data_8QGM
# 
_entry.id   8QGM 
# 
_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   8QGM         pdb_00008qgm 10.2210/pdb8qgm/pdb 
WWPDB D_1292133182 ?            ?                   
# 
_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                        8QGM 
_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 
;8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-amino]prop-1-ynyl]-6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-[(dimethylsulfamoylamino)methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purine
;
689.703   1  ?        ? ? ? 
4 water       nat water 18.015    85 ?        ? ? ? 
# 
_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 
;8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-amino]prop-1-ynyl]-6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-[(dimethylsulfamoylamino)methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purine
;
V0I 
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 
V0I non-polymer         . 
;8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-amino]prop-1-ynyl]-6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-[(dimethylsulfamoylamino)methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purine
;
? 'C26 H35 N13 O8 S' 689.703 
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 264 264 264 ASP ASP A . n 
A 1 265 LEU 265 265 ?   ?   ?   A . n 
A 1 266 GLU 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 HIS 269 269 ?   ?   ?   A . n 
A 1 270 HIS 270 270 ?   ?   ?   A . n 
A 1 271 HIS 271 271 ?   ?   ?   A . n 
A 1 272 HIS 272 272 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V0I 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V0I 
_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 V0I 1  302 1   V0I SNC A . 
D 4 HOH 1  401 5   HOH HOH A . 
D 4 HOH 2  402 101 HOH HOH A . 
D 4 HOH 3  403 80  HOH HOH A . 
D 4 HOH 4  404 105 HOH HOH A . 
D 4 HOH 5  405 60  HOH HOH A . 
D 4 HOH 6  406 74  HOH HOH A . 
D 4 HOH 7  407 55  HOH HOH A . 
D 4 HOH 8  408 6   HOH HOH A . 
D 4 HOH 9  409 4   HOH HOH A . 
D 4 HOH 10 410 109 HOH HOH A . 
D 4 HOH 11 411 53  HOH HOH A . 
D 4 HOH 12 412 17  HOH HOH A . 
D 4 HOH 13 413 93  HOH HOH A . 
D 4 HOH 14 414 7   HOH HOH A . 
D 4 HOH 15 415 42  HOH HOH A . 
D 4 HOH 16 416 33  HOH HOH A . 
D 4 HOH 17 417 30  HOH HOH A . 
D 4 HOH 18 418 37  HOH HOH A . 
D 4 HOH 19 419 44  HOH HOH A . 
D 4 HOH 20 420 18  HOH HOH A . 
D 4 HOH 21 421 1   HOH HOH A . 
D 4 HOH 22 422 25  HOH HOH A . 
D 4 HOH 23 423 45  HOH HOH A . 
D 4 HOH 24 424 39  HOH HOH A . 
D 4 HOH 25 425 36  HOH HOH A . 
D 4 HOH 26 426 23  HOH HOH A . 
D 4 HOH 27 427 22  HOH HOH A . 
D 4 HOH 28 428 38  HOH HOH A . 
D 4 HOH 29 429 72  HOH HOH A . 
D 4 HOH 30 430 8   HOH HOH A . 
D 4 HOH 31 431 12  HOH HOH A . 
D 4 HOH 32 432 10  HOH HOH A . 
D 4 HOH 33 433 2   HOH HOH A . 
D 4 HOH 34 434 92  HOH HOH A . 
D 4 HOH 35 435 70  HOH HOH A . 
D 4 HOH 36 436 27  HOH HOH A . 
D 4 HOH 37 437 32  HOH HOH A . 
D 4 HOH 38 438 57  HOH HOH A . 
D 4 HOH 39 439 13  HOH HOH A . 
D 4 HOH 40 440 14  HOH HOH A . 
D 4 HOH 41 441 3   HOH HOH A . 
D 4 HOH 42 442 24  HOH HOH A . 
D 4 HOH 43 443 56  HOH HOH A . 
D 4 HOH 44 444 51  HOH HOH A . 
D 4 HOH 45 445 48  HOH HOH A . 
D 4 HOH 46 446 59  HOH HOH A . 
D 4 HOH 47 447 91  HOH HOH A . 
D 4 HOH 48 448 68  HOH HOH A . 
D 4 HOH 49 449 29  HOH HOH A . 
D 4 HOH 50 450 63  HOH HOH A . 
D 4 HOH 51 451 11  HOH HOH A . 
D 4 HOH 52 452 26  HOH HOH A . 
D 4 HOH 53 453 46  HOH HOH A . 
D 4 HOH 54 454 87  HOH HOH A . 
D 4 HOH 55 455 58  HOH HOH A . 
D 4 HOH 56 456 69  HOH HOH A . 
D 4 HOH 57 457 82  HOH HOH A . 
D 4 HOH 58 458 66  HOH HOH A . 
D 4 HOH 59 459 16  HOH HOH A . 
D 4 HOH 60 460 9   HOH HOH A . 
D 4 HOH 61 461 62  HOH HOH A . 
D 4 HOH 62 462 21  HOH HOH A . 
D 4 HOH 63 463 19  HOH HOH A . 
D 4 HOH 64 464 34  HOH HOH A . 
D 4 HOH 65 465 76  HOH HOH A . 
D 4 HOH 66 466 78  HOH HOH A . 
D 4 HOH 67 467 111 HOH HOH A . 
D 4 HOH 68 468 71  HOH HOH A . 
D 4 HOH 69 469 35  HOH HOH A . 
D 4 HOH 70 470 83  HOH HOH A . 
D 4 HOH 71 471 49  HOH HOH A . 
D 4 HOH 72 472 28  HOH HOH A . 
D 4 HOH 73 473 110 HOH HOH A . 
D 4 HOH 74 474 106 HOH HOH A . 
D 4 HOH 75 475 96  HOH HOH A . 
D 4 HOH 76 476 99  HOH HOH A . 
D 4 HOH 77 477 40  HOH HOH A . 
D 4 HOH 78 478 15  HOH HOH A . 
D 4 HOH 79 479 86  HOH HOH A . 
D 4 HOH 80 480 98  HOH HOH A . 
D 4 HOH 81 481 52  HOH HOH A . 
D 4 HOH 82 482 90  HOH HOH A . 
D 4 HOH 83 483 89  HOH HOH A . 
D 4 HOH 84 484 50  HOH HOH A . 
D 4 HOH 85 485 75  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
6  1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
7  1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
8  1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
9  1 Y 1 A LYS 108 ? CG  ? A LYS 108 CG  
10 1 Y 1 A LYS 108 ? CD  ? A LYS 108 CD  
11 1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
12 1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
13 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
14 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
15 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
16 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  ? ? ? 1.19.1_4122 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QGM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.850 
_cell.length_a_esd                 ? 
_cell.length_b                     74.354 
_cell.length_b_esd                 ? 
_cell.length_c                     118.435 
_cell.length_c_esd                 ? 
