data_8QG5
# 
_entry.id   8QG5 
# 
_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   8QG5         pdb_00008qg5 10.2210/pdb8qg5/pdb 
WWPDB D_1292132969 ?            ?                   
# 
_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                        8QG5 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8A9V 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gilles.labesse@cbs.cnrs.fr 
_pdbx_contact_author.name_first         Gilles 
_pdbx_contact_author.name_last          Labesse 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6861-3300 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gelin, M.'   1 ? 
'Labesse, G.' 2 ? 
'Lionne, C.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a di-adenosine derivative' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gelin, M.'      1 ? 
primary 'Labesse, G.'    2 ? 
primary 'Clement, D.'    3 ? 
primary 'Pochet, S.'     4 ? 
primary 'Lionne, C.'     5 ? 
primary 'Leseigneur, C.' 6 ? 
primary 'Huteau, V.'     7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'NAD kinase 1' 31045.279 1  2.7.1.23 ? ? ? 
2 non-polymer syn 'CITRIC ACID' 192.124   1  ?        ? ? ? 
3 non-polymer syn 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-(phenylmethyl)purin-8-yl]prop-2-ynyl-methyl-amino]methyl]oxolane-3,4-diol
;
541.564   1  ?        ? ? ? 
4 water       nat water 18.015    39 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ATP-dependent NAD kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-(phenylmethyl)purin-8-yl]prop-2-ynyl-methyl-amino]methyl]oxolane-3,4-diol
;
UY6 
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 
UY6 non-polymer         . 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-(phenylmethyl)purin-8-yl]prop-2-ynyl-methyl-amino]methyl]oxolane-3,4-diol
;
? 'C26 H27 N11 O3' 541.564 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ILE 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 LYS 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ASP 264 264 ?   ?   ?   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        UY6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UY6 
_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 UY6 1  302 1   UY6 PDB A . 
D 4 HOH 1  401 22  HOH HOH A . 
D 4 HOH 2  402 28  HOH HOH A . 
D 4 HOH 3  403 25  HOH HOH A . 
D 4 HOH 4  404 1   HOH HOH A . 
D 4 HOH 5  405 20  HOH HOH A . 
D 4 HOH 6  406 143 HOH HOH A . 
D 4 HOH 7  407 15  HOH HOH A . 
D 4 HOH 8  408 34  HOH HOH A . 
D 4 HOH 9  409 24  HOH HOH A . 
D 4 HOH 10 410 144 HOH HOH A . 
D 4 HOH 11 411 21  HOH HOH A . 
D 4 HOH 12 412 10  HOH HOH A . 
D 4 HOH 13 413 139 HOH HOH A . 
D 4 HOH 14 414 33  HOH HOH A . 
D 4 HOH 15 415 30  HOH HOH A . 
D 4 HOH 16 416 29  HOH HOH A . 
D 4 HOH 17 417 3   HOH HOH A . 
D 4 HOH 18 418 5   HOH HOH A . 
D 4 HOH 19 419 53  HOH HOH A . 
D 4 HOH 20 420 7   HOH HOH A . 
D 4 HOH 21 421 145 HOH HOH A . 
D 4 HOH 22 422 86  HOH HOH A . 
D 4 HOH 23 423 146 HOH HOH A . 
D 4 HOH 24 424 26  HOH HOH A . 
D 4 HOH 25 425 98  HOH HOH A . 
D 4 HOH 26 426 136 HOH HOH A . 
D 4 HOH 27 427 134 HOH HOH A . 
D 4 HOH 28 428 102 HOH HOH A . 
D 4 HOH 29 429 48  HOH HOH A . 
D 4 HOH 30 430 49  HOH HOH A . 
D 4 HOH 31 431 82  HOH HOH A . 
D 4 HOH 32 432 117 HOH HOH A . 
D 4 HOH 33 433 38  HOH HOH A . 
D 4 HOH 34 434 66  HOH HOH A . 
D 4 HOH 35 435 141 HOH HOH A . 
D 4 HOH 36 436 138 HOH HOH A . 
D 4 HOH 37 437 131 HOH HOH A . 
D 4 HOH 38 438 32  HOH HOH A . 
D 4 HOH 39 439 142 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A LYS 92  ? CG  ? A LYS 92  CG  
6  1 Y 1 A LYS 92  ? CD  ? A LYS 92  CD  
7  1 Y 1 A LYS 92  ? CE  ? A LYS 92  CE  
8  1 Y 1 A LYS 92  ? NZ  ? A LYS 92  NZ  
9  1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
10 1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
11 1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
12 1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
13 1 Y 1 A LYS 114 ? CG  ? A LYS 114 CG  
14 1 Y 1 A LYS 114 ? CD  ? A LYS 114 CD  
15 1 Y 1 A LYS 114 ? CE  ? A LYS 114 CE  
16 1 Y 1 A LYS 114 ? NZ  ? A LYS 114 NZ  
17 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
18 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
19 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
20 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QG5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.853 
_cell.length_a_esd                 ? 
_cell.length_b                     76.192 
_cell.length_b_esd                 ? 
_cell.length_c                     118.920 
_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                         8QG5 
_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                   8QG5 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.36 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 325 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-09-16 
_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   0.872600 
_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 ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.872600 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QG5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.63 
_reflns.d_resolution_low                               64.15 
_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                                     8809 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.144 
_reflns.pdbx_Rpim_I_all                                0.058 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       54727 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.132 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.63 
_reflns_shell.d_res_low                                     2.75 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6674 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1070 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.2 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.2 
_reflns_shell.pdbx_Rrim_I_all                               0.897 
_reflns_shell.pdbx_Rpim_I_all                               0.356 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.901 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.822 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8QG5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.630 
_refine.ls_d_res_low                             55.569 
_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                     8794 
_refine.ls_number_reflns_R_free                  435 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.83 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2094 
_refine.ls_R_factor_R_free                       0.2228 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2087 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.59 
_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                            0.32 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.630 
_refine_hist.d_res_low                        55.569 
_refine_hist.number_atoms_solvent             39 
_refine_hist.number_atoms_total               2154 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2062 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 2183 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.753  ? 2959 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.134 ? 1275 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.087  ? 318  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 376  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.6302 3.0108 . . 132 2737 100.00 . . . . 0.2868 . . . . . . . . . . . 0.3378 
'X-RAY DIFFRACTION' 3.0108 3.7932 . . 139 2763 100.00 . . . . 0.2268 . . . . . . . . . . . 0.2275 
'X-RAY DIFFRACTION' 3.7932 55.569 . . 164 2859 100.00 . . . . 0.1788 . . . . . . . . . . . 0.1952 
# 
_struct.entry_id                     8QG5 
_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        8QG5 
_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              8QG5 
_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 8QG5 LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QG5 GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QG5 HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QG5 HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QG5 HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QG5 HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QG5 HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QG5 HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D 
1 2 A,B,C,D 
1 3 A,B,C,D 
1 4 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 62.8530000000 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 62.8530000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 58  ? ILE A 62  ? ARG A 58  ILE A 62  5 ? 5  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? LYS A 92  ? GLU A 82  LYS A 92  1 ? 11 
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  ? LYS A 108 ? GLN A 96  LYS A 108 
AA2 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? 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 TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 1 2 O PHE A 201 ? O PHE A 201 N MET A 179 ? N MET A 179 
AA3 2 3 O GLN A 180 ? O GLN A 180 N SER A 155 ? N SER A 155 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 5 6 N VAL A 221 ? N VAL A 221 O LEU A 224 ? O LEU A 224 
# 
_pdbx_entry_details.entry_id                   8QG5 
_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 ASP A 32  ? ? -161.49 116.61  
2 1 GLU A 94  ? ? 52.71   73.08   
3 1 TYR A 109 ? ? -121.22 -137.84 
4 1 ASN A 122 ? ? -95.08  -76.65  
5 1 ALA A 162 ? ? -102.93 -119.24 
6 1 ASN A 189 ? ? -140.49 -143.52 
7 1 ASN A 213 ? ? -131.07 -76.42  
8 1 ASP A 222 ? ? 59.19   -127.25 
9 1 ILE A 262 ? ? -93.23  -61.82  
# 
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 13.3997 24.7990 22.5059 0.4583 ? 0.0381 ? -0.0027 ? 0.5669 ? -0.1438 ? 0.3975 ? 4.7713 ? -1.3699 ? 
-2.9124 ? 3.3167 ? 1.6679 ? 6.9519 ? 0.1032 ? -0.7512 ? 0.3555 ? 0.1933  ? -0.0088 ? -0.0283 ? -0.5263 ? -0.0505 ? -0.0709 ? 
2 'X-RAY DIFFRACTION' ? refined 19.0525 13.7206 -1.9052 0.2544 ? 0.0234 ? 0.0467  ? 0.3248 ? 0.0242  ? 0.3043 ? 2.1614 ? -0.1047 ? 
0.5301  ? 2.3333 ? 0.5504 ? 4.7556 ? 0.0870 ? 0.1258  ? 0.1378 ? -0.0686 ? -0.0992 ? 0.3294  ? -0.0604 ? -0.3648 ? 0.0101  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 101 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 102 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 ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A ASP 264 ? A ASP 264 
5  1 Y 1 A LEU 265 ? A LEU 265 
6  1 Y 1 A GLU 266 ? A GLU 266 
7  1 Y 1 A HIS 267 ? A HIS 267 
8  1 Y 1 A HIS 268 ? A HIS 268 
9  1 Y 1 A HIS 269 ? A HIS 269 
10 1 Y 1 A HIS 270 ? A HIS 270 
11 1 Y 1 A HIS 271 ? A HIS 271 
12 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 
UY6 C2   C Y N 393 
UY6 C4   C Y N 394 
UY6 C5   C Y N 395 
UY6 C6   C Y N 396 
UY6 N9   N Y N 397 
UY6 C8   C Y N 398 
UY6 CAA  C N R 399 
UY6 CAB  C N S 400 
UY6 CAD  C N R 401 
UY6 CAF  C N R 402 
UY6 CAR  C N N 403 
UY6 CAT  C N N 404 
UY6 CAU  C N N 405 
UY6 CAV  C N N 406 
UY6 CAW  C N N 407 
UY6 CAX  C Y N 408 
UY6 CAZ  C N N 409 
UY6 CBA  C Y N 410 
UY6 CBB  C Y N 411 
UY6 CBC  C Y N 412 
UY6 CBD  C Y N 413 
UY6 CBE  C Y N 414 
UY6 CBF  C Y N 415 
UY6 CBG  C Y N 416 
UY6 CBH  C Y N 417 
UY6 CBJ  C Y N 418 
UY6 CBM  C Y N 419 
UY6 N1   N Y N 420 
UY6 N3   N Y N 421 
UY6 N6   N N N 422 
UY6 N7   N Y N 423 
UY6 NAS  N N N 424 
UY6 NAY  N Y N 425 
UY6 NBI  N Y N 426 
UY6 NBK  N N N 427 
UY6 NBL  N Y N 428 
UY6 NBN  N Y N 429 
UY6 OAC  O N N 430 
UY6 OAE  O N N 431 
UY6 OAQ  O N N 432 
UY6 H1   H N N 433 
UY6 H2   H N N 434 
UY6 H3   H N N 435 
UY6 H4   H N N 436 
UY6 H5   H N N 437 
UY6 H6   H N N 438 
UY6 H7   H N N 439 
UY6 H8   H N N 440 
UY6 H9   H N N 441 
UY6 H10  H N N 442 
UY6 H11  H N N 443 
UY6 H12  H N N 444 
UY6 H13  H N N 445 
UY6 H14  H N N 446 
UY6 H15  H N N 447 
UY6 H16  H N N 448 
UY6 H17  H N N 449 
UY6 H18  H N N 450 
UY6 H19  H N N 451 
UY6 H20  H N N 452 
UY6 H21  H N N 453 
UY6 H22  H N N 454 
UY6 H23  H N N 455 
UY6 H25  H N N 456 
UY6 H26  H N N 457 
UY6 H27  H N N 458 
UY6 H28  H N N 459 
VAL N    N N N 460 
VAL CA   C N S 461 
VAL C    C N N 462 
VAL O    O N N 463 
VAL CB   C N N 464 
VAL CG1  C N N 465 
VAL CG2  C N N 466 
VAL OXT  O N N 467 
VAL H    H N N 468 
VAL H2   H N N 469 
VAL HA   H N N 470 
VAL HB   H N N 471 
VAL HG11 H N N 472 
VAL HG12 H N N 473 
VAL HG13 H N N 474 
VAL HG21 H N N 475 
VAL HG22 H N N 476 
VAL HG23 H N N 477 
VAL HXT  H N N 478 
# 
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 
UY6 N6  C6   sing N N 378 
UY6 N7  C8   doub Y N 379 
UY6 N7  C5   sing Y N 380 
UY6 C8  N9   sing Y N 381 
UY6 C6  C5   doub Y N 382 
UY6 C6  N1   sing Y N 383 
UY6 C5  C4   sing Y N 384 
UY6 CAD CAB  sing N N 385 
UY6 CAD OAE  sing N N 386 
UY6 CAD CAF  sing N N 387 
UY6 N1  C2   doub Y N 388 
UY6 N9  C4   sing Y N 389 
UY6 N9  CAF  sing N N 390 
UY6 OAC CAB  sing N N 391 
UY6 C4  N3   doub Y N 392 
UY6 CAB CAA  sing N N 393 
UY6 CAF OAQ  sing N N 394 
UY6 C2  N3   sing Y N 395 
UY6 OAQ CAA  sing N N 396 
UY6 CAA CAR  sing N N 397 
UY6 CAR NAS  sing N N 398 
UY6 NBK CBJ  sing N N 399 
UY6 NAS CAT  sing N N 400 
UY6 NAS CAU  sing N N 401 
UY6 CBJ CBH  doub Y N 402 
UY6 CBJ NBL  sing Y N 403 
UY6 NBI CBH  sing Y N 404 
UY6 NBI CAX  doub Y N 405 
UY6 CBH CBG  sing Y N 406 
UY6 NBL CBM  doub Y N 407 
UY6 CBC CBD  doub Y N 408 
UY6 CBC CBB  sing Y N 409 
UY6 CBD CBE  sing Y N 410 
UY6 CAU CAV  sing N N 411 
UY6 CAV CAW  trip N N 412 
UY6 CAW CAX  sing N N 413 
UY6 CAX NAY  sing Y N 414 
UY6 CBB CBA  doub Y N 415 
UY6 CBG NAY  sing Y N 416 
UY6 CBG NBN  doub Y N 417 
UY6 CBE CBF  doub Y N 418 
UY6 CBM NBN  sing Y N 419 
UY6 NAY CAZ  sing N N 420 
UY6 CBA CBF  sing Y N 421 
UY6 CBA CAZ  sing N N 422 
UY6 C2  H1   sing N N 423 
UY6 C8  H2   sing N N 424 
UY6 CAA H3   sing N N 425 
UY6 CAB H4   sing N N 426 
UY6 CAD H5   sing N N 427 
UY6 CAF H6   sing N N 428 
UY6 CAR H7   sing N N 429 
UY6 CAR H8   sing N N 430 
UY6 CAT H9   sing N N 431 
UY6 CAT H10  sing N N 432 
UY6 CAT H11  sing N N 433 
UY6 CAU H12  sing N N 434 
UY6 CAU H13  sing N N 435 
UY6 CAZ H14  sing N N 436 
UY6 CAZ H15  sing N N 437 
UY6 CBB H16  sing N N 438 
UY6 CBC H17  sing N N 439 
UY6 CBD H18  sing N N 440 
UY6 CBE H19  sing N N 441 
UY6 CBF H20  sing N N 442 
UY6 CBM H21  sing N N 443 
UY6 N6  H22  sing N N 444 
UY6 N6  H23  sing N N 445 
UY6 NBK H25  sing N N 446 
UY6 NBK H26  sing N N 447 
UY6 OAC H27  sing N N 448 
UY6 OAE H28  sing N N 449 
VAL N   CA   sing N N 450 
VAL N   H    sing N N 451 
VAL N   H2   sing N N 452 
VAL CA  C    sing N N 453 
VAL CA  CB   sing N N 454 
VAL CA  HA   sing N N 455 
VAL C   O    doub N N 456 
VAL C   OXT  sing N N 457 
VAL CB  CG1  sing N N 458 
VAL CB  CG2  sing N N 459 
VAL CB  HB   sing N N 460 
VAL CG1 HG11 sing N N 461 
VAL CG1 HG12 sing N N 462 
VAL CG1 HG13 sing N N 463 
VAL CG2 HG21 sing N N 464 
VAL CG2 HG22 sing N N 465 
VAL CG2 HG23 sing N N 466 
VAL OXT HXT  sing N N 467 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-17-CE18-0011-02 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   8A9V 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    8QG5 
_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]   0.015910 
_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]   0.013125 
_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]   0.008409 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 10.875 37.510 25.523  0.60 73.69  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.398 37.323 24.158  0.60 72.43  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.475  36.111 24.066  0.60 68.64  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.330  35.357 25.028  0.60 58.39  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.579 37.173 23.196  0.60 62.02  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.485 35.990 23.498  0.60 63.69  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 13.970 35.968 22.474  0.60 64.55  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 14.780 37.471 23.016  0.60 70.70  ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 8.850  35.930 22.904  1.00 67.02  ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 7.913  34.833 22.708  1.00 63.90  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.656  33.523 22.480  1.00 59.75  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.688  33.486 21.803  1.00 58.60  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 6.988  35.126 21.526  1.00 64.37  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.006  36.264 21.769  1.00 68.26  ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.199  36.573 20.517  0.87 70.29  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.181  37.677 20.764  1.00 75.38  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.103  37.248 21.696  0.97 76.17  ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.122  32.442 23.046  1.00 58.06  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 8.756  31.136 22.945  1.00 55.16  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.689  30.052 22.996  1.00 54.98  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.540  30.295 23.375  1.00 57.51  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 9.786  30.923 24.063  1.00 54.72  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.175  30.521 25.389  1.00 55.49  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.627  31.470 26.242  1.00 59.18  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.151  29.190 25.789  1.00 53.00  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.069  31.105 27.454  1.00 60.13  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.593  28.816 26.996  1.00 54.08  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.056  29.777 27.826  1.00 57.40  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.502  29.409 29.030  1.00 58.31  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.088  28.841 22.612  1.00 52.63  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.237  27.668 22.754  1.00 52.47  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.127  26.446 22.924  1.00 50.45  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.300  26.452 22.542  1.00 49.73  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.286  27.499 21.560  1.00 53.61  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 6.937  27.024 20.266  1.00 54.02  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.021  25.225 20.116  1.00 53.52  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.345  24.769 20.554  1.00 55.75  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.559  25.395 23.510  1.00 50.13  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.287  24.163 23.790  1.00 48.87  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.450  22.981 23.324  1.00 50.02  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.264  22.883 23.660  1.00 51.76  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.626  24.023 25.287  1.00 49.06  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.347  25.273 25.796  1.00 50.00  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.484  22.792 25.521  1.00 47.72  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.651  25.240 27.273  1.00 51.55  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.068  22.088 22.557  1.00 49.25  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.453  20.839 22.139  1.00 50.13  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.146  19.676 22.839  1.00 50.94  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.314  19.765 23.227  1.00 50.14  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 7.518  20.671 20.615  1.00 49.49  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 6.868  19.452 20.233  1.00 51.99  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 8.957  20.647 20.140  1.00 46.78  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.408  18.580 23.006  1.00 53.85  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 7.865  17.457 23.811  1.00 55.93  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.678  16.147 23.060  1.00 58.28  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.792  16.017 22.211  1.00 58.75  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.116  17.396 25.149  1.00 57.92  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.425  16.207 25.854  1.00 59.36  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.532  15.174 23.390  1.00 60.53  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.424  13.844 22.796  1.00 62.86  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.117  13.163 23.177  1.00 68.35  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.555  12.406 22.378  1.00 69.76  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.617  12.988 23.226  1.00 62.64  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.671  11.598 22.611  1.00 63.50  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.542 10.675 23.453  1.00 65.80  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.824 9.362  22.744  0.79 68.39  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 11.797 9.533  21.629  0.72 66.80  ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.621  13.413 24.386  1.00 73.54  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.354  12.868 24.834  1.00 75.60  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.445  11.860 25.960  1.00 77.44  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.413  11.296 26.343  1.00 80.45  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.633  11.611 26.503  1.00 74.57  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 6.804  10.652 27.581  1.00 75.92  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 6.907  11.378 28.922  1.00 75.64  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 6.830  12.606 29.006  1.00 73.57  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.033  9.774  27.329  1.00 75.05  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.302  10.583 27.151  1.00 72.02  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.214  11.725 26.659  0.87 69.48  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.388 10.075 27.500  0.88 73.27  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.081  10.593 29.989  1.00 77.98  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.158  11.160 31.331  1.00 78.35  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.361  12.082 31.479  1.00 75.11  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.265  13.146 32.103  1.00 74.71  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.221  10.039 32.368  1.00 82.61  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.899  9.723  33.040  1.00 85.26  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.933  8.408  33.793  0.67 89.57  ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.565  7.455  33.290  1.00 90.02  ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 5.336  8.327  34.887  0.96 92.72  ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.500  11.693 30.908  1.00 73.06  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.730 12.448 31.112  1.00 70.75  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.674 13.802 30.415  1.00 66.72  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 11.111 14.813 30.977  1.00 65.77  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.919 11.627 30.616  1.00 70.87  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.227 11.888 31.342  0.89 71.93  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.206 10.751 31.090  1.00 73.59  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.550 11.264 30.606  0.84 71.48  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 16.230 12.098 31.633  0.90 72.49  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.127 13.847 29.199  1.00 65.08  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.135 15.084 28.427  1.00 61.72  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.009  16.022 28.844  1.00 62.16  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.214  17.239 28.923  1.00 60.80  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.038 14.770 26.934  1.00 59.19  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.051 13.863 26.532  1.00 59.72  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.816  15.481 29.106  1.00 63.96  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.684  16.330 29.467  1.00 63.36  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 6.934  17.062 30.779  1.00 63.69  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.634  18.256 30.899  1.00 63.02  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.405  15.497 29.559  1.00 65.27  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.800  15.203 28.200  1.00 64.87  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.364  15.659 27.184  1.00 62.19  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.756  14.518 28.149  0.84 67.59  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.487  16.367 31.773  1.00 65.45  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 7.722  16.985 33.071  1.00 66.81  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 8.953  17.881 33.080  1.00 64.07  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.061  18.753 33.949  1.00 64.83  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 7.840  15.906 34.149  1.00 70.67  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 6.610  14.997 34.257  1.00 73.01  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 6.713  14.073 35.461  1.00 78.38  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 5.326  15.818 34.309  1.00 71.79  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 9.881  17.688 32.141  1.00 61.14  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 10.962 18.650 31.963  1.00 58.62  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.481 19.896 31.232  1.00 55.31  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 10.993 20.994 31.478  1.00 54.59  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.125 18.004 31.207  1.00 56.96  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.315 18.901 30.853  1.00 55.35  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 13.929 19.509 32.105  1.00 56.33  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.358 18.128 30.059  1.00 55.36  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.498  19.744 30.341  1.00 53.60  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 8.928  20.898 29.654  1.00 51.79  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.221  21.829 30.632  1.00 54.45  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.331  23.056 30.523  1.00 54.40  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 7.964  20.428 28.563  1.00 49.60  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.102  21.526 27.964  1.00 48.54  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.209  20.981 26.861  1.00 48.25  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.295  21.995 26.342  1.00 48.47  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.088  22.236 26.842  1.00 50.81  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.645  21.536 27.878  1.00 52.99  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.322  23.178 26.308  1.00 51.22  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.495  21.263 31.600  1.00 56.67  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.791  22.090 32.574  1.00 58.89  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.754  22.820 33.500  1.00 59.69  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.458  23.937 33.942  1.00 61.04  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.820  21.234 33.388  1.00 61.68  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.619  20.656 32.635  1.00 61.40  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.786  19.775 33.553  1.00 63.43  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.771  21.770 32.042  1.00 61.46  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.904  22.214 33.809  1.00 59.59  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.877  22.881 34.668  1.00 61.49  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.506 24.078 33.967  1.00 60.58  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.791 25.098 34.606  1.00 63.15  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.954 21.894 35.116  1.00 62.52  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.525 21.067 36.311  1.00 66.12  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.679  21.488 37.099  1.00 69.88  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.114 19.886 36.457  1.00 65.99  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.731 23.976 32.655  1.00 57.25  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.289 25.106 31.921  1.00 56.09  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.270 26.230 31.781  1.00 56.18  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.624 27.411 31.872  1.00 57.86  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.786 24.653 30.549  1.00 54.05  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 12.965 23.694 30.605  1.00 55.86  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.713 23.419 28.988  1.00 55.34  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.249 25.078 28.577  1.00 55.40  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 8.999  25.882 31.562  1.00 55.15  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 7.951  26.898 31.499  1.00 56.02  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 7.834  27.621 32.834  1.00 58.72  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.687  28.849 32.882  1.00 60.41  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.613  26.262 31.077  1.00 55.83  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.708  25.716 29.652  1.00 53.07  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.479  27.269 31.187  1.00 58.26  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.424  25.092 29.153  1.00 49.14  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 7.904  26.874 33.939  1.00 59.78  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 7.877  27.500 35.256  1.00 63.06  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.108  28.370 35.477  1.00 64.15  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.016  29.441 36.087  1.00 66.81  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.769  26.432 36.344  1.00 61.72  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.268 27.925 34.991  1.00 62.67  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.455 28.760 35.067  1.00 63.90  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.341 30.003 34.205  1.00 63.59  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.791 31.083 34.597  1.00 65.90  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.736 29.868 33.022  1.00 61.16  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.481 31.034 32.183  1.00 61.65  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.436  31.952 32.802  1.00 64.51  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.423  33.155 32.517  1.00 66.55  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.039 30.592 30.789  1.00 58.86  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.171 30.176 29.896  1.00 57.39  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.285 30.985 29.745  1.00 59.21  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.125 28.973 29.212  1.00 54.40  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.329 30.603 28.923  1.00 57.86  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.165 28.585 28.390  1.00 52.75  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.269 29.401 28.246  1.00 54.48  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.556  31.407 33.645  1.00 64.99  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.571  32.228 34.326  1.00 68.26  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.175  33.248 35.268  1.00 72.58  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.499  34.213 35.640  1.00 74.17  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.433  33.057 35.665  1.00 74.38  ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.151 34.010 36.497  1.00 78.22  ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 10.911 35.045 35.674  1.00 78.89  ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.780 35.739 36.215  1.00 80.77  ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.115 33.274 37.430  1.00 78.56  ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.489 32.127 38.210  1.00 77.12  ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.265  32.552 38.997  0.52 75.50  ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 8.234  31.851 38.919  1.00 73.99  ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 9.332  33.588 39.691  1.00 79.24  ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 10.607 35.161 34.383  1.00 78.03  ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.281 36.102 33.500  1.00 79.80  ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.253 36.776 32.603  1.00 81.66  ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.079  36.398 32.568  1.00 80.47  ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.352 35.410 32.646  1.00 75.46  ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.542 34.905 33.428  1.00 74.97  ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 14.629 35.731 33.683  1.00 77.70  ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 13.584 33.602 33.904  1.00 72.50  ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 15.721 35.275 34.395  1.00 74.62  ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 14.672 33.136 34.617  1.00 73.42  ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 15.738 33.977 34.859  1.00 76.37  ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 16.824 33.518 35.569  1.00 78.16  ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 10.714 37.788 31.866  1.00 85.60  ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 9.880  38.478 30.882  1.00 89.05  ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 9.881  37.664 29.586  1.00 88.71  ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.467 38.033 28.566  1.00 89.14  ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.373 39.903 30.667  1.00 93.93  ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.413  40.739 29.837  0.51 96.58  ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 9.317  40.512 28.613  0.71 94.77  ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 8.743  41.621 30.415  0.59 100.94 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.213  36.515 29.654  1.00 89.56  ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.085  35.598 28.530  1.00 87.17  ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.628  35.183 28.406  1.00 86.60  ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 6.997  34.818 29.403  1.00 87.27  ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 9.979  34.366 28.711  1.00 85.78  ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.469 34.655 28.610  1.00 88.25  ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.037 34.823 26.907  1.00 89.88  ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 11.814 33.149 26.311  0.78 85.72  ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.099  35.239 27.188  1.00 83.97  ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.700  34.939 26.915  1.00 81.34  ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.614  33.651 26.107  1.00 75.93  ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.223  33.545 25.038  1.00 75.11  ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.037  36.091 26.161  1.00 83.43  ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.626  35.796 25.684  1.00 84.60  ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.061  36.909 24.825  0.64 89.40  ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 1.936  36.751 24.306  0.60 91.04  ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 3.745  37.942 24.665  1.00 92.04  ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 4.861  32.679 26.615  1.00 72.40  ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.639  31.452 25.865  1.00 67.97  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.672  31.719 24.719  1.00 69.39  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.602  32.305 24.917  1.00 74.32  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.096  30.350 26.775  1.00 65.65  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.043  28.987 26.115  1.00 62.35  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 2.941  28.599 25.361  1.00 62.67  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.095  28.090 26.244  1.00 59.68  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 2.891  27.358 24.755  1.00 60.63  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.052  26.845 25.642  1.00 57.70  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 3.948  26.485 24.899  1.00 58.34  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 3.900  25.248 24.297  1.00 57.36  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.051  31.290 23.518  1.00 65.01  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.236  31.520 22.328  1.00 65.36  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.689  30.544 21.257  1.00 63.93  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 4.839  30.608 20.813  1.00 62.99  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.377  32.967 21.844  1.00 67.62  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.337  33.345 20.802  1.00 71.28  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 1.767  32.440 20.158  1.00 71.04  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.090  34.556 20.625  0.87 75.33  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 2.797  29.644 20.845  1.00 64.19  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.088  28.696 19.779  1.00 62.02  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.502  29.131 18.438  1.00 63.71  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.402  28.314 17.517  1.00 63.03  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.590  27.299 20.158  1.00 60.27  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.145  27.294 20.613  1.00 62.08  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.479  28.345 20.515  0.83 64.37  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.677  26.232 21.076  0.83 61.58  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.117  30.400 18.312  1.00 66.42  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.611  30.936 17.053  1.00 69.39  ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 2.740  31.665 16.338  1.00 69.10  ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.103  31.317 15.209  1.00 68.69  ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.407  31.867 17.277  1.00 74.17  ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? -0.056 32.459 15.955  1.00 76.81  ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.726 31.115 17.957  1.00 75.84  ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.306  32.682 16.992  1.00 70.12  ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.446  33.431 16.468  1.00 70.32  ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.585  33.402 17.484  1.00 67.88  ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 5.930  34.437 18.072  1.00 69.95  ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.065  34.873 16.139  1.00 75.08  ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 2.839  35.026 15.252  1.00 78.78  ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.573  36.474 14.880  0.72 84.59  ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 3.179  36.961 13.902  1.00 86.14  ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 1.765  37.129 15.574  1.00 88.44  ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.195  32.242 17.714  1.00 63.27  ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.326  32.190 18.639  1.00 61.51  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.616  32.633 17.969  1.00 60.56  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.793  32.517 16.755  1.00 60.25  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.391  30.710 19.031  1.00 58.63  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 6.913  30.003 17.817  1.00 57.60  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 5.892  30.910 17.155  1.00 60.94  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.519  33.162 18.791  1.00 60.17  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 10.867 33.491 18.352  1.00 58.76  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 11.896 32.467 18.806  1.00 55.98  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 12.986 32.408 18.227  1.00 54.88  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.262 34.883 18.860  1.00 60.98  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.513 36.013 18.170  0.74 64.14  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 10.538 37.303 18.960  0.66 68.62  ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 10.481 37.237 20.204  1.00 68.85  ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.615 38.382 18.337  0.73 72.52  ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.567 31.660 19.812  1.00 54.62  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.435 30.600 20.310  1.00 52.02  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.613 29.322 20.372  1.00 49.22  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.572 29.285 21.038  1.00 48.69  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.017 30.929 21.694  1.00 52.96  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 13.810 32.236 21.652  1.00 54.87  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 13.886 29.783 22.182  1.00 51.45  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.003 32.189 20.738  0.38 54.11  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.073 28.280 19.684  1.00 47.46  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.415 26.979 19.684  1.00 45.97  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.341 25.984 20.368  1.00 45.15  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.472 25.765 19.916  1.00 44.48  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.057 26.520 18.263  1.00 44.68  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.702 25.041 18.256  1.00 42.65  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 9.902  27.345 17.722  1.00 46.66  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 11.862 25.384 21.453  1.00 45.34  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.630 24.430 22.243  1.00 45.41  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.057 23.040 22.010  1.00 44.51  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 10.844 22.831 22.142  1.00 44.97  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 12.611 24.794 23.737  1.00 47.78  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.146 26.212 23.944  1.00 48.86  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.419 23.787 24.544  1.00 48.60  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.069 26.691 25.376  1.00 50.55  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 12.926 22.096 21.661  1.00 44.23  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.546 20.712 21.421  1.00 45.23  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.138 19.833 22.514  1.00 44.85  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.332 19.929 22.814  1.00 44.23  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.025 20.244 20.045  1.00 46.61  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.776 18.862 19.861  1.00 48.59  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.303 18.983 23.105  1.00 45.46  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.719 18.090 24.180  1.00 46.80  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.368 16.665 23.778  1.00 47.52  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.186 16.333 23.624  1.00 46.82  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.060 18.453 25.520  1.00 48.57  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.419 19.886 25.918  1.00 48.78  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.487 17.478 26.606  1.00 50.78  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 11.850 20.314 27.251  1.00 51.22  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.388 15.829 23.608  1.00 49.80  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.192 14.450 23.211  1.00 52.28  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.363 13.901 22.422  1.00 52.51  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.416 13.596 22.989  1.00 53.25  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.189 13.770 21.111  1.00 51.16  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.261 13.321 20.247  1.00 50.93  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.338 14.133 18.972  1.00 50.45  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.647 15.147 18.838  1.00 49.79  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.178 13.703 18.027  1.00 51.56  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.237 14.386 16.739  1.00 50.56  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 14.932 14.235 15.968  1.00 49.44  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.589 15.104 15.160  1.00 48.65  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.410 13.861 15.912  1.00 51.22  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.749 14.374 16.408  1.00 51.55  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 18.775 15.449 17.044  1.00 51.64  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.774 13.707 16.157  1.00 51.89  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.197 13.146 16.202  1.00 49.84  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.885 13.009 15.592  1.00 50.10  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 11.904 14.047 16.098  1.00 50.54  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.111 14.594 15.325  1.00 51.66  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 11.938 14.329 17.402  1.00 50.09  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.120 15.405 17.948  1.00 48.83  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.566 16.760 17.414  1.00 46.63  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.730 17.644 17.189  1.00 46.17  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.179 15.385 19.477  1.00 49.38  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 10.762 14.101 19.955  1.00 52.97  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.269 16.455 20.068  1.00 48.00  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 12.871 16.936 17.194  1.00 45.92  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.367 18.194 16.647  1.00 45.16  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 12.892 18.396 15.214  1.00 44.65  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.545 19.516 14.823  1.00 45.13  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 14.894 18.231 16.718  1.00 45.11  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.489 19.560 16.343  1.00 45.03  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.760 19.869 15.018  1.00 45.17  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.784 20.500 17.317  1.00 45.31  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.307 21.090 14.674  1.00 45.50  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.332 21.722 16.978  1.00 45.87  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.594 22.017 15.655  1.00 46.01  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 12.879 17.325 14.416  1.00 43.83  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.423 