  . GLN A 232 ? 0.4248 0.7064 0.5611 0.1388  -0.1403 -0.0062 232 GLN A CB  
1833 N N   . GLU A 233 ? 0.4112 0.6362 0.5325 0.1134  -0.1028 -0.0032 233 GLU A N   
1834 C CA  . GLU A 233 ? 0.4110 0.5979 0.5098 0.1125  -0.0916 0.0027  233 GLU A CA  
1835 C C   . GLU A 233 ? 0.4023 0.5894 0.5151 0.1087  -0.0781 0.0009  233 GLU A C   
1836 O O   . GLU A 233 ? 0.4137 0.6229 0.5475 0.1162  -0.0772 -0.0017 233 GLU A O   
1837 C CB  . GLU A 233 ? 0.4578 0.6215 0.5355 0.1305  -0.0948 0.0110  233 GLU A CB  
1838 C CG  . GLU A 233 ? 0.4858 0.6102 0.5381 0.1274  -0.0848 0.0173  233 GLU A CG  
1839 C CD  . GLU A 233 ? 0.5236 0.6240 0.5561 0.1442  -0.0864 0.0257  233 GLU A CD  
1840 O OE1 . GLU A 233 ? 0.5216 0.6341 0.5623 0.1600  -0.0930 0.0266  233 GLU A OE1 
1841 O OE2 . GLU A 233 ? 0.5427 0.6119 0.5514 0.1418  -0.0808 0.0316  233 GLU A OE2 
1842 N N   . ILE A 234 ? 0.3700 0.5334 0.4706 0.0978  -0.0677 0.0022  234 ILE A N   
1843 C CA  . ILE A 234 ? 0.3535 0.5093 0.4599 0.0949  -0.0549 0.0016  234 ILE A CA  
1844 C C   . ILE A 234 ? 0.3690 0.4892 0.4521 0.0984  -0.0492 0.0078  234 ILE A C   
1845 O O   . ILE A 234 ? 0.4238 0.5264 0.4898 0.0911  -0.0490 0.0103  234 ILE A O   
1846 C CB  . ILE A 234 ? 0.3809 0.5435 0.4955 0.0770  -0.0480 -0.0032 234 ILE A CB  
1847 C CG1 . ILE A 234 ? 0.4132 0.6094 0.5495 0.0703  -0.0537 -0.0092 234 ILE A CG1 
1848 C CG2 . ILE A 234 ? 0.3439 0.5006 0.4637 0.0756  -0.0357 -0.0040 234 ILE A CG2 
1849 C CD1 . ILE A 234 ? 0.4103 0.6081 0.5499 0.0517  -0.0481 -0.0130 234 ILE A CD1 
1850 N N   . ARG A 235 ? 0.3331 0.4425 0.4152 0.1093  -0.0443 0.0099  235 ARG A N   
1851 C CA  . ARG A 235 ? 0.3394 0.4148 0.4003 0.1120  -0.0391 0.0156  235 ARG A CA  
1852 C C   . ARG A 235 ? 0.3262 0.3919 0.3903 0.1066  -0.0278 0.0131  235 ARG A C   
1853 O O   . ARG A 235 ? 0.3200 0.3974 0.3977 0.1121  -0.0245 0.0093  235 ARG A O   
1854 C CB  . ARG A 235 ? 0.3433 0.4058 0.3943 0.1298  -0.0435 0.0209  235 ARG A CB  
1855 C CG  . ARG A 235 ? 0.3932 0.4611 0.4362 0.1377  -0.0555 0.0246  235 ARG A CG  
1856 C CD  . ARG A 235 ? 0.4317 0.4872 0.4654 0.1576  -0.0599 0.0301  235 ARG A CD  
1857 N NE  . ARG A 235 ? 0.4938 0.5102 0.5011 0.1600  -0.0549 0.0379  235 ARG A NE  
1858 C CZ  . ARG A 235 ? 0.5218 0.5208 0.5067 0.1586  -0.0581 0.0442  235 ARG A CZ  
1859 N NH1 . ARG A 235 ? 0.5424 0.5062 0.5045 0.1598  -0.0519 0.0514  235 ARG A NH1 
1860 N NH2 . ARG A 235 ? 0.5182 0.5344 0.5026 0.1552  -0.0669 0.0430  235 ARG A NH2 
1861 N N   . TYR A 236 ? 0.3126 0.3575 0.3635 0.0968  -0.0221 0.0150  236 TYR A N   
1862 C CA  . TYR A 236 ? 0.3562 0.3893 0.4067 0.0909  -0.0127 0.0128  236 TYR A CA  
1863 C C   . TYR A 236 ? 0.3864 0.3893 0.4199 0.0944  -0.0092 0.0174  236 TYR A C   
1864 O O   . TYR A 236 ? 0.3506 0.3389 0.3699 0.0934  -0.0111 0.0228  236 TYR A O   
1865 C CB  . TYR A 236 ? 0.3520 0.3872 0.4025 0.0758  -0.0091 0.0109  236 TYR A CB  
1866 C CG  . TYR A 236 ? 0.3390 0.3994 0.4047 0.0698  -0.0105 0.0062  236 TYR A CG  