_cell.volume                       553464.338 
_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                         8QGM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QGM 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.80 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.965459 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965459 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          26.12 
_reflns.entry_id                                       8QGM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.333 
_reflns.d_resolution_low                               62.973 
_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                                     56722 
_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                           91.58 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.046 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.040 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.657 
_reflns_shell.d_res_low                                     1.685 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6271 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1698 
_reflns_shell.percent_possible_obs                          9.2 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.901 
_reflns_shell.pdbx_Rpim_I_all                               0.443 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.777 
_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                               38.88 
_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                                 8QGM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.66 
_refine.ls_d_res_low                             62.97 
_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                     56722 
_refine.ls_number_reflns_R_free                  2863 
_refine.ls_number_reflns_R_work                  53859 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.98 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1611 
_refine.ls_R_factor_R_free                       0.2013 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1588 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.8383 
_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                            0.2118 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        62.97 
_refine_hist.number_atoms_solvent             85 
_refine_hist.number_atoms_total               2220 
_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        2074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         61 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0104  ? 2203 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1517  ? 2990 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0719  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0072  ? 410  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.5889 ? 825  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.66 1.69  . . 164 2937 98.20 . . . . 0.3449 . . . . . . . . . . . 0.3835 
'X-RAY DIFFRACTION' 1.69 1.72  . . 129 2978 97.92 . . . . 0.3123 . . . . . . . . . . . 0.3480 
'X-RAY DIFFRACTION' 1.72 1.75  . . 176 2984 97.59 . . . . 0.2752 . . . . . . . . . . . 0.3128 
'X-RAY DIFFRACTION' 1.75 1.78  . . 157 2954 98.05 . . . . 0.2431 . . . . . . . . . . . 0.2674 
'X-RAY DIFFRACTION' 1.78 1.82  . . 138 2972 98.14 . . . . 0.2132 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 1.82 1.87  . . 146 2919 95.01 . . . . 0.1988 . . . . . . . . . . . 0.2673 
'X-RAY DIFFRACTION' 1.87 1.87  . . 2   13   19.48 . . . . 0.1732 . . . . . . . . . . . 0.0924 
'X-RAY DIFFRACTION' 1.94 1.96  . . 64  1562 95.14 . . . . 0.1935 . . . . . . . . . . . 0.2449 
'X-RAY DIFFRACTION' 1.96 2.02  . . 166 2955 96.84 . . . . 0.1785 . . . . . . . . . . . 0.2612 
'X-RAY DIFFRACTION' 2.02 2.09  . . 149 2857 95.95 . . . . 0.1834 . . . . . . . . . . . 0.2315 
'X-RAY DIFFRACTION' 2.09 2.16  . . 168 2891 96.13 . . . . 0.1530 . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 2.16 2.25  . . 164 2834 93.72 . . . . 0.1606 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 2.25 2.35  . . 149 2926 96.30 . . . . 0.1458 . . . . . . . . . . . 0.2268 
'X-RAY DIFFRACTION' 2.35 2.47  . . 140 2931 96.75 . . . . 0.1625 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 2.48 2.63  . . 159 2938 97.21 . . . . 0.1591 . . . . . . . . . . . 0.1762 
'X-RAY DIFFRACTION' 2.63 2.83  . . 142 2899 95.60 . . . . 0.1578 . . . . . . . . . . . 0.2381 
'X-RAY DIFFRACTION' 2.83 3.12  . . 140 2874 94.45 . . . . 0.1638 . . . . . . . . . . . 0.1835 
'X-RAY DIFFRACTION' 3.12 3.57  . . 157 2811 93.45 . . . . 0.1430 . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 3.57 4.49  . . 145 2765 90.60 . . . . 0.1269 . . . . . . . . . . . 0.1461 
'X-RAY DIFFRACTION' 4.50 62.97 . . 208 2859 96.17 . . . . 0.1438 . . . . . . . . . . . 0.1931 
# 
_struct.entry_id                     8QGM 
_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        8QGM 
_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              8QGM 
_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 8QGM LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGM GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGM HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGM HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGM HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGM HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGM HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGM HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12810 ? 
1 MORE         -46   ? 
1 'SSA (A^2)'  40110 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 62.8500000000 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 62.8500000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 GLU A 56  ? ILE A 62  ? GLU A 56  ILE A 62  5 ? 7  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 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 GLU A 115 ? ALA A 120 ? GLU A 115 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 ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
AA2 4 5 O GLN A 210 ? O GLN A 210 N ASP A 136 ? N ASP A 136 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 1 2 O LEU A 199 ? O LEU A 199 N LEU A 181 ? N LEU A 181 
AA3 2 3 O THR A 182 ? O THR A 182 N CYS A 153 ? N CYS A 153 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N THR A 125 ? N THR A 125 O SER A 220 ? O SER A 220 
AA3 5 6 N PHE A 217 ? N PHE A 217 O HIS A 228 ? O HIS A 228 
# 
_pdbx_entry_details.entry_id                   8QGM 
_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 LEU A 72  ? ? -58.58  102.26  
2 1 GLU A 94  ? ? 57.83   15.20   
3 1 TYR A 109 ? ? -118.13 -164.34 
4 1 ASN A 122 ? ? -99.17  -69.55  
5 1 ALA A 162 ? ? -101.87 -128.51 
6 1 HIS A 204 ? ? 82.46   -8.21   
7 1 ASN A 213 ? ? -127.93 -88.61  
8 1 ASP A 222 ? ? 55.18   -135.79 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A 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 LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
V0I N    N N N 393 
V0I C    C N N 394 
V0I O    O N N 395 
V0I C1   C N N 396 
V0I C10  C Y N 397 
V0I C11  C N N 398 
V0I C12  C N N 399 
V0I C13  C N N 400 
V0I C14  C Y N 401 
V0I C15  C Y N 402 
V0I C16  C Y N 403 
V0I C17  C N R 404 
V0I C18  C N R 405 
V0I C19  C N S 406 
V0I C2   C N R 407 
V0I C20  C N R 408 
V0I C21  C N N 409 
V0I C22  C N N 410 
V0I C23  C N N 411 
V0I C24  C Y N 412 
V0I C25  C Y N 413 
V0I C3   C N R 414 
V0I C4   C N R 415 
V0I C5   C N S 416 
V0I C6   C Y N 417 
V0I C7   C Y N 418 
V0I C8   C Y N 419 
V0I C9   C Y N 420 
V0I N1   N Y N 421 
V0I N10  N Y N 422 
V0I N11  N Y N 423 
V0I N12  N N N 424 
V0I N2   N Y N 425 
V0I N3   N Y N 426 
V0I N4   N Y N 427 
V0I N5   N N N 428 
V0I N6   N Y N 429 
V0I N7   N Y N 430 
V0I N8   N N N 431 
V0I N9   N N N 432 
V0I O1   O N N 433 
V0I O2   O N N 434 
V0I O3   O N N 435 
V0I O4   O N N 436 
V0I O5   O N N 437 
V0I O6   O N N 438 
V0I O7   O N N 439 
V0I S    S N N 440 
V0I H9   H N N 441 
V0I H10  H N N 442 
V0I H8   H N N 443 
V0I H12  H N N 444 
V0I H11  H N N 445 
V0I H20  H N N 446 
V0I H19  H N N 447 
V0I H4   H N N 448 
V0I H5   H N N 449 
V0I H6   H N N 450 
V0I H    H N N 451 
V0I H7   H N N 452 
V0I H23  H N N 453 
V0I H24  H N N 454 
V0I H28  H N N 455 
V0I H26  H N N 456 
V0I H27  H N N 457 
V0I H31  H N N 458 
V0I H30  H N N 459 
V0I H29  H N N 460 
V0I H32  H N N 461 
V0I H1   H N N 462 
V0I H2   H N N 463 
V0I H3   H N N 464 
V0I H15  H N N 465 
V0I H16  H N N 466 
V0I H34  H N N 467 
V0I H33  H N N 468 
V0I H18  H N N 469 
V0I H17  H N N 470 
V0I H25  H N N 471 
V0I H13  H N N 472 
V0I H14  H N N 473 
V0I H21  H N N 474 
V0I H22  H N N 475 
VAL N    N N N 476 
VAL CA   C N S 477 
VAL C    C N N 478 
VAL O    O N N 479 
VAL CB   C N N 480 
VAL CG1  C N N 481 
VAL CG2  C N N 482 
VAL OXT  O N N 483 
VAL H    H N N 484 
VAL H2   H N N 485 
VAL HA   H N N 486 
VAL HB   H N N 487 
VAL HG11 H N N 488 
VAL HG12 H N N 489 
VAL HG13 H N N 490 
VAL HG21 H N N 491 
VAL HG22 H N N 492 
VAL HG23 H N N 493 
VAL HXT  H N N 494 
# 
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 
V0I C   N    sing N N 378 
V0I C1  N    sing N N 379 
V0I C2  C1   sing N N 380 
V0I C2  O    sing N N 381 
V0I O   C3   sing N N 382 
V0I C3  C4   sing N N 383 
V0I C4  C5   sing N N 384 
V0I C5  C2   sing N N 385 
V0I O1  C5   sing N N 386 
V0I O2  C4   sing N N 387 
V0I N1  C3   sing N N 388 
V0I N1  C6   sing Y N 389 
V0I C6  N2   doub Y N 390 
V0I N2  C7   sing Y N 391 
V0I C7  C8   doub Y N 392 
V0I C8  N1   sing Y N 393 
V0I N3  C8   sing Y N 394 
V0I C9  N3   doub Y N 395 
V0I N4  C9   sing Y N 396 
V0I C10 N4   doub Y N 397 
V0I C7  C10  sing Y N 398 
V0I N5  C10  sing N N 399 
V0I N   C11  sing N N 400 
V0I C11 C12  sing N N 401 
V0I C12 C13  trip N N 402 
V0I C13 C14  sing N N 403 
V0I C14 N6   doub Y N 404 
V0I N6  C15  sing Y N 405 
V0I C15 C16  doub Y N 406 
V0I C16 N7   sing Y N 407 
V0I C14 N7   sing Y N 408 
V0I N7  C17  sing N N 409 
V0I C17 O3   sing N N 410 
V0I O3  C18  sing N N 411 
V0I C19 C18  sing N N 412 
V0I C20 C19  sing N N 413 
V0I C17 C20  sing N N 414 
V0I O4  C20  sing N N 415 
V0I O5  C19  sing N N 416 
V0I C18 C21  sing N N 417 
V0I C21 N8   sing N N 418 
V0I N8  S    sing N N 419 
V0I O6  S    doub N N 420 