17.435 13.035  1.00 43.18  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 10.960 17.855 12.969  1.00 44.51  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.567 18.626 12.085  1.00 45.85  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.636 16.110 12.304  1.00 43.78  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 13.772 16.058 11.281  1.00 44.11  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 15.084 16.525 11.893  1.00 42.82  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 13.910 14.651 10.723  1.00 46.29  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.139 17.358 13.896  1.00 44.80  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 8.744  17.780 13.941  1.00 46.05  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.630  19.257 14.292  1.00 46.21  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 7.795  19.972 13.725  1.00 48.03  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 7.969  16.924 14.943  1.00 46.76  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 7.966  15.561 14.554  1.00 48.02  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.469  19.735 15.216  1.00 44.55  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.459  21.151 15.564  1.00 44.82  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 9.900  22.018 14.392  1.00 46.38  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.433  23.154 14.254  1.00 47.74  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.353 21.403 16.779  1.00 43.15  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 10.794 21.505 13.545  1.00 46.12  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.247 22.271 12.389  1.00 46.11  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.139 22.402 11.353  1.00 47.98  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 9.822  23.511 10.906  1.00 49.13  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.488 21.611 11.784  1.00 44.66  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 12.783 22.042 10.374  1.00 44.75  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.356 23.277 10.115  1.00 45.87  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.495 21.206 9.308   1.00 44.31  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.628 23.672 8.815   1.00 47.28  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 12.765 21.595 8.010   1.00 46.26  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.332 22.829 7.762   1.00 47.62  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.534  21.277 10.961  1.00 48.97  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.459  21.306 9.977   1.00 52.02  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.197  21.963 10.512  1.00 56.28  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.370  22.425 9.718   1.00 59.66  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.138  19.889 9.506   1.00 51.75  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.225  19.263 8.688   1.00 50.97  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.399  19.537 7.348   1.00 52.14  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.194 18.378 9.020   1.00 49.42  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.428 18.846 6.890   1.00 51.12  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 10.929 18.136 7.884   1.00 49.53  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.026  22.015 11.834  1.00 57.11  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 5.854  22.677 12.395  1.00 60.45  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 5.913  24.185 12.188  1.00 62.34  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 4.867  24.840 12.124  1.00 65.61  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.723  22.339 13.881  1.00 60.81  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.463  22.876 14.550  1.00 65.80  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.428  22.570 16.035  1.00 68.42  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.109  21.659 16.507  1.00 68.06  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.639  23.335 16.782  1.00 70.67  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.118  24.746 12.062  1.00 61.26  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.307  26.182 11.892  1.00 63.10  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.215  26.494 10.708  1.00 64.61  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 8.948  27.486 10.730  1.00 65.73  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 7.876  26.816 13.162  1.00 61.49  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 6.973  26.708 14.368  1.00 61.66  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 5.949  27.622 14.576  1.00 64.14  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.151  25.698 15.304  1.00 60.02  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.123  27.529 15.678  1.00 65.04  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.329  25.597 16.409  1.00 61.07  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.317  26.516 16.591  1.00 63.50  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.495  26.422 17.689  1.00 64.22  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.174  25.671 9.658   1.00 65.25  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.047  25.909 8.513   1.00 65.79  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.627  27.117 7.685   1.00 68.55  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.253  27.379 6.651   1.00 69.70  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.111  24.663 7.625   1.00 65.60  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.759  24.099 7.215   1.00 68.00  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.881  22.976 6.199   1.00 68.54  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 7.751  23.251 4.986   1.00 71.30  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 8.120  21.820 6.611   1.00 67.17  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.597  27.849 8.109   1.00 70.22  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.137  29.051 7.427   1.00 73.88  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.732  30.323 8.018   1.00 73.57  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.612  31.390 7.407   1.00 76.94  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.605  29.129 7.483   1.00 76.85  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 4.901  27.804 7.188   1.00 76.63  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 4.339  27.723 5.778   0.77 80.14  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 3.677  28.688 5.339   0.76 84.11  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 4.558  26.690 5.111   0.76 79.31  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.367  30.238 9.185   1.00 70.92  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.936  31.381 9.900   1.00 71.61  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.370 31.084 10.328  1.00 68.07  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.787 31.376 11.452  1.00 68.35  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.087  31.743 11.118  1.00 73.13  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.639  31.271 11.055  0.72 75.17  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.785  31.872 12.169  1.00 78.46  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.586  32.477 13.230  1.00 78.24  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 6.806  33.783 13.348  0.94 80.65  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 6.287  34.627 12.464  0.98 83.99  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.550  34.243 14.345  1.00 79.57  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.151 30.507 9.408   1.00 64.71  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.517 30.096 9.724   1.00 63.21  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.415 31.288 10.034  1.00 67.71  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.245 31.226 10.949  1.00 68.78  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.101 29.289 8.565   1.00 61.87  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.535 27.874 8.418   1.00 61.47  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.079 27.184 7.181   1.00 61.51  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.855 27.061 9.657   1.00 60.47  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.269 32.377 9.285   1.00 72.42  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 14.168 33.518 9.407   1.00 76.35  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.915 34.362 10.655  1.00 75.41  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.555 35.406 10.813  1.00 77.77  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 14.075 34.395 8.155   1.00 82.73  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 12.716 34.313 7.476   1.00 84.71  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 11.879 33.481 7.885   1.00 83.80  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 12.488 35.088 6.523   1.00 90.08  ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 13.009 33.938 11.543  1.00 72.62  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.766 34.664 12.785  1.00 73.12  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.608 33.718 13.972  1.00 68.98  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 11.979 34.087 14.971  1.00 69.93  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 11.531 35.565 12.656  1.00 76.70  ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.382 34.931 11.895  1.00 77.13  ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 9.464  35.958 11.264  0.79 82.80  ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 8.341  36.154 11.776  0.61 84.54  ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 9.872  36.577 10.259  0.97 86.10  ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.161 32.511 13.885  1.00 64.37  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.089 31.521 14.950  1.00 60.23  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.485 30.957 15.166  1.00 57.56  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.189 30.645 14.199  1.00 57.60  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.091 30.394 14.618  1.00 58.32  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.663 30.944 14.574  1.00 59.98  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.191 29.267 15.631  1.00 56.23  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.612  29.900 14.259  1.00 58.73  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 14.891 30.845 16.428  1.00 56.03  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.144 30.201 16.807  1.00 53.93  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.797 28.898 17.515  1.00 52.10  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.189 28.913 18.590  1.00 54.36  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 16.987 31.112 17.695  1.00 55.24  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.175 27.778 16.909  1.00 48.87  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 15.839 26.467 17.439  1.00 46.40  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 16.860 26.016 18.476  1.00 48.27  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.054 26.312 18.376  1.00 49.69  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.759 25.434 16.314  1.00 43.15  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.592 25.632 15.390  1.00 43.37  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 14.701 26.451 14.279  1.00 45.04  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.386 24.995 15.631  1.00 42.74  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.629 26.634 13.426  1.00 46.07  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.310 25.173 14.782  1.00 44.03  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.432 25.994 13.678  1.00 45.58  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.371 25.299 19.486  1.00 48.38  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.209 24.684 20.508  1.00 48.97  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.734 23.252 20.707  1.00 48.75  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.531 22.973 20.652  1.00 47.55  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.170 25.460 21.843  1.00 49.89  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 17.494 26.939 21.623  1.00 52.24  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.152 24.865 22.837  1.00 49.53  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.487 27.753 22.897  0.92 55.01  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.679 22.343 20.932  1.00 51.44  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.340 20.951 21.144  1.00 51.92  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 17.866 20.379 22.445  1.00 54.44  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.044 20.546 22.778  1.00 56.60  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 16.996 19.706 23.192  1.00 52.76  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.361 19.029 24.432  1.00 53.40  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.055 17.551 24.254  1.00 53.18  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 15.911 17.181 23.959  1.00 53.49  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.611 19.603 25.644  1.00 53.08  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 16.988 21.069 25.858  1.00 53.26  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 16.904 18.781 26.891  1.00 54.36  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.242 21.729 26.991  1.00 54.65  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.068 16.710 24.428  1.00 53.30  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 17.921 15.273 24.251  1.00 54.32  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.735 14.615 25.614  1.00 58.96  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.623 14.678 26.471  1.00 61.51  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.124 14.685 23.507  1.00 54.80  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.407 14.730 24.279  1.00 57.50  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 20.745 13.775 25.214  1.00 61.20  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.435 15.611 24.254  1.00 58.40  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 21.924 14.066 25.732  1.00 63.12  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.365 15.175 25.166  1.00 61.73  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.567 14.006 25.820  1.00 61.01  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.349 13.223 27.029  1.00 65.93  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.978 11.841 26.922  1.00 68.81  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 17.370 11.261 27.941  1.00 71.10  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.853 13.098 27.321  1.00 64.81  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.164 12.677 26.137  1.00 62.26  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.288 14.433 27.788  1.00 63.13  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 17.081 11.302 25.711  0.86 67.85  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.742 10.030 25.509  0.86 70.24  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 19.232 10.203 25.306  0.86 69.63  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.938 10.674 26.202  0.86 71.23  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.721 9.829  24.132  1.00 68.08  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 21.129 9.957  23.793  0.54 67.96  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.378 11.257 23.033  0.76 66.40  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.452 11.957 22.618  1.00 64.66  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.591 8.749  22.971  1.00 68.22  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 21.517 7.451  23.714  0.78 73.06  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 22.406 7.112  24.711  0.49 76.94  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 20.656 6.411  23.609  0.79 74.76  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 22.097 5.919  25.188  0.89 80.66  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 21.039 5.472  24.536  0.28 79.31  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.659 11.574 22.861  0.93 69.40  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 23.056 12.798 22.176  0.93 67.19  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.589 12.790 20.727  0.93 64.04  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.964 11.907 19.949  0.93 65.57  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.574 12.962 22.232  0.93 69.32  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 25.139 14.046 21.307  0.93 66.09  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 24.889 15.433 21.876  0.93 65.37  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.617 13.833 21.018  0.93 67.25  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 21.770 13.777 20.366  1.00 59.10  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.400 13.998 18.988  1.00 54.72  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.237 15.093 18.349  1.00 52.54  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 22.876 15.892 19.028  1.00 55.22  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.230 15.125 17.016  1.00 48.94  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.985 16.159 16.318  1.00 46.76  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.280 17.507 16.358  1.00 46.57  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 22.940 18.550 16.286  1.00 48.29  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.251 15.735 14.876  1.00 43.65  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.432 14.825 14.730  1.00 43.71  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.361 13.507 15.143  1.00 43.44  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.617 15.291 14.193  1.00 45.79  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.448 12.666 15.012  1.00 45.82  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.708 14.457 14.061  1.00 48.02  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 26.624 13.142 14.472  1.00 48.22  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 20.955 17.511 16.482  1.00 45.30  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.194 18.739 16.665  1.00 45.31  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 19.830 18.984 18.121  1.00 46.69  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 19.793 20.135 18.564  1.00 47.08  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 18.920 18.706 15.816  1.00 43.84  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.169 18.427 14.351  1.00 43.27  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 19.933 19.293 13.579  1.00 42.91  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.633 17.302 13.737  1.00 43.32  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.163 19.043 12.240  1.00 42.34  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 18.857 17.044 12.397  1.00 43.12  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.622 17.918 11.654  1.00 42.48  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 19.848 17.668 10.320  1.00 42.27  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.565 17.921 18.878  1.00 48.51  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.304 18.010 20.313  1.00 50.24  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 20.613 17.696 21.030  1.00 52.95  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 20.892 16.550 21.383  1.00 54.70  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.187 17.059 20.725  1.00 49.71  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.423 18.730 21.242  1.00 54.19  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.758 18.590 21.809  1.00 57.95  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 22.877 19.322 23.141  1.00 60.53  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 23.900 19.940 23.445  1.00 63.39  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.812 19.084 20.821  1.00 59.09  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.474 20.442 20.236  1.00 59.61  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.491 21.064 20.691  1.00 59.38  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.190 20.886 19.314  0.81 60.76  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 21.826 19.259 23.956  1.00 59.75  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.828 19.844 25.292  1.00 61.38  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.308 18.810 26.277  1.00 60.44  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.184 18.317 26.129  1.00 59.02  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 20.980 21.118 25.348  1.00 61.73  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.732 22.358 24.972  0.60 63.52  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.903 22.864 23.716  0.60 62.13  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.414 23.252 25.861  0.60 67.03  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.650 24.017 23.768  0.60 64.44  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.976 24.276 25.074  0.60 67.26  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.604 23.284 27.246  0.60 70.29  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.715 25.321 25.625  0.60 70.50  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.339 24.323 27.791  0.60 73.41  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.884 25.327 26.982  0.60 73.43  ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 22.124 18.482 27.275  1.00 61.43  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.727 17.512 28.280  1.00 62.56  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.618 18.083 29.164  1.00 62.62  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.559 19.294 29.395  1.00 63.47  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.928 17.111 29.132  1.00 67.01  ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 23.889 16.164 28.427  0.99 68.37  ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 25.266 16.142 29.080  1.00 72.96  ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 25.202 15.986 30.530  0.87 76.85  ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 25.496 16.951 31.397  0.59 78.51  ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 25.880 18.142 30.959  1.00 78.81  ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 25.411 16.724 32.701  1.00 80.10  ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.718 17.230 29.661  1.00 62.54  ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.614 17.735 30.495  1.00 62.81  ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 19.078 18.418 31.770  1.00 66.89  ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.389 19.320 32.262  1.00 66.76  ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.798 16.470 30.797  1.00 63.08  ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 18.150 15.517 29.699  1.00 61.91  ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.590 15.789 29.385  1.00 62.67  ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.225 18.016 32.324  1.00 71.03  ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.741 18.665 33.523  1.00 75.59  ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 21.148 20.110 33.268  1.00 76.25  ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.195 20.904 34.214  1.00 78.87  ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.929 17.881 34.079  1.00 79.56  ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.441 20.467 32.020  1.00 74.37  ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.821 21.824 31.656  1.00 74.55  ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.624 22.688 31.279  1.00 71.71  ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.812 23.785 30.741  1.00 71.23  ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.823 21.795 30.499  1.00 73.89  ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 24.118 21.059 30.803  0.39 78.25  ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.956 20.830 29.559  0.87 79.45  ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 24.371 20.724 28.460  1.00 76.72  ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 26.198 20.761 29.677  0.83 83.81  ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.401 22.222 31.549  1.00 70.44  ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 18.207 22.966 31.165  1.00 67.34  ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 17.983 24.196 32.037  1.00 69.22  ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.502 25.219 31.537  1.00 68.49  ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.978 22.057 31.221  1.00 65.46  ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.305 24.117 33.332  1.00 71.47  ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.131 25.276 34.202  1.00 72.65  ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.052 26.417 33.790  1.00 73.71  ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.634 27.580 33.752  1.00 74.45  ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.374 24.885 35.660  0.70 75.81  ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.121 24.375 36.344  0.60 76.35  ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 16.011 24.713 35.882  0.60 74.38  ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.245 23.643 37.348  0.60 79.52  ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.312 26.104 33.477  1.00 74.52  ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.222 27.120 32.964  1.00 75.55  ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.828 27.587 31.571  1.00 72.42  ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.228 28.681 31.159  1.00 74.27  ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.655 26.586 32.949  1.00 77.05  ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.052 26.783 30.840  1.00 68.33  ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.606 27.192 29.513  1.00 65.47  ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.515 28.251 29.602  1.00 66.27  ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.449 29.154 28.761  1.00 65.35  ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.113 25.976 28.730  1.00 61.33  ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.939 26.153 27.222  1.00 58.99  ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.294 26.306 26.547  1.00 59.90  ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.166 24.985 26.629  1.00 56.67  ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.653 28.159 30.618  1.00 68.40  ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.571 29.127 30.776  1.00 69.36  ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.130 30.512 31.079  1.00 73.89  ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.623 31.526 30.582  1.00 73.92  ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.593 28.658 31.871  1.00 69.07  ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.557 29.731 32.168  1.00 69.74  ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.914 27.360 31.458  1.00 66.14  ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.191 30.579 31.885  1.00 78.24  ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.731 31.872 32.293  1.00 83.61  ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.362 32.607 31.116  1.00 85.22  ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 19.031 33.768 30.847  1.00 87.33  ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.750 31.685 33.418  0.71 87.72  ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 19.243 30.864 34.594  0.96 88.64  ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 19.843 31.359 35.902  1.00 94.31  ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 20.457 30.224 36.708  0.96 95.60  ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 19.464 29.165 37.033  1.00 92.89  ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.279 31.946 30.404  1.00 85.57  ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 20.968 32.597 29.294  1.00 86.53  ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 19.999 32.952 28.173  1.00 83.66  ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.146 33.993 27.521  1.00 85.64  ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.087 31.697 28.771  1.00 85.83  ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.191 31.302 29.755  1.00 88.02  ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 24.153 30.322 29.104  1.00 86.77  ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 23.932 32.531 30.254  1.00 91.60  ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 18.999 32.099 27.938  1.00 79.69  ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.010 32.354 26.898  1.00 78.26  ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.130 33.551 27.225  1.00 82.66  ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 16.512 34.117 26.317  1.00 83.45  ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.152 31.103 26.690  1.00 74.60  ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 16.239 31.028 25.465  0.54 73.61  ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 17.036 31.224 24.187  1.00 74.01  ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 15.491 29.702 25.429  1.00 71.35  ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 17.066 33.954 28.495  0.84 87.03  ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 16.233 35.078 28.901  1.00 90.58  ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 16.990 36.402 28.909  1.00 96.66  ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.416 37.436 28.545  1.00 98.06  ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 15.641 34.817 30.290  1.00 90.94  ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 18.265 36.395 29.309  1.00 102.50 ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 19.083 37.597 29.366  1.00 111.63 ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 19.566 38.048 27.997  1.00 117.66 ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 20.543 38.810 27.920  1.00 124.34 ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.292 37.366 30.272  1.00 112.80 ? 92  LYS A CB  1 
ATOM   728  N N   . GLY A 1 93  ? 18.917 37.608 26.919  1.00 115.94 ? 93  GLY A N   1 
ATOM   729  C CA  . GLY A 1 93  ? 19.443 37.883 25.593  1.00 119.91 ? 93  GLY A CA  1 
ATOM   730  C C   . GLY A 1 93  ? 20.833 37.306 25.428  1.00 122.84 ? 93  GLY A C   1 
ATOM   731  O O   . GLY A 1 93  ? 21.163 36.247 25.975  1.00 125.03 ? 93  GLY A O   1 
ATOM   732  N N   . GLU A 1 94  ? 21.659 38.009 24.657  1.00 125.13 ? 94  GLU A N   1 
ATOM   733  C CA  . GLU A 1 94  ? 23.097 37.751 24.561  1.00 126.78 ? 94  GLU A CA  1 
ATOM   734  C C   . GLU A 1 94  ? 23.397 36.286 24.232  1.00 122.16 ? 94  GLU A C   1 
ATOM   735  O O   . GLU A 1 94  ? 23.862 35.506 25.064  1.00 121.95 ? 94  GLU A O   1 
ATOM   736  C CB  . GLU A 1 94  ? 23.802 38.157 25.858  1.00 130.85 ? 94  GLU A CB  1 
ATOM   737  N N   . TYR A 1 95  ? 23.128 35.940 22.978  1.00 113.02 ? 95  TYR A N   1 
ATOM   738  C CA  . TYR A 1 95  ? 23.493 34.637 22.445  1.00 103.06 ? 95  TYR A CA  1 
ATOM   739  C C   . TYR A 1 95  ? 23.673 34.780 20.943  1.00 97.20  ? 95  TYR A C   1 
ATOM   740  O O   . TYR A 1 95  ? 23.065 35.645 20.307  1.00 97.97  ? 95  TYR A O   1 
ATOM   741  C CB  . TYR A 1 95  ? 22.452 33.554 22.781  1.00 97.13  ? 95  TYR A CB  1 
ATOM   742  C CG  . TYR A 1 95  ? 21.038 33.822 22.292  1.00 93.93  ? 95  TYR A CG  1 
ATOM   743  C CD1 . TYR A 1 95  ? 20.654 33.506 20.992  1.00 91.02  ? 95  TYR A CD1 1 
ATOM   744  C CD2 . TYR A 1 95  ? 20.079 34.353 23.144  1.00 94.67  ? 95  TYR A CD2 1 
ATOM   745  C CE1 . TYR A 1 95  ? 19.366 33.740 20.552  1.00 89.72  ? 95  TYR A CE1 1 
ATOM   746  C CE2 . TYR A 1 95  ? 18.789 34.587 22.712  1.00 93.33  ? 95  TYR A CE2 1 
ATOM   747  C CZ  . TYR A 1 95  ? 18.440 34.278 21.414  1.00 90.82  ? 95  TYR A CZ  1 
ATOM   748  O OH  . TYR A 1 95  ? 17.161 34.505 20.964  1.00 89.66  ? 95  TYR A OH  1 
ATOM   749  N N   . GLN A 1 96  ? 24.520 33.923 20.383  1.00 90.97  ? 96  GLN A N   1 
ATOM   750  C CA  . GLN A 1 96  ? 24.801 33.947 18.957  1.00 86.11  ? 96  GLN A CA  1 
ATOM   751  C C   . GLN A 1 96  ? 23.816 33.066 18.196  1.00 78.56  ? 96  GLN A C   1 
ATOM   752  O O   . GLN A 1 96  ? 23.033 32.310 18.774  1.00 75.22  ? 96  GLN A O   1 
ATOM   753  C CB  . GLN A 1 96  ? 26.233 33.491 18.680  1.00 86.18  ? 96  GLN A CB  1 
ATOM   754  C CG  . GLN A 1 96  ? 27.302 34.470 19.115  1.00 90.10  ? 96  GLN A CG  1 
ATOM   755  C CD  . GLN A 1 96  ? 28.687 33.865 19.062  0.59 89.99  ? 96  GLN A CD  1 
ATOM   756  O OE1 . GLN A 1 96  ? 29.050 33.048 19.908  0.59 88.73  ? 96  GLN A OE1 1 
ATOM   757  N NE2 . GLN A 1 96  ? 29.467 34.256 18.061  0.59 91.67  ? 96  GLN A NE2 1 
ATOM   758  N N   . LYS A 1 97  ? 23.871 33.173 16.871  1.00 76.05  ? 97  LYS A N   1 
ATOM   759  C CA  . LYS A 1 97  ? 23.025 32.395 15.977  1.00 69.57  ? 97  LYS A CA  1 
ATOM   760  C C   . LYS A 1 97  ? 23.893 31.726 14.927  1.00 66.61  ? 97  LYS A C   1 
ATOM   761  O O   . LYS A 1 97  ? 24.779 32.365 14.352  1.00 69.25  ? 97  LYS A O   1 
ATOM   762  C CB  . LYS A 1 97  ? 21.967 33.272 15.298  1.00 69.55  ? 97  LYS A CB  1 
ATOM   763  C CG  . LYS A 1 97  ? 20.890 33.785 16.229  1.00 68.96  ? 97  LYS A CG  1 
ATOM   764  C CD  . LYS A 1 97  ? 19.734 34.370 15.440  1.00 69.06  ? 97  LYS A CD  1 
ATOM   765  C CE  . LYS A 1 97  ? 18.603 34.809 16.351  1.00 69.58  ? 97  LYS A CE  1 
ATOM   766  N NZ  . LYS A 1 97  ? 17.401 35.214 15.571  1.00 70.28  ? 97  LYS A NZ  1 
ATOM   767  N N   . VAL A 1 98  ? 23.646 30.442 14.688  1.00 61.52  ? 98  VAL A N   1 
ATOM   768  C CA  . VAL A 1 98  ? 24.316 29.684 13.641  1.00 59.21  ? 98  VAL A CA  1 
ATOM   769  C C   . VAL A 1 98  ? 23.248 29.137 12.706  1.00 55.52  ? 98  VAL A C   1 
ATOM   770  O O   . VAL A 1 98  ? 22.146 28.791 13.145  1.00 53.81  ? 98  VAL A O   1 
ATOM   771  C CB  . VAL A 1 98  ? 25.195 28.553 14.222  1.00 57.75  ? 98  VAL A CB  1 
ATOM   772  C CG1 . VAL A 1 98  ? 25.196 28.605 15.744  1.00 57.30  ? 98  VAL A CG1 1 
ATOM   773  C CG2 . VAL A 1 98  ? 24.741 27.182 13.733  1.00 55.51  ? 98  VAL A CG2 1 
ATOM   774  N N   . SER A 1 99  ? 23.561 29.090 11.414  1.00 54.91  ? 99  SER A N   1 
ATOM   775  C CA  . SER A 1 99  ? 22.598 28.705 10.394  1.00 53.34  ? 99  SER A CA  1 
ATOM   776  C C   . SER A 1 99  ? 23.116 27.518 9.595   1.00 52.11  ? 99  SER A C   1 
ATOM   777  O O   . SER A 1 99  ? 24.300 27.458 9.248   1.00 53.61  ? 99  SER A O   1 
ATOM   778  C CB  . SER A 1 99  ? 22.296 29.876 9.456   1.00 56.66  ? 99  SER A CB  1 
ATOM   779  O OG  . SER A 1 99  ? 21.799 30.992 10.175  1.00 59.09  ? 99  SER A OG  1 
ATOM   780  N N   . TYR A 1 100 ? 22.215 26.575 9.299   1.00 49.91  ? 100 TYR A N   1 
ATOM   781  C CA  . TYR A 1 100 ? 22.517 25.400 8.497   1.00 48.91  ? 100 TYR A CA  1 
ATOM   782  C C   . TYR A 1 100 ? 21.766 25.445 7.169   1.00 49.59  ? 100 TYR A C   1 
ATOM   783  O O   . TYR A 1 100 ? 20.650 25.971 7.096   1.00 49.81  ? 100 TYR A O   1 
ATOM   784  C CB  . TYR A 1 100 ? 22.149 24.104 9.230   1.00 46.46  ? 100 TYR A CB  1 
ATOM   785  C CG  . TYR A 1 100 ? 23.118 23.695 10.319  1.00 46.76  ? 100 TYR A CG  1 
ATOM   786  C CD1 . TYR A 1 100 ? 24.184 24.511 10.675  1.00 48.76  ? 100 TYR A CD1 1 
ATOM   787  C CD2 . TYR A 1 100 ? 22.973 22.481 10.979  1.00 45.36  ? 100 TYR A CD2 1 
ATOM   788  C CE1 . TYR A 1 100 ? 25.070 24.136 11.669  1.00 49.64  ? 100 TYR A CE1 1 
ATOM   789  C CE2 . TYR A 1 100 ? 23.855 22.097 11.971  1.00 45.87  ? 100 TYR A CE2 1 
ATOM   790  C CZ  . TYR A 1 100 ? 24.902 22.926 12.310  1.00 48.83  ? 100 TYR A CZ  1 
ATOM   791  O OH  . TYR A 1 100 ? 25.781 22.544 13.297  1.00 51.62  ? 100 TYR A OH  1 
ATOM   792  N N   . PRO A 1 101 ? 22.347 24.903 6.102   1.00 49.96  ? 101 PRO A N   1 
ATOM   793  C CA  . PRO A 1 101 ? 21.657 24.895 4.809   1.00 50.59  ? 101 PRO A CA  1 
ATOM   794  C C   . PRO A 1 101 ? 20.487 23.924 4.808   1.00 48.85  ? 101 PRO A C   1 
ATOM   795  O O   . PRO A 1 101 ? 20.374 23.033 5.653   1.00 46.35  ? 101 PRO A O   1 
ATOM   796  C CB  . PRO A 1 101 ? 22.744 24.451 3.821   1.00 51.33  ? 101 PRO A CB  1 
ATOM   797  C CG  . PRO A 1 101 ? 24.043 24.605 4.559   1.00 51.65  ? 101 PRO A CG  1 
ATOM   798  C CD  . PRO A 1 101 ? 23.710 24.363 5.995   1.00 49.99  ? 101 PRO A CD  1 
ATOM   799  N N   . LEU A 1 102 ? 19.605 24.111 3.829   1.00 40.88  ? 102 LEU A N   1 
ATOM   800  C CA  . LEU A 1 102 ? 18.420 23.284 3.673   1.00 41.34  ? 102 LEU A CA  1 
ATOM   801  C C   . LEU A 1 102 ? 18.293 22.843 2.222   1.00 41.71  ? 102 LEU A C   1 
ATOM   802  O O   . LEU A 1 102 ? 18.893 23.428 1.317   1.00 42.20  ? 102 LEU A O   1 
ATOM   803  C CB  . LEU A 1 102 ? 17.152 24.031 4.108   1.00 43.45  ? 102 LEU A CB  1 
ATOM   804  C CG  . LEU A 1 102 ? 17.109 24.485 5.568   1.00 44.14  ? 102 LEU A CG  1 
ATOM   805  C CD1 . LEU A 1 102 ? 15.887 25.346 5.822   1.00 46.03  ? 102 LEU A CD1 1 
ATOM   806  C CD2 . LEU A 1 102 ? 17.122 23.285 6.499   1.00 42.37  ? 102 LEU A CD2 1 
ATOM   807  N N   . LEU A 1 103 ? 17.498 21.798 2.010   1.00 41.55  ? 103 LEU A N   1 
ATOM   808  C CA  . LEU A 1 103 ? 17.265 21.235 0.687   1.00 40.53  ? 103 LEU A CA  1 
ATOM   809  C C   . LEU A 1 103 ? 15.858 21.581 0.222   1.00 42.41  ? 103 LEU A C   1 
ATOM   810  O O   . LEU A 1 103 ? 14.891 21.406 0.971   1.00 43.25  ? 103 LEU A O   1 
ATOM   811  C CB  . LEU A 1 103 ? 17.456 19.717 0.693   1.00 39.11  ? 103 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 103 ? 17.163 19.006 -0.630  1.00 39.27  ? 103 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 103 ? 18.157 19.428 -1.703  1.00 38.80  ? 103 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 103 ? 17.169 17.497 -0.448  1.00 38.70  ? 103 LEU A CD2 1 
ATOM   815  N N   . LYS A 1 104 ? 15.750 22.063 -1.012  1.00 43.79  ? 104 LYS A N   1 
ATOM   816  C CA  . LYS A 1 104 ? 14.473 22.388 -1.630  1.00 44.89  ? 104 LYS A CA  1 
ATOM   817  C C   . LYS A 1 104 ? 14.124 21.314 -2.650  1.00 43.96  ? 104 LYS A C   1 
ATOM   818  O O   . LYS A 1 104 ? 14.923 21.018 -3.545  1.00 42.62  ? 104 LYS A O   1 
ATOM   819  C CB  . LYS A 1 104 ? 14.521 23.762 -2.300  1.00 46.19  ? 104 LYS A CB  1 
ATOM   820  C CG  . LYS A 1 104 ? 13.290 24.094 -3.127  1.00 48.77  ? 104 LYS A CG  1 
ATOM   821  C CD  . LYS A 1 104 ? 13.503 25.358 -3.944  1.00 51.25  ? 104 LYS A CD  1 
ATOM   822  C CE  . LYS A 1 104 ? 12.353 25.596 -4.909  1.00 54.61  ? 104 LYS A CE  1 
ATOM   823  N NZ  . LYS A 1 104 ? 12.608 26.764 -5.798  1.00 57.34  ? 104 LYS A NZ  1 
ATOM   824  N N   . THR A 1 105 ? 12.936 20.731 -2.509  1.00 44.69  ? 105 THR A N   1 
ATOM   825  C CA  . THR A 1 105 ? 12.446 19.696 -3.409  1.00 43.51  ? 105 THR A CA  1 
ATOM   826  C C   . THR A 1 105 ? 11.202 20.202 -4.122  1.00 45.23  ? 105 THR A C   1 
ATOM   827  O O   . THR A 1 105 ? 10.278 20.706 -3.477  1.00 46.25  ? 105 THR A O   1 
ATOM   828  C CB  . THR A 1 105 ? 12.129 18.405 -2.649  1.00 41.70  ? 105 THR A CB  1 
ATOM   829  O OG1 . THR A 1 105 ? 13.323 17.906 -2.033  1.00 40.50  ? 105 THR A OG1 1 
ATOM   830  C CG2 . THR A 1 105 ? 11.568 17.351 -3.592  1.00 40.89  ? 105 THR A CG2 1 
ATOM   831  N N   . THR A 1 106 ? 11.181 20.068 -5.445  1.00 45.63  ? 106 THR A N   1 
ATOM   832  C CA  . THR A 1 106 ? 10.048 20.476 -6.266  1.00 48.43  ? 106 THR A CA  1 
ATOM   833  C C   . THR A 1 106 ? 9.547  19.274 -7.052  1.00 49.21  ? 106 THR A C   1 
ATOM   834  O O   . THR A 1 106 ? 10.344 18.540 -7.645  1.00 47.22  ? 106 THR A O   1 
ATOM   835  C CB  . THR A 1 106 ? 10.435 21.612 -7.218  1.00 48.76  ? 106 THR A CB  1 
ATOM   836  O OG1 . THR A 1 106 ? 10.971 22.706 -6.464  1.00 49.47  ? 106 THR A OG1 1 
ATOM   837  C CG2 . THR A 1 106 ? 9.223  22.093 -7.996  1.00 50.54  ? 106 THR A CG2 1 
ATOM   838  N N   . VAL A 1 107 ? 8.232  19.069 -7.047  1.00 52.73  ? 107 VAL A N   1 
ATOM   839  C CA  . VAL A 1 107 ? 7.595  17.963 -7.753  1.00 55.95  ? 107 VAL A CA  1 
ATOM   840  C C   . VAL A 1 107 ? 6.581  18.542 -8.730  1.00 60.49  ? 107 VAL A C   1 
ATOM   841  O O   . VAL A 1 107 ? 5.706  19.321 -8.336  1.00 62.15  ? 107 VAL A O   1 
ATOM   842  C CB  . VAL A 1 107 ? 6.917  16.979 -6.781  1.00 57.22  ? 107 VAL A CB  1 
ATOM   843  C CG1 . VAL A 1 107 ? 6.368  15.780 -7.539  1.00 42.70  ? 107 VAL A CG1 1 
ATOM   844  C CG2 . VAL A 1 107 ? 7.893  16.537 -5.701  1.00 55.12  ? 107 VAL A CG2 1 
ATOM   845  N N   . LYS A 1 108 ? 6.702  18.162 -9.999  1.00 62.49  ? 108 LYS A N   1 
ATOM   846  C CA  . LYS A 1 108 ? 5.805  18.622 -11.050 1.00 66.91  ? 108 LYS A CA  1 
ATOM   847  C C   . LYS A 1 108 ? 4.912  17.479 -11.512 1.00 68.86  ? 108 LYS A C   1 
ATOM   848  O O   . LYS A 1 108 ? 5.353  16.329 -11.599 1.00 66.73  ? 108 LYS A O   1 
ATOM   849  C CB  . LYS A 1 108 ? 6.590  19.184 -12.239 1.00 68.03  ? 108 LYS A CB  1 
ATOM   850  C CG  . LYS A 1 108 ? 7.218  20.544 -11.984 1.00 69.96  ? 108 LYS A CG  1 
ATOM   851  C CD  . LYS A 1 108 ? 7.987  21.031 -13.203 1.00 72.86  ? 108 LYS A CD  1 
ATOM   852  C CE  . LYS A 1 108 ? 8.433  22.474 -13.038 1.00 75.80  ? 108 LYS A CE  1 
ATOM   853  N NZ  . LYS A 1 108 ? 9.234  22.672 -11.799 1.00 74.37  ? 108 LYS A NZ  1 
ATOM   854  N N   . TYR A 1 109 ? 3.654  17.804 -11.809 1.00 73.26  ? 109 TYR A N   1 
ATOM   855  C CA  . TYR A 1 109 ? 2.691  16.806 -12.260 1.00 76.04  ? 109 TYR A CA  1 
ATOM   856  C C   . TYR A 1 109 ? 2.145  17.171 -13.635 1.00 79.70  ? 109 TYR A C   1 
ATOM   857  O O   . TYR A 1 109 ? 2.898  17.601 -14.515 1.00 79.67  ? 109 TYR A O   1 
ATOM   858  C CB  . TYR A 1 109 ? 1.545  16.670 -11.255 1.00 78.04  ? 109 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 109 ? 1.992  16.573 -9.813  1.00 76.74  ? 109 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 109 ? 2.103  17.709 -9.024  1.00 77.13  ? 109 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 109 ? 2.298  15.345 -9.240  1.00 75.56  ? 109 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 109 ? 2.508  17.629 -7.707  1.00 75.80  ? 109 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 109 ? 2.704  15.255 -7.921  1.00 74.66  ? 109 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 109 ? 2.808  16.401 -7.159  1.00 74.86  ? 109 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 109 ? 3.212  16.321 -5.846  1.00 73.71  ? 109 TYR A OH  1 
ATOM   866  N N   . GLY A 1 110 ? 0.840  17.005 -13.825 1.00 83.38  ? 110 GLY A N   1 
ATOM   867  C CA  . GLY A 1 110 ? 0.203  17.328 -15.088 1.00 86.72  ? 110 GLY A CA  1 
ATOM   868  C C   . GLY A 1 110 ? -1.311 17.314 -15.014 1.00 91.61  ? 110 GLY A C   1 
ATOM   869  O O   . GLY A 1 110 ? -1.954 18.365 -15.018 1.00 94.74  ? 110 GLY A O   1 
ATOM   870  N N   . LYS A 1 114 ? -0.732 20.484 -9.941  0.70 64.55  ? 114 LYS A N   1 
ATOM   871  C CA  . LYS A 1 114 ? -0.066 21.708 -9.511  0.70 79.24  ? 114 LYS A CA  1 
ATOM   872  C C   . LYS A 1 114 ? 1.273  21.402 -8.851  0.70 79.37  ? 114 LYS A C   1 
ATOM   873  O O   . LYS A 1 114 ? 1.366  20.535 -7.983  0.70 81.38  ? 114 LYS A O   1 
ATOM   874  C CB  . LYS A 1 114 ? -0.959 22.495 -8.549  0.50 66.51  ? 114 LYS A CB  1 
ATOM   875  N N   . GLU A 1 115 ? 2.305  22.128 -9.276  1.00 77.41  ? 115 GLU A N   1 
ATOM   876  C CA  . GLU A 1 115 ? 3.652  21.930 -8.755  1.00 70.93  ? 115 GLU A CA  1 
ATOM   877  C C   . GLU A 1 115 ? 3.694  22.155 -7.248  1.00 68.45  ? 115 GLU A C   1 
ATOM   878  O O   . GLU A 1 115 ? 3.146  23.136 -6.738  1.00 69.63  ? 115 GLU A O   1 
ATOM   879  C CB  . GLU A 1 115 ? 4.615  22.880 -9.464  1.00 70.17  ? 115 GLU A CB  1 
ATOM   880  C CG  . GLU A 1 115 ? 5.881  23.199 -8.696  1.00 68.94  ? 115 GLU A CG  1 
ATOM   881  C CD  . GLU A 1 115 ? 6.730  24.238 -9.401  1.00 72.03  ? 115 GLU A CD  1 
ATOM   882  O OE1 . GLU A 1 115 ? 7.059  25.269 -8.777  0.86 73.20  ? 115 GLU A OE1 1 
ATOM   883  O OE2 . GLU A 1 115 ? 7.057  24.027 -10.588 1.00 72.88  ? 115 GLU A OE2 1 
ATOM   884  N N   . ALA A 1 116 ? 4.351  21.241 -6.536  1.00 65.57  ? 116 ALA A N   1 
ATOM   885  C CA  . ALA A 1 116 ? 4.460  21.295 -5.086  1.00 64.26  ? 116 ALA A CA  1 
ATOM   886  C C   . ALA A 1 116 ? 5.925  21.320 -4.672  1.00 59.58  ? 116 ALA A C   1 
ATOM   887  O O   . ALA A 1 116 ? 6.761  20.631 -5.265  1.00 57.56  ? 116 ALA A O   1 
ATOM   888  C CB  . ALA A 1 116 ? 3.755  20.102 -4.433  1.00 64.49  ? 116 ALA A CB  1 
ATOM   889  N N   . THR A 1 117 ? 6.228  22.112 -3.646  1.00 58.29  ? 117 THR A N   1 
ATOM   890  C CA  . THR A 1 117 ? 7.581  22.253 -3.131  1.00 54.49  ? 117 THR A CA  1 
ATOM   891  C C   . THR A 1 117 ? 7.633  21.848 -1.663  1.00 53.36  ? 117 THR A C   1 
ATOM   892  O O   . THR A 1 117 ? 6.652  21.991 -0.927  1.00 55.29  ? 117 THR A O   1 
ATOM   893  C CB  . THR A 1 117 ? 8.096  23.691 -3.288  1.00 54.27  ? 117 THR A CB  1 
ATOM   894  O OG1 . THR A 1 117 ? 7.134  24.607 -2.750  1.00 56.81  ? 117 THR A OG1 1 
ATOM   895  C CG2 . THR A 1 117 ? 8.338  24.014 -4.754  1.00 54.47  ? 117 THR A CG2 1 
ATOM   896  N N   . TYR A 1 118 ? 8.792  21.344 -1.245  1.00 50.48  ? 118 TYR A N   1 
ATOM   897  C CA  . TYR A 1 118 ? 8.999  20.895 0.124   1.00 49.64  ? 118 TYR A CA  1 
ATOM   898  C C   . TYR A 1 118 ? 10.346 21.399 0.621   1.00 48.16  ? 118 TYR A C   1 
ATOM   899  O O   . TYR A 1 118 ? 11.186 21.868 -0.152  1.00 48.35  ? 118 TYR A O   1 
ATOM   900  C CB  . TYR A 1 118 ? 8.925  19.366 0.232   1.00 48.18  ? 118 TYR A CB  1 
ATOM   901  C CG  . TYR A 1 118 ? 7.627  18.781 -0.275  1.00 50.18  ? 118 TYR A CG  1 
ATOM   902  C CD1 . TYR A 1 118 ? 6.510  18.706 0.546   1.00 52.43  ? 118 TYR A CD1 1 
ATOM   903  C CD2 . TYR A 1 118 ? 7.519  18.303 -1.574  1.00 49.59  ? 118 TYR A CD2 1 
ATOM   904  C CE1 . TYR A 1 118 ? 5.321  18.173 0.087   1.00 54.90  ? 118 TYR A CE1 1 
ATOM   905  C CE2 . TYR A 1 118 ? 6.334  17.767 -2.042  1.00 51.92  ? 118 TYR A CE2 1 
ATOM   906  C CZ  . TYR A 1 118 ? 5.238  17.705 -1.207  1.00 54.80  ? 118 TYR A CZ  1 
ATOM   907  O OH  . TYR A 1 118 ? 4.055  17.174 -1.666  1.00 57.40  ? 118 TYR A OH  1 
ATOM   908  N N   . LEU A 1 119 ? 10.547 21.294 1.933   1.00 47.61  ? 119 LEU A N   1 
ATOM   909  C CA  . LEU A 1 119 ? 11.777 21.728 2.581   1.00 45.85  ? 119 LEU A CA  1 
ATOM   910  C C   . LEU A 1 119 ? 12.260 20.617 3.500   1.00 44.55  ? 119 LEU A C   1 
ATOM   911  O O   . LEU A 1 119 ? 11.496 20.124 4.335   1.00 45.94  ? 119 LEU A O   1 
ATOM   912  C CB  . LEU A 1 119 ? 11.557 23.023 3.369   1.00 47.03  ? 119 LEU A CB  1 
ATOM   913  C CG  . LEU A 1 119 ? 12.712 24.023 3.377   1.00 46.41  ? 119 LEU A CG  1 
ATOM   914  C CD1 . LEU A 1 119 ? 13.072 24.426 1.957   1.00 46.68  ? 119 LEU A CD1 1 
ATOM   915  C CD2 . LEU A 1 119 ? 12.347 25.244 4.200   1.00 48.51  ? 119 LEU A CD2 1 
ATOM   916  N N   . ALA A 1 120 ? 13.523 20.225 3.348   1.00 42.23  ? 120 ALA A N   1 
ATOM   917  C CA  . ALA A 1 120 ? 14.089 19.100 4.078   1.00 41.11  ? 120 ALA A CA  1 
ATOM   918  C C   . ALA A 1 120 ? 15.277 19.563 4.908   1.00 41.33  ? 120 ALA A C   1 
ATOM   919  O O   . ALA A 1 120 ? 16.161 20.261 4.400   1.00 41.86  ? 120 ALA A O   1 
ATOM   920  C CB  . ALA A 1 120 ? 14.519 17.985 3.121   1.00 39.56  ? 120 ALA A CB  1 
ATOM   921  N N   . LEU A 1 121 ? 15.293 19.170 6.182   1.00 41.45  ? 121 LEU A N   1 
ATOM   922  C CA  . LEU A 1 121 ? 16.439 19.420 7.046   1.00 40.82  ? 121 LEU A CA  1 
ATOM   923  C C   . LEU A 1 121 ? 17.450 18.283 7.007   1.00 39.23  ? 121 LEU A C   1 
ATOM   924  O O   . LEU A 1 121 ? 18.658 18.533 7.100   1.00 38.54  ? 121 LEU A O   1 
ATOM   925  C CB  . LEU A 1 121 ? 15.976 19.651 8.488   1.00 42.49  ? 121 LEU A CB  1 
ATOM   926  C CG  . LEU A 1 121 ? 17.059 19.827 9.556   1.00 42.63  ? 121 LEU A CG  1 
ATOM   927  C CD1 . LEU A 1 121 ? 17.959 21.011 9.233   1.00 42.33  ? 121 LEU A CD1 1 
ATOM   928  C CD2 . LEU A 1 121 ? 16.436 19.985 10.935  1.00 44.61  ? 121 LEU A CD2 1 