1867 C CD1 . TYR A 236 ? 0.3350 0.4111 0.4153 0.0718  -0.0069 0.0017  236 TYR A CD1 
1868 C CD2 . TYR A 236 ? 0.3695 0.4370 0.4342 0.0619  -0.0147 0.0061  236 TYR A CD2 
1869 C CE1 . TYR A 236 ? 0.3642 0.4632 0.4586 0.0649  -0.0069 -0.0021 236 TYR A CE1 
1870 C CE2 . TYR A 236 ? 0.3870 0.4758 0.4654 0.0546  -0.0153 0.0016  236 TYR A CE2 
1871 C CZ  . TYR A 236 ? 0.4004 0.5049 0.4939 0.0557  -0.0111 -0.0021 236 TYR A CZ  
1872 O OH  . TYR A 236 ? 0.4838 0.6092 0.5913 0.0475  -0.0103 -0.0061 236 TYR A OH  
1873 N N   . GLU A 237 ? 0.3758 0.3684 0.4100 0.0978  -0.0034 0.0149  237 GLU A N   
1874 C CA  . GLU A 237 ? 0.3763 0.3387 0.3951 0.0975  0.0011  0.0179  237 GLU A CA  
1875 C C   . GLU A 237 ? 0.3716 0.3286 0.3939 0.0951  0.0079  0.0120  237 GLU A C   
1876 O O   . GLU A 237 ? 0.3270 0.3006 0.3613 0.0995  0.0091  0.0068  237 GLU A O   
1877 C CB  . GLU A 237 ? 0.4293 0.3737 0.4364 0.1114  -0.0020 0.0235  237 GLU A CB  
1878 C CG  . GLU A 237 ? 0.4578 0.4121 0.4741 0.1262  -0.0042 0.0208  237 GLU A CG  
1879 C CD  . GLU A 237 ? 0.5150 0.4631 0.5231 0.1415  -0.0112 0.0270  237 GLU A CD  
1880 O OE1 . GLU A 237 ? 0.5580 0.4750 0.5471 0.1450  -0.0095 0.0328  237 GLU A OE1 
1881 O OE2 . GLU A 237 ? 0.5141 0.4881 0.5341 0.1494  -0.0186 0.0262  237 GLU A OE2 
1882 N N   . VAL A 238 ? 0.3774 0.3116 0.3886 0.0879  0.0124  0.0126  238 VAL A N   
1883 C CA  . VAL A 238 ? 0.3829 0.3089 0.3943 0.0856  0.0180  0.0064  238 VAL A CA  
1884 C C   . VAL A 238 ? 0.4325 0.3485 0.4418 0.1005  0.0187  0.0049  238 VAL A C   
1885 O O   . VAL A 238 ? 0.4230 0.3210 0.4224 0.1093  0.0167  0.0102  238 VAL A O   
1886 C CB  . VAL A 238 ? 0.3719 0.2763 0.3728 0.0741  0.0216  0.0069  238 VAL A CB  
1887 C CG1 . VAL A 238 ? 0.3723 0.2656 0.3709 0.0717  0.0263  -0.0007 238 VAL A CG1 
1888 C CG2 . VAL A 238 ? 0.3711 0.2886 0.3759 0.0617  0.0209  0.0079  238 VAL A CG2 
1889 N N   . SER A 239 ? 0.3758 0.3022 0.3932 0.1042  0.0220  -0.0021 239 SER A N   
1890 C CA  . SER A 239 ? 0.3794 0.2996 0.3965 0.1206  0.0230  -0.0041 239 SER A CA  
1891 C C   . SER A 239 ? 0.4181 0.3011 0.4177 0.1220  0.0268  -0.0048 239 SER A C   
1892 O O   . SER A 239 ? 0.4461 0.3141 0.4377 0.1086  0.0295  -0.0064 239 SER A O   
1893 C CB  . SER A 239 ? 0.3813 0.3247 0.4120 0.1242  0.0270  -0.0116 239 SER A CB  
1894 O OG  . SER A 239 ? 0.4551 0.3927 0.4858 0.1411  0.0293  -0.0147 239 SER A OG  
1895 N N   . ALA A 240 ? 0.4566 0.3241 0.4502 0.1384  0.0265  -0.0035 240 ALA A N   
1896 C CA  . ALA A 240 ? 0.5252 0.3563 0.5023 0.1411  0.0312  -0.0064 240 ALA A CA  
1897 C C   . ALA A 240 ? 0.5429 0.3768 0.5227 0.1422  0.0370  -0.0169 240 ALA A C   
1898 O O   . ALA A 240 ? 0.5957 0.4001 0.5614 0.1394  0.0411  -0.0215 240 ALA A O   
1899 C CB  . ALA A 240 ? 0.5450 0.3555 0.5126 0.1603  0.0292  -0.0016 240 ALA A CB  
1900 N N   . LYS A 241 ? 0.4770 0.3446 0.4737 0.1461  0.0377  -0.0209 241 LYS A N   