V0I S   O7   doub N N 421 
V0I N9  S    sing N N 422 
V0I C22 N9   sing N N 423 
V0I C23 N9   sing N N 424 
V0I N10 C16  sing Y N 425 
V0I C24 N10  doub Y N 426 
V0I N11 C24  sing Y N 427 
V0I C25 N11  doub Y N 428 
V0I C15 C25  sing Y N 429 
V0I N12 C25  sing N N 430 
V0I C   H9   sing N N 431 
V0I C   H10  sing N N 432 
V0I C   H8   sing N N 433 
V0I C1  H12  sing N N 434 
V0I C1  H11  sing N N 435 
V0I C11 H20  sing N N 436 
V0I C11 H19  sing N N 437 
V0I C17 H4   sing N N 438 
V0I C18 H5   sing N N 439 
V0I C19 H6   sing N N 440 
V0I C2  H    sing N N 441 
V0I C20 H7   sing N N 442 
V0I C21 H23  sing N N 443 
V0I C21 H24  sing N N 444 
V0I C22 H28  sing N N 445 
V0I C22 H26  sing N N 446 
V0I C22 H27  sing N N 447 
V0I C23 H31  sing N N 448 
V0I C23 H30  sing N N 449 
V0I C23 H29  sing N N 450 
V0I C24 H32  sing N N 451 
V0I C3  H1   sing N N 452 
V0I C4  H2   sing N N 453 
V0I C5  H3   sing N N 454 
V0I C6  H15  sing N N 455 
V0I C9  H16  sing N N 456 
V0I N12 H34  sing N N 457 
V0I N12 H33  sing N N 458 
V0I N5  H18  sing N N 459 
V0I N5  H17  sing N N 460 
V0I N8  H25  sing N N 461 
V0I O1  H13  sing N N 462 
V0I O2  H14  sing N N 463 
V0I O4  H21  sing N N 464 
V0I O5  H22  sing N N 465 
VAL N   CA   sing N N 466 
VAL N   H    sing N N 467 
VAL N   H2   sing N N 468 
VAL CA  C    sing N N 469 
VAL CA  CB   sing N N 470 
VAL CA  HA   sing N N 471 
VAL C   O    doub N N 472 
VAL C   OXT  sing N N 473 
VAL CB  CG1  sing N N 474 
VAL CB  CG2  sing N N 475 
VAL CB  HB   sing N N 476 
VAL CG1 HG11 sing N N 477 
VAL CG1 HG12 sing N N 478 
VAL CG1 HG13 sing N N 479 
VAL CG2 HG21 sing N N 480 
VAL CG2 HG22 sing N N 481 
VAL CG2 HG23 sing N N 482 
VAL OXT HXT  sing N N 483 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-17-CE18-0011-02 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   8A9V 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8QGM 
_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]   0.015911 
_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]   0.013449 
_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]   0.008443 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 12.27811 35.66321  24.89973  1.000 59.14040 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 11.04691 36.24549  24.38678  1.000 58.00725 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.94530  35.19019  24.34225  1.000 54.39886 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.80023  34.41720  25.28809  1.000 52.84313 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.28642 36.83261  23.00372  0.700 60.22236 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.66559 37.46142  22.81830  0.700 62.71991 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 13.67865 36.61937  21.57684  0.700 65.03376 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 14.16719 35.13481  22.44870  0.700 64.43021 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 9.16880  35.16197  23.25161  1.000 52.08540 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.19643  34.09288  23.05095  1.000 49.28006 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.93608  32.79650  22.77063  1.000 46.11393 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.89500  32.78235  21.99775  1.000 46.18306 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.25630  34.41495  21.88681  1.000 50.44167 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.28956  35.57111  22.14731  1.000 52.91050 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.28014  35.71799  20.99722  1.000 55.87315 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.17289  36.72805  21.31492  1.000 58.92623 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 4.50414  38.12637  20.91275  1.000 61.36480 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.51013  31.70944  23.42057  1.000 42.79400 ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 9.11576  30.39729  23.20329  1.000 40.09480 ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 8.01422  29.34242  23.17522  1.000 39.92282 ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.87259  29.59482  23.57713  1.000 40.94005 ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.15208 30.06942  24.30899  1.000 37.25869 ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.49458  29.71359  25.60888  1.000 36.42050 ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 9.00280  30.70735  26.44992  1.000 37.80618 ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.33776  28.39778  25.98232  1.000 34.99705 ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.35841  30.40273  27.63995  1.000 37.45656 ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.68000  28.06705  27.15669  1.000 35.35482 ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.19383  29.08383  27.99252  1.000 37.49715 ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.54660  28.77807  29.18209  1.000 38.92302 ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.35427  28.13539  22.73040  1.000 38.41125 ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.48007  27.00568  23.01498  1.000 36.90995 ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.34560  25.77413  23.18859  1.000 34.65672 ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.53133  25.77123  22.85689  1.000 34.60739 ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.41154  26.80726  21.93407  1.000 38.73594 ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 6.97878  26.41363  20.57830  1.000 39.64896 ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.26775  24.63645  20.46521  1.000 40.92067 ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.57094  24.01532  20.46575  1.000 42.27395 ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.74973  24.71738  23.72836  1.000 33.72512 ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.46542  23.47220  23.95582  1.000 33.85188 ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.65245  22.31300  23.40409  1.000 34.42613 ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.49596  22.12652  23.78521  1.000 33.70459 ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.75160  23.24804  25.45141  1.000 31.77209 ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.45310  24.45756  26.03224  1.000 30.24665 ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.56130  21.98490  25.60334  1.000 32.35559 ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.85187  24.27219  27.57364  1.000 31.62856 ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.26450  21.51770  22.52111  1.000 34.65846 ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.66915  20.27017  22.08305  1.000 37.37602 ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.30618  19.12247  22.83628  1.000 37.46229 ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.48372  19.17415  23.19568  1.000 39.93333 ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 7.87522  20.03616  20.58193  1.000 40.96713 ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 9.26211  19.80010  20.33198  1.000 43.91505 ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.48056  21.22958  19.81956  1.000 42.64651 ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.52762  18.08145  23.07130  1.000 36.05736 ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 8.00128  16.93688  23.82216  1.000 36.66422 ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.75427  15.66453  23.02824  1.000 38.74993 ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.76422  15.54745  22.28728  1.000 40.49585 ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.30148  16.85766  25.20108  1.000 36.92498 ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.31042  15.52979  25.67072  1.000 37.99412 ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.67375  14.71382  23.18770  1.000 37.83258 ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.46141  13.37474  22.66759  1.000 40.10273 ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.18624  12.74446  23.21696  1.000 41.44187 ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.60049  11.86805  22.56884  1.000 43.40158 ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.67741  12.50121  22.98319  1.000 42.25918 ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.46590  11.03429  22.67798  1.000 45.66999 ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.60963 10.16869  23.13150  1.000 49.72879 ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 10.46108 8.79065   22.50847  1.000 53.63390 ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 10.21311 8.89024   21.01223  1.000 56.56366 ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.73897  13.15190  24.40569  1.000 40.62038 ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.48551  12.64909  24.91597  1.000 42.47134 ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.58547  11.49601  25.89133  1.000 45.40666 ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.55010  11.04653  26.39418  1.000 48.50891 ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.77647  10.99368  26.17258  1.000 45.14307 ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 6.86333  10.02336  27.24173  1.000 49.80406 ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 6.89726  10.76492  28.56807  1.000 48.21017 ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.01744  11.98618  28.60305  1.000 47.83164 ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.09088  9.13990   27.08556  1.000 56.95682 ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.36161  9.93678   26.87668  1.000 63.97630 ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.29964  11.18561  26.86629  1.000 64.99897 ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.42516 9.30515   26.70321  1.000 68.46709 ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 6.80570  10.01191  29.66884  1.000 47.80968 ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 6.74042  10.64598  30.98552  1.000 48.86266 ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 7.96835  11.51398  31.24975  1.000 47.31042 ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 7.84662  12.64071  31.72972  1.000 47.41042 ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 6.57745  9.58663   32.07800  1.000 51.94386 ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.24145  8.88846   32.05987  0.700 54.99897 ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.00124  8.07592   33.32160  0.700 57.95549 ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 5.80504  7.16208   33.60951  0.700 59.39113 ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 4.01225  8.36108   34.02852  0.700 58.41746 ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.15598  11.03818  30.87753  1.000 46.41751 ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.37261 11.80179  31.15188  1.000 46.41945 ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.38345 13.14782  30.42560  1.000 42.79187 ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.77123 14.17163  30.99770  1.000 41.15545 ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.59159 10.96659  30.76338  1.000 49.26666 ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 12.92161 11.67358  30.92062  1.000 51.70309 ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.08530 10.70849  30.76410  1.000 54.41286 ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.43424 11.39806  31.05120  1.000 57.52144 ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 15.56361 11.92990  32.45618  1.000 57.49815 ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 9.99885  13.16358  29.14814  1.000 39.70095 ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.05326 14.40425  28.39037  1.000 36.58596 ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 8.93382  15.36067  28.76269  1.000 36.11772 ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.13616  16.58289  28.79325  1.000 35.25143 ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 9.99524  14.07713  26.90616  1.000 37.07590 ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.04059 13.15579  26.61877  1.000 38.94050 ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.73876  14.83626  29.01422  1.000 37.26937 ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.64181  15.70057  29.45754  1.000 38.52082 ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 6.97016  16.39031  30.78222  1.000 37.99933 ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.68816  17.58130  30.95812  1.000 35.45391 ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.34970  14.89172  29.57559  0.800 39.14995 ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.66582  14.68587  28.23526  0.700 40.83976 ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.18445  15.18516  27.20396  0.700 40.02967 ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.59250  14.03228  28.22300  0.700 42.99806 ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.57115  15.65972  31.72381  1.000 39.60594 ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 7.88955  16.25240  33.01901  1.000 40.65674 ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 8.99206  17.29147  32.89099  1.000 37.65332 ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 8.91814  18.36469  33.50567  1.000 37.31776 ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.30335  15.17213  34.01820  1.000 44.31011 ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.28418  14.09370  34.37655  1.000 50.21194 ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 7.89047  13.13271  35.41276  1.000 52.28989 ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 5.98040  14.72520  34.91042  1.000 51.59031 ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.01100 17.00742  32.07884  1.000 35.60414 ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.03239 18.01065  31.83992  1.000 35.03336 ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.41468 19.26571  31.23192  1.000 34.84998 ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 10.73871 20.39248  31.62725  1.000 35.31905 ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.10854 17.43706  30.91044  1.000 34.32155 ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.36386 18.28803  30.82463  1.000 34.61413 ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 13.97340 18.44871  32.18888  1.000 34.88275 ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.38581 17.63438  29.89647  1.000 35.45162 ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.51588  19.08563  30.27093  1.000 33.24487 ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 8.84891  20.22797  29.66322  1.000 30.96892 ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.08660  21.02970  30.70901  1.000 31.74810 ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.18732  22.25882  30.75885  1.000 32.92433 ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 7.92030  19.75317  28.53136  1.000 29.91191 ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 6.98414  20.82145  28.04770  1.000 31.10213 ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.22626  20.34133  26.78904  1.000 31.98958 ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.32794  21.37300  26.29535  1.000 33.62997 ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.16953  21.68950  26.86430  1.000 35.69535 ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.71728  21.03989  27.93031  1.000 37.24430 ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.43131  22.66509  26.33990  1.000 35.17682 ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.33112  20.35127  31.56601  1.000 31.90952 ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.58189  21.07670  32.59967  1.000 32.67705 ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.52103  21.82769  33.53424  1.000 32.77865 ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.26246  22.98220  33.90212  1.000 32.88621 ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.69118  20.11160  33.37828  1.000 33.88173 ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.37895  19.72124  32.68622  1.000 35.77036 ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.46168  18.97467  33.64337  1.000 36.56567 ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.66665  20.97219  32.14651  1.000 35.09723 ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.62931  21.20054  33.90428  1.000 32.74760 ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.57059  21.85777  34.79816  1.000 33.89840 ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.26520 23.03078  34.13331  1.000 32.75929 ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.52226 24.03854  34.80101  1.000 35.46244 ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.59235 20.86306  35.29850  1.000 36.87687 ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.14318 20.19635  36.55422  1.000 39.79190 ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.19838  20.67511  37.21120  1.000 40.17140 ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 10.78411 19.08725  36.90449  1.000 40.84684 ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.54812 22.94430  32.81036  1.000 30.09503 ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.16344 24.08676  32.16245  1.000 30.87557 ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.16710 25.22580  32.03231  1.000 33.22840 ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.53385 26.39809  32.14893  1.000 34.07249 ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.71217 23.68245  30.78834  1.000 31.54361 ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 12.93045 22.80959  30.87756  1.000 34.67064 ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.57681 22.53258  29.19428  1.000 37.80130 ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.55113 24.02387  28.91737  1.000 35.95864 ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 8.90063  24.90323  31.76633  1.000 33.29013 ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 7.88868  25.94473  31.67688  1.000 33.06990 ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 7.78875  26.67880  33.00259  1.000 33.59008 ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.66953  27.90887  33.04736  1.000 34.22702 ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.53885  25.34656  31.25371  1.000 32.02255 ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.55184  24.95553  29.76233  1.000 33.19519 ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.42766  26.35459  31.54659  1.000 31.48577 ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.39267  24.09704  29.38540  1.000 34.23575 ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 7.86979  25.94076  34.10557  1.000 33.53689 ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 7.82277  26.59183  35.41021  1.000 34.50720 ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.03658  27.49181  35.61650  1.000 35.93145 ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 8.91034  28.60722  36.14127  1.000 36.86478 ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.73520  25.55010  36.52563  1.000 33.50123 ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.21724 27.03611  35.18973  1.000 36.32740 ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.39508 27.87830  35.29880  1.000 36.93153 ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.29158 29.11924  34.43864  1.000 38.47036 ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.68198 30.21192  34.86082  1.000 39.41616 ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.79776 28.96695  33.19861  1.000 37.84627 ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.63890 30.14420  32.35276  1.000 37.80057 ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.65904  31.13496  32.95362  1.000 40.86548 ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.78790  32.34325  32.73114  1.000 43.90463 ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.17870 29.74762  30.95732  1.000 35.84414 ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.27933 29.20196  30.08499  1.000 37.20989 ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.47384 29.90023  29.92459  1.000 40.27487 ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.13153 27.98226  29.43081  1.000 35.63107 ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.49741 29.38950  29.10045  1.000 40.14209 ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.14462 27.46802  28.63287  1.000 37.32460 ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.32815 28.17216  28.46219  1.000 38.72573 ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.66776  30.65422  33.70042  1.000 40.71055 ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.71241  31.56945  34.30414  1.000 42.46942 ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.32980  32.54942  35.28421  1.000 44.89725 ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.71182  33.56535  35.60124  1.000 45.05346 ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.54318  32.27857  35.75099  1.000 48.53783 ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.25776 33.19203  36.63250  1.000 51.86151 ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.01637 34.28315  35.88334  1.000 53.24512 ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.66390 35.10847  36.53333  1.000 54.42832 ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.21793 32.39696  37.53224  1.000 53.80749 ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.51311 31.31959  38.31761  1.000 56.35962 ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.51104  31.90838  39.34366  1.000 61.75165 ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 9.66246  33.10696  39.72709  1.000 63.22882 ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.57087  31.17599  39.76476  1.000 63.67680 ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 10.93737 34.32682  34.54446  1.000 53.45405 ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.57903 35.36241  33.73575  1.000 53.99019 ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.54756 36.00772  32.80606  1.000 58.20660 ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.36411  35.65272  32.80692  1.000 58.85740 ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.74350 34.78887  32.91667  1.000 51.46403 ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.83054 34.10170  33.73163  1.000 50.11592 ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.76702 32.74438  34.00497  1.000 49.14571 ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 14.93144 34.81147  34.20703  1.000 49.78593 ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.76798 32.10463  34.72636  1.000 49.57570 ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 15.93693 34.18193  34.94073  1.000 49.55894 ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 15.85270 32.82845  35.19013  1.000 50.14532 ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 16.85251 32.19034  35.90978  1.000 50.76135 ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 11.00577 36.97440  32.00359  1.000 61.19003 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 10.17451 37.62232  30.98236  1.000 64.18693 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 10.15258 36.74199  29.72941  1.000 64.56502 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.76034 37.03487  28.69560  1.000 64.17627 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.69540 39.01878  30.66724  1.000 66.72572 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.81380  39.76257  29.67327  1.000 69.47438 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 8.65017  39.33832  29.47858  1.000 71.06730 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 10.28206 40.76431  29.08170  1.000 70.10249 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.44249  35.62315  29.85021  1.000 63.80968 ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.32720  34.64082  28.78315  1.000 62.34791 ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.86905  34.23587  28.68484  1.000 59.30697 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.31961  33.67301  29.63698  1.000 59.96084 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.20922 33.41627  29.04922  1.000 64.52733 ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.69993 33.72089  29.18056  1.000 67.17486 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.57574 34.06775  27.63141  1.000 68.63749 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 12.55996 32.46017  26.83519  1.000 69.24332 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.24952  34.52367  27.54279  1.000 56.20502 ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.86655  34.15587  27.26686  1.000 54.23693 ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.82772  32.86719  26.44089  1.000 50.82094 ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.53414  32.74300  25.43018  1.000 49.32115 ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 5.15453  35.30261  26.53024  1.000 56.54263 ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.75456  34.99042  25.98422  1.000 58.85805 ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.29809  36.00256  24.93355  0.700 61.25050 ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 3.99931  37.02044  24.74307  0.700 62.19181 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.24944  35.77864  24.28364  0.700 62.23046 ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.01777  31.90493  26.87934  1.000 48.67765 ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.80154  30.68459  26.10666  1.000 46.69301 ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.87203  30.99411  24.94152  1.000 46.52019 ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.73996  31.42761  25.15452  1.000 46.44190 ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.19371  29.59321  26.98628  1.000 43.64836 ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.21471  28.25863  26.31586  1.000 40.22998 ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.27936  27.92025  25.33384  1.000 39.34964 ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.19540  27.34462  26.63689  1.000 39.22408 ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.33926  26.69148  24.68203  1.000 40.23065 ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.26724  26.12963  26.01621  1.000 39.95461 ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.34438  25.79769  25.02910  1.000 40.73569 ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.44312  24.55251  24.45351  1.000 41.93028 ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.33312  30.75807  23.71575  1.000 46.80228 ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.54743  31.09739  22.53075  1.000 48.85926 ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.91944  30.09612  21.45705  1.000 47.39983 ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 5.04189  30.14188  20.92994  1.000 46.76527 ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.81991  32.52456  22.06903  1.000 52.64701 ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.91781  32.95592  20.92364  1.000 55.75636 ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.47380  32.10886  20.11887  1.000 56.55479 ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.64709  34.16050  20.82427  1.000 57.12630 ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 2.99875  29.19094  21.13580  1.000 46.49373 ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.30669  28.18821  20.13063  1.000 47.57627 ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.74438  28.54414  18.76497  1.000 47.48763 ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.79334  27.71080  17.85955  1.000 47.54949 ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.83485  26.80272  20.56834  1.000 48.79033 ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.35103  26.70014  20.67217  1.000 53.04064 ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.66012  27.67642  20.31851  1.000 55.41410 ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.88415  25.62563  21.11000  1.000 54.00881 ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.22260  29.75337  18.60431  1.000 46.58167 ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.88693  30.25986  17.27894  1.000 46.69649 ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.05471  31.02577  16.68164  1.000 47.71726 ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.51353  30.70053  15.58544  1.000 47.84932 ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.60990  31.12397  17.32154  1.000 46.78664 ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.32625  31.70204  15.94299  1.000 46.76791 ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.56735 30.29596  17.77449  1.000 46.47351 ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.58450  32.02364  17.39283  1.000 47.96714 ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.73110  32.80332  16.92212  1.000 50.05389 ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.90525  32.77531  17.90171  1.000 48.38015 ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.38137  33.82681  18.34639  1.000 50.99895 ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.30892  34.24278  16.64148  1.000 53.76190 ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.22316  34.35290  15.57790  0.800 57.76400 ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.87761  35.78915  15.20459  0.700 60.43454 ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 3.19447  36.71252  15.99138  0.700 61.64019 ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 2.27593  35.98833  14.12289  0.700 60.78013 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.42748  31.59995  18.23233  1.000 44.10463 ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.63560  31.55735  19.06270  1.000 42.70368 ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.83456  32.15132  18.33594  1.000 43.28279 ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.89032  32.21975  17.10609  1.000 44.06171 ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.83829  30.05916  19.32118  1.000 41.30944 ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.19378  29.40040  18.10119  1.000 41.94580 ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 5.98357  30.24768  17.84508  1.000 42.23739 ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.81128  32.59052  19.13386  1.000 42.75316 ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.14178 32.91092  18.64108  1.000 43.37516 ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.18106 31.87700  19.04455  1.000 40.06684 ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.23961 31.79776  18.40737  1.000 39.74139 ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.55329 34.30470  19.14086  1.000 48.41153 ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.62257 35.38628  18.55762  0.800 52.99396 ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 10.98335 36.81342  18.93465  0.700 56.35754 ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 11.10057 37.09772  20.13314  0.700 57.10030 ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 11.12966 37.66082  18.02834  0.700 57.93780 ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.88965 31.08766  20.07614  1.000 36.97377 ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.68613 29.95783  20.52284  1.000 35.90874 ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.78067 28.74235  20.52032  1.000 35.38722 ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.67668 28.78449  21.08476  1.000 36.70159 ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.24729 30.17779  21.94135  1.000 38.55180 ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 14.09013 31.44888  21.98784  1.000 42.13091 ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 14.05210 28.95554  22.38126  1.000 37.92673 ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.34161 31.39219  21.11873  1.000 43.72077 ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.24685 27.66768  19.90459  1.000 33.40832 ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.56619 26.38412  19.89243  1.000 32.02851 ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.50645 25.36849  20.52729  1.000 31.91774 ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.61520 25.12886  20.02722  1.000 32.71064 ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.15947 25.96004  18.47327  1.000 31.56659 ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.69991 24.54080  18.49054  1.000 32.42111 ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.06899 26.86175  17.96489  1.000 31.34566 ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.07841 24.80329  21.64755  1.000 30.93865 ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.82004 23.77540  22.35018  1.000 30.62518 ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.15637 22.44821  22.06162  1.000 29.53354 ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 10.93982 22.30237  22.22461  1.000 30.18320 ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 12.84915 24.04538  23.86350  1.000 31.62698 ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.47108 25.40403  24.09968  1.000 31.26861 ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.61946 22.94496  24.55898  1.000 31.13405 ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.15169 25.93953  25.45450  1.000 30.20786 ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 12.94852 21.49118  21.64457  1.000 28.82411 ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.50131 20.14412  21.35143  1.000 31.11990 ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.08214 19.22481  22.42112  1.000 31.67622 ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.29651 19.20484  22.62049  1.000 34.41073 ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 12.96825 19.75433  19.93723  1.000 33.04041 ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 12.80743 18.38773  19.71172  1.000 36.43464 ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.23169 18.48736  23.12973  1.000 30.05286 ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.69209 17.55993  24.17058  1.000 31.11848 ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.35691 16.14429  23.71842  1.000 34.42128 ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.17972 15.74085  23.70567  1.000 36.75589 ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.06333 17.86278  25.53696  1.000 30.16826 ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.33201 19.31732  25.90691  1.000 29.49654 ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.61562 16.88465  26.59946  1.000 32.43131 ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 11.77402 19.75653  27.31385  1.000 30.04418 ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.38656 15.39431  23.33858  1.000 33.57388 ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.19147 14.03629  22.89589  1.000 34.35580 ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.39049 13.53312  22.14369  1.000 35.89043 ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.50785 13.52022  22.67102  1.000 40.13251 ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.16332 13.06613  20.93978  1.000 32.99370 ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.24204 12.56674  20.11466  1.000 32.92918 ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.29501 13.39116  18.85489  1.000 31.80166 ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.69085 14.46522  18.78792  1.000 29.89781 ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.01269 12.89237  17.84564  1.000 31.71858 ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.12581 13.62916  16.59301  1.000 29.75295 ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 14.81038 13.62885  15.83267  1.000 30.85186 ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.53340 14.57774  15.09598  1.000 31.13799 ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.23283 13.02700  15.74574  1.000 30.23427 ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.61678 13.34883  16.27027  1.000 32.89738 ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 18.84995 14.49539  16.74924  1.000 33.32253 ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.47235 12.43232  16.22567  1.000 32.81666 ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 13.99203 12.57755  15.99631  1.000 31.33869 ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.65980 12.59533  15.40842  1.000 30.02778 ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 11.80619 13.72157  15.95889  1.000 30.42657 ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.11204 14.40780  15.20259  1.000 31.37265 ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 11.85700 13.93438  17.29364  1.000 29.09111 ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.14679 15.04757  17.91106  1.000 29.24176 ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.64747 16.36029  17.36567  1.000 28.48702 ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.85634 17.26716  17.08940  1.000 27.65741 ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.33757 14.98723  19.43376  1.000 30.29542 ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 10.97870 13.67148  19.83217  1.000 34.15115 ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.46193 15.99722  20.15371  1.000 27.61843 ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 12.96292 16.47120  17.19589  1.000 28.22604 ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.53111 17.69705  16.67404  1.000 28.62402 ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.08821 17.91593  15.22377  1.000 28.92493 ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.66314 19.01342  14.85052  1.000 29.64850 ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.05959 17.66654  16.76655  1.000 29.85543 ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.66664 18.98391  16.43002  1.000 31.15711 ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.97717 19.30503  15.09514  1.000 31.57034 ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.84635 19.92776  17.42763  1.000 32.30198 ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.49470 20.53372  14.76953  1.000 32.23897 ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.38044 21.16744  17.13428  1.000 33.91961 ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.68891 21.48588  15.78876  1.000 33.30264 ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.16517 16.87045  14.40452  1.000 28.09775 ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.68663 16.99382  13.02295  1.000 28.37739 ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.22332 17.42382  12.98087  1.000 30.35495 ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.83005 18.23738  12.13504  1.000 31.27218 ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.86054 15.66159  12.29684  1.000 30.86164 ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 13.89191 15.36325  11.20469  1.000 34.16186 ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.88792 16.46028  11.00171  1.000 33.89723 ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.53244 14.01480  11.42648  1.000 35.61519 ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.38023 16.87424  13.87023  1.000 31.07512 ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 8.97225  17.28266  13.85361  1.000 31.66249 ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.80598  18.74068  14.25609  1.000 31.29090 ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 7.90976  19.43022  13.74495  1.000 33.39091 ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.13034  16.39238  14.76680  1.000 35.00683 ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.00858  15.11348  14.18613  1.000 37.86982 ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.62159  19.21957  15.20478  1.000 31.96981 ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.56825  20.62739  15.58038  1.000 30.52613 ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 9.95102  21.51953  14.41445  1.000 30.31548 ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.32654  22.55992  14.18549  1.000 31.71961 ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.49470 20.89022  16.76450  1.000 30.68824 ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.03518 21.16728  13.72146  1.000 28.48314 ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.43411 21.89920  12.51819  1.000 30.08955 ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.27255 22.00375  11.52382  1.000 31.78589 ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 9.96216  23.08969  11.01483  1.000 32.29530 ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.64809 21.20614  11.88949  1.000 28.83876 ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 12.94168 21.65203  10.48758  1.000 28.88981 ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.52075 22.88535  10.25059  1.000 30.65418 ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.66365 20.83760  9.40723   1.000 28.14844 ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.79790 23.31047  8.95026   1.000 30.65836 ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 12.94787 21.26053  8.08066   1.000 29.14379 ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.51842 22.49889  7.86560   1.000 29.59814 ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.59243  20.88854  11.26202  1.000 30.97215 ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.51848  20.91824  