ATOM   929  N N   . ASN A 1 122 ? 16.985 17.042 6.868   1.00 39.36  ? 122 ASN A N   1 
ATOM   930  C CA  . ASN A 1 122 ? 17.886 15.904 6.740   1.00 39.12  ? 122 ASN A CA  1 
ATOM   931  C C   . ASN A 1 122 ? 18.121 15.562 5.275   1.00 39.68  ? 122 ASN A C   1 
ATOM   932  O O   . ASN A 1 122 ? 19.175 15.888 4.719   1.00 40.13  ? 122 ASN A O   1 
ATOM   933  C CB  . ASN A 1 122 ? 17.334 14.687 7.485   1.00 39.44  ? 122 ASN A CB  1 
ATOM   934  C CG  . ASN A 1 122 ? 17.636 14.726 8.969   1.00 40.08  ? 122 ASN A CG  1 
ATOM   935  O OD1 . ASN A 1 122 ? 18.465 15.513 9.425   1.00 40.23  ? 122 ASN A OD1 1 
ATOM   936  N ND2 . ASN A 1 122 ? 16.974 13.862 9.729   1.00 41.15  ? 122 ASN A ND2 1 
ATOM   937  N N   . GLU A 1 123 ? 17.148 14.914 4.639   1.00 39.77  ? 123 GLU A N   1 
ATOM   938  C CA  . GLU A 1 123 ? 17.317 14.476 3.260   1.00 38.72  ? 123 GLU A CA  1 
ATOM   939  C C   . GLU A 1 123 ? 15.950 14.273 2.622   1.00 39.57  ? 123 GLU A C   1 
ATOM   940  O O   . GLU A 1 123 ? 14.912 14.327 3.285   1.00 40.24  ? 123 GLU A O   1 
ATOM   941  C CB  . GLU A 1 123 ? 18.141 13.186 3.181   1.00 38.22  ? 123 GLU A CB  1 
ATOM   942  C CG  . GLU A 1 123 ? 17.376 11.932 3.581   1.00 39.44  ? 123 GLU A CG  1 
ATOM   943  C CD  . GLU A 1 123 ? 17.100 11.859 5.069   1.00 41.06  ? 123 GLU A CD  1 
ATOM   944  O OE1 . GLU A 1 123 ? 18.050 12.035 5.860   1.00 40.89  ? 123 GLU A OE1 1 
ATOM   945  O OE2 . GLU A 1 123 ? 15.931 11.634 5.446   1.00 42.59  ? 123 GLU A OE2 1 
ATOM   946  N N   . SER A 1 124 ? 15.972 14.038 1.312   1.00 39.43  ? 124 SER A N   1 
ATOM   947  C CA  . SER A 1 124 ? 14.792 13.673 0.540   1.00 40.03  ? 124 SER A CA  1 
ATOM   948  C C   . SER A 1 124 ? 15.142 12.473 -0.325  1.00 37.97  ? 124 SER A C   1 
ATOM   949  O O   . SER A 1 124 ? 16.191 12.464 -0.978  1.00 37.91  ? 124 SER A O   1 
ATOM   950  C CB  . SER A 1 124 ? 14.308 14.838 -0.331  1.00 41.29  ? 124 SER A CB  1 
ATOM   951  O OG  . SER A 1 124 ? 13.209 14.449 -1.138  1.00 42.08  ? 124 SER A OG  1 
ATOM   952  N N   . THR A 1 125 ? 14.279 11.460 -0.320  1.00 38.14  ? 125 THR A N   1 
ATOM   953  C CA  . THR A 1 125 ? 14.531 10.221 -1.040  1.00 38.88  ? 125 THR A CA  1 
ATOM   954  C C   . THR A 1 125 ? 13.404 9.944  -2.024  1.00 41.38  ? 125 THR A C   1 
ATOM   955  O O   . THR A 1 125 ? 12.258 10.353 -1.815  1.00 43.09  ? 125 THR A O   1 
ATOM   956  C CB  . THR A 1 125 ? 14.674 9.028  -0.083  1.00 39.66  ? 125 THR A CB  1 
ATOM   957  O OG1 . THR A 1 125 ? 13.402 8.727  0.505   1.00 40.75  ? 125 THR A OG1 1 
ATOM   958  C CG2 . THR A 1 125 ? 15.677 9.337  1.021   1.00 39.53  ? 125 THR A CG2 1 
ATOM   959  N N   . VAL A 1 126 ? 13.744 9.242  -3.102  1.00 42.37  ? 126 VAL A N   1 
ATOM   960  C CA  . VAL A 1 126 ? 12.782 8.811  -4.110  1.00 44.31  ? 126 VAL A CA  1 
ATOM   961  C C   . VAL A 1 126 ? 12.906 7.302  -4.259  1.00 46.23  ? 126 VAL A C   1 
ATOM   962  O O   . VAL A 1 126 ? 14.000 6.789  -4.523  1.00 45.32  ? 126 VAL A O   1 
ATOM   963  C CB  . VAL A 1 126 ? 13.007 9.507  -5.461  1.00 42.79  ? 126 VAL A CB  1 
ATOM   964  C CG1 . VAL A 1 126 ? 11.893 9.142  -6.434  1.00 45.49  ? 126 VAL A CG1 1 
ATOM   965  C CG2 . VAL A 1 126 ? 13.094 11.010 -5.284  1.00 40.77  ? 126 VAL A CG2 1 
ATOM   966  N N   . LYS A 1 127 ? 11.792 6.596  -4.087  1.00 49.67  ? 127 LYS A N   1 
ATOM   967  C CA  . LYS A 1 127 ? 11.721 5.164  -4.325  1.00 52.72  ? 127 LYS A CA  1 
ATOM   968  C C   . LYS A 1 127 ? 10.554 4.879  -5.260  1.00 57.19  ? 127 LYS A C   1 
ATOM   969  O O   . LYS A 1 127 ? 9.758  5.764  -5.585  1.00 59.12  ? 127 LYS A O   1 
ATOM   970  C CB  . LYS A 1 127 ? 11.571 4.376  -3.015  1.00 53.77  ? 127 LYS A CB  1 
ATOM   971  C CG  . LYS A 1 127 ? 12.743 4.529  -2.057  1.00 53.70  ? 127 LYS A CG  1 
ATOM   972  C CD  . LYS A 1 127 ? 12.573 3.638  -0.836  1.00 57.04  ? 127 LYS A CD  1 
ATOM   973  C CE  . LYS A 1 127 ? 13.683 3.869  0.179   1.00 57.15  ? 127 LYS A CE  1 
ATOM   974  N NZ  . LYS A 1 127 ? 13.525 3.005  1.382   1.00 59.73  ? 127 LYS A NZ  1 
ATOM   975  N N   . SER A 1 128 ? 10.455 3.628  -5.694  1.00 59.83  ? 128 SER A N   1 
ATOM   976  C CA  . SER A 1 128 ? 9.429  3.217  -6.640  1.00 64.39  ? 128 SER A CA  1 
ATOM   977  C C   . SER A 1 128 ? 8.216  2.654  -5.911  1.00 69.25  ? 128 SER A C   1 
ATOM   978  O O   . SER A 1 128 ? 8.331  2.064  -4.834  1.00 69.02  ? 128 SER A O   1 
ATOM   979  C CB  . SER A 1 128 ? 9.974  2.176  -7.619  1.00 65.44  ? 128 SER A CB  1 
ATOM   980  O OG  . SER A 1 128 ? 8.966  1.755  -8.522  1.00 68.21  ? 128 SER A OG  1 
ATOM   981  N N   . SER A 1 129 ? 7.044  2.844  -6.518  1.00 74.30  ? 129 SER A N   1 
ATOM   982  C CA  . SER A 1 129 ? 5.788  2.340  -5.964  1.00 79.52  ? 129 SER A CA  1 
ATOM   983  C C   . SER A 1 129 ? 5.530  0.950  -6.538  1.00 85.28  ? 129 SER A C   1 
ATOM   984  O O   . SER A 1 129 ? 4.746  0.756  -7.469  1.00 87.44  ? 129 SER A O   1 
ATOM   985  C CB  . SER A 1 129 ? 4.643  3.297  -6.269  1.00 80.15  ? 129 SER A CB  1 
ATOM   986  O OG  . SER A 1 129 ? 4.409  3.379  -7.664  1.00 80.31  ? 129 SER A OG  1 
ATOM   987  N N   . GLY A 1 130 ? 6.218  -0.034 -5.966  0.97 89.31  ? 130 GLY A N   1 
ATOM   988  C CA  . GLY A 1 130 ? 6.038  -1.413 -6.375  0.97 92.07  ? 130 GLY A CA  1 
ATOM   989  C C   . GLY A 1 130 ? 7.028  -1.885 -7.419  0.97 91.00  ? 130 GLY A C   1 
ATOM   990  O O   . GLY A 1 130 ? 7.917  -2.689 -7.121  0.97 91.02  ? 130 GLY A O   1 
ATOM   991  N N   . GLY A 1 131 ? 6.889  -1.390 -8.648  1.00 87.30  ? 131 GLY A N   1 
ATOM   992  C CA  . GLY A 1 131 ? 7.712  -1.825 -9.751  1.00 81.74  ? 131 GLY A CA  1 
ATOM   993  C C   . GLY A 1 131 ? 9.157  -1.381 -9.637  1.00 74.08  ? 131 GLY A C   1 
ATOM   994  O O   . GLY A 1 131 ? 9.589  -0.843 -8.614  1.00 70.43  ? 131 GLY A O   1 
ATOM   995  N N   . PRO A 1 132 ? 9.936  -1.606 -10.693 0.98 71.09  ? 132 PRO A N   1 
ATOM   996  C CA  . PRO A 1 132 ? 11.351 -1.224 -10.657 0.98 66.25  ? 132 PRO A CA  1 
ATOM   997  C C   . PRO A 1 132 ? 11.530 0.283  -10.754 0.98 60.73  ? 132 PRO A C   1 
ATOM   998  O O   . PRO A 1 132 ? 10.735 0.991  -11.375 0.98 61.05  ? 132 PRO A O   1 
ATOM   999  C CB  . PRO A 1 132 ? 11.941 -1.935 -11.879 0.98 67.93  ? 132 PRO A CB  1 
ATOM   1000 C CG  . PRO A 1 132 ? 10.789 -2.078 -12.814 0.98 71.42  ? 132 PRO A CG  1 
ATOM   1001 C CD  . PRO A 1 132 ? 9.573  -2.279 -11.952 0.98 73.63  ? 132 PRO A CD  1 
ATOM   1002 N N   . PHE A 1 133 ? 12.597 0.770  -10.127 1.00 55.08  ? 133 PHE A N   1 
ATOM   1003 C CA  . PHE A 1 133 ? 12.896 2.196  -10.093 1.00 49.34  ? 133 PHE A CA  1 
ATOM   1004 C C   . PHE A 1 133 ? 13.889 2.532  -11.199 1.00 46.46  ? 133 PHE A C   1 
ATOM   1005 O O   . PHE A 1 133 ? 15.038 2.077  -11.171 1.00 45.84  ? 133 PHE A O   1 
ATOM   1006 C CB  . PHE A 1 133 ? 13.447 2.597  -8.725  1.00 46.50  ? 133 PHE A CB  1 
ATOM   1007 C CG  . PHE A 1 133 ? 13.769 4.060  -8.600  1.00 43.77  ? 133 PHE A CG  1 
ATOM   1008 C CD1 . PHE A 1 133 ? 12.759 4.999  -8.463  1.00 43.20  ? 133 PHE A CD1 1 
ATOM   1009 C CD2 . PHE A 1 133 ? 15.084 4.493  -8.606  1.00 42.48  ? 133 PHE A CD2 1 
ATOM   1010 C CE1 . PHE A 1 133 ? 13.057 6.344  -8.344  1.00 42.19  ? 133 PHE A CE1 1 
ATOM   1011 C CE2 . PHE A 1 133 ? 15.387 5.835  -8.486  1.00 41.13  ? 133 PHE A CE2 1 
ATOM   1012 C CZ  . PHE A 1 133 ? 14.373 6.762  -8.354  1.00 40.94  ? 133 PHE A CZ  1 
ATOM   1013 N N   . VAL A 1 134 ? 13.438 3.315  -12.179 1.00 45.37  ? 134 VAL A N   1 
ATOM   1014 C CA  . VAL A 1 134 ? 14.266 3.758  -13.298 1.00 43.96  ? 134 VAL A CA  1 
ATOM   1015 C C   . VAL A 1 134 ? 13.991 5.238  -13.521 1.00 43.14  ? 134 VAL A C   1 
ATOM   1016 O O   . VAL A 1 134 ? 12.846 5.624  -13.783 1.00 45.58  ? 134 VAL A O   1 
ATOM   1017 C CB  . VAL A 1 134 ? 13.987 2.969  -14.591 1.00 45.77  ? 134 VAL A CB  1 
ATOM   1018 C CG1 . VAL A 1 134 ? 14.890 3.450  -15.713 1.00 44.97  ? 134 VAL A CG1 1 
ATOM   1019 C CG2 . VAL A 1 134 ? 14.165 1.474  -14.371 1.00 47.14  ? 134 VAL A CG2 1 
ATOM   1020 N N   . VAL A 1 135 ? 15.025 6.068  -13.406 1.00 40.77  ? 135 VAL A N   1 
ATOM   1021 C CA  . VAL A 1 135 ? 14.903 7.505  -13.623 1.00 41.31  ? 135 VAL A CA  1 
ATOM   1022 C C   . VAL A 1 135 ? 16.117 7.994  -14.397 1.00 41.67  ? 135 VAL A C   1 
ATOM   1023 O O   . VAL A 1 135 ? 17.227 7.476  -14.228 1.00 42.07  ? 135 VAL A O   1 
ATOM   1024 C CB  . VAL A 1 135 ? 14.768 8.288  -12.297 1.00 40.80  ? 135 VAL A CB  1 
ATOM   1025 C CG1 . VAL A 1 135 ? 13.425 8.015  -11.639 1.00 41.91  ? 135 VAL A CG1 1 
ATOM   1026 C CG2 . VAL A 1 135 ? 15.915 7.947  -11.357 1.00 39.41  ? 135 VAL A CG2 1 
ATOM   1027 N N   . ASP A 1 136 ? 15.902 8.993  -15.250 1.00 42.87  ? 136 ASP A N   1 
ATOM   1028 C CA  . ASP A 1 136 ? 16.991 9.697  -15.912 1.00 44.06  ? 136 ASP A CA  1 
ATOM   1029 C C   . ASP A 1 136 ? 17.445 10.855 -15.033 1.00 44.35  ? 136 ASP A C   1 
ATOM   1030 O O   . ASP A 1 136 ? 16.626 11.674 -14.602 1.00 45.68  ? 136 ASP A O   1 
ATOM   1031 C CB  . ASP A 1 136 ? 16.555 10.207 -17.285 1.00 45.90  ? 136 ASP A CB  1 
ATOM   1032 C CG  . ASP A 1 136 ? 16.455 9.098  -18.313 1.00 48.22  ? 136 ASP A CG  1 
ATOM   1033 O OD1 . ASP A 1 136 ? 17.325 8.204  -18.308 1.00 48.18  ? 136 ASP A OD1 1 
ATOM   1034 O OD2 . ASP A 1 136 ? 15.505 9.118  -19.124 0.69 50.45  ? 136 ASP A OD2 1 
ATOM   1035 N N   . VAL A 1 137 ? 18.744 10.914 -14.758 1.00 43.68  ? 137 VAL A N   1 
ATOM   1036 C CA  . VAL A 1 137 ? 19.323 11.942 -13.902 1.00 41.75  ? 137 VAL A CA  1 
ATOM   1037 C C   . VAL A 1 137 ? 19.863 13.059 -14.782 1.00 42.54  ? 137 VAL A C   1 
ATOM   1038 O O   . VAL A 1 137 ? 20.649 12.813 -15.706 1.00 43.03  ? 137 VAL A O   1 
ATOM   1039 C CB  . VAL A 1 137 ? 20.425 11.361 -12.999 1.00 39.82  ? 137 VAL A CB  1 
ATOM   1040 C CG1 . VAL A 1 137 ? 20.953 12.430 -12.057 1.00 38.54  ? 137 VAL A CG1 1 
ATOM   1041 C CG2 . VAL A 1 137 ? 19.887 10.170 -12.218 1.00 38.13  ? 137 VAL A CG2 1 
ATOM   1042 N N   . VAL A 1 138 ? 19.437 14.287 -14.498 1.00 42.43  ? 138 VAL A N   1 
ATOM   1043 C CA  . VAL A 1 138 ? 19.791 15.456 -15.294 1.00 43.24  ? 138 VAL A CA  1 
ATOM   1044 C C   . VAL A 1 138 ? 20.396 16.496 -14.362 1.00 42.46  ? 138 VAL A C   1 
ATOM   1045 O O   . VAL A 1 138 ? 19.771 16.879 -13.366 1.00 42.14  ? 138 VAL A O   1 
ATOM   1046 C CB  . VAL A 1 138 ? 18.574 16.035 -16.036 1.00 45.15  ? 138 VAL A CB  1 
ATOM   1047 C CG1 . VAL A 1 138 ? 18.975 17.250 -16.848 1.00 46.96  ? 138 VAL A CG1 1 
ATOM   1048 C CG2 . VAL A 1 138 ? 17.942 14.977 -16.927 1.00 46.46  ? 138 VAL A CG2 1 
ATOM   1049 N N   . ILE A 1 139 ? 21.605 16.952 -14.683 1.00 42.75  ? 139 ILE A N   1 
ATOM   1050 C CA  . ILE A 1 139 ? 22.319 17.945 -13.888 1.00 42.10  ? 139 ILE A CA  1 
ATOM   1051 C C   . ILE A 1 139 ? 22.484 19.188 -14.750 1.00 43.78  ? 139 ILE A C   1 
ATOM   1052 O O   . ILE A 1 139 ? 23.217 19.164 -15.747 1.00 45.00  ? 139 ILE A O   1 
ATOM   1053 C CB  . ILE A 1 139 ? 23.681 17.429 -13.403 1.00 40.97  ? 139 ILE A CB  1 
ATOM   1054 C CG1 . ILE A 1 139 ? 23.520 16.096 -12.669 1.00 38.81  ? 139 ILE A CG1 1 
ATOM   1055 C CG2 . ILE A 1 139 ? 24.345 18.455 -12.497 1.00 41.38  ? 139 ILE A CG2 1 
ATOM   1056 C CD1 . ILE A 1 139 ? 24.826 15.506 -12.188 1.00 37.35  ? 139 ILE A CD1 1 
ATOM   1057 N N   . ASN A 1 140 ? 21.808 20.272 -14.366 1.00 44.46  ? 140 ASN A N   1 
ATOM   1058 C CA  . ASN A 1 140 ? 21.871 21.549 -15.081 1.00 46.76  ? 140 ASN A CA  1 
ATOM   1059 C C   . ASN A 1 140 ? 21.517 21.370 -16.557 1.00 49.52  ? 140 ASN A C   1 
ATOM   1060 O O   . ASN A 1 140 ? 22.267 21.757 -17.457 1.00 52.69  ? 140 ASN A O   1 
ATOM   1061 C CB  . ASN A 1 140 ? 23.246 22.203 -14.916 1.00 46.63  ? 140 ASN A CB  1 
ATOM   1062 C CG  . ASN A 1 140 ? 23.580 22.505 -13.463 1.00 45.14  ? 140 ASN A CG  1 
ATOM   1063 O OD1 . ASN A 1 140 ? 22.694 22.774 -12.652 1.00 43.86  ? 140 ASN A OD1 1 
ATOM   1064 N ND2 . ASN A 1 140 ? 24.865 22.460 -13.129 1.00 45.14  ? 140 ASN A ND2 1 
ATOM   1065 N N   . ASP A 1 141 ? 20.353 20.762 -16.795 1.00 49.37  ? 141 ASP A N   1 
ATOM   1066 C CA  . ASP A 1 141 ? 19.791 20.516 -18.123 1.00 52.06  ? 141 ASP A CA  1 
ATOM   1067 C C   . ASP A 1 141 ? 20.655 19.602 -18.983 1.00 54.10  ? 141 ASP A C   1 
ATOM   1068 O O   . ASP A 1 141 ? 20.526 19.611 -20.212 1.00 57.32  ? 141 ASP A O   1 
ATOM   1069 C CB  . ASP A 1 141 ? 19.526 21.826 -18.875 1.00 54.67  ? 141 ASP A CB  1 
ATOM   1070 C CG  . ASP A 1 141 ? 18.646 22.778 -18.095 0.56 56.06  ? 141 ASP A CG  1 
ATOM   1071 O OD1 . ASP A 1 141 ? 17.825 22.305 -17.279 0.77 55.80  ? 141 ASP A OD1 1 
ATOM   1072 O OD2 . ASP A 1 141 ? 18.774 24.003 -18.300 0.27 45.23  ? 141 ASP A OD2 1 
ATOM   1073 N N   . ILE A 1 142 ? 21.529 18.805 -18.373 1.00 53.80  ? 142 ILE A N   1 
ATOM   1074 C CA  . ILE A 1 142 ? 22.402 17.884 -19.093 1.00 55.73  ? 142 ILE A CA  1 
ATOM   1075 C C   . ILE A 1 142 ? 22.164 16.480 -18.557 1.00 52.24  ? 142 ILE A C   1 
ATOM   1076 O O   . ILE A 1 142 ? 22.240 16.254 -17.343 1.00 49.01  ? 142 ILE A O   1 
ATOM   1077 C CB  . ILE A 1 142 ? 23.886 18.275 -18.954 1.00 59.27  ? 142 ILE A CB  1 
ATOM   1078 C CG1 . ILE A 1 142 ? 24.096 19.742 -19.334 1.00 64.23  ? 142 ILE A CG1 1 
ATOM   1079 C CG2 . ILE A 1 142 ? 24.758 17.378 -19.820 1.00 59.32  ? 142 ILE A CG2 1 
ATOM   1080 C CD1 . ILE A 1 142 ? 25.528 20.212 -19.186 1.00 66.74  ? 142 ILE A CD1 1 
ATOM   1081 N N   . HIS A 1 143 ? 21.882 15.542 -19.459 1.00 52.04  ? 143 HIS A N   1 
ATOM   1082 C CA  . HIS A 1 143 ? 21.673 14.157 -19.057 1.00 50.61  ? 143 HIS A CA  1 
ATOM   1083 C C   . HIS A 1 143 ? 22.972 13.562 -18.531 1.00 48.57  ? 143 HIS A C   1 
ATOM   1084 O O   . HIS A 1 143 ? 24.015 13.637 -19.188 1.00 50.45  ? 143 HIS A O   1 
ATOM   1085 C CB  . HIS A 1 143 ? 21.149 13.336 -20.234 1.00 52.61  ? 143 HIS A CB  1 
ATOM   1086 C CG  . HIS A 1 143 ? 20.916 11.894 -19.910 1.00 53.48  ? 143 HIS A CG  1 
ATOM   1087 N ND1 . HIS A 1 143 ? 21.905 10.939 -20.009 1.00 53.31  ? 143 HIS A ND1 1 
ATOM   1088 C CD2 . HIS A 1 143 ? 19.805 11.242 -19.490 1.00 53.22  ? 143 HIS A CD2 1 
ATOM   1089 C CE1 . HIS A 1 143 ? 21.414 9.762  -19.663 1.00 53.20  ? 143 HIS A CE1 1 
ATOM   1090 N NE2 . HIS A 1 143 ? 20.142 9.919  -19.343 1.00 52.79  ? 143 HIS A NE2 1 
ATOM   1091 N N   . PHE A 1 144 ? 22.909 12.969 -17.340 1.00 44.83  ? 144 PHE A N   1 
ATOM   1092 C CA  . PHE A 1 144 ? 24.082 12.414 -16.676 1.00 42.29  ? 144 PHE A CA  1 
ATOM   1093 C C   . PHE A 1 144 ? 24.094 10.894 -16.660 1.00 41.75  ? 144 PHE A C   1 
ATOM   1094 O O   . PHE A 1 144 ? 25.104 10.281 -17.020 1.00 43.56  ? 144 PHE A O   1 
ATOM   1095 C CB  . PHE A 1 144 ? 24.175 12.951 -15.239 1.00 39.88  ? 144 PHE A CB  1 
ATOM   1096 C CG  . PHE A 1 144 ? 25.372 12.452 -14.482 1.00 38.82  ? 144 PHE A CG  1 
ATOM   1097 C CD1 . PHE A 1 144 ? 26.645 12.888 -14.808 1.00 39.11  ? 144 PHE A CD1 1 
ATOM   1098 C CD2 . PHE A 1 144 ? 25.224 11.551 -13.440 1.00 38.01  ? 144 PHE A CD2 1 
ATOM   1099 C CE1 . PHE A 1 144 ? 27.750 12.430 -14.113 1.00 38.63  ? 144 PHE A CE1 1 
ATOM   1100 C CE2 . PHE A 1 144 ? 26.325 11.090 -12.740 1.00 37.47  ? 144 PHE A CE2 1 
ATOM   1101 C CZ  . PHE A 1 144 ? 27.589 11.531 -13.077 1.00 37.70  ? 144 PHE A CZ  1 
ATOM   1102 N N   . GLU A 1 145 ? 22.995 10.263 -16.253 1.00 39.68  ? 145 GLU A N   1 
ATOM   1103 C CA  . GLU A 1 145 ? 22.949 8.811  -16.154 1.00 38.76  ? 145 GLU A CA  1 
ATOM   1104 C C   . GLU A 1 145 ? 21.498 8.361  -16.109 1.00 40.07  ? 145 GLU A C   1 
ATOM   1105 O O   . GLU A 1 145 ? 20.604 9.121  -15.727 1.00 40.59  ? 145 GLU A O   1 
ATOM   1106 C CB  . GLU A 1 145 ? 23.698 8.310  -14.913 1.00 36.12  ? 145 GLU A CB  1 
ATOM   1107 C CG  . GLU A 1 145 ? 23.052 8.738  -13.603 1.00 34.84  ? 145 GLU A CG  1 
ATOM   1108 C CD  . GLU A 1 145 ? 23.830 8.286  -12.384 1.00 34.07  ? 145 GLU A CD  1 
ATOM   1109 O OE1 . GLU A 1 145 ? 23.404 8.609  -11.255 0.73 33.21  ? 145 GLU A OE1 1 
ATOM   1110 O OE2 . GLU A 1 145 ? 24.867 7.610  -12.551 0.62 34.71  ? 145 GLU A OE2 1 
ATOM   1111 N N   . ARG A 1 146 ? 21.278 7.110  -16.506 1.00 40.85  ? 146 ARG A N   1 
ATOM   1112 C CA  . ARG A 1 146 ? 19.980 6.454  -16.364 1.00 41.79  ? 146 ARG A CA  1 
ATOM   1113 C C   . ARG A 1 146 ? 20.089 5.489  -15.190 1.00 41.85  ? 146 ARG A C   1 
ATOM   1114 O O   . ARG A 1 146 ? 20.618 4.382  -15.325 1.00 42.88  ? 146 ARG A O   1 
ATOM   1115 C CB  . ARG A 1 146 ? 19.573 5.743  -17.651 1.00 42.83  ? 146 ARG A CB  1 
ATOM   1116 C CG  . ARG A 1 146 ? 18.304 4.913  -17.515 1.00 43.78  ? 146 ARG A CG  1 
ATOM   1117 C CD  . ARG A 1 146 ? 17.641 4.666  -18.861 1.00 45.77  ? 146 ARG A CD  1 
ATOM   1118 N NE  . ARG A 1 146 ? 16.960 5.857  -19.361 1.00 46.39  ? 146 ARG A NE  1 
ATOM   1119 C CZ  . ARG A 1 146 ? 16.217 5.887  -20.463 1.00 48.93  ? 146 ARG A CZ  1 
ATOM   1120 N NH1 . ARG A 1 146 ? 16.055 4.788  -21.188 1.00 50.52  ? 146 ARG A NH1 1 
ATOM   1121 N NH2 . ARG A 1 146 ? 15.634 7.016  -20.841 1.00 49.49  ? 146 ARG A NH2 1 
ATOM   1122 N N   . PHE A 1 147 ? 19.590 5.917  -14.034 1.00 40.67  ? 147 PHE A N   1 
ATOM   1123 C CA  . PHE A 1 147 ? 19.719 5.143  -12.808 1.00 40.14  ? 147 PHE A CA  1 
ATOM   1124 C C   . PHE A 1 147 ? 18.648 4.062  -12.746 1.00 41.78  ? 147 PHE A C   1 
ATOM   1125 O O   . PHE A 1 147 ? 17.473 4.323  -13.021 1.00 43.90  ? 147 PHE A O   1 
ATOM   1126 C CB  . PHE A 1 147 ? 19.613 6.064  -11.592 1.00 38.96  ? 147 PHE A CB  1 
ATOM   1127 C CG  . PHE A 1 147 ? 19.773 5.359  -10.273 1.00 38.46  ? 147 PHE A CG  1 
ATOM   1128 C CD1 . PHE A 1 147 ? 18.676 4.818  -9.621  1.00 39.74  ? 147 PHE A CD1 1 
ATOM   1129 C CD2 . PHE A 1 147 ? 21.019 5.248  -9.680  1.00 36.58  ? 147 PHE A CD2 1 
ATOM   1130 C CE1 . PHE A 1 147 ? 18.821 4.171  -8.410  1.00 39.36  ? 147 PHE A CE1 1 
ATOM   1131 C CE2 . PHE A 1 147 ? 21.169 4.605  -8.468  1.00 36.06  ? 147 PHE A CE2 1 
ATOM   1132 C CZ  . PHE A 1 147 ? 20.069 4.065  -7.832  1.00 37.51  ? 147 PHE A CZ  1 
ATOM   1133 N N   . ARG A 1 148 ? 19.057 2.848  -12.381 1.00 41.61  ? 148 ARG A N   1 
ATOM   1134 C CA  . ARG A 1 148 ? 18.121 1.773  -12.077 1.00 44.01  ? 148 ARG A CA  1 
ATOM   1135 C C   . ARG A 1 148 ? 18.607 1.046  -10.834 1.00 44.34  ? 148 ARG A C   1 
ATOM   1136 O O   . ARG A 1 148 ? 19.669 0.416  -10.856 1.00 44.54  ? 148 ARG A O   1 
ATOM   1137 C CB  . ARG A 1 148 ? 17.968 0.793  -13.244 1.00 47.43  ? 148 ARG A CB  1 
ATOM   1138 C CG  . ARG A 1 148 ? 17.034 -0.359 -12.906 0.80 49.95  ? 148 ARG A CG  1 
ATOM   1139 C CD  . ARG A 1 148 ? 16.674 -1.208 -14.110 0.70 52.35  ? 148 ARG A CD  1 
ATOM   1140 N NE  . ARG A 1 148 ? 15.801 -2.313 -13.723 0.70 54.02  ? 148 ARG A NE  1 
ATOM   1141 C CZ  . ARG A 1 148 ? 15.161 -3.101 -14.581 0.60 45.09  ? 148 ARG A CZ  1 
ATOM   1142 N NH1 . ARG A 1 148 ? 15.288 -2.907 -15.886 0.60 45.98  ? 148 ARG A NH1 1 
ATOM   1143 N NH2 . ARG A 1 148 ? 14.389 -4.081 -14.132 0.60 47.10  ? 148 ARG A NH2 1 
ATOM   1144 N N   . GLY A 1 149 ? 17.829 1.135  -9.759  1.00 45.37  ? 149 GLY A N   1 
ATOM   1145 C CA  . GLY A 1 149 ? 18.156 0.478  -8.510  1.00 44.61  ? 149 GLY A CA  1 
ATOM   1146 C C   . GLY A 1 149 ? 16.997 0.519  -7.537  1.00 43.57  ? 149 GLY A C   1 
ATOM   1147 O O   . GLY A 1 149 ? 15.844 0.319  -7.931  1.00 45.30  ? 149 GLY A O   1 
ATOM   1148 N N   . ASP A 1 150 ? 17.285 0.780  -6.263  1.00 41.38  ? 150 ASP A N   1 
ATOM   1149 C CA  . ASP A 1 150 ? 16.230 0.910  -5.266  1.00 39.81  ? 150 ASP A CA  1 
ATOM   1150 C C   . ASP A 1 150 ? 15.771 2.348  -5.078  1.00 39.41  ? 150 ASP A C   1 
ATOM   1151 O O   . ASP A 1 150 ? 14.600 2.576  -4.755  1.00 42.14  ? 150 ASP A O   1 
ATOM   1152 C CB  . ASP A 1 150 ? 16.693 0.341  -3.922  1.00 37.91  ? 150 ASP A CB  1 
ATOM   1153 C CG  . ASP A 1 150 ? 16.689 -1.173 -3.899  1.00 41.19  ? 150 ASP A CG  1 
ATOM   1154 O OD1 . ASP A 1 150 ? 16.392 -1.784 -4.948  1.00 43.70  ? 150 ASP A OD1 1 
ATOM   1155 O OD2 . ASP A 1 150 ? 16.977 -1.754 -2.831  1.00 42.30  ? 150 ASP A OD2 1 
ATOM   1156 N N   . GLY A 1 151 ? 16.653 3.319  -5.270  1.00 36.90  ? 151 GLY A N   1 
ATOM   1157 C CA  . GLY A 1 151 ? 16.259 4.706  -5.159  1.00 36.34  ? 151 GLY A CA  1 
ATOM   1158 C C   . GLY A 1 151 ? 17.468 5.613  -5.040  1.00 34.98  ? 151 GLY A C   1 
ATOM   1159 O O   . GLY A 1 151 ? 18.611 5.188  -5.202  1.00 34.52  ? 151 GLY A O   1 
ATOM   1160 N N   . LEU A 1 152 ? 17.177 6.880  -4.753  1.00 35.13  ? 152 LEU A N   1 
ATOM   1161 C CA  . LEU A 1 152 ? 18.191 7.911  -4.595  1.00 33.74  ? 152 LEU A CA  1 
ATOM   1162 C C   . LEU A 1 152 ? 17.906 8.709  -3.331  1.00 33.81  ? 152 LEU A C   1 
ATOM   1163 O O   . LEU A 1 152 ? 16.801 8.675  -2.784  1.00 34.48  ? 152 LEU A O   1 
ATOM   1164 C CB  . LEU A 1 152 ? 18.238 8.843  -5.812  1.00 33.26  ? 152 LEU A CB  1 
ATOM   1165 C CG  . LEU A 1 152 ? 18.730 8.215  -7.117  1.00 32.48  ? 152 LEU A CG  1 
ATOM   1166 C CD1 . LEU A 1 152 ? 18.454 9.136  -8.293  1.00 34.59  ? 152 LEU A CD1 1 
ATOM   1167 C CD2 . LEU A 1 152 ? 20.214 7.893  -7.024  1.00 28.69  ? 152 LEU A CD2 1 
ATOM   1168 N N   . CYS A 1 153 ? 18.921 9.438  -2.871  1.00 34.62  ? 153 CYS A N   1 
ATOM   1169 C CA  . CYS A 1 153 ? 18.817 10.192 -1.626  1.00 36.34  ? 153 CYS A CA  1 
ATOM   1170 C C   . CYS A 1 153 ? 19.638 11.464 -1.744  1.00 35.70  ? 153 CYS A C   1 
ATOM   1171 O O   . CYS A 1 153 ? 20.863 11.399 -1.880  1.00 34.89  ? 153 CYS A O   1 
ATOM   1172 C CB  . CYS A 1 153 ? 19.296 9.352  -0.439  1.00 38.11  ? 153 CYS A CB  1 
ATOM   1173 S SG  . CYS A 1 153 ? 19.415 10.251 1.126   1.00 39.11  ? 153 CYS A SG  1 
ATOM   1174 N N   . MET A 1 154 ? 18.968 12.612 -1.690  1.00 36.88  ? 154 MET A N   1 
ATOM   1175 C CA  . MET A 1 154 ? 19.628 13.912 -1.685  1.00 37.63  ? 154 MET A CA  1 
ATOM   1176 C C   . MET A 1 154 ? 19.627 14.445 -0.258  1.00 39.95  ? 154 MET A C   1 
ATOM   1177 O O   . MET A 1 154 ? 18.560 14.624 0.339   1.00 42.13  ? 154 MET A O   1 
ATOM   1178 C CB  . MET A 1 154 ? 18.931 14.889 -2.631  1.00 37.86  ? 154 MET A CB  1 
ATOM   1179 C CG  . MET A 1 154 ? 19.671 16.205 -2.808  1.00 39.07  ? 154 MET A CG  1 
ATOM   1180 S SD  . MET A 1 154 ? 21.201 16.029 -3.747  1.00 40.32  ? 154 MET A SD  1 
ATOM   1181 C CE  . MET A 1 154 ? 20.562 15.888 -5.414  1.00 42.63  ? 154 MET A CE  1 
ATOM   1182 N N   . SER A 1 155 ? 20.816 14.702 0.281   1.00 40.49  ? 155 SER A N   1 
ATOM   1183 C CA  . SER A 1 155 ? 20.985 15.016 1.691   1.00 39.80  ? 155 SER A CA  1 
ATOM   1184 C C   . SER A 1 155 ? 21.508 16.432 1.887   1.00 37.67  ? 155 SER A C   1 
ATOM   1185 O O   . SER A 1 155 ? 22.274 16.952 1.070   1.00 37.83  ? 155 SER A O   1 
ATOM   1186 C CB  . SER A 1 155 ? 21.945 14.026 2.359   1.00 40.43  ? 155 SER A CB  1 
ATOM   1187 O OG  . SER A 1 155 ? 22.368 14.506 3.622   1.00 41.14  ? 155 SER A OG  1 
ATOM   1188 N N   . THR A 1 156 ? 21.085 17.044 2.989   1.00 35.70  ? 156 THR A N   1 
ATOM   1189 C CA  . THR A 1 156 ? 21.638 18.309 3.444   1.00 35.13  ? 156 THR A CA  1 
ATOM   1190 C C   . THR A 1 156 ? 22.979 18.059 4.126   1.00 33.95  ? 156 THR A C   1 
ATOM   1191 O O   . THR A 1 156 ? 23.341 16.913 4.403   1.00 33.83  ? 156 THR A O   1 
ATOM   1192 C CB  . THR A 1 156 ? 20.656 18.989 4.396   1.00 36.77  ? 156 THR A CB  1 
ATOM   1193 O OG1 . THR A 1 156 ? 20.595 18.257 5.627   1.00 38.58  ? 156 THR A OG1 1 
ATOM   1194 C CG2 . THR A 1 156 ? 19.267 19.045 3.780   1.00 36.34  ? 156 THR A CG2 1 
ATOM   1195 N N   . PRO A 1 157 ? 23.760 19.115 4.392   1.00 33.77  ? 157 PRO A N   1 
ATOM   1196 C CA  . PRO A 1 157 ? 25.018 18.909 5.136   1.00 33.69  ? 157 PRO A CA  1 
ATOM   1197 C C   . PRO A 1 157 ? 24.817 18.257 6.494   1.00 34.03  ? 157 PRO A C   1 
ATOM   1198 O O   . PRO A 1 157 ? 25.467 17.248 6.799   1.00 33.31  ? 157 PRO A O   1 
ATOM   1199 C CB  . PRO A 1 157 ? 25.580 20.331 5.258   1.00 35.33  ? 157 PRO A CB  1 
ATOM   1200 C CG  . PRO A 1 157 ? 25.032 21.049 4.085   1.00 36.43  ? 157 PRO A CG  1 
ATOM   1201 C CD  . PRO A 1 157 ? 23.659 20.485 3.856   1.00 35.29  ? 157 PRO A CD  1 
ATOM   1202 N N   . SER A 1 158 ? 23.929 18.807 7.326   1.00 34.72  ? 158 SER A N   1 
ATOM   1203 C CA  . SER A 1 158 ? 23.665 18.205 8.628   1.00 34.69  ? 158 SER A CA  1 
ATOM   1204 C C   . SER A 1 158 ? 22.955 16.863 8.508   1.00 34.45  ? 158 SER A C   1 
ATOM   1205 O O   . SER A 1 158 ? 22.973 16.079 9.463   1.00 35.95  ? 158 SER A O   1 
ATOM   1206 C CB  . SER A 1 158 ? 22.840 19.157 9.495   1.00 35.88  ? 158 SER A CB  1 
ATOM   1207 O OG  . SER A 1 158 ? 21.587 19.438 8.897   1.00 36.52  ? 158 SER A OG  1 
ATOM   1208 N N   . GLY A 1 159 ? 22.334 16.581 7.363   1.00 33.41  ? 159 GLY A N   1 
ATOM   1209 C CA  . GLY A 1 159 ? 21.717 15.289 7.140   1.00 33.22  ? 159 GLY A CA  1 
ATOM   1210 C C   . GLY A 1 159 ? 22.661 14.198 6.685   1.00 33.27  ? 159 GLY A C   1 
ATOM   1211 O O   . GLY A 1 159 ? 22.236 13.045 6.565   1.00 33.71  ? 159 GLY A O   1 
ATOM   1212 N N   . THR A 1 160 ? 23.930 14.534 6.430   1.00 33.33  ? 160 THR A N   1 
ATOM   1213 C CA  . THR A 1 160 ? 24.886 13.532 5.970   1.00 33.68  ? 160 THR A CA  1 
ATOM   1214 C C   . THR A 1 160 ? 25.166 12.483 7.039   1.00 34.90  ? 160 THR A C   1 
ATOM   1215 O O   . THR A 1 160 ? 25.532 11.348 6.713   1.00 35.30  ? 160 THR A O   1 
ATOM   1216 C CB  . THR A 1 160 ? 26.191 14.202 5.532   1.00 34.73  ? 160 THR A CB  1 
ATOM   1217 O OG1 . THR A 1 160 ? 26.660 15.080 6.565   1.00 34.72  ? 160 THR A OG1 1 
ATOM   1218 C CG2 . THR A 1 160 ? 25.974 14.997 4.260   1.00 37.24  ? 160 THR A CG2 1 
ATOM   1219 N N   . THR A 1 161 ? 25.000 12.840 8.313   1.00 34.67  ? 161 THR A N   1 
ATOM   1220 C CA  . THR A 1 161 ? 25.204 11.910 9.417   1.00 35.58  ? 161 THR A CA  1 
ATOM   1221 C C   . THR A 1 161 ? 24.037 10.949 9.606   1.00 35.22  ? 161 THR A C   1 
ATOM   1222 O O   . THR A 1 161 ? 24.123 10.057 10.457  1.00 35.76  ? 161 THR A O   1 
ATOM   1223 C CB  . THR A 1 161 ? 25.445 12.684 10.717  1.00 38.03  ? 161 THR A CB  1 
ATOM   1224 O OG1 . THR A 1 161 ? 24.282 13.459 11.039  1.00 38.83  ? 161 THR A OG1 1 
ATOM   1225 C CG2 . THR A 1 161 ? 26.634 13.617 10.564  1.00 38.91  ? 161 THR A CG2 1 
ATOM   1226 N N   . ALA A 1 162 ? 22.962 11.103 8.833   1.00 35.34  ? 162 ALA A N   1 
ATOM   1227 C CA  . ALA A 1 162 ? 21.780 10.262 8.972   1.00 36.68  ? 162 ALA A CA  1 
ATOM   1228 C C   . ALA A 1 162 ? 21.714 9.204  7.876   1.00 36.02  ? 162 ALA A C   1 
ATOM   1229 O O   . ALA A 1 162 ? 22.609 8.360  7.763   1.00 35.76  ? 162 ALA A O   1 
ATOM   1230 C CB  . ALA A 1 162 ? 20.514 11.120 8.952   1.00 37.09  ? 162 ALA A CB  1 
ATOM   1231 N N   . TYR A 1 163 ? 20.649 9.246  7.069   1.00 35.86  ? 163 TYR A N   1 
ATOM   1232 C CA  . TYR A 1 163 ? 20.454 8.246  6.022   1.00 36.10  ? 163 TYR A CA  1 
ATOM   1233 C C   . TYR A 1 163 ? 21.599 8.267  5.017   1.00 35.14  ? 163 TYR A C   1 
ATOM   1234 O O   . TYR A 1 163 ? 22.012 7.216  4.512   1.00 37.14  ? 163 TYR A O   1 
ATOM   1235 C CB  . TYR A 1 163 ? 19.114 8.486  5.322   1.00 37.39  ? 163 TYR A CB  1 
ATOM   1236 C CG  . TYR A 1 163 ? 18.545 7.289  4.583   1.00 39.78  ? 163 TYR A CG  1 
ATOM   1237 C CD1 . TYR A 1 163 ? 19.197 6.063  4.586   1.00 40.02  ? 163 TYR A CD1 1 
ATOM   1238 C CD2 . TYR A 1 163 ? 17.351 7.392  3.879   1.00 42.23  ? 163 TYR A CD2 1 
ATOM   1239 C CE1 . TYR A 1 163 ? 18.676 4.974  3.911   1.00 41.73  ? 163 TYR A CE1 1 
ATOM   1240 C CE2 . TYR A 1 163 ? 16.823 6.308  3.201   1.00 43.52  ? 163 TYR A CE2 1 
ATOM   1241 C CZ  . TYR A 1 163 ? 17.490 5.102  3.220   1.00 42.91  ? 163 TYR A CZ  1 
ATOM   1242 O OH  . TYR A 1 163 ? 16.967 4.023  2.545   1.00 43.34  ? 163 TYR A OH  1 
ATOM   1243 N N   . ASN A 1 164 ? 22.128 9.456  4.719   1.00 32.69  ? 164 ASN A N   1 
ATOM   1244 C CA  . ASN A 1 164 ? 23.237 9.569  3.777   1.00 32.72  ? 164 ASN A CA  1 
ATOM   1245 C C   . ASN A 1 164 ? 24.431 8.731  4.218   1.00 35.00  ? 164 ASN A C   1 
ATOM   1246 O O   . ASN A 1 164 ? 25.119 8.129  3.384   1.00 34.99  ? 164 ASN A O   1 
ATOM   1247 C CB  . ASN A 1 164 ? 23.636 11.037 3.623   1.00 32.19  ? 164 ASN A CB  1 
ATOM   1248 C CG  . ASN A 1 164 ? 24.924 11.216 2.843   1.00 33.34  ? 164 ASN A CG  1 
ATOM   1249 O OD1 . ASN A 1 164 ? 24.913 11.297 1.616   1.00 35.73  ? 164 ASN A OD1 1 
ATOM   1250 N ND2 . ASN A 1 164 ? 26.043 11.292 3.556   1.00 32.68  ? 164 ASN A ND2 1 
ATOM   1251 N N   . LYS A 1 165 ? 24.689 8.674  5.527   1.00 36.32  ? 165 LYS A N   1 
ATOM   1252 C CA  . LYS A 1 165 ? 25.834 7.917  6.024   1.00 36.21  ? 165 LYS A CA  1 
ATOM   1253 C C   . LYS A 1 165 ? 25.650 6.420  5.807   1.00 36.00  ? 165 LYS A C   1 
ATOM   1254 O O   . LYS A 1 165 ? 26.604 5.719  5.449   1.00 35.68  ? 165 LYS A O   1 
ATOM   1255 C CB  . LYS A 1 165 ? 26.057 8.222  7.505   1.00 36.35  ? 165 LYS A CB  1 
ATOM   1256 C CG  . LYS A 1 165 ? 27.187 7.428  8.138   1.00 36.70  ? 165 LYS A CG  1 
ATOM   1257 C CD  . LYS A 1 165 ? 27.450 7.879  9.563   1.00 36.70  ? 165 LYS A CD  1 
ATOM   1258 C CE  . LYS A 1 165 ? 28.518 7.022  10.218  1.00 38.62  ? 165 LYS A CE  1 
ATOM   1259 N NZ  . LYS A 1 165 ? 28.094 5.598  10.313  1.00 40.57  ? 165 LYS A NZ  1 
ATOM   1260 N N   . SER A 1 166 ? 24.432 5.913  6.015   1.00 35.76  ? 166 SER A N   1 
ATOM   1261 C CA  . SER A 1 166 ? 24.174 4.488  5.842   1.00 36.91  ? 166 SER A CA  1 
ATOM   1262 C C   . SER A 1 166 ? 24.321 4.044  4.393   1.00 37.35  ? 166 SER A C   1 
ATOM   1263 O O   . SER A 1 166 ? 24.562 2.859  4.142   1.00 38.00  ? 166 SER A O   1 
ATOM   1264 C CB  . SER A 1 166 ? 22.774 4.143  6.350   1.00 38.16  ? 166 SER A CB  1 
ATOM   1265 O OG  . SER A 1 166 ? 22.623 4.504  7.713   1.00 39.81  ? 166 SER A OG  1 
ATOM   1266 N N   . LEU A 1 167 ? 24.182 4.963  3.440   1.00 37.27  ? 167 LEU A N   1 
ATOM   1267 C CA  . LEU A 1 167 ? 24.298 4.653  2.023   1.00 37.93  ? 167 LEU A CA  1 
ATOM   1268 C C   . LEU A 1 167 ? 25.720 4.813  1.499   1.00 38.16  ? 167 LEU A C   1 
ATOM   1269 O O   . LEU A 1 167 ? 25.933 4.733  0.285   1.00 40.37  ? 167 LEU A O   1 
ATOM   1270 C CB  . LEU A 1 167 ? 23.341 5.535  1.217   1.00 36.43  ? 167 LEU A CB  1 
ATOM   1271 C CG  . LEU A 1 167 ? 21.855 5.357  1.534   1.00 34.91  ? 167 LEU A CG  1 
ATOM   1272 C CD1 . LEU A 1 167 ? 21.020 6.428  0.852   1.00 34.25  ? 167 LEU A CD1 1 
ATOM   1273 C CD2 . LEU A 1 167 ? 21.391 3.971  1.120   1.00 35.01  ? 167 LEU A CD2 1 
ATOM   1274 N N   . GLY A 1 168 ? 26.693 5.032  2.381   1.00 37.03  ? 168 GLY A N   1 
ATOM   1275 C CA  . GLY A 1 168 ? 28.069 5.221  1.978   1.00 36.12  ? 168 GLY A CA  1 
ATOM   1276 C C   . GLY A 1 168 ? 28.464 6.655  1.703   1.00 34.93  ? 168 GLY A C   1 
ATOM   1277 O O   . GLY A 1 168 ? 29.603 6.895  1.281   1.00 35.96  ? 168 GLY A O   1 
ATOM   1278 N N   . GLY A 1 169 ? 27.569 7.613  1.928   1.00 33.70  ? 169 GLY A N   1 
ATOM   1279 C CA  . GLY A 1 169 ? 27.876 9.001  1.659   1.00 33.20  ? 169 GLY A CA  1 
ATOM   1280 C C   . GLY A 1 169 ? 28.921 9.559  2.605   1.00 34.00  ? 169 GLY A C   1 
ATOM   1281 O O   . GLY A 1 169 ? 29.270 8.973  3.632   1.00 33.41  ? 169 GLY A O   1 
ATOM   1282 N N   . ALA A 1 170 ? 29.434 10.727 2.240   1.00 34.95  ? 170 ALA A N   1 
ATOM   1283 C CA  . ALA A 1 170 ? 30.456 11.391 3.031   1.00 35.88  ? 170 ALA A CA  1 
ATOM   1284 C C   . ALA A 1 170 ? 29.820 12.290 4.083   1.00 36.38  ? 170 ALA A C   1 
ATOM   1285 O O   . ALA A 1 170 ? 28.745 12.859 3.875   1.00 37.78  ? 170 ALA A O   1 
ATOM   1286 C CB  . ALA A 1 170 ? 31.384 12.214 2.136   1.00 35.28  ? 170 ALA A CB  1 
ATOM   1287 N N   . LEU A 1 171 ? 30.495 12.407 5.224   1.00 35.91  ? 171 LEU A N   1 
ATOM   1288 C CA  . LEU A 1 171 ? 30.070 13.343 6.254   1.00 35.26  ? 171 LEU A CA  1 
ATOM   1289 C C   . LEU A 1 171 ? 30.607 14.729 5.920   1.00 37.08  ? 171 LEU A C   1 
ATOM   1290 O O   . LEU A 1 171 ? 31.813 14.907 5.719   1.00 40.22  ? 171 LEU A O   1 
ATOM   1291 C CB  . LEU A 1 171 ? 30.553 12.889 7.631   1.00 35.25  ? 171 LEU A CB  1 
ATOM   1292 C CG  . LEU A 1 171 ? 30.164 11.466 8.043   1.00 36.05  ? 171 LEU A CG  1 
ATOM   1293 C CD1 . LEU A 1 171 ? 30.560 11.193 9.486   1.00 37.23  ? 171 LEU A CD1 1 
ATOM   1294 C CD2 . LEU A 1 171 ? 28.677 11.211 7.834   1.00 36.33  ? 171 LEU A CD2 1 
ATOM   1295 N N   . MET A 1 172 ? 29.707 15.706 5.855   1.00 36.33  ? 172 MET A N   1 
ATOM   1296 C CA  . MET A 1 172 ? 30.006 17.023 5.312   1.00 38.18  ? 172 MET A CA  1 
ATOM   1297 C C   . MET A 1 172 ? 29.688 18.077 6.358   1.00 40.89  ? 172 MET A C   1 
ATOM   1298 O O   . MET A 1 172 ? 28.618 18.040 6.972   1.00 42.48  ? 172 MET A O   1 
ATOM   1299 C CB  . MET A 1 172 ? 29.195 17.256 4.036   1.00 38.34  ? 172 MET A CB  1 
ATOM   1300 C CG  . MET A 1 172 ? 29.611 18.440 3.198   0.85 39.39  ? 172 MET A CG  1 
ATOM   1301 S SD  . MET A 1 172 ? 28.800 18.339 1.592   0.78 38.81  ? 172 MET A SD  1 
ATOM   1302 C CE  . MET A 1 172 ? 27.110 18.026 2.093   0.75 37.64  ? 172 MET A CE  1 
ATOM   1303 N N   . HIS A 1 173 ? 30.614 19.010 6.555   1.00 42.71  ? 173 HIS A N   1 
ATOM   1304 C CA  . HIS A 1 173 ? 30.438 20.015 7.590   1.00 44.67  ? 173 HIS A CA  1 
ATOM   1305 C C   . HIS A 1 173 ? 29.296 20.955 7.221   1.00 47.86  ? 173 HIS A C   1 
ATOM   1306 O O   . HIS A 1 173 ? 29.133 21.307 6.044   1.00 48.69  ? 173 HIS A O   1 
ATOM   1307 C CB  . HIS A 1 173 ? 31.735 20.798 7.793   1.00 45.62  ? 173 HIS A CB  1 
ATOM   1308 C CG  . HIS A 1 173 ? 31.707 21.714 8.975   1.00 47.55  ? 173 HIS A CG  1 
ATOM   1309 N ND1 . HIS A 1 173 ? 31.364 23.045 8.875   1.00 48.71  ? 173 HIS A ND1 1 
ATOM   1310 C CD2 . HIS A 1 173 ? 31.972 21.491 10.284  1.00 48.20  ? 173 HIS A CD2 1 
ATOM   1311 C CE1 . HIS A 1 173 ? 31.423 23.604 10.071  1.00 50.18  ? 173 HIS A CE1 1 
ATOM   1312 N NE2 . HIS A 1 173 ? 31.790 22.683 10.943  1.00 49.58  ? 173 HIS A NE2 1 
ATOM   1313 N N   . PRO A 1 174 ? 28.475 21.382 8.187   1.00 51.74  ? 174 PRO A N   1 
ATOM   1314 C CA  . PRO A 1 174 ? 27.290 22.186 7.848   1.00 52.05  ? 174 PRO A CA  1 
ATOM   1315 C C   . PRO A 1 174 ? 27.604 23.582 7.336   1.00 53.35  ? 174 PRO A C   1 
ATOM   1316 O O   . PRO A 1 174 ? 26.722 24.210 6.739   1.00 54.24  ? 174 PRO A O   1 
ATOM   1317 C CB  . PRO A 1 174 ? 26.509 22.243 9.169   1.00 52.47  ? 174 PRO A CB  1 
ATOM   1318 C CG  . PRO A 1 174 ? 27.025 21.086 9.972   1.00 51.87  ? 174 PRO A CG  1 
ATOM   1319 C CD  . PRO A 1 174 ? 28.467 20.957 9.598   1.00 51.97  ? 174 PRO A CD  1 
ATOM   1320 N N   . SER A 1 175 ? 28.819 24.094 7.539   1.00 52.22  ? 175 SER A N   1 
ATOM   1321 C CA  . SER A 1 175 ? 29.139 25.417 7.018   1.00 53.30  ? 175 SER A CA  1 
ATOM   1322 C C   . SER A 1 175 ? 29.249 25.436 5.499   1.00 51.58  ? 175 SER A C   1 
ATOM   1323 O O   . SER A 1 175 ? 29.335 26.521 4.915   1.00 53.17  ? 175 SER A O   1 
ATOM   1324 C CB  . SER A 1 175 ? 30.439 25.932 7.637   1.00 55.86  ? 175 SER A CB  1 
ATOM   1325 O OG  . SER A 1 175 ? 31.545 25.142 7.237   1.00 55.90  ? 175 SER A OG  1 
ATOM   1326 N N   . ILE A 1 176 ? 29.242 24.274 4.854   1.00 47.95  ? 176 ILE A N   1 
ATOM   1327 C CA  . ILE A 1 176 ? 29.316 24.182 3.402   1.00 45.76  ? 176 ILE A CA  1 
ATOM   1328 C C   . ILE A 1 176 ? 27.897 24.166 2.849   1.00 43.85  ? 176 ILE A C   1 
ATOM   1329 O O   . ILE A 1 176 ? 27.123 23.246 3.132   1.00 41.10  ? 176 ILE A O   1 
ATOM   1330 C CB  . ILE A 1 176 ? 30.089 22.929 2.966   1.00 43.87  ? 176 ILE A CB  1 
ATOM   1331 C CG1 . ILE A 1 176 ? 31.483 22.913 3.600   1.00 43.30  ? 176 ILE A CG1 1 
ATOM   1332 C CG2 . ILE A 1 176 ? 30.178 22.859 1.449   1.00 44.45  ? 176 ILE A CG2 1 
ATOM   1333 C CD1 . ILE A 1 176 ? 32.270 21.656 3.306   1.00 41.49  ? 176 ILE A CD1 1 
ATOM   1334 N N   . GLU A 1 177 ? 27.553 25.185 2.064   1.00 45.27  ? 177 GLU A N   1 
ATOM   1335 C CA  . GLU A 1 177 ? 26.238 25.264 1.430   1.00 44.82  ? 177 GLU A CA  1 
ATOM   1336 C C   . GLU A 1 177 ? 26.243 24.329 0.228   1.00 44.27  ? 177 GLU A C   1 
ATOM   1337 O O   . GLU A 1 177 ? 26.655 24.697 -0.874  1.00 45.92  ? 177 GLU A O   1 
ATOM   1338 C CB  . GLU A 1 177 ? 25.915 26.696 1.022   1.00 46.28  ? 177 GLU A CB  1 
ATOM   1339 C CG  . GLU A 1 177 ? 26.173 27.729 2.106   1.00 48.54  ? 177 GLU A CG  1 
ATOM   1340 C CD  . GLU A 1 177 ? 25.657 29.104 1.731   1.00 53.10  ? 177 GLU A CD  1 
ATOM   1341 O OE1 . GLU A 1 177 ? 24.482 29.402 2.034   0.71 54.94  ? 177 GLU A OE1 1 
ATOM   1342 O OE2 . GLU A 1 177 ? 26.423 29.883 1.126   0.79 56.01  ? 177 GLU A OE2 1 
ATOM   1343 N N   . ALA A 1 178 ? 25.778 23.101 0.439   1.00 42.35  ? 178 ALA A N   1 
ATOM   1344 C CA  . ALA A 1 178 ? 25.834 22.079 -0.597  1.00 40.34  ? 178 ALA A CA  1 
ATOM   1345 C C   . ALA A 1 178 ? 24.750 21.040 -0.335  1.00 40.23  ? 178 ALA A C   1 
ATOM   1346 O O   . ALA A 1 178 ? 23.998 21.123 0.640   1.00 40.29  ? 178 ALA A O   1 
ATOM   1347 C CB  . ALA A 1 178 ? 27.221 21.432 -0.656  1.00 38.13  ? 178 ALA A CB  1 
ATOM   1348 N N   . MET A 1 179 ? 24.676 20.056 -1.230  1.00 39.78  ? 179 MET A N   1 
ATOM   1349 C CA  . MET A 1 179 ? 23.771 18.925 -1.095  1.00 38.78  ? 179 MET A CA  1 
ATOM   1350 C C   . MET A 1 179 ? 24.445 17.706 -1.707  1.00 38.05  ? 179 MET A C   1 
ATOM   1351 O O   . MET A 1 179 ? 25.197 17.821 -2.679  1.00 38.83  ? 179 MET A O   1 
ATOM   1352 C CB  . MET A 1 179 ? 22.420 19.190 -1.771  1.00 39.17  ? 179 MET A CB  1 
ATOM   1353 C CG  . MET A 1 179 ? 22.517 19.492 -3.258  1.00 39.15  ? 179 MET A CG  1 
ATOM   1354 S SD  . MET A 1 179 ? 20.908 19.610 -4.063  1.00 39.80  ? 179 MET A SD  1 
ATOM   1355 C CE  . MET A 1 179 ? 21.401 19.921 -5.757  1.00 40.47  ? 179 MET A CE  1 
ATOM   1356 N N   . GLN A 1 180 ? 24.175 16.537 -1.130  1.00 37.33  ? 180 GLN A N   1 
ATOM   1357 C CA  . GLN A 1 180 ? 24.842 15.303 -1.525  1.00 38.16  ? 180 GLN A CA  1 
ATOM   1358 C C   . GLN A 1 180 ? 23.817 14.269 -1.966  1.00 37.54  ? 180 GLN A C   1 
ATOM   1359 O O   . GLN A 1 180 ? 22.805 14.063 -1.287  1.00 38.31  ? 180 GLN A O   1 
ATOM   1360 C CB  . GLN A 1 180 ? 25.695 14.749 -0.380  1.00 40.05  ? 180 GLN A CB  1 
ATOM   1361 C CG  . GLN A 1 180 ? 26.532 13.541 -0.765  1.00 42.91  ? 180 GLN A CG  1 
ATOM   1362 C CD  . GLN A 1 180 ? 27.473 13.109 0.340   1.00 46.46  ? 180 GLN A CD  1 
ATOM   1363 O OE1 . GLN A 1 180 ? 28.208 12.131 0.199   1.00 46.84  ? 180 GLN A OE1 1 
ATOM   1364 N NE2 . GLN A 1 180 ? 27.457 13.839 1.449   1.00 50.19  ? 180 GLN A NE2 1 
ATOM   1365 N N   . LEU A 1 181 ? 24.090 13.616 -3.093  1.00 36.94  ? 181 LEU A N   1 
ATOM   1366 C CA  . LEU A 1 181 ? 23.225 12.590 -3.660  1.00 36.05  ? 181 LEU A CA  1 
ATOM   1367 C C   . LEU A 1 181 ? 23.916 11.236 -3.567  1.00 35.06  ? 181 LEU A C   1 
ATOM   1368 O O   . LEU A 1 181 ? 25.095 11.113 -3.914  1.00 34.84  ? 181 LEU A O   1 
ATOM   1369 C CB  . LEU A 1 181 ? 22.885 12.909 -5.118  1.00 36.34  ? 181 LEU A CB  1 
ATOM   1370 C CG  . LEU A 1 181 ? 22.048 11.881 -5.884  1.00 36.21  ? 181 LEU A CG  1 
ATOM   1371 C CD1 . LEU A 1 181 ? 20.586 11.949 -5.468  1.00 35.62  ? 181 LEU A CD1 1 
ATOM   1372 C CD2 . LEU A 1 181 ? 22.199 12.072 -7.387  1.00 36.59  ? 181 LEU A CD2 1 
ATOM   1373 N N   . THR A 1 182 ? 23.181 10.225 -3.106  1.00 34.44  ? 182 THR A N   1 
ATOM   1374 C CA  . THR A 1 182 ? 23.712 8.878  -2.955  1.00 34.57  ? 182 THR A CA  1 
ATOM   1375 C C   . THR A 1 182 ? 22.789 7.878  -3.639  1.00 35.50  ? 182 THR A C   1 
ATOM   1376 O O   . THR A 1 182 ? 21.639 8.182  -3.964  1.00 35.91  ? 182 THR A O   1 
ATOM   1377 C CB  . THR A 1 182 ? 23.894 8.503  -1.476  1.00 34.61  ? 182 THR A CB  1 
ATOM   1378 O OG1 . THR A 1 182 ? 22.701 8.820  -0.749  1.00 36.24  ? 182 THR A OG1 1 
ATOM   1379 C CG2 . THR A 1 182 ? 25.067 9.260  -0.875  1.00 33.33  ? 182 THR A CG2 1 
ATOM   1380 N N   . GLU A 1 183 ? 23.311 6.672  -3.852  1.00 36.51  ? 183 GLU A N   1 
ATOM   1381 C CA  . GLU A 1 183 ? 22.605 5.614  -4.559  1.00 37.50  ? 183 GLU A CA  1 
ATOM   1382 C C   . GLU A 1 183 ? 22.121 4.545  -3.587  1.00 38.59  ? 183 GLU A C   1 
ATOM   1383 O O   . GLU A 1 183 ? 22.713 4.332  -2.524  1.00 38.68  ? 183 GLU A O   1 
ATOM   1384 C CB  . GLU A 1 183 ? 23.500 4.969  -5.622  1.00 38.07  ? 183 GLU A CB  1 
ATOM   1385 C CG  . GLU A 1 183 ? 24.007 5.932  -6.682  1.00 39.27  ? 183 GLU A CG  1 
ATOM   1386 C CD  . GLU A 1 183 ? 24.834 5.239  -7.749  1.00 41.48  ? 183 GLU A CD  1 
ATOM   1387 O OE1 . GLU A 1 183 ? 25.191 4.058  -7.552  1.00 43.46  ? 183 GLU A OE1 1 
ATOM   1388 O OE2 . GLU A 1 183 ? 25.125 5.873  -8.786  1.00 41.28  ? 183 GLU A OE2 1 
ATOM   1389 N N   . MET A 1 184 ? 21.041 3.866  -3.968  1.00 38.98  ? 184 MET A N   1 
ATOM   1390 C CA  . MET A 1 184 ? 20.459 2.778  -3.184  1.00 39.30  ? 184 MET A CA  1 
ATOM   1391 C C   . MET A 1 184 ? 20.495 1.507  -4.026  1.00 40.56  ? 184 MET A C   1 
ATOM   1392 O O   . MET A 1 184 ? 19.612 1.290  -4.862  1.00 42.74  ? 184 MET A O   1 
ATOM   1393 C CB  . MET A 1 184 ? 19.031 3.102  -2.757  1.00 39.71  ? 184 MET A CB  1 
ATOM   1394 C CG  . MET A 1 184 ? 18.883 4.325  -1.879  1.00 39.85  ? 184 MET A CG  1 
ATOM   1395 S SD  . MET A 1 184 ? 17.166 4.540  -1.366  1.00 42.59  ? 184 MET A SD  1 
ATOM   1396 C CE  . MET A 1 184 ? 17.266 6.088  -0.474  1.00 42.46  ? 184 MET A CE  1 
ATOM   1397 N N   . ALA A 1 185 ? 21.510 0.674  -3.799  1.00 40.06  ? 185 ALA A N   1 
ATOM   1398 C CA  . ALA A 1 185 ? 21.639 -0.631 -4.447  1.00 41.74  ? 185 ALA A CA  1 
ATOM   1399 C C   . ALA A 1 185 ? 21.475 -0.519 -5.964  1.00 42.62  ? 185 ALA A C   1 
ATOM   1400 O O   . ALA A 1 185 ? 20.577 -1.109 -6.566  1.00 44.67  ? 185 ALA A O   1 
ATOM   1401 C CB  . ALA A 1 185 ? 20.635 -1.628 -3.861  1.00 42.92  ? 185 ALA A CB  1 
ATOM   1402 N N   . SER A 1 186 ? 22.362 0.258  -6.578  1.00 39.97  ? 186 SER A N   1 
ATOM   1403 C CA  A SER A 1 186 ? 22.280 0.476  -8.015  0.71 40.05  ? 186 SER A CA  1 
ATOM   1404 C CA  B SER A 1 186 ? 22.282 0.474  -8.015  0.29 40.80  ? 186 SER A CA  1 
ATOM   1405 C C   . SER A 1 186 ? 22.730 -0.760 -8.779  1.00 42.65  ? 186 SER A C   1 
ATOM   1406 O O   . SER A 1 186 ? 23.510 -1.582 -8.287  1.00 44.67  ? 186 SER A O   1 
ATOM   1407 C CB  A SER A 1 186 ? 23.124 1.684  -8.426  0.71 38.02  ? 186 SER A CB  1 
ATOM   1408 C CB  B SER A 1 186 ? 23.132 1.672  -8.429  0.29 37.93  ? 186 SER A CB  1 
ATOM   1409 O OG  A SER A 1 186 ? 24.509 1.425  -8.277  0.71 38.30  ? 186 SER A OG  1 
ATOM   1410 O OG  B SER A 1 186 ? 23.086 1.845  -9.834  0.29 38.91  ? 186 SER A OG  1 
ATOM   1411 N N   . ILE A 1 187 ? 22.229 -0.888 -10.004 1.00 45.40  ? 187 ILE A N   1 
ATOM   1412 C CA  . ILE A 1 187 ? 22.567 -1.987 -10.898 1.00 48.76  ? 187 ILE A CA  1 
ATOM   1413 C C   . ILE A 1 187 ? 23.656 -1.507 -11.843 1.00 50.47  ? 187 ILE A C   1 
ATOM   1414 O O   . ILE A 1 187 ? 23.545 -0.421 -12.425 1.00 49.22  ? 187 ILE A O   1 
ATOM   1415 C CB  . ILE A 1 187 ? 21.337 -2.472 -11.683 1.00 49.87  ? 187 ILE A CB  1 
ATOM   1416 C CG1 . ILE A 1 187 ? 20.215 -2.863 -10.717 1.00 50.09  ? 187 ILE A CG1 1 
ATOM   1417 C CG2 . ILE A 1 187 ? 21.705 -3.640 -12.585 1.00 51.70  ? 187 ILE A CG2 1 
ATOM   1418 C CD1 . ILE A 1 187 ? 18.867 -3.011 -11.375 0.75 51.21  ? 187 ILE A CD1 1 
ATOM   1419 N N   . ASN A 1 188 ? 24.712 -2.303 -11.992 1.00 54.44  ? 188 ASN A N   1 
ATOM   1420 C CA  . ASN A 1 188 ? 25.820 -1.955 -12.877 1.00 57.14  ? 188 ASN A CA  1 
ATOM   1421 C C   . ASN A 1 188 ? 26.291 -3.215 -13.583 1.00 62.62  ? 188 ASN A C   1 
ATOM   1422 O O   . ASN A 1 188 ? 26.877 -4.099 -12.951 1.00 63.53  ? 188 ASN A O   1 
ATOM   1423 C CB  . ASN A 1 188 ? 26.969 -1.307 -12.109 1.00 54.92  ? 188 ASN A CB  1 
ATOM   1424 C CG  . ASN A 1 188 ? 26.793 0.186  -11.955 1.00 51.83  ? 188 ASN A CG  1 
ATOM   1425 O OD1 . ASN A 1 188 ? 27.234 0.964  -12.801 1.00 52.48  ? 188 ASN A OD1 1 
ATOM   1426 N ND2 . ASN A 1 188 ? 26.151 0.597  -10.868 1.00 48.79  ? 188 ASN A ND2 1 
ATOM   1427 N N   . ASN A 1 189 ? 26.043 -3.289 -14.889 1.00 67.28  ? 189 ASN A N   1 
ATOM   1428 C CA  . ASN A 1 189 ? 26.545 -4.382 -15.710 1.00 73.11  ? 189 ASN A CA  1 
ATOM   1429 C C   . ASN A 1 189 ? 27.000 -3.847 -17.062 0.25 77.35  ? 189 ASN A C   1 
ATOM   1430 O O   . ASN A 1 189 ? 27.545 -2.741 -17.147 0.57 75.83  ? 189 ASN A O   1 
ATOM   1431 C CB  . ASN A 1 189 ? 25.478 -5.467 -15.878 1.00 74.58  ? 189 ASN A CB  1 
ATOM   1432 C CG  . ASN A 1 189 ? 24.126 -4.905 -16.276 1.00 73.46  ? 189 ASN A CG  1 
ATOM   1433 O OD1 . ASN A 1 189 ? 24.038 -3.925 -17.015 1.00 72.97  ? 189 ASN A OD1 1 
ATOM   1434 N ND2 . ASN A 1 189 ? 23.062 -5.525 -15.781 1.00 73.57  ? 189 ASN A ND2 1 
ATOM   1435 N N   . ARG A 1 190 ? 26.779 -4.621 -18.125 1.00 84.30  ? 190 ARG A N   1 
ATOM   1436 C CA  . ARG A 1 190 ? 27.192 -4.176 -19.451 1.00 86.25  ? 190 ARG A CA  1 
ATOM   1437 C C   . ARG A 1 190 ? 26.257 -3.109 -20.006 1.00 85.76  ? 190 ARG A C   1 
ATOM   1438 O O   . ARG A 1 190 ? 26.698 -2.229 -20.756 1.00 86.30  ? 190 ARG A O   1 
ATOM   1439 C CB  . ARG A 1 190 ? 27.257 -5.363 -20.412 1.00 89.40  ? 190 ARG A CB  1 
ATOM   1440 C CG  . ARG A 1 190 ? 27.945 -5.053 -21.734 1.00 90.53  ? 190 ARG A CG  1 
ATOM   1441 C CD  . ARG A 1 190 ? 27.408 -5.918 -22.867 0.60 92.86  ? 190 ARG A CD  1 
ATOM   1442 N NE  . ARG A 1 190 ? 27.486 -7.347 -22.576 0.40 95.04  ? 190 ARG A NE  1 
ATOM   1443 C CZ  . ARG A 1 190 ? 26.446 -8.094 -22.216 0.40 97.02  ? 190 ARG A CZ  1 
ATOM   1444 N NH1 . ARG A 1 190 ? 26.609 -9.387 -21.971 0.40 100.43 ? 190 ARG A NH1 1 
ATOM   1445 N NH2 . ARG A 1 190 ? 25.244 -7.547 -22.100 0.40 96.03  ? 190 ARG A NH2 1 
ATOM   1446 N N   . VAL A 1 191 ? 24.975 -3.157 -19.647 1.00 84.18  ? 191 VAL A N   1 
ATOM   1447 C CA  . VAL A 1 191 ? 23.976 -2.317 -20.298 1.00 83.22  ? 191 VAL A CA  1 
ATOM   1448 C C   . VAL A 1 191 ? 23.565 -1.163 -19.389 1.00 78.24  ? 191 VAL A C   1 
ATOM   1449 O O   . VAL A 1 191 ? 23.220 -0.077 -19.869 1.00 76.59  ? 191 VAL A O   1 
ATOM   1450 C CB  . VAL A 1 191 ? 22.761 -3.160 -20.740 1.00 85.86  ? 191 VAL A CB  1 
ATOM   1451 C CG1 . VAL A 1 191 ? 23.094 -4.650 -20.664 1.00 88.34  ? 191 VAL A CG1 1 
ATOM   1452 C CG2 . VAL A 1 191 ? 21.523 -2.836 -19.916 1.00 84.05  ? 191 VAL A CG2 1 
ATOM   1453 N N   . TYR A 1 192 ? 23.613 -1.375 -18.077 1.00 75.59  ? 192 TYR A N   1 
ATOM   1454 C CA  . TYR A 1 192 ? 23.272 -0.348 -17.100 1.00 71.23  ? 192 TYR A CA  1 
ATOM   1455 C C   . TYR A 1 192 ? 24.538 0.095  -16.378 1.00 66.24  ? 192 TYR A C   1 
ATOM   1456 O O   . TYR A 1 192 ? 25.265 -0.737 -15.827 1.00 66.27  ? 192 TYR A O   1 
ATOM   1457 C CB  . TYR A 1 192 ? 22.234 -0.860 -16.096 1.00 72.14  ? 192 TYR A CB  1 
ATOM   1458 C CG  . TYR A 1 192 ? 20.800 -0.620 -16.518 1.00 74.03  ? 192 TYR A CG  1 
ATOM   1459 C CD1 . TYR A 1 192 ? 20.230 0.642  -16.411 1.00 73.58  ? 192 TYR A CD1 1 
ATOM   1460 C CD2 . TYR A 1 192 ? 20.013 -1.654 -17.012 1.00 76.85  ? 192 TYR A CD2 1 
ATOM   1461 C CE1 . TYR A 1 192 ? 18.922 0.870  -16.792 1.00 74.69  ? 192 TYR A CE1 1 
ATOM   1462 C CE2 . TYR A 1 192 ? 18.703 -1.435 -17.397 1.00 78.25  ? 192 TYR A CE2 1 
ATOM   1463 C CZ  . TYR A 1 192 ? 18.163 -0.170 -17.283 1.00 76.96  ? 192 TYR A CZ  1 
ATOM   1464 O OH  . TYR A 1 192 ? 16.861 0.056  -17.662 1.00 78.10  ? 192 TYR A OH  1 
ATOM   1465 N N   . ARG A 1 193 ? 24.800 1.401  -16.388 1.00 62.04  ? 193 ARG A N   1 
ATOM   1466 C CA  . ARG A 1 193 ? 26.006 1.961  -15.787 1.00 59.81  ? 193 ARG A CA  1 
ATOM   1467 C C   . ARG A 1 193 ? 25.648 3.251  -15.067 1.00 56.37  ? 193 ARG A C   1 
ATOM   1468 O O   . ARG A 1 193 ? 25.100 4.173  -15.679 1.00 57.72  ? 193 ARG A O   1 
ATOM   1469 C CB  . ARG A 1 193 ? 27.085 2.222  -16.845 1.00 62.08  ? 193 ARG A CB  1 
ATOM   1470 C CG  . ARG A 1 193 ? 28.189 1.174  -16.890 0.80 65.81  ? 193 ARG A CG  1 
ATOM   1471 C CD  . ARG A 1 193 ? 28.987 1.265  -18.184 0.70 69.38  ? 193 ARG A CD  1 
ATOM   1472 N NE  . ARG A 1 193 ? 29.759 2.501  -18.289 0.70 69.43  ? 193 ARG A NE  1 
ATOM   1473 C CZ  . ARG A 1 193 ? 31.087 2.558  -18.276 0.60 70.25  ? 193 ARG A CZ  1 
ATOM   1474 N NH1 . ARG A 1 193 ? 31.703 3.728  -18.379 0.60 70.35  ? 193 ARG A NH1 1 
ATOM   1475 N NH2 . ARG A 1 193 ? 31.801 1.447  -18.171 0.60 71.77  ? 193 ARG A NH2 1 
ATOM   1476 N N   . THR A 1 194 ? 25.957 3.311  -13.775 1.00 52.07  ? 194 THR A N   1 
ATOM   1477 C CA  . THR A 1 194 ? 25.808 4.516  -12.974 1.00 48.31  ? 194 THR A CA  1 
ATOM   1478 C C   . THR A 1 194 ? 27.173 4.940  -12.448 1.00 47.10  ? 194 THR A C   1 