1901 C CA  . LYS A 241 ? 0.4755 0.3476 0.4737 0.1481  0.0442  -0.0306 241 LYS A CA  
1902 C C   . LYS A 241 ? 0.4771 0.3537 0.4735 0.1290  0.0462  -0.0345 241 LYS A C   
1903 O O   . LYS A 241 ? 0.4439 0.3318 0.4447 0.1163  0.0425  -0.0299 241 LYS A O   
1904 C CB  . LYS A 241 ? 0.4630 0.3705 0.4805 0.1604  0.0454  -0.0328 241 LYS A CB  
1905 C CG  . LYS A 241 ? 0.4859 0.3956 0.5085 0.1812  0.0417  -0.0287 241 LYS A CG  
1906 C CD  . LYS A 241 ? 0.4710 0.4242 0.5180 0.1898  0.0416  -0.0303 241 LYS A CD  
1907 C CE  . LYS A 241 ? 0.4944 0.4548 0.5489 0.2113  0.0364  -0.0266 241 LYS A CE  
1908 N NZ  . LYS A 241 ? 0.4850 0.4921 0.5667 0.2183  0.0364  -0.0293 241 LYS A NZ  
1909 N N   . LYS A 242 ? 0.4826 0.3486 0.4706 0.1278  0.0517  -0.0433 242 LYS A N   
1910 C CA  . LYS A 242 ? 0.4901 0.3590 0.4741 0.1115  0.0528  -0.0477 242 LYS A CA  
1911 C C   . LYS A 242 ? 0.4770 0.3590 0.4620 0.1161  0.0593  -0.0560 242 LYS A C   
1912 O O   . LYS A 242 ? 0.4757 0.3517 0.4585 0.1306  0.0641  -0.0607 242 LYS A O   
1913 C CB  . LYS A 242 ? 0.5069 0.3422 0.4736 0.1013  0.0520  -0.0503 242 LYS A CB  
1914 C CG  . LYS A 242 ? 0.5334 0.3566 0.4986 0.0942  0.0471  -0.0415 242 LYS A CG  
1915 C CD  . LYS A 242 ? 0.5774 0.3707 0.5283 0.0817  0.0471  -0.0445 242 LYS A CD  
1916 C CE  . LYS A 242 ? 0.5935 0.4017 0.5486 0.0642  0.0445  -0.0457 242 LYS A CE  
1917 N NZ  . LYS A 242 ? 0.5965 0.4117 0.5582 0.0558  0.0410  -0.0367 242 LYS A NZ  
1918 N N   . ILE A 243 ? 0.4522 0.3519 0.4399 0.1044  0.0599  -0.0574 243 ILE A N   
1919 C CA  . ILE A 243 ? 0.4437 0.3516 0.4273 0.1060  0.0667  -0.0653 243 ILE A CA  
1920 C C   . ILE A 243 ? 0.4637 0.3451 0.4271 0.0981  0.0667  -0.0726 243 ILE A C   
1921 O O   . ILE A 243 ? 0.4804 0.3516 0.4387 0.0852  0.0610  -0.0707 243 ILE A O   
1922 C CB  . ILE A 243 ? 0.3956 0.3346 0.3902 0.0983  0.0680  -0.0626 243 ILE A CB  
1923 C CG1 . ILE A 243 ? 0.4194 0.3655 0.4073 0.1008  0.0766  -0.0702 243 ILE A CG1 
1924 C CG2 . ILE A 243 ? 0.3957 0.3331 0.3863 0.0824  0.0621  -0.0590 243 ILE A CG2 
1925 C CD1 . ILE A 243 ? 0.4053 0.3761 0.3994 0.0912  0.0785  -0.0672 243 ILE A CD1 
1926 N N   . HIS A 244 ? 0.4945 0.3656 0.4467 0.1061  0.0732  -0.0816 244 HIS A N   
1927 C CA  . HIS A 244 ? 0.5173 0.3615 0.4482 0.1002  0.0733  -0.0907 244 HIS A CA  
1928 C C   . HIS A 244 ? 0.5082 0.3659 0.4316 0.0962  0.0775  -0.0964 244 HIS A C   
1929 O O   . HIS A 244 ? 0.5010 0.3759 0.4291 0.1059  0.0854  -0.0982 244 HIS A O   
1930 C CB  . HIS A 244 ? 0.5826 0.3980 0.5015 0.1135  0.0775  -0.0975 244 HIS A CB  
1931 C CG  . HIS A 244 ? 0.6364 0.4365 0.5602 0.1198  0.0741  -0.0908 244 HIS A CG  
1932 N ND1 . HIS A 244 ? 0.6480 0.4280 0.5669 0.1080  0.0677  -0.0869 244 HIS A ND1 
1933 C CD2 . HIS A 244 ? 0.6566 0.4603 0.5899 0.1366  0.0761  -0.0867 244 HIS A CD2 
1934 C CE1 . HIS A 244 ? 0.6622 0.4308 0.5846 0.1171  0.0665  -0.0803 244 HIS A CE1 
1935 N NE2 . HIS A 244 ? 0.6585 0.4412 0.5895 0.1351  0.0707  -0.0800 244 HIS A NE2 
1936 N N   . PHE A 245 ? 0.5103 0.3613 0.4222 0.0821  0.0724  -0.0990 245 PHE A N   
1937 C CA  . PHE A 245 ? 0.5598 0.4176 0.4586 0.0781  0.0752  -0.1050 245 PHE A CA  
1938 C C   . PHE A 245 ? 0.5948 0.4239 0.4694 0.0777  0.0755  -0.1172 245 PHE A C   
1939 O O   . PHE A 245 ? 0.6184 0.4237 0.4864 0.0716  0.0696  -0.1202 245 PHE A O   
1940 C CB  . PHE A 245 ? 0.5609 0.4327 0.4620 0.0638  0.0681  -0.0996 245 PHE A CB  
1941 C CG  . PHE A 245 ? 0.5304 0.4286 0.4516 0.0629  0.0680  -0.0888 245 PHE A CG  
1942 C CD1 . PHE A 245 ? 0.5171 0.4173 0.4536 0.0607  0.0626  -0.0810 245 PHE A CD1 
1943 C CD2 . PHE A 245 ? 0.5349 0.4545 0.4582 0.0634  0.0734  -0.0864 245 PHE A CD2 
1944 C CE1 . PHE A 245 ? 0.4996 0.4223 0.4526 0.0594  0.0619  -0.0721 245 PHE A CE1 
1945 C CE2 . PHE A 245 ? 0.5159 0.4577 0.4570 0.0611  0.0730  -0.0770 245 PHE A CE2 
1946 C CZ  . PHE A 245 ? 0.4745 0.4179 0.4305 0.0594  0.0668  -0.0703 245 PHE A CZ  
1947 N N   . ALA A 246 ? 0.6233 0.4540 0.4838 0.0832  0.0827  -0.1246 246 ALA A N   
1948 C CA  . ALA A 246 ? 0.6607 0.4671 0.4952 0.0793  0.0810  -0.1366 246 ALA A CA  
1949 C C   . ALA A 246 ? 0.7217 0.5363 0.5501 0.0639  0.0720  -0.1352 246 ALA A C   
1950 O O   . ALA A 246 ? 0.7449 0.5840 0.5801 0.0615  0.0728  -0.1282 246 ALA A O   
1951 C CB  . ALA A 246 ? 0.7007 0.5059 0.5201 0.0913  0.0925  -0.1450 246 ALA A CB  
1952 N N   . ARG A 247 ? 0.7773 0.5723 0.5944 0.0532  0.0629  -0.1414 247 ARG A N   
1953 C CA  . ARG A 247 ? 0.8236 0.6273 0.6331 0.0406  0.0538  -0.1420 247 ARG A CA  
1954 C C   . ARG A 247 ? 0.9097 0.6914 0.6910 0.0378  0.0513  -0.1564 247 ARG A C   
1955 O O   . ARG A 247 ? 0.9271 0.6816 0.6992 0.0381  0.0512  -0.1652 247 ARG A O   
1956 C CB  . ARG A 247 ? 0.8041 0.6129 0.6299 0.0279  0.0430  -0.1354 247 ARG A CB  
1957 C CG  . ARG A 247 ? 0.7613 0.5919 0.6132 0.0293  0.0441  -0.1212 247 ARG A CG  
1958 C CD  . ARG A 247 ? 0.7316 0.5899 0.5893 0.0300  0.0454  -0.1129 247 ARG A CD  
1959 N NE  . ARG A 247 ? 0.7215 0.5959 0.6027 0.0304  0.0456  -0.1011 247 ARG A NE  
1960 C CZ  . ARG A 247 ? 0.6740 0.5701 0.5646 0.0319  0.0482  -0.0927 247 ARG A CZ  
1961 N NH1 . ARG A 247 ? 0.6722 0.5770 0.5511 0.0330  0.0516  -0.0933 247 ARG A NH1 
1962 N NH2 . ARG A 247 ? 0.6592 0.5665 0.5693 0.0318  0.0474  -0.0836 247 ARG A NH2 
1963 N N   . PHE A 248 ? 1.0071 0.7986 0.7724 0.0355  0.0494  -0.1588 248 PHE A N   
1964 C CA  . PHE A 248 ? 1.0763 0.8482 0.8125 0.0324  0.0457  -0.1729 248 PHE A CA  
1965 C C   . PHE A 248 ? 1.0676 0.8461 0.7984 0.0185  0.0309  -0.1744 248 PHE A C   
1966 O O   . PHE A 248 ? 1.1000 0.8630 0.8075 0.0137  0.0248  -0.1868 248 PHE A O   
1967 C CB  . PHE A 248 ? 1.1702 0.9426 0.8848 0.0438  0.0569  -0.1777 248 PHE A CB  
1968 C CG  . PHE A 248 ? 1.2349 1.0323 0.9470 0.0436  0.0582  -0.1691 248 PHE A CG  
1969 C CD1 . PHE A 248 ? 1.2169 1.0385 0.9531 0.0456  0.0627  -0.1550 248 PHE A CD1 
1970 C CD2 . PHE A 248 ? 1.2843 1.0785 0.9670 0.0420  0.0555  -0.1756 248 PHE A CD2 