ATOM   1479 O O   . THR A 1 194 ? 28.174 4.236  -12.611 1.00 48.87  ? 194 THR A O   1 
ATOM   1480 C CB  . THR A 1 194 ? 24.829 4.303  -11.812 1.00 47.05  ? 194 THR A CB  1 
ATOM   1481 O OG1 . THR A 1 194 ? 25.332 3.284  -10.938 1.00 47.68  ? 194 THR A OG1 1 
ATOM   1482 C CG2 . THR A 1 194 ? 23.463 3.889  -12.336 1.00 47.50  ? 194 THR A CG2 1 
ATOM   1483 N N   . ILE A 1 195 ? 27.211 6.110  -11.809 1.00 44.97  ? 195 ILE A N   1 
ATOM   1484 C CA  . ILE A 1 195 ? 28.490 6.639  -11.349 1.00 44.58  ? 195 ILE A CA  1 
ATOM   1485 C C   . ILE A 1 195 ? 28.973 5.906  -10.097 1.00 45.16  ? 195 ILE A C   1 
ATOM   1486 O O   . ILE A 1 195 ? 30.184 5.756  -9.893  1.00 45.83  ? 195 ILE A O   1 
ATOM   1487 C CB  . ILE A 1 195 ? 28.393 8.162  -11.132 1.00 43.06  ? 195 ILE A CB  1 
ATOM   1488 C CG1 . ILE A 1 195 ? 29.771 8.753  -10.817 1.00 43.56  ? 195 ILE A CG1 1 
ATOM   1489 C CG2 . ILE A 1 195 ? 27.385 8.506  -10.039 1.00 41.00  ? 195 ILE A CG2 1 
ATOM   1490 C CD1 . ILE A 1 195 ? 30.767 8.605  -11.945 1.00 45.12  ? 195 ILE A CD1 1 
ATOM   1491 N N   A GLY A 1 196 ? 28.053 5.423  -9.263  0.57 45.47  ? 196 GLY A N   1 
ATOM   1492 N N   B GLY A 1 196 ? 28.061 5.449  -9.243  0.43 45.45  ? 196 GLY A N   1 
ATOM   1493 C CA  A GLY A 1 196 ? 28.410 4.709  -8.055  0.57 45.28  ? 196 GLY A CA  1 
ATOM   1494 C CA  B GLY A 1 196 ? 28.438 4.678  -8.074  0.43 45.35  ? 196 GLY A CA  1 
ATOM   1495 C C   A GLY A 1 196 ? 28.785 5.621  -6.906  0.57 44.02  ? 196 GLY A C   1 
ATOM   1496 C C   B GLY A 1 196 ? 28.945 5.497  -6.904  0.43 44.20  ? 196 GLY A C   1 
ATOM   1497 O O   A GLY A 1 196 ? 28.337 5.426  -5.772  0.57 43.70  ? 196 GLY A O   1 
ATOM   1498 O O   B GLY A 1 196 ? 28.758 5.113  -5.745  0.43 44.53  ? 196 GLY A O   1 
ATOM   1499 N N   . SER A 1 197 ? 29.600 6.630  -7.193  1.00 43.86  ? 197 SER A N   1 
ATOM   1500 C CA  . SER A 1 197 ? 30.112 7.514  -6.161  1.00 41.67  ? 197 SER A CA  1 
ATOM   1501 C C   . SER A 1 197 ? 29.054 8.528  -5.739  1.00 38.18  ? 197 SER A C   1 
ATOM   1502 O O   . SER A 1 197 ? 28.174 8.886  -6.528  1.00 36.77  ? 197 SER A O   1 
ATOM   1503 C CB  . SER A 1 197 ? 31.350 8.252  -6.660  1.00 41.37  ? 197 SER A CB  1 
ATOM   1504 O OG  . SER A 1 197 ? 32.404 7.346  -6.928  1.00 42.41  ? 197 SER A OG  1 
ATOM   1505 N N   . PRO A 1 198 ? 29.112 8.986  -4.492  1.00 35.13  ? 198 PRO A N   1 
ATOM   1506 C CA  . PRO A 1 198 ? 28.258 10.103 -4.081  1.00 33.33  ? 198 PRO A CA  1 
ATOM   1507 C C   . PRO A 1 198 ? 28.686 11.387 -4.769  1.00 32.38  ? 198 PRO A C   1 
ATOM   1508 O O   . PRO A 1 198 ? 29.861 11.594 -5.076  1.00 32.74  ? 198 PRO A O   1 
ATOM   1509 C CB  . PRO A 1 198 ? 28.476 10.184 -2.563  1.00 33.42  ? 198 PRO A CB  1 
ATOM   1510 C CG  . PRO A 1 198 ? 29.052 8.852  -2.180  1.00 33.96  ? 198 PRO A CG  1 
ATOM   1511 C CD  . PRO A 1 198 ? 29.857 8.414  -3.360  1.00 34.96  ? 198 PRO A CD  1 
ATOM   1512 N N   . LEU A 1 199 ? 27.711 12.257 -5.013  1.00 32.01  ? 199 LEU A N   1 
ATOM   1513 C CA  . LEU A 1 199 ? 27.934 13.519 -5.705  1.00 32.99  ? 199 LEU A CA  1 
ATOM   1514 C C   . LEU A 1 199 ? 27.559 14.668 -4.782  1.00 33.97  ? 199 LEU A C   1 
ATOM   1515 O O   . LEU A 1 199 ? 26.507 14.633 -4.137  1.00 34.77  ? 199 LEU A O   1 
ATOM   1516 C CB  . LEU A 1 199 ? 27.119 13.587 -6.998  1.00 32.28  ? 199 LEU A CB  1 
ATOM   1517 C CG  . LEU A 1 199 ? 27.298 12.415 -7.968  1.00 31.59  ? 199 LEU A CG  1 
ATOM   1518 C CD1 . LEU A 1 199 ? 26.508 12.648 -9.246  1.00 32.26  ? 199 LEU A CD1 1 
ATOM   1519 C CD2 . LEU A 1 199 ? 28.769 12.184 -8.278  1.00 31.99  ? 199 LEU A CD2 1 
ATOM   1520 N N   . VAL A 1 200 ? 28.420 15.681 -4.719  1.00 34.19  ? 200 VAL A N   1 
ATOM   1521 C CA  . VAL A 1 200 ? 28.214 16.854 -3.875  1.00 33.94  ? 200 VAL A CA  1 
ATOM   1522 C C   . VAL A 1 200 ? 28.033 18.061 -4.785  1.00 34.86  ? 200 VAL A C   1 
ATOM   1523 O O   . VAL A 1 200 ? 28.943 18.418 -5.545  1.00 36.33  ? 200 VAL A O   1 
ATOM   1524 C CB  . VAL A 1 200 ? 29.384 17.063 -2.901  1.00 34.27  ? 200 VAL A CB  1 
ATOM   1525 C CG1 . VAL A 1 200 ? 29.140 18.287 -2.035  1.00 33.36  ? 200 VAL A CG1 1 
ATOM   1526 C CG2 . VAL A 1 200 ? 29.586 15.823 -2.038  1.00 34.63  ? 200 VAL A CG2 1 
ATOM   1527 N N   . PHE A 1 201 ? 26.857 18.694 -4.708  1.00 34.51  ? 201 PHE A N   1 
ATOM   1528 C CA  . PHE A 1 201 ? 26.523 19.813 -5.574  1.00 36.09  ? 201 PHE A CA  1 
ATOM   1529 C C   . PHE A 1 201 ? 26.540 21.126 -4.800  1.00 38.61  ? 201 PHE A C   1 
ATOM   1530 O O   . PHE A 1 201 ? 26.052 21.181 -3.667  1.00 39.05  ? 201 PHE A O   1 
ATOM   1531 C CB  . PHE A 1 201 ? 25.139 19.621 -6.207  1.00 35.08  ? 201 PHE A CB  1 
ATOM   1532 C CG  . PHE A 1 201 ? 24.980 18.318 -6.934  1.00 34.74  ? 201 PHE A CG  1 
ATOM   1533 C CD1 . PHE A 1 201 ? 25.336 18.207 -8.267  1.00 35.95  ? 201 PHE A CD1 1 
ATOM   1534 C CD2 . PHE A 1 201 ? 24.474 17.204 -6.285  1.00 34.12  ? 201 PHE A CD2 1 
ATOM   1535 C CE1 . PHE A 1 201 ? 25.191 17.011 -8.941  1.00 36.32  ? 201 PHE A CE1 1 
ATOM   1536 C CE2 . PHE A 1 201 ? 24.326 16.003 -6.954  1.00 35.00  ? 201 PHE A CE2 1 
ATOM   1537 C CZ  . PHE A 1 201 ? 24.685 15.906 -8.284  1.00 36.03  ? 201 PHE A CZ  1 
ATOM   1538 N N   . PRO A 1 202 ? 27.088 22.197 -5.380  1.00 41.06  ? 202 PRO A N   1 
ATOM   1539 C CA  . PRO A 1 202 ? 27.059 23.497 -4.698  1.00 42.76  ? 202 PRO A CA  1 
ATOM   1540 C C   . PRO A 1 202 ? 25.717 24.191 -4.877  1.00 44.22  ? 202 PRO A C   1 
ATOM   1541 O O   . PRO A 1 202 ? 24.775 23.600 -5.417  1.00 43.20  ? 202 PRO A O   1 
ATOM   1542 C CB  . PRO A 1 202 ? 28.190 24.268 -5.384  1.00 43.73  ? 202 PRO A CB  1 
ATOM   1543 C CG  . PRO A 1 202 ? 28.210 23.720 -6.769  1.00 43.66  ? 202 PRO A CG  1 
ATOM   1544 C CD  . PRO A 1 202 ? 27.832 22.254 -6.652  1.00 41.75  ? 202 PRO A CD  1 
ATOM   1545 N N   . LYS A 1 203 ? 25.619 25.443 -4.434  1.00 46.19  ? 203 LYS A N   1 
ATOM   1546 C CA  . LYS A 1 203 ? 24.400 26.206 -4.654  1.00 47.04  ? 203 LYS A CA  1 
ATOM   1547 C C   . LYS A 1 203 ? 24.174 26.432 -6.144  1.00 47.64  ? 203 LYS A C   1 
ATOM   1548 O O   . LYS A 1 203 ? 25.107 26.398 -6.951  1.00 47.78  ? 203 LYS A O   1 
ATOM   1549 C CB  A LYS A 1 203 ? 24.468 27.552 -3.928  0.50 48.95  ? 203 LYS A CB  1 
ATOM   1550 C CB  B LYS A 1 203 ? 24.464 27.549 -3.924  0.50 48.94  ? 203 LYS A CB  1 
ATOM   1551 C CG  A LYS A 1 203 ? 23.564 27.655 -2.709  0.50 48.51  ? 203 LYS A CG  1 
ATOM   1552 C CG  B LYS A 1 203 ? 24.586 27.444 -2.414  0.50 47.90  ? 203 LYS A CG  1 
ATOM   1553 C CD  A LYS A 1 203 ? 23.484 29.089 -2.207  0.50 50.88  ? 203 LYS A CD  1 
ATOM   1554 C CD  B LYS A 1 203 ? 24.544 28.820 -1.765  0.50 50.33  ? 203 LYS A CD  1 
ATOM   1555 C CE  A LYS A 1 203 ? 22.459 29.227 -1.092  0.50 50.74  ? 203 LYS A CE  1 
ATOM   1556 C CE  B LYS A 1 203 ? 25.637 29.725 -2.315  0.50 52.75  ? 203 LYS A CE  1 
ATOM   1557 N NZ  A LYS A 1 203 ? 22.302 30.641 -0.651  0.50 53.54  ? 203 LYS A NZ  1 
ATOM   1558 N NZ  B LYS A 1 203 ? 25.558 31.100 -1.750  0.50 55.73  ? 203 LYS A NZ  1 
ATOM   1559 N N   . HIS A 1 204 ? 22.910 26.652 -6.503  1.00 49.08  ? 204 HIS A N   1 
ATOM   1560 C CA  . HIS A 1 204 ? 22.442 26.969 -7.850  1.00 50.67  ? 204 HIS A CA  1 
ATOM   1561 C C   . HIS A 1 204 ? 22.615 25.816 -8.833  1.00 48.30  ? 204 HIS A C   1 
ATOM   1562 O O   . HIS A 1 204 ? 22.314 25.986 -10.021 1.00 51.52  ? 204 HIS A O   1 
ATOM   1563 C CB  . HIS A 1 204 ? 23.121 28.223 -8.422  1.00 54.08  ? 204 HIS A CB  1 
ATOM   1564 C CG  . HIS A 1 204 ? 23.106 29.391 -7.486  1.00 56.48  ? 204 HIS A CG  1 
ATOM   1565 N ND1 . HIS A 1 204 ? 24.203 29.758 -6.736  1.00 57.04  ? 204 HIS A ND1 1 
ATOM   1566 C CD2 . HIS A 1 204 ? 22.123 30.266 -7.168  1.00 58.41  ? 204 HIS A CD2 1 
ATOM   1567 C CE1 . HIS A 1 204 ? 23.898 30.814 -6.003  1.00 58.68  ? 204 HIS A CE1 1 
ATOM   1568 N NE2 . HIS A 1 204 ? 22.642 31.142 -6.246  1.00 59.49  ? 204 HIS A NE2 1 
ATOM   1569 N N   . HIS A 1 205 ? 23.088 24.655 -8.390  1.00 43.21  ? 205 HIS A N   1 
ATOM   1570 C CA  . HIS A 1 205 ? 23.100 23.458 -9.221  1.00 39.97  ? 205 HIS A CA  1 
ATOM   1571 C C   . HIS A 1 205 ? 21.778 22.722 -9.051  1.00 39.38  ? 205 HIS A C   1 
ATOM   1572 O O   . HIS A 1 205 ? 21.373 22.410 -7.927  1.00 39.11  ? 205 HIS A O   1 
ATOM   1573 C CB  . HIS A 1 205 ? 24.269 22.543 -8.854  1.00 37.34  ? 205 HIS A CB  1 
ATOM   1574 C CG  . HIS A 1 205 ? 25.569 22.939 -9.482  1.00 38.79  ? 205 HIS A CG  1 
ATOM   1575 N ND1 . HIS A 1 205 ? 26.497 22.016 -9.914  1.00 38.73  ? 205 HIS A ND1 1 
ATOM   1576 C CD2 . HIS A 1 205 ? 26.096 24.157 -9.752  1.00 41.52  ? 205 HIS A CD2 1 
ATOM   1577 C CE1 . HIS A 1 205 ? 27.540 22.648 -10.423 1.00 40.41  ? 205 HIS A CE1 1 
ATOM   1578 N NE2 . HIS A 1 205 ? 27.321 23.948 -10.337 1.00 42.11  ? 205 HIS A NE2 1 
ATOM   1579 N N   . VAL A 1 206 ? 21.106 22.452 -10.166 1.00 39.95  ? 206 VAL A N   1 
ATOM   1580 C CA  . VAL A 1 206 ? 19.782 21.840 -10.164 1.00 39.78  ? 206 VAL A CA  1 
ATOM   1581 C C   . VAL A 1 206 ? 19.913 20.403 -10.648 1.00 39.02  ? 206 VAL A C   1 
ATOM   1582 O O   . VAL A 1 206 ? 20.298 20.159 -11.798 1.00 39.45  ? 206 VAL A O   1 
ATOM   1583 C CB  . VAL A 1 206 ? 18.793 22.627 -11.037 1.00 41.48  ? 206 VAL A CB  1 
ATOM   1584 C CG1 . VAL A 1 206 ? 17.447 21.924 -11.075 1.00 41.53  ? 206 VAL A CG1 1 
ATOM   1585 C CG2 . VAL A 1 206 ? 18.643 24.048 -10.516 1.00 42.90  ? 206 VAL A CG2 1 
ATOM   1586 N N   . VAL A 1 207 ? 19.595 19.456 -9.771  1.00 37.90  ? 207 VAL A N   1 
ATOM   1587 C CA  . VAL A 1 207 ? 19.545 18.040 -10.115 1.00 36.92  ? 207 VAL A CA  1 
ATOM   1588 C C   . VAL A 1 207 ? 18.090 17.663 -10.347 1.00 37.79  ? 207 VAL A C   1 
ATOM   1589 O O   . VAL A 1 207 ? 17.238 17.879 -9.475  1.00 37.27  ? 207 VAL A O   1 
ATOM   1590 C CB  . VAL A 1 207 ? 20.174 17.173 -9.011  1.00 35.16  ? 207 VAL A CB  1 
ATOM   1591 C CG1 . VAL A 1 207 ? 20.133 15.705 -9.402  1.00 33.78  ? 207 VAL A CG1 1 
ATOM   1592 C CG2 . VAL A 1 207 ? 21.601 17.619 -8.741  1.00 35.65  ? 207 VAL A CG2 1 
ATOM   1593 N N   . SER A 1 208 ? 17.802 17.104 -11.520 1.00 39.48  ? 208 SER A N   1 
ATOM   1594 C CA  . SER A 1 208 ? 16.436 16.822 -11.945 1.00 41.97  ? 208 SER A CA  1 
ATOM   1595 C C   . SER A 1 208 ? 16.295 15.340 -12.259 1.00 40.20  ? 208 SER A C   1 
ATOM   1596 O O   . SER A 1 208 ? 17.030 14.808 -13.098 1.00 39.43  ? 208 SER A O   1 
ATOM   1597 C CB  . SER A 1 208 ? 16.064 17.668 -13.163 1.00 45.85  ? 208 SER A CB  1 
ATOM   1598 O OG  . SER A 1 208 ? 14.785 17.316 -13.656 1.00 47.89  ? 208 SER A OG  1 
ATOM   1599 N N   . LEU A 1 209 ? 15.353 14.682 -11.590 1.00 40.38  ? 209 LEU A N   1 
ATOM   1600 C CA  . LEU A 1 209 ? 15.014 13.294 -11.866 1.00 41.79  ? 209 LEU A CA  1 
ATOM   1601 C C   . LEU A 1 209 ? 13.773 13.241 -12.747 1.00 46.09  ? 209 LEU A C   1 
ATOM   1602 O O   . LEU A 1 209 ? 12.800 13.964 -12.510 1.00 48.18  ? 209 LEU A O   1 
ATOM   1603 C CB  . LEU A 1 209 ? 14.766 12.517 -10.571 1.00 40.27  ? 209 LEU A CB  1 
ATOM   1604 C CG  . LEU A 1 209 ? 15.843 12.580 -9.486  1.00 38.19  ? 209 LEU A CG  1 
ATOM   1605 C CD1 . LEU A 1 209 ? 15.483 11.660 -8.329  1.00 37.13  ? 209 LEU A CD1 1 
ATOM   1606 C CD2 . LEU A 1 209 ? 17.208 12.226 -10.054 1.00 38.12  ? 209 LEU A CD2 1 
ATOM   1607 N N   . GLN A 1 210 ? 13.812 12.386 -13.767 1.00 47.38  ? 210 GLN A N   1 
ATOM   1608 C CA  . GLN A 1 210 ? 12.718 12.284 -14.716 1.00 49.77  ? 210 GLN A CA  1 
ATOM   1609 C C   . GLN A 1 210 ? 12.375 10.820 -14.969 1.00 50.73  ? 210 GLN A C   1 
ATOM   1610 O O   . GLN A 1 210 ? 13.274 9.991  -15.146 1.00 50.09  ? 210 GLN A O   1 
ATOM   1611 C CB  . GLN A 1 210 ? 13.077 12.976 -16.039 1.00 50.58  ? 210 GLN A CB  1 
ATOM   1612 C CG  . GLN A 1 210 ? 13.339 14.467 -15.894 1.00 51.35  ? 210 GLN A CG  1 
ATOM   1613 C CD  . GLN A 1 210 ? 13.933 15.086 -17.144 1.00 54.25  ? 210 GLN A CD  1 
ATOM   1614 O OE1 . GLN A 1 210 ? 13.944 14.473 -18.212 1.00 56.34  ? 210 GLN A OE1 1 
ATOM   1615 N NE2 . GLN A 1 210 ? 14.437 16.307 -17.014 1.00 54.85  ? 210 GLN A NE2 1 
ATOM   1616 N N   . PRO A 1 211 ? 11.090 10.478 -14.993 1.00 53.17  ? 211 PRO A N   1 
ATOM   1617 C CA  . PRO A 1 211 ? 10.704 9.072  -15.156 1.00 54.29  ? 211 PRO A CA  1 
ATOM   1618 C C   . PRO A 1 211 ? 10.960 8.573  -16.569 1.00 57.19  ? 211 PRO A C   1 
ATOM   1619 O O   . PRO A 1 211 ? 11.002 9.334  -17.538 1.00 58.04  ? 211 PRO A O   1 
ATOM   1620 C CB  . PRO A 1 211 ? 9.207  9.078  -14.834 1.00 55.86  ? 211 PRO A CB  1 
ATOM   1621 C CG  . PRO A 1 211 ? 8.764  10.456 -15.196 1.00 56.30  ? 211 PRO A CG  1 
ATOM   1622 C CD  . PRO A 1 211 ? 9.919  11.362 -14.863 1.00 54.74  ? 211 PRO A CD  1 
ATOM   1623 N N   . VAL A 1 212 ? 11.131 7.257  -16.670 1.00 59.47  ? 212 VAL A N   1 
ATOM   1624 C CA  . VAL A 1 212 ? 11.332 6.585  -17.942 1.00 64.15  ? 212 VAL A CA  1 
ATOM   1625 C C   . VAL A 1 212 ? 10.106 5.782  -18.352 1.00 69.10  ? 212 VAL A C   1 
ATOM   1626 O O   . VAL A 1 212 ? 9.702  5.810  -19.517 1.00 72.53  ? 212 VAL A O   1 
ATOM   1627 C CB  . VAL A 1 212 ? 12.590 5.690  -17.892 1.00 64.52  ? 212 VAL A CB  1 
ATOM   1628 C CG1 . VAL A 1 212 ? 12.840 5.036  -19.243 1.00 66.51  ? 212 VAL A CG1 1 
ATOM   1629 C CG2 . VAL A 1 212 ? 13.799 6.501  -17.451 1.00 63.36  ? 212 VAL A CG2 1 
ATOM   1630 N N   . ASN A 1 213 ? 9.497  5.063  -17.409 1.00 70.91  ? 213 ASN A N   1 
ATOM   1631 C CA  . ASN A 1 213 ? 8.277  4.312  -17.680 1.00 75.52  ? 213 ASN A CA  1 
ATOM   1632 C C   . ASN A 1 213 ? 7.223  4.597  -16.618 1.00 74.58  ? 213 ASN A C   1 
ATOM   1633 O O   . ASN A 1 213 ? 6.272  5.346  -16.864 1.00 76.74  ? 213 ASN A O   1 
ATOM   1634 C CB  . ASN A 1 213 ? 8.572  2.813  -17.752 1.00 79.73  ? 213 ASN A CB  1 
ATOM   1635 C CG  . ASN A 1 213 ? 8.670  2.308  -19.177 1.00 84.08  ? 213 ASN A CG  1 
ATOM   1636 O OD1 . ASN A 1 213 ? 9.674  2.521  -19.856 1.00 85.92  ? 213 ASN A OD1 1 
ATOM   1637 N ND2 . ASN A 1 213 ? 7.624  1.630  -19.637 0.54 87.30  ? 213 ASN A ND2 1 
ATOM   1638 N N   . ASP A 1 214 ? 7.384  4.004  -15.437 1.00 71.99  ? 214 ASP A N   1 
ATOM   1639 C CA  . ASP A 1 214 ? 6.446  4.239  -14.348 1.00 72.30  ? 214 ASP A CA  1 
ATOM   1640 C C   . ASP A 1 214 ? 6.577  5.674  -13.853 1.00 70.96  ? 214 ASP A C   1 
ATOM   1641 O O   . ASP A 1 214 ? 7.686  6.165  -13.623 1.00 69.57  ? 214 ASP A O   1 
ATOM   1642 C CB  . ASP A 1 214 ? 6.701  3.249  -13.211 1.00 71.81  ? 214 ASP A CB  1 
ATOM   1643 C CG  . ASP A 1 214 ? 5.524  3.130  -12.261 1.00 75.37  ? 214 ASP A CG  1 
ATOM   1644 O OD1 . ASP A 1 214 ? 4.967  4.173  -11.856 1.00 76.19  ? 214 ASP A OD1 1 
ATOM   1645 O OD2 . ASP A 1 214 ? 5.151  1.988  -11.921 1.00 78.05  ? 214 ASP A OD2 1 
ATOM   1646 N N   . LYS A 1 215 ? 5.440  6.349  -13.695 1.00 72.05  ? 215 LYS A N   1 
ATOM   1647 C CA  . LYS A 1 215 ? 5.411  7.751  -13.302 1.00 69.21  ? 215 LYS A CA  1 
ATOM   1648 C C   . LYS A 1 215 ? 4.929  7.949  -11.870 1.00 66.52  ? 215 LYS A C   1 
ATOM   1649 O O   . LYS A 1 215 ? 4.586  9.074  -11.491 1.00 66.28  ? 215 LYS A O   1 
ATOM   1650 C CB  . LYS A 1 215 ? 4.538  8.546  -14.275 1.00 71.52  ? 215 LYS A CB  1 
ATOM   1651 C CG  . LYS A 1 215 ? 4.683  8.094  -15.722 1.00 72.23  ? 215 LYS A CG  1 
ATOM   1652 C CD  . LYS A 1 215 ? 3.984  9.034  -16.691 1.00 73.68  ? 215 LYS A CD  1 
ATOM   1653 C CE  . LYS A 1 215 ? 4.799  10.295 -16.927 0.54 71.42  ? 215 LYS A CE  1 
ATOM   1654 N NZ  . LYS A 1 215 ? 4.227  11.124 -18.025 0.73 73.78  ? 215 LYS A NZ  1 
ATOM   1655 N N   . ASP A 1 216 ? 4.898  6.889  -11.068 1.00 64.54  ? 216 ASP A N   1 
ATOM   1656 C CA  . ASP A 1 216 ? 4.510  6.958  -9.666  1.00 63.54  ? 216 ASP A CA  1 
ATOM   1657 C C   . ASP A 1 216 ? 5.736  6.709  -8.799  1.00 60.60  ? 216 ASP A C   1 
ATOM   1658 O O   . ASP A 1 216 ? 6.511  5.784  -9.064  1.00 60.28  ? 216 ASP A O   1 
ATOM   1659 C CB  . ASP A 1 216 ? 3.415  5.938  -9.349  1.00 66.15  ? 216 ASP A CB  1 
ATOM   1660 C CG  . ASP A 1 216 ? 2.201  6.085  -10.247 1.00 70.07  ? 216 ASP A CG  1 
ATOM   1661 O OD1 . ASP A 1 216 ? 1.974  7.200  -10.763 1.00 70.71  ? 216 ASP A OD1 1 
ATOM   1662 O OD2 . ASP A 1 216 ? 1.471  5.090  -10.434 1.00 73.20  ? 216 ASP A OD2 1 
ATOM   1663 N N   . PHE A 1 217 ? 5.913  7.534  -7.768  1.00 58.61  ? 217 PHE A N   1 
ATOM   1664 C CA  . PHE A 1 217 ? 7.087  7.450  -6.913  1.00 54.90  ? 217 PHE A CA  1 
ATOM   1665 C C   . PHE A 1 217 ? 6.694  7.673  -5.461  1.00 53.91  ? 217 PHE A C   1 
ATOM   1666 O O   . PHE A 1 217 ? 5.766  8.427  -5.159  1.00 55.01  ? 217 PHE A O   1 
ATOM   1667 C CB  . PHE A 1 217 ? 8.155  8.478  -7.312  1.00 52.38  ? 217 PHE A CB  1 
ATOM   1668 C CG  . PHE A 1 217 ? 8.578  8.386  -8.747  1.00 52.05  ? 217 PHE A CG  1 
ATOM   1669 C CD1 . PHE A 1 217 ? 9.568  7.500  -9.136  1.00 51.25  ? 217 PHE A CD1 1 
ATOM   1670 C CD2 . PHE A 1 217 ? 7.990  9.191  -9.708  1.00 52.90  ? 217 PHE A CD2 1 
ATOM   1671 C CE1 . PHE A 1 217 ? 9.962  7.416  -10.458 1.00 51.48  ? 217 PHE A CE1 1 
ATOM   1672 C CE2 . PHE A 1 217 ? 8.379  9.112  -11.031 1.00 53.12  ? 217 PHE A CE2 1 
ATOM   1673 C CZ  . PHE A 1 217 ? 9.366  8.224  -11.406 1.00 52.27  ? 217 PHE A CZ  1 
ATOM   1674 N N   . GLN A 1 218 ? 7.419  7.008  -4.564  1.00 51.96  ? 218 GLN A N   1 
ATOM   1675 C CA  . GLN A 1 218 ? 7.275  7.202  -3.124  1.00 50.66  ? 218 GLN A CA  1 
ATOM   1676 C C   . GLN A 1 218 ? 8.353  8.193  -2.696  1.00 47.76  ? 218 GLN A C   1 
ATOM   1677 O O   . GLN A 1 218 ? 9.530  7.840  -2.588  1.00 46.36  ? 218 GLN A O   1 
ATOM   1678 C CB  . GLN A 1 218 ? 7.394  5.877  -2.378  1.00 50.44  ? 218 GLN A CB  1 
ATOM   1679 C CG  . GLN A 1 218 ? 6.925  5.934  -0.930  1.00 51.55  ? 218 GLN A CG  1 
ATOM   1680 C CD  . GLN A 1 218 ? 5.414  5.991  -0.805  1.00 55.32  ? 218 GLN A CD  1 
ATOM   1681 O OE1 . GLN A 1 218 ? 4.691  5.369  -1.583  1.00 58.67  ? 218 GLN A OE1 1 
ATOM   1682 N NE2 . GLN A 1 218 ? 4.930  6.740  0.179   1.00 55.39  ? 218 GLN A NE2 1 
ATOM   1683 N N   . ILE A 1 219 ? 7.951  9.439  -2.468  1.00 47.50  ? 219 ILE A N   1 
ATOM   1684 C CA  . ILE A 1 219 ? 8.878  10.518 -2.142  1.00 45.03  ? 219 ILE A CA  1 
ATOM   1685 C C   . ILE A 1 219 ? 8.809  10.797 -0.649  1.00 45.20  ? 219 ILE A C   1 
ATOM   1686 O O   . ILE A 1 219 ? 7.717  10.895 -0.073  1.00 46.33  ? 219 ILE A O   1 
ATOM   1687 C CB  . ILE A 1 219 ? 8.564  11.784 -2.956  1.00 45.18  ? 219 ILE A CB  1 
ATOM   1688 C CG1 . ILE A 1 219 ? 8.595  11.467 -4.452  1.00 44.78  ? 219 ILE A CG1 1 
ATOM   1689 C CG2 . ILE A 1 219 ? 9.559  12.891 -2.631  1.00 43.68  ? 219 ILE A CG2 1 
ATOM   1690 C CD1 . ILE A 1 219 ? 8.189  12.627 -5.333  1.00 45.52  ? 219 ILE A CD1 1 
ATOM   1691 N N   . SER A 1 220 ? 9.974  10.933 -0.022  1.00 44.39  ? 220 SER A N   1 
ATOM   1692 C CA  . SER A 1 220 ? 10.078 11.225 1.399   1.00 44.77  ? 220 SER A CA  1 
ATOM   1693 C C   . SER A 1 220 ? 10.805 12.545 1.602   1.00 44.58  ? 220 SER A C   1 
ATOM   1694 O O   . SER A 1 220 ? 11.702 12.893 0.831   1.00 43.10  ? 220 SER A O   1 
ATOM   1695 C CB  . SER A 1 220 ? 10.819 10.111 2.146   1.00 42.77  ? 220 SER A CB  1 
ATOM   1696 O OG  . SER A 1 220 ? 12.207 10.144 1.870   1.00 39.85  ? 220 SER A OG  1 
ATOM   1697 N N   . VAL A 1 221 ? 10.407 13.271 2.644   1.00 46.09  ? 221 VAL A N   1 
ATOM   1698 C CA  . VAL A 1 221 ? 11.064 14.502 3.076   1.00 45.10  ? 221 VAL A CA  1 
ATOM   1699 C C   . VAL A 1 221 ? 11.189 14.385 4.591   1.00 45.72  ? 221 VAL A C   1 
ATOM   1700 O O   . VAL A 1 221 ? 10.209 14.590 5.318   1.00 48.93  ? 221 VAL A O   1 
ATOM   1701 C CB  . VAL A 1 221 ? 10.289 15.763 2.673   1.00 45.95  ? 221 VAL A CB  1 
ATOM   1702 C CG1 . VAL A 1 221 ? 10.939 16.995 3.281   1.00 45.66  ? 221 VAL A CG1 1 
ATOM   1703 C CG2 . VAL A 1 221 ? 10.208 15.880 1.157   1.00 45.19  ? 221 VAL A CG2 1 
ATOM   1704 N N   . ASP A 1 222 ? 12.380 14.034 5.070   1.00 43.94  ? 222 ASP A N   1 
ATOM   1705 C CA  . ASP A 1 222 ? 12.632 13.760 6.495   1.00 45.15  ? 222 ASP A CA  1 
ATOM   1706 C C   . ASP A 1 222 ? 11.704 12.610 6.896   1.00 49.68  ? 222 ASP A C   1 
ATOM   1707 O O   . ASP A 1 222 ? 11.710 11.569 6.225   1.00 50.88  ? 222 ASP A O   1 
ATOM   1708 C CB  . ASP A 1 222 ? 12.489 15.042 7.305   1.00 45.56  ? 222 ASP A CB  1 
ATOM   1709 C CG  . ASP A 1 222 ? 13.458 16.118 6.864   1.00 45.39  ? 222 ASP A CG  1 
ATOM   1710 O OD1 . ASP A 1 222 ? 14.481 15.772 6.237   1.00 43.95  ? 222 ASP A OD1 1 
ATOM   1711 O OD2 . ASP A 1 222 ? 13.200 17.307 7.145   1.00 47.12  ? 222 ASP A OD2 1 
ATOM   1712 N N   . HIS A 1 223 ? 10.904 12.748 7.957   1.00 53.38  ? 223 HIS A N   1 
ATOM   1713 C CA  . HIS A 1 223 ? 10.030 11.648 8.356   1.00 57.09  ? 223 HIS A CA  1 
ATOM   1714 C C   . HIS A 1 223 ? 8.817  11.533 7.442   1.00 59.54  ? 223 HIS A C   1 
ATOM   1715 O O   . HIS A 1 223 ? 8.279  10.433 7.263   1.00 61.56  ? 223 HIS A O   1 
ATOM   1716 C CB  . HIS A 1 223 ? 9.584  11.830 9.808   1.00 59.21  ? 223 HIS A CB  1 
ATOM   1717 C CG  . HIS A 1 223 ? 8.853  10.649 10.367  0.80 61.54  ? 223 HIS A CG  1 
ATOM   1718 N ND1 . HIS A 1 223 ? 9.487  9.473  10.706  0.80 61.28  ? 223 HIS A ND1 1 
ATOM   1719 C CD2 . HIS A 1 223 ? 7.540  10.462 10.645  0.80 64.68  ? 223 HIS A CD2 1 
ATOM   1720 C CE1 . HIS A 1 223 ? 8.598  8.613  11.170  0.80 63.68  ? 223 HIS A CE1 1 
ATOM   1721 N NE2 . HIS A 1 223 ? 7.409  9.188  11.143  0.80 65.80  ? 223 HIS A NE2 1 
ATOM   1722 N N   . LEU A 1 224 ? 8.376  12.644 6.857   1.00 59.70  ? 224 LEU A N   1 
ATOM   1723 C CA  . LEU A 1 224 ? 7.217  12.628 5.976   1.00 62.00  ? 224 LEU A CA  1 
ATOM   1724 C C   . LEU A 1 224 ? 7.526  11.865 4.693   1.00 62.03  ? 224 LEU A C   1 
ATOM   1725 O O   . LEU A 1 224 ? 8.614  11.987 4.125   1.00 61.32  ? 224 LEU A O   1 
ATOM   1726 C CB  . LEU A 1 224 ? 6.787  14.058 5.649   1.00 63.20  ? 224 LEU A CB  1 
ATOM   1727 C CG  . LEU A 1 224 ? 5.658  14.233 4.632   1.00 66.99  ? 224 LEU A CG  1 
ATOM   1728 C CD1 . LEU A 1 224 ? 4.368  13.616 5.150   1.00 69.76  ? 224 LEU A CD1 1 
ATOM   1729 C CD2 . LEU A 1 224 ? 5.460  15.703 4.295   1.00 69.05  ? 224 LEU A CD2 1 
ATOM   1730 N N   . SER A 1 225 ? 6.557  11.073 4.239   1.00 63.27  ? 225 SER A N   1 
ATOM   1731 C CA  . SER A 1 225 ? 6.707  10.295 3.011   1.00 62.90  ? 225 SER A CA  1 
ATOM   1732 C C   . SER A 1 225 ? 5.322  9.993  2.463   1.00 65.77  ? 225 SER A C   1 
ATOM   1733 O O   . SER A 1 225 ? 4.490  9.422  3.175   1.00 68.44  ? 225 SER A O   1 
ATOM   1734 C CB  . SER A 1 225 ? 7.479  9.001  3.277   1.00 62.64  ? 225 SER A CB  1 
ATOM   1735 O OG  . SER A 1 225 ? 7.578  8.214  2.103   1.00 63.32  ? 225 SER A OG  1 
ATOM   1736 N N   . ILE A 1 226 ? 5.075  10.373 1.211   1.00 65.15  ? 226 ILE A N   1 
ATOM   1737 C CA  . ILE A 1 226 ? 3.780  10.172 0.573   1.00 67.21  ? 226 ILE A CA  1 
ATOM   1738 C C   . ILE A 1 226 ? 3.994  9.718  -0.864  1.00 65.65  ? 226 ILE A C   1 
ATOM   1739 O O   . ILE A 1 226 ? 4.982  10.077 -1.511  1.00 63.08  ? 226 ILE A O   1 
ATOM   1740 C CB  . ILE A 1 226 ? 2.910  11.449 0.610   1.00 69.11  ? 226 ILE A CB  1 
ATOM   1741 C CG1 . ILE A 1 226 ? 3.726  12.666 0.166   1.00 67.93  ? 226 ILE A CG1 1 
ATOM   1742 C CG2 . ILE A 1 226 ? 2.320  11.659 1.998   1.00 69.99  ? 226 ILE A CG2 1 
ATOM   1743 C CD1 . ILE A 1 226 ? 2.957  13.970 0.220   1.00 70.21  ? 226 ILE A CD1 1 
ATOM   1744 N N   . LEU A 1 227 ? 3.052  8.919  -1.360  1.00 66.91  ? 227 LEU A N   1 
ATOM   1745 C CA  . LEU A 1 227 ? 3.099  8.431  -2.733  1.00 66.52  ? 227 LEU A CA  1 
ATOM   1746 C C   . LEU A 1 227 ? 2.601  9.517  -3.678  1.00 67.89  ? 227 LEU A C   1 
ATOM   1747 O O   . LEU A 1 227 ? 1.445  9.945  -3.589  1.00 71.16  ? 227 LEU A O   1 
ATOM   1748 C CB  . LEU A 1 227 ? 2.259  7.163  -2.874  1.00 69.05  ? 227 LEU A CB  1 
ATOM   1749 C CG  . LEU A 1 227 ? 1.954  6.671  -4.291  1.00 70.73  ? 227 LEU A CG  1 
ATOM   1750 C CD1 . LEU A 1 227 ? 3.234  6.404  -5.066  1.00 68.21  ? 227 LEU A CD1 1 
ATOM   1751 C CD2 . LEU A 1 227 ? 1.082  5.425  -4.250  1.00 74.23  ? 227 LEU A CD2 1 
ATOM   1752 N N   . HIS A 1 228 ? 3.471  9.962  -4.580  1.00 66.20  ? 228 HIS A N   1 
ATOM   1753 C CA  . HIS A 1 228 ? 3.131  10.978 -5.566  1.00 67.26  ? 228 HIS A CA  1 
ATOM   1754 C C   . HIS A 1 228 ? 2.756  10.306 -6.880  1.00 68.33  ? 228 HIS A C   1 
ATOM   1755 O O   . HIS A 1 228 ? 3.486  9.438  -7.371  1.00 67.09  ? 228 HIS A O   1 
ATOM   1756 C CB  . HIS A 1 228 ? 4.295  11.948 -5.770  1.00 65.17  ? 228 HIS A CB  1 
ATOM   1757 C CG  . HIS A 1 228 ? 4.540  12.849 -4.600  1.00 64.35  ? 228 HIS A CG  1 
ATOM   1758 N ND1 . HIS A 1 228 ? 4.132  14.165 -4.576  1.00 65.96  ? 228 HIS A ND1 1 
ATOM   1759 C CD2 . HIS A 1 228 ? 5.144  12.621 -3.409  1.00 63.46  ? 228 HIS A CD2 1 
ATOM   1760 C CE1 . HIS A 1 228 ? 4.478  14.711 -3.424  1.00 65.29  ? 228 HIS A CE1 1 
ATOM   1761 N NE2 . HIS A 1 228 ? 5.093  13.796 -2.698  1.00 63.85  ? 228 HIS A NE2 1 
ATOM   1762 N N   . ARG A 1 229 ? 1.621  10.710 -7.443  1.00 70.98  ? 229 ARG A N   1 
ATOM   1763 C CA  . ARG A 1 229 ? 1.054  10.078 -8.625  1.00 73.12  ? 229 ARG A CA  1 
ATOM   1764 C C   . ARG A 1 229 ? 1.241  10.972 -9.844  1.00 74.14  ? 229 ARG A C   1 
ATOM   1765 O O   . ARG A 1 229 ? 1.106  12.197 -9.753  1.00 74.69  ? 229 ARG A O   1 
ATOM   1766 C CB  . ARG A 1 229 ? -0.435 9.782  -8.420  1.00 76.64  ? 229 ARG A CB  1 
ATOM   1767 C CG  . ARG A 1 229 ? -0.972 8.660  -9.290  1.00 78.82  ? 229 ARG A CG  1 
ATOM   1768 C CD  . ARG A 1 229 ? -0.628 7.294  -8.713  1.00 77.60  ? 229 ARG A CD  1 
ATOM   1769 N NE  . ARG A 1 229 ? -1.515 6.917  -7.615  0.78 78.92  ? 229 ARG A NE  1 
ATOM   1770 C CZ  . ARG A 1 229 ? -1.479 5.741  -6.996  0.88 78.31  ? 229 ARG A CZ  1 
ATOM   1771 N NH1 . ARG A 1 229 ? -0.598 4.822  -7.365  1.00 77.11  ? 229 ARG A NH1 1 
ATOM   1772 N NH2 . ARG A 1 229 ? -2.326 5.483  -6.009  0.89 79.55  ? 229 ARG A NH2 1 
ATOM   1773 N N   . ASP A 1 230 ? 1.547  10.347 -10.980 1.00 74.81  ? 230 ASP A N   1 
ATOM   1774 C CA  . ASP A 1 230 ? 1.720  11.033 -12.261 1.00 76.10  ? 230 ASP A CA  1 
ATOM   1775 C C   . ASP A 1 230 ? 2.757  12.152 -12.148 1.00 72.78  ? 230 ASP A C   1 
ATOM   1776 O O   . ASP A 1 230 ? 2.478  13.332 -12.373 1.00 73.81  ? 230 ASP A O   1 
ATOM   1777 C CB  . ASP A 1 230 ? 0.378  11.561 -12.779 1.00 81.91  ? 230 ASP A CB  1 
ATOM   1778 C CG  . ASP A 1 230 ? 0.460  12.064 -14.207 1.00 84.80  ? 230 ASP A CG  1 
ATOM   1779 O OD1 . ASP A 1 230 ? 0.890  11.291 -15.090 1.00 85.18  ? 230 ASP A OD1 1 
ATOM   1780 O OD2 . ASP A 1 230 ? 0.085  13.231 -14.448 1.00 87.09  ? 230 ASP A OD2 1 
ATOM   1781 N N   . VAL A 1 231 ? 3.973  11.752 -11.790 1.00 69.08  ? 231 VAL A N   1 
ATOM   1782 C CA  . VAL A 1 231 ? 5.080  12.681 -11.606 1.00 65.76  ? 231 VAL A CA  1 
ATOM   1783 C C   . VAL A 1 231 ? 5.750  12.929 -12.949 1.00 64.81  ? 231 VAL A C   1 
ATOM   1784 O O   . VAL A 1 231 ? 6.067  11.984 -13.681 1.00 65.02  ? 231 VAL A O   1 
ATOM   1785 C CB  . VAL A 1 231 ? 6.088  12.135 -10.583 1.00 62.83  ? 231 VAL A CB  1 
ATOM   1786 C CG1 . VAL A 1 231 ? 7.317  13.032 -10.517 1.00 59.98  ? 231 VAL A CG1 1 
ATOM   1787 C CG2 . VAL A 1 231 ? 5.439  12.010 -9.216  1.00 64.01  ? 231 VAL A CG2 1 
ATOM   1788 N N   . GLN A 1 232 ? 5.961  14.202 -13.276 1.00 64.13  ? 232 GLN A N   1 
ATOM   1789 C CA  . GLN A 1 232 ? 6.674  14.581 -14.487 1.00 63.12  ? 232 GLN A CA  1 
ATOM   1790 C C   . GLN A 1 232 ? 8.134  14.929 -14.237 1.00 60.60  ? 232 GLN A C   1 
ATOM   1791 O O   . GLN A 1 232 ? 8.960  14.762 -15.141 1.00 60.41  ? 232 GLN A O   1 
ATOM   1792 C CB  . GLN A 1 232 ? 5.985  15.773 -15.161 1.00 65.18  ? 232 GLN A CB  1 
ATOM   1793 N N   . GLU A 1 233 ? 8.472  15.395 -13.036 1.00 58.32  ? 233 GLU A N   1 
ATOM   1794 C CA  . GLU A 1 233 ? 9.833  15.812 -12.728 1.00 54.04  ? 233 GLU A CA  1 
ATOM   1795 C C   . GLU A 1 233 ? 9.966  16.023 -11.226 1.00 51.77  ? 233 GLU A C   1 
ATOM   1796 O O   . GLU A 1 233 ? 9.015  16.438 -10.559 1.00 52.85  ? 233 GLU A O   1 
ATOM   1797 C CB  . GLU A 1 233 ? 10.204 17.100 -13.476 1.00 54.23  ? 233 GLU A CB  1 
ATOM   1798 C CG  . GLU A 1 233 ? 11.646 17.537 -13.292 1.00 52.59  ? 233 GLU A CG  1 
ATOM   1799 C CD  . GLU A 1 233 ? 11.938 18.870 -13.948 1.00 55.10  ? 233 GLU A CD  1 
ATOM   1800 O OE1 . GLU A 1 233 ? 10.982 19.534 -14.399 1.00 58.43  ? 233 GLU A OE1 1 
ATOM   1801 O OE2 . GLU A 1 233 ? 13.125 19.254 -14.012 1.00 54.62  ? 233 GLU A OE2 1 
ATOM   1802 N N   . ILE A 1 234 ? 11.156 15.722 -10.708 1.00 48.88  ? 234 ILE A N   1 
ATOM   1803 C CA  . ILE A 1 234 ? 11.548 16.048 -9.342  1.00 46.87  ? 234 ILE A CA  1 
ATOM   1804 C C   . ILE A 1 234 ? 12.832 16.861 -9.414  1.00 47.46  ? 234 ILE A C   1 
ATOM   1805 O O   . ILE A 1 234 ? 13.810 16.427 -10.034 1.00 47.48  ? 234 ILE A O   1 
ATOM   1806 C CB  . ILE A 1 234 ? 11.750 14.786 -8.482  1.00 43.69  ? 234 ILE A CB  1 
ATOM   1807 C CG1 . ILE A 1 234 ? 10.555 13.841 -8.617  1.00 43.24  ? 234 ILE A CG1 1 
ATOM   1808 C CG2 . ILE A 1 234 ? 11.961 15.166 -7.024  1.00 43.13  ? 234 ILE A CG2 1 
ATOM   1809 C CD1 . ILE A 1 234 ? 10.766 12.502 -7.946  1.00 40.95  ? 234 ILE A CD1 1 
ATOM   1810 N N   . ARG A 1 235 ? 12.831 18.035 -8.788  1.00 49.09  ? 235 ARG A N   1 
ATOM   1811 C CA  . ARG A 1 235 ? 13.959 18.955 -8.849  1.00 50.04  ? 235 ARG A CA  1 
ATOM   1812 C C   . ARG A 1 235 ? 14.567 19.132 -7.466  1.00 48.67  ? 235 ARG A C   1 
ATOM   1813 O O   . ARG A 1 235 ? 13.847 19.372 -6.490  1.00 49.59  ? 235 ARG A O   1 
ATOM   1814 C CB  . ARG A 1 235 ? 13.534 20.311 -9.422  1.00 53.40  ? 235 ARG A CB  1 
ATOM   1815 C CG  . ARG A 1 235 ? 13.357 20.307 -10.933 1.00 56.92  ? 235 ARG A CG  1 
ATOM   1816 C CD  . ARG A 1 235 ? 12.902 21.661 -11.462 1.00 62.11  ? 235 ARG A CD  1 
ATOM   1817 N NE  . ARG A 1 235 ? 13.868 22.724 -11.195 0.69 64.53  ? 235 ARG A NE  1 
ATOM   1818 C CZ  . ARG A 1 235 ? 13.744 23.619 -10.220 1.00 66.83  ? 235 ARG A CZ  1 
ATOM   1819 N NH1 . ARG A 1 235 ? 12.691 23.583 -9.415  0.19 67.10  ? 235 ARG A NH1 1 
ATOM   1820 N NH2 . ARG A 1 235 ? 14.672 24.551 -10.050 0.97 68.77  ? 235 ARG A NH2 1 
ATOM   1821 N N   . TYR A 1 236 ? 15.891 19.019 -7.391  1.00 46.87  ? 236 TYR A N   1 
ATOM   1822 C CA  . TYR A 1 236 ? 16.646 19.194 -6.159  1.00 44.72  ? 236 TYR A CA  1 
ATOM   1823 C C   . TYR A 1 236 ? 17.595 20.374 -6.304  1.00 45.40  ? 236 TYR A C   1 
ATOM   1824 O O   . TYR A 1 236 ? 18.213 20.559 -7.357  1.00 46.08  ? 236 TYR A O   1 
ATOM   1825 C CB  . TYR A 1 236 ? 17.445 17.934 -5.815  1.00 42.33  ? 236 TYR A CB  1 
ATOM   1826 C CG  . TYR A 1 236 ? 16.608 16.782 -5.313  1.00 43.61  ? 236 TYR A CG  1 
ATOM   1827 C CD1 . TYR A 1 236 ? 15.608 16.983 -4.372  1.00 46.57  ? 236 TYR A CD1 1 
ATOM   1828 C CD2 . TYR A 1 236 ? 16.819 15.493 -5.781  1.00 43.70  ? 236 TYR A CD2 1 
ATOM   1829 C CE1 . TYR A 1 236 ? 14.843 15.931 -3.909  1.00 48.33  ? 236 TYR A CE1 1 
ATOM   1830 C CE2 . TYR A 1 236 ? 16.058 14.434 -5.326  1.00 45.51  ? 236 TYR A CE2 1 
ATOM   1831 C CZ  . TYR A 1 236 ? 15.072 14.660 -4.390  1.00 47.78  ? 236 TYR A CZ  1 
ATOM   1832 O OH  . TYR A 1 236 ? 14.310 13.612 -3.930  1.00 48.81  ? 236 TYR A OH  1 
ATOM   1833 N N   . GLU A 1 237 ? 17.713 21.164 -5.240  1.00 45.18  ? 237 GLU A N   1 
ATOM   1834 C CA  . GLU A 1 237 ? 18.608 22.313 -5.226  1.00 45.14  ? 237 GLU A CA  1 
ATOM   1835 C C   . GLU A 1 237 ? 18.751 22.809 -3.796  1.00 45.34  ? 237 GLU A C   1 
ATOM   1836 O O   . GLU A 1 237 ? 17.845 22.640 -2.975  1.00 46.53  ? 237 GLU A O   1 
ATOM   1837 C CB  . GLU A 1 237 ? 18.096 23.440 -6.135  1.00 46.52  ? 237 GLU A CB  1 
ATOM   1838 C CG  . GLU A 1 237 ? 16.613 23.735 -5.992  1.00 47.82  ? 237 GLU A CG  1 
ATOM   1839 C CD  . GLU A 1 237 ? 16.132 24.777 -6.982  0.40 50.51  ? 237 GLU A CD  1 
ATOM   1840 O OE1 . GLU A 1 237 ? 16.923 25.680 -7.327  1.00 51.62  ? 237 GLU A OE1 1 
ATOM   1841 O OE2 . GLU A 1 237 ? 14.967 24.689 -7.423  0.81 51.95  ? 237 GLU A OE2 1 
ATOM   1842 N N   . VAL A 1 238 ? 19.902 23.415 -3.510  1.00 44.81  ? 238 VAL A N   1 
ATOM   1843 C CA  . VAL A 1 238 ? 20.140 23.997 -2.194  1.00 44.46  ? 238 VAL A CA  1 
ATOM   1844 C C   . VAL A 1 238 ? 19.200 25.180 -2.006  1.00 46.86  ? 238 VAL A C   1 
ATOM   1845 O O   . VAL A 1 238 ? 19.211 26.132 -2.795  1.00 49.20  ? 238 VAL A O   1 
ATOM   1846 C CB  . VAL A 1 238 ? 21.607 24.418 -2.035  1.00 44.53  ? 238 VAL A CB  1 
ATOM   1847 C CG1 . VAL A 1 238 ? 21.828 25.060 -0.673  1.00 44.92  ? 238 VAL A CG1 1 
ATOM   1848 C CG2 . VAL A 1 238 ? 22.524 23.220 -2.220  1.00 43.05  ? 238 VAL A CG2 1 
ATOM   1849 N N   . SER A 1 239 ? 18.381 25.121 -0.961  1.00 46.80  ? 239 SER A N   1 
ATOM   1850 C CA  . SER A 1 239 ? 17.378 26.149 -0.730  1.00 49.40  ? 239 SER A CA  1 
ATOM   1851 C C   . SER A 1 239 ? 18.024 27.467 -0.317  1.00 51.07  ? 239 SER A C   1 
ATOM   1852 O O   . SER A 1 239 ? 19.098 27.500 0.290   1.00 50.88  ? 239 SER A O   1 
ATOM   1853 C CB  . SER A 1 239 ? 16.392 25.698 0.346   1.00 49.87  ? 239 SER A CB  1 
ATOM   1854 O OG  . SER A 1 239 ? 15.458 26.722 0.643   1.00 52.82  ? 239 SER A OG  1 
ATOM   1855 N N   . ALA A 1 240 ? 17.350 28.565 -0.662  1.00 53.34  ? 240 ALA A N   1 
ATOM   1856 C CA  . ALA A 1 240 ? 17.744 29.888 -0.198  1.00 55.42  ? 240 ALA A CA  1 
ATOM   1857 C C   . ALA A 1 240 ? 17.397 30.122 1.265   1.00 57.06  ? 240 ALA A C   1 
ATOM   1858 O O   . ALA A 1 240 ? 17.899 31.083 1.859   1.00 58.47  ? 240 ALA A O   1 
ATOM   1859 C CB  . ALA A 1 240 ? 17.086 30.969 -1.061  1.00 57.10  ? 240 ALA A CB  1 
ATOM   1860 N N   . LYS A 1 241 ? 16.558 29.274 1.853   1.00 56.88  ? 241 LYS A N   1 
ATOM   1861 C CA  . LYS A 1 241 ? 16.211 29.370 3.261   1.00 57.14  ? 241 LYS A CA  1 
ATOM   1862 C C   . LYS A 1 241 ? 17.241 28.638 4.110   1.00 54.00  ? 241 LYS A C   1 
ATOM   1863 O O   . LYS A 1 241 ? 17.908 27.708 3.650   1.00 51.95  ? 241 LYS A O   1 
ATOM   1864 C CB  . LYS A 1 241 ? 14.821 28.787 3.517   1.00 58.37  ? 241 LYS A CB  1 
ATOM   1865 C CG  . LYS A 1 241 ? 13.704 29.456 2.733   1.00 61.65  ? 241 LYS A CG  1 
ATOM   1866 C CD  . LYS A 1 241 ? 12.352 28.866 3.105   0.86 64.37  ? 241 LYS A CD  1 
ATOM   1867 C CE  . LYS A 1 241 ? 11.220 29.542 2.349   1.00 69.46  ? 241 LYS A CE  1 
ATOM   1868 N NZ  . LYS A 1 241 ? 11.334 29.335 0.880   1.00 70.66  ? 241 LYS A NZ  1 
ATOM   1869 N N   . LYS A 1 242 ? 17.364 29.070 5.364   1.00 53.79  ? 242 LYS A N   1 
ATOM   1870 C CA  . LYS A 1 242 ? 18.313 28.489 6.302   1.00 51.10  ? 242 LYS A CA  1 
ATOM   1871 C C   . LYS A 1 242 ? 17.651 28.358 7.665   1.00 50.58  ? 242 LYS A C   1 
ATOM   1872 O O   . LYS A 1 242 ? 16.858 29.216 8.063   1.00 53.80  ? 242 LYS A O   1 
ATOM   1873 C CB  . LYS A 1 242 ? 19.587 29.343 6.414   1.00 52.47  ? 242 LYS A CB  1 
ATOM   1874 C CG  . LYS A 1 242 ? 20.248 29.664 5.078   1.00 53.87  ? 242 LYS A CG  1 
ATOM   1875 C CD  . LYS A 1 242 ? 21.391 30.654 5.233   1.00 56.93  ? 242 LYS A CD  1 
ATOM   1876 C CE  . LYS A 1 242 ? 22.589 30.015 5.913   1.00 56.49  ? 242 LYS A CE  1 
ATOM   1877 N NZ  . LYS A 1 242 ? 23.105 28.850 5.143   1.00 55.42  ? 242 LYS A NZ  1 
ATOM   1878 N N   . ILE A 1 243 ? 17.975 27.281 8.374   1.00 46.52  ? 243 ILE A N   1 
ATOM   1879 C CA  . ILE A 1 243 ? 17.478 27.058 9.727   1.00 45.41  ? 243 ILE A CA  1 
ATOM   1880 C C   . ILE A 1 243 ? 18.461 27.677 10.711  1.00 46.55  ? 243 ILE A C   1 
ATOM   1881 O O   . ILE A 1 243 ? 19.679 27.518 10.578  1.00 46.29  ? 243 ILE A O   1 
ATOM   1882 C CB  . ILE A 1 243 ? 17.269 25.555 10.000  1.00 42.68  ? 243 ILE A CB  1 
ATOM   1883 C CG1 . ILE A 1 243 ? 16.815 25.325 11.443  1.00 43.10  ? 243 ILE A CG1 1 
ATOM   1884 C CG2 . ILE A 1 243 ? 18.534 24.759 9.694   1.00 40.53  ? 243 ILE A CG2 1 
ATOM   1885 C CD1 . ILE A 1 243 ? 16.566 23.869 11.782  1.00 41.16  ? 243 ILE A CD1 1 
ATOM   1886 N N   . HIS A 1 244 ? 17.935 28.400 11.696  1.00 48.49  ? 244 HIS A N   1 
ATOM   1887 C CA  . HIS A 1 244 ? 18.751 29.155 12.636  1.00 50.53  ? 244 HIS A CA  1 
ATOM   1888 C C   . HIS A 1 244 ? 18.739 28.483 14.002  1.00 51.02  ? 244 HIS A C   1 
ATOM   1889 O O   . HIS A 1 244 ? 17.669 28.199 14.552  1.00 50.75  ? 244 HIS A O   1 
ATOM   1890 C CB  . HIS A 1 244 ? 18.253 30.597 12.753  1.00 53.39  ? 244 HIS A CB  1 
ATOM   1891 C CG  . HIS A 1 244 ? 18.236 31.335 11.451  1.00 54.29  ? 244 HIS A CG  1 
ATOM   1892 N ND1 . HIS A 1 244 ? 19.387 31.712 10.794  1.00 53.66  ? 244 HIS A ND1 1 
ATOM   1893 C CD2 . HIS A 1 244 ? 17.207 31.767 10.684  1.00 55.55  ? 244 HIS A CD2 1 
ATOM   1894 C CE1 . HIS A 1 244 ? 19.068 32.344 9.679   1.00 54.89  ? 244 HIS A CE1 1 
ATOM   1895 N NE2 . HIS A 1 244 ? 17.752 32.391 9.588   1.00 55.84  ? 244 HIS A NE2 1 
ATOM   1896 N N   . PHE A 1 245 ? 19.929 28.235 14.543  1.00 52.22  ? 245 PHE A N   1 
ATOM   1897 C CA  . PHE A 1 245 ? 20.098 27.681 15.876  1.00 54.29  ? 245 PHE A CA  1 
ATOM   1898 C C   . PHE A 1 245 ? 20.579 28.764 16.833  1.00 60.41  ? 245 PHE A C   1 
ATOM   1899 O O   . PHE A 1 245 ? 21.200 29.748 16.424  1.00 60.60  ? 245 PHE A O   1 
ATOM   1900 C CB  . PHE A 1 245 ? 21.102 26.524 15.879  1.00 49.84  ? 245 PHE A CB  1 
ATOM   1901 C CG  . PHE A 1 245 ? 20.701 25.364 15.015  1.00 45.60  ? 245 PHE A CG  1 
ATOM   1902 C CD1 . PHE A 1 245 ? 19.956 24.320 15.536  1.00 44.45  ? 245 PHE A CD1 1 
ATOM   1903 C CD2 . PHE A 1 245 ? 21.084 25.309 13.685  1.00 43.42  ? 245 PHE A CD2 1 
ATOM   1904 C CE1 . PHE A 1 245 ? 19.593 23.247 14.745  1.00 42.28  ? 245 PHE A CE1 1 
ATOM   1905 C CE2 . PHE A 1 245 ? 20.722 24.239 12.889  1.00 41.34  ? 245 PHE A CE2 1 
ATOM   1906 C CZ  . PHE A 1 245 ? 19.976 23.207 13.420  1.00 40.83  ? 245 PHE A CZ  1 
ATOM   1907 N N   . ALA A 1 246 ? 20.287 28.569 18.115  1.00 65.85  ? 246 ALA A N   1 
ATOM   1908 C CA  . ALA A 1 246 ? 20.785 29.434 19.175  1.00 72.10  ? 246 ALA A CA  1 
ATOM   1909 C C   . ALA A 1 246 ? 21.895 28.699 19.913  1.00 71.73  ? 246 ALA A C   1 
ATOM   1910 O O   . ALA A 1 246 ? 21.660 27.632 20.490  1.00 70.71  ? 246 ALA A O   1 
ATOM   1911 C CB  . ALA A 1 246 ? 19.664 29.828 20.136  1.00 76.89  ? 246 ALA A CB  1 
ATOM   1912 N N   . ARG A 1 247 ? 23.101 29.259 19.885  1.00 74.08  ? 247 ARG A N   1 
ATOM   1913 C CA  . ARG A 1 247 ? 24.252 28.658 20.540  1.00 75.62  ? 247 ARG A CA  1 
ATOM   1914 C C   . ARG A 1 247 ? 24.601 29.442 21.797  1.00 77.44  ? 247 ARG A C   1 
ATOM   1915 O O   . ARG A 1 247 ? 24.481 30.671 21.833  1.00 79.66  ? 247 ARG A O   1 
ATOM   1916 C CB  . ARG A 1 247 ? 25.464 28.597 19.600  1.00 76.96  ? 247 ARG A CB  1 
ATOM   1917 C CG  . ARG A 1 247 ? 26.123 29.939 19.313  1.00 81.62  ? 247 ARG A CG  1 
ATOM   1918 C CD  . ARG A 1 247 ? 27.347 29.784 18.417  1.00 83.17  ? 247 ARG A CD  1 
ATOM   1919 N NE  . ARG A 1 247 ? 28.396 28.978 19.037  1.00 83.82  ? 247 ARG A NE  1 
ATOM   1920 C CZ  . ARG A 1 247 ? 29.394 29.478 19.759  1.00 85.54  ? 247 ARG A CZ  1 
ATOM   1921 N NH1 . ARG A 1 247 ? 29.482 30.786 19.957  1.00 88.30  ? 247 ARG A NH1 1 
ATOM   1922 N NH2 . ARG A 1 247 ? 30.305 28.670 20.284  1.00 84.68  ? 247 ARG A NH2 1 
ATOM   1923 N N   . PHE A 1 248 ? 25.017 28.717 22.833  1.00 76.49  ? 248 PHE A N   1 
ATOM   1924 C CA  . PHE A 1 248 ? 25.463 29.315 24.081  1.00 78.73  ? 248 PHE A CA  1 
ATOM   1925 C C   . PHE A 1 248 ? 26.873 28.892 24.460  1.00 77.75  ? 248 PHE A C   1 
ATOM   1926 O O   . PHE A 1 248 ? 27.412 29.399 25.451  1.00 80.57  ? 248 PHE A O   1 
ATOM   1927 C CB  . PHE A 1 248 ? 24.502 28.954 25.222  1.00 81.04  ? 248 PHE A CB  1 
ATOM   1928 C CG  . PHE A 1 248 ? 23.098 29.443 25.010  0.80 83.10  ? 248 PHE A CG  1 
ATOM   1929 C CD1 . PHE A 1 248 ? 22.712 30.693 25.463  0.80 86.59  ? 248 PHE A CD1 1 
ATOM   1930 C CD2 . PHE A 1 248 ? 22.164 28.651 24.361  0.80 81.61  ? 248 PHE A CD2 1 
ATOM   1931 C CE1 . PHE A 1 248 ? 21.421 31.146 25.272  0.80 87.77  ? 248 PHE A CE1 1 
ATOM   1932 C CE2 . PHE A 1 248 ? 20.872 29.099 24.167  0.80 82.84  ? 248 PHE A CE2 1 
ATOM   1933 C CZ  . PHE A 1 248 ? 20.501 30.347 24.624  0.80 85.85  ? 248 PHE A CZ  1 
ATOM   1934 N N   . ARG A 1 249 ? 27.482 27.986 23.703  1.00 74.02  ? 249 ARG A N   1 
ATOM   1935 C CA  . ARG A 1 249 ? 28.780 27.424 24.049  1.00 72.99  ? 249 ARG A CA  1 
ATOM   1936 C C   . ARG A 1 249 ? 29.394 26.835 22.787  1.00 69.13  ? 249 ARG A C   1 
ATOM   1937 O O   . ARG A 1 249 ? 28.834 26.938 21.692  1.00 66.86  ? 249 ARG A O   1 
ATOM   1938 C CB  . ARG A 1 249 ? 28.642 26.365 25.144  1.00 73.46  ? 249 ARG A CB  1 
ATOM   1939 C CG  . ARG A 1 249 ? 27.748 25.208 24.737  0.55 71.67  ? 249 ARG A CG  1 
ATOM   1940 C CD  . ARG A 1 249 ? 27.598 24.186 25.845  1.00 72.69  ? 249 ARG A CD  1 
ATOM   1941 N NE  . ARG A 1 249 ? 26.872 23.009 25.380  0.57 70.57  ? 249 ARG A NE  1 
ATOM   1942 C CZ  . ARG A 1 249 ? 26.578 21.962 26.142  0.36 70.43  ? 249 ARG A CZ  1 
ATOM   1943 N NH1 . ARG A 1 249 ? 26.948 21.942 27.415  0.78 71.93  ? 249 ARG A NH1 1 
ATOM   1944 N NH2 . ARG A 1 249 ? 25.914 20.934 25.630  1.00 68.85  ? 249 ARG A NH2 1 
ATOM   1945 N N   . SER A 1 250 ? 30.550 26.199 22.951  1.00 67.69  ? 250 SER A N   1 
ATOM   1946 C CA  . SER A 1 250 ? 31.260 25.565 21.849  1.00 62.92  ? 250 SER A CA  1 
ATOM   1947 C C   . SER A 1 250 ? 30.940 24.075 21.836  1.00 58.84  ? 250 SER A C   1 
ATOM   1948 O O   . SER A 1 250 ? 31.253 23.360 22.794  1.00 59.51  ? 250 SER A O   1 
ATOM   1949 C CB  . SER A 1 250 ? 32.766 25.791 21.970  1.00 63.31  ? 250 SER A CB  1 
ATOM   1950 O OG  . SER A 1 250 ? 33.465 25.141 20.922  0.92 60.55  ? 250 SER A OG  1 
ATOM   1951 N N   . PHE A 1 251 ? 30.311 23.616 20.756  1.00 54.85  ? 251 PHE A N   1 
ATOM   1952 C CA  . PHE A 1 251 ? 30.076 22.191 20.527  1.00 51.85  ? 251 PHE A CA  1 
ATOM   1953 C C   . PHE A 1 251 ? 30.314 21.937 19.046  1.00 50.55  ? 251 PHE A C   1 
ATOM   1954 O O   . PHE A 1 251 ? 29.378 21.957 18.236  1.00 49.95  ? 251 PHE A O   1 
ATOM   1955 C CB  . PHE A 1 251 ? 28.666 21.776 20.950  1.00 50.63  ? 251 PHE A CB  1 
ATOM   1956 C CG  . PHE A 1 251 ? 28.517 20.301 21.217  1.00 50.19  ? 251 PHE A CG  1 
ATOM   1957 C CD1 . PHE A 1 251 ? 29.587 19.436 21.051  1.00 49.03  ? 251 PHE A CD1 1 
ATOM   1958 C CD2 . PHE A 1 251 ? 27.303 19.781 21.634  1.00 51.74  ? 251 PHE A CD2 1 
ATOM   1959 C CE1 . PHE A 1 251 ? 29.448 18.082 21.296  1.00 48.74  ? 251 PHE A CE1 1 
ATOM   1960 C CE2 . PHE A 1 251 ? 27.159 18.428 21.880  1.00 51.67  ? 251 PHE A CE2 1 
ATOM   1961 C CZ  . PHE A 1 251 ? 28.233 17.578 21.711  1.00 50.03  ? 251 PHE A CZ  1 
ATOM   1962 N N   . PRO A 1 252 ? 31.567 21.708 18.653  1.00 50.45  ? 252 PRO A N   1 
ATOM   1963 C CA  . PRO A 1 252 ? 31.886 21.572 17.226  1.00 48.95  ? 252 PRO A CA  1 
ATOM   1964 C C   . PRO A 1 252 ? 31.150 20.408 16.581  1.00 46.80  ? 252 PRO A C   1 
ATOM   1965 O O   . PRO A 1 252 ? 30.752 19.441 17.236  1.00 46.25  ? 252 PRO A O   1 
ATOM   1966 C CB  . PRO A 1 252 ? 33.403 21.342 17.220  1.00 49.82  ? 252 PRO A CB  1 
ATOM   1967 C CG  . PRO A 1 252 ? 33.879 21.910 18.518  1.00 51.94  ? 252 PRO A CG  1 
ATOM   1968 C CD  . PRO A 1 252 ? 32.772 21.661 19.497  1.00 51.86  ? 252 PRO A CD  1 
ATOM   1969 N N   . PHE A 1 253 ? 30.971 20.519 15.262  1.00 45.51  ? 253 PHE A N   1 
ATOM   1970 C CA  . PHE A 1 253 ? 30.275 19.478 14.513  1.00 42.80  ? 253 PHE A CA  1 
ATOM   1971 C C   . PHE A 1 253 ? 31.042 18.161 14.558  1.00 40.88  ? 253 PHE A C   1 
ATOM   1972 O O   . PHE A 1 253 ? 30.469 17.105 14.849  1.00 38.26  ? 253 PHE A O   1 
ATOM   1973 C CB  . PHE A 1 253 ? 30.056 19.932 13.070  1.00 43.15  ? 253 PHE A CB  1 
ATOM   1974 C CG  . PHE A 1 253 ? 29.498 18.861 12.177  1.00 42.81  ? 253 PHE A CG  1 
ATOM   1975 C CD1 . PHE A 1 253 ? 28.152 18.540 12.214  1.00 42.40  ? 253 PHE A CD1 1 
ATOM   1976 C CD2 . PHE A 1 253 ? 30.319 18.182 11.292  1.00 43.30  ? 253 PHE A CD2 1 
ATOM   1977 C CE1 . PHE A 1 253 ? 27.636 17.558 11.390  1.00 42.29  ? 253 PHE A CE1 1 
ATOM   1978 C CE2 . PHE A 1 253 ? 29.810 17.199 10.466  1.00 43.86  ? 253 PHE A CE2 1 
ATOM   1979 C CZ  . PHE A 1 253 ? 28.466 16.887 10.515  1.00 43.42  ? 253 PHE A CZ  1 
ATOM   1980 N N   . TRP A 1 254 ? 32.346 18.204 14.268  1.00 42.32  ? 254 TRP A N   1 
ATOM   1981 C CA  . TRP A 1 254 ? 33.150 16.986 14.321  1.00 42.05  ? 254 TRP A CA  1 
ATOM   1982 C C   . TRP A 1 254 ? 33.220 16.434 15.737  1.00 42.17  ? 254 TRP A C   1 
ATOM   1983 O O   . TRP A 1 254 ? 33.240 15.214 15.935  1.00 41.48  ? 254 TRP A O   1 
ATOM   1984 C CB  . TRP A 1 254 ? 34.555 17.252 13.785  1.00 42.31  ? 254 TRP A CB  1 
ATOM   1985 C CG  . TRP A 1 254 ? 34.573 17.799 12.395  1.00 40.78  ? 254 TRP A CG  1 
ATOM   1986 C CD1 . TRP A 1 254 ? 35.026 19.024 12.005  1.00 41.24  ? 254 TRP A CD1 1 
ATOM   1987 C CD2 . TRP A 1 254 ? 34.108 17.146 11.207  1.00 39.25  ? 254 TRP A CD2 1 
ATOM   1988 N NE1 . TRP A 1 254 ? 34.879 19.174 10.648  1.00 40.66  ? 254 TRP A NE1 1 
ATOM   1989 C CE2 . TRP A 1 254 ? 34.317 18.035 10.134  1.00 39.67  ? 254 TRP A CE2 1 
ATOM   1990 C CE3 . TRP A 1 254 ? 33.538 15.896 10.946  1.00 38.03  ? 254 TRP A CE3 1 
ATOM   1991 C CZ2 . TRP A 1 254 ? 33.977 17.715 8.822   1.00 39.18  ? 254 TRP A CZ2 1 
ATOM   1992 C CZ3 . TRP A 1 254 ? 33.201 15.580 9.641   1.00 37.26  ? 254 TRP A CZ3 1 
ATOM   1993 C CH2 . TRP A 1 254 ? 33.421 16.486 8.597   1.00 38.03  ? 254 TRP A CH2 1 
ATOM   1994 N N   . ARG A 1 255 ? 33.269 17.319 16.735  1.00 43.25  ? 255 ARG A N   1 
ATOM   1995 C CA  . ARG A 1 255 ? 33.153 16.871 18.117  1.00 44.74  ? 255 ARG A CA  1 
ATOM   1996 C C   . ARG A 1 255 ? 31.810 16.191 18.351  1.00 44.67  ? 255 ARG A C   1 
ATOM   1997 O O   . ARG A 1 255 ? 31.727 15.190 19.073  1.00 46.05  ? 255 ARG A O   1 
ATOM   1998 C CB  . ARG A 1 255 ? 33.343 18.058 19.064  1.00 45.96  ? 255 ARG A CB  1 
ATOM   1999 C CG  . ARG A 1 255 ? 32.825 17.834 20.470  0.80 46.97  ? 255 ARG A CG  1 
ATOM   2000 C CD  . ARG A 1 255 ? 33.941 17.818 21.500  0.70 49.08  ? 255 ARG A CD  1 
ATOM   2001 N NE  . ARG A 1 255 ? 33.395 17.740 22.851  0.60 50.11  ? 255 ARG A NE  1 
ATOM   2002 C CZ  . ARG A 1 255 ? 33.065 16.604 23.456  0.60 49.53  ? 255 ARG A CZ  1 
ATOM   2003 N NH1 . ARG A 1 255 ? 33.236 15.447 22.831  0.60 49.53  ? 255 ARG A NH1 1 
ATOM   2004 N NH2 . ARG A 1 255 ? 32.567 16.623 24.684  0.60 49.01  ? 255 ARG A NH2 1 
ATOM   2005 N N   . ARG A 1 256 ? 30.748 16.709 17.728  1.00 43.37  ? 256 ARG A N   1 
ATOM   2006 C CA  . ARG A 1 256 ? 29.440 16.074 17.841  1.00 42.98  ? 256 ARG A CA  1 
ATOM   2007 C C   . ARG A 1 256 ? 29.383 14.772 17.051  1.00 42.65  ? 256 ARG A C   1 
ATOM   2008 O O   . ARG A 1 256 ? 28.622 13.864 17.405  1.00 43.60  ? 256 ARG A O   1 
ATOM   2009 C CB  . ARG A 1 256 ? 28.353 17.043 17.374  1.00 43.15  ? 256 ARG A CB  1 
ATOM   2010 C CG  . ARG A 1 256 ? 26.971 16.757 17.942  1.00 45.83  ? 256 ARG A CG  1 
ATOM   2011 C CD  . ARG A 1 256 ? 26.096 18.010 17.967  1.00 48.44  ? 256 ARG A CD  1 
ATOM   2012 N NE  . ARG A 1 256 ? 25.751 18.487 16.629  1.00 48.10  ? 256 ARG A NE  1 
ATOM   2013 C CZ  . ARG A 1 256 ? 26.319 19.532 16.035  1.00 47.71  ? 256 ARG A CZ  1 
ATOM   2014 N NH1 . ARG A 1 256 ? 27.264 20.221 16.660  1.00 48.11  ? 256 ARG A NH1 1 
ATOM   2015 N NH2 . ARG A 1 256 ? 25.939 19.892 14.816  1.00 46.85  ? 256 ARG A NH2 1 
ATOM   2016 N N   . VAL A 1 257 ? 30.181 14.660 15.985  1.00 41.46  ? 257 VAL A N   1 
ATOM   2017 C CA  . VAL A 1 257 ? 30.255 13.408 15.238  1.00 40.29  ? 257 VAL A CA  1 
ATOM   2018 C C   . VAL A 1 257 ? 31.002 12.354 16.043  1.00 42.12  ? 257 VAL A C   1 
ATOM   2019 O O   . VAL A 1 257 ? 30.617 11.178 16.067  1.00 43.01  ? 257 VAL A O   1 
ATOM   2020 C CB  . VAL A 1 257 ? 30.915 13.642 13.865  1.00 39.14  ? 257 VAL A CB  1 
ATOM   2021 C CG1 . VAL A 1 257 ? 31.191 12.318 13.168  1.00 38.08  ? 257 VAL A CG1 1 
ATOM   2022 C CG2 . VAL A 1 257 ? 30.041 14.529 12.991  1.00 38.42  ? 257 VAL A CG2 1 
ATOM   2023 N N   . HIS A 1 258 ? 32.079 12.760 16.720  1.00 43.35  ? 258 HIS A N   1 
ATOM   2024 C CA  . HIS A 1 258 ? 32.887 11.818 17.488  1.00 45.33  ? 258 HIS A CA  1 
ATOM   2025 C C   . HIS A 1 258 ? 32.075 11.165 18.599  1.00 47.41  ? 258 HIS A C   1 
ATOM   2026 O O   . HIS A 1 258 ? 32.138 9.946  18.796  1.00 49.45  ? 258 HIS A O   1 
ATOM   2027 C CB  . HIS A 1 258 ? 34.108 12.534 18.065  1.00 47.20  ? 258 HIS A CB  1 
ATOM   2028 C CG  . HIS A 1 258 ? 34.760 11.802 19.197  1.00 49.51  ? 258 HIS A CG  1 