1971 C CE1 . PHE A 248 ? 1.2209 1.0613 0.9525 0.0450  0.0646  -0.1473 248 PHE A CE1 
1972 C CE2 . PHE A 248 ? 1.2810 1.0943 0.9580 0.0424  0.0574  -0.1670 248 PHE A CE2 
1973 C CZ  . PHE A 248 ? 1.2482 1.0837 0.9497 0.0436  0.0623  -0.1528 248 PHE A CZ  
1974 N N   . ARG A 249 ? 0.9221 0.7229 0.6740 0.0122  0.0245  -0.1629 249 ARG A N   
1975 C CA  . ARG A 249 ? 0.8776 0.6876 0.6297 -0.0001 0.0098  -0.1637 249 ARG A CA  
1976 C C   . ARG A 249 ? 0.7990 0.6277 0.5814 -0.0053 0.0059  -0.1511 249 ARG A C   
1977 O O   . ARG A 249 ? 0.7380 0.5720 0.5380 0.0006  0.0141  -0.1422 249 ARG A O   
1978 C CB  . ARG A 249 ? 0.9036 0.7251 0.6349 0.0018  0.0065  -0.1638 249 ARG A CB  
1979 N N   . SER A 250 ? 0.7792 0.6188 0.5677 -0.0160 -0.0069 -0.1512 250 SER A N   
1980 C CA  . SER A 250 ? 0.7299 0.5893 0.5451 -0.0204 -0.0108 -0.1397 250 SER A CA  
1981 C C   . SER A 250 ? 0.6602 0.5404 0.4763 -0.0137 -0.0091 -0.1290 250 SER A C   
1982 O O   . SER A 250 ? 0.6621 0.5486 0.4614 -0.0130 -0.0148 -0.1308 250 SER A O   
1983 C CB  . SER A 250 ? 0.7612 0.6273 0.5844 -0.0338 -0.0245 -0.1440 250 SER A CB  
1984 O OG  . SER A 250 ? 0.7278 0.6130 0.5772 -0.0371 -0.0266 -0.1331 250 SER A OG  
1985 N N   . PHE A 251 ? 0.6487 0.5376 0.4825 -0.0088 -0.0014 -0.1181 251 PHE A N   
1986 C CA  . PHE A 251 ? 0.6004 0.5084 0.4401 -0.0051 -0.0008 -0.1068 251 PHE A CA  
1987 C C   . PHE A 251 ? 0.5460 0.4637 0.4127 -0.0077 -0.0008 -0.0979 251 PHE A C   
1988 O O   . PHE A 251 ? 0.5605 0.4783 0.4379 -0.0026 0.0079  -0.0921 251 PHE A O   
1989 C CB  . PHE A 251 ? 0.6309 0.5385 0.4605 0.0044  0.0112  -0.1034 251 PHE A CB  
1990 C CG  . PHE A 251 ? 0.6505 0.5729 0.4787 0.0068  0.0116  -0.0934 251 PHE A CG  
1991 C CD1 . PHE A 251 ? 0.6334 0.5676 0.4688 0.0026  0.0015  -0.0881 251 PHE A CD1 
1992 C CD2 . PHE A 251 ? 0.6624 0.5864 0.4817 0.0132  0.0227  -0.0896 251 PHE A CD2 
1993 C CE1 . PHE A 251 ? 0.6175 0.5613 0.4492 0.0055  0.0018  -0.0788 251 PHE A CE1 
1994 C CE2 . PHE A 251 ? 0.6628 0.5968 0.4791 0.0142  0.0237  -0.0801 251 PHE A CE2 
1995 C CZ  . PHE A 251 ? 0.6481 0.5903 0.4695 0.0107  0.0129  -0.0746 251 PHE A CZ  
1996 N N   . PRO A 252 ? 0.4844 0.4113 0.3626 -0.0154 -0.0106 -0.0970 252 PRO A N   
1997 C CA  . PRO A 252 ? 0.4640 0.3982 0.3663 -0.0185 -0.0101 -0.0897 252 PRO A CA  
1998 C C   . PRO A 252 ? 0.4410 0.3872 0.3526 -0.0122 -0.0048 -0.0782 252 PRO A C   
1999 O O   . PRO A 252 ? 0.4289 0.3838 0.3328 -0.0085 -0.0059 -0.0741 252 PRO A O   
2000 C CB  . PRO A 252 ? 0.4535 0.3994 0.3643 -0.0274 -0.0216 -0.0918 252 PRO A CB  
2001 C CG  . PRO A 252 ? 0.4769 0.4149 0.3694 -0.0315 -0.0285 -0.1035 252 PRO A CG  
2002 C CD  . PRO A 252 ? 0.4891 0.4188 0.3585 -0.0223 -0.0226 -0.1048 252 PRO A CD  
2003 N N   . PHE A 253 ? 0.4061 0.3513 0.3333 -0.0113 0.0006  -0.0729 253 PHE A N   
2004 C CA  . PHE A 253 ? 0.3751 0.3312 0.3126 -0.0068 0.0047  -0.0627 253 PHE A CA  
2005 C C   . PHE A 253 ? 0.3711 0.3419 0.3114 -0.0080 -0.0018 -0.0575 253 PHE A C   
2006 O O   . PHE A 253 ? 0.3609 0.3374 0.2971 -0.0035 0.0007  -0.0517 253 PHE A O   
2007 C CB  . PHE A 253 ? 0.3857 0.3394 0.3395 -0.0075 0.0079  -0.0585 253 PHE A CB  
2008 C CG  . PHE A 253 ? 0.3508 0.3147 0.3149 -0.0037 0.0112  -0.0494 253 PHE A CG  
2009 C CD1 . PHE A 253 ? 0.3968 0.3611 0.3595 0.0027  0.0181  -0.0469 253 PHE A CD1 
2010 C CD2 . PHE A 253 ? 0.3558 0.3293 0.3313 -0.0067 0.0075  -0.0438 253 PHE A CD2 
2011 C CE1 . PHE A 253 ? 0.4073 0.3808 0.3799 0.0050  0.0205  -0.0392 253 PHE A CE1 
2012 C CE2 . PHE A 253 ? 0.3794 0.3601 0.3630 -0.0035 0.0104  -0.0361 253 PHE A CE2 
2013 C CZ  . PHE A 253 ? 0.4128 0.3929 0.3945 0.0019  0.0164  -0.0340 253 PHE A CZ  
2014 N N   . TRP A 254 ? 0.3801 0.3575 0.3280 -0.0141 -0.0097 -0.0594 254 TRP A N   
2015 C CA  . TRP A 254 ? 0.4007 0.3933 0.3535 -0.0131 -0.0155 -0.0539 254 TRP A CA  
2016 C C   . TRP A 254 ? 0.3696 0.3639 0.3040 -0.0094 -0.0201 -0.0553 254 TRP A C   
2017 O O   . TRP A 254 ? 0.3554 0.3571 0.2875 -0.0050 -0.0221 -0.0489 254 TRP A O   
2018 C CB  . TRP A 254 ? 0.4091 0.4124 0.3772 -0.0199 -0.0225 -0.0556 254 TRP A CB  
2019 C CG  . TRP A 254 ? 0.3514 0.3534 0.3366 -0.0234 -0.0175 -0.0522 254 TRP A CG  
2020 C CD1 . TRP A 254 ? 0.3597 0.3562 0.3528 -0.0316 -0.0174 -0.0567 254 TRP A CD1 
2021 C CD2 . TRP A 254 ? 0.3746 0.3791 0.3685 -0.0192 -0.0117 -0.0436 254 TRP A CD2 
2022 N NE1 . TRP A 254 ? 0.3226 0.3175 0.3277 -0.0321 -0.0115 -0.0506 254 TRP A NE1 
2023 C CE2 . TRP A 254 ? 0.3392 0.3396 0.3448 -0.0243 -0.0084 -0.0430 254 TRP A CE2 
2024 C CE3 . TRP A 254 ? 0.3825 0.3905 0.3739 -0.0123 -0.0090 -0.0367 254 TRP A CE3 
2025 C CZ2 . TRP A 254 ? 0.3727 0.3738 0.3866 -0.0216 -0.0032 -0.0358 254 TRP A CZ2 
2026 C CZ3 . TRP A 254 ? 0.3671 0.3758 0.3680 -0.0105 -0.0041 -0.0305 254 TRP A CZ3 
2027 C CH2 . TRP A 254 ? 0.3706 0.3764 0.3822 -0.0147 -0.0016 -0.0301 254 TRP A CH2 
2028 N N   . ARG A 255 ? 0.3737 0.3588 0.2923 -0.0107 -0.0215 -0.0636 255 ARG A N   
2029 C CA  . ARG A 255 ? 0.3827 0.3669 0.2796 -0.0063 -0.0244 -0.0643 255 ARG A CA  
2030 C C   . ARG A 255 ? 0.4160 0.3942 0.3027 -0.0001 -0.0140 -0.0582 255 ARG A C   
2031 O O   . ARG A 255 ? 0.4202 0.4002 0.2942 0.0041  -0.0149 -0.0529 255 ARG A O   
2032 C CB  . ARG A 255 ? 0.3978 0.3733 0.2783 -0.0094 -0.0288 -0.0756 255 ARG A CB  
2033 C CG  . ARG A 255 ? 0.4429 0.4169 0.2982 -0.0043 -0.0318 -0.0756 255 ARG A CG  
2034 C CD  . ARG A 255 ? 0.5101 0.4754 0.3468 -0.0069 -0.0369 -0.0872 255 ARG A CD  
2035 N NE  . ARG A 255 ? 0.5236 0.4969 0.3693 -0.0146 -0.0496 -0.0945 255 ARG A NE  
2036 C CZ  . ARG A 255 ? 0.5476 0.5372 0.3966 -0.0147 -0.0619 -0.0930 255 ARG A CZ  
2037 N NH1 . ARG A 255 ? 0.5626 0.5593 0.4050 -0.0066 -0.0632 -0.0836 255 ARG A NH1 
2038 N NH2 . ARG A 255 ? 0.5329 0.5317 0.3918 -0.0230 -0.0730 -0.1011 255 ARG A NH2 
2039 N N   . ARG A 256 ? 0.4092 0.3805 0.3016 0.0005  -0.0040 -0.0586 256 ARG A N   