ATOM   2029 N ND1 . HIS A 1 258 ? 34.394 11.989 20.513  1.00 51.32  ? 258 HIS A ND1 1 
ATOM   2030 C CD2 . HIS A 1 258 ? 35.753 10.882 19.210  1.00 51.23  ? 258 HIS A CD2 1 
ATOM   2031 C CE1 . HIS A 1 258 ? 35.134 11.216 21.287  1.00 52.96  ? 258 HIS A CE1 1 
ATOM   2032 N NE2 . HIS A 1 258 ? 35.966 10.534 20.521  1.00 53.14  ? 258 HIS A NE2 1 
ATOM   2033 N N   . ASP A 1 259 ? 31.301 11.963 19.338  1.00 46.98  ? 259 ASP A N   1 
ATOM   2034 C CA  . ASP A 1 259 ? 30.558 11.422 20.471  1.00 48.61  ? 259 ASP A CA  1 
ATOM   2035 C C   . ASP A 1 259 ? 29.465 10.458 20.028  1.00 48.37  ? 259 ASP A C   1 
ATOM   2036 O O   . ASP A 1 259 ? 29.101 9.549  20.782  1.00 50.26  ? 259 ASP A O   1 
ATOM   2037 C CB  . ASP A 1 259 ? 29.956 12.558 21.297  1.00 49.64  ? 259 ASP A CB  1 
ATOM   2038 C CG  . ASP A 1 259 ? 31.009 13.400 21.990  1.00 52.09  ? 259 ASP A CG  1 
ATOM   2039 O OD1 . ASP A 1 259 ? 32.207 13.069 21.877  1.00 52.82  ? 259 ASP A OD1 1 
ATOM   2040 O OD2 . ASP A 1 259 ? 30.637 14.394 22.649  1.00 53.67  ? 259 ASP A OD2 1 
ATOM   2041 N N   . SER A 1 260 ? 28.937 10.630 18.815  1.00 46.07  ? 260 SER A N   1 
ATOM   2042 C CA  . SER A 1 260 ? 27.825 9.799  18.370  1.00 44.94  ? 260 SER A CA  1 
ATOM   2043 C C   . SER A 1 260 ? 28.285 8.479  17.765  1.00 44.66  ? 260 SER A C   1 
ATOM   2044 O O   . SER A 1 260 ? 27.588 7.468  17.900  1.00 44.39  ? 260 SER A O   1 
ATOM   2045 C CB  . SER A 1 260 ? 26.969 10.561 17.357  1.00 43.09  ? 260 SER A CB  1 
ATOM   2046 O OG  . SER A 1 260 ? 26.399 11.722 17.936  1.00 43.29  ? 260 SER A OG  1 
ATOM   2047 N N   . PHE A 1 261 ? 29.440 8.460  17.103  1.00 44.86  ? 261 PHE A N   1 
ATOM   2048 C CA  . PHE A 1 261 ? 29.879 7.281  16.369  1.00 45.02  ? 261 PHE A CA  1 
ATOM   2049 C C   . PHE A 1 261 ? 31.144 6.635  16.913  1.00 46.95  ? 261 PHE A C   1 
ATOM   2050 O O   . PHE A 1 261 ? 31.324 5.429  16.729  1.00 46.95  ? 261 PHE A O   1 
ATOM   2051 C CB  . PHE A 1 261 ? 30.097 7.628  14.889  1.00 42.27  ? 261 PHE A CB  1 
ATOM   2052 C CG  . PHE A 1 261 ? 28.859 8.119  14.197  1.00 39.08  ? 261 PHE A CG  1 
ATOM   2053 C CD1 . PHE A 1 261 ? 27.866 7.232  13.818  1.00 37.97  ? 261 PHE A CD1 1 
ATOM   2054 C CD2 . PHE A 1 261 ? 28.687 9.466  13.928  1.00 37.89  ? 261 PHE A CD2 1 
ATOM   2055 C CE1 . PHE A 1 261 ? 26.722 7.679  13.184  1.00 36.81  ? 261 PHE A CE1 1 
ATOM   2056 C CE2 . PHE A 1 261 ? 27.546 9.920  13.293  1.00 36.42  ? 261 PHE A CE2 1 
ATOM   2057 C CZ  . PHE A 1 261 ? 26.562 9.024  12.920  1.00 35.66  ? 261 PHE A CZ  1 
ATOM   2058 N N   . ILE A 1 262 ? 32.022 7.389  17.571  1.00 48.99  ? 262 ILE A N   1 
ATOM   2059 C CA  . ILE A 1 262 ? 33.248 6.815  18.115  1.00 53.25  ? 262 ILE A CA  1 
ATOM   2060 C C   . ILE A 1 262 ? 33.004 6.409  19.562  1.00 57.69  ? 262 ILE A C   1 
ATOM   2061 O O   . ILE A 1 262 ? 33.104 5.228  19.914  1.00 59.77  ? 262 ILE A O   1 
ATOM   2062 C CB  . ILE A 1 262 ? 34.427 7.798  18.004  1.00 53.80  ? 262 ILE A CB  1 
ATOM   2063 C CG1 . ILE A 1 262 ? 34.463 8.435  16.613  1.00 52.04  ? 262 ILE A CG1 1 
ATOM   2064 C CG2 . ILE A 1 262 ? 35.739 7.086  18.293  1.00 55.71  ? 262 ILE A CG2 1 
ATOM   2065 C CD1 . ILE A 1 262 ? 34.664 7.444  15.488  1.00 51.46  ? 262 ILE A CD1 1 
ATOM   2066 N N   . GLU A 1 263 ? 32.683 7.384  20.407  1.00 60.38  ? 263 GLU A N   1 
ATOM   2067 C CA  . GLU A 1 263 ? 32.386 7.129  21.813  1.00 63.70  ? 263 GLU A CA  1 
ATOM   2068 C C   . GLU A 1 263 ? 31.666 8.318  22.443  1.00 63.56  ? 263 GLU A C   1 
ATOM   2069 O O   . GLU A 1 263 ? 32.238 9.052  23.249  1.00 65.06  ? 263 GLU A O   1 
ATOM   2070 C CB  . GLU A 1 263 ? 33.668 6.809  22.588  1.00 68.10  ? 263 GLU A CB  1 
ATOM   2071 C CG  . GLU A 1 263 ? 34.876 7.638  22.179  0.02 69.60  ? 263 GLU A CG  1 
ATOM   2072 C CD  . GLU A 1 263 ? 36.142 7.210  22.893  0.69 74.11  ? 263 GLU A CD  1 
ATOM   2073 O OE1 . GLU A 1 263 ? 36.048 6.764  24.055  0.64 76.36  ? 263 GLU A OE1 1 
ATOM   2074 O OE2 . GLU A 1 263 ? 37.230 7.311  22.288  1.00 75.42  ? 263 GLU A OE2 1 
HETATM 2075 C C1  . CIT B 2 .   ? 31.532 23.997 14.387  0.93 59.53  ? 301 CIT A C1  1 
HETATM 2076 O O1  . CIT B 2 .   ? 31.253 22.796 14.182  0.93 59.45  ? 301 CIT A O1  1 
HETATM 2077 O O2  . CIT B 2 .   ? 32.713 24.297 14.666  0.93 59.51  ? 301 CIT A O2  1 
HETATM 2078 C C2  . CIT B 2 .   ? 30.479 25.077 14.299  0.93 59.95  ? 301 CIT A C2  1 
HETATM 2079 C C3  . CIT B 2 .   ? 29.248 24.747 15.139  0.93 61.02  ? 301 CIT A C3  1 
HETATM 2080 O O7  . CIT B 2 .   ? 29.680 24.244 16.429  0.93 61.16  ? 301 CIT A O7  1 
HETATM 2081 C C4  . CIT B 2 .   ? 28.399 25.994 15.352  0.93 62.03  ? 301 CIT A C4  1 
HETATM 2082 C C5  . CIT B 2 .   ? 29.037 26.852 16.419  0.93 63.57  ? 301 CIT A C5  1 
HETATM 2083 O O3  . CIT B 2 .   ? 29.515 27.970 16.132  0.93 64.37  ? 301 CIT A O3  1 
HETATM 2084 O O4  . CIT B 2 .   ? 29.089 26.457 17.604  0.93 63.75  ? 301 CIT A O4  1 
HETATM 2085 C C6  . CIT B 2 .   ? 28.417 23.678 14.448  0.93 61.46  ? 301 CIT A C6  1 
HETATM 2086 O O5  . CIT B 2 .   ? 27.672 23.986 13.493  0.93 61.68  ? 301 CIT A O5  1 
HETATM 2087 O O6  . CIT B 2 .   ? 28.482 22.482 14.809  0.93 61.75  ? 301 CIT A O6  1 
HETATM 2088 C C2  . UY6 C 3 .   ? 19.887 6.096  8.794   1.00 68.64  ? 302 UY6 A C2  1 
HETATM 2089 C C4  . UY6 C 3 .   ? 17.642 6.394  8.265   1.00 70.93  ? 302 UY6 A C4  1 
HETATM 2090 C C5  . UY6 C 3 .   ? 17.612 5.177  7.593   1.00 71.41  ? 302 UY6 A C5  1 
HETATM 2091 C C6  . UY6 C 3 .   ? 18.755 4.396  7.520   1.00 69.53  ? 302 UY6 A C6  1 
HETATM 2092 N N9  . UY6 C 3 .   ? 16.416 6.912  8.172   1.00 71.96  ? 302 UY6 A N9  1 
HETATM 2093 C C8  . UY6 C 3 .   ? 15.662 6.061  7.474   1.00 71.02  ? 302 UY6 A C8  1 
HETATM 2094 C CAA . UY6 C 3 .   ? 14.871 9.990  9.734   1.00 71.72  ? 302 UY6 A CAA 1 
HETATM 2095 C CAB . UY6 C 3 .   ? 15.055 10.338 8.306   1.00 70.71  ? 302 UY6 A CAB 1 
HETATM 2096 C CAD . UY6 C 3 .   ? 16.291 9.511  7.964   1.00 70.84  ? 302 UY6 A CAD 1 
HETATM 2097 C CAF . UY6 C 3 .   ? 15.877 8.223  8.717   1.00 71.16  ? 302 UY6 A CAF 1 
HETATM 2098 C CAR . UY6 C 3 .   ? 13.587 10.638 10.271  1.00 70.91  ? 302 UY6 A CAR 1 
HETATM 2099 C CAT . UY6 C 3 .   ? 13.586 9.103  12.184  1.00 68.62  ? 302 UY6 A CAT 1 
HETATM 2100 C CAU . UY6 C 3 .   ? 13.936 11.419 12.627  1.00 68.83  ? 302 UY6 A CAU 1 
HETATM 2101 C CAV . UY6 C 3 .   ? 15.400 11.500 12.666  1.00 68.42  ? 302 UY6 A CAV 1 
HETATM 2102 C CAW . UY6 C 3 .   ? 16.614 11.600 12.707  1.00 68.28  ? 302 UY6 A CAW 1 
HETATM 2103 C CAX . UY6 C 3 .   ? 18.038 11.713 12.746  1.00 67.76  ? 302 UY6 A CAX 1 
HETATM 2104 C CAZ . UY6 C 3 .   ? 18.424 10.014 14.515  1.00 68.99  ? 302 UY6 A CAZ 1 
HETATM 2105 C CBA . UY6 C 3 .   ? 18.448 8.646  13.844  1.00 69.98  ? 302 UY6 A CBA 1 
HETATM 2106 C CBB . UY6 C 3 .   ? 17.334 8.189  13.150  1.00 69.42  ? 302 UY6 A CBB 1 
HETATM 2107 C CBC . UY6 C 3 .   ? 17.367 6.942  12.540  1.00 69.34  ? 302 UY6 A CBC 1 
HETATM 2108 C CBD . UY6 C 3 .   ? 18.513 6.161  12.627  1.00 70.13  ? 302 UY6 A CBD 1 
HETATM 2109 C CBE . UY6 C 3 .   ? 19.627 6.618  13.320  1.00 71.08  ? 302 UY6 A CBE 1 
HETATM 2110 C CBF . UY6 C 3 .   ? 19.594 7.865  13.929  1.00 70.66  ? 302 UY6 A CBF 1 
HETATM 2111 C CBG . UY6 C 3 .   ? 20.107 11.369 13.317  1.00 68.23  ? 302 UY6 A CBG 1 
HETATM 2112 C CBH . UY6 C 3 .   ? 20.066 12.340 12.328  1.00 67.41  ? 302 UY6 A CBH 1 
HETATM 2113 C CBJ . UY6 C 3 .   ? 21.254 12.903 11.883  1.00 67.73  ? 302 UY6 A CBJ 1 
HETATM 2114 C CBM . UY6 C 3 .   ? 22.416 11.479 13.447  1.00 67.47  ? 302 UY6 A CBM 1 
HETATM 2115 N N1  . UY6 C 3 .   ? 19.918 4.862  8.130   1.00 68.61  ? 302 UY6 A N1  1 
HETATM 2116 N N3  . UY6 C 3 .   ? 18.777 6.818  8.845   1.00 69.58  ? 302 UY6 A N3  1 
HETATM 2117 N N6  . UY6 C 3 .   ? 18.736 3.230  6.878   1.00 69.61  ? 302 UY6 A N6  1 
HETATM 2118 N N7  . UY6 C 3 .   ? 16.385 5.004  7.121   1.00 71.09  ? 302 UY6 A N7  1 
HETATM 2119 N NAS . UY6 C 3 .   ? 13.273 10.464 11.712  1.00 69.43  ? 302 UY6 A NAS 1 
HETATM 2120 N NAY . UY6 C 3 .   ? 18.850 11.026 13.541  1.00 69.08  ? 302 UY6 A NAY 1 
HETATM 2121 N NBI . UY6 C 3 .   ? 18.787 12.529 12.001  1.00 68.08  ? 302 UY6 A NBI 1 
HETATM 2122 N NBK . UY6 C 3 .   ? 21.256 13.837 10.936  1.00 67.47  ? 302 UY6 A NBK 1 
HETATM 2123 N NBL . UY6 C 3 .   ? 22.452 12.466 12.453  1.00 67.53  ? 302 UY6 A NBL 1 
HETATM 2124 N NBN . UY6 C 3 .   ? 21.268 10.964 13.851  1.00 67.49  ? 302 UY6 A NBN 1 
HETATM 2125 O OAC . UY6 C 3 .   ? 15.366 11.730 8.191   1.00 69.51  ? 302 UY6 A OAC 1 
HETATM 2126 O OAE . UY6 C 3 .   ? 17.446 10.084 8.572   1.00 69.53  ? 302 UY6 A OAE 1 
HETATM 2127 O OAQ . UY6 C 3 .   ? 14.587 8.579  9.347   1.00 72.14  ? 302 UY6 A OAQ 1 
HETATM 2128 O O   . HOH D 4 .   ? 24.298 8.094  -9.085  1.00 29.72  ? 401 HOH A O   1 
HETATM 2129 O O   . HOH D 4 .   ? 33.073 21.272 13.830  1.00 35.79  ? 402 HOH A O   1 
HETATM 2130 O O   . HOH D 4 .   ? 25.835 9.491  -6.524  1.00 29.94  ? 403 HOH A O   1 
HETATM 2131 O O   . HOH D 4 .   ? 33.515 6.629  -4.818  1.00 24.76  ? 404 HOH A O   1 
HETATM 2132 O O   . HOH D 4 .   ? 13.480 22.462 -6.320  1.00 39.38  ? 405 HOH A O   1 
HETATM 2133 O O   . HOH D 4 .   ? 30.416 9.634  24.988  1.00 48.08  ? 406 HOH A O   1 
HETATM 2134 O O   . HOH D 4 .   ? 25.839 6.347  -3.375  1.00 43.44  ? 407 HOH A O   1 
HETATM 2135 O O   . HOH D 4 .   ? 13.624 10.856 4.487   1.00 29.84  ? 408 HOH A O   1 
HETATM 2136 O O   . HOH D 4 .   ? 20.523 11.513 4.975   1.00 32.39  ? 409 HOH A O   1 
HETATM 2137 O O   . HOH D 4 .   ? 14.823 17.399 20.634  1.00 45.15  ? 410 HOH A O   1 
HETATM 2138 O O   . HOH D 4 .   ? 20.312 26.786 2.519   1.00 30.02  ? 411 HOH A O   1 
HETATM 2139 O O   . HOH D 4 .   ? 21.032 27.550 -4.874  1.00 51.76  ? 412 HOH A O   1 
HETATM 2140 O O   . HOH D 4 .   ? 4.620  19.005 29.347  1.00 43.51  ? 413 HOH A O   1 
HETATM 2141 O O   . HOH D 4 .   ? 23.310 0.557  -1.663  1.00 35.39  ? 414 HOH A O   1 
HETATM 2142 O O   . HOH D 4 .   ? 26.859 21.403 -14.822 1.00 50.42  ? 415 HOH A O   1 
HETATM 2143 O O   . HOH D 4 .   ? 22.358 21.274 6.873   1.00 25.37  ? 416 HOH A O   1 
HETATM 2144 O O   . HOH D 4 .   ? 23.691 5.713  -17.604 1.00 48.15  ? 417 HOH A O   1 
HETATM 2145 O O   . HOH D 4 .   ? 27.981 26.336 -2.797  1.00 40.55  ? 418 HOH A O   1 
HETATM 2146 O O   . HOH D 4 .   ? 29.178 2.260  -10.799 1.00 52.91  ? 419 HOH A O   1 
HETATM 2147 O O   . HOH D 4 .   ? 23.398 7.428  11.340  1.00 55.00  ? 420 HOH A O   1 
HETATM 2148 O O   . HOH D 4 .   ? 2.454  20.471 -11.639 1.00 53.20  ? 421 HOH A O   1 
HETATM 2149 O O   . HOH D 4 .   ? 10.435 26.723 -0.102  1.00 42.08  ? 422 HOH A O   1 
HETATM 2150 O O   . HOH D 4 .   ? 10.248 15.043 9.752   1.00 66.19  ? 423 HOH A O   1 
HETATM 2151 O O   . HOH D 4 .   ? 23.940 5.255  10.322  1.00 51.06  ? 424 HOH A O   1 
HETATM 2152 O O   . HOH D 4 .   ? 18.488 20.193 -14.425 1.00 53.09  ? 425 HOH A O   1 
HETATM 2153 O O   . HOH D 4 .   ? 1.094  39.481 22.465  1.00 77.02  ? 426 HOH A O   1 
HETATM 2154 O O   . HOH D 4 .   ? -0.702 12.723 -6.744  1.00 45.90  ? 427 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 29.688 4.064  7.988   1.00 50.20  ? 428 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 31.564 4.450  -4.282  1.00 37.63  ? 429 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 16.239 10.397 17.904  1.00 47.23  ? 430 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 12.628 11.430 18.862  1.00 41.76  ? 431 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 21.522 25.833 -13.604 1.00 64.45  ? 432 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 25.449 16.740 25.498  1.00 59.36  ? 433 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 25.487 23.062 -17.316 1.00 37.41  ? 434 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 6.376  14.569 0.544   1.00 56.15  ? 435 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 23.570 23.280 16.708  1.00 36.72  ? 436 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 4.542  32.611 5.921   1.00 67.94  ? 437 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 9.052  34.802 5.156   1.00 60.94  ? 438 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 24.373 26.345 -13.413 1.00 49.41  ? 439 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   ? 1.1393 0.7785 0.8820 0.1004  0.1669  -0.3528 1   MET A N   
2    C CA  . MET A 1   ? 1.1311 0.7475 0.8733 0.1333  0.1662  -0.3130 1   MET A CA  
3    C C   . MET A 1   ? 1.0446 0.7526 0.8110 0.1573  0.1386  -0.2875 1   MET A C   
4    O O   . MET A 1   ? 0.8847 0.6663 0.6674 0.1446  0.1225  -0.2965 1   MET A O   
5    C CB  . MET A 1   ? 1.0063 0.5937 0.7563 0.1040  0.1679  -0.3012 1   MET A CB  
6    C CG  . MET A 1   ? 0.9883 0.6590 0.7726 0.0662  0.1407  -0.3024 1   MET A CG  
7    S SD  . MET A 1   ? 1.0063 0.6443 0.8021 0.0296  0.1480  -0.2962 1   MET A SD  
8    C CE  . MET A 1   ? 1.1177 0.6730 0.8955 -0.0067 0.1840  -0.3414 1   MET A CE  
9    N N   . LYS A 2   ? 1.0258 0.7286 0.7921 0.1914  0.1350  -0.2567 2   LYS A N   
10   C CA  . LYS A 2   ? 0.9491 0.7376 0.7413 0.2112  0.1119  -0.2374 2   LYS A CA  
11   C C   . LYS A 2   ? 0.8691 0.7118 0.6892 0.1773  0.0898  -0.2254 2   LYS A C   
12   O O   . LYS A 2   ? 0.8660 0.6759 0.6847 0.1564  0.0906  -0.2184 2   LYS A O   
13   C CB  . LYS A 2   ? 0.9634 0.7370 0.7455 0.2608  0.1139  -0.2136 2   LYS A CB  
14   C CG  . LYS A 2   ? 1.0338 0.7692 0.7904 0.3075  0.1337  -0.2211 2   LYS A CG  
15   C CD  . LYS A 2   ? 1.0684 0.7922 0.8102 0.3629  0.1338  -0.1949 2   LYS A CD  
16   C CE  . LYS A 2   ? 1.1466 0.8456 0.8719 0.4064  0.1499  -0.1953 2   LYS A CE  
17   N NZ  . LYS A 2   ? 1.1161 0.9062 0.8718 0.4169  0.1399  -0.2099 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.8130 0.7356 0.6574 0.1727  0.0737  -0.2227 3   TYR A N   
19   C CA  . TYR A 3   ? 0.7532 0.7221 0.6203 0.1444  0.0562  -0.2107 3   TYR A CA  
20   C C   . TYR A 3   ? 0.7193 0.7595 0.6103 0.1541  0.0454  -0.1997 3   TYR A C   
21   O O   . TYR A 3   ? 0.7414 0.8084 0.6353 0.1771  0.0506  -0.2059 3   TYR A O   
22   C CB  . TYR A 3   ? 0.7438 0.7257 0.6095 0.1102  0.0536  -0.2269 3   TYR A CB  
23   C CG  . TYR A 3   ? 0.7360 0.7704 0.6019 0.1101  0.0520  -0.2369 3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.7932 0.8143 0.6408 0.1226  0.0655  -0.2594 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.6807 0.7722 0.5610 0.0987  0.0408  -0.2232 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.7901 0.8604 0.6343 0.1233  0.0664  -0.2682 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.6818 0.8164 0.5565 0.0993  0.0439  -0.2290 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.7323 0.8595 0.5892 0.1114  0.0560  -0.2516 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.7322 0.9034 0.5800 0.1127  0.0612  -0.2571 3   TYR A OH  
30   N N   . MET A 4   ? 0.6733 0.7437 0.5826 0.1350  0.0331  -0.1852 4   MET A N   
31   C CA  . MET A 4   ? 0.6426 0.7753 0.5758 0.1328  0.0274  -0.1778 4   MET A CA  
32   C C   . MET A 4   ? 0.6100 0.7559 0.5510 0.1039  0.0205  -0.1666 4   MET A C   
33   O O   . MET A 4   ? 0.6130 0.7288 0.5477 0.0914  0.0159  -0.1621 4   MET A O   
34   C CB  . MET A 4   ? 0.6444 0.7990 0.5936 0.1544  0.0220  -0.1705 4   MET A CB  
35   C CG  . MET A 4   ? 0.6549 0.7912 0.6064 0.1481  0.0124  -0.1567 4   MET A CG  
36   S SD  . MET A 4   ? 0.6251 0.8049 0.6035 0.1185  0.0052  -0.1482 4   MET A SD  
37   C CE  . MET A 4   ? 0.6198 0.8722 0.6264 0.1249  0.0095  -0.1591 4   MET A CE  
38   N N   . ILE A 5   ? 0.5869 0.7766 0.5410 0.0946  0.0228  -0.1618 5   ILE A N   
39   C CA  . ILE A 5   ? 0.5681 0.7652 0.5237 0.0732  0.0207  -0.1480 5   ILE A CA  
40   C C   . ILE A 5   ? 0.5650 0.7916 0.5441 0.0658  0.0246  -0.1395 5   ILE A C   
41   O O   . ILE A 5   ? 0.5704 0.8331 0.5630 0.0691  0.0336  -0.1465 5   ILE A O   
42   C CB  . ILE A 5   ? 0.5726 0.7827 0.5086 0.0664  0.0261  -0.1499 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.5986 0.7868 0.5143 0.0697  0.0230  -0.1677 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.5567 0.7687 0.4877 0.0529  0.0241  -0.1314 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.6188 0.8286 0.5114 0.0656  0.0256  -0.1748 5   ILE A CD1 
46   N N   . THR A 6   ? 0.5577 0.7705 0.5432 0.0539  0.0201  -0.1276 6   THR A N   
47   C CA  . THR A 6   ? 0.5557 0.7875 0.5614 0.0399  0.0269  -0.1226 6   THR A CA  
48   C C   . THR A 6   ? 0.5751 0.7917 0.5685 0.0249  0.0366  -0.1056 6   THR A C   
49   O O   . THR A 6   ? 0.5788 0.7741 0.5521 0.0282  0.0308  -0.0964 6   THR A O   
50   C CB  . THR A 6   ? 0.5457 0.7701 0.5647 0.0410  0.0168  -0.1243 6   THR A CB  
51   O OG1 . THR A 6   ? 0.5634 0.8083 0.6038 0.0228  0.0250  -0.1264 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.5301 0.7132 0.5339 0.0398  0.0090  -0.1131 6   THR A CG2 
53   N N   . SER A 7   ? 0.6039 0.8329 0.6092 0.0091  0.0533  -0.1019 7   SER A N   
54   C CA  . SER A 7   ? 0.6437 0.8514 0.6301 -0.0006 0.0697  -0.0821 7   SER A CA  
55   C C   . SER A 7   ? 0.6748 0.8637 0.6757 -0.0201 0.0832  -0.0775 7   SER A C   
56   O O   . SER A 7   ? 0.6633 0.8745 0.6943 -0.0325 0.0843  -0.0952 7   SER A O   
57   C CB  . SER A 7   ? 0.6659 0.8944 0.6406 -0.0026 0.0888  -0.0797 7   SER A CB  
58   O OG  . SER A 7   ? 0.7008 0.9025 0.6521 -0.0098 0.1099  -0.0565 7   SER A OG  
59   N N   . LYS A 8   ? 0.7242 0.8735 0.7021 -0.0210 0.0940  -0.0553 8   LYS A N   
60   C CA  . LYS A 8   ? 0.7622 0.8790 0.7473 -0.0397 0.1131  -0.0503 8   LYS A CA  
61   C C   . LYS A 8   ? 0.8227 0.9510 0.8232 -0.0656 0.1428  -0.0578 8   LYS A C   
62   O O   . LYS A 8   ? 0.8342 0.9572 0.8592 -0.0903 0.1555  -0.0720 8   LYS A O   
63   C CB  . LYS A 8   ? 0.7870 0.8550 0.7380 -0.0272 0.1217  -0.0212 8   LYS A CB  
64   C CG  . LYS A 8   ? 0.8144 0.8325 0.7659 -0.0427 0.1448  -0.0144 8   LYS A CG  
65   C CD  . LYS A 8   ? 0.8741 0.8426 0.7833 -0.0246 0.1635  0.0204  8   LYS A CD  
66   C CE  . LYS A 8   ? 0.9292 0.8352 0.8342 -0.0336 0.1863  0.0279  8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.9064 0.8097 0.8221 -0.0216 0.1626  0.0211  8   LYS A NZ  
68   N N   . GLY A 9   ? 0.8868 1.0332 0.8740 -0.0628 0.1560  -0.0514 9   GLY A N   
69   C CA  . GLY A 9   ? 0.9015 1.0654 0.9055 -0.0890 0.1877  -0.0597 9   GLY A CA  
70   C C   . GLY A 9   ? 0.9526 1.0708 0.9190 -0.0943 0.2250  -0.0307 9   GLY A C   
71   O O   . GLY A 9   ? 0.9842 1.1091 0.9635 -0.1211 0.2590  -0.0361 9   GLY A O   
72   N N   . ASP A 10  ? 0.9463 1.0212 0.8660 -0.0685 0.2216  -0.0001 10  ASP A N   
73   C CA  . ASP A 10  ? 0.9952 1.0215 0.8679 -0.0639 0.2569  0.0335  10  ASP A CA  
74   C C   . ASP A 10  ? 0.9939 1.0501 0.8300 -0.0388 0.2518  0.0459  10  ASP A C   
75   O O   . ASP A 10  ? 0.9452 1.0550 0.7953 -0.0284 0.2230  0.0256  10  ASP A O   
76   C CB  . ASP A 10  ? 1.0165 0.9782 0.8568 -0.0452 0.2588  0.0612  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.9739 0.9576 0.8049 -0.0113 0.2154  0.0636  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.9146 0.9485 0.7769 -0.0125 0.1839  0.0368  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 1.0133 0.9648 0.8059 0.0171  0.2149  0.0920  10  ASP A OD2 
80   N N   . GLU A 11  ? 1.0542 1.0707 0.8380 -0.0275 0.2827  0.0798  11  GLU A N   
81   C CA  . GLU A 11  ? 1.0638 1.1089 0.8045 -0.0028 0.2811  0.0922  11  GLU A CA  
82   C C   . GLU A 11  ? 1.0178 1.0945 0.7417 0.0318  0.2353  0.0898  11  GLU A C   
83   O O   . GLU A 11  ? 0.9978 1.1245 0.7164 0.0421  0.2170  0.0737  11  GLU A O   
84   C CB  . GLU A 11  ? 1.1570 1.1464 0.8354 0.0082  0.3242  0.1345  11  GLU A CB  
85   C CG  . GLU A 11  ? 1.1908 1.1803 0.8682 -0.0193 0.3706  0.1346  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.2919 1.2026 0.9086 -0.0145 0.4232  0.1794  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.3254 1.1674 0.9274 -0.0095 0.4348  0.2006  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.3431 1.2564 0.9233 -0.0137 0.4557  0.1946  11  GLU A OE2 
89   N N   . LYS A 12  ? 1.0029 1.0525 0.7204 0.0482  0.2185  0.1024  12  LYS A N   
90   C CA  . LYS A 12  ? 0.9671 1.0511 0.6698 0.0786  0.1791  0.0999  12  LYS A CA  
91   C C   . LYS A 12  ? 0.8852 1.0154 0.6345 0.0668  0.1452  0.0604  12  LYS A C   
92   O O   . LYS A 12  ? 0.8624 1.0349 0.6015 0.0805  0.1213  0.0461  12  LYS A O   
93   C CB  . LYS A 12  ? 0.9851 1.0328 0.6749 0.0990  0.1734  0.1227  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.9997 1.0810 0.6525 0.1393  0.1471  0.1354  12  LYS A CG  
95   C CD  . LYS A 12  ? 1.0428 1.0812 0.6719 0.1667  0.1545  0.1680  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.9952 1.0769 0.6437 0.1857  0.1152  0.1557  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.9914 1.1465 0.6166 0.2099  0.0865  0.1474  12  LYS A NZ  
98   N N   . SER A 13  ? 0.8514 0.9725 0.6488 0.0421  0.1446  0.0416  13  SER A N   
99   C CA  . SER A 13  ? 0.7856 0.9393 0.6202 0.0366  0.1152  0.0098  13  SER A CA  
100  C C   . SER A 13  ? 0.7744 0.9651 0.6223 0.0287  0.1179  -0.0130 13  SER A C   
101  O O   . SER A 13  ? 0.7470 0.9642 0.5991 0.0369  0.0963  -0.0335 13  SER A O   
102  C CB  . SER A 13  ? 0.7474 0.8805 0.6210 0.0201  0.1117  0.0003  13  SER A CB  
103  O OG  . SER A 13  ? 0.7705 0.8667 0.6319 0.0288  0.1126  0.0205  13  SER A OG  
104  N N   . ASP A 14  ? 0.7942 0.9861 0.6498 0.0121  0.1471  -0.0115 14  ASP A N   
105  C CA  . ASP A 14  ? 0.7670 1.0009 0.6397 0.0070  0.1516  -0.0341 14  ASP A CA  
106  C C   . ASP A 14  ? 0.7771 1.0326 0.6103 0.0267  0.1476  -0.0343 14  ASP A C   
107  O O   . ASP A 14  ? 0.7555 1.0407 0.5982 0.0336  0.1341  -0.0590 14  ASP A O   
108  C CB  . ASP A 14  ? 0.7833 1.0218 0.6748 -0.0176 0.1876  -0.0332 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.7588 1.0034 0.7025 -0.0401 0.1863  -0.0514 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.7207 0.9619 0.6804 -0.0329 0.1578  -0.0611 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.7813 1.0374 0.7496 -0.0663 0.2149  -0.0578 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.8209 1.0603 0.6056 0.0386  0.1599  -0.0075 15  LEU A N   
113  C CA  . LEU A 15  ? 0.8437 1.1098 0.5850 0.0581  0.1560  -0.0091 15  LEU A CA  
114  C C   . LEU A 15  ? 0.8071 1.0889 0.5384 0.0747  0.1193  -0.0235 15  LEU A C   
115  O O   . LEU A 15  ? 0.8144 1.1267 0.5222 0.0855  0.1102  -0.0406 15  LEU A O   
116  C CB  . LEU A 15  ? 0.9175 1.1641 0.6035 0.0694  0.1835  0.0268  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.9514 1.1777 0.6448 0.0472  0.2283  0.0402  15  LEU A CG  
118  C CD1 . LEU A 15  ? 1.0502 1.2506 0.6773 0.0621  0.2604  0.0782  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.9095 1.1794 0.6390 0.0315  0.2366  0.0092  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.7700 1.0336 0.5195 0.0746  0.1003  -0.0199 16  LEU A N   
121  C CA  . LEU A 16  ? 0.7305 1.0127 0.4841 0.0820  0.0683  -0.0404 16  LEU A CA  
122  C C   . LEU A 16  ? 0.6748 0.9609 0.4657 0.0700  0.0581  -0.0735 16  LEU A C   
123  O O   . LEU A 16  ? 0.6618 0.9636 0.4487 0.0728  0.0414  -0.0984 16  LEU A O   
124  C CB  . LEU A 16  ? 0.7128 0.9774 0.4742 0.0869  0.0551  -0.0247 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.6808 0.9664 0.4557 0.0887  0.0255  -0.0467 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.6892 1.0206 0.4304 0.1018  0.0120  -0.0608 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.6820 0.9532 0.4681 0.0944  0.0172  -0.0292 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.6465 0.9184 0.4718 0.0576  0.0692  -0.0752 17  ARG A N   
129  C CA  . ARG A 17  ? 0.6127 0.8879 0.4673 0.0546  0.0617  -0.1021 17  ARG A CA  
130  C C   . ARG A 17  ? 0.6434 0.9422 0.4833 0.0622  0.0687  -0.1222 17  ARG A C   
131  O O   . ARG A 17  ? 0.6428 0.9387 0.4855 0.0673  0.0585  -0.1467 17  ARG A O   
132  C CB  . ARG A 17  ? 0.5744 0.8439 0.4664 0.0441  0.0709  -0.0998 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.5484 0.8299 0.4660 0.0495  0.0667  -0.1235 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.5291 0.8200 0.4841 0.0409  0.0717  -0.1234 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.5177 0.8298 0.4941 0.0543  0.0675  -0.1437 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.5299 0.8817 0.5189 0.0595  0.0811  -0.1554 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.5535 0.9248 0.5349 0.0479  0.1021  -0.1490 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.5224 0.8943 0.5293 0.0792  0.0757  -0.1722 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.6716 0.9888 0.4928 0.0630  0.0899  -0.1121 18  LEU A N   
140  C CA  . LEU A 18  ? 0.6968 1.0391 0.5018 0.0715  0.0995  -0.1315 18  LEU A CA  
141  C C   . LEU A 18  ? 0.7174 1.0670 0.4834 0.0813  0.0850  -0.1462 18  LEU A C   
142  O O   . LEU A 18  ? 0.7342 1.0924 0.4928 0.0875  0.0847  -0.1744 18  LEU A O   
143  C CB  . LEU A 18  ? 0.7300 1.0909 0.5227 0.0680  0.1297  -0.1156 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.7086 1.0781 0.5461 0.0531  0.1487  -0.1125 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.7343 1.1189 0.5567 0.0443  0.1843  -0.0969 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.6897 1.0817 0.5639 0.0604  0.1424  -0.1415 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.7246 1.0742 0.4655 0.0838  0.0733  -0.1302 19  ASN A N   
148  C CA  . ASN A 19  ? 0.7525 1.1238 0.4602 0.0913  0.0563  -0.1494 19  ASN A CA  
149  C C   . ASN A 19  ? 0.7372 1.0950 0.4693 0.0825  0.0374  -0.1814 19  ASN A C   
150  O O   . ASN A 19  ? 0.7713 1.1415 0.4865 0.0821  0.0312  -0.2138 19  ASN A O   
151  C CB  . ASN A 19  ? 0.7709 1.1561 0.4484 0.1015  0.0468  -0.1235 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.8275 1.2284 0.4562 0.1166  0.0667  -0.0985 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.8768 1.2921 0.4864 0.1189  0.0822  -0.1105 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.8361 1.2307 0.4405 0.1295  0.0691  -0.0622 19  ASN A ND2 
155  N N   . MET A 20  ? 0.6925 1.0214 0.4615 0.0740  0.0310  -0.1741 20  MET A N   
156  C CA  . MET A 20  ? 0.6786 0.9849 0.4677 0.0650  0.0194  -0.2007 20  MET A CA  
157  C C   . MET A 20  ? 0.6844 0.9694 0.4808 0.0688  0.0315  -0.2236 20  MET A C   
158  O O   . MET A 20  ? 0.7133 0.9807 0.5044 0.0646  0.0294  -0.2542 20  MET A O   
159  C CB  . MET A 20  ? 0.6508 0.9315 0.4713 0.0580  0.0120  -0.1838 20  MET A CB  
160  C CG  . MET A 20  ? 0.6694 0.9684 0.4846 0.0578  -0.0005 -0.1650 20  MET A CG  
161  S SD  . MET A 20  ? 0.6609 0.9299 0.5118 0.0487  -0.0086 -0.1539 20  MET A SD  
162  C CE  . MET A 20  ? 0.6644 0.9132 0.5272 0.0347  -0.0134 -0.1916 20  MET A CE  
163  N N   . ILE A 21  ? 0.6664 0.9534 0.4756 0.0771  0.0462  -0.2109 21  ILE A N   
164  C CA  . ILE A 21  ? 0.6789 0.9553 0.4945 0.0887  0.0582  -0.2309 21  ILE A CA  
165  C C   . ILE A 21  ? 0.7192 1.0106 0.5012 0.0942  0.0657  -0.2568 21  ILE A C   
166  O O   . ILE A 21  ? 0.7511 1.0171 0.5272 0.1004  0.0705  -0.2852 21  ILE A O   
167  C CB  . ILE A 21  ? 0.6615 0.9572 0.5028 0.0960  0.0714  -0.2146 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.6209 0.9012 0.4945 0.0906  0.0627  -0.1970 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.6891 0.9885 0.5359 0.1150  0.0842  -0.2352 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.5513 0.8602 0.4557 0.0933  0.0735  -0.1879 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.7295 1.0578 0.4840 0.0938  0.0689  -0.2472 22  ALA A N   
172  C CA  . ALA A 22  ? 0.7773 1.1256 0.4932 0.0994  0.0746  -0.2730 22  ALA A CA  
173  C C   . ALA A 22  ? 0.7996 1.1377 0.5002 0.0886  0.0581  -0.3045 22  ALA A C   
174  O O   . ALA A 22  ? 0.8421 1.1719 0.5244 0.0895  0.0638  -0.3399 22  ALA A O   
175  C CB  . ALA A 22  ? 0.7578 1.1469 0.4405 0.1039  0.0821  -0.2509 22  ALA A CB  
176  N N   . GLY A 23  ? 0.7770 1.1163 0.4877 0.0765  0.0394  -0.2943 23  GLY A N   
177  C CA  . GLY A 23  ? 0.7951 1.1309 0.5021 0.0605  0.0252  -0.3280 23  GLY A CA  
178  C C   . GLY A 23  ? 0.8040 1.0800 0.5322 0.0523  0.0339  -0.3526 23  GLY A C   
179  O O   . GLY A 23  ? 0.8424 1.1008 0.5607 0.0396  0.0360  -0.3901 23  GLY A O   
180  N N   . PHE A 24  ? 0.7760 1.0151 0.5327 0.0597  0.0405  -0.3290 24  PHE A N   
181  C CA  . PHE A 24  ? 0.7994 0.9755 0.5676 0.0612  0.0525  -0.3453 24  PHE A CA  
182  C C   . PHE A 24  ? 0.8476 1.0067 0.5967 0.0789  0.0717  -0.3684 24  PHE A C   
183  O O   . PHE A 24  ? 0.8945 0.9960 0.6380 0.0802  0.0849  -0.3931 24  PHE A O   
184  C CB  . PHE A 24  ? 0.7622 0.9143 0.5600 0.0710  0.0525  -0.3127 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.7407 0.8831 0.5568 0.0534  0.0393  -0.2996 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.7735 0.8875 0.5886 0.0323  0.0387  -0.3244 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.6898 0.8518 0.5254 0.0558  0.0304  -0.2653 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.7509 0.8619 0.5856 0.0161  0.0290  -0.3132 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.6663 0.8201 0.5177 0.0422  0.0200  -0.2541 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.6956 0.8270 0.5475 0.0233  0.0190  -0.2771 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.8427 1.0467 0.5800 0.0935  0.0772  -0.3603 25  GLY A N   
192  C CA  . GLY A 25  ? 0.8928 1.0884 0.6126 0.1117  0.0964  -0.3822 25  GLY A CA  
193  C C   . GLY A 25  ? 0.9643 1.1353 0.6580 0.0970  0.0983  -0.4141 25  GLY A C   
194  O O   . GLY A 25  ? 1.0000 1.1372 0.6809 0.1097  0.1158  -0.4313 25  GLY A O   
195  N N   . GLU A 26  ? 0.9828 1.1736 0.6696 0.0716  0.0809  -0.4231 26  GLU A N   
196  C CA  . GLU A 26  ? 1.0427 1.2183 0.7108 0.0527  0.0800  -0.4571 26  GLU A CA  
197  C C   . GLU A 26  ? 1.0693 1.1781 0.7500 0.0327  0.0853  -0.4790 26  GLU A C   
198  O O   . GLU A 26  ? 1.0976 1.1997 0.7714 0.0082  0.0822  -0.5082 26  GLU A O   
199  C CB  . GLU A 26  ? 1.0276 1.2723 0.6849 0.0384  0.0576  -0.4562 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.9961 1.2994 0.6347 0.0581  0.0551  -0.4279 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.9854 1.2812 0.6023 0.0761  0.0757  -0.4341 26  GLU A CD  
202  O OE1 . GLU A 26  ? 0.9599 1.2722 0.5792 0.0949  0.0873  -0.4079 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 1.0459 1.3203 0.6447 0.0703  0.0820  -0.4663 26  GLU A OE2 
204  N N   . TYR A 27  ? 1.0684 1.1292 0.7673 0.0424  0.0946  -0.4653 27  TYR A N   
205  C CA  . TYR A 27  ? 1.1123 1.1000 0.8198 0.0254  0.1049  -0.4796 27  TYR A CA  
206  C C   . TYR A 27  ? 1.1615 1.0757 0.8653 0.0563  0.1285  -0.4703 27  TYR A C   
207  O O   . TYR A 27  ? 1.1394 1.0743 0.8439 0.0894  0.1327  -0.4528 27  TYR A O   
208  C CB  . TYR A 27  ? 1.0416 1.0492 0.7763 0.0036  0.0889  -0.4676 27  TYR A CB  
209  C CG  . TYR A 27  ? 1.0100 1.0876 0.7510 -0.0239 0.0659  -0.4783 27  TYR A CG  
210  C CD1 . TYR A 27  ? 1.0463 1.1119 0.7940 -0.0570 0.0668  -0.5088 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.9520 1.1099 0.6928 -0.0144 0.0448  -0.4565 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.9779 1.1207 0.7364 -0.0776 0.0445  -0.5196 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.9403 1.1649 0.6843 -0.0308 0.0235  -0.4628 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.9746 1.1971 0.7300 -0.0613 0.0220  -0.4954 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.9683 1.2694 0.7319 -0.0733 -0.0002 -0.5030 27  TYR A OH  
216  N N   . ASP A 28  ? 1.2402 1.0709 0.9412 0.0471  0.1447  -0.4801 28  ASP A N   
217  C CA  . ASP A 28  ? 1.3125 1.0654 1.0056 0.0819  0.1673  -0.4665 28  ASP A CA  
218  C C   . ASP A 28  ? 1.2965 1.0593 1.0146 0.0913  0.1601  -0.4370 28  ASP A C   
219  O O   . ASP A 28  ? 1.3212 1.0237 1.0422 0.0823  0.1696  -0.4288 28  ASP A O   
220  C CB  . ASP A 28  ? 1.4120 1.0685 1.0882 0.0707  0.1887  -0.4847 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.4759 1.0549 1.1387 0.1167  0.2111  -0.4688 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.4573 1.0126 1.1311 0.1324  0.2137  -0.4403 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 1.5482 1.0959 1.1911 0.1393  0.2249  -0.4840 28  ASP A OD2 
224  N N   . MET A 29  ? 1.2753 1.1164 1.0113 0.1086  0.1404  -0.4101 29  MET A N   
225  C CA  . MET A 29  ? 1.2288 1.0925 0.9906 0.1184  0.1250  -0.3682 29  MET A CA  
226  C C   . MET A 29  ? 1.2056 1.1081 0.9765 0.1585  0.1237  -0.3465 29  MET A C   
227  O O   . MET A 29  ? 1.1961 1.1535 0.9661 0.1642  0.1223  -0.3543 29  MET A O   
228  C CB  . MET A 29  ? 1.1823 1.1127 0.9643 0.0877  0.1000  -0.3570 29  MET A CB  
229  C CG  . MET A 29  ? 1.2200 1.1288 1.0042 0.0491  0.0981  -0.3756 29  MET A CG  
230  S SD  . MET A 29  ? 1.2570 1.1036 1.0544 0.0457  0.1041  -0.3510 29  MET A SD  
231  C CE  . MET A 29  ? 1.1714 1.0892 0.9964 0.0554  0.0775  -0.3077 29  MET A CE  
232  N N   . GLU A 30  ? 1.1771 1.0566 0.9566 0.1861  0.1249  -0.3209 30  GLU A N   
233  C CA  . GLU A 30  ? 1.1245 1.0480 0.9182 0.2257  0.1232  -0.3043 30  GLU A CA  
234  C C   . GLU A 30  ? 1.0263 1.0070 0.8517 0.2192  0.1018  -0.2749 30  GLU A C   
235  O O   . GLU A 30  ? 1.0253 0.9754 0.8531 0.2135  0.0955  -0.2586 30  GLU A O   
236  C CB  . GLU A 30  ? 1.1789 1.0377 0.9535 0.2711  0.1414  -0.3010 30  GLU A CB  
237  C CG  . GLU A 30  ? 1.1677 1.0846 0.9621 0.3164  0.1361  -0.2841 30  GLU A CG  
238  C CD  . GLU A 30  ? 1.2554 1.1111 1.0302 0.3636  0.1504  -0.2721 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.2516 1.1609 1.0465 0.3988  0.1421  -0.2551 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 1.3315 1.0900 1.0757 0.3584  0.1692  -0.2768 30  GLU A OE2 
241  N N   . TYR A 31  ? 0.9476 1.0076 0.7958 0.2184  0.0941  -0.2696 31  TYR A N   
242  C CA  . TYR A 31  ? 0.8640 0.9756 0.7431 0.2112  0.0782  -0.2463 31  TYR A CA  
243  C C   . TYR A 31  ? 0.8749 0.9952 0.7665 0.2493  0.0765  -0.2354 31  TYR A C   
244  O O   . TYR A 31  ? 0.9306 1.0697 0.8234 0.2839  0.0860  -0.2438 31  TYR A O   
245  C CB  . TYR A 31  ? 0.8037 0.9896 0.7013 0.1959  0.0770  -0.2452 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.7380 0.9659 0.6649 0.1785  0.0650  -0.2247 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.7160 0.9916 0.6735 0.1947  0.0625  -0.2193 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.7070 0.9294 0.6312 0.1470  0.0567  -0.2135 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.6699 0.9800 0.6538 0.1744  0.0541  -0.2064 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.6649 0.9149 0.6125 0.1317  0.0497  -0.1963 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.6497 0.9403 0.6268 0.1428  0.0494  -0.1943 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.6215 0.9363 0.6216 0.1233  0.0449  -0.1828 31  TYR A OH  
253  N N   . ASP A 32  ? 0.8195 0.9313 0.7193 0.2460  0.0641  -0.2174 32  ASP A N   
254  C CA  . ASP A 32  ? 0.8174 0.9421 0.7238 0.2844  0.0589  -0.2065 32  ASP A CA  
255  C C   . ASP A 32  ? 0.7889 0.9295 0.7106 0.2661  0.0421  -0.1899 32  ASP A C   
256  O O   . ASP A 32  ? 0.8013 0.8861 0.7061 0.2477  0.0412  -0.1816 32  ASP A O   
257  C CB  . ASP A 32  ? 0.8867 0.9280 0.7547 0.3204  0.0727  -0.2051 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.9261 0.9886 0.7935 0.3745  0.0687  -0.1938 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.8876 1.0262 0.7856 0.3766  0.0506  -0.1873 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 1.0085 1.0111 0.8427 0.4165  0.0846  -0.1925 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.7551 0.9737 0.7103 0.2690  0.0309  -0.1884 33  ASP A N   
262  C CA  . ASP A 33  ? 0.7165 0.9540 0.6861 0.2535  0.0159  -0.1772 33  ASP A CA  
263  C C   . ASP A 33  ? 0.7361 0.9850 0.6997 0.2950  0.0062  -0.1704 33  ASP A C   
264  O O   . ASP A 33  ? 0.7094 0.9962 0.6892 0.2876  -0.0078 -0.1671 33  ASP A O   
265  C CB  . ASP A 33  ? 0.6564 0.9681 0.6656 0.2218  0.0121  -0.1833 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.6432 1.0336 0.6819 0.2387  0.0167  -0.1985 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.6738 1.0684 0.7035 0.2818  0.0189  -0.2033 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.6075 1.0540 0.6781 0.2095  0.0209  -0.2054 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.7908 1.0057 0.7271 0.3409  0.0144  -0.1686 34  VAL A N   
270  C CA  . VAL A 34  ? 0.8331 1.0514 0.7519 0.3904  0.0066  -0.1574 34  VAL A CA  
271  C C   . VAL A 34  ? 0.8810 0.9934 0.7513 0.3960  0.0159  -0.1383 34  VAL A C   
272  O O   . VAL A 34  ? 0.8806 0.9887 0.7408 0.3974  0.0056  -0.1252 34  VAL A O   
273  C CB  . VAL A 34  ? 0.8854 1.1321 0.8005 0.4471  0.0125  -0.1636 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.9293 1.1727 0.8163 0.4973  0.0026  -0.1449 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.8506 1.2116 0.8194 0.4380  0.0061  -0.1846 34  VAL A CG2 
276  N N   . GLU A 35  ? 0.9326 0.9591 0.7724 0.3966  0.0378  -0.1391 35  GLU A N   
277  C CA  . GLU A 35  ? 0.9853 0.9046 0.7821 0.3923  0.0542  -0.1251 35  GLU A CA  
278  C C   . GLU A 35  ? 0.9673 0.8434 0.7684 0.3385  0.0657  -0.1387 35  GLU A C   
279  O O   . GLU A 35  ? 1.0261 0.8300 0.8017 0.3393  0.0881  -0.1477 35  GLU A O   
280  C CB  . GLU A 35  ? 1.0867 0.9305 0.8356 0.4483  0.0756  -0.1149 35  GLU A CB  
281  C CG  . GLU A 35  ? 1.1169 1.0157 0.8609 0.5033  0.0613  -0.0994 35  GLU A CG  
282  C CD  . GLU A 35  ? 1.2342 1.0518 0.9281 0.5413  0.0813  -0.0785 35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.2927 1.0371 0.9432 0.5510  0.0924  -0.0549 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.2798 1.1047 0.9759 0.5613  0.0884  -0.0853 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.8845 0.8035 0.7160 0.2925  0.0515  -0.1423 36  PRO A N   
286  C CA  . PRO A 36  ? 0.8708 0.7608 0.7054 0.2465  0.0590  -0.1548 36  PRO A CA  
287  C C   . PRO A 36  ? 0.8912 0.7060 0.7037 0.2283  0.0710  -0.1470 36  PRO A C   
288  O O   . PRO A 36  ? 0.8966 0.6950 0.6978 0.2404  0.0688  -0.1282 36  PRO A O   
289  C CB  . PRO A 36  ? 0.7962 0.7632 0.6683 0.2144  0.0401  -0.1565 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.7673 0.7711 0.6501 0.2292  0.0258  -0.1419 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.8187 0.8151 0.6818 0.2814  0.0292  -0.1367 36  PRO A CD  
292  N N   . GLU A 37  ? 0.9021 0.6755 0.7088 0.1977  0.0850  -0.1643 37  GLU A N   
293  C CA  . GLU A 37  ? 0.9067 0.6224 0.7034 0.1683  0.0981  -0.1639 37  GLU A CA  
294  C C   . GLU A 37  ? 0.8444 0.6101 0.6723 0.1240  0.0832  -0.1712 37  GLU A C   
295  O O   . GLU A 37  ? 0.8378 0.5799 0.6676 0.1010  0.0886  -0.1671 37  GLU A O   
296  C CB  . GLU A 37  ? 0.9714 0.6043 0.7413 0.1615  0.1278  -0.1832 37  GLU A CB  
297  C CG  . GLU A 37  ? 1.0510 0.6068 0.7793 0.2089  0.1506  -0.1697 37  GLU A CG  
298  C CD  . GLU A 37  ? 1.1417 0.6214 0.8443 0.2079  0.1806  -0.1937 37  GLU A CD  
299  O OE1 . GLU A 37  ? 1.1271 0.6432 0.8459 0.1882  0.1751  -0.2216 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 1.2380 0.6172 0.9002 0.2273  0.2120  -0.1848 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.7971 0.6311 0.6473 0.1148  0.0666  -0.1801 38  ILE A N   
302  C CA  . ILE A 38  ? 0.7391 0.6237 0.6137 0.0826  0.0518  -0.1827 38  ILE A CA  
303  C C   . ILE A 38  ? 0.6758 0.6253 0.5692 0.0922  0.0342  -0.1692 38  ILE A C   
304  O O   . ILE A 38  ? 0.6589 0.6374 0.5537 0.1066  0.0330  -0.1743 38  ILE A O   
305  C CB  . ILE A 38  ? 0.7465 0.6439 0.6218 0.0584  0.0540  -0.2095 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.7979 0.6291 0.6577 0.0418  0.0756  -0.2301 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.7009 0.6568 0.5971 0.0349  0.0371  -0.2077 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.7930 0.6015 0.6614 0.0197  0.0810  -0.2238 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.6417 0.6120 0.5497 0.0826  0.0239  -0.1541 39  VAL A N   
310  C CA  . VAL A 39  ? 0.5992 0.6219 0.5255 0.0845  0.0118  -0.1435 39  VAL A CA  
311  C C   . VAL A 39  ? 0.5760 0.6260 0.5135 0.0610  0.0054  -0.1412 39  VAL A C   
312  O O   . VAL A 39  ? 0.5702 0.6086 0.5113 0.0481  0.0037  -0.1369 39  VAL A O   
313  C CB  . VAL A 39  ? 0.5818 0.6039 0.5117 0.0970  0.0068  -0.1293 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.5335 0.6023 0.4848 0.0870  -0.0021 -0.1230 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.6135 0.6280 0.5314 0.1295  0.0096  -0.1299 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.5648 0.6519 0.5058 0.0585  0.0035  -0.1428 40  ILE A N   
317  C CA  . ILE A 40  ? 0.5564 0.6695 0.4996 0.0448  -0.0013 -0.1370 40  ILE A CA  
318  C C   . ILE A 40  ? 0.5347 0.6678 0.4888 0.0445  -0.0011 -0.1202 40  ILE A C   
319  O O   . ILE A 40  ? 0.5328 0.6831 0.4925 0.0498  0.0040  -0.1211 40  ILE A O   
320  C CB  . ILE A 40  ? 0.5839 0.7182 0.5131 0.0431  0.0003  -0.1501 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.6093 0.7186 0.5285 0.0385  0.0034  -0.1734 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.5858 0.7503 0.5103 0.0367  -0.0056 -0.1402 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.6291 0.7596 0.5318 0.0366  0.0050  -0.1929 40  ILE A CD1 
324  N N   . SER A 41  ? 0.5303 0.6614 0.4890 0.0375  -0.0043 -0.1072 41  SER A N   
325  C CA  . SER A 41  ? 0.5386 0.6755 0.5045 0.0341  0.0004  -0.0925 41  SER A CA  
326  C C   . SER A 41  ? 0.5342 0.6825 0.4874 0.0334  0.0036  -0.0795 41  SER A C   
327  O O   . SER A 41  ? 0.5269 0.6800 0.4737 0.0358  -0.0038 -0.0776 41  SER A O   
328  C CB  . SER A 41  ? 0.5594 0.6766 0.5351 0.0318  -0.0023 -0.0865 41  SER A CB  
329  O OG  . SER A 41  ? 0.5833 0.6987 0.5641 0.0257  0.0051  -0.0756 41  SER A OG  
330  N N   . ILE A 42  ? 0.5409 0.6964 0.4899 0.0313  0.0160  -0.0706 42  ILE A N   
331  C CA  . ILE A 42  ? 0.5638 0.7230 0.4912 0.0360  0.0237  -0.0527 42  ILE A CA  
332  C C   . ILE A 42  ? 0.5803 0.7150 0.5104 0.0293  0.0407  -0.0359 42  ILE A C   
333  O O   . ILE A 42  ? 0.5672 0.7022 0.5093 0.0167  0.0545  -0.0408 42  ILE A O   
334  C CB  . ILE A 42  ? 0.5847 0.7670 0.4936 0.0396  0.0305  -0.0563 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.5828 0.7830 0.4875 0.0439  0.0162  -0.0781 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.6229 0.8061 0.5005 0.0496  0.0403  -0.0331 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.6131 0.8371 0.4960 0.0489  0.0224  -0.0855 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.6188 0.7338 0.5394 0.0372  0.0414  -0.0187 43  GLY A N   
339  C CA  . GLY A 43  ? 0.6630 0.7417 0.5818 0.0315  0.0612  -0.0034 43  GLY A CA  
340  C C   . GLY A 43  ? 0.6728 0.7296 0.5928 0.0412  0.0562  0.0057  43  GLY A C   
341  O O   . GLY A 43  ? 0.6876 0.7471 0.5885 0.0620  0.0527  0.0225  43  GLY A O   
342  N N   . GLY A 44  ? 0.6539 0.6948 0.5953 0.0289  0.0554  -0.0062 44  GLY A N   
343  C CA  . GLY A 44  ? 0.6564 0.6781 0.6005 0.0375  0.0520  -0.0008 44  GLY A CA  
344  C C   . GLY A 44  ? 0.6402 0.6712 0.6054 0.0299  0.0373  -0.0204 44  GLY A C   
345  O O   . GLY A 44  ? 0.6216 0.6737 0.5964 0.0227  0.0280  -0.0360 44  GLY A O   
346  N N   . ASP A 45  ? 0.6589 0.6722 0.6278 0.0348  0.0372  -0.0183 45  ASP A N   
347  C CA  . ASP A 45  ? 0.6408 0.6575 0.6227 0.0290  0.0273  -0.0341 45  ASP A CA  
348  C C   . ASP A 45  ? 0.6254 0.6381 0.6150 0.0132  0.0310  -0.0501 45  ASP A C   
349  O O   . ASP A 45  ? 0.6091 0.6354 0.6041 0.0123  0.0201  -0.0633 45  ASP A O   
350  C CB  . ASP A 45  ? 0.6545 0.6549 0.6369 0.0381  0.0297  -0.0285 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.6493 0.6749 0.6344 0.0523  0.0208  -0.0212 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.6401 0.6938 0.6282 0.0498  0.0099  -0.0274 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.6551 0.6758 0.6408 0.0657  0.0254  -0.0119 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.6363 0.6320 0.6255 0.0013  0.0477  -0.0499 46  GLY A N   
355  C CA  . GLY A 46  ? 0.6308 0.6388 0.6340 -0.0175 0.0505  -0.0710 46  GLY A CA  
356  C C   . GLY A 46  ? 0.6195 0.6687 0.6320 -0.0183 0.0407  -0.0804 46  GLY A C   
357  O O   . GLY A 46  ? 0.6204 0.6977 0.6446 -0.0204 0.0304  -0.0988 46  GLY A O   
358  N N   . THR A 47  ? 0.6143 0.6699 0.6190 -0.0129 0.0438  -0.0681 47  THR A N   
359  C CA  . THR A 47  ? 0.5843 0.6760 0.5951 -0.0097 0.0356  -0.0772 47  THR A CA  
360  C C   . THR A 47  ? 0.5545 0.6548 0.5624 0.0058  0.0165  -0.0823 47  THR A C   
361  O O   . THR A 47  ? 0.5386 0.6629 0.5529 0.0115  0.0091  -0.0948 47  THR A O   
362  C CB  . THR A 47  ? 0.5951 0.6893 0.5919 -0.0062 0.0443  -0.0636 47  THR A CB  
363  O OG1 . THR A 47  ? 0.6480 0.7231 0.6414 -0.0200 0.0682  -0.0548 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.5637 0.6938 0.5661 -0.0028 0.0391  -0.0755 47  THR A CG2 
365  N N   . PHE A 48  ? 0.5556 0.6357 0.5536 0.0137  0.0112  -0.0727 48  PHE A N   
366  C CA  . PHE A 48  ? 0.5479 0.6263 0.5418 0.0236  0.0000  -0.0773 48  PHE A CA  
367  C C   . PHE A 48  ? 0.5415 0.6180 0.5371 0.0271  -0.0047 -0.0863 48  PHE A C   
368  O O   . PHE A 48  ? 0.5488 0.6279 0.5381 0.0387  -0.0108 -0.0917 48  PHE A O   
369  C CB  . PHE A 48  ? 0.5531 0.6186 0.5423 0.0265  -0.0014 -0.0681 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.5554 0.6145 0.5410 0.0302  -0.0065 -0.0741 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.5646 0.6051 0.5467 0.0330  -0.0059 -0.0750 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.5570 0.6249 0.5396 0.0294  -0.0087 -0.0799 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.5765 0.6007 0.5515 0.0345  -0.0039 -0.0784 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.5704 0.6229 0.5494 0.0278  -0.0074 -0.0879 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.5821 0.6093 0.5569 0.0301  -0.0032 -0.0855 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.5321 0.6016 0.5317 0.0197  -0.0007 -0.0881 49  LEU A N   
377  C CA  . LEU A 49  ? 0.5227 0.5981 0.5200 0.0241  -0.0069 -0.0991 49  LEU A CA  
378  C C   . LEU A 49  ? 0.5236 0.6377 0.5297 0.0282  -0.0135 -0.1140 49  LEU A C   
379  O O   . LEU A 49  ? 0.5398 0.6660 0.5364 0.0452  -0.0233 -0.1194 49  LEU A O   
380  C CB  . LEU A 49  ? 0.5337 0.5960 0.5338 0.0121  0.0004  -0.1037 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.5509 0.5875 0.5375 0.0192  0.0008  -0.0982 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.5415 0.5609 0.5245 0.0256  0.0033  -0.0813 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.5836 0.6031 0.5721 0.0073  0.0113  -0.1052 49  LEU A CD2 
384  N N   . SER A 50  ? 0.5143 0.6507 0.5372 0.0153  -0.0068 -0.1197 50  SER A N   
385  C CA  . SER A 50  ? 0.5090 0.6940 0.5467 0.0197  -0.0121 -0.1357 50  SER A CA  
386  C C   . SER A 50  ? 0.5141 0.7018 0.5399 0.0448  -0.0196 -0.1306 50  SER A C   
387  O O   . SER A 50  ? 0.5271 0.7450 0.5528 0.0648  -0.0291 -0.1398 50  SER A O   
388  C CB  . SER A 50  ? 0.5042 0.7096 0.5630 -0.0029 0.0025  -0.1422 50  SER A CB  
389  O OG  . SER A 50  ? 0.5207 0.7149 0.5891 -0.0277 0.0146  -0.1496 50  SER A OG  
390  N N   . ALA A 51  ? 0.5073 0.6643 0.5211 0.0458  -0.0148 -0.1174 51  ALA A N   
391  C CA  . ALA A 51  ? 0.5184 0.6662 0.5182 0.0657  -0.0177 -0.1159 51  ALA A CA  
392  C C   . ALA A 51  ? 0.5544 0.6743 0.5333 0.0849  -0.0228 -0.1113 51  ALA A C   
393  O O   . ALA A 51  ? 0.5780 0.6928 0.5433 0.1084  -0.0240 -0.1123 51  ALA A O   
394  C CB  . ALA A 51  ? 0.5073 0.6327 0.4994 0.0577  -0.0116 -0.1086 51  ALA A CB  
395  N N   . PHE A 52  ? 0.5608 0.6584 0.5332 0.0776  -0.0228 -0.1048 52  PHE A N   
396  C CA  . PHE A 52  ? 0.5787 0.6468 0.5267 0.0950  -0.0234 -0.0981 52  PHE A CA  
397  C C   . PHE A 52  ? 0.5947 0.6931 0.5352 0.1178  -0.0333 -0.1047 52  PHE A C   
398  O O   . PHE A 52  ? 0.6219 0.7066 0.5384 0.1467  -0.0337 -0.0992 52  PHE A O   
399  C CB  . PHE A 52  ? 0.5696 0.6129 0.5144 0.0811  -0.0190 -0.0909 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.5867 0.6080 0.5057 0.0970  -0.0181 -0.0849 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.6233 0.6019 0.5177 0.1088  -0.0080 -0.0746 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.5759 0.6160 0.4918 0.0988  -0.0243 -0.0907 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.6599 0.6128 0.5237 0.1252  -0.0029 -0.0654 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.6167 0.6387 0.5024 0.1163  -0.0230 -0.0843 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.6581 0.6353 0.5159 0.1310  -0.0116 -0.0692 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.5870 0.7273 0.5462 0.1064  -0.0403 -0.1176 53  HIS A N   