2040 C CA  . ARG A 256 ? 0.4478 0.4178 0.3363 0.0051  0.0062  -0.0526 256 ARG A CA  
2041 C C   . ARG A 256 ? 0.4218 0.4001 0.3206 0.0060  0.0061  -0.0426 256 ARG A C   
2042 O O   . ARG A 256 ? 0.4137 0.3913 0.3024 0.0085  0.0102  -0.0370 256 ARG A O   
2043 C CB  . ARG A 256 ? 0.4725 0.4377 0.3698 0.0065  0.0155  -0.0549 256 ARG A CB  
2044 C CG  . ARG A 256 ? 0.5359 0.4899 0.4199 0.0079  0.0186  -0.0645 256 ARG A CG  
2045 C CD  . ARG A 256 ? 0.5154 0.4671 0.4032 0.0131  0.0305  -0.0648 256 ARG A CD  
2046 N NE  . ARG A 256 ? 0.4276 0.3807 0.3361 0.0135  0.0318  -0.0623 256 ARG A NE  
2047 C CZ  . ARG A 256 ? 0.4812 0.4248 0.3947 0.0118  0.0286  -0.0672 256 ARG A CZ  
2048 N NH1 . ARG A 256 ? 0.5437 0.4768 0.4451 0.0083  0.0233  -0.0754 256 ARG A NH1 
2049 N NH2 . ARG A 256 ? 0.4896 0.4332 0.4192 0.0131  0.0304  -0.0638 256 ARG A NH2 
2050 N N   . VAL A 257 ? 0.3738 0.3583 0.2915 0.0037  0.0022  -0.0403 257 VAL A N   
2051 C CA  . VAL A 257 ? 0.3441 0.3350 0.2696 0.0050  0.0015  -0.0319 257 VAL A CA  
2052 C C   . VAL A 257 ? 0.3631 0.3558 0.2752 0.0078  -0.0050 -0.0291 257 VAL A C   
2053 O O   . VAL A 257 ? 0.3873 0.3775 0.2921 0.0107  -0.0021 -0.0222 257 VAL A O   
2054 C CB  . VAL A 257 ? 0.3401 0.3373 0.2859 0.0023  -0.0017 -0.0310 257 VAL A CB  
2055 C CG1 . VAL A 257 ? 0.3349 0.3385 0.2870 0.0046  -0.0037 -0.0236 257 VAL A CG1 
2056 C CG2 . VAL A 257 ? 0.3251 0.3184 0.2814 0.0013  0.0051  -0.0318 257 VAL A CG2 
2057 N N   . HIS A 258 ? 0.3773 0.3740 0.2855 0.0069  -0.0144 -0.0343 258 HIS A N   
2058 C CA  . HIS A 258 ? 0.3894 0.3891 0.2843 0.0111  -0.0223 -0.0317 258 HIS A CA  
2059 C C   . HIS A 258 ? 0.4336 0.4221 0.3033 0.0146  -0.0174 -0.0292 258 HIS A C   
2060 O O   . HIS A 258 ? 0.4607 0.4458 0.3190 0.0192  -0.0179 -0.0219 258 HIS A O   
2061 C CB  . HIS A 258 ? 0.3776 0.3848 0.2720 0.0087  -0.0336 -0.0396 258 HIS A CB  
2062 C CG  . HIS A 258 ? 0.3715 0.3823 0.2495 0.0143  -0.0434 -0.0381 258 HIS A CG  
2063 N ND1 . HIS A 258 ? 0.4224 0.4243 0.2737 0.0166  -0.0450 -0.0410 258 HIS A ND1 
2064 C CD2 . HIS A 258 ? 0.3530 0.3755 0.2364 0.0191  -0.0524 -0.0342 258 HIS A CD2 
2065 C CE1 . HIS A 258 ? 0.3991 0.4062 0.2391 0.0226  -0.0551 -0.0382 258 HIS A CE1 
2066 N NE2 . HIS A 258 ? 0.4388 0.4589 0.2987 0.0247  -0.0600 -0.0342 258 HIS A NE2 
2067 N N   . ASP A 259 ? 0.4351 0.4165 0.2945 0.0128  -0.0123 -0.0352 259 ASP A N   
2068 C CA  . ASP A 259 ? 0.4635 0.4350 0.2972 0.0157  -0.0068 -0.0335 259 ASP A CA  
2069 C C   . ASP A 259 ? 0.5048 0.4721 0.3390 0.0163  0.0042  -0.0247 259 ASP A C   
2070 O O   . ASP A 259 ? 0.5369 0.4962 0.3506 0.0188  0.0075  -0.0192 259 ASP A O   
2071 C CB  . ASP A 259 ? 0.4749 0.4403 0.2990 0.0141  -0.0024 -0.0427 259 ASP A CB  
2072 C CG  . ASP A 259 ? 0.5562 0.5217 0.3686 0.0134  -0.0140 -0.0514 259 ASP A CG  
2073 O OD1 . ASP A 259 ? 0.5367 0.5096 0.3490 0.0146  -0.0259 -0.0499 259 ASP A OD1 
2074 O OD2 . ASP A 259 ? 0.5872 0.5456 0.3902 0.0119  -0.0115 -0.0603 259 ASP A OD2 