407  C CA  . HIS A 53  ? 0.6109 0.7981 0.5674 0.1265  -0.0531 -0.1301 53  HIS A CA  
408  C C   . HIS A 53  ? 0.6458 0.8786 0.6141 0.1464  -0.0590 -0.1386 53  HIS A C   
409  O O   . HIS A 53  ? 0.6791 0.9502 0.6376 0.1772  -0.0709 -0.1444 53  HIS A O   
410  C CB  . HIS A 53  ? 0.5880 0.8117 0.5667 0.1014  -0.0567 -0.1492 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.5962 0.7815 0.5589 0.0907  -0.0522 -0.1439 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.6216 0.8045 0.5548 0.1112  -0.0592 -0.1428 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.5862 0.7355 0.5559 0.0657  -0.0402 -0.1385 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.6231 0.7707 0.5485 0.0961  -0.0508 -0.1391 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.6019 0.7293 0.5505 0.0698  -0.0396 -0.1364 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.6495 0.8836 0.6368 0.1332  -0.0508 -0.1395 54  GLN A N   
417  C CA  . GLN A 54  ? 0.6734 0.9509 0.6725 0.1538  -0.0535 -0.1481 54  GLN A CA  
418  C C   . GLN A 54  ? 0.7212 0.9620 0.6854 0.1948  -0.0525 -0.1346 54  GLN A C   
419  O O   . GLN A 54  ? 0.7496 1.0290 0.7141 0.2279  -0.0582 -0.1402 54  GLN A O   
420  C CB  . GLN A 54  ? 0.6683 0.9517 0.6905 0.1292  -0.0419 -0.1517 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.7082 1.0441 0.7480 0.1466  -0.0415 -0.1636 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.7366 1.0721 0.7910 0.1230  -0.0271 -0.1649 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.7388 1.0509 0.7964 0.0916  -0.0188 -0.1592 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.7551 1.1157 0.8142 0.1420  -0.0228 -0.1711 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.7423 0.9085 0.6766 0.1938  -0.0429 -0.1175 55  TYR A N   
426  C CA  . TYR A 55  ? 0.7963 0.9079 0.6934 0.2267  -0.0340 -0.1040 55  TYR A CA  
427  C C   . TYR A 55  ? 0.8456 0.9032 0.7062 0.2358  -0.0289 -0.0874 55  TYR A C   
428  O O   . TYR A 55  ? 0.8932 0.8799 0.7244 0.2423  -0.0121 -0.0747 55  TYR A O   
429  C CB  . TYR A 55  ? 0.7912 0.8576 0.6874 0.2118  -0.0189 -0.1038 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.7691 0.8816 0.6919 0.2087  -0.0198 -0.1181 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.7985 0.9246 0.7140 0.2452  -0.0179 -0.1222 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.7297 0.8698 0.6812 0.1725  -0.0199 -0.1258 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.7866 0.9580 0.7268 0.2424  -0.0162 -0.1361 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.7229 0.9031 0.6944 0.1693  -0.0169 -0.1372 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.7489 0.9472 0.7166 0.2027  -0.0151 -0.1436 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.7367 0.9783 0.7249 0.1997  -0.0098 -0.1559 55  TYR A OH  
437  N N   . GLU A 56  ? 0.8432 0.9320 0.7039 0.2345  -0.0405 -0.0893 56  GLU A N   
438  C CA  . GLU A 56  ? 0.8788 0.9187 0.7022 0.2431  -0.0337 -0.0732 56  GLU A CA  
439  C C   . GLU A 56  ? 0.9399 0.9506 0.7140 0.2944  -0.0293 -0.0565 56  GLU A C   
440  O O   . GLU A 56  ? 0.9815 0.9501 0.7167 0.3067  -0.0209 -0.0403 56  GLU A O   
441  C CB  . GLU A 56  ? 0.8592 0.9404 0.6928 0.2282  -0.0464 -0.0827 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.8551 1.0226 0.7059 0.2427  -0.0677 -0.1026 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.8505 1.0500 0.7037 0.2281  -0.0776 -0.1157 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.8951 1.1026 0.7115 0.2586  -0.0851 -0.1111 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.8175 1.0298 0.7048 0.1878  -0.0760 -0.1302 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.9557 0.9852 0.7272 0.3276  -0.0323 -0.0583 57  GLU A N   
447  C CA  . GLU A 57  ? 1.0304 1.0262 0.7503 0.3850  -0.0256 -0.0392 57  GLU A CA  
448  C C   . GLU A 57  ? 1.0695 0.9653 0.7606 0.3900  0.0042  -0.0244 57  GLU A C   
449  O O   . GLU A 57  ? 1.1493 0.9869 0.7871 0.4351  0.0194  -0.0029 57  GLU A O   
450  C CB  . GLU A 57  ? 1.0351 1.1160 0.7688 0.4257  -0.0458 -0.0510 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.9805 1.1726 0.7586 0.4077  -0.0734 -0.0769 57  GLU A CG  
452  C CD  . GLU A 57  ? 1.0174 1.2615 0.7659 0.4499  -0.0924 -0.0752 57  GLU A CD  
453  O OE1 . GLU A 57  ? 1.0793 1.3264 0.7899 0.5115  -0.0946 -0.0609 57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.9903 1.2725 0.7504 0.4240  -0.1048 -0.0887 57  GLU A OE2 
455  N N   . ARG A 58  ? 1.0332 0.9063 0.7551 0.3455  0.0144  -0.0362 58  ARG A N   
456  C CA  . ARG A 58  ? 1.0772 0.8637 0.7798 0.3403  0.0425  -0.0322 58  ARG A CA  
457  C C   . ARG A 58  ? 1.0385 0.7890 0.7589 0.2841  0.0552  -0.0381 58  ARG A C   
458  O O   . ARG A 58  ? 1.0424 0.7738 0.7809 0.2561  0.0650  -0.0522 58  ARG A O   
459  C CB  . ARG A 58  ? 1.0813 0.8921 0.8051 0.3484  0.0407  -0.0482 58  ARG A CB  
460  C CG  . ARG A 58  ? 1.0680 0.9749 0.8133 0.3807  0.0157  -0.0565 58  ARG A CG  
461  C CD  . ARG A 58  ? 1.1012 1.0215 0.8586 0.3980  0.0205  -0.0693 58  ARG A CD  
462  N NE  . ARG A 58  ? 1.1228 0.9731 0.8769 0.3676  0.0429  -0.0768 58  ARG A NE  
463  C CZ  . ARG A 58  ? 1.1974 0.9561 0.9109 0.3886  0.0699  -0.0701 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 1.2682 0.9870 0.9360 0.4457  0.0793  -0.0498 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 1.2005 0.9064 0.9163 0.3535  0.0886  -0.0845 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.9991 0.7457 0.7139 0.2694  0.0548  -0.0289 59  LEU A N   
467  C CA  . LEU A 59  ? 0.9782 0.7080 0.7156 0.2197  0.0642  -0.0352 59  LEU A CA  
468  C C   . LEU A 59  ? 1.0705 0.7142 0.7879 0.2044  0.0971  -0.0339 59  LEU A C   
469  O O   . LEU A 59  ? 1.0739 0.7183 0.8210 0.1637  0.1026  -0.0508 59  LEU A O   
470  C CB  . LEU A 59  ? 0.9588 0.7014 0.6907 0.2136  0.0598  -0.0254 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.9155 0.7419 0.6783 0.2094  0.0306  -0.0356 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.9190 0.7497 0.6684 0.2076  0.0291  -0.0278 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.8741 0.7378 0.6856 0.1710  0.0222  -0.0527 59  LEU A CD2 
474  N N   . ASP A 60  ? 1.1721 0.7414 0.8379 0.2366  0.1209  -0.0152 60  ASP A N   
475  C CA  . ASP A 60  ? 1.2613 0.7357 0.9040 0.2180  0.1599  -0.0141 60  ASP A CA  
476  C C   . ASP A 60  ? 1.2572 0.7016 0.9065 0.2106  0.1715  -0.0337 60  ASP A C   
477  O O   . ASP A 60  ? 1.3223 0.6815 0.9510 0.1939  0.2072  -0.0377 60  ASP A O   
478  C CB  . ASP A 60  ? 1.3918 0.7836 0.9680 0.2579  0.1874  0.0166  60  ASP A CB  
479  C CG  . ASP A 60  ? 1.4164 0.8411 0.9610 0.3223  0.1661  0.0348  60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.3618 0.8794 0.9427 0.3294  0.1302  0.0211  60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.5269 0.8864 1.0093 0.3665  0.1868  0.0626  60  ASP A OD2 
482  N N   . GLU A 61  ? 1.1907 0.7012 0.8675 0.2199  0.1453  -0.0481 61  GLU A N   
483  C CA  . GLU A 61  ? 1.2020 0.6913 0.8850 0.2125  0.1552  -0.0698 61  GLU A CA  
484  C C   . GLU A 61  ? 1.1025 0.6823 0.8363 0.1862  0.1268  -0.0929 61  GLU A C   
485  O O   . GLU A 61  ? 1.1100 0.6984 0.8485 0.1932  0.1260  -0.1088 61  GLU A O   
486  C CB  . GLU A 61  ? 1.2729 0.7250 0.9164 0.2705  0.1639  -0.0585 61  GLU A CB  
487  C CG  . GLU A 61  ? 1.2567 0.7772 0.8966 0.3188  0.1357  -0.0409 61  GLU A CG  
488  C CD  . GLU A 61  ? 1.3641 0.8319 0.9499 0.3856  0.1504  -0.0196 61  GLU A CD  
489  O OE1 . GLU A 61  ? 1.3721 0.8768 0.9631 0.4209  0.1400  -0.0262 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 1.4487 0.8380 0.9846 0.4051  0.1743  0.0052  61  GLU A OE2 
491  N N   . ILE A 62  ? 1.0119 0.6546 0.7794 0.1589  0.1064  -0.0937 62  ILE A N   
492  C CA  . ILE A 62  ? 0.9196 0.6405 0.7284 0.1361  0.0831  -0.1100 62  ILE A CA  
493  C C   . ILE A 62  ? 0.8721 0.6087 0.7064 0.0923  0.0824  -0.1182 62  ILE A C   
494  O O   . ILE A 62  ? 0.8769 0.6025 0.7093 0.0852  0.0864  -0.1057 62  ILE A O   
495  C CB  . ILE A 62  ? 0.8660 0.6589 0.6909 0.1563  0.0569  -0.1008 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.8905 0.6893 0.6992 0.2003  0.0550  -0.0982 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.8046 0.6647 0.6671 0.1292  0.0395  -0.1127 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.8406 0.7197 0.6710 0.2160  0.0310  -0.0959 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.8352 0.6020 0.6916 0.0659  0.0776  -0.1396 63  ALA A N   
500  C CA  . ALA A 63  ? 0.7871 0.5902 0.6718 0.0303  0.0715  -0.1491 63  ALA A CA  
501  C C   . ALA A 63  ? 0.7314 0.6089 0.6391 0.0311  0.0463  -0.1471 63  ALA A C   
502  O O   . ALA A 63  ? 0.7512 0.6538 0.6604 0.0345  0.0399  -0.1580 63  ALA A O   
503  C CB  . ALA A 63  ? 0.8086 0.5928 0.6973 0.0000  0.0863  -0.1774 63  ALA A CB  
504  N N   . PHE A 64  ? 0.6760 0.5829 0.5981 0.0286  0.0357  -0.1328 64  PHE A N   
505  C CA  . PHE A 64  ? 0.6205 0.5831 0.5594 0.0304  0.0178  -0.1271 64  PHE A CA  
506  C C   . PHE A 64  ? 0.6256 0.6270 0.5814 0.0104  0.0114  -0.1368 64  PHE A C   
507  O O   . PHE A 64  ? 0.6407 0.6411 0.6061 -0.0073 0.0165  -0.1451 64  PHE A O   
508  C CB  . PHE A 64  ? 0.5752 0.5455 0.5186 0.0380  0.0121  -0.1096 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.5880 0.5436 0.5161 0.0618  0.0118  -0.1018 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.6316 0.5424 0.5373 0.0740  0.0226  -0.0949 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.5660 0.5568 0.5013 0.0728  0.0019  -0.1018 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.6520 0.5586 0.5397 0.1026  0.0196  -0.0872 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.5845 0.5785 0.5101 0.0961  -0.0013 -0.0987 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.6257 0.5802 0.5260 0.1139  0.0055  -0.0910 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.6131 0.6532 0.5718 0.0146  0.0011  -0.1359 65  ILE A N   
516  C CA  . ILE A 65  ? 0.6029 0.6872 0.5705 0.0054  -0.0076 -0.1397 65  ILE A CA  
517  C C   . ILE A 65  ? 0.5918 0.7000 0.5606 0.0164  -0.0140 -0.1200 65  ILE A C   
518  O O   . ILE A 65  ? 0.5800 0.6829 0.5438 0.0252  -0.0117 -0.1137 65  ILE A O   
519  C CB  . ILE A 65  ? 0.6118 0.7132 0.5706 -0.0006 -0.0085 -0.1618 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.6558 0.7185 0.6107 -0.0143 0.0042  -0.1846 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.5872 0.7434 0.5514 -0.0060 -0.0201 -0.1663 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.6897 0.7654 0.6349 -0.0233 0.0053  -0.2126 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.6147 0.7493 0.5905 0.0161  -0.0197 -0.1110 66  GLY A N   
524  C CA  . GLY A 66  ? 0.6190 0.7630 0.5908 0.0267  -0.0200 -0.0906 66  GLY A CA  
525  C C   . GLY A 66  ? 0.6418 0.8233 0.6032 0.0347  -0.0256 -0.0851 66  GLY A C   
526  O O   . GLY A 66  ? 0.6568 0.8697 0.6240 0.0346  -0.0338 -0.0920 66  GLY A O   
527  N N   . ILE A 67  ? 0.6256 0.8084 0.5707 0.0426  -0.0201 -0.0729 67  ILE A N   
528  C CA  . ILE A 67  ? 0.6310 0.8428 0.5552 0.0565  -0.0221 -0.0608 67  ILE A CA  
529  C C   . ILE A 67  ? 0.6398 0.8261 0.5546 0.0666  -0.0090 -0.0326 67  ILE A C   
530  O O   . ILE A 67  ? 0.6525 0.8116 0.5683 0.0585  0.0045  -0.0284 67  ILE A O   
531  C CB  . ILE A 67  ? 0.6276 0.8575 0.5319 0.0569  -0.0209 -0.0709 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.6217 0.8693 0.5326 0.0455  -0.0308 -0.1026 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.6451 0.9018 0.5186 0.0759  -0.0206 -0.0529 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.6413 0.9034 0.5317 0.0461  -0.0283 -0.1173 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.6409 0.8368 0.5476 0.0842  -0.0111 -0.0154 68  HIS A N   
536  C CA  . HIS A 68  ? 0.6705 0.8298 0.5637 0.0960  0.0059  0.0122  68  HIS A CA  
537  C C   . HIS A 68  ? 0.7403 0.9051 0.5949 0.1157  0.0152  0.0340  68  HIS A C   
538  O O   . HIS A 68  ? 0.7646 0.9710 0.6013 0.1381  0.0026  0.0392  68  HIS A O   
539  C CB  . HIS A 68  ? 0.6737 0.8307 0.5777 0.1095  0.0023  0.0211  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.6927 0.9031 0.5890 0.1343  -0.0130 0.0251  68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.7490 0.9650 0.6114 0.1667  -0.0078 0.0525  68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.6785 0.9437 0.5968 0.1318  -0.0325 0.0040  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.7506 1.0324 0.6154 0.1868  -0.0277 0.0472  68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.7095 1.0245 0.6115 0.1625  -0.0426 0.0154  68  HIS A NE2 
545  N N   . THR A 69  ? 0.7831 0.9107 0.6243 0.1070  0.0380  0.0452  69  THR A N   
546  C CA  . THR A 69  ? 0.8629 0.9813 0.6610 0.1260  0.0551  0.0719  69  THR A CA  
547  C C   . THR A 69  ? 0.9209 0.9974 0.6960 0.1503  0.0716  0.1046  69  THR A C   
548  O O   . THR A 69  ? 0.9639 1.0420 0.6958 0.1814  0.0787  0.1316  69  THR A O   
549  C CB  . THR A 69  ? 0.8578 0.9526 0.6521 0.1042  0.0789  0.0705  69  THR A CB  
550  O OG1 . THR A 69  ? 0.8279 0.8847 0.6529 0.0789  0.0923  0.0622  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.8183 0.9578 0.6224 0.0926  0.0647  0.0434  69  THR A CG2 
552  N N   . GLY A 70  ? 0.9141 0.9511 0.7127 0.1400  0.0792  0.1029  70  GLY A N   
553  C CA  . GLY A 70  ? 0.9668 0.9577 0.7446 0.1648  0.0964  0.1310  70  GLY A CA  
554  C C   . GLY A 70  ? 0.9424 0.9753 0.7279 0.1943  0.0722  0.1323  70  GLY A C   
555  O O   . GLY A 70  ? 0.9474 1.0399 0.7191 0.2182  0.0521  0.1347  70  GLY A O   
556  N N   . HIS A 71  ? 0.9229 0.9319 0.7319 0.1920  0.0740  0.1277  71  HIS A N   
557  C CA  . HIS A 71  ? 0.9022 0.9540 0.7261 0.2171  0.0544  0.1263  71  HIS A CA  
558  C C   . HIS A 71  ? 0.8512 0.9516 0.7203 0.1892  0.0299  0.0907  71  HIS A C   
559  O O   . HIS A 71  ? 0.8269 0.9173 0.7126 0.1552  0.0292  0.0702  71  HIS A O   
560  C CB  . HIS A 71  ? 0.9263 0.9203 0.7453 0.2348  0.0750  0.1433  71  HIS A CB  
561  C CG  . HIS A 71  ? 1.0239 0.9594 0.7928 0.2683  0.1037  0.1818  71  HIS A CG  
562  N ND1 . HIS A 71  ? 1.0734 1.0411 0.8087 0.3195  0.0976  0.2095  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 1.0839 0.9286 0.8279 0.2582  0.1414  0.1973  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 1.1626 1.0535 0.8488 0.3438  0.1318  0.2452  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.1699 0.9817 0.8618 0.3040  0.1609  0.2375  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.8648 1.0193 0.7530 0.2059  0.0118  0.0841  72  LEU A N   
567  C CA  . LEU A 72  ? 0.8094 1.0060 0.7377 0.1798  -0.0061 0.0521  72  LEU A CA  
568  C C   . LEU A 72  ? 0.7798 0.9257 0.7276 0.1543  0.0052  0.0417  72  LEU A C   
569  O O   . LEU A 72  ? 0.8097 0.9233 0.7585 0.1660  0.0175  0.0520  72  LEU A O   
570  C CB  . LEU A 72  ? 0.8062 1.0729 0.7548 0.2012  -0.0223 0.0468  72  LEU A CB  
571  C CG  . LEU A 72  ? 0.7405 1.0383 0.7322 0.1724  -0.0316 0.0162  72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.7157 1.0509 0.7172 0.1446  -0.0455 -0.0114 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.7272 1.0830 0.7449 0.1933  -0.0383 0.0138  72  LEU A CD2 
574  N N   . GLY A 73  ? 0.7151 0.8552 0.6752 0.1229  0.0012  0.0209  73  GLY A N   
575  C CA  . GLY A 73  ? 0.6652 0.7724 0.6417 0.1021  0.0069  0.0083  73  GLY A CA  
576  C C   . GLY A 73  ? 0.6182 0.7580 0.6203 0.0909  -0.0037 -0.0109 73  GLY A C   
577  O O   . GLY A 73  ? 0.6326 0.8209 0.6446 0.0895  -0.0158 -0.0216 73  GLY A O   
578  N N   . PHE A 74  ? 0.5786 0.6907 0.5901 0.0809  0.0032  -0.0169 74  PHE A N   
579  C CA  . PHE A 74  ? 0.5375 0.6700 0.5692 0.0683  -0.0001 -0.0326 74  PHE A CA  
580  C C   . PHE A 74  ? 0.5373 0.6643 0.5679 0.0475  -0.0041 -0.0483 74  PHE A C   
581  O O   . PHE A 74  ? 0.5477 0.6946 0.5923 0.0349  -0.0053 -0.0626 74  PHE A O   
582  C CB  . PHE A 74  ? 0.5067 0.6101 0.5416 0.0684  0.0111  -0.0316 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.4981 0.6196 0.5430 0.0890  0.0161  -0.0224 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.5057 0.6088 0.5359 0.1118  0.0221  -0.0049 74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.5054 0.6607 0.5738 0.0868  0.0182  -0.0311 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.5291 0.6462 0.5657 0.1378  0.0281  0.0052  74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.5212 0.7014 0.6019 0.1099  0.0229  -0.0237 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.5359 0.6967 0.5996 0.1384  0.0269  -0.0048 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.5352 0.6354 0.5504 0.0437  -0.0036 -0.0472 75  TYR A N   
590  C CA  . TYR A 75  ? 0.5386 0.6335 0.5495 0.0316  -0.0067 -0.0601 75  TYR A CA  
591  C C   . TYR A 75  ? 0.5502 0.6693 0.5546 0.0327  -0.0135 -0.0631 75  TYR A C   
592  O O   . TYR A 75  ? 0.5522 0.6798 0.5570 0.0235  -0.0165 -0.0783 75  TYR A O   
593  C CB  . TYR A 75  ? 0.5343 0.5965 0.5347 0.0301  -0.0029 -0.0602 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.5349 0.5749 0.5344 0.0310  0.0030  -0.0585 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.5323 0.5647 0.5335 0.0269  0.0077  -0.0629 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.5420 0.5668 0.5370 0.0341  0.0069  -0.0545 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.5338 0.5465 0.5285 0.0297  0.0148  -0.0604 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.5469 0.5543 0.5372 0.0356  0.0120  -0.0561 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.5410 0.5437 0.5295 0.0353  0.0152  -0.0576 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.5472 0.5332 0.5256 0.0387  0.0218  -0.0582 75  TYR A OH  
601  N N   . ALA A 76  ? 0.5745 0.6998 0.5689 0.0443  -0.0129 -0.0490 76  ALA A N   
602  C CA  . ALA A 76  ? 0.5921 0.7428 0.5738 0.0493  -0.0176 -0.0484 76  ALA A CA  
603  C C   . ALA A 76  ? 0.6116 0.8053 0.5950 0.0631  -0.0257 -0.0441 76  ALA A C   
604  O O   . ALA A 76  ? 0.6373 0.8322 0.6088 0.0831  -0.0223 -0.0235 76  ALA A O   
605  C CB  . ALA A 76  ? 0.5980 0.7276 0.5633 0.0540  -0.0075 -0.0337 76  ALA A CB  
606  N N   . ASP A 77  ? 0.6103 0.8405 0.6082 0.0533  -0.0351 -0.0648 77  ASP A N   
607  C CA  . ASP A 77  ? 0.6346 0.9241 0.6430 0.0641  -0.0459 -0.0686 77  ASP A CA  
608  C C   . ASP A 77  ? 0.6535 0.9924 0.6540 0.0612  -0.0583 -0.0872 77  ASP A C   
609  O O   . ASP A 77  ? 0.6647 1.0591 0.6845 0.0530  -0.0684 -0.1099 77  ASP A O   
610  C CB  . ASP A 77  ? 0.6341 0.9369 0.6741 0.0504  -0.0443 -0.0830 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.6477 0.9209 0.6963 0.0209  -0.0371 -0.1051 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.6579 0.9083 0.6900 0.0137  -0.0364 -0.1120 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.6566 0.9261 0.7259 0.0068  -0.0293 -0.1143 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.6579 0.9815 0.6308 0.0660  -0.0565 -0.0809 78  TRP A N   
615  C CA  . TRP A 78  ? 0.6689 1.0375 0.6259 0.0667  -0.0670 -0.0975 78  TRP A CA  
616  C C   . TRP A 78  ? 0.6686 1.0395 0.5884 0.0942  -0.0649 -0.0699 78  TRP A C   
617  O O   . TRP A 78  ? 0.6723 0.9927 0.5772 0.0949  -0.0499 -0.0520 78  TRP A O   
618  C CB  . TRP A 78  ? 0.6822 1.0246 0.6386 0.0423  -0.0620 -0.1227 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.6923 1.0466 0.6746 0.0160  -0.0638 -0.1566 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.6807 0.9952 0.6847 -0.0013 -0.0531 -0.1617 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.7176 1.1245 0.7046 0.0016  -0.0735 -0.1918 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.6983 1.0299 0.7202 -0.0272 -0.0518 -0.1957 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.7169 1.1071 0.7317 -0.0283 -0.0647 -0.2177 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.7452 1.2124 0.7130 0.0104  -0.0875 -0.2056 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.7401 1.1695 0.7690 -0.0548 -0.0675 -0.2601 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.7645 1.2790 0.7456 -0.0134 -0.0947 -0.2495 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.7606 1.2550 0.7745 -0.0481 -0.0838 -0.2780 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.6659 1.0980 0.5700 0.1171  -0.0784 -0.0670 79  ARG A N   
629  C CA  . ARG A 79  ? 0.6951 1.1271 0.5548 0.1480  -0.0735 -0.0369 79  ARG A CA  
630  C C   . ARG A 79  ? 0.7075 1.1308 0.5410 0.1381  -0.0681 -0.0464 79  ARG A C   
631  O O   . ARG A 79  ? 0.7070 1.1527 0.5519 0.1160  -0.0764 -0.0816 79  ARG A O   
632  C CB  . ARG A 79  ? 0.7307 1.2397 0.5757 0.1815  -0.0920 -0.0318 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.7417 1.2547 0.6015 0.2059  -0.0921 -0.0102 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.7648 1.3788 0.6283 0.2343  -0.1166 -0.0191 79  ARG A CD  
635  N NE  . ARG A 79  ? 0.8147 1.4760 0.6294 0.2642  -0.1270 -0.0109 79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.8097 1.5487 0.6246 0.2532  -0.1481 -0.0477 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.7866 1.5578 0.6500 0.2103  -0.1580 -0.0953 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.8347 1.6035 0.6051 0.2804  -0.1513 -0.0380 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.7305 1.1175 0.5284 0.1530  -0.0502 -0.0164 80  PRO A N   
640  C CA  . PRO A 80  ? 0.7436 1.1252 0.5179 0.1442  -0.0416 -0.0251 80  PRO A CA  
641  C C   . PRO A 80  ? 0.7810 1.2306 0.5299 0.1539  -0.0592 -0.0464 80  PRO A C   
642  O O   . PRO A 80  ? 0.7799 1.2337 0.5228 0.1381  -0.0574 -0.0710 80  PRO A O   
643  C CB  . PRO A 80  ? 0.7740 1.1084 0.5145 0.1602  -0.0155 0.0152  80  PRO A CB  
644  C CG  . PRO A 80  ? 0.7670 1.0590 0.5264 0.1638  -0.0070 0.0366  80  PRO A CG  
645  C CD  . PRO A 80  ? 0.7537 1.0938 0.5338 0.1743  -0.0316 0.0247  80  PRO A CD  
646  N N   . ALA A 81  ? 0.8195 1.3271 0.5524 0.1816  -0.0766 -0.0397 81  ALA A N   
647  C CA  . ALA A 81  ? 0.8589 1.4450 0.5682 0.1908  -0.0971 -0.0657 81  ALA A CA  
648  C C   . ALA A 81  ? 0.8427 1.4621 0.5924 0.1541  -0.1125 -0.1204 81  ALA A C   
649  O O   . ALA A 81  ? 0.8656 1.5330 0.5979 0.1485  -0.1234 -0.1528 81  ALA A O   
650  C CB  . ALA A 81  ? 0.8947 1.5467 0.5813 0.2331  -0.1149 -0.0471 81  ALA A CB  
651  N N   . GLU A 82  ? 0.8119 1.4025 0.6112 0.1288  -0.1106 -0.1320 82  GLU A N   
652  C CA  . GLU A 82  ? 0.7974 1.4017 0.6336 0.0915  -0.1173 -0.1806 82  GLU A CA  
653  C C   . GLU A 82  ? 0.7834 1.3177 0.6236 0.0657  -0.0988 -0.1939 82  GLU A C   
654  O O   . GLU A 82  ? 0.7730 1.2917 0.6416 0.0356  -0.0964 -0.2273 82  GLU A O   
655  C CB  . GLU A 82  ? 0.7715 1.3808 0.6551 0.0794  -0.1213 -0.1846 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.7981 1.4886 0.6865 0.1064  -0.1407 -0.1771 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.7994 1.4856 0.7336 0.0988  -0.1389 -0.1733 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.7870 1.3939 0.7340 0.0863  -0.1206 -0.1572 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.8194 1.5879 0.7771 0.1061  -0.1558 -0.1881 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.7905 1.2831 0.6028 0.0781  -0.0834 -0.1684 83  ALA A N   
661  C CA  . ALA A 83  ? 0.7684 1.2037 0.5867 0.0606  -0.0665 -0.1789 83  ALA A CA  
662  C C   . ALA A 83  ? 0.7910 1.2439 0.5950 0.0479  -0.0678 -0.2200 83  ALA A C   
663  O O   . ALA A 83  ? 0.7907 1.2013 0.6103 0.0290  -0.0576 -0.2425 83  ALA A O   
664  C CB  . ALA A 83  ? 0.7633 1.1617 0.5623 0.0753  -0.0484 -0.1434 83  ALA A CB  
665  N N   . ASP A 84  ? 0.8111 1.3231 0.5815 0.0608  -0.0788 -0.2301 84  ASP A N   
666  C CA  . ASP A 84  ? 0.8253 1.3561 0.5792 0.0477  -0.0797 -0.2743 84  ASP A CA  
667  C C   . ASP A 84  ? 0.8250 1.3618 0.6139 0.0155  -0.0863 -0.3193 84  ASP A C   
668  O O   . ASP A 84  ? 0.8459 1.3419 0.6410 -0.0052 -0.0733 -0.3498 84  ASP A O   
669  C CB  . ASP A 84  ? 0.8578 1.4479 0.5746 0.0693  -0.0894 -0.2696 84  ASP A CB  
670  C CG  . ASP A 84  ? 0.8857 1.4568 0.5586 0.0900  -0.0724 -0.2442 84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.8762 1.3969 0.5530 0.0818  -0.0534 -0.2458 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.9260 1.5307 0.5647 0.1151  -0.0754 -0.2209 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.8116 1.3918 0.6279 0.0114  -0.1016 -0.3198 85  LYS A N   
674  C CA  . LYS A 85  ? 0.8108 1.3904 0.6693 -0.0236 -0.1007 -0.3571 85  LYS A CA  
675  C C   . LYS A 85  ? 0.7898 1.2926 0.6691 -0.0432 -0.0838 -0.3589 85  LYS A C   
676  O O   . LYS A 85  ? 0.8147 1.2898 0.7174 -0.0752 -0.0729 -0.3926 85  LYS A O   
677  C CB  . LYS A 85  ? 0.7958 1.4491 0.6827 -0.0203 -0.1186 -0.3552 85  LYS A CB  
678  N N   . LEU A 86  ? 0.7549 1.2090 0.6324 -0.0230 -0.0751 -0.3128 86  LEU A N   
679  C CA  . LEU A 86  ? 0.7377 1.1133 0.6365 -0.0343 -0.0572 -0.3032 86  LEU A CA  
680  C C   . LEU A 86  ? 0.7729 1.0891 0.6560 -0.0394 -0.0389 -0.3205 86  LEU A C   
681  O O   . LEU A 86  ? 0.7769 1.0333 0.6726 -0.0550 -0.0231 -0.3325 86  LEU A O   
682  C CB  . LEU A 86  ? 0.6921 1.0442 0.5939 -0.0120 -0.0554 -0.2544 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.6756 0.9653 0.6005 -0.0198 -0.0427 -0.2415 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.6717 0.9779 0.6264 -0.0383 -0.0462 -0.2528 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.6542 0.9225 0.5764 0.0009  -0.0399 -0.2006 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.8055 1.1354 0.6581 -0.0233 -0.0384 -0.3204 87  VAL A N   
687  C CA  . VAL A 87  ? 0.8396 1.1190 0.6768 -0.0224 -0.0204 -0.3369 87  VAL A CA  
688  C C   . VAL A 87  ? 0.9025 1.1660 0.7392 -0.0496 -0.0128 -0.3880 87  VAL A C   
689  O O   . VAL A 87  ? 0.9267 1.1198 0.7623 -0.0550 0.0078  -0.4013 87  VAL A O   
690  C CB  . VAL A 87  ? 0.8374 1.1444 0.6427 0.0001  -0.0198 -0.3268 87  VAL A CB  
691  C CG1 . VAL A 87  ? 0.8649 1.1300 0.6547 0.0032  -0.0011 -0.3498 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.7991 1.1062 0.6077 0.0207  -0.0189 -0.2788 87  VAL A CG2 
693  N N   . LYS A 88  ? 0.9360 1.2623 0.7743 -0.0658 -0.0276 -0.4155 88  LYS A N   
694  C CA  . LYS A 88  ? 1.0070 1.3155 0.8542 -0.0943 -0.0177 -0.4543 88  LYS A CA  
695  C C   . LYS A 88  ? 1.0362 1.2892 0.9125 -0.1228 -0.0016 -0.4671 88  LYS A C   
696  O O   . LYS A 88  ? 1.0902 1.2668 0.9611 -0.1355 0.0229  -0.4848 88  LYS A O   
697  C CB  . LYS A 88  ? 1.0278 1.4244 0.8809 -0.1014 -0.0378 -0.4699 88  LYS A CB  
698  C CG  . LYS A 88  ? 1.0325 1.4838 0.8519 -0.0705 -0.0523 -0.4519 88  LYS A CG  
699  C CD  . LYS A 88  ? 1.0875 1.5950 0.9008 -0.0792 -0.0612 -0.4823 88  LYS A CD  
700  C CE  . LYS A 88  ? 1.0763 1.6759 0.8802 -0.0546 -0.0857 -0.4622 88  LYS A CE  
701  N NZ  . LYS A 88  ? 1.0555 1.6533 0.8206 -0.0177 -0.0866 -0.4206 88  LYS A NZ  
702  N N   . LEU A 89  ? 1.0200 1.3068 0.9245 -0.1311 -0.0123 -0.4561 89  LEU A N   
703  C CA  . LEU A 89  ? 1.0390 1.2771 0.9715 -0.1602 0.0059  -0.4665 89  LEU A CA  
704  C C   . LEU A 89  ? 1.0413 1.1780 0.9595 -0.1490 0.0296  -0.4484 89  LEU A C   
705  O O   . LEU A 89  ? 1.0907 1.1515 1.0118 -0.1690 0.0566  -0.4616 89  LEU A O   
706  C CB  . LEU A 89  ? 0.9977 1.3002 0.9633 -0.1664 -0.0108 -0.4556 89  LEU A CB  
707  C CG  . LEU A 89  ? 0.9831 1.3934 0.9678 -0.1701 -0.0338 -0.4686 89  LEU A CG  
708  C CD1 . LEU A 89  ? 0.9378 1.4058 0.9532 -0.1662 -0.0486 -0.4514 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 1.0205 1.4358 1.0241 -0.2063 -0.0202 -0.5110 89  LEU A CD2 
710  N N   . LEU A 90  ? 0.9971 1.1284 0.9025 -0.1115 0.0217  -0.4041 90  LEU A N   
711  C CA  . LEU A 90  ? 1.0093 1.0590 0.9053 -0.0911 0.0396  -0.3754 90  LEU A CA  
712  C C   . LEU A 90  ? 1.0961 1.0796 0.9649 -0.0852 0.0621  -0.3968 90  LEU A C   
713  O O   . LEU A 90  ? 1.1352 1.0417 0.9940 -0.0706 0.0820  -0.3815 90  LEU A O   
714  C CB  . LEU A 90  ? 0.9550 1.0308 0.8488 -0.0572 0.0247  -0.3311 90  LEU A CB  
715  C CG  . LEU A 90  ? 0.9619 0.9812 0.8538 -0.0342 0.0350  -0.2982 90  LEU A CG  
716  C CD1 . LEU A 90  ? 0.9750 0.9555 0.8817 -0.0477 0.0442  -0.2896 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 0.9188 0.9782 0.8141 -0.0103 0.0201  -0.2641 90  LEU A CD2 
718  N N   . ALA A 91  ? 1.1471 1.1593 1.0003 -0.0928 0.0599  -0.4320 91  ALA A N   
719  C CA  . ALA A 91  ? 1.2220 1.1717 1.0477 -0.0848 0.0825  -0.4541 91  ALA A CA  
720  C C   . ALA A 91  ? 1.3168 1.2103 1.1454 -0.1169 0.1034  -0.4811 91  ALA A C   
721  O O   . ALA A 91  ? 1.3710 1.1746 1.1800 -0.1071 0.1302  -0.4822 91  ALA A O   
722  C CB  . ALA A 91  ? 1.2140 1.2204 1.0208 -0.0700 0.0693  -0.4617 91  ALA A CB  
723  N N   . LYS A 92  ? 1.3644 1.3120 1.2181 -0.1526 0.0928  -0.5020 92  LYS A N   
724  C CA  . LYS A 92  ? 1.4895 1.3985 1.3536 -0.1893 0.1137  -0.5316 92  LYS A CA  
725  C C   . LYS A 92  ? 1.5858 1.4219 1.4628 -0.2053 0.1391  -0.5198 92  LYS A C   
726  O O   . LYS A 92  ? 1.6680 1.4918 1.5647 -0.2435 0.1561  -0.5424 92  LYS A O   
727  C CB  . LYS A 92  ? 1.4613 1.4708 1.3537 -0.2199 0.0934  -0.5595 92  LYS A CB  
728  N N   . GLY A 93  ? 1.5830 1.3731 1.4491 -0.1775 0.1444  -0.4854 93  GLY A N   
729  C CA  . GLY A 93  ? 1.6507 1.3794 1.5261 -0.1902 0.1669  -0.4693 93  GLY A CA  
730  C C   . GLY A 93  ? 1.6488 1.4521 1.5666 -0.2262 0.1546  -0.4792 93  GLY A C   
731  O O   . GLY A 93  ? 1.6369 1.5402 1.5737 -0.2243 0.1219  -0.4817 93  GLY A O   
732  N N   . GLU A 94  ? 1.6888 1.4448 1.6206 -0.2562 0.1828  -0.4826 94  GLU A N   
733  C CA  . GLU A 94  ? 1.6709 1.4981 1.6482 -0.2958 0.1789  -0.4998 94  GLU A CA  
734  C C   . GLU A 94  ? 1.5778 1.4867 1.5771 -0.2830 0.1473  -0.4816 94  GLU A C   
735  O O   . GLU A 94  ? 1.5321 1.5484 1.5532 -0.2836 0.1151  -0.4936 94  GLU A O   
736  C CB  . GLU A 94  ? 1.6902 1.5924 1.6891 -0.3248 0.1694  -0.5423 94  GLU A CB  
737  N N   . TYR A 95  ? 1.4840 1.3368 1.4736 -0.2682 0.1586  -0.4503 95  TYR A N   
738  C CA  . TYR A 95  ? 1.3287 1.2467 1.3405 -0.2559 0.1344  -0.4263 95  TYR A CA  
739  C C   . TYR A 95  ? 1.2797 1.1258 1.2878 -0.2549 0.1610  -0.3956 95  TYR A C   
740  O O   . TYR A 95  ? 1.3368 1.0752 1.3103 -0.2465 0.1922  -0.3838 95  TYR A O   
741  C CB  . TYR A 95  ? 1.2468 1.2022 1.2413 -0.2065 0.1015  -0.3903 95  TYR A CB  
742  C CG  . TYR A 95  ? 1.2475 1.1191 1.2023 -0.1688 0.1124  -0.3595 95  TYR A CG  
743  C CD1 . TYR A 95  ? 1.2295 1.0550 1.1740 -0.1446 0.1195  -0.3185 95  TYR A CD1 
744  C CD2 . TYR A 95  ? 1.2734 1.1223 1.2014 -0.1543 0.1140  -0.3730 95  TYR A CD2 
745  C CE1 . TYR A 95  ? 1.2443 1.0095 1.1551 -0.1068 0.1260  -0.2930 95  TYR A CE1 
746  C CE2 . TYR A 95  ? 1.2879 1.0739 1.1844 -0.1161 0.1226  -0.3465 95  TYR A CE2 
747  C CZ  . TYR A 95  ? 1.2711 1.0192 1.1603 -0.0920 0.1274  -0.3068 95  TYR A CZ  
748  O OH  . TYR A 95  ? 1.2823 0.9820 1.1424 -0.0509 0.1330  -0.2825 95  TYR A OH  
749  N N   . GLN A 96  ? 1.1700 1.0761 1.2102 -0.2597 0.1496  -0.3817 96  GLN A N   
750  C CA  . GLN A 96  ? 1.1282 0.9784 1.1651 -0.2590 0.1738  -0.3533 96  GLN A CA  
751  C C   . GLN A 96  ? 1.0476 0.8795 1.0580 -0.2077 0.1574  -0.3020 96  GLN A C   
752  O O   . GLN A 96  ? 0.9943 0.8662 0.9975 -0.1773 0.1274  -0.2891 96  GLN A O   
753  C CB  . GLN A 96  ? 1.0873 1.0135 1.1739 -0.2902 0.1730  -0.3670 96  GLN A CB  
754  C CG  . GLN A 96  ? 1.1217 1.0615 1.2402 -0.3492 0.1980  -0.4205 96  GLN A CG  
755  C CD  . GLN A 96  ? 1.0644 1.1135 1.2412 -0.3748 0.1882  -0.4381 96  GLN A CD  
756  O OE1 . GLN A 96  ? 1.0014 1.1640 1.2058 -0.3655 0.1502  -0.4501 96  GLN A OE1 
757  N NE2 . GLN A 96  ? 1.0911 1.1094 1.2828 -0.3992 0.2231  -0.4339 96  GLN A NE2 
758  N N   . LYS A 97  ? 1.0409 0.8126 1.0359 -0.2002 0.1797  -0.2746 97  LYS A N   
759  C CA  . LYS A 97  ? 0.9724 0.7284 0.9427 -0.1558 0.1668  -0.2309 97  LYS A CA  
760  C C   . LYS A 97  ? 0.9217 0.6995 0.9098 -0.1612 0.1713  -0.2143 97  LYS A C   
761  O O   . LYS A 97  ? 0.9633 0.7092 0.9585 -0.1908 0.2030  -0.2232 97  LYS A O   
762  C CB  . LYS A 97  ? 1.0240 0.6763 0.9423 -0.1283 0.1896  -0.2102 97  LYS A CB  
763  C CG  . LYS A 97  ? 1.0300 0.6627 0.9275 -0.1105 0.1830  -0.2205 97  LYS A CG  
764  C CD  . LYS A 97  ? 1.0759 0.6250 0.9231 -0.0681 0.1979  -0.1921 97  LYS A CD  
765  C CE  . LYS A 97  ? 1.0919 0.6302 0.9215 -0.0450 0.1907  -0.2017 97  LYS A CE  
766  N NZ  . LYS A 97  ? 1.1357 0.6139 0.9205 0.0058  0.1987  -0.1719 97  LYS A NZ  
767  N N   . VAL A 98  ? 0.8375 0.6672 0.8326 -0.1343 0.1430  -0.1917 98  VAL A N   
768  C CA  . VAL A 98  ? 0.7985 0.6465 0.8049 -0.1314 0.1458  -0.1737 98  VAL A CA  
769  C C   . VAL A 98  ? 0.7750 0.5893 0.7451 -0.0911 0.1375  -0.1397 98  VAL A C   
770  O O   . VAL A 98  ? 0.7555 0.5769 0.7120 -0.0663 0.1163  -0.1325 98  VAL A O   
771  C CB  . VAL A 98  ? 0.7316 0.6794 0.7832 -0.1379 0.1212  -0.1833 98  VAL A CB  
772  C CG1 . VAL A 98  ? 0.7015 0.7043 0.7714 -0.1474 0.1009  -0.2092 98  VAL A CG1 
773  C CG2 . VAL A 98  ? 0.6978 0.6685 0.7429 -0.1040 0.0996  -0.1550 98  VAL A CG2 
774  N N   . SER A 99  ? 0.7835 0.5651 0.7378 -0.0858 0.1555  -0.1214 99  SER A N   
775  C CA  . SER A 99  ? 0.7866 0.5375 0.7024 -0.0488 0.1498  -0.0933 99  SER A CA  
776  C C   . SER A 99  ? 0.7539 0.5439 0.6821 -0.0425 0.1416  -0.0819 99  SER A C   
777  O O   . SER A 99  ? 0.7608 0.5655 0.7105 -0.0640 0.1579  -0.0873 99  SER A O   
778  C CB  . SER A 99  ? 0.8751 0.5358 0.7420 -0.0384 0.1820  -0.0783 99  SER A CB  
779  O OG  . SER A 99  ? 0.9265 0.5406 0.7782 -0.0411 0.1933  -0.0889 99  SER A OG  
780  N N   . TYR A 100 ? 0.7242 0.5322 0.6400 -0.0142 0.1183  -0.0690 100 TYR A N   
781  C CA  . TYR A 100 ? 0.7006 0.5364 0.6213 -0.0049 0.1112  -0.0600 100 TYR A CA  
782  C C   . TYR A 100 ? 0.7376 0.5348 0.6119 0.0221  0.1157  -0.0421 100 TYR A C   
783  O O   . TYR A 100 ? 0.7589 0.5302 0.6033 0.0430  0.1104  -0.0358 100 TYR A O   
784  C CB  . TYR A 100 ? 0.6436 0.5335 0.5884 0.0023  0.0827  -0.0639 100 TYR A CB  
785  C CG  . TYR A 100 ? 0.6162 0.5574 0.6031 -0.0157 0.0764  -0.0769 100 TYR A CG  
786  C CD1 . TYR A 100 ? 0.6315 0.5812 0.6398 -0.0410 0.0917  -0.0908 100 TYR A CD1 
787  C CD2 . TYR A 100 ? 0.5790 0.5618 0.5827 -0.0067 0.0565  -0.0759 100 TYR A CD2 
788  C CE1 . TYR A 100 ? 0.6090 0.6206 0.6563 -0.0537 0.0822  -0.1053 100 TYR A CE1 
789  C CE2 . TYR A 100 ? 0.5580 0.5914 0.5936 -0.0148 0.0494  -0.0845 100 TYR A CE2 
790  C CZ  . TYR A 100 ? 0.5809 0.6352 0.6392 -0.0368 0.0597  -0.1001 100 TYR A CZ  
791  O OH  . TYR A 100 ? 0.5839 0.7030 0.6745 -0.0415 0.0491  -0.1114 100 TYR A OH  
792  N N   . PRO A 101 ? 0.7447 0.5427 0.6108 0.0253  0.1250  -0.0346 101 PRO A N   
793  C CA  . PRO A 101 ? 0.7782 0.5480 0.5958 0.0532  0.1272  -0.0195 101 PRO A CA  
794  C C   . PRO A 101 ? 0.7455 0.5498 0.5607 0.0732  0.0969  -0.0233 101 PRO A C   
795  O O   . PRO A 101 ? 0.6887 0.5332 0.5391 0.0639  0.0788  -0.0345 101 PRO A O   
796  C CB  . PRO A 101 ? 0.7879 0.5587 0.6038 0.0466  0.1459  -0.0154 101 PRO A CB  
797  C CG  . PRO A 101 ? 0.7696 0.5606 0.6324 0.0139  0.1601  -0.0269 101 PRO A CG  
798  C CD  . PRO A 101 ? 0.7242 0.5519 0.6231 0.0057  0.1360  -0.0405 101 PRO A CD  
799  N N   . LEU A 102 ? 0.5548 0.4462 0.5521 0.0732  0.0733  -0.0042 102 LEU A N   
800  C CA  . LEU A 102 ? 0.5394 0.4721 0.5592 0.0846  0.0755  -0.0055 102 LEU A CA  
801  C C   . LEU A 102 ? 0.5370 0.4827 0.5650 0.0850  0.0679  0.0069  102 LEU A C   
802  O O   . LEU A 102 ? 0.5566 0.4758 0.5709 0.0824  0.0616  0.0166  102 LEU A O   
803  C CB  . LEU A 102 ? 0.5632 0.4979 0.5897 0.1091  0.0782  -0.0155 102 LEU A CB  
804  C CG  . LEU A 102 ? 0.5789 0.5029 0.5953 0.1123  0.0870  -0.0304 102 LEU A CG  
805  C CD1 . LEU A 102 ? 0.6009 0.5253 0.6228 0.1412  0.0891  -0.0410 102 LEU A CD1 
806  C CD2 . LEU A 102 ? 0.5421 0.5016 0.5662 0.0983  0.0963  -0.0348 102 LEU A CD2 
807  N N   . LEU A 103 ? 0.5148 0.5009 0.5629 0.0865  0.0686  0.0064  103 LEU A N   
808  C CA  . LEU A 103 ? 0.4939 0.4966 0.5495 0.0867  0.0606  0.0156  103 LEU A CA  
809  C C   . LEU A 103 ? 0.5053 0.5285 0.5775 0.1080  0.0555  0.0136  103 LEU A C   
810  O O   . LEU A 103 ? 0.5003 0.5522 0.5909 0.1155  0.0612  0.0038  103 LEU A O   
811  C CB  . LEU A 103 ? 0.4638 0.4945 0.5277 0.0707  0.0626  0.0159  103 LEU A CB  
812  C CG  . LEU A 103 ? 0.4579 0.5064 0.5279 0.0701  0.0540  0.0225  103 LEU A CG  
813  C CD1 . LEU A 103 ? 0.4665 0.4903 0.5175 0.0676  0.0482  0.0328  103 LEU A CD1 
814  C CD2 . LEU A 103 ? 0.4411 0.5118 0.5176 0.0555  0.0561  0.0201  103 LEU A CD2 
815  N N   . LYS A 104 ? 0.5290 0.5405 0.5945 0.1177  0.0448  0.0229  104 LYS A N   
816  C CA  . LYS A 104 ? 0.5308 0.5635 0.6112 0.1402  0.0362  0.0222  104 LYS A CA  
817  C C   . LYS A 104 ? 0.5036 0.5708 0.5960 0.1333  0.0284  0.0266  104 LYS A C   
818  O O   . LYS A 104 ? 0.4972 0.5494 0.5727 0.1225  0.0238  0.0361  104 LYS A O   
819  C CB  . LYS A 104 ? 0.5689 0.5584 0.6277 0.1590  0.0271  0.0302  104 LYS A CB  
820  C CG  . LYS A 104 ? 0.5907 0.6007 0.6615 0.1853  0.0143  0.0316  104 LYS A CG  
821  C CD  . LYS A 104 ? 0.6500 0.6072 0.6902 0.2017  0.0036  0.0435  104 LYS A CD  
822  C CE  . LYS A 104 ? 0.6825 0.6611 0.7314 0.2290  -0.0123 0.0470  104 LYS A CE  
823  N NZ  . LYS A 104 ? 0.7487 0.6693 0.7606 0.2442  -0.0241 0.0618  104 LYS A NZ  
824  N N   . THR A 105 ? 0.4873 0.6024 0.6084 0.1385  0.0275  0.0186  105 THR A N   
825  C CA  . THR A 105 ? 0.4563 0.6064 0.5904 0.1307  0.0188  0.0200  105 THR A CA  
826  C C   . THR A 105 ? 0.4626 0.6416 0.6141 0.1546  0.0058  0.0189  105 THR A C   
827  O O   . THR A 105 ? 0.4605 0.6637 0.6333 0.1716  0.0087  0.0103  105 THR A O   
828  C CB  . THR A 105 ? 0.4153 0.6004 0.5689 0.1102  0.0277  0.0117  105 THR A CB  
829  O OG1 . THR A 105 ? 0.4159 0.5725 0.5505 0.0913  0.0372  0.0135  105 THR A OG1 
830  C CG2 . THR A 105 ? 0.3904 0.6076 0.5557 0.1005  0.0173  0.0115  105 THR A CG2 
831  N N   . THR A 106 ? 0.4711 0.6497 0.6128 0.1574  -0.0087 0.0268  106 THR A N   
832  C CA  . THR A 106 ? 0.4924 0.6998 0.6480 0.1806  -0.0248 0.0268  106 THR A CA  
833  C C   . THR A 106 ? 0.4834 0.7329 0.6534 0.1664  -0.0347 0.0239  106 THR A C   
834  O O   . THR A 106 ? 0.4709 0.7026 0.6205 0.1477  -0.0358 0.0288  106 THR A O   
835  C CB  . THR A 106 ? 0.5229 0.6842 0.6457 0.2003  -0.0365 0.0403  106 THR A CB  
836  O OG1 . THR A 106 ? 0.5531 0.6676 0.6588 0.2093  -0.0275 0.0423  106 THR A OG1 
837  C CG2 . THR A 106 ? 0.5314 0.7216 0.6670 0.2291  -0.0552 0.0403  106 THR A CG2 
838  N N   . VAL A 107 ? 0.4971 0.8039 0.7025 0.1751  -0.0418 0.0146  107 VAL A N   
839  C CA  . VAL A 107 ? 0.5173 0.8687 0.7398 0.1602  -0.0530 0.0097  107 VAL A CA  
840  C C   . VAL A 107 ? 0.5602 0.9436 0.7945 0.1869  -0.0744 0.0101  107 VAL A C   
841  O O   . VAL A 107 ? 0.5636 0.9757 0.8223 0.2122  -0.0764 0.0051  107 VAL A O   
842  C CB  . VAL A 107 ? 0.5052 0.9054 0.7634 0.1382  -0.0415 -0.0030 107 VAL A CB  
843  C CG1 . VAL A 107 ? 0.3048 0.7420 0.5756 0.1171  -0.0537 -0.0082 107 VAL A CG1 
844  C CG2 . VAL A 107 ? 0.4953 0.8604 0.7385 0.1168  -0.0211 -0.0024 107 VAL A CG2 
845  N N   . LYS A 108 ? 0.5932 0.9724 0.8086 0.1835  -0.0911 0.0155  108 LYS A N   
846  C CA  . LYS A 108 ? 0.6378 1.0458 0.8586 0.2081  -0.1148 0.0170  108 LYS A CA  
847  C C   . LYS A 108 ? 0.6321 1.1023 0.8817 0.1903  -0.1271 0.0054  108 LYS A C   
848  O O   . LYS A 108 ? 0.6097 1.0742 0.8515 0.1589  -0.1227 0.0018  108 LYS A O   
849  C CB  . LYS A 108 ? 0.6867 1.0406 0.8576 0.2194  -0.1265 0.0329  108 LYS A CB  
850  C CG  . LYS A 108 ? 0.7401 1.0355 0.8827 0.2412  -0.1201 0.0454  108 LYS A CG  
851  C CD  . LYS A 108 ? 0.8112 1.0549 0.9023 0.2472  -0.1304 0.0627  108 LYS A CD  
852  C CE  . LYS A 108 ? 0.8779 1.0624 0.9399 0.2692  -0.1275 0.0760  108 LYS A CE  
853  N NZ  . LYS A 108 ? 0.8694 1.0231 0.9331 0.2553  -0.1041 0.0734  108 LYS A NZ  
854  N N   . TYR A 109 ? 0.6574 1.1865 0.9398 0.2111  -0.1437 -0.0011 109 TYR A N   
855  C CA  . TYR A 109 ? 0.6597 1.2556 0.9739 0.1937  -0.1578 -0.0133 109 TYR A CA  
856  C C   . TYR A 109 ? 0.7033 1.3173 1.0077 0.2169  -0.1878 -0.0099 109 TYR A C   
857  O O   . TYR A 109 ? 0.7374 1.2963 0.9936 0.2282  -0.1962 0.0035  109 TYR A O   
858  C CB  . TYR A 109 ? 0.6407 1.3109 1.0137 0.1915  -0.1496 -0.0276 109 TYR A CB  
859  C CG  . TYR A 109 ? 0.6275 1.2805 1.0078 0.1767  -0.1201 -0.0298 109 TYR A CG  
860  C CD1 . TYR A 109 ? 0.6387 1.2728 1.0191 0.2050  -0.1081 -0.0271 109 TYR A CD1 
861  C CD2 . TYR A 109 ? 0.6122 1.2636 0.9952 0.1351  -0.1054 -0.0347 109 TYR A CD2 
862  C CE1 . TYR A 109 ? 0.6260 1.2445 1.0097 0.1917  -0.0821 -0.0299 109 TYR A CE1 
863  C CE2 . TYR A 109 ? 0.6056 1.2401 0.9910 0.1224  -0.0796 -0.0356 109 TYR A CE2 
864  C CZ  . TYR A 109 ? 0.6127 1.2330 0.9989 0.1506  -0.0681 -0.0336 109 TYR A CZ  
865  O OH  . TYR A 109 ? 0.6037 1.2076 0.9893 0.1384  -0.0435 -0.0354 109 TYR A OH  
866  N N   . GLY A 110 ? 0.7196 1.3894 1.0590 0.2156  -0.1980 -0.0202 110 GLY A N   
867  C CA  . GLY A 110 ? 0.7634 1.4408 1.0906 0.2320  -0.2233 -0.0172 110 GLY A CA  
868  C C   . GLY A 110 ? 0.7871 1.5322 1.1614 0.2346  -0.2306 -0.0290 110 GLY A C   
869  O O   . GLY A 110 ? 0.8225 1.5728 1.2045 0.2663  -0.2352 -0.0262 110 GLY A O   
870  N N   . LYS A 114 ? 0.4534 1.1348 0.8646 0.2960  -0.1418 -0.0310 114 LYS A N   
871  C CA  . LYS A 114 ? 0.6710 1.2881 1.0518 0.3238  -0.1342 -0.0232 114 LYS A CA  
872  C C   . LYS A 114 ? 0.6951 1.2670 1.0536 0.3062  -0.1164 -0.0183 114 LYS A C   
873  O O   . LYS A 114 ? 0.7035 1.3042 1.0843 0.2791  -0.0990 -0.0265 114 LYS A O   
874  C CB  . LYS A 114 ? 0.4932 1.1338 0.9001 0.3452  -0.1232 -0.0336 114 LYS A CB  
875  N N   . GLU A 115 ? 0.7097 1.2093 1.0222 0.3209  -0.1207 -0.0040 115 GLU A N   
876  C CA  . GLU A 115 ? 0.6514 1.1046 0.9392 0.3072  -0.1056 0.0023  115 GLU A CA  
877  C C   . GLU A 115 ? 0.6141 1.0685 0.9184 0.3057  -0.0815 -0.0077 115 GLU A C   
878  O O   . GLU A 115 ? 0.6303 1.0765 0.9386 0.3291  -0.0782 -0.0126 115 GLU A O   
879  C CB  . GLU A 115 ? 0.6883 1.0574 0.9206 0.3220  -0.1131 0.0202  115 GLU A CB  
880  C CG  . GLU A 115 ? 0.7062 1.0063 0.9070 0.3066  -0.0927 0.0260  115 GLU A CG  
881  C CD  . GLU A 115 ? 0.7893 1.0100 0.9374 0.3200  -0.1001 0.0440  115 GLU A CD  
882  O OE1 . GLU A 115 ? 0.8263 0.9983 0.9568 0.3350  -0.0929 0.0459  115 GLU A OE1 
883  O OE2 . GLU A 115 ? 0.8139 1.0197 0.9357 0.3144  -0.1132 0.0559  115 GLU A OE2 
884  N N   . ALA A 116 ? 0.5802 1.0277 0.8834 0.2684  -0.0626 -0.0100 116 ALA A N   
885  C CA  . ALA A 116 ? 0.5596 1.0080 0.8739 0.2617  -0.0392 -0.0190 116 ALA A CA  
886  C C   . ALA A 116 ? 0.5390 0.9129 0.8118 0.2421  -0.0262 -0.0103 116 ALA A C   
887  O O   . ALA A 116 ? 0.5298 0.8769 0.7801 0.2178  -0.0289 -0.0015 116 ALA A O   
888  C CB  . ALA A 116 ? 0.5255 1.0441 0.8805 0.2339  -0.0277 -0.0310 116 ALA A CB  
889  N N   . THR A 117 ? 0.5359 0.8795 0.7992 0.2534  -0.0125 -0.0142 117 THR A N   
890  C CA  . THR A 117 ? 0.5217 0.7998 0.7489 0.2363  -0.0007 -0.0078 117 THR A CA  
891  C C   . THR A 117 ? 0.4985 0.7915 0.7375 0.2207  0.0207  -0.0188 117 THR A C   
892  O O   . THR A 117 ? 0.4978 0.8370 0.7658 0.2338  0.0284  -0.0314 117 THR A O   
893  C CB  . THR A 117 ? 0.5521 0.7642 0.7456 0.2615  -0.0060 -0.0011 117 THR A CB  
894  O OG1 . THR A 117 ? 0.5734 0.8020 0.7832 0.2962  -0.0059 -0.0121 117 THR A OG1 
895  C CG2 . THR A 117 ? 0.5722 0.7559 0.7417 0.2699  -0.0254 0.0141  117 THR A CG2 
896  N N   . TYR A 118 ? 0.4823 0.7382 0.6977 0.1936  0.0303  -0.0140 118 TYR A N   
897  C CA  . TYR A 118 ? 0.4684 0.7308 0.6868 0.1766  0.0493  -0.0220 118 TYR A CA  
898  C C   . TYR A 118 ? 0.4834 0.6811 0.6652 0.1697  0.0551  -0.0175 118 TYR A C   
899  O O   . TYR A 118 ? 0.5093 0.6619 0.6660 0.1708  0.0459  -0.0071 118 TYR A O   
900  C CB  . TYR A 118 ? 0.4342 0.7307 0.6659 0.1443  0.0545  -0.0219 118 TYR A CB  
901  C CG  . TYR A 118 ? 0.4251 0.7878 0.6938 0.1444  0.0482  -0.0269 118 TYR A CG  
902  C CD1 . TYR A 118 ? 0.4234 0.8438 0.7249 0.1480  0.0593  -0.0387 118 TYR A CD1 
903  C CD2 . TYR A 118 ? 0.4141 0.7851 0.6849 0.1398  0.0312  -0.0207 118 TYR A CD2 
904  C CE1 . TYR A 118 ? 0.4195 0.9075 0.7588 0.1453  0.0533  -0.0440 118 TYR A CE1 
905  C CE2 . TYR A 118 ? 0.4112 0.8452 0.7165 0.1378  0.0235  -0.0264 118 TYR A CE2 
906  C CZ  . TYR A 118 ? 0.4155 0.9096 0.7569 0.1396  0.0344  -0.0380 118 TYR A CZ  
907  O OH  . TYR A 118 ? 0.4125 0.9762 0.7922 0.1349  0.0266  -0.0444 118 TYR A OH  
908  N N   . LEU A 119 ? 0.4780 0.6743 0.6567 0.1611  0.0707  -0.0255 119 LEU A N   
909  C CA  . LEU A 119 ? 0.4842 0.6268 0.6312 0.1528  0.0762  -0.0240 119 LEU A CA  
910  C C   . LEU A 119 ? 0.4655 0.6179 0.6091 0.1255  0.0880  -0.0255 119 LEU A C   
911  O O   . LEU A 119 ? 0.4649 0.6556 0.6249 0.1217  0.0994  -0.0336 119 LEU A O   
912  C CB  . LEU A 119 ? 0.5099 0.6294 0.6476 0.1765  0.0811  -0.0343 119 LEU A CB  
913  C CG  . LEU A 119 ? 0.5367 0.5877 0.6390 0.1772  0.0769  -0.0302 119 LEU A CG  
914  C CD1 . LEU A 119 ? 0.5533 0.5760 0.6443 0.1813  0.0616  -0.0160 119 LEU A CD1 
915  C CD2 . LEU A 119 ? 0.5747 0.6017 0.6667 0.2016  0.0813  -0.0432 119 LEU A CD2 
916  N N   . ALA A 120 ? 0.4546 0.5737 0.5761 0.1072  0.0855  -0.0174 120 ALA A N   
917  C CA  . ALA A 120 ? 0.4418 0.5644 0.5560 0.0835  0.0931  -0.0167 120 ALA A CA  
918  C C   . ALA A 120 ? 0.4666 0.5496 0.5542 0.0780  0.0968  -0.0180 120 ALA A C   
919  O O   . ALA A 120 ? 0.4898 0.5385 0.5623 0.0799  0.0896  -0.0132 120 ALA A O   
920  C CB  . ALA A 120 ? 0.4211 0.5469 0.5350 0.0674  0.0851  -0.0073 120 ALA A CB  
921  N N   . LEU A 121 ? 0.4683 0.5576 0.5491 0.0695  0.1078  -0.0243 121 LEU A N   
922  C CA  . LEU A 121 ? 0.4795 0.5367 0.5348 0.0618  0.1098  -0.0263 121 LEU A CA  
923  C C   . LEU A 121 ? 0.4651 0.5162 0.5093 0.0425  0.1063  -0.0182 121 LEU A C   
924  O O   . LEU A 121 ? 0.4704 0.4959 0.4981 0.0369  0.1014  -0.0164 121 LEU A O   
925  C CB  . LEU A 121 ? 0.5006 0.5651 0.5485 0.0651  0.1226  -0.0378 121 LEU A CB  
926  C CG  . LEU A 121 ? 0.5215 0.5573 0.5410 0.0564  0.1241  -0.0418 121 LEU A CG  
927  C CD1 . LEU A 121 ? 0.5353 0.5315 0.5416 0.0613  0.1151  -0.0433 121 LEU A CD1 
928  C CD2 . LEU A 121 ? 0.5459 0.5931 0.5562 0.0607  0.1378  -0.0537 121 LEU A CD2 
929  N N   . ASN A 122 ? 0.4563 0.5303 0.5089 0.0323  0.1080  -0.0140 122 ASN A N   
930  C CA  . ASN A 122 ? 0.4607 0.5249 0.5009 0.0178  0.1032  -0.0068 122 ASN A CA  
931  C C   . ASN A 122 ? 0.4650 0.5293 0.5135 0.0179  0.0928  0.0003  122 ASN A C   
932  O O   . ASN A 122 ? 0.4794 0.5259 0.5196 0.0190  0.0860  0.0038  122 ASN A O   
933  C CB  . ASN A 122 ? 0.4613 0.5394 0.4977 0.0048  0.1107  -0.0058 122 ASN A CB  
934  C CG  . ASN A 122 ? 0.4797 0.5483 0.4949 0.0009  0.1191  -0.0098 122 ASN A CG  
935  O OD1 . ASN A 122 ? 0.4923 0.5419 0.4942 0.0064  0.1169  -0.0136 122 ASN A OD1 
936  N ND2 . ASN A 122 ? 0.4911 0.5720 0.5005 -0.0104 0.1284  -0.0086 122 ASN A ND2 
937  N N   . GLU A 123 ? 0.4534 0.5401 0.5176 0.0155  0.0916  0.0017  123 GLU A N   
938  C CA  . GLU A 123 ? 0.4386 0.5256 0.5069 0.0151  0.0813  0.0071  123 GLU A CA  
939  C C   . GLU A 123 ? 0.4317 0.5492 0.5224 0.0166  0.0793  0.0054  123 GLU A C   
940  O O   . GLU A 123 ? 0.4271 0.5695 0.5324 0.0161  0.0871  0.0003  123 GLU A O   
941  C CB  . GLU A 123 ? 0.4423 0.5154 0.4946 0.0033  0.0776  0.0109  123 GLU A CB  
942  C CG  . GLU A 123 ? 0.4546 0.5367 0.5071 -0.0106 0.0807  0.0106  123 GLU A CG  
943  C CD  . GLU A 123 ? 0.4771 0.5605 0.5225 -0.0172 0.0922  0.0085  123 GLU A CD  
944  O OE1 . GLU A 123 ? 0.4878 0.5513 0.5146 -0.0155 0.0937  0.0089  123 GLU A OE1 
945  O OE2 . GLU A 123 ? 0.4843 0.5914 0.5424 -0.0245 0.0997  0.0061  123 GLU A OE2 
946  N N   . SER A 124 ? 0.4284 0.5476 0.5220 0.0184  0.0688  0.0091  124 SER A N   
947  C CA  . SER A 124 ? 0.4194 0.5687 0.5328 0.0178  0.0630  0.0073  124 SER A CA  
948  C C   . SER A 124 ? 0.3997 0.5405 0.5025 0.0061  0.0545  0.0098  124 SER A C   
949  O O   . SER A 124 ? 0.4124 0.5301 0.4979 0.0096  0.0492  0.0137  124 SER A O   
950  C CB  . SER A 124 ? 0.4283 0.5874 0.5532 0.0372  0.0557  0.0081  124 SER A CB  
951  O OG  . SER A 124 ? 0.4208 0.6129 0.5651 0.0372  0.0474  0.0060  124 SER A OG  
952  N N   . THR A 125 ? 0.3924 0.5520 0.5048 -0.0085 0.0536  0.0067  125 THR A N   
953  C CA  . THR A 125 ? 0.4109 0.5567 0.5098 -0.0210 0.0453  0.0069  125 THR A CA  
954  C C   . THR A 125 ? 0.4262 0.6023 0.5436 -0.0250 0.0351  0.0030  125 THR A C   
955  O O   . THR A 125 ? 0.4261 0.6406 0.5705 -0.0245 0.0371  -0.0004 125 THR A O   
956  C CB  . THR A 125 ? 0.4316 0.5595 0.5159 -0.0402 0.0516  0.0070  125 THR A CB  
957  O OG1 . THR A 125 ? 0.4288 0.5871 0.5326 -0.0552 0.0580  0.0040  125 THR A OG1 
958  C CG2 . THR A 125 ? 0.4436 0.5475 0.5110 -0.0354 0.0606  0.0102  125 THR A CG2 
959  N N   . VAL A 126 ? 0.4487 0.6100 0.5512 -0.0281 0.0237  0.0023  126 VAL A N   
960  C CA  . VAL A 126 ? 0.4610 0.6470 0.5756 -0.0345 0.0112  -0.0026 126 VAL A CA  
961  C C   . VAL A 126 ? 0.4996 0.6617 0.5952 -0.0555 0.0066  -0.0065 126 VAL A C   
962  O O   . VAL A 126 ? 0.5106 0.6340 0.5772 -0.0523 0.0047  -0.0055 126 VAL A O   
963  C CB  . VAL A 126 ? 0.4428 0.6309 0.5520 -0.0160 -0.0008 -0.0008 126 VAL A CB  
964  C CG1 . VAL A 126 ? 0.4618 0.6814 0.5852 -0.0216 -0.0155 -0.0069 126 VAL A CG1 
965  C CG2 . VAL A 126 ? 0.4116 0.6072 0.5301 0.0052  0.0035  0.0048  126 VAL A CG2 
966  N N   . LYS A 127 ? 0.5303 0.7153 0.6418 -0.0768 0.0049  -0.0115 127 LYS A N   
967  C CA  . LYS A 127 ? 0.5837 0.7431 0.6762 -0.0999 -0.0017 -0.0161 127 LYS A CA  
968  C C   . LYS A 127 ? 0.6218 0.8174 0.7339 -0.1120 -0.0155 -0.0241 127 LYS A C   
969  O O   . LYS A 127 ? 0.6197 0.8641 0.7625 -0.1018 -0.0190 -0.0254 127 LYS A O   
970  C CB  . LYS A 127 ? 0.6047 0.7476 0.6906 -0.1228 0.0106  -0.0134 127 LYS A CB  
971  C CG  . LYS A 127 ? 0.6238 0.7298 0.6868 -0.1116 0.0216  -0.0061 127 LYS A CG  
972  C CD  . LYS A 127 ? 0.6780 0.7622 0.7270 -0.1350 0.0317  -0.0023 127 LYS A CD  
973  C CE  . LYS A 127 ? 0.6970 0.7501 0.7243 -0.1221 0.0412  0.0047  127 LYS A CE  
974  N NZ  . LYS A 127 ? 0.7445 0.7728 0.7522 -0.1439 0.0504  0.0102  127 LYS A NZ  
975  N N   . SER A 128 ? 0.6703 0.8401 0.7630 -0.1331 -0.0248 -0.0301 128 SER A N   
976  C CA  . SER A 128 ? 0.7134 0.9131 0.8201 -0.1480 -0.0406 -0.0396 128 SER A CA  
977  C C   . SER A 128 ? 0.7553 0.9877 0.8881 -0.1814 -0.0357 -0.0424 128 SER A C   
978  O O   . SER A 128 ? 0.7641 0.9720 0.8865 -0.2000 -0.0226 -0.0377 128 SER A O   
979  C CB  . SER A 128 ? 0.7554 0.9072 0.8238 -0.1534 -0.0550 -0.0470 128 SER A CB  
980  O OG  . SER A 128 ? 0.7772 0.9572 0.8573 -0.1701 -0.0719 -0.0576 128 SER A OG  
981  N N   . SER A 129 ? 0.7885 1.0793 0.9551 -0.1894 -0.0466 -0.0498 129 SER A N   
982  C CA  . SER A 129 ? 0.8291 1.1651 1.0272 -0.2236 -0.0427 -0.0540 129 SER A CA  
983  C C   . SER A 129 ? 0.9192 1.2251 1.0958 -0.2580 -0.0566 -0.0627 129 SER A C   
984  O O   . SER A 129 ? 0.9295 1.2704 1.1223 -0.2687 -0.0743 -0.0731 129 SER A O   
985  C CB  . SER A 129 ? 0.7911 1.2131 1.0412 -0.2127 -0.0477 -0.0587 129 SER A CB  
986  O OG  . SER A 129 ? 0.7880 1.2249 1.0386 -0.2029 -0.0711 -0.0665 129 SER A OG  
987  N N   . GLY A 130 ? 1.0067 1.2433 1.1432 -0.2749 -0.0497 -0.0587 130 GLY A N   
988  C CA  . GLY A 130 ? 1.0654 1.2589 1.1739 -0.3087 -0.0618 -0.0665 130 GLY A CA  
989  C C   . GLY A 130 ? 1.0884 1.2184 1.1508 -0.2912 -0.0775 -0.0729 130 GLY A C   
990  O O   . GLY A 130 ? 1.1285 1.1838 1.1461 -0.2927 -0.0749 -0.0704 130 GLY A O   
991  N N   . GLY A 131 ? 1.0287 1.1883 1.0999 -0.2727 -0.0939 -0.0812 131 GLY A N   
992  C CA  . GLY A 131 ? 0.9897 1.0981 1.0181 -0.2570 -0.1089 -0.0893 131 GLY A CA  
993  C C   . GLY A 131 ? 0.9161 0.9826 0.9161 -0.2201 -0.0992 -0.0812 131 GLY A C   
994  O O   . GLY A 131 ? 0.8665 0.9340 0.8755 -0.2094 -0.0816 -0.0691 131 GLY A O   
995  N N   . PRO A 132 ? 0.9014 0.9332 0.8664 -0.2008 -0.1105 -0.0886 132 PRO A N   
996  C CA  . PRO A 132 ? 0.8599 0.8579 0.7995 -0.1671 -0.1012 -0.0821 132 PRO A CA  
997  C C   . PRO A 132 ? 0.7645 0.8114 0.7317 -0.1391 -0.0940 -0.0722 132 PRO A C   
998  O O   . PRO A 132 ? 0.7428 0.8407 0.7359 -0.1360 -0.1026 -0.0735 132 PRO A O   
999  C CB  . PRO A 132 ? 0.9094 0.8658 0.8060 -0.1574 -0.1159 -0.0956 132 PRO A CB  
1000 C CG  . PRO A 132 ? 0.9380 0.9286 0.8471 -0.1754 -0.1345 -0.1070 132 PRO A CG  
1001 C CD  . PRO A 132 ? 0.9434 0.9656 0.8885 -0.2104 -0.1320 -0.1046 132 PRO A CD  
1002 N N   . PHE A 133 ? 0.7014 0.7302 0.6610 -0.1184 -0.0794 -0.0623 133 PHE A N   
1003 C CA  . PHE A 133 ? 0.6100 0.6739 0.5906 -0.0939 -0.0712 -0.0520 133 PHE A CA  
1004 C C   . PHE A 133 ? 0.5869 0.6374 0.5410 -0.0683 -0.0755 -0.0532 133 PHE A C   
1005 O O   . PHE A 133 ? 0.6018 0.6130 0.5268 -0.0577 -0.0705 -0.0542 133 PHE A O   
1006 C CB  . PHE A 133 ? 0.5740 0.6298 0.5629 -0.0896 -0.0529 -0.0411 133 PHE A CB  
1007 C CG  . PHE A 133 ? 0.5235 0.6082 0.5313 -0.0669 -0.0444 -0.0313 133 PHE A CG  
1008 C CD1 . PHE A 133 ? 0.4885 0.6213 0.5317 -0.0662 -0.0442 -0.0281 133 PHE A CD1 
1009 C CD2 . PHE A 133 ? 0.5205 0.5836 0.5102 -0.0466 -0.0371 -0.0259 133 PHE A CD2 
1010 C CE1 . PHE A 133 ? 0.4660 0.6158 0.5214 -0.0449 -0.0374 -0.0195 133 PHE A CE1 
1011 C CE2 . PHE A 133 ? 0.4917 0.5753 0.4957 -0.0296 -0.0298 -0.0169 133 PHE A CE2 
1012 C CZ  . PHE A 133 ? 0.4663 0.5886 0.5007 -0.0286 -0.0303 -0.0136 133 PHE A CZ  
1013 N N   . VAL A 134 ? 0.5586 0.6435 0.5218 -0.0579 -0.0848 -0.0529 134 VAL A N   
1014 C CA  . VAL A 134 ? 0.5516 0.6298 0.4891 -0.0355 -0.0879 -0.0522 134 VAL A CA  
1015 C C   . VAL A 134 ? 0.5215 0.6374 0.4802 -0.0197 -0.0866 -0.0404 134 VAL A C   
1016 O O   . VAL A 134 ? 0.5326 0.6848 0.5144 -0.0234 -0.0972 -0.0411 134 VAL A O   
1017 C CB  . VAL A 134 ? 0.5865 0.6557 0.4970 -0.0395 -0.1059 -0.0661 134 VAL A CB  
1018 C CG1 . VAL A 134 ? 0.5880 0.6520 0.4688 -0.0161 -0.1063 -0.0644 134 VAL A CG1 
1019 C CG2 . VAL A 134 ? 0.6268 0.6510 0.5131 -0.0558 -0.1092 -0.0790 134 VAL A CG2 
1020 N N   . VAL A 135 ? 0.4970 0.6041 0.4478 -0.0022 -0.0743 -0.0299 135 VAL A N   
1021 C CA  . VAL A 135 ? 0.4921 0.6224 0.4551 0.0132  -0.0725 -0.0175 135 VAL A CA  
1022 C C   . VAL A 135 ? 0.5122 0.6260 0.4449 0.0289  -0.0669 -0.0110 135 VAL A C   
1023 O O   . VAL A 135 ? 0.5311 0.6215 0.4458 0.0301  -0.0573 -0.0135 135 VAL A O   
1024 C CB  . VAL A 135 ? 0.4724 0.6124 0.4655 0.0134  -0.0596 -0.0090 135 VAL A CB  
1025 C CG1 . VAL A 135 ? 0.4660 0.6343 0.4921 -0.0007 -0.0640 -0.0143 135 VAL A CG1 
1026 C CG2 . VAL A 135 ? 0.4671 0.5786 0.4515 0.0110  -0.0441 -0.0074 135 VAL A CG2 
1027 N N   . ASP A 136 ? 0.5250 0.6524 0.4514 0.0413  -0.0730 -0.0023 136 ASP A N   
1028 C CA  . ASP A 136 ? 0.5531 0.6683 0.4526 0.0536  -0.0651 0.0076  136 ASP A CA  
1029 C C   . ASP A 136 ? 0.5527 0.6645 0.4677 0.0579  -0.0512 0.0212  136 ASP A C   
1030 O O   . ASP A 136 ? 0.5582 0.6821 0.4955 0.0615  -0.0544 0.0273  136 ASP A O   
1031 C CB  . ASP A 136 ? 0.5806 0.7054 0.4582 0.0636  -0.0789 0.0122  136 ASP A CB  
1032 C CG  . ASP A 136 ? 0.6196 0.7420 0.4704 0.0606  -0.0909 -0.0020 136 ASP A CG  
1033 O OD1 . ASP A 136 ? 0.6311 0.7352 0.4645 0.0575  -0.0832 -0.0113 136 ASP A OD1 
1034 O OD2 . ASP A 136 ? 0.6441 0.7827 0.4903 0.0626  -0.1092 -0.0050 136 ASP A OD2 
1035 N N   . VAL A 137 ? 0.5530 0.6499 0.4568 0.0581  -0.0363 0.0246  137 VAL A N   
1036 C CA  . VAL A 137 ? 0.5265 0.6174 0.4422 0.0589  -0.0232 0.0356  137 VAL A CA  
1037 C C   . VAL A 137 ? 0.5460 0.6311 0.4391 0.0659  -0.0202 0.0498  137 VAL A C   
1038 O O   . VAL A 137 ? 0.5619 0.6453 0.4279 0.0673  -0.0170 0.0503  137 VAL A O   
1039 C CB  . VAL A 137 ? 0.5039 0.5859 0.4232 0.0533  -0.0100 0.0308  137 VAL A CB  
1040 C CG1 . VAL A 137 ? 0.4848 0.5621 0.4174 0.0519  0.0015  0.0405  137 VAL A CG1 
1041 C CG2 . VAL A 137 ? 0.4786 0.5587 0.4117 0.0456  -0.0138 0.0184  137 VAL A CG2 
1042 N N   . VAL A 138 ? 0.5435 0.6236 0.4452 0.0703  -0.0208 0.0613  138 VAL A N   
1043 C CA  . VAL A 138 ? 0.5665 0.6330 0.4435 0.0756  -0.0196 0.0774  138 VAL A CA  
1044 C C   . VAL A 138 ? 0.5593 0.6088 0.4450 0.0713  -0.0073 0.0865  138 VAL A C   
1045 O O   . VAL A 138 ? 0.5479 0.5954 0.4579 0.0737  -0.0084 0.0845  138 VAL A O   
1046 C CB  . VAL A 138 ? 0.5920 0.6608 0.4628 0.0884  -0.0369 0.0834  138 VAL A CB  
1047 C CG1 . VAL A 138 ? 0.6333 0.6794 0.4717 0.0937  -0.0359 0.1024  138 VAL A CG1 
1048 C CG2 . VAL A 138 ? 0.6048 0.6927 0.4678 0.0903  -0.0511 0.0724  138 VAL A CG2 
1049 N N   . ILE A 139 ? 0.5731 0.6123 0.4389 0.0639  0.0047  0.0954  139 ILE A N   
1050 C CA  . ILE A 139 ? 0.5691 0.5908 0.4396 0.0556  0.0161  0.1037  139 ILE A CA  
1051 C C   . ILE A 139 ? 0.6090 0.6057 0.4486 0.0557  0.0160  0.1225  139 ILE A C   
1052 O O   . ILE A 139 ? 0.6328 0.6319 0.4453 0.0501  0.0216  0.1297  139 ILE A O   
1053 C CB  . ILE A 139 ? 0.5489 0.5826 0.4253 0.0430  0.0308  0.0979  139 ILE A CB  
1054 C CG1 . ILE A 139 ? 0.5080 0.5597 0.4068 0.0449  0.0291  0.0807  139 ILE A CG1 
1055 C CG2 . ILE A 139 ? 0.5570 0.5747 0.4407 0.0322  0.0404  0.1045  139 ILE A CG2 
1056 C CD1 . ILE A 139 ? 0.4833 0.5482 0.3876 0.0376  0.0408  0.0741  139 ILE A CD1 
1057 N N   . ASN A 140 ? 0.6258 0.5966 0.4669 0.0625  0.0100  0.1304  140 ASN A N   
1058 C CA  . ASN A 140 ? 0.6778 0.6133 0.4856 0.0638  0.0080  0.1499  140 ASN A CA  
1059 C C   . ASN A 140 ? 0.7220 0.6611 0.4983 0.0725  -0.0016 0.1580  140 ASN A C   
1060 O O   . ASN A 140 ? 0.7779 0.7045 0.5196 0.0634  0.0051  0.1718  140 ASN A O   
1061 C CB  . ASN A 140 ? 0.6865 0.6046 0.4806 0.0422  0.0246  0.1595  140 ASN A CB  
1062 C CG  . ASN A 140 ? 0.6610 0.5722 0.4821 0.0336  0.0318  0.1516  140 ASN A CG  
1063 O OD1 . ASN A 140 ? 0.6423 0.5432 0.4811 0.0458  0.0243  0.1454  140 ASN A OD1 
1064 N ND2 . ASN A 140 ? 0.6568 0.5771 0.4811 0.0130  0.0462  0.1509  140 ASN A ND2 
1065 N N   . ASP A 141 ? 0.7095 0.6684 0.4978 0.0889  -0.0175 0.1488  141 ASP A N   
1066 C CA  . ASP A 141 ? 0.7502 0.7164 0.5116 0.0999  -0.0314 0.1532  141 ASP A CA  
1067 C C   . ASP A 141 ? 0.7766 0.7618 0.5172 0.0895  -0.0232 0.1494  141 ASP A C   
1068 O O   . ASP A 141 ? 0.8296 0.8133 0.5350 0.0950  -0.0306 0.1569  141 ASP A O   
1069 C CB  . ASP A 141 ? 0.8086 0.7364 0.5321 0.1097  -0.0396 0.1751  141 ASP A CB  
1070 C CG  . ASP A 141 ? 0.8283 0.7336 0.5683 0.1252  -0.0489 0.1779  141 ASP A CG  
1071 O OD1 . ASP A 141 ? 0.8028 0.7341 0.5831 0.1339  -0.0548 0.1620  141 ASP A OD1 
1072 O OD2 . ASP A 141 ? 0.7161 0.5760 0.4265 0.1287  -0.0499 0.1960  141 ASP A OD2 
1073 N N   . ILE A 142 ? 0.7604 0.7638 0.5201 0.0767  -0.0088 0.1372  142 ILE A N   
1074 C CA  . ILE A 142 ? 0.7838 0.8074 0.5265 0.0702  0.0001  0.1305  142 ILE A CA  
1075 C C   . ILE A 142 ? 0.7221 0.7701 0.4928 0.0721  -0.0032 0.1080  142 ILE A C   
1076 O O   . ILE A 142 ? 0.6692 0.7203 0.4726 0.0677  0.0016  0.1000  142 ILE A O   
1077 C CB  . ILE A 142 ? 0.8316 0.8541 0.5664 0.0537  0.0218  0.1380  142 ILE A CB  
1078 C CG1 . ILE A 142 ? 0.9145 0.9045 0.6213 0.0471  0.0255  0.1617  142 ILE A CG1 
1079 C CG2 . ILE A 142 ? 0.8302 0.8781 0.5454 0.0512  0.0314  0.1307  142 ILE A CG2 
1080 C CD1 . ILE A 142 ? 0.9479 0.9393 0.6488 0.0258  0.0469  0.1698  142 ILE A CD1 
1081 N N   . HIS A 143 ? 0.7206 0.7822 0.4746 0.0779  -0.0118 0.0980  143 HIS A N   
1082 C CA  . HIS A 143 ? 0.6910 0.7677 0.4642 0.0781  -0.0159 0.0769  143 HIS A CA  
1083 C C   . HIS A 143 ? 0.6606 0.7444 0.4406 0.0715  0.0017  0.0691  143 HIS A C   
1084 O O   . HIS A 143 ? 0.6899 0.7801 0.4469 0.0698  0.0140  0.0728  143 HIS A O   
1085 C CB  . HIS A 143 ? 0.7223 0.8068 0.4698 0.0849  -0.0297 0.0672  143 HIS A CB  
1086 C CG  . HIS A 143 ? 0.7265 0.8181 0.4872 0.0833  -0.0353 0.0454  143 HIS A CG  
1087 N ND1 . HIS A 143 ? 0.7277 0.8208 0.4771 0.0829  -0.0251 0.0330  143 HIS A ND1 
1088 C CD2 . HIS A 143 ? 0.7144 0.8103 0.4972 0.0813  -0.0500 0.0339  143 HIS A CD2 
1089 C CE1 . HIS A 143 ? 0.7237 0.8138 0.4837 0.0813  -0.0343 0.0154  143 HIS A CE1 
1090 N NE2 . HIS A 143 ? 0.7109 0.8035 0.4915 0.0779  -0.0489 0.0160  143 HIS A NE2 
1091 N N   . PHE A 144 ? 0.6024 0.6875 0.4136 0.0684  0.0030  0.0585  144 PHE A N   
1092 C CA  . PHE A 144 ? 0.5647 0.6566 0.3855 0.0649  0.0169  0.0510  144 PHE A CA  
1093 C C   . PHE A 144 ? 0.5579 0.6514 0.3770 0.0699  0.0121  0.0316  144 PHE A C   
1094 O O   . PHE A 144 ? 0.5827 0.6845 0.3880 0.0747  0.0205  0.0240  144 PHE A O   
1095 C CB  . PHE A 144 ? 0.5255 0.6123 0.3775 0.0580  0.0226  0.0549  144 PHE A CB  
1096 C CG  . PHE A 144 ? 0.5053 0.6013 0.3685 0.0554  0.0347  0.0480  144 PHE A CG  
1097 C CD1 . PHE A 144 ? 0.5069 0.6172 0.3617 0.0518  0.0486  0.0535  144 PHE A CD1 
1098 C CD2 . PHE A 144 ? 0.4901 0.5823 0.3719 0.0563  0.0317  0.0364  144 PHE A CD2 
1099 C CE1 . PHE A 144 ? 0.4912 0.6170 0.3596 0.0514  0.0581  0.0462  144 PHE A CE1 
1100 C CE2 . PHE A 144 ? 0.4776 0.5781 0.3679 0.0570  0.0405  0.0304  144 PHE A CE2 
1101 C CZ  . PHE A 144 ? 0.4757 0.5955 0.3612 0.0558  0.0529  0.0346  144 PHE A CZ  
1102 N N   . GLU A 145 ? 0.5301 0.6156 0.3621 0.0687  -0.0012 0.0231  145 GLU A N   
1103 C CA  . GLU A 145 ? 0.5226 0.6001 0.3501 0.0705  -0.0068 0.0053  145 GLU A CA  
1104 C C   . GLU A 145 ? 0.5381 0.6103 0.3743 0.0647  -0.0236 -0.0008 145 GLU A C   
1105 O O   . GLU A 145 ? 0.5356 0.6146 0.3922 0.0605  -0.0283 0.0076  145 GLU A O   
1106 C CB  . GLU A 145 ? 0.4852 0.5570 0.3300 0.0693  0.0022  0.0006  145 GLU A CB  
1107 C CG  . GLU A 145 ? 0.4602 0.5283 0.3355 0.0603  0.0018  0.0064  145 GLU A CG  
1108 C CD  . GLU A 145 ? 0.4484 0.5102 0.3359 0.0597  0.0097  0.0028  145 GLU A CD  
1109 O OE1 . GLU A 145 ? 0.4314 0.4901 0.3404 0.0525  0.0109  0.0070  145 GLU A OE1 
1110 O OE2 . GLU A 145 ? 0.4610 0.5223 0.3356 0.0681  0.0144  -0.0046 145 GLU A OE2 
1111 N N   . ARG A 146 ? 0.5570 0.6178 0.3775 0.0646  -0.0327 -0.0166 146 ARG A N   
1112 C CA  . ARG A 146 ? 0.5672 0.6234 0.3973 0.0543  -0.0483 -0.0252 146 ARG A CA  
1113 C C   . ARG A 146 ? 0.5706 0.6070 0.4125 0.0464  -0.0453 -0.0330 146 ARG A C   
1114 O O   . ARG A 146 ? 0.5983 0.6119 0.4189 0.0495  -0.0464 -0.0456 146 ARG A O   
1115 C CB  . ARG A 146 ? 0.5917 0.6437 0.3920 0.0560  -0.0628 -0.0376 146 ARG A CB  
1116 C CG  . ARG A 146 ? 0.6019 0.6497 0.4118 0.0412  -0.0796 -0.0490 146 ARG A CG  
1117 C CD  . ARG A 146 ? 0.6330 0.6872 0.4188 0.0418  -0.0973 -0.0578 146 ARG A CD  
1118 N NE  . ARG A 146 ? 0.6278 0.7114 0.4235 0.0464  -0.1040 -0.0448 146 ARG A NE  
1119 C CZ  . ARG A 146 ? 0.6610 0.7576 0.4406 0.0479  -0.1218 -0.0490 146 ARG A CZ  
1120 N NH1 . ARG A 146 ? 0.6946 0.7776 0.4473 0.0429  -0.1344 -0.0673 146 ARG A NH1 
1121 N NH2 . ARG A 146 ? 0.6572 0.7779 0.4451 0.0554  -0.1285 -0.0355 146 ARG A NH2 
1122 N N   . PHE A 147 ? 0.5434 0.5860 0.4161 0.0375  -0.0415 -0.0255 147 PHE A N   
1123 C CA  . PHE A 147 ? 0.5401 0.5634 0.4218 0.0295  -0.0370 -0.0295 147 PHE A CA  
1124 C C   . PHE A 147 ? 0.5655 0.5757 0.4463 0.0133  -0.0496 -0.0402 147 PHE A C   
1125 O O   . PHE A 147 ? 0.5801 0.6113 0.4764 0.0036  -0.0590 -0.0401 147 PHE A O   
1126 C CB  . PHE A 147 ? 0.5109 0.5469 0.4223 0.0258  -0.0270 -0.0176 147 PHE A CB  
1127 C CG  . PHE A 147 ? 0.5089 0.5258 0.4264 0.0178  -0.0217 -0.0196 147 PHE A CG  
1128 C CD1 . PHE A 147 ? 0.5220 0.5358 0.4522 0.0008  -0.0262 -0.0223 147 PHE A CD1 
1129 C CD2 . PHE A 147 ? 0.4919 0.4962 0.4019 0.0268  -0.0123 -0.0181 147 PHE A CD2 
1130 C CE1 . PHE A 147 ? 0.5242 0.5168 0.4543 -0.0076 -0.0208 -0.0222 147 PHE A CE1 
1131 C CE2 . PHE A 147 ? 0.4916 0.4759 0.4027 0.0211  -0.0091 -0.0187 147 PHE A CE2 
1132 C CZ  . PHE A 147 ? 0.5104 0.4858 0.4290 0.0037  -0.0130 -0.0200 147 PHE A CZ  
1133 N N   . ARG A 148 ? 0.5811 0.5566 0.4434 0.0102  -0.0504 -0.0495 148 ARG A N   
1134 C CA  . ARG A 148 ? 0.6192 0.5738 0.4790 -0.0103 -0.0603 -0.0580 148 ARG A CA  
1135 C C   . ARG A 148 ? 0.6365 0.5573 0.4908 -0.0145 -0.0532 -0.0568 148 ARG A C   
1136 O O   . ARG A 148 ? 0.6579 0.5481 0.4863 -0.0002 -0.0512 -0.0619 148 ARG A O   
1137 C CB  . ARG A 148 ? 0.6806 0.6128 0.5085 -0.0114 -0.0747 -0.0739 148 ARG A CB  
1138 C CG  . ARG A 148 ? 0.7234 0.6283 0.5462 -0.0370 -0.0853 -0.0830 148 ARG A CG  
1139 C CD  . ARG A 148 ? 0.7701 0.6559 0.5632 -0.0419 -0.1023 -0.0999 148 ARG A CD  
1140 N NE  . ARG A 148 ? 0.8029 0.6589 0.5906 -0.0709 -0.1122 -0.1082 148 ARG A NE  
1141 C CZ  . ARG A 148 ? 0.7019 0.5418 0.4694 -0.0854 -0.1294 -0.1237 148 ARG A CZ  
1142 N NH1 . ARG A 148 ? 0.7151 0.5672 0.4646 -0.0712 -0.1389 -0.1330 148 ARG A NH1 
1143 N NH2 . ARG A 148 ? 0.7384 0.5494 0.5018 -0.1161 -0.1371 -0.1299 148 ARG A NH2 
1144 N N   . GLY A 149 ? 0.6396 0.5674 0.5170 -0.0327 -0.0493 -0.0501 149 GLY A N   
1145 C CA  . GLY A 149 ? 0.6434 0.5386 0.5131 -0.0392 -0.0430 -0.0467 149 GLY A CA  
1146 C C   . GLY A 149 ? 0.6176 0.5265 0.5115 -0.0646 -0.0396 -0.0409 149 GLY A C   
1147 O O   . GLY A 149 ? 0.6300 0.5553 0.5357 -0.0838 -0.0474 -0.0455 149 GLY A O   
1148 N N   . ASP A 150 ? 0.5880 0.4943 0.4897 -0.0651 -0.0278 -0.0314 150 ASP A N   
1149 C CA  . ASP A 150 ? 0.5545 0.4792 0.4789 -0.0878 -0.0213 -0.0255 150 ASP A CA  
1150 C C   . ASP A 150 ? 0.5187 0.4977 0.4809 -0.0814 -0.0135 -0.0194 150 ASP A C   
1151 O O   . ASP A 150 ? 0.5338 0.5451 0.5221 -0.0980 -0.0113 -0.0187 150 ASP A O   
1152 C CB  . ASP A 150 ? 0.5483 0.4371 0.4551 -0.0932 -0.0130 -0.0187 150 ASP A CB  
1153 C CG  . ASP A 150 ? 0.6213 0.4522 0.4915 -0.1078 -0.0213 -0.0232 150 ASP A CG  
1154 O OD1 . ASP A 150 ? 0.6614 0.4792 0.5198 -0.1131 -0.0334 -0.0335 150 ASP A OD1 
1155 O OD2 . ASP A 150 ? 0.6541 0.4489 0.5040 -0.1138 -0.0164 -0.0166 150 ASP A OD2 
1156 N N   . GLY A 151 ? 0.4824 0.4722 0.4477 -0.0582 -0.0092 -0.0154 151 GLY A N   
1157 C CA  . GLY A 151 ? 0.4513 0.4828 0.4465 -0.0504 -0.0034 -0.0100 151 GLY A CA  
1158 C C   . GLY A 151 ? 0.4365 0.4653 0.4275 -0.0297 0.0034  -0.0044 151 GLY A C   
1159 O O   . GLY A 151 ? 0.4464 0.4503 0.4151 -0.0201 0.0030  -0.0054 151 GLY A O   
1160 N N   . LEU A 152 ? 0.4217 0.4779 0.4351 -0.0232 0.0093  0.0009  152 LEU A N   
1161 C CA  . LEU A 152 ? 0.4048 0.4602 0.4168 -0.0081 0.0159  0.0066  152 LEU A CA  
1162 C C   . LEU A 152 ? 0.3967 0.4625 0.4253 -0.0095 0.0261  0.0104  152 LEU A C   
1163 O O   . LEU A 152 ? 0.3940 0.4768 0.4392 -0.0189 0.0286  0.0089  152 LEU A O   
1164 C CB  . LEU A 152 ? 0.3931 0.4631 0.4074 0.0042  0.0109  0.0092  152 LEU A CB  
1165 C CG  . LEU A 152 ? 0.3936 0.4541 0.3865 0.0088  0.0025  0.0054  152 LEU A CG  
1166 C CD1 . LEU A 152 ? 0.4145 0.4915 0.4083 0.0183  -0.0033 0.0093  152 LEU A CD1 
1167 C CD2 . LEU A 152 ? 0.3583 0.3998 0.3320 0.0161  0.0077  0.0052  152 LEU A CD2 
1168 N N   . CYS A 153 ? 0.4112 0.4691 0.4351 -0.0007 0.0323  0.0142  153 CYS A N   
1169 C CA  . CYS A 153 ? 0.4283 0.4904 0.4620 -0.0011 0.0416  0.0161  153 CYS A CA  
1170 C C   . CYS A 153 ? 0.4208 0.4812 0.4543 0.0097  0.0443  0.0200  153 CYS A C   
1171 O O   . CYS A 153 ? 0.4186 0.4678 0.4394 0.0127  0.0444  0.0214  153 CYS A O   
1172 C CB  . CYS A 153 ? 0.4614 0.5051 0.4815 -0.0088 0.0464  0.0156  153 CYS A CB  
1173 S SG  . CYS A 153 ? 0.4721 0.5176 0.4962 -0.0083 0.0574  0.0167  153 CYS A SG  
1174 N N   . MET A 154 ? 0.4274 0.4990 0.4748 0.0155  0.0462  0.0213  154 MET A N   
1175 C CA  . MET A 154 ? 0.4408 0.5035 0.4854 0.0231  0.0488  0.0251  154 MET A CA  
1176 C C   . MET A 154 ? 0.4708 0.5288 0.5184 0.0219  0.0571  0.0222  154 MET A C   
1177 O O   . MET A 154 ? 0.4901 0.5604 0.5502 0.0233  0.0607  0.0184  154 MET A O   
1178 C CB  . MET A 154 ? 0.4396 0.5083 0.4906 0.0334  0.0436  0.0288  154 MET A CB  
1179 C CG  . MET A 154 ? 0.4643 0.5144 0.5058 0.0388  0.0452  0.0347  154 MET A CG  
1180 S SD  . MET A 154 ? 0.4896 0.5302 0.5123 0.0334  0.0446  0.0408  154 MET A SD  
1181 C CE  . MET A 154 ? 0.5180 0.5667 0.5349 0.0405  0.0350  0.0457  154 MET A CE  
1182 N N   . SER A 155 ? 0.4861 0.5300 0.5225 0.0193  0.0600  0.0228  155 SER A N   
1183 C CA  . SER A 155 ? 0.4804 0.5179 0.5141 0.0166  0.0665  0.0186  155 SER A CA  
1184 C C   . SER A 155 ? 0.4591 0.4828 0.4894 0.0198  0.0680  0.0188  155 SER A C   
1185 O O   . SER A 155 ? 0.4652 0.4814 0.4907 0.0193  0.0648  0.0237  155 SER A O   
1186 C CB  . SER A 155 ? 0.4943 0.5262 0.5155 0.0100  0.0664  0.0177  155 SER A CB  
1187 O OG  . SER A 155 ? 0.5080 0.5325 0.5225 0.0079  0.0707  0.0142  155 SER A OG  
1188 N N   . THR A 156 ? 0.4358 0.4546 0.4661 0.0218  0.0734  0.0131  156 THR A N   
1189 C CA  . THR A 156 ? 0.4380 0.4367 0.4602 0.0225  0.0745  0.0106  156 THR A CA  
1190 C C   . THR A 156 ? 0.4284 0.4220 0.4395 0.0119  0.0739  0.0090  156 THR A C   
1191 O O   . THR A 156 ? 0.4241 0.4284 0.4328 0.0079  0.0731  0.0094  156 THR A O   
1192 C CB  . THR A 156 ? 0.4590 0.4547 0.4832 0.0308  0.0804  0.0025  156 THR A CB  
1193 O OG1 . THR A 156 ? 0.4806 0.4852 0.5001 0.0253  0.0863  -0.0031 156 THR A OG1 
1194 C CG2 . THR A 156 ? 0.4427 0.4549 0.4831 0.0431  0.0804  0.0029  156 THR A CG2 
1195 N N   . PRO A 157 ? 0.4346 0.4109 0.4377 0.0072  0.0730  0.0071  157 PRO A N   
1196 C CA  . PRO A 157 ? 0.4356 0.4138 0.4309 -0.0031 0.0709  0.0039  157 PRO A CA  
1197 C C   . PRO A 157 ? 0.4409 0.4234 0.4286 -0.0025 0.0733  -0.0028 157 PRO A C   
1198 O O   . PRO A 157 ? 0.4293 0.4231 0.4132 -0.0052 0.0702  -0.0018 157 PRO A O   
1199 C CB  . PRO A 157 ? 0.4663 0.4219 0.4541 -0.0101 0.0698  0.0013  157 PRO A CB  
1200 C CG  . PRO A 157 ? 0.4839 0.4261 0.4743 -0.0050 0.0697  0.0085  157 PRO A CG  
1201 C CD  . PRO A 157 ? 0.4627 0.4160 0.4622 0.0095  0.0719  0.0091  157 PRO A CD  
1202 N N   . SER A 158 ? 0.4544 0.4273 0.4373 0.0025  0.0788  -0.0097 158 SER A N   
1203 C CA  . SER A 158 ? 0.4564 0.4336 0.4282 0.0022  0.0828  -0.0152 158 SER A CA  
1204 C C   . SER A 158 ? 0.4465 0.4398 0.4227 0.0032  0.0859  -0.0098 158 SER A C   
1205 O O   . SER A 158 ? 0.4695 0.4644 0.4322 -0.0002 0.0880  -0.0105 158 SER A O   
1206 C CB  . SER A 158 ? 0.4774 0.4434 0.4424 0.0085  0.0899  -0.0252 158 SER A CB  
1207 O OG  . SER A 158 ? 0.4786 0.4509 0.4582 0.0193  0.0950  -0.0246 158 SER A OG  
1208 N N   . GLY A 159 ? 0.4250 0.4275 0.4168 0.0065  0.0855  -0.0041 159 GLY A N   
1209 C CA  . GLY A 159 ? 0.4175 0.4320 0.4126 0.0040  0.0867  0.0005  159 GLY A CA  
1210 C C   . GLY A 159 ? 0.4212 0.4335 0.4096 0.0004  0.0791  0.0060  159 GLY A C   
1211 O O   . GLY A 159 ? 0.4271 0.4411 0.4127 -0.0028 0.0789  0.0094  159 GLY A O   
1212 N N   . THR A 160 ? 0.4240 0.4330 0.4095 0.0007  0.0730  0.0063  160 THR A N   
1213 C CA  . THR A 160 ? 0.4291 0.4406 0.4099 0.0015  0.0659  0.0098  160 THR A CA  
1214 C C   . THR A 160 ? 0.4534 0.4571 0.4154 0.0009  0.0638  0.0099  160 THR A C   
1215 O O   . THR A 160 ? 0.4623 0.4620 0.4168 0.0041  0.0584  0.0130  160 THR A O   
1216 C CB  . THR A 160 ? 0.4387 0.4571 0.4239 0.0010  0.0613  0.0092  160 THR A CB  
1217 O OG1 . THR A 160 ? 0.4418 0.4560 0.4214 -0.0035 0.0616  0.0039  160 THR A OG1 
1218 C CG2 . THR A 160 ? 0.4654 0.4867 0.4630 0.0010  0.0627  0.0125  160 THR A CG2 
1219 N N   . THR A 161 ? 0.4562 0.4544 0.4068 -0.0021 0.0675  0.0065  161 THR A N   
1220 C CA  . THR A 161 ? 0.4792 0.4665 0.4062 -0.0028 0.0656  0.0081  161 THR A CA  
1221 C C   . THR A 161 ? 0.4804 0.4589 0.3989 -0.0082 0.0719  0.0129  161 THR A C   
1222 O O   . THR A 161 ? 0.5005 0.4638 0.3945 -0.0105 0.0707  0.0168  161 THR A O   
1223 C CB  . THR A 161 ? 0.5154 0.5003 0.4294 -0.0049 0.0674  0.0021  161 THR A CB  
1224 O OG1 . THR A 161 ? 0.5233 0.5096 0.4424 -0.0077 0.0788  -0.0021 161 THR A OG1 
1225 C CG2 . THR A 161 ? 0.5209 0.5143 0.4431 -0.0041 0.0601  -0.0032 161 THR A CG2 
1226 N N   . ALA A 162 ? 0.4726 0.4606 0.4097 -0.0113 0.0779  0.0132  162 ALA A N   
1227 C CA  . ALA A 162 ? 0.4911 0.4775 0.4250 -0.0205 0.0846  0.0168  162 ALA A CA  
1228 C C   . ALA A 162 ? 0.4845 0.4635 0.4204 -0.0223 0.0778  0.0211  162 ALA A C   
1229 O O   . ALA A 162 ? 0.4931 0.4536 0.4121 -0.0179 0.0689  0.0239  162 ALA A O   
1230 C CB  . ALA A 162 ? 0.4821 0.4903 0.4369 -0.0226 0.0954  0.0123  162 ALA A CB  
1231 N N   . TYR A 163 ? 0.4709 0.4649 0.4268 -0.0271 0.0810  0.0203  163 TYR A N   
1232 C CA  . TYR A 163 ? 0.4765 0.4628 0.4325 -0.0307 0.0742  0.0225  163 TYR A CA  
1233 C C   . TYR A 163 ? 0.4660 0.4471 0.4220 -0.0180 0.0640  0.0215  163 TYR A C   
1234 O O   . TYR A 163 ? 0.5022 0.4649 0.4442 -0.0164 0.0564  0.0226  163 TYR A O   
1235 C CB  . TYR A 163 ? 0.4763 0.4873 0.4572 -0.0374 0.0779  0.0203  163 TYR A CB  
1236 C CG  . TYR A 163 ? 0.5103 0.5131 0.4881 -0.0488 0.0725  0.0216  163 TYR A CG  
1237 C CD1 . TYR A 163 ? 0.5343 0.5020 0.4844 -0.0516 0.0655  0.0246  163 TYR A CD1 
1238 C CD2 . TYR A 163 ? 0.5247 0.5539 0.5260 -0.0560 0.0732  0.0188  163 TYR A CD2 
1239 C CE1 . TYR A 163 ? 0.5629 0.5162 0.5062 -0.0631 0.0596  0.0244  163 TYR A CE1 
1240 C CE2 . TYR A 163 ? 0.5448 0.5663 0.5426 -0.0692 0.0669  0.0184  163 TYR A CE2 
1241 C CZ  . TYR A 163 ? 0.5608 0.5414 0.5281 -0.0736 0.0604  0.0210  163 TYR A CZ  
1242 O OH  . TYR A 163 ? 0.5736 0.5397 0.5335 -0.0878 0.0533  0.0194  163 TYR A OH  
1243 N N   . ASN A 164 ? 0.4255 0.4215 0.3953 -0.0093 0.0642  0.0191  164 ASN A N   
1244 C CA  . ASN A 164 ? 0.4248 0.4224 0.3959 0.0004  0.0571  0.0186  164 ASN A CA  
1245 C C   . ASN A 164 ? 0.4650 0.4482 0.4166 0.0067  0.0509  0.0189  164 ASN A C   
1246 O O   . ASN A 164 ? 0.4672 0.4479 0.4145 0.0148  0.0445  0.0178  164 ASN A O   
1247 C CB  . ASN A 164 ? 0.4087 0.4207 0.3937 0.0041  0.0597  0.0174  164 ASN A CB  
1248 C CG  . ASN A 164 ? 0.4210 0.4392 0.4067 0.0106  0.0549  0.0175  164 ASN A CG  
1249 O OD1 . ASN A 164 ? 0.4470 0.4719 0.4386 0.0134  0.0531  0.0187  164 ASN A OD1 
1250 N ND2 . ASN A 164 ? 0.4142 0.4338 0.3936 0.0126  0.0528  0.0159  164 ASN A ND2 
1251 N N   . LYS A 165 ? 0.4892 0.4638 0.4273 0.0051  0.0521  0.0197  165 LYS A N   
1252 C CA  . LYS A 165 ? 0.4983 0.4606 0.4171 0.0141  0.0440  0.0201  165 LYS A CA  
1253 C C   . LYS A 165 ? 0.5121 0.4460 0.4096 0.0160  0.0384  0.0228  165 LYS A C   
1254 O O   . LYS A 165 ? 0.5143 0.4401 0.4013 0.0296  0.0295  0.0213  165 LYS A O   
1255 C CB  . LYS A 165 ? 0.5059 0.4639 0.4112 0.0117  0.0455  0.0206  165 LYS A CB  
1256 C CG  . LYS A 165 ? 0.5218 0.4676 0.4049 0.0230  0.0349  0.0217  165 LYS A CG  
1257 C CD  . LYS A 165 ? 0.5267 0.4719 0.3959 0.0206  0.0350  0.0214  165 LYS A CD  
1258 C CE  . LYS A 165 ? 0.5633 0.4960 0.4079 0.0340  0.0221  0.0233  165 LYS A CE  
1259 N NZ  . LYS A 165 ? 0.6108 0.5049 0.4260 0.0361  0.0188  0.0308  165 LYS A NZ  
1260 N N   . SER A 166 ? 0.5166 0.4350 0.4070 0.0023  0.0433  0.0262  166 SER A N   
1261 C CA  . SER A 166 ? 0.5508 0.4346 0.4171 -0.0005 0.0377  0.0291  166 SER A CA  
1262 C C   . SER A 166 ? 0.5547 0.4373 0.4269 0.0066  0.0313  0.0242  166 SER A C   
1263 O O   . SER A 166 ? 0.5820 0.4315 0.4302 0.0116  0.0232  0.0240  166 SER A O   
1264 C CB  . SER A 166 ? 0.5716 0.4455 0.4328 -0.0222 0.0460  0.0336  166 SER A CB  
1265 O OG  . SER A 166 ? 0.5955 0.4704 0.4469 -0.0283 0.0534  0.0376  166 SER A OG  
1266 N N   . LEU A 167 ? 0.5343 0.4482 0.4336 0.0079  0.0342  0.0204  167 LEU A N   
1267 C CA  . LEU A 167 ? 0.5406 0.4568 0.4438 0.0145  0.0290  0.0156  167 LEU A CA  
1268 C C   . LEU A 167 ? 0.5389 0.4678 0.4430 0.0339  0.0247  0.0116  167 LEU A C   
1269 O O   . LEU A 167 ? 0.5630 0.5002 0.4706 0.0409  0.0223  0.0071  167 LEU A O   
1270 C CB  . LEU A 167 ? 0.5043 0.4473 0.4327 0.0059  0.0337  0.0147  167 LEU A CB  
1271 C CG  . LEU A 167 ? 0.4833 0.4255 0.4175 -0.0127 0.0378  0.0166  167 LEU A CG  
1272 C CD1 . LEU A 167 ? 0.4549 0.4298 0.4168 -0.0154 0.0412  0.0155  167 LEU A CD1 
1273 C CD2 . LEU A 167 ? 0.5008 0.4136 0.4157 -0.0213 0.0309  0.0147  167 LEU A CD2 
1274 N N   . GLY A 168 ? 0.5240 0.4581 0.4250 0.0423  0.0237  0.0126  168 GLY A N   
1275 C CA  . GLY A 168 ? 0.5034 0.4591 0.4100 0.0592  0.0204  0.0083  168 GLY A CA  
1276 C C   . GLY A 168 ? 0.4668 0.4609 0.3996 0.0551  0.0270  0.0084  168 GLY A C   
1277 O O   . GLY A 168 ? 0.4687 0.4879 0.4098 0.0652  0.0259  0.0050  168 GLY A O   
1278 N N   . GLY A 169 ? 0.4454 0.4445 0.3906 0.0406  0.0338  0.0119  169 GLY A N   
1279 C CA  . GLY A 169 ? 0.4240 0.4489 0.3886 0.0357  0.0392  0.0127  169 GLY A CA  
1280 C C   . GLY A 169 ? 0.4283 0.4671 0.3965 0.0364  0.0383  0.0114  169 GLY A C   
1281 O O   . GLY A 169 ? 0.4282 0.4574 0.3838 0.0409  0.0334  0.0105  169 GLY A O   
1282 N N   . ALA A 170 ? 0.4279 0.4884 0.4115 0.0307  0.0422  0.0116  170 ALA A N   
1283 C CA  . ALA A 170 ? 0.4321 0.5096 0.4217 0.0273  0.0407  0.0091  170 ALA A CA  
1284 C C   . ALA A 170 ? 0.4434 0.5072 0.4315 0.0163  0.0437  0.0093  170 ALA A C   
1285 O O   . ALA A 170 ? 0.4648 0.5156 0.4551 0.0106  0.0492  0.0116  170 ALA A O   
1286 C CB  . ALA A 170 ? 0.4096 0.5161 0.4148 0.0225  0.0440  0.0091  170 ALA A CB  
1287 N N   . LEU A 171 ? 0.4375 0.5058 0.4209 0.0153  0.0392  0.0056  171 LEU A N   
1288 C CA  . LEU A 171 ? 0.4345 0.4912 0.4138 0.0056  0.0418  0.0033  171 LEU A CA  
1289 C C   . LEU A 171 ? 0.4496 0.5173 0.4421 -0.0063 0.0441  0.0015  171 LEU A C   
1290 O O   . LEU A 171 ? 0.4778 0.5705 0.4798 -0.0096 0.0402  -0.0006 171 LEU A O   
1291 C CB  . LEU A 171 ? 0.4404 0.4948 0.4042 0.0088  0.0348  -0.0002 171 LEU A CB  
1292 C CG  . LEU A 171 ? 0.4629 0.4998 0.4071 0.0193  0.0314  0.0034  171 LEU A CG  
1293 C CD1 . LEU A 171 ? 0.4870 0.5173 0.4104 0.0217  0.0245  0.0015  171 LEU A CD1 
1294 C CD2 . LEU A 171 ? 0.4752 0.4905 0.4147 0.0154  0.0400  0.0077  171 LEU A CD2 
1295 N N   . MET A 172 ? 0.4462 0.4954 0.4389 -0.0128 0.0503  0.0022  172 MET A N   
1296 C CA  . MET A 172 ? 0.4677 0.5151 0.4679 -0.0242 0.0530  0.0029  172 MET A CA  
1297 C C   . MET A 172 ? 0.5123 0.5381 0.5034 -0.0313 0.0537  -0.0034 172 MET A C   
1298 O O   . MET A 172 ? 0.5410 0.5496 0.5236 -0.0250 0.0572  -0.0057 172 MET A O   
1299 C CB  . MET A 172 ? 0.4712 0.5098 0.4758 -0.0214 0.0581  0.0102  172 MET A CB  
1300 C CG  . MET A 172 ? 0.4847 0.5191 0.4926 -0.0327 0.0606  0.0146  172 MET A CG  
1301 S SD  . MET A 172 ? 0.4785 0.5087 0.4875 -0.0253 0.0639  0.0245  172 MET A SD  
1302 C CE  . MET A 172 ? 0.4703 0.4828 0.4770 -0.0123 0.0643  0.0221  172 MET A CE  
1303 N N   . HIS A 173 ? 0.5341 0.5620 0.5266 -0.0453 0.0509  -0.0072 173 HIS A N   
1304 C CA  . HIS A 173 ? 0.5711 0.5751 0.5512 -0.0526 0.0500  -0.0156 173 HIS A CA  
1305 C C   . HIS A 173 ? 0.6245 0.5948 0.5990 -0.0494 0.0563  -0.0140 173 HIS A C   
1306 O O   . HIS A 173 ? 0.6348 0.5999 0.6153 -0.0504 0.0590  -0.0056 173 HIS A O   
1307 C CB  . HIS A 173 ? 0.5790 0.5925 0.5621 -0.0718 0.0443  -0.0205 173 HIS A CB  
1308 C CG  . HIS A 173 ? 0.6171 0.6057 0.5840 -0.0800 0.0409  -0.0320 173 HIS A CG  
1309 N ND1 . HIS A 173 ? 0.6477 0.5986 0.6046 -0.0894 0.0433  -0.0346 173 HIS A ND1 
1310 C CD2 . HIS A 173 ? 0.6279 0.6206 0.5830 -0.0794 0.0345  -0.0421 173 HIS A CD2 
1311 C CE1 . HIS A 173 ? 0.6778 0.6105 0.6181 -0.0942 0.0389  -0.0474 173 HIS A CE1 
1312 N NE2 . HIS A 173 ? 0.6619 0.6214 0.6007 -0.0888 0.0337  -0.0521 173 HIS A NE2 
1313 N N   . PRO A 174 ? 0.6856 0.6332 0.6469 -0.0435 0.0586  -0.0221 174 PRO A N   
1314 C CA  . PRO A 174 ? 0.7002 0.6196 0.6577 -0.0343 0.0641  -0.0217 174 PRO A CA  
1315 C C   . PRO A 174 ? 0.7295 0.6174 0.6802 -0.0444 0.0623  -0.0209 174 PRO A C   
1316 O O   . PRO A 174 ? 0.7495 0.6138 0.6976 -0.0344 0.0650  -0.0173 174 PRO A O   
1317 C CB  . PRO A 174 ? 0.7133 0.6226 0.6577 -0.0253 0.0677  -0.0331 174 PRO A CB  
1318 C CG  . PRO A 174 ? 0.6982 0.6328 0.6400 -0.0273 0.0652  -0.0345 174 PRO A CG  
1319 C CD  . PRO A 174 ? 0.6917 0.6426 0.6403 -0.0407 0.0569  -0.0314 174 PRO A CD  
1320 N N   . SER A 175 ? 0.7170 0.6030 0.6640 -0.0642 0.0572  -0.0238 175 SER A N   
1321 C CA  . SER A 175 ? 0.7458 0.5963 0.6829 -0.0782 0.0558  -0.0216 175 SER A CA  
1322 C C   . SER A 175 ? 0.7199 0.5746 0.6651 -0.0815 0.0582  -0.0057 175 SER A C   
1323 O O   . SER A 175 ? 0.7562 0.5751 0.6891 -0.0914 0.0579  -0.0003 175 SER A O   
1324 C CB  . SER A 175 ? 0.7795 0.6312 0.7119 -0.1034 0.0495  -0.0293 175 SER A CB  
1325 O OG  . SER A 175 ? 0.7575 0.6574 0.7091 -0.1148 0.0475  -0.0239 175 SER A OG  
1326 N N   . ILE A 176 ? 0.6557 0.5490 0.6173 -0.0734 0.0604  0.0017  176 ILE A N   
1327 C CA  . ILE A 176 ? 0.6237 0.5245 0.5905 -0.0746 0.0630  0.0157  176 ILE A CA  
1328 C C   . ILE A 176 ? 0.6063 0.4898 0.5700 -0.0529 0.0647  0.0207  176 ILE A C   
1329 O O   . ILE A 176 ? 0.5623 0.4644 0.5348 -0.0368 0.0656  0.0173  176 ILE A O   
1330 C CB  . ILE A 176 ? 0.5774 0.5282 0.5612 -0.0757 0.0637  0.0189  176 ILE A CB  
1331 C CG1 . ILE A 176 ? 0.5593 0.5358 0.5501 -0.0940 0.0605  0.0123  176 ILE A CG1 
1332 C CG2 . ILE A 176 ? 0.5815 0.5403 0.5670 -0.0768 0.0673  0.0321  176 ILE A CG2 
1333 C CD1 . ILE A 176 ? 0.5140 0.5411 0.5215 -0.0898 0.0600  0.0130  176 ILE A CD1 
1334 N N   . GLU A 177 ? 0.6405 0.4884 0.5910 -0.0531 0.0644  0.0289  177 GLU A N   
1335 C CA  . GLU A 177 ? 0.6401 0.4744 0.5883 -0.0311 0.0637  0.0341  177 GLU A CA  
1336 C C   . GLU A 177 ? 0.6191 0.4856 0.5772 -0.0277 0.0644  0.0446  177 GLU A C   
1337 O O   . GLU A 177 ? 0.6456 0.5045 0.5945 -0.0358 0.0647  0.0567  177 GLU A O   
1338 C CB  . GLU A 177 ? 0.6842 0.4642 0.6100 -0.0300 0.0610  0.0398  177 GLU A CB  
1339 C CG  . GLU A 177 ? 0.7313 0.4715 0.6415 -0.0381 0.0595  0.0289  177 GLU A CG  
1340 C CD  . GLU A 177 ? 0.8187 0.4960 0.7028 -0.0312 0.0556  0.0336  177 GLU A CD  
1341 O OE1 . GLU A 177 ? 0.8489 0.5088 0.7299 -0.0046 0.0537  0.0272  177 GLU A OE1 
1342 O OE2 . GLU A 177 ? 0.8723 0.5178 0.7381 -0.0519 0.0544  0.0439  177 GLU A OE2 
1343 N N   . ALA A 178 ? 0.5784 0.4788 0.5520 -0.0166 0.0650  0.0399  178 ALA A N   
1344 C CA  . ALA A 178 ? 0.5405 0.4705 0.5217 -0.0136 0.0648  0.0466  178 ALA A CA  
1345 C C   . ALA A 178 ? 0.5285 0.4780 0.5219 0.0019  0.0637  0.0410  178 ALA A C   
1346 O O   . ALA A 178 ? 0.5296 0.4744 0.5269 0.0094  0.0647  0.0330  178 ALA A O   
1347 C CB  . ALA A 178 ? 0.5015 0.4595 0.4879 -0.0281 0.0671  0.0463  178 ALA A CB  
1348 N N   . MET A 179 ? 0.5138 0.4858 0.5120 0.0053  0.0623  0.0449  179 MET A N   
1349 C CA  . MET A 179 ? 0.4913 0.4822 0.4999 0.0147  0.0607  0.0402  179 MET A CA  
1350 C C   . MET A 179 ? 0.4749 0.4869 0.4838 0.0116  0.0598  0.0410  179 MET A C   
1351 O O   . MET A 179 ? 0.4857 0.5016 0.4879 0.0077  0.0600  0.0470  179 MET A O   
1352 C CB  . MET A 179 ? 0.4958 0.4847 0.5079 0.0277  0.0566  0.0430  179 MET A CB  
1353 C CG  . MET A 179 ? 0.5002 0.4850 0.5022 0.0299  0.0522  0.0534  179 MET A CG  
1354 S SD  . MET A 179 ? 0.5048 0.4950 0.5123 0.0475  0.0437  0.0556  179 MET A SD  
1355 C CE  . MET A 179 ? 0.5233 0.5049 0.5097 0.0469  0.0389  0.0691  179 MET A CE  
1356 N N   . GLN A 180 ? 0.4602 0.4839 0.4744 0.0135  0.0592  0.0349  180 GLN A N   
1357 C CA  . GLN A 180 ? 0.4673 0.5044 0.4784 0.0133  0.0574  0.0334  180 GLN A CA  
1358 C C   . GLN A 180 ? 0.4575 0.4988 0.4701 0.0182  0.0534  0.0315  180 GLN A C   
1359 O O   . GLN A 180 ? 0.4655 0.5057 0.4845 0.0182  0.0537  0.0284  180 GLN A O   
1360 C CB  . GLN A 180 ? 0.4905 0.5307 0.5004 0.0101  0.0585  0.0281  180 GLN A CB  
1361 C CG  . GLN A 180 ? 0.5247 0.5761 0.5295 0.0140  0.0557  0.0259  180 GLN A CG  
1362 C CD  . GLN A 180 ? 0.5692 0.6245 0.5717 0.0139  0.0546  0.0214  180 GLN A CD  
1363 O OE1 . GLN A 180 ? 0.5729 0.6361 0.5707 0.0207  0.0513  0.0186  180 GLN A OE1 
1364 N NE2 . GLN A 180 ? 0.6179 0.6671 0.6220 0.0081  0.0563  0.0199  180 GLN A NE2 
1365 N N   . LEU A 181 ? 0.4500 0.4975 0.4559 0.0211  0.0499  0.0324  181 LEU A N   
1366 C CA  . LEU A 181 ? 0.4387 0.4882 0.4430 0.0235  0.0443  0.0293  181 LEU A CA  
1367 C C   . LEU A 181 ? 0.4306 0.4769 0.4246 0.0247  0.0423  0.0238  181 LEU A C   
1368 O O   . LEU A 181 ? 0.4283 0.4799 0.4154 0.0287  0.0437  0.0233  181 LEU A O   
1369 C CB  . LEU A 181 ? 0.4423 0.4967 0.4416 0.0278  0.0398  0.0333  181 LEU A CB  
1370 C CG  . LEU A 181 ? 0.4408 0.4985 0.4364 0.0291  0.0318  0.0287  181 LEU A CG  
1371 C CD1 . LEU A 181 ? 0.4262 0.4900 0.4373 0.0265  0.0285  0.0271  181 LEU A CD1 
1372 C CD2 . LEU A 181 ? 0.4485 0.5108 0.4310 0.0344  0.0275  0.0320  181 LEU A CD2 
1373 N N   . THR A 182 ? 0.4263 0.4638 0.4184 0.0215  0.0392  0.0197  182 THR A N   
1374 C CA  . THR A 182 ? 0.4374 0.4615 0.4145 0.0238  0.0357  0.0147  182 THR A CA  
1375 C C   . THR A 182 ? 0.4548 0.4695 0.4246 0.0201  0.0287  0.0105  182 THR A C   
1376 O O   . THR A 182 ? 0.4532 0.4771 0.4340 0.0139  0.0268  0.0113  182 THR A O   
1377 C CB  . THR A 182 ? 0.4430 0.4550 0.4169 0.0202  0.0381  0.0145  182 THR A CB  
1378 O OG1 . THR A 182 ? 0.4599 0.4731 0.4440 0.0103  0.0416  0.0162  182 THR A OG1 
1379 C CG2 . THR A 182 ? 0.4227 0.4438 0.3999 0.0245  0.0420  0.0161  182 THR A CG2 
1380 N N   . GLU A 183 ? 0.4800 0.4763 0.4309 0.0248  0.0238  0.0050  183 GLU A N   
1381 C CA  . GLU A 183 ? 0.5019 0.4825 0.4402 0.0205  0.0157  -0.0009 183 GLU A CA  
1382 C C   . GLU A 183 ? 0.5288 0.4813 0.4562 0.0097  0.0136  -0.0020 183 GLU A C   
1383 O O   . GLU A 183 ? 0.5367 0.4760 0.4571 0.0121  0.0167  0.0007  183 GLU A O   
1384 C CB  . GLU A 183 ? 0.5183 0.4913 0.4368 0.0344  0.0110  -0.0079 183 GLU A CB  
1385 C CG  . GLU A 183 ? 0.5227 0.5226 0.4465 0.0428  0.0144  -0.0059 183 GLU A CG  
1386 C CD  . GLU A 183 ? 0.5590 0.5553 0.4617 0.0567  0.0115  -0.0142 183 GLU A CD  
1387 O OE1 . GLU A 183 ? 0.5985 0.5696 0.4831 0.0637  0.0068  -0.0222 183 GLU A OE1 
1388 O OE2 . GLU A 183 ? 0.5501 0.5668 0.4515 0.0616  0.0142  -0.0128 183 GLU A OE2 
1389 N N   . MET A 184 ? 0.5380 0.4810 0.4622 -0.0036 0.0077  -0.0057 184 MET A N   
1390 C CA  . MET A 184 ? 0.5567 0.4695 0.4672 -0.0193 0.0057  -0.0060 184 MET A CA  
1391 C C   . MET A 184 ? 0.5932 0.4716 0.4765 -0.0197 -0.0054 -0.0148 184 MET A C   
1392 O O   . MET A 184 ? 0.6177 0.5021 0.5043 -0.0307 -0.0120 -0.0202 184 MET A O   
1393 C CB  . MET A 184 ? 0.5472 0.4816 0.4801 -0.0403 0.0094  -0.0030 184 MET A CB  
1394 C CG  . MET A 184 ? 0.5310 0.4954 0.4879 -0.0387 0.0204  0.0036  184 MET A CG  
1395 S SD  . MET A 184 ? 0.5468 0.5412 0.5301 -0.0609 0.0257  0.0046  184 MET A SD  
1396 C CE  . MET A 184 ? 0.5281 0.5519 0.5334 -0.0499 0.0379  0.0095  184 MET A CE  
1397 N N   . ALA A 185 ? 0.6082 0.4504 0.4636 -0.0064 -0.0086 -0.0174 185 ALA A N   
1398 C CA  . ALA A 185 ? 0.6550 0.4532 0.4777 -0.0037 -0.0195 -0.0271 185 ALA A CA  
1399 C C   . ALA A 185 ? 0.6606 0.4748 0.4839 0.0015  -0.0257 -0.0369 185 ALA A C   
1400 O O   . ALA A 185 ? 0.6937 0.4945 0.5091 -0.0141 -0.0341 -0.0435 185 ALA A O   
1401 C CB  . ALA A 185 ? 0.6879 0.4477 0.4950 -0.0300 -0.0236 -0.0257 185 ALA A CB  
1402 N N   . SER A 186 ? 0.6143 0.4586 0.4460 0.0222  -0.0215 -0.0376 186 SER A N   
1403 C CA  A SER A 186 ? 0.6102 0.4722 0.4393 0.0284  -0.0259 -0.0452 186 SER A CA  
1404 C CA  B SER A 186 ? 0.6197 0.4816 0.4488 0.0284  -0.0259 -0.0452 186 SER A CA  
1405 C C   . SER A 186 ? 0.6684 0.4912 0.4608 0.0401  -0.0353 -0.0595 186 SER A C   
1406 O O   . SER A 186 ? 0.7129 0.5009 0.4835 0.0531  -0.0368 -0.0631 186 SER A O   
1407 C CB  A SER A 186 ? 0.5652 0.4690 0.4105 0.0442  -0.0169 -0.0401 186 SER A CB  
1408 C CB  B SER A 186 ? 0.5642 0.4677 0.4092 0.0444  -0.0169 -0.0403 186 SER A CB  
1409 O OG  A SER A 186 ? 0.5741 0.4733 0.4077 0.0654  -0.0129 -0.0432 186 SER A OG  
1410 O OG  B SER A 186 ? 0.5747 0.4925 0.4112 0.0505  -0.0206 -0.0464 186 SER A OG  
1411 N N   . ILE A 187 ? 0.7049 0.5319 0.4881 0.0374  -0.0429 -0.0685 187 ILE A N   
1412 C CA  . ILE A 187 ? 0.7721 0.5627 0.5179 0.0489  -0.0524 -0.0848 187 ILE A CA  
1413 C C   . ILE A 187 ? 0.7862 0.6052 0.5263 0.0753  -0.0463 -0.0894 187 ILE A C   
1414 O O   . ILE A 187 ? 0.7495 0.6125 0.5080 0.0744  -0.0410 -0.0829 187 ILE A O   
1415 C CB  . ILE A 187 ? 0.7937 0.5718 0.5296 0.0281  -0.0656 -0.0938 187 ILE A CB  
1416 C CG1 . ILE A 187 ? 0.7988 0.5588 0.5457 -0.0025 -0.0692 -0.0880 187 ILE A CG1 
1417 C CG2 . ILE A 187 ? 0.8463 0.5798 0.5383 0.0403  -0.0764 -0.1129 187 ILE A CG2 
1418 C CD1 . ILE A 187 ? 0.8079 0.5773 0.5605 -0.0279 -0.0808 -0.0940 187 ILE A CD1 
1419 N N   . ASN A 188 ? 0.8536 0.6477 0.5670 0.0993  -0.0467 -0.1003 188 ASN A N   
1420 C CA  . ASN A 188 ? 0.8796 0.7045 0.5868 0.1249  -0.0389 -0.1064 188 ASN A CA  
1421 C C   . ASN A 188 ? 0.9766 0.7608 0.6418 0.1456  -0.0470 -0.1269 188 ASN A C   
1422 O O   . ASN A 188 ? 1.0063 0.7529 0.6547 0.1607  -0.0502 -0.1328 188 ASN A O   
1423 C CB  . ASN A 188 ? 0.8332 0.6906 0.5630 0.1394  -0.0260 -0.0970 188 ASN A CB  
1424 C CG  . ASN A 188 ? 0.7655 0.6728 0.5308 0.1256  -0.0157 -0.0803 188 ASN A CG  
1425 O OD1 . ASN A 188 ? 0.7596 0.7050 0.5295 0.1314  -0.0077 -0.0784 188 ASN A OD1 
1426 N ND2 . ASN A 188 ? 0.7205 0.6254 0.5080 0.1073  -0.0154 -0.0682 188 ASN A ND2 
1427 N N   . ASN A 189 ? 1.0405 0.8299 0.6858 0.1480  -0.0510 -0.1382 189 ASN A N   
1428 C CA  . ASN A 189 ? 1.1402 0.8948 0.7427 0.1706  -0.0575 -0.1603 189 ASN A CA  
1429 C C   . ASN A 189 ? 1.1830 0.9801 0.7759 0.1848  -0.0500 -0.1671 189 ASN A C   
1430 O O   . ASN A 189 ? 1.1366 0.9897 0.7551 0.1879  -0.0355 -0.1545 189 ASN A O   
1431 C CB  . ASN A 189 ? 1.1897 0.8819 0.7622 0.1529  -0.0759 -0.1723 189 ASN A CB  
1432 C CG  . ASN A 189 ? 1.1640 0.8750 0.7520 0.1206  -0.0827 -0.1657 189 ASN A CG  
1433 O OD1 . ASN A 189 ? 1.1365 0.8976 0.7384 0.1200  -0.0772 -0.1600 189 ASN A OD1 
1434 N ND2 . ASN A 189 ? 1.1794 0.8512 0.7646 0.0934  -0.0951 -0.1661 189 ASN A ND2 
1435 N N   . ARG A 190 ? 1.2938 1.0625 0.8469 0.1919  -0.0598 -0.1868 190 ARG A N   
1436 C CA  . ARG A 190 ? 1.3110 1.1178 0.8482 0.2055  -0.0525 -0.1939 190 ARG A CA  
1437 C C   . ARG A 190 ? 1.2877 1.1300 0.8406 0.1809  -0.0538 -0.1799 190 ARG A C   
1438 O O   . ARG A 190 ? 1.2783 1.1676 0.8331 0.1874  -0.0420 -0.1735 190 ARG A O   
1439 C CB  . ARG A 190 ? 1.3812 1.1456 0.8700 0.2212  -0.0629 -0.2197 190 ARG A CB  
1440 C CG  . ARG A 190 ? 1.3835 1.1919 0.8644 0.2361  -0.0513 -0.2232 190 ARG A CG  
1441 C CD  . ARG A 190 ? 1.4363 1.2111 0.8809 0.2335  -0.0647 -0.2407 190 ARG A CD  
1442 N NE  . ARG A 190 ? 1.4916 1.2034 0.9162 0.2417  -0.0761 -0.2557 190 ARG A NE  
1443 C CZ  . ARG A 190 ? 1.5410 1.1946 0.9507 0.2206  -0.0948 -0.2620 190 ARG A CZ  
1444 N NH1 . ARG A 190 ? 1.6108 1.2052 0.9999 0.2284  -0.1038 -0.2733 190 ARG A NH1 
1445 N NH2 . ARG A 190 ? 1.5257 1.1816 0.9415 0.1908  -0.1051 -0.2561 190 ARG A NH2 
1446 N N   . VAL A 191 ? 1.2709 1.0929 0.8348 0.1529  -0.0679 -0.1745 191 VAL A N   
1447 C CA  . VAL A 191 ? 1.2458 1.0970 0.8192 0.1335  -0.0739 -0.1653 191 VAL A CA  
1448 C C   . VAL A 191 ? 1.1557 1.0403 0.7769 0.1165  -0.0671 -0.1407 191 VAL A C   
1449 O O   . VAL A 191 ? 1.1181 1.0402 0.7518 0.1106  -0.0647 -0.1278 191 VAL A O   
1450 C CB  . VAL A 191 ? 1.2988 1.1130 0.8505 0.1148  -0.0962 -0.1799 191 VAL A CB  
1451 C CG1 . VAL A 191 ? 1.3635 1.1151 0.8781 0.1248  -0.1044 -0.2024 191 VAL A CG1 
1452 C CG2 . VAL A 191 ? 1.2620 1.0810 0.8503 0.0842  -0.1045 -0.1666 191 VAL A CG2 
1453 N N   . TYR A 192 ? 1.1198 0.9883 0.7641 0.1101  -0.0642 -0.1342 192 TYR A N   
1454 C CA  . TYR A 192 ? 1.0411 0.9371 0.7282 0.0959  -0.0571 -0.1132 192 TYR A CA  
1455 C C   . TYR A 192 ? 0.9668 0.8805 0.6694 0.1114  -0.0401 -0.1047 192 TYR A C   
1456 O O   . TYR A 192 ? 0.9791 0.8671 0.6715 0.1243  -0.0385 -0.1127 192 TYR A O   
1457 C CB  . TYR A 192 ? 1.0565 0.9256 0.7590 0.0728  -0.0667 -0.1115 192 TYR A CB  
1458 C CG  . TYR A 192 ? 1.0728 0.9543 0.7856 0.0504  -0.0799 -0.1105 192 TYR A CG  
1459 C CD1 . TYR A 192 ? 1.0420 0.9664 0.7873 0.0428  -0.0765 -0.0944 192 TYR A CD1 
1460 C CD2 . TYR A 192 ? 1.1266 0.9770 0.8164 0.0373  -0.0968 -0.1263 192 TYR A CD2 
1461 C CE1 . TYR A 192 ? 1.0462 0.9879 0.8036 0.0259  -0.0897 -0.0942 192 TYR A CE1 
1462 C CE2 . TYR A 192 ? 1.1335 1.0032 0.8366 0.0164  -0.1101 -0.1264 192 TYR A CE2 
1463 C CZ  . TYR A 192 ? 1.0892 1.0074 0.8274 0.0123  -0.1065 -0.1103 192 TYR A CZ  
1464 O OH  . TYR A 192 ? 1.0901 1.0332 0.8441 -0.0050 -0.1209 -0.1110 192 TYR A OH  
1465 N N   . ARG A 193 ? 0.8919 0.8478 0.6176 0.1101  -0.0287 -0.0886 193 ARG A N   
1466 C CA  . ARG A 193 ? 0.8500 0.8299 0.5926 0.1211  -0.0128 -0.0804 193 ARG A CA  
1467 C C   . ARG A 193 ? 0.7868 0.7910 0.5641 0.1058  -0.0067 -0.0607 193 ARG A C   
1468 O O   . ARG A 193 ? 0.7963 0.8194 0.5775 0.0979  -0.0071 -0.0513 193 ARG A O   
1469 C CB  . ARG A 193 ? 0.8749 0.8837 0.6001 0.1388  -0.0016 -0.0845 193 ARG A CB  
1470 C CG  . ARG A 193 ? 0.9318 0.9307 0.6380 0.1632  0.0018  -0.1015 193 ARG A CG  
1471 C CD  . ARG A 193 ? 0.9755 1.0028 0.6579 0.1798  0.0114  -0.1096 193 ARG A CD  
1472 N NE  . ARG A 193 ? 0.9524 1.0308 0.6549 0.1767  0.0290  -0.0943 193 ARG A NE  
1473 C CZ  . ARG A 193 ? 0.9488 1.0624 0.6578 0.1924  0.0440  -0.0975 193 ARG A CZ  
1474 N NH1 . ARG A 193 ? 0.9290 1.0878 0.6562 0.1834  0.0596  -0.0825 193 ARG A NH1 
1475 N NH2 . ARG A 193 ? 0.9755 1.0792 0.6722 0.2172  0.0429  -0.1162 193 ARG A NH2 
1476 N N   . THR A 194 ? 0.7262 0.7270 0.5252 0.1032  -0.0021 -0.0550 194 THR A N   
1477 C CA  . THR A 194 ? 0.6616 0.6829 0.4912 0.0915  0.0049  -0.0386 194 THR A CA  
1478 C C   . THR A 194 ? 0.6350 0.6784 0.4761 0.1006  0.0178  -0.0347 194 THR A C   
1479 O O   . THR A 194 ? 0.6608 0.7063 0.4898 0.1172  0.0208  -0.0448 194 THR A O   
1480 C CB  . THR A 194 ? 0.6469 0.6479 0.4930 0.0769  -0.0014 -0.0354 194 THR A CB  
1481 O OG1 . THR A 194 ? 0.6656 0.6411 0.5050 0.0829  -0.0026 -0.0422 194 THR A OG1 
1482 C CG2 . THR A 194 ? 0.6592 0.6468 0.4987 0.0652  -0.0143 -0.0400 194 THR A CG2 
1483 N N   . ILE A 195 ? 0.5942 0.6553 0.4592 0.0902  0.0248  -0.0211 195 ILE A N   
1484 C CA  . ILE A 195 ? 0.5763 0.6633 0.4544 0.0946  0.0364  -0.0172 195 ILE A CA  
1485 C C   . ILE A 195 ? 0.5849 0.6602 0.4706 0.1009  0.0341  -0.0225 195 ILE A C   
1486 O O   . ILE A 195 ? 0.5853 0.6810 0.4749 0.1127  0.0398  -0.0266 195 ILE A O   
1487 C CB  . ILE A 195 ? 0.5453 0.6492 0.4417 0.0799  0.0435  -0.0017 195 ILE A CB  
1488 C CG1 . ILE A 195 ? 0.5372 0.6717 0.4463 0.0802  0.0554  0.0016  195 ILE A CG1 
1489 C CG2 . ILE A 195 ? 0.5199 0.6053 0.4328 0.0684  0.0382  0.0041  195 ILE A CG2 
1490 C CD1 . ILE A 195 ? 0.5518 0.7148 0.4479 0.0897  0.0640  -0.0029 195 ILE A CD1 
1491 N N   A GLY A 196 ? 0.5988 0.6434 0.4856 0.0936  0.0258  -0.0226 196 GLY A N   
1492 N N   B GLY A 196 ? 0.5981 0.6432 0.4855 0.0934  0.0260  -0.0223 196 GLY A N   
1493 C CA  A GLY A 196 ? 0.6020 0.6289 0.4897 0.0988  0.0227  -0.0255 196 GLY A CA  
1494 C CA  B GLY A 196 ? 0.6031 0.6299 0.4901 0.0994  0.0226  -0.0259 196 GLY A CA  
1495 C C   A GLY A 196 ? 0.5728 0.6165 0.4833 0.0912  0.0285  -0.0164 196 GLY A C   
1496 C C   B GLY A 196 ? 0.5754 0.6194 0.4844 0.0938  0.0283  -0.0176 196 GLY A C   
1497 O O   A GLY A 196 ? 0.5742 0.5983 0.4878 0.0845  0.0252  -0.0135 196 GLY A O   
1498 O O   B GLY A 196 ? 0.5861 0.6102 0.4957 0.0914  0.0245  -0.0164 196 GLY A O   
1499 N N   . SER A 197 ? 0.5544 0.6335 0.4785 0.0902  0.0375  -0.0118 197 SER A N   
1500 C CA  . SER A 197 ? 0.5146 0.6103 0.4585 0.0824  0.0422  -0.0052 197 SER A CA  
1501 C C   . SER A 197 ? 0.4701 0.5560 0.4246 0.0647  0.0434  0.0044  197 SER A C   
1502 O O   . SER A 197 ? 0.4552 0.5356 0.4063 0.0591  0.0428  0.0080  197 SER A O   
1503 C CB  . SER A 197 ? 0.4934 0.6304 0.4480 0.0836  0.0516  -0.0039 197 SER A CB  
1504 O OG  . SER A 197 ? 0.5027 0.6570 0.4518 0.1031  0.0513  -0.0143 197 SER A OG  
1505 N N   . PRO A 198 ? 0.4284 0.5121 0.3942 0.0579  0.0442  0.0077  198 PRO A N   
1506 C CA  . PRO A 198 ? 0.4041 0.4820 0.3803 0.0440  0.0468  0.0153  198 PRO A CA  
1507 C C   . PRO A 198 ? 0.3840 0.4797 0.3667 0.0370  0.0535  0.0220  198 PRO A C   
1508 O O   . PRO A 198 ? 0.3797 0.4989 0.3652 0.0377  0.0582  0.0215  198 PRO A O   
1509 C CB  . PRO A 198 ? 0.4050 0.4775 0.3871 0.0407  0.0463  0.0147  198 PRO A CB  
1510 C CG  . PRO A 198 ? 0.4180 0.4837 0.3888 0.0530  0.0407  0.0082  198 PRO A CG  
1511 C CD  . PRO A 198 ? 0.4265 0.5093 0.3925 0.0647  0.0411  0.0036  198 PRO A CD  