2075 N N   . SER A 260 ? 0.4642 0.4359 0.3205 0.0137  0.0097  -0.0231 260 SER A N   
2076 C CA  . SER A 260 ? 0.4913 0.4606 0.3501 0.0126  0.0200  -0.0162 260 SER A CA  
2077 C C   . SER A 260 ? 0.4785 0.4466 0.3402 0.0136  0.0170  -0.0079 260 SER A C   
2078 O O   . SER A 260 ? 0.5061 0.4672 0.3594 0.0126  0.0240  -0.0015 260 SER A O   
2079 C CB  . SER A 260 ? 0.4898 0.4651 0.3701 0.0099  0.0266  -0.0186 260 SER A CB  
2080 O OG  . SER A 260 ? 0.5159 0.4909 0.3954 0.0102  0.0299  -0.0265 260 SER A OG  
2081 N N   . PHE A 261 ? 0.4022 0.3765 0.2761 0.0152  0.0077  -0.0079 261 PHE A N   
2082 C CA  . PHE A 261 ? 0.4073 0.3801 0.2860 0.0172  0.0060  -0.0008 261 PHE A CA  
2083 C C   . PHE A 261 ? 0.4575 0.4298 0.3259 0.0235  -0.0041 0.0019  261 PHE A C   
2084 O O   . PHE A 261 ? 0.4719 0.4377 0.3362 0.0270  -0.0044 0.0087  261 PHE A O   
2085 C CB  . PHE A 261 ? 0.3814 0.3629 0.2852 0.0150  0.0055  -0.0019 261 PHE A CB  
2086 C CG  . PHE A 261 ? 0.3743 0.3570 0.2891 0.0104  0.0143  -0.0033 261 PHE A CG  
2087 C CD1 . PHE A 261 ? 0.3723 0.3500 0.2854 0.0080  0.0219  0.0015  261 PHE A CD1 
2088 C CD2 . PHE A 261 ? 0.3540 0.3424 0.2804 0.0086  0.0147  -0.0095 261 PHE A CD2 
2089 C CE1 . PHE A 261 ? 0.3604 0.3427 0.2853 0.0043  0.0290  -0.0001 261 PHE A CE1 
2090 C CE2 . PHE A 261 ? 0.3494 0.3397 0.2855 0.0065  0.0220  -0.0106 261 PHE A CE2 
2091 C CZ  . PHE A 261 ? 0.3579 0.3472 0.2946 0.0045  0.0288  -0.0060 261 PHE A CZ  
2092 N N   . ILE A 262 ? 0.4229 0.4016 0.2868 0.0254  -0.0127 -0.0035 262 ILE A N   
2093 C CA  . ILE A 262 ? 0.4235 0.4067 0.2819 0.0322  -0.0241 -0.0018 262 ILE A CA  
2094 C C   . ILE A 262 ? 0.5040 0.4770 0.3325 0.0369  -0.0269 0.0003  262 ILE A C   
2095 O O   . ILE A 262 ? 0.5599 0.5243 0.3737 0.0436  -0.0292 0.0077  262 ILE A O   
2096 C CB  . ILE A 262 ? 0.4032 0.4038 0.2793 0.0304  -0.0336 -0.0095 262 ILE A CB  
2097 C CG1 . ILE A 262 ? 0.4250 0.4339 0.3283 0.0262  -0.0299 -0.0102 262 ILE A CG1 
2098 C CG2 . ILE A 262 ? 0.4131 0.4229 0.2856 0.0380  -0.0461 -0.0083 262 ILE A CG2 
2099 C CD1 . ILE A 262 ? 0.4439 0.4519 0.3536 0.0310  -0.0285 -0.0028 262 ILE A CD1 
2100 N N   . GLU A 263 ? 0.5258 0.4975 0.3430 0.0339  -0.0263 -0.0059 263 GLU A N   
2101 C CA  . GLU A 263 ? 0.6834 0.6459 0.4704 0.0391  -0.0302 -0.0040 263 GLU A CA  
2102 C C   . GLU A 263 ? 0.7696 0.7238 0.5405 0.0349  -0.0216 -0.0084 263 GLU A C   
2103 O O   . GLU A 263 ? 0.8293 0.7895 0.6028 0.0319  -0.0251 -0.0179 263 GLU A O   
2104 C CB  . GLU A 263 ? 0.7527 0.7281 0.5391 0.0438  -0.0467 -0.0088 263 GLU A CB  
2105 C CG  . GLU A 263 ? 0.8276 0.7952 0.5816 0.0506  -0.0539 -0.0074 263 GLU A CG  
2106 C CD  . GLU A 263 ? 0.8623 0.8166 0.5980 0.0596  -0.0537 0.0046  263 GLU A CD  
2107 O OE1 . GLU A 263 ? 0.8621 0.8161 0.6128 0.0614  -0.0509 0.0107  263 GLU A OE1 
2108 O OE2 . GLU A 263 ? 0.9139 0.8559 0.6177 0.0651  -0.0562 0.0080  263 GLU A OE2 
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