1512 N N   . LEU A 199 ? 0.3824 0.4671 0.3668 0.0299  0.0538  0.0285  199 LEU A N   
1513 C CA  . LEU A 199 ? 0.3932 0.4832 0.3773 0.0226  0.0589  0.0372  199 LEU A CA  
1514 C C   . LEU A 199 ? 0.4075 0.4834 0.3998 0.0138  0.0603  0.0415  199 LEU A C   
1515 O O   . LEU A 199 ? 0.4210 0.4828 0.4174 0.0158  0.0569  0.0397  199 LEU A O   
1516 C CB  . LEU A 199 ? 0.3898 0.4744 0.3624 0.0262  0.0559  0.0416  199 LEU A CB  
1517 C CG  . LEU A 199 ? 0.3824 0.4756 0.3423 0.0357  0.0532  0.0352  199 LEU A CG  
1518 C CD1 . LEU A 199 ? 0.3970 0.4857 0.3432 0.0379  0.0491  0.0399  199 LEU A CD1 
1519 C CD2 . LEU A 199 ? 0.3803 0.4975 0.3378 0.0382  0.0605  0.0323  199 LEU A CD2 
1520 N N   . VAL A 200 ? 0.4083 0.4887 0.4021 0.0035  0.0657  0.0462  200 VAL A N   
1521 C CA  . VAL A 200 ? 0.4101 0.4721 0.4073 -0.0054 0.0667  0.0488  200 VAL A CA  
1522 C C   . VAL A 200 ? 0.4308 0.4767 0.4171 -0.0116 0.0688  0.0599  200 VAL A C   
1523 O O   . VAL A 200 ? 0.4479 0.5047 0.4280 -0.0210 0.0741  0.0660  200 VAL A O   
1524 C CB  . VAL A 200 ? 0.4075 0.4819 0.4127 -0.0152 0.0691  0.0442  200 VAL A CB  
1525 C CG1 . VAL A 200 ? 0.4043 0.4543 0.4088 -0.0248 0.0693  0.0450  200 VAL A CG1 
1526 C CG2 . VAL A 200 ? 0.4060 0.4928 0.4169 -0.0063 0.0653  0.0348  200 VAL A CG2 
1527 N N   . PHE A 201 ? 0.4359 0.4565 0.4188 -0.0060 0.0649  0.0630  201 PHE A N   
1528 C CA  . PHE A 201 ? 0.4686 0.4662 0.4365 -0.0075 0.0644  0.0745  201 PHE A CA  
1529 C C   . PHE A 201 ? 0.5122 0.4787 0.4761 -0.0151 0.0652  0.0763  201 PHE A C   
1530 O O   . PHE A 201 ? 0.5173 0.4761 0.4902 -0.0105 0.0637  0.0677  201 PHE A O   
1531 C CB  . PHE A 201 ? 0.4588 0.4501 0.4238 0.0086  0.0568  0.0765  201 PHE A CB  
1532 C CG  . PHE A 201 ? 0.4458 0.4620 0.4123 0.0154  0.0540  0.0726  201 PHE A CG  
1533 C CD1 . PHE A 201 ? 0.4643 0.4872 0.4145 0.0151  0.0543  0.0796  201 PHE A CD1 
1534 C CD2 . PHE A 201 ? 0.4289 0.4582 0.4092 0.0209  0.0511  0.0618  201 PHE A CD2 
1535 C CE1 . PHE A 201 ? 0.4634 0.5053 0.4114 0.0221  0.0510  0.0738  201 PHE A CE1 
1536 C CE2 . PHE A 201 ? 0.4358 0.4805 0.4136 0.0258  0.0474  0.0573  201 PHE A CE2 
1537 C CZ  . PHE A 201 ? 0.4521 0.5028 0.4139 0.0273  0.0469  0.0623  201 PHE A CZ  
1538 N N   . PRO A 202 ? 0.5559 0.5010 0.5030 -0.0275 0.0680  0.0872  202 PRO A N   
1539 C CA  . PRO A 202 ? 0.5937 0.4992 0.5316 -0.0350 0.0675  0.0885  202 PRO A CA  
1540 C C   . PRO A 202 ? 0.6275 0.4980 0.5547 -0.0165 0.0604  0.0922  202 PRO A C   
1541 O O   . PRO A 202 ? 0.6085 0.4925 0.5403 0.0012  0.0554  0.0926  202 PRO A O   
1542 C CB  . PRO A 202 ? 0.6147 0.5106 0.5364 -0.0583 0.0734  0.1002  202 PRO A CB  
1543 C CG  . PRO A 202 ? 0.6098 0.5258 0.5232 -0.0540 0.0752  0.1098  202 PRO A CG  
1544 C CD  . PRO A 202 ? 0.5661 0.5211 0.4992 -0.0374 0.0728  0.0986  202 PRO A CD  
1545 N N   . LYS A 203 ? 0.6722 0.4979 0.5847 -0.0196 0.0588  0.0940  203 LYS A N   
1546 C CA  . LYS A 203 ? 0.6990 0.4890 0.5992 0.0017  0.0512  0.0977  203 LYS A CA  
1547 C C   . LYS A 203 ? 0.7173 0.4961 0.5968 0.0066  0.0470  0.1145  203 LYS A C   
1548 O O   . LYS A 203 ? 0.7215 0.5056 0.5884 -0.0117 0.0522  0.1253  203 LYS A O   
1549 C CB  A LYS A 203 ? 0.7473 0.4830 0.6297 -0.0024 0.0500  0.0959  203 LYS A CB  
1550 C CB  B LYS A 203 ? 0.7471 0.4829 0.6296 -0.0023 0.0500  0.0958  203 LYS A CB  
1551 C CG  A LYS A 203 ? 0.7392 0.4700 0.6339 0.0165  0.0478  0.0797  203 LYS A CG  
1552 C CG  B LYS A 203 ? 0.7268 0.4689 0.6242 -0.0050 0.0529  0.0781  203 LYS A CG  
1553 C CD  A LYS A 203 ? 0.7986 0.4661 0.6685 0.0179  0.0447  0.0781  203 LYS A CD  
1554 C CD  B LYS A 203 ? 0.7849 0.4672 0.6601 -0.0064 0.0503  0.0746  203 LYS A CD  
1555 C CE  A LYS A 203 ? 0.7945 0.4590 0.6744 0.0419  0.0434  0.0611  203 LYS A CE  
1556 C CE  B LYS A 203 ? 0.8369 0.4810 0.6862 -0.0345 0.0516  0.0873  203 LYS A CE  
1557 N NZ  A LYS A 203 ? 0.8616 0.4588 0.7137 0.0481  0.0393  0.0577  203 LYS A NZ  
1558 N NZ  B LYS A 203 ? 0.9068 0.4818 0.7288 -0.0365 0.0475  0.0840  203 LYS A NZ  
1559 N N   . HIS A 204 ? 0.7404 0.5077 0.6166 0.0324  0.0377  0.1164  204 HIS A N   
1560 C CA  . HIS A 204 ? 0.7734 0.5252 0.6267 0.0435  0.0299  0.1320  204 HIS A CA  
1561 C C   . HIS A 204 ? 0.7263 0.5235 0.5853 0.0406  0.0308  0.1351  204 HIS A C   
1562 O O   . HIS A 204 ? 0.7773 0.5658 0.6145 0.0481  0.0244  0.1480  204 HIS A O   
1563 C CB  . HIS A 204 ? 0.8486 0.5436 0.6628 0.0288  0.0309  0.1494  204 HIS A CB  
1564 C CG  . HIS A 204 ? 0.9007 0.5420 0.7032 0.0281  0.0298  0.1457  204 HIS A CG  
1565 N ND1 . HIS A 204 ? 0.9131 0.5404 0.7139 0.0002  0.0385  0.1417  204 HIS A ND1 
1566 C CD2 . HIS A 204 ? 0.9430 0.5416 0.7345 0.0531  0.0203  0.1436  204 HIS A CD2 
1567 C CE1 . HIS A 204 ? 0.9566 0.5303 0.7428 0.0063  0.0343  0.1372  204 HIS A CE1 
1568 N NE2 . HIS A 204 ? 0.9754 0.5298 0.7553 0.0398  0.0238  0.1381  204 HIS A NE2 
1569 N N   . HIS A 205 ? 0.6387 0.4805 0.5225 0.0314  0.0375  0.1236  205 HIS A N   
1570 C CA  . HIS A 205 ? 0.5824 0.4646 0.4719 0.0330  0.0368  0.1225  205 HIS A CA  
1571 C C   . HIS A 205 ? 0.5597 0.4661 0.4705 0.0535  0.0276  0.1121  205 HIS A C   
1572 O O   . HIS A 205 ? 0.5445 0.4626 0.4789 0.0570  0.0290  0.0995  205 HIS A O   
1573 C CB  . HIS A 205 ? 0.5337 0.4483 0.4368 0.0155  0.0474  0.1148  205 HIS A CB  
1574 C CG  . HIS A 205 ? 0.5594 0.4705 0.4439 -0.0049 0.0567  0.1255  205 HIS A CG  
1575 N ND1 . HIS A 205 ? 0.5448 0.4932 0.4335 -0.0138 0.0642  0.1225  205 HIS A ND1 
1576 C CD2 . HIS A 205 ? 0.6136 0.4893 0.4747 -0.0191 0.0603  0.1389  205 HIS A CD2 
1577 C CE1 . HIS A 205 ? 0.5733 0.5168 0.4454 -0.0329 0.0732  0.1333  205 HIS A CE1 
1578 N NE2 . HIS A 205 ? 0.6159 0.5137 0.4701 -0.0387 0.0711  0.1442  205 HIS A NE2 
1579 N N   . VAL A 206 ? 0.5670 0.4827 0.4683 0.0654  0.0181  0.1175  206 VAL A N   
1580 C CA  . VAL A 206 ? 0.5495 0.4912 0.4709 0.0829  0.0075  0.1085  206 VAL A CA  
1581 C C   . VAL A 206 ? 0.5252 0.5033 0.4541 0.0768  0.0072  0.1011  206 VAL A C   
1582 O O   . VAL A 206 ? 0.5371 0.5176 0.4444 0.0744  0.0052  0.1079  206 VAL A O   
1583 C CB  . VAL A 206 ? 0.5814 0.5074 0.4872 0.1033  -0.0068 0.1183  206 VAL A CB  
1584 C CG1 . VAL A 206 ? 0.5609 0.5247 0.4924 0.1192  -0.0184 0.1076  206 VAL A CG1 
1585 C CG2 . VAL A 206 ? 0.6177 0.4997 0.5127 0.1123  -0.0074 0.1245  206 VAL A CG2 
1586 N N   . VAL A 207 ? 0.4938 0.4968 0.4495 0.0744  0.0093  0.0871  207 VAL A N   
1587 C CA  . VAL A 207 ? 0.4700 0.5007 0.4321 0.0697  0.0071  0.0782  207 VAL A CA  
1588 C C   . VAL A 207 ? 0.4685 0.5210 0.4463 0.0807  -0.0057 0.0722  207 VAL A C   
1589 O O   . VAL A 207 ? 0.4512 0.5128 0.4520 0.0864  -0.0064 0.0665  207 VAL A O   
1590 C CB  . VAL A 207 ? 0.4398 0.4791 0.4168 0.0580  0.0169  0.0679  207 VAL A CB  
1591 C CG1 . VAL A 207 ? 0.4159 0.4740 0.3937 0.0542  0.0134  0.0589  207 VAL A CG1 
1592 C CG2 . VAL A 207 ? 0.4545 0.4795 0.4204 0.0476  0.0280  0.0728  207 VAL A CG2 
1593 N N   . SER A 208 ? 0.4900 0.5545 0.4556 0.0833  -0.0157 0.0724  208 SER A N   
1594 C CA  . SER A 208 ? 0.5088 0.5979 0.4879 0.0929  -0.0307 0.0673  208 SER A CA  
1595 C C   . SER A 208 ? 0.4785 0.5881 0.4610 0.0822  -0.0349 0.0554  208 SER A C   
1596 O O   . SER A 208 ? 0.4792 0.5817 0.4373 0.0778  -0.0349 0.0558  208 SER A O   
1597 C CB  . SER A 208 ? 0.5684 0.6490 0.5248 0.1079  -0.0434 0.0789  208 SER A CB  
1598 O OG  . SER A 208 ? 0.5797 0.6904 0.5497 0.1172  -0.0602 0.0727  208 SER A OG  
1599 N N   . LEU A 209 ? 0.4632 0.5969 0.4741 0.0775  -0.0381 0.0445  209 LEU A N   
1600 C CA  . LEU A 209 ? 0.4749 0.6242 0.4888 0.0654  -0.0444 0.0328  209 LEU A CA  
1601 C C   . LEU A 209 ? 0.5174 0.6949 0.5388 0.0716  -0.0630 0.0295  209 LEU A C   
1602 O O   . LEU A 209 ? 0.5291 0.7283 0.5731 0.0825  -0.0687 0.0309  209 LEU A O   
1603 C CB  . LEU A 209 ? 0.4452 0.6022 0.4828 0.0512  -0.0359 0.0238  209 LEU A CB  
1604 C CG  . LEU A 209 ? 0.4276 0.5616 0.4619 0.0461  -0.0194 0.0261  209 LEU A CG  
1605 C CD1 . LEU A 209 ? 0.4063 0.5466 0.4577 0.0315  -0.0134 0.0178  209 LEU A CD1 
1606 C CD2 . LEU A 209 ? 0.4440 0.5549 0.4494 0.0449  -0.0153 0.0283  209 LEU A CD2 
1607 N N   . GLN A 210 ? 0.5398 0.7185 0.5419 0.0663  -0.0733 0.0237  210 GLN A N   
1608 C CA  . GLN A 210 ? 0.5598 0.7661 0.5651 0.0712  -0.0935 0.0196  210 GLN A CA  
1609 C C   . GLN A 210 ? 0.5688 0.7845 0.5741 0.0525  -0.1015 0.0042  210 GLN A C   
1610 O O   . GLN A 210 ? 0.5777 0.7669 0.5584 0.0439  -0.0958 -0.0004 210 GLN A O   
1611 C CB  . GLN A 210 ? 0.5864 0.7795 0.5560 0.0867  -0.1024 0.0301  210 GLN A CB  
1612 C CG  . GLN A 210 ? 0.6035 0.7800 0.5676 0.1038  -0.0969 0.0466  210 GLN A CG  
1613 C CD  . GLN A 210 ? 0.6621 0.8162 0.5828 0.1142  -0.1015 0.0596  210 GLN A CD  
1614 O OE1 . GLN A 210 ? 0.6952 0.8538 0.5917 0.1126  -0.1117 0.0556  210 GLN A OE1 
1615 N NE2 . GLN A 210 ? 0.6830 0.8105 0.5906 0.1238  -0.0937 0.0753  210 GLN A NE2 
1616 N N   . PRO A 211 ? 0.5782 0.8313 0.6106 0.0460  -0.1151 -0.0046 211 PRO A N   
1617 C CA  . PRO A 211 ? 0.5906 0.8490 0.6231 0.0235  -0.1231 -0.0199 211 PRO A CA  
1618 C C   . PRO A 211 ? 0.6441 0.8899 0.6388 0.0254  -0.1381 -0.0253 211 PRO A C   
1619 O O   . PRO A 211 ? 0.6602 0.9093 0.6359 0.0436  -0.1474 -0.0178 211 PRO A O   
1620 C CB  . PRO A 211 ? 0.5786 0.8895 0.6544 0.0164  -0.1337 -0.0265 211 PRO A CB  
1621 C CG  . PRO A 211 ? 0.5732 0.9071 0.6588 0.0435  -0.1410 -0.0162 211 PRO A CG  
1622 C CD  . PRO A 211 ? 0.5738 0.8675 0.6386 0.0590  -0.1242 -0.0020 211 PRO A CD  
1623 N N   . VAL A 212 ? 0.6839 0.9115 0.6641 0.0064  -0.1404 -0.0387 212 VAL A N   
1624 C CA  . VAL A 212 ? 0.7606 0.9739 0.7029 0.0058  -0.1547 -0.0483 212 VAL A CA  
1625 C C   . VAL A 212 ? 0.8099 1.0506 0.7651 -0.0128 -0.1759 -0.0637 212 VAL A C   
1626 O O   . VAL A 212 ? 0.8545 1.1092 0.7921 -0.0071 -0.1953 -0.0687 212 VAL A O   
1627 C CB  . VAL A 212 ? 0.7929 0.9578 0.7006 0.0020  -0.1427 -0.0540 212 VAL A CB  
1628 C CG1 . VAL A 212 ? 0.8378 0.9869 0.7023 0.0048  -0.1563 -0.0656 212 VAL A CG1 
1629 C CG2 . VAL A 212 ? 0.7868 0.9335 0.6871 0.0180  -0.1221 -0.0395 212 VAL A CG2 
1630 N N   . ASN A 213 ? 0.8201 1.0697 0.8046 -0.0370 -0.1730 -0.0711 213 ASN A N   
1631 C CA  . ASN A 213 ? 0.8620 1.1429 0.8647 -0.0604 -0.1920 -0.0857 213 ASN A CA  
1632 C C   . ASN A 213 ? 0.8155 1.1448 0.8734 -0.0730 -0.1873 -0.0834 213 ASN A C   
1633 O O   . ASN A 213 ? 0.8141 1.1984 0.9031 -0.0635 -0.1988 -0.0817 213 ASN A O   
1634 C CB  . ASN A 213 ? 0.9397 1.1762 0.9136 -0.0854 -0.1948 -0.1011 213 ASN A CB  
1635 C CG  . ASN A 213 ? 1.0137 1.2349 0.9462 -0.0825 -0.2148 -0.1139 213 ASN A CG  
1636 O OD1 . ASN A 213 ? 1.0601 1.2513 0.9531 -0.0609 -0.2111 -0.1110 213 ASN A OD1 
1637 N ND2 . ASN A 213 ? 1.0439 1.2883 0.9848 -0.1055 -0.2360 -0.1291 213 ASN A ND2 
1638 N N   . ASP A 214 ? 0.7853 1.0959 0.8542 -0.0929 -0.1704 -0.0834 214 ASP A N   
1639 C CA  . ASP A 214 ? 0.7572 1.1138 0.8758 -0.1061 -0.1620 -0.0812 214 ASP A CA  
1640 C C   . ASP A 214 ? 0.7260 1.1044 0.8657 -0.0762 -0.1501 -0.0669 214 ASP A C   
1641 O O   . ASP A 214 ? 0.7295 1.0680 0.8460 -0.0581 -0.1364 -0.0566 214 ASP A O   
1642 C CB  . ASP A 214 ? 0.7635 1.0860 0.8791 -0.1343 -0.1458 -0.0827 214 ASP A CB  
1643 C CG  . ASP A 214 ? 0.7754 1.1497 0.9387 -0.1591 -0.1400 -0.0847 214 ASP A CG  
1644 O OD1 . ASP A 214 ? 0.7556 1.1822 0.9570 -0.1430 -0.1347 -0.0788 214 ASP A OD1 
1645 O OD2 . ASP A 214 ? 0.8141 1.1760 0.9753 -0.1949 -0.1404 -0.0924 214 ASP A OD2 
1646 N N   . LYS A 215 ? 0.7036 1.1463 0.8875 -0.0709 -0.1558 -0.0673 215 LYS A N   
1647 C CA  . LYS A 215 ? 0.6543 1.1176 0.8576 -0.0400 -0.1477 -0.0558 215 LYS A CA  
1648 C C   . LYS A 215 ? 0.5978 1.0895 0.8401 -0.0481 -0.1286 -0.0546 215 LYS A C   
1649 O O   . LYS A 215 ? 0.5771 1.0979 0.8435 -0.0238 -0.1240 -0.0490 215 LYS A O   
1650 C CB  . LYS A 215 ? 0.6618 1.1746 0.8812 -0.0176 -0.1699 -0.0567 215 LYS A CB  
1651 C CG  . LYS A 215 ? 0.6873 1.1854 0.8715 -0.0176 -0.1924 -0.0619 215 LYS A CG  
1652 C CD  . LYS A 215 ? 0.6897 1.2285 0.8813 0.0107  -0.2147 -0.0592 215 LYS A CD  
1653 C CE  . LYS A 215 ? 0.6824 1.1852 0.8462 0.0461  -0.2087 -0.0418 215 LYS A CE  
1654 N NZ  . LYS A 215 ? 0.7056 1.2344 0.8631 0.0742  -0.2329 -0.0374 215 LYS A NZ  
1655 N N   . ASP A 216 ? 0.5754 1.0561 0.8207 -0.0810 -0.1174 -0.0596 216 ASP A N   
1656 C CA  . ASP A 216 ? 0.5450 1.0485 0.8206 -0.0923 -0.0969 -0.0580 216 ASP A CA  
1657 C C   . ASP A 216 ? 0.5404 0.9787 0.7836 -0.0954 -0.0771 -0.0499 216 ASP A C   
1658 O O   . ASP A 216 ? 0.5662 0.9514 0.7728 -0.1090 -0.0789 -0.0509 216 ASP A O   
1659 C CB  . ASP A 216 ? 0.5541 1.1004 0.8588 -0.1312 -0.0989 -0.0686 216 ASP A CB  
1660 C CG  . ASP A 216 ? 0.5688 1.1858 0.9078 -0.1307 -0.1212 -0.0785 216 ASP A CG  
1661 O OD1 . ASP A 216 ? 0.5626 1.2093 0.9146 -0.0955 -0.1307 -0.0758 216 ASP A OD1 
1662 O OD2 . ASP A 216 ? 0.5958 1.2377 0.9477 -0.1658 -0.1302 -0.0890 216 ASP A OD2 
1663 N N   . PHE A 217 ? 0.5095 0.9522 0.7652 -0.0810 -0.0593 -0.0430 217 PHE A N   
1664 C CA  . PHE A 217 ? 0.4909 0.8772 0.7177 -0.0804 -0.0420 -0.0352 217 PHE A CA  
1665 C C   . PHE A 217 ? 0.4634 0.8717 0.7133 -0.0876 -0.0217 -0.0336 217 PHE A C   
1666 O O   . PHE A 217 ? 0.4466 0.9103 0.7333 -0.0773 -0.0188 -0.0364 217 PHE A O   
1667 C CB  . PHE A 217 ? 0.4783 0.8305 0.6815 -0.0483 -0.0419 -0.0267 217 PHE A CB  
1668 C CG  . PHE A 217 ? 0.4890 0.8221 0.6666 -0.0389 -0.0595 -0.0271 217 PHE A CG  
1669 C CD1 . PHE A 217 ? 0.5080 0.7912 0.6479 -0.0478 -0.0609 -0.0279 217 PHE A CD1 
1670 C CD2 . PHE A 217 ? 0.4854 0.8502 0.6742 -0.0189 -0.0747 -0.0269 217 PHE A CD2 
1671 C CE1 . PHE A 217 ? 0.5247 0.7925 0.6387 -0.0383 -0.0754 -0.0293 217 PHE A CE1 
1672 C CE2 . PHE A 217 ? 0.5036 0.8505 0.6643 -0.0105 -0.0903 -0.0267 217 PHE A CE2 
1673 C CZ  . PHE A 217 ? 0.5211 0.8207 0.6444 -0.0209 -0.0897 -0.0283 217 PHE A CZ  
1674 N N   . GLN A 218 ? 0.4613 0.8258 0.6871 -0.1033 -0.0080 -0.0296 218 GLN A N   
1675 C CA  . GLN A 218 ? 0.4381 0.8121 0.6745 -0.1092 0.0126  -0.0266 218 GLN A CA  
1676 C C   . GLN A 218 ? 0.4188 0.7590 0.6370 -0.0815 0.0210  -0.0196 218 GLN A C   
1677 O O   . GLN A 218 ? 0.4306 0.7166 0.6143 -0.0812 0.0228  -0.0146 218 GLN A O   
1678 C CB  . GLN A 218 ? 0.4521 0.7958 0.6687 -0.1437 0.0212  -0.0252 218 GLN A CB  
1679 C CG  . GLN A 218 ? 0.4543 0.8201 0.6844 -0.1566 0.0423  -0.0228 218 GLN A CG  
1680 C CD  . GLN A 218 ? 0.4608 0.9038 0.7373 -0.1716 0.0456  -0.0300 218 GLN A CD  
1681 O OE1 . GLN A 218 ? 0.4897 0.9583 0.7812 -0.1907 0.0327  -0.0361 218 GLN A OE1 
1682 N NE2 . GLN A 218 ? 0.4402 0.9239 0.7403 -0.1629 0.0627  -0.0306 218 GLN A NE2 
1683 N N   . ILE A 219 ? 0.3968 0.7696 0.6383 -0.0578 0.0251  -0.0202 219 ILE A N   
1684 C CA  . ILE A 219 ? 0.3812 0.7230 0.6067 -0.0322 0.0311  -0.0147 219 ILE A CA  
1685 C C   . ILE A 219 ? 0.3800 0.7270 0.6103 -0.0346 0.0508  -0.0151 219 ILE A C   
1686 O O   . ILE A 219 ? 0.3680 0.7644 0.6280 -0.0392 0.0590  -0.0207 219 ILE A O   
1687 C CB  . ILE A 219 ? 0.3721 0.7333 0.6114 -0.0017 0.0205  -0.0148 219 ILE A CB  
1688 C CG1 . ILE A 219 ? 0.3712 0.7287 0.6017 -0.0002 0.0006  -0.0141 219 ILE A CG1 
1689 C CG2 . ILE A 219 ? 0.3728 0.6949 0.5918 0.0203  0.0264  -0.0088 219 ILE A CG2 
1690 C CD1 . ILE A 219 ? 0.3711 0.7469 0.6115 0.0290  -0.0122 -0.0126 219 ILE A CD1 
1691 N N   . SER A 220 ? 0.3952 0.6951 0.5963 -0.0312 0.0583  -0.0098 220 SER A N   
1692 C CA  . SER A 220 ? 0.4021 0.6994 0.5997 -0.0322 0.0758  -0.0102 220 SER A CA  
1693 C C   . SER A 220 ? 0.4104 0.6853 0.5982 -0.0060 0.0776  -0.0090 220 SER A C   
1694 O O   . SER A 220 ? 0.4079 0.6509 0.5789 0.0047  0.0678  -0.0044 220 SER A O   
1695 C CB  . SER A 220 ? 0.3994 0.6586 0.5672 -0.0546 0.0825  -0.0053 220 SER A CB  
1696 O OG  . SER A 220 ? 0.3886 0.5987 0.5268 -0.0460 0.0764  -0.0002 220 SER A OG  
1697 N N   . VAL A 221 ? 0.4210 0.7123 0.6179 0.0030  0.0906  -0.0138 221 VAL A N   
1698 C CA  . VAL A 221 ? 0.4215 0.6865 0.6055 0.0244  0.0938  -0.0146 221 VAL A CA  
1699 C C   . VAL A 221 ? 0.4345 0.6954 0.6070 0.0158  0.1107  -0.0177 221 VAL A C   
1700 O O   . VAL A 221 ? 0.4564 0.7554 0.6472 0.0179  0.1226  -0.0249 221 VAL A O   
1701 C CB  . VAL A 221 ? 0.4171 0.7059 0.6227 0.0521  0.0898  -0.0200 221 VAL A CB  
1702 C CG1 . VAL A 221 ? 0.4309 0.6852 0.6187 0.0710  0.0943  -0.0220 221 VAL A CG1 
1703 C CG2 . VAL A 221 ? 0.4055 0.6950 0.6166 0.0610  0.0716  -0.0153 221 VAL A CG2 
1704 N N   . ASP A 222 ? 0.4364 0.6548 0.5782 0.0069  0.1119  -0.0126 222 ASP A N   
1705 C CA  . ASP A 222 ? 0.4611 0.6700 0.5844 -0.0033 0.1257  -0.0138 222 ASP A CA  
1706 C C   . ASP A 222 ? 0.5056 0.7444 0.6377 -0.0263 0.1345  -0.0129 222 ASP A C   
1707 O O   . ASP A 222 ? 0.5229 0.7566 0.6538 -0.0426 0.1267  -0.0074 222 ASP A O   
1708 C CB  . ASP A 222 ? 0.4652 0.6771 0.5887 0.0159  0.1344  -0.0225 222 ASP A CB  
1709 C CG  . ASP A 222 ? 0.4795 0.6545 0.5905 0.0331  0.1246  -0.0222 222 ASP A CG  
1710 O OD1 . ASP A 222 ? 0.4756 0.6220 0.5725 0.0270  0.1144  -0.0146 222 ASP A OD1 
1711 O OD2 . ASP A 222 ? 0.5007 0.6748 0.6149 0.0524  0.1274  -0.0299 222 ASP A OD2 
1712 N N   . HIS A 223 ? 0.5400 0.8091 0.6793 -0.0297 0.1510  -0.0184 223 HIS A N   
1713 C CA  . HIS A 223 ? 0.5749 0.8731 0.7213 -0.0563 0.1611  -0.0162 223 HIS A CA  
1714 C C   . HIS A 223 ? 0.5746 0.9257 0.7619 -0.0591 0.1570  -0.0204 223 HIS A C   
1715 O O   . HIS A 223 ? 0.5932 0.9593 0.7864 -0.0860 0.1576  -0.0167 223 HIS A O   
1716 C CB  . HIS A 223 ? 0.5978 0.9153 0.7367 -0.0605 0.1822  -0.0205 223 HIS A CB  
1717 C CG  . HIS A 223 ? 0.6206 0.9599 0.7578 -0.0930 0.1950  -0.0154 223 HIS A CG  
1718 N ND1 . HIS A 223 ? 0.6441 0.9392 0.7452 -0.1172 0.1936  -0.0037 223 HIS A ND1 
1719 C CD2 . HIS A 223 ? 0.6304 1.0306 0.7965 -0.1062 0.2094  -0.0201 223 HIS A CD2 
1720 C CE1 . HIS A 223 ? 0.6645 0.9861 0.7688 -0.1462 0.2067  -0.0001 223 HIS A CE1 
1721 N NE2 . HIS A 223 ? 0.6571 1.0415 0.8014 -0.1396 0.2150  -0.0095 223 HIS A NE2 
1722 N N   . LEU A 224 ? 0.5589 0.9366 0.7728 -0.0321 0.1514  -0.0280 224 LEU A N   
1723 C CA  . LEU A 224 ? 0.5561 0.9891 0.8105 -0.0305 0.1450  -0.0329 224 LEU A CA  
1724 C C   . LEU A 224 ? 0.5639 0.9775 0.8152 -0.0420 0.1259  -0.0265 224 LEU A C   
1725 O O   . LEU A 224 ? 0.5800 0.9434 0.8066 -0.0336 0.1143  -0.0208 224 LEU A O   
1726 C CB  . LEU A 224 ? 0.5560 1.0124 0.8329 0.0066  0.1410  -0.0417 224 LEU A CB  
1727 C CG  . LEU A 224 ? 0.5711 1.0847 0.8897 0.0167  0.1299  -0.0470 224 LEU A CG  
1728 C CD1 . LEU A 224 ? 0.5703 1.1569 0.9235 -0.0029 0.1435  -0.0536 224 LEU A CD1 
1729 C CD2 . LEU A 224 ? 0.5919 1.1101 0.9216 0.0583  0.1230  -0.0535 224 LEU A CD2 
1730 N N   . SER A 225 ? 0.5571 1.0134 0.8336 -0.0625 0.1231  -0.0283 225 SER A N   
1731 C CA  . SER A 225 ? 0.5583 0.9998 0.8317 -0.0748 0.1046  -0.0248 225 SER A CA  
1732 C C   . SER A 225 ? 0.5578 1.0681 0.8732 -0.0863 0.1000  -0.0319 225 SER A C   
1733 O O   . SER A 225 ? 0.5725 1.1230 0.9049 -0.1109 0.1137  -0.0345 225 SER A O   
1734 C CB  . SER A 225 ? 0.5848 0.9738 0.8213 -0.1036 0.1055  -0.0167 225 SER A CB  
1735 O OG  . SER A 225 ? 0.6002 0.9739 0.8317 -0.1149 0.0879  -0.0157 225 SER A OG  
1736 N N   . ILE A 226 ? 0.5392 1.0653 0.8709 -0.0698 0.0808  -0.0347 226 ILE A N   
1737 C CA  . ILE A 226 ? 0.5279 1.1240 0.9018 -0.0772 0.0723  -0.0426 226 ILE A CA  
1738 C C   . ILE A 226 ? 0.5173 1.0948 0.8823 -0.0802 0.0482  -0.0414 226 ILE A C   
1739 O O   . ILE A 226 ? 0.5118 1.0372 0.8476 -0.0617 0.0378  -0.0359 226 ILE A O   
1740 C CB  . ILE A 226 ? 0.5189 1.1756 0.9314 -0.0429 0.0732  -0.0509 226 ILE A CB  
1741 C CG1 . ILE A 226 ? 0.5259 1.1376 0.9175 -0.0029 0.0641  -0.0472 226 ILE A CG1 
1742 C CG2 . ILE A 226 ? 0.5154 1.2030 0.9411 -0.0458 0.0971  -0.0552 226 ILE A CG2 
1743 C CD1 . ILE A 226 ? 0.5297 1.1866 0.9513 0.0353  0.0636  -0.0550 226 ILE A CD1 
1744 N N   . LEU A 227 ? 0.5100 1.1326 0.8998 -0.1053 0.0399  -0.0473 227 LEU A N   
1745 C CA  . LEU A 227 ? 0.5112 1.1229 0.8935 -0.1101 0.0160  -0.0488 227 LEU A CA  
1746 C C   . LEU A 227 ? 0.5071 1.1588 0.9137 -0.0743 -0.0009 -0.0528 227 LEU A C   
1747 O O   . LEU A 227 ? 0.5084 1.2352 0.9600 -0.0668 -0.0014 -0.0606 227 LEU A O   
1748 C CB  . LEU A 227 ? 0.5275 1.1707 0.9255 -0.1533 0.0122  -0.0547 227 LEU A CB  
1749 C CG  . LEU A 227 ? 0.5454 1.1969 0.9451 -0.1606 -0.0140 -0.0607 227 LEU A CG  
1750 C CD1 . LEU A 227 ? 0.5579 1.1276 0.9060 -0.1515 -0.0255 -0.0551 227 LEU A CD1 
1751 C CD2 . LEU A 227 ? 0.5741 1.2563 0.9900 -0.2084 -0.0158 -0.0675 227 LEU A CD2 
1752 N N   . HIS A 228 ? 0.5121 1.1150 0.8881 -0.0514 -0.0146 -0.0471 228 HIS A N   
1753 C CA  . HIS A 228 ? 0.5138 1.1403 0.9015 -0.0168 -0.0326 -0.0479 228 HIS A CA  
1754 C C   . HIS A 228 ? 0.5226 1.1637 0.9100 -0.0285 -0.0566 -0.0523 228 HIS A C   
1755 O O   . HIS A 228 ? 0.5348 1.1267 0.8877 -0.0473 -0.0619 -0.0503 228 HIS A O   
1756 C CB  . HIS A 228 ? 0.5204 1.0842 0.8717 0.0135  -0.0324 -0.0377 228 HIS A CB  
1757 C CG  . HIS A 228 ? 0.5124 1.0667 0.8660 0.0307  -0.0132 -0.0355 228 HIS A CG  
1758 N ND1 . HIS A 228 ? 0.5214 1.0949 0.8900 0.0670  -0.0154 -0.0363 228 HIS A ND1 
1759 C CD2 . HIS A 228 ? 0.5155 1.0405 0.8553 0.0176  0.0074  -0.0333 228 HIS A CD2 
1760 C CE1 . HIS A 228 ? 0.5205 1.0760 0.8842 0.0744  0.0036  -0.0360 228 HIS A CE1 
1761 N NE2 . HIS A 228 ? 0.5169 1.0452 0.8637 0.0445  0.0175  -0.0340 228 HIS A NE2 
1762 N N   . ARG A 229 ? 0.5208 1.2305 0.9457 -0.0156 -0.0717 -0.0595 229 ARG A N   
1763 C CA  . ARG A 229 ? 0.5365 1.2741 0.9676 -0.0283 -0.0961 -0.0663 229 ARG A CA  
1764 C C   . ARG A 229 ? 0.5591 1.2851 0.9727 0.0088  -0.1181 -0.0615 229 ARG A C   
1765 O O   . ARG A 229 ? 0.5597 1.2961 0.9822 0.0460  -0.1182 -0.0571 229 ARG A O   
1766 C CB  . ARG A 229 ? 0.5355 1.3576 1.0189 -0.0439 -0.0988 -0.0776 229 ARG A CB  
1767 C CG  . ARG A 229 ? 0.5587 1.3939 1.0422 -0.0761 -0.1173 -0.0857 229 ARG A CG  
1768 C CD  . ARG A 229 ? 0.5576 1.3641 1.0268 -0.1251 -0.1052 -0.0879 229 ARG A CD  
1769 N NE  . ARG A 229 ? 0.5548 1.3920 1.0519 -0.1484 -0.0851 -0.0897 229 ARG A NE  
1770 C CZ  . ARG A 229 ? 0.5586 1.3723 1.0445 -0.1919 -0.0730 -0.0900 229 ARG A CZ  
1771 N NH1 . ARG A 229 ? 0.5752 1.3318 1.0230 -0.2161 -0.0796 -0.0899 229 ARG A NH1 
1772 N NH2 . ARG A 229 ? 0.5565 1.4001 1.0657 -0.2102 -0.0546 -0.0903 229 ARG A NH2 
1773 N N   . ASP A 230 ? 0.5857 1.2864 0.9704 -0.0015 -0.1366 -0.0625 230 ASP A N   
1774 C CA  . ASP A 230 ? 0.6141 1.3021 0.9752 0.0287  -0.1589 -0.0574 230 ASP A CA  
1775 C C   . ASP A 230 ? 0.6029 1.2317 0.9307 0.0607  -0.1490 -0.0426 230 ASP A C   
1776 O O   . ASP A 230 ? 0.6101 1.2507 0.9436 0.0963  -0.1562 -0.0369 230 ASP A O   
1777 C CB  . ASP A 230 ? 0.6465 1.4156 1.0500 0.0478  -0.1800 -0.0646 230 ASP A CB  
1778 C CG  . ASP A 230 ? 0.6973 1.4533 1.0714 0.0741  -0.2067 -0.0596 230 ASP A CG  
1779 O OD1 . ASP A 230 ? 0.7231 1.4499 1.0636 0.0569  -0.2188 -0.0616 230 ASP A OD1 
1780 O OD2 . ASP A 230 ? 0.7249 1.4833 1.1009 0.1107  -0.2124 -0.0523 230 ASP A OD2 
1781 N N   . VAL A 231 ? 0.5898 1.1532 0.8817 0.0471  -0.1330 -0.0365 231 VAL A N   
1782 C CA  . VAL A 231 ? 0.5776 1.0835 0.8375 0.0693  -0.1215 -0.0232 231 VAL A CA  
1783 C C   . VAL A 231 ? 0.5926 1.0607 0.8092 0.0829  -0.1368 -0.0152 231 VAL A C   
1784 O O   . VAL A 231 ? 0.6079 1.0611 0.8016 0.0650  -0.1448 -0.0195 231 VAL A O   
1785 C CB  . VAL A 231 ? 0.5610 1.0214 0.8049 0.0489  -0.0981 -0.0211 231 VAL A CB  
1786 C CG1 . VAL A 231 ? 0.5555 0.9584 0.7653 0.0679  -0.0885 -0.0083 231 VAL A CG1 
1787 C CG2 . VAL A 231 ? 0.5517 1.0473 0.8332 0.0373  -0.0816 -0.0271 231 VAL A CG2 
1788 N N   . GLN A 232 ? 0.5948 1.0449 0.7968 0.1145  -0.1404 -0.0037 232 GLN A N   
1789 C CA  . GLN A 232 ? 0.6108 1.0208 0.7668 0.1276  -0.1516 0.0071  232 GLN A CA  
1790 C C   . GLN A 232 ? 0.6127 0.9584 0.7316 0.1268  -0.1334 0.0187  232 GLN A C   
1791 O O   . GLN A 232 ? 0.6347 0.9470 0.7136 0.1246  -0.1366 0.0247  232 GLN A O   
1792 C CB  . GLN A 232 ? 0.6314 1.0575 0.7878 0.1624  -0.1699 0.0146  232 GLN A CB  
1793 N N   . GLU A 233 ? 0.5844 0.9156 0.7158 0.1277  -0.1143 0.0210  233 GLU A N   
1794 C CA  . GLU A 233 ? 0.5589 0.8348 0.6595 0.1263  -0.0980 0.0313  233 GLU A CA  
1795 C C   . GLU A 233 ? 0.5239 0.7966 0.6465 0.1217  -0.0786 0.0282  233 GLU A C   
1796 O O   . GLU A 233 ? 0.5159 0.8211 0.6709 0.1320  -0.0783 0.0229  233 GLU A O   
1797 C CB  . GLU A 233 ? 0.5827 0.8255 0.6522 0.1503  -0.1044 0.0468  233 GLU A CB  
1798 C CG  . GLU A 233 ? 0.5906 0.7799 0.6278 0.1447  -0.0883 0.0577  233 GLU A CG  
1799 C CD  . GLU A 233 ? 0.6450 0.7981 0.6506 0.1649  -0.0937 0.0743  233 GLU A CD  
1800 O OE1 . GLU A 233 ? 0.6814 0.8476 0.6912 0.1876  -0.1099 0.0774  233 GLU A OE1 
1801 O OE2 . GLU A 233 ? 0.6625 0.7742 0.6387 0.1576  -0.0821 0.0846  233 GLU A OE2 
1802 N N   . ILE A 234 ? 0.5055 0.7420 0.6098 0.1072  -0.0629 0.0308  234 ILE A N   
1803 C CA  . ILE A 234 ? 0.4811 0.7041 0.5954 0.1039  -0.0449 0.0300  234 ILE A CA  
1804 C C   . ILE A 234 ? 0.5156 0.6895 0.5981 0.1085  -0.0371 0.0415  234 ILE A C   
1805 O O   . ILE A 234 ? 0.5317 0.6840 0.5883 0.0988  -0.0359 0.0457  234 ILE A O   
1806 C CB  . ILE A 234 ? 0.4352 0.6650 0.5597 0.0788  -0.0339 0.0211  234 ILE A CB  
1807 C CG1 . ILE A 234 ? 0.4055 0.6809 0.5564 0.0673  -0.0426 0.0105  234 ILE A CG1 
1808 C CG2 . ILE A 234 ? 0.4270 0.6492 0.5625 0.0773  -0.0169 0.0195  234 ILE A CG2 
1809 C CD1 . ILE A 234 ? 0.3771 0.6495 0.5294 0.0401  -0.0339 0.0036  234 ILE A CD1 
1810 N N   . ARG A 235 ? 0.5413 0.6985 0.6255 0.1226  -0.0317 0.0455  235 ARG A N   
1811 C CA  . ARG A 235 ? 0.5789 0.6888 0.6335 0.1249  -0.0253 0.0567  235 ARG A CA  
1812 C C   . ARG A 235 ? 0.5649 0.6591 0.6253 0.1161  -0.0091 0.0525  235 ARG A C   
1813 O O   . ARG A 235 ? 0.5641 0.6735 0.6467 0.1229  -0.0047 0.0445  235 ARG A O   
1814 C CB  . ARG A 235 ? 0.6325 0.7226 0.6740 0.1490  -0.0355 0.0663  235 ARG A CB  
1815 C CG  . ARG A 235 ? 0.6840 0.7744 0.7041 0.1566  -0.0513 0.0753  235 ARG A CG  
1816 C CD  . ARG A 235 ? 0.7639 0.8293 0.7668 0.1828  -0.0630 0.0865  235 ARG A CD  
1817 N NE  . ARG A 235 ? 0.8227 0.8321 0.7970 0.1813  -0.0536 0.0977  235 ARG A NE  
1818 C CZ  . ARG A 235 ? 0.8572 0.8444 0.8376 0.1915  -0.0479 0.0952  235 ARG A CZ  
1819 N NH1 . ARG A 235 ? 0.8382 0.8584 0.8529 0.2060  -0.0490 0.0819  235 ARG A NH1 
1820 N NH2 . ARG A 235 ? 0.9096 0.8425 0.8608 0.1860  -0.0407 0.1051  235 ARG A NH2 
1821 N N   . TYR A 236 ? 0.5578 0.6252 0.5980 0.1017  -0.0004 0.0571  236 TYR A N   
1822 C CA  . TYR A 236 ? 0.5357 0.5867 0.5768 0.0922  0.0129  0.0537  236 TYR A CA  
1823 C C   . TYR A 236 ? 0.5662 0.5760 0.5827 0.0926  0.0160  0.0637  236 TYR A C   
1824 O O   . TYR A 236 ? 0.5870 0.5824 0.5816 0.0895  0.0127  0.0741  236 TYR A O   
1825 C CB  . TYR A 236 ? 0.5025 0.5620 0.5440 0.0733  0.0199  0.0489  236 TYR A CB  
1826 C CG  . TYR A 236 ? 0.5014 0.5916 0.5641 0.0675  0.0198  0.0388  236 TYR A CG  
1827 C CD1 . TYR A 236 ? 0.5254 0.6338 0.6102 0.0724  0.0233  0.0318  236 TYR A CD1 
1828 C CD2 . TYR A 236 ? 0.5006 0.6003 0.5596 0.0562  0.0170  0.0359  236 TYR A CD2 
1829 C CE1 . TYR A 236 ? 0.5318 0.6693 0.6351 0.0627  0.0248  0.0239  236 TYR A CE1 
1830 C CE2 . TYR A 236 ? 0.5110 0.6324 0.5858 0.0470  0.0168  0.0276  236 TYR A CE2 
1831 C CZ  . TYR A 236 ? 0.5255 0.6670 0.6230 0.0485  0.0212  0.0225  236 TYR A CZ  
1832 O OH  . TYR A 236 ? 0.5259 0.6903 0.6384 0.0353  0.0225  0.0155  236 TYR A OH  
1833 N N   . GLU A 237 ? 0.5693 0.5598 0.5874 0.0946  0.0227  0.0603  237 GLU A N   
1834 C CA  . GLU A 237 ? 0.5911 0.5384 0.5856 0.0909  0.0256  0.0683  237 GLU A CA  
1835 C C   . GLU A 237 ? 0.5966 0.5298 0.5963 0.0891  0.0337  0.0590  237 GLU A C   
1836 O O   . GLU A 237 ? 0.5989 0.5512 0.6177 0.0992  0.0355  0.0483  237 GLU A O   
1837 C CB  . GLU A 237 ? 0.6242 0.5432 0.6002 0.1081  0.0156  0.0791  237 GLU A CB  
1838 C CG  . GLU A 237 ? 0.6299 0.5640 0.6230 0.1340  0.0073  0.0730  237 GLU A CG  
1839 C CD  . GLU A 237 ? 0.6809 0.5857 0.6524 0.1544  -0.0054 0.0849  237 GLU A CD  
1840 O OE1 . GLU A 237 ? 0.7221 0.5776 0.6618 0.1487  -0.0049 0.0968  237 GLU A OE1 
1841 O OE2 . GLU A 237 ? 0.6858 0.6169 0.6711 0.1754  -0.0166 0.0827  237 GLU A OE2 
1842 N N   . VAL A 238 ? 0.6060 0.5084 0.5883 0.0748  0.0388  0.0625  238 VAL A N   
1843 C CA  . VAL A 238 ? 0.6081 0.4915 0.5897 0.0719  0.0449  0.0531  238 VAL A CA  
1844 C C   . VAL A 238 ? 0.6505 0.5045 0.6254 0.0939  0.0404  0.0509  238 VAL A C   
1845 O O   . VAL A 238 ? 0.6994 0.5167 0.6531 0.1005  0.0339  0.0615  238 VAL A O   
1846 C CB  . VAL A 238 ? 0.6228 0.4817 0.5874 0.0494  0.0494  0.0572  238 VAL A CB  
1847 C CG1 . VAL A 238 ? 0.6362 0.4733 0.5973 0.0459  0.0536  0.0460  238 VAL A CG1 
1848 C CG2 . VAL A 238 ? 0.5899 0.4828 0.5631 0.0328  0.0533  0.0579  238 VAL A CG2 
1849 N N   . SER A 239 ? 0.6394 0.5086 0.6302 0.1064  0.0441  0.0373  239 SER A N   
1850 C CA  . SER A 239 ? 0.6799 0.5289 0.6680 0.1327  0.0402  0.0320  239 SER A CA  
1851 C C   . SER A 239 ? 0.7316 0.5185 0.6904 0.1307  0.0402  0.0318  239 SER A C   
1852 O O   . SER A 239 ? 0.7378 0.5091 0.6865 0.1081  0.0458  0.0295  239 SER A O   
1853 C CB  . SER A 239 ? 0.6645 0.5523 0.6779 0.1448  0.0470  0.0160  239 SER A CB  
1854 O OG  . SER A 239 ? 0.7080 0.5793 0.7197 0.1734  0.0444  0.0084  239 SER A OG  
1855 N N   . ALA A 240 ? 0.7775 0.5277 0.7215 0.1550  0.0323  0.0338  240 ALA A N   
1856 C CA  . ALA A 240 ? 0.8364 0.5197 0.7497 0.1570  0.0310  0.0313  240 ALA A CA  
1857 C C   . ALA A 240 ? 0.8552 0.5387 0.7740 0.1664  0.0385  0.0105  240 ALA A C   
1858 O O   . ALA A 240 ? 0.9001 0.5290 0.7926 0.1622  0.0386  0.0047  240 ALA A O   
1859 C CB  . ALA A 240 ? 0.8803 0.5178 0.7714 0.1838  0.0187  0.0406  240 ALA A CB  
1860 N N   . LYS A 241 ? 0.8229 0.5653 0.7729 0.1773  0.0449  -0.0010 241 LYS A N   
1861 C CA  . LYS A 241 ? 0.8219 0.5726 0.7767 0.1851  0.0543  -0.0207 241 LYS A CA  
1862 C C   . LYS A 241 ? 0.7777 0.5418 0.7323 0.1537  0.0630  -0.0247 241 LYS A C   
1863 O O   . LYS A 241 ? 0.7403 0.5297 0.7039 0.1312  0.0633  -0.0144 241 LYS A O   
1864 C CB  . LYS A 241 ? 0.8058 0.6180 0.7939 0.2088  0.0589  -0.0303 241 LYS A CB  
1865 C CG  . LYS A 241 ? 0.8463 0.6565 0.8398 0.2444  0.0488  -0.0284 241 LYS A CG  
1866 C CD  . LYS A 241 ? 0.8442 0.7258 0.8759 0.2650  0.0547  -0.0404 241 LYS A CD  
1867 C CE  . LYS A 241 ? 0.9039 0.7909 0.9445 0.3039  0.0428  -0.0400 241 LYS A CE  
1868 N NZ  . LYS A 241 ? 0.9206 0.8051 0.9592 0.3001  0.0282  -0.0206 241 LYS A NZ  
1869 N N   . LYS A 242 ? 0.7851 0.5316 0.7273 0.1545  0.0693  -0.0406 242 LYS A N   
1870 C CA  . LYS A 242 ? 0.7490 0.5053 0.6871 0.1280  0.0757  -0.0460 242 LYS A CA  
1871 C C   . LYS A 242 ? 0.7345 0.5118 0.6757 0.1400  0.0862  -0.0648 242 LYS A C   
1872 O O   . LYS A 242 ? 0.7839 0.5425 0.7175 0.1657  0.0878  -0.0773 242 LYS A O   
1873 C CB  . LYS A 242 ? 0.7953 0.4948 0.7035 0.1071  0.0703  -0.0449 242 LYS A CB  
1874 C CG  . LYS A 242 ? 0.8245 0.4980 0.7245 0.0943  0.0618  -0.0260 242 LYS A CG  
1875 C CD  . LYS A 242 ? 0.8924 0.5081 0.7624 0.0721  0.0573  -0.0259 242 LYS A CD  
1876 C CE  . LYS A 242 ? 0.8776 0.5171 0.7516 0.0417  0.0603  -0.0295 242 LYS A CE  
1877 N NZ  . LYS A 242 ? 0.8401 0.5291 0.7363 0.0273  0.0615  -0.0156 242 LYS A NZ  
1878 N N   . ILE A 243 ? 0.6675 0.4827 0.6173 0.1226  0.0935  -0.0668 243 ILE A N   
1879 C CA  . ILE A 243 ? 0.6473 0.4832 0.5950 0.1289  0.1050  -0.0829 243 ILE A CA  
1880 C C   . ILE A 243 ? 0.6859 0.4807 0.6022 0.1161  0.1036  -0.0937 243 ILE A C   
1881 O O   . ILE A 243 ? 0.6904 0.4708 0.5977 0.0916  0.0969  -0.0866 243 ILE A O   
1882 C CB  . ILE A 243 ? 0.5870 0.4798 0.5547 0.1162  0.1129  -0.0779 243 ILE A CB  
1883 C CG1 . ILE A 243 ? 0.5885 0.5008 0.5483 0.1195  0.1261  -0.0928 243 ILE A CG1 
1884 C CG2 . ILE A 243 ? 0.5611 0.4534 0.5255 0.0888  0.1068  -0.0655 243 ILE A CG2 
1885 C CD1 . ILE A 243 ? 0.5431 0.5040 0.5167 0.1054  0.1346  -0.0867 243 ILE A CD1 
1886 N N   . HIS A 244 ? 0.7213 0.4997 0.6214 0.1332  0.1096  -0.1123 244 HIS A N   
1887 C CA  . HIS A 244 ? 0.7733 0.5067 0.6398 0.1237  0.1068  -0.1259 244 HIS A CA  
1888 C C   . HIS A 244 ? 0.7725 0.5356 0.6304 0.1179  0.1172  -0.1375 244 HIS A C   
1889 O O   . HIS A 244 ? 0.7551 0.5519 0.6213 0.1358  0.1300  -0.1460 244 HIS A O   
1890 C CB  . HIS A 244 ? 0.8347 0.5143 0.6793 0.1484  0.1043  -0.1403 244 HIS A CB  
1891 C CG  . HIS A 244 ? 0.8586 0.5002 0.7040 0.1557  0.0933  -0.1278 244 HIS A CG  
1892 N ND1 . HIS A 244 ? 0.8687 0.4697 0.7005 0.1303  0.0821  -0.1158 244 HIS A ND1 
1893 C CD2 . HIS A 244 ? 0.8715 0.5109 0.7281 0.1854  0.0916  -0.1248 244 HIS A CD2 
1894 C CE1 . HIS A 244 ? 0.8947 0.4654 0.7254 0.1430  0.0747  -0.1047 244 HIS A CE1 
1895 N NE2 . HIS A 244 ? 0.8948 0.4869 0.7400 0.1778  0.0791  -0.1100 244 HIS A NE2 
1896 N N   . PHE A 245 ? 0.7966 0.5496 0.6377 0.0926  0.1116  -0.1375 245 PHE A N   
1897 C CA  . PHE A 245 ? 0.8221 0.5943 0.6465 0.0855  0.1183  -0.1477 245 PHE A CA  
1898 C C   . PHE A 245 ? 0.9279 0.6523 0.7151 0.0849  0.1139  -0.1680 245 PHE A C   
1899 O O   . PHE A 245 ? 0.9509 0.6263 0.7255 0.0785  0.1026  -0.1704 245 PHE A O   
1900 C CB  . PHE A 245 ? 0.7550 0.5535 0.5852 0.0599  0.1129  -0.1340 245 PHE A CB  
1901 C CG  . PHE A 245 ? 0.6768 0.5175 0.5383 0.0586  0.1164  -0.1157 245 PHE A CG  
1902 C CD1 . PHE A 245 ? 0.6466 0.5278 0.5147 0.0616  0.1283  -0.1135 245 PHE A CD1 
1903 C CD2 . PHE A 245 ? 0.6434 0.4815 0.5248 0.0525  0.1079  -0.1007 245 PHE A CD2 
1904 C CE1 . PHE A 245 ? 0.5990 0.5140 0.4933 0.0579  0.1303  -0.0978 245 PHE A CE1 
1905 C CE2 . PHE A 245 ? 0.5966 0.4705 0.5034 0.0513  0.1101  -0.0859 245 PHE A CE2 
1906 C CZ  . PHE A 245 ? 0.5756 0.4865 0.4892 0.0537  0.1206  -0.0849 245 PHE A CZ  
1907 N N   . ALA A 246 ? 0.9995 0.7364 0.7661 0.0899  0.1231  -0.1827 246 ALA A N   
1908 C CA  . ALA A 246 ? 1.1055 0.8014 0.8325 0.0874  0.1187  -0.2040 246 ALA A CA  
1909 C C   . ALA A 246 ? 1.1009 0.8113 0.8133 0.0615  0.1115  -0.2015 246 ALA A C   
1910 O O   . ALA A 246 ? 1.0738 0.8259 0.7872 0.0600  0.1202  -0.1963 246 ALA A O   
1911 C CB  . ALA A 246 ? 1.1713 0.8700 0.8802 0.1145  0.1341  -0.2249 246 ALA A CB  
1912 N N   . ARG A 247 ? 1.1465 0.8233 0.8449 0.0407  0.0952  -0.2045 247 ARG A N   
1913 C CA  . ARG A 247 ? 1.1648 0.8571 0.8513 0.0173  0.0849  -0.2033 247 ARG A CA  
1914 C C   . ARG A 247 ? 1.2135 0.8724 0.8566 0.0144  0.0795  -0.2281 247 ARG A C   
1915 O O   . ARG A 247 ? 1.2647 0.8732 0.8890 0.0197  0.0765  -0.2442 247 ARG A O   
1916 C CB  . ARG A 247 ? 1.1751 0.8671 0.8820 -0.0072 0.0695  -0.1889 247 ARG A CB  
1917 C CG  . ARG A 247 ? 1.2563 0.8949 0.9500 -0.0208 0.0575  -0.1987 247 ARG A CG  
1918 C CD  . ARG A 247 ? 1.2648 0.9145 0.9808 -0.0480 0.0449  -0.1836 247 ARG A CD  
1919 N NE  . ARG A 247 ? 1.2603 0.9480 0.9767 -0.0655 0.0353  -0.1827 247 ARG A NE  
1920 C CZ  . ARG A 247 ? 1.2928 0.9679 0.9893 -0.0860 0.0214  -0.1967 247 ARG A CZ  
1921 N NH1 . ARG A 247 ? 1.3542 0.9744 1.0266 -0.0941 0.0161  -0.2130 247 ARG A NH1 
1922 N NH2 . ARG A 247 ? 1.2674 0.9832 0.9669 -0.0980 0.0114  -0.1949 247 ARG A NH2 
1923 N N   . PHE A 248 ? 1.1995 0.8835 0.8233 0.0068  0.0777  -0.2313 248 PHE A N   
1924 C CA  . PHE A 248 ? 1.2512 0.9092 0.8311 0.0015  0.0703  -0.2545 248 PHE A CA  
1925 C C   . PHE A 248 ? 1.2361 0.9086 0.8094 -0.0245 0.0509  -0.2517 248 PHE A C   
1926 O O   . PHE A 248 ? 1.2906 0.9428 0.8280 -0.0329 0.0406  -0.2711 248 PHE A O   
1927 C CB  . PHE A 248 ? 1.2844 0.9584 0.8364 0.0212  0.0873  -0.2654 248 PHE A CB  
1928 C CG  . PHE A 248 ? 1.3110 0.9775 0.8687 0.0493  0.1067  -0.2727 248 PHE A CG  
1929 C CD1 . PHE A 248 ? 1.3805 1.0003 0.9090 0.0644  0.1085  -0.2985 248 PHE A CD1 
1930 C CD2 . PHE A 248 ? 1.2672 0.9742 0.8594 0.0615  0.1222  -0.2551 248 PHE A CD2 
1931 C CE1 . PHE A 248 ? 1.3942 1.0111 0.9295 0.0945  0.1256  -0.3064 248 PHE A CE1 
1932 C CE2 . PHE A 248 ? 1.2791 0.9877 0.8807 0.0885  0.1389  -0.2627 248 PHE A CE2 
1933 C CZ  . PHE A 248 ? 1.3409 1.0061 0.9149 0.1067  0.1407  -0.2884 248 PHE A CZ  
1934 N N   . ARG A 249 ? 1.1657 0.8742 0.7724 -0.0360 0.0449  -0.2296 249 ARG A N   
1935 C CA  . ARG A 249 ? 1.1450 0.8784 0.7501 -0.0558 0.0267  -0.2258 249 ARG A CA  
1936 C C   . ARG A 249 ? 1.0717 0.8335 0.7213 -0.0662 0.0213  -0.2037 249 ARG A C   
1937 O O   . ARG A 249 ? 1.0354 0.7927 0.7121 -0.0599 0.0308  -0.1924 249 ARG A O   
1938 C CB  . ARG A 249 ? 1.1497 0.9116 0.7297 -0.0477 0.0295  -0.2237 249 ARG A CB  
1939 C CG  . ARG A 249 ? 1.1110 0.9023 0.7097 -0.0330 0.0463  -0.2032 249 ARG A CG  
1940 C CD  . ARG A 249 ? 1.1275 0.9393 0.6950 -0.0275 0.0497  -0.1995 249 ARG A CD  
1941 N NE  . ARG A 249 ? 1.0859 0.9234 0.6721 -0.0192 0.0636  -0.1780 249 ARG A NE  
1942 C CZ  . ARG A 249 ? 1.0871 0.9401 0.6489 -0.0153 0.0698  -0.1689 249 ARG A CZ  
1943 N NH1 . ARG A 249 ? 1.1231 0.9706 0.6395 -0.0168 0.0632  -0.1790 249 ARG A NH1 
1944 N NH2 . ARG A 249 ? 1.0549 0.9265 0.6346 -0.0112 0.0819  -0.1495 249 ARG A NH2 
1945 N N   . SER A 250 ? 1.0408 0.8342 0.6967 -0.0802 0.0056  -0.1982 250 SER A N   
1946 C CA  . SER A 250 ? 0.9561 0.7825 0.6521 -0.0887 -0.0001 -0.1793 250 SER A CA  
1947 C C   . SER A 250 ? 0.8904 0.7514 0.5938 -0.0737 0.0059  -0.1617 250 SER A C   
1948 O O   . SER A 250 ? 0.9011 0.7781 0.5820 -0.0703 -0.0011 -0.1626 250 SER A O   
1949 C CB  . SER A 250 ? 0.9525 0.7977 0.6551 -0.1120 -0.0215 -0.1850 250 SER A CB  
1950 O OG  . SER A 250 ? 0.8918 0.7749 0.6337 -0.1178 -0.0255 -0.1680 250 SER A OG  
1951 N N   . PHE A 251 ? 0.8280 0.6967 0.5595 -0.0652 0.0178  -0.1457 251 PHE A N   
1952 C CA  . PHE A 251 ? 0.7771 0.6742 0.5186 -0.0543 0.0222  -0.1280 251 PHE A CA  
1953 C C   . PHE A 251 ? 0.7424 0.6547 0.5236 -0.0569 0.0228  -0.1134 251 PHE A C   
1954 O O   . PHE A 251 ? 0.7322 0.6369 0.5287 -0.0491 0.0358  -0.1061 251 PHE A O   
1955 C CB  . PHE A 251 ? 0.7697 0.6585 0.4954 -0.0387 0.0406  -0.1256 251 PHE A CB  
1956 C CG  . PHE A 251 ? 0.7597 0.6690 0.4784 -0.0318 0.0426  -0.1107 251 PHE A CG  
1957 C CD1 . PHE A 251 ? 0.7358 0.6659 0.4613 -0.0346 0.0275  -0.1009 251 PHE A CD1 
1958 C CD2 . PHE A 251 ? 0.7848 0.6920 0.4892 -0.0224 0.0597  -0.1065 251 PHE A CD2 
1959 C CE1 . PHE A 251 ? 0.7330 0.6724 0.4467 -0.0269 0.0281  -0.0869 251 PHE A CE1 
1960 C CE2 . PHE A 251 ? 0.7837 0.7023 0.4772 -0.0193 0.0615  -0.0916 251 PHE A CE2 
1961 C CZ  . PHE A 251 ? 0.7583 0.6885 0.4542 -0.0209 0.0451  -0.0816 251 PHE A CZ  
1962 N N   . PRO A 252 ? 0.7268 0.6643 0.5256 -0.0674 0.0087  -0.1098 252 PRO A N   
1963 C CA  . PRO A 252 ? 0.6907 0.6441 0.5251 -0.0712 0.0100  -0.0977 252 PRO A CA  
1964 C C   . PRO A 252 ? 0.6562 0.6202 0.5018 -0.0557 0.0197  -0.0820 252 PRO A C   
1965 O O   . PRO A 252 ? 0.6537 0.6210 0.4824 -0.0448 0.0215  -0.0779 252 PRO A O   
1966 C CB  . PRO A 252 ? 0.6855 0.6742 0.5332 -0.0826 -0.0069 -0.0988 252 PRO A CB  
1967 C CG  . PRO A 252 ? 0.7236 0.7050 0.5447 -0.0913 -0.0184 -0.1151 252 PRO A CG  
1968 C CD  . PRO A 252 ? 0.7425 0.6983 0.5297 -0.0766 -0.0095 -0.1184 252 PRO A CD  
1969 N N   . PHE A 253 ? 0.6303 0.5968 0.5019 -0.0565 0.0255  -0.0731 253 PHE A N   
1970 C CA  . PHE A 253 ? 0.5892 0.5643 0.4725 -0.0440 0.0336  -0.0596 253 PHE A CA  
1971 C C   . PHE A 253 ? 0.5554 0.5572 0.4408 -0.0381 0.0246  -0.0523 253 PHE A C   
1972 O O   . PHE A 253 ? 0.5269 0.5262 0.4004 -0.0273 0.0280  -0.0455 253 PHE A O   
1973 C CB  . PHE A 253 ? 0.5862 0.5592 0.4939 -0.0465 0.0393  -0.0525 253 PHE A CB  
1974 C CG  . PHE A 253 ? 0.5737 0.5584 0.4946 -0.0358 0.0448  -0.0400 253 PHE A CG  
1975 C CD1 . PHE A 253 ? 0.5737 0.5471 0.4902 -0.0261 0.0552  -0.0372 253 PHE A CD1 
1976 C CD2 . PHE A 253 ? 0.5662 0.5751 0.5039 -0.0358 0.0396  -0.0325 253 PHE A CD2 
1977 C CE1 . PHE A 253 ? 0.5653 0.5482 0.4931 -0.0191 0.0588  -0.0269 253 PHE A CE1 
1978 C CE2 . PHE A 253 ? 0.5685 0.5835 0.5145 -0.0261 0.0436  -0.0229 253 PHE A CE2 
1979 C CZ  . PHE A 253 ? 0.5697 0.5700 0.5102 -0.0191 0.0526  -0.0201 253 PHE A CZ  
1980 N N   . TRP A 254 ? 0.5602 0.5877 0.4601 -0.0449 0.0131  -0.0536 254 TRP A N   
1981 C CA  . TRP A 254 ? 0.5471 0.6013 0.4491 -0.0348 0.0029  -0.0483 254 TRP A CA  
1982 C C   . TRP A 254 ? 0.5612 0.6094 0.4319 -0.0277 -0.0053 -0.0517 254 TRP A C   
1983 O O   . TRP A 254 ? 0.5558 0.6056 0.4147 -0.0138 -0.0093 -0.0438 254 TRP A O   
1984 C CB  . TRP A 254 ? 0.5297 0.6212 0.4566 -0.0432 -0.0074 -0.0513 254 TRP A CB  
1985 C CG  . TRP A 254 ? 0.4996 0.5973 0.4526 -0.0520 0.0012  -0.0467 254 TRP A CG  
1986 C CD1 . TRP A 254 ? 0.5005 0.6003 0.4661 -0.0723 0.0021  -0.0513 254 TRP A CD1 
1987 C CD2 . TRP A 254 ? 0.4756 0.5746 0.4411 -0.0422 0.0096  -0.0361 254 TRP A CD2 
1988 N NE1 . TRP A 254 ? 0.4861 0.5888 0.4699 -0.0750 0.0112  -0.0427 254 TRP A NE1 
1989 C CE2 . TRP A 254 ? 0.4730 0.5770 0.4574 -0.0559 0.0156  -0.0341 254 TRP A CE2 
1990 C CE3 . TRP A 254 ? 0.4640 0.5575 0.4234 -0.0245 0.0121  -0.0282 254 TRP A CE3 
1991 C CZ2 . TRP A 254 ? 0.4616 0.5684 0.4585 -0.0507 0.0237  -0.0249 254 TRP A CZ2 
1992 C CZ3 . TRP A 254 ? 0.4488 0.5445 0.4224 -0.0202 0.0195  -0.0206 254 TRP A CZ3 
1993 C CH2 . TRP A 254 ? 0.4497 0.5536 0.4416 -0.0323 0.0252  -0.0192 254 TRP A CH2 
1994 N N   . ARG A 255 ? 0.5843 0.6216 0.4373 -0.0370 -0.0084 -0.0633 255 ARG A N   
1995 C CA  . ARG A 255 ? 0.6187 0.6456 0.4355 -0.0305 -0.0140 -0.0663 255 ARG A CA  
1996 C C   . ARG A 255 ? 0.6332 0.6343 0.4297 -0.0213 0.0007  -0.0577 255 ARG A C   
1997 O O   . ARG A 255 ? 0.6617 0.6568 0.4313 -0.0122 -0.0028 -0.0511 255 ARG A O   
1998 C CB  . ARG A 255 ? 0.6432 0.6600 0.4430 -0.0431 -0.0185 -0.0826 255 ARG A CB  
1999 C CG  . ARG A 255 ? 0.6770 0.6741 0.4333 -0.0372 -0.0180 -0.0869 255 ARG A CG  
2000 C CD  . ARG A 255 ? 0.7050 0.7182 0.4418 -0.0393 -0.0388 -0.0957 255 ARG A CD  
2001 N NE  . ARG A 255 ? 0.7409 0.7320 0.4310 -0.0350 -0.0370 -0.1006 255 ARG A NE  
2002 C CZ  . ARG A 255 ? 0.7460 0.7298 0.4063 -0.0221 -0.0364 -0.0891 255 ARG A CZ  
2003 N NH1 . ARG A 255 ? 0.7389 0.7318 0.4112 -0.0112 -0.0389 -0.0730 255 ARG A NH1 
2004 N NH2 . ARG A 255 ? 0.7609 0.7253 0.3760 -0.0204 -0.0331 -0.0937 255 ARG A NH2 
2005 N N   . ARG A 256 ? 0.6176 0.6041 0.4262 -0.0241 0.0168  -0.0570 256 ARG A N   
2006 C CA  . ARG A 256 ? 0.6219 0.5929 0.4184 -0.0178 0.0317  -0.0492 256 ARG A CA  
2007 C C   . ARG A 256 ? 0.6125 0.5890 0.4189 -0.0106 0.0313  -0.0345 256 ARG A C   
2008 O O   . ARG A 256 ? 0.6350 0.5991 0.4226 -0.0072 0.0382  -0.0262 256 ARG A O   
2009 C CB  . ARG A 256 ? 0.6231 0.5831 0.4333 -0.0204 0.0470  -0.0542 256 ARG A CB  
2010 C CG  . ARG A 256 ? 0.6660 0.6159 0.4596 -0.0163 0.0632  -0.0528 256 ARG A CG  
2011 C CD  . ARG A 256 ? 0.7006 0.6406 0.4993 -0.0153 0.0749  -0.0645 256 ARG A CD  
2012 N NE  . ARG A 256 ? 0.6847 0.6264 0.5163 -0.0138 0.0782  -0.0614 256 ARG A NE  
2013 C CZ  . ARG A 256 ? 0.6782 0.6117 0.5230 -0.0178 0.0718  -0.0669 256 ARG A CZ  
2014 N NH1 . ARG A 256 ? 0.6907 0.6155 0.5217 -0.0255 0.0617  -0.0772 256 ARG A NH1 
2015 N NH2 . ARG A 256 ? 0.6592 0.5919 0.5289 -0.0156 0.0750  -0.0618 256 ARG A NH2 
2016 N N   . VAL A 257 ? 0.5826 0.5764 0.4161 -0.0094 0.0237  -0.0316 257 VAL A N   
2017 C CA  . VAL A 257 ? 0.5649 0.5616 0.4044 -0.0004 0.0214  -0.0201 257 VAL A CA  
2018 C C   . VAL A 257 ? 0.5972 0.5923 0.4108 0.0097  0.0077  -0.0160 257 VAL A C   
2019 O O   . VAL A 257 ? 0.6201 0.5978 0.4164 0.0170  0.0083  -0.0058 257 VAL A O   
2020 C CB  . VAL A 257 ? 0.5317 0.5498 0.4056 -0.0004 0.0184  -0.0197 257 VAL A CB  
2021 C CG1 . VAL A 257 ? 0.5164 0.5377 0.3926 0.0118  0.0135  -0.0109 257 VAL A CG1 
2022 C CG2 . VAL A 257 ? 0.5178 0.5304 0.4114 -0.0079 0.0312  -0.0204 257 VAL A CG2 
2023 N N   . HIS A 258 ? 0.6090 0.6204 0.4177 0.0100  -0.0060 -0.0238 258 HIS A N   
2024 C CA  . HIS A 258 ? 0.6419 0.6547 0.4258 0.0228  -0.0222 -0.0203 258 HIS A CA  
2025 C C   . HIS A 258 ? 0.6942 0.6737 0.4335 0.0247  -0.0179 -0.0132 258 HIS A C   
2026 O O   . HIS A 258 ? 0.7339 0.6956 0.4493 0.0363  -0.0242 -0.0023 258 HIS A O   
2027 C CB  . HIS A 258 ? 0.6542 0.6960 0.4431 0.0202  -0.0382 -0.0320 258 HIS A CB  
2028 C CG  . HIS A 258 ? 0.6952 0.7356 0.4503 0.0329  -0.0556 -0.0304 258 HIS A CG  
2029 N ND1 . HIS A 258 ? 0.7380 0.7582 0.4536 0.0292  -0.0564 -0.0328 258 HIS A ND1 
2030 C CD2 . HIS A 258 ? 0.7125 0.7691 0.4651 0.0514  -0.0736 -0.0265 258 HIS A CD2 
2031 C CE1 . HIS A 258 ? 0.7673 0.7894 0.4556 0.0438  -0.0750 -0.0293 258 HIS A CE1 
2032 N NE2 . HIS A 258 ? 0.7547 0.7986 0.4657 0.0586  -0.0863 -0.0256 258 HIS A NE2 
2033 N N   . ASP A 259 ? 0.6973 0.6657 0.4220 0.0134  -0.0066 -0.0193 259 ASP A N   
2034 C CA  . ASP A 259 ? 0.7418 0.6834 0.4219 0.0130  -0.0005 -0.0131 259 ASP A CA  
2035 C C   . ASP A 259 ? 0.7479 0.6676 0.4224 0.0116  0.0136  0.0007  259 ASP A C   
2036 O O   . ASP A 259 ? 0.7932 0.6879 0.4284 0.0126  0.0149  0.0114  259 ASP A O   
2037 C CB  . ASP A 259 ? 0.7597 0.6987 0.4276 0.0027  0.0104  -0.0252 259 ASP A CB  
2038 C CG  . ASP A 259 ? 0.7881 0.7414 0.4498 0.0015  -0.0055 -0.0394 259 ASP A CG  
2039 O OD1 . ASP A 259 ? 0.7890 0.7601 0.4578 0.0085  -0.0250 -0.0390 259 ASP A OD1 
2040 O OD2 . ASP A 259 ? 0.8137 0.7621 0.4636 -0.0061 0.0012  -0.0520 259 ASP A OD2 
2041 N N   . SER A 260 ? 0.7041 0.6314 0.4150 0.0079  0.0234  0.0011  260 SER A N   
2042 C CA  . SER A 260 ? 0.6963 0.6064 0.4049 0.0032  0.0365  0.0121  260 SER A CA  
2043 C C   . SER A 260 ? 0.6997 0.5946 0.4027 0.0126  0.0257  0.0233  260 SER A C   
2044 O O   . SER A 260 ? 0.7131 0.5808 0.3926 0.0084  0.0312  0.0348  260 SER A O   
2045 C CB  . SER A 260 ? 0.6549 0.5800 0.4023 -0.0039 0.0506  0.0070  260 SER A CB  
2046 O OG  . SER A 260 ? 0.6543 0.5872 0.4031 -0.0097 0.0615  -0.0036 260 SER A OG  
2047 N N   . PHE A 261 ? 0.6901 0.6014 0.4129 0.0248  0.0108  0.0198  261 PHE A N   
2048 C CA  . PHE A 261 ? 0.6969 0.5955 0.4180 0.0374  0.0011  0.0274  261 PHE A CA  
2049 C C   . PHE A 261 ? 0.7296 0.6257 0.4287 0.0564  -0.0198 0.0291  261 PHE A C   
2050 O O   . PHE A 261 ? 0.7454 0.6145 0.4240 0.0689  -0.0281 0.0378  261 PHE A O   
2051 C CB  . PHE A 261 ? 0.6394 0.5624 0.4044 0.0394  0.0027  0.0220  261 PHE A CB  
2052 C CG  . PHE A 261 ? 0.5915 0.5158 0.3776 0.0248  0.0201  0.0216  261 PHE A CG  
2053 C CD1 . PHE A 261 ? 0.5884 0.4886 0.3655 0.0192  0.0276  0.0298  261 PHE A CD1 
2054 C CD2 . PHE A 261 ? 0.5591 0.5075 0.3730 0.0167  0.0277  0.0128  261 PHE A CD2 
2055 C CE1 . PHE A 261 ? 0.5639 0.4717 0.3631 0.0069  0.0417  0.0286  261 PHE A CE1 
2056 C CE2 . PHE A 261 ? 0.5336 0.4840 0.3663 0.0073  0.0416  0.0124  261 PHE A CE2 
2057 C CZ  . PHE A 261 ? 0.5312 0.4652 0.3584 0.0029  0.0484  0.0200  261 PHE A CZ  
2058 N N   . ILE A 262 ? 0.7456 0.6682 0.4477 0.0596  -0.0299 0.0204  262 ILE A N   
2059 C CA  . ILE A 262 ? 0.8038 0.7317 0.4878 0.0795  -0.0519 0.0208  262 ILE A CA  
2060 C C   . ILE A 262 ? 0.8883 0.7847 0.5188 0.0797  -0.0563 0.0283  262 ILE A C   
2061 O O   . ILE A 262 ? 0.9390 0.8003 0.5318 0.0931  -0.0658 0.0403  262 ILE A O   
2062 C CB  . ILE A 262 ? 0.7820 0.7619 0.5001 0.0816  -0.0629 0.0067  262 ILE A CB  
2063 C CG1 . ILE A 262 ? 0.7335 0.7425 0.5013 0.0743  -0.0532 0.0004  262 ILE A CG1 
2064 C CG2 . ILE A 262 ? 0.8037 0.7997 0.5133 0.1062  -0.0868 0.0064  262 ILE A CG2 
2065 C CD1 . ILE A 262 ? 0.7233 0.7293 0.5026 0.0899  -0.0551 0.0055  262 ILE A CD1 
2066 N N   . GLU A 263 ? 0.9220 0.8270 0.5451 0.0653  -0.0496 0.0214  263 GLU A N   
2067 C CA  . GLU A 263 ? 0.9910 0.8687 0.5607 0.0633  -0.0511 0.0275  263 GLU A CA  
2068 C C   . GLU A 263 ? 0.9866 0.8730 0.5554 0.0444  -0.0355 0.0174  263 GLU A C   
2069 O O   . GLU A 263 ? 1.0033 0.9062 0.5626 0.0440  -0.0448 0.0067  263 GLU A O   
2070 C CB  . GLU A 263 ? 1.0515 0.9380 0.5979 0.0825  -0.0777 0.0265  263 GLU A CB  
2071 C CG  . GLU A 263 ? 1.0379 0.9781 0.6283 0.0879  -0.0921 0.0105  263 GLU A CG  
2072 C CD  . GLU A 263 ? 1.0964 1.0519 0.6674 0.1091  -0.1203 0.0094  263 GLU A CD  
2073 O OE1 . GLU A 263 ? 1.1522 1.0790 0.6700 0.1144  -0.1282 0.0169  263 GLU A OE1 
2074 O OE2 . GLU A 263 ? 1.0862 1.0848 0.6947 0.1209  -0.1346 0.0011  263 GLU A OE2 
# 