10.26590  1.000 30.88631 ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.28080  21.62669  10.78231  1.000 34.85067 ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.55751  22.24716  9.99895   1.000 37.15912 ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.21932  19.49868  9.78952   1.000 29.02717 ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.26520  18.98801  8.85608   1.000 30.33795 ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.34859  19.42946  7.55323   1.000 31.87608 ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.33270 18.17290  9.04854   1.000 29.90573 ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.39593 18.86803  6.96434   1.000 30.18728 ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.01462 18.11056  7.85431   1.000 29.59420 ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.05998  21.61982  12.10129  1.000 37.02542 ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 5.94390  22.37247  12.65840  1.000 36.93081 ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.10837  23.85941  12.38227  1.000 37.91238 ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.11207  24.55060  12.13165  1.000 38.82540 ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.83049  22.07970  14.16082  1.000 37.98742 ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.66472  22.72222  14.83520  1.000 40.88522 ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.54366  22.34856  16.36501  1.000 44.99974 ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.13734  21.35845  16.83554  1.000 44.83064 ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.76473  23.14678  17.12187  1.000 46.29456 ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.35786  24.35272  12.30885  1.000 38.42847 ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.62279  25.78440  12.15107  1.000 38.99284 ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.36469  26.13295  10.86197  1.000 39.42140 ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.00377  27.18867  10.77486  1.000 40.20242 ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.38888  26.30781  13.36262  1.000 38.91609 ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.51430  26.23092  14.59331  1.000 40.30670 ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.48054  27.13320  14.76768  1.000 41.15871 ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.66367  25.21433  15.51139  1.000 39.92348 ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.63521  27.06679  15.85314  1.000 41.68201 ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.84036  25.13602  16.63601  1.000 40.33406 ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.82323  26.07198  16.79267  1.000 41.33732 ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.96290  26.02242  17.86011  1.000 40.49498 ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.24849  25.30481  9.82853   1.000 39.62890 ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.06774  25.57191  8.64700   1.000 41.75548 ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.67616  26.84572  7.90588   1.000 42.32670 ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.43926  27.28557  7.03463   1.000 42.54621 ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.04395  24.38391  7.67445   1.000 43.59407 ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.69032  23.98113  7.18205   1.000 45.87953 ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.78303  22.90750  6.10654   0.700 48.67429 ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.17015  21.76268  6.42425   0.700 47.36423 ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 7.48773  23.22157  4.93157   0.700 51.70435 ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.53586  27.45072  8.22272   1.000 43.00825 ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.15325  28.72115  7.62474   1.000 44.82401 ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.71956  29.93019  8.36503   1.000 44.48305 ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.59528  31.05263  7.86468   1.000 45.15764 ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.62308  28.83584  7.55231   1.000 47.70045 ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 4.98272  27.75279  6.68693   0.700 51.07273 ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 5.64796  27.61976  5.32383   0.600 53.74803 ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 5.76585  28.64311  4.60293   0.600 54.07392 ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 6.06548  26.48920  4.97810   0.600 54.90066 ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.35635  29.74304  9.52080   1.000 43.48549 ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.90127  30.87647  10.26355  1.000 44.08910 ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.36892 30.66308  10.60270  1.000 43.04204 ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.85331 31.14344  11.64159  1.000 42.14977 ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.09364  31.14777  11.53750  1.000 45.55566 ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.72269  31.77202  11.24044  1.000 49.08189 ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.99530  32.28429  12.49736  1.000 53.09605 ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.76787  33.29118  13.21784  1.000 57.50653 ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.37975  33.07128  14.37963  1.000 60.97435 ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.31714  31.89313  14.98227  1.000 62.07836 ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 8.07838  34.05405  14.94685  1.000 61.70675 ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.09305 29.96583  9.72454   1.000 41.08453 ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.47349 29.62490  10.03330  1.000 40.39904 ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.34392 30.85614  10.20742  1.000 43.69105 ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.34124 30.80761  10.93273  1.000 45.17022 ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.04914 28.74493  8.94816   1.000 38.05807 ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.40772 27.36889  8.85529   1.000 38.02573 ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 12.95471 26.69492  7.63515   1.000 37.98937 ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.72529 26.53492  10.06934  1.000 37.48763 ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.01714 31.95318  9.54197   1.000 45.81723 ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 13.84195 33.13767  9.72185   1.000 50.05020 ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.58489 33.83476  11.05387  1.000 48.85218 ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.35419 34.72021  11.44154  1.000 50.54477 ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.62668 34.11886  8.56025   1.000 55.78881 ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 14.85854 34.24779  7.68553   0.700 60.82526 ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 15.76475 33.38636  7.80296   0.700 61.48837 ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 14.93174 35.21125  6.88748   0.700 63.90846 ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.53450 33.46528  11.76594  1.000 45.74703 ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.20687 34.13823  13.00844  1.000 44.35408 ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.48274 33.27815  14.23338  1.000 42.08810 ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.17725 33.70346  15.34927  1.000 43.94448 ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 10.74268 34.56944  12.99619  1.000 45.83498 ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.44904 35.71281  12.05115  0.700 48.08839 ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 9.36573  35.36822  11.05546  0.600 50.59468 ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 9.66089  34.65313  10.06804  0.600 51.72916 ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 8.21636  35.80554  11.27407  0.600 51.52267 ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.06129 32.09570  14.06357  1.000 38.41689 ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.11640 31.09700  15.12030  1.000 37.43899 ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.53917 30.59671  15.29380  1.000 38.47834 ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.24594 30.35241  14.30983  1.000 40.55402 ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.16701 29.92732  14.79599  1.000 36.54440 ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.72583 30.40091  14.92865  1.000 36.74608 ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.42331 28.70705  15.69325  1.000 35.72330 ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.74583  29.29865  14.64059  1.000 38.50246 ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 14.95563 30.39941  16.54622  1.000 36.63405 ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.13931 29.59765  16.80848  1.000 36.78739 ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.73868 28.36071  17.59487  1.000 35.50590 ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 14.93421 28.44310  18.54043  1.000 36.35788 ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.20178 30.38665  17.56535  1.000 38.97898 ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.29473 27.22438  17.19616  1.000 32.48118 ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 15.96306 25.91894  17.73963  1.000 31.19971 ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.00488 25.48967  18.76290  1.000 33.42127 ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.18703 25.83584  18.65728  1.000 36.65167 ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.87202 24.87466  16.62726  1.000 29.39876 ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.72156 25.07848  15.69267  1.000 29.09582 ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 14.84022 25.87470  14.57490  1.000 29.59301 ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.52042 24.42399  15.91338  1.000 30.59057 ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.73932 26.04790  13.70416  1.000 30.57262 ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.43368 24.58118  15.07912  1.000 30.14818 ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.53488 25.38432  13.95482  1.000 30.20158 ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.54022 24.73912  19.76391  1.000 31.08530 ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.39151 24.10287  20.76319  1.000 30.93473 ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.82106 22.72121  20.99806  1.000 30.90157 ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.60635 22.57172  21.18138  1.000 31.62716 ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.42305 24.89017  22.09107  1.000 32.77403 ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 17.76730 26.35146  21.86854  1.000 34.96420 ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.42202 24.25022  23.08616  1.000 32.65634 ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 17.47896 27.21215  23.06731  1.000 35.48298 ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.68505 21.72803  21.04652  1.000 30.55012 ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.28433 20.36357  21.31997  1.000 31.61099 ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 17.86035 19.81570  22.61178  1.000 33.83909 ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.04950 19.98196  22.90236  1.000 35.92345 ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.00119 19.17200  23.40436  1.000 33.42822 ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.40138 18.42754  24.59024  1.000 33.53880 ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.16565 16.96195  24.28872  1.000 36.95564 ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.07440 16.60609  23.83600  1.000 39.49685 ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.55479 18.88179  25.78742  1.000 32.21262 ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 16.74358 20.36814  25.98165  1.000 32.26166 ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 16.85546 18.04088  27.03990  1.000 31.82525 ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 15.88459 20.90135  27.08922  1.000 33.80459 ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.15555 16.10176  24.52274  1.000 40.09375 ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 17.91710 14.68702  24.26325  1.000 45.83391 ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.61433 13.95638  25.55693  1.000 46.32609 ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.37457 14.03634  26.52529  1.000 45.20424 ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.05659 14.00289  23.49192  1.000 50.09742 ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.38040 14.03944  24.16986  1.000 53.97238 ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 20.80208 13.04229  25.02072  1.000 56.76243 ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.39429 14.93185  24.09722  1.000 56.13518 ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.01370 13.32825  25.46499  1.000 58.38039 ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.39630 14.47042  24.91963  1.000 58.75153 ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.48986 13.26451  25.57207  1.000 48.39064 ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.12150 12.49012  26.74192  1.000 55.85850 ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.42156 11.01365  26.56494  1.000 62.46672 ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 16.43113 10.27447  27.55739  1.000 63.99967 ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.63978 12.70206  27.10153  1.000 56.18763 ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 13.83015 12.63196  25.92718  1.000 58.35221 ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.43814 14.06272  27.74612  1.000 54.27847 ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 16.70455 10.58108  25.34452  1.000 66.77285 ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.28579 9.28466   25.08846  1.000 70.07123 ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 18.78623 9.37695   24.94019  1.000 74.20730 ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.45053 10.20278  25.57815  1.000 74.93933 ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.32875 8.52907   24.07703  1.000 77.27873 ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 20.72130 8.64204   23.66273  1.000 80.58150 ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.03982 10.05939  23.18713  1.000 80.32155 ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.13269 10.88287  23.00016  1.000 80.79863 ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.01496 7.63516   22.54946  1.000 82.77678 ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 19.89651 7.48154   21.55960  1.000 85.60029 ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 18.68820 6.89769   21.88418  1.000 86.69709 ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 19.80572 7.83074   20.25158  1.000 86.92403 ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 17.90247 6.89450   20.82138  1.000 87.28793 ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 18.55770 7.45040   19.81477  1.000 87.64078 ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.33147 10.35307  22.99400  1.000 77.52584 ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 22.69638 11.60318  22.33570  1.000 73.37691 ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.05390 11.63484  20.94774  1.000 69.45211 ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.48551 10.93665  20.03533  1.000 71.51440 ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.22037 11.77232  22.24010  1.000 73.05268 ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 24.86209 13.06802  22.77012  1.000 72.29649 ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 25.27252 12.93840  24.26719  1.000 72.17642 ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.05025 13.48509  21.90920  1.000 71.01325 ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 20.96678 12.38510  20.81971  1.000 63.22054 ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 20.40787 12.67025  19.52896  1.000 53.84823 ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 21.24870 13.73925  18.85639  1.000 47.10848 ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 21.73300 14.67507  19.48226  1.000 47.53957 ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 21.42164 13.58512  17.55370  1.000 40.88940 ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.44179 14.35096  16.86433  1.000 34.92356 ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.17812 15.85251  16.91461  1.000 34.31127 ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.12105 16.62942  17.04242  1.000 37.37528 ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 22.54846 13.85340  15.42502  1.000 33.63501 ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 23.71813 14.36643  14.73614  1.000 34.13384 ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.94563 13.81794  14.98656  1.000 34.67891 ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 23.60792 15.43249  13.88147  1.000 35.66170 ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 26.08614 14.29651  14.40227  1.000 35.61201 ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 24.72938 15.90372  13.20522  1.000 38.17299 ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 25.99245 15.33453  13.49409  1.000 38.23793 ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 20.91139 16.29370  16.82172  1.000 31.78208 ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.59928 17.72155  16.82887  1.000 30.60844 ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 20.51104 18.31256  18.24718  1.000 34.91250 ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.30377 19.52435  18.40324  1.000 36.51457 ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.28812 17.95386  16.07982  1.000 30.01134 ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.45453 17.76131  14.57675  1.000 29.11636 ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.25176 18.63012  13.84774  1.000 29.14831 ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.82044 16.71876  13.88263  1.000 28.18959 ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.43194 18.46930  12.44977  1.000 28.98444 ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 19.01277 16.55129  12.48699  1.000 26.81523 ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.81541 17.43677  11.80216  1.000 28.24218 ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.01797 17.31343  10.43053  1.000 28.46200 ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 20.67747 17.49025  19.26531  1.000 35.32504 ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 20.56336 17.91290  20.66665  1.000 34.54184 ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 21.87716 18.50325  21.17002  1.000 38.06526 ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 22.95296 17.99042  20.86839  1.000 38.92966 ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 20.19143 16.69464  21.47993  1.000 31.62314 ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.79584 19.57891  21.95281  1.000 40.79420 ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.96728 20.18674  22.58596  1.000 41.18357 ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 23.00324 20.02832  24.08616  1.000 40.36117 ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.00212 20.42604  24.70348  1.000 41.71353 ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.03047 21.68956  22.30373  1.000 44.27952 ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.27164 21.99246  20.83453  1.000 48.25015 ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 23.80053 21.11516  20.11519  1.000 48.24858 ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 22.90495 23.10122  20.39467  1.000 51.24879 ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 21.92640 19.53979  24.68782  1.000 36.78269 ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.76198 19.56230  26.12630  1.000 40.08839 ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.24925 18.21316  26.57257  1.000 40.88048 ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.43375 17.58809  25.88635  1.000 40.31649 ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 20.78837 20.66800  26.55820  1.000 42.80537 ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.26741 21.99070  26.12329  1.000 47.17064 ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.04026 22.58325  24.92281  1.000 48.86583 ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.10381 22.89335  26.86951  1.000 50.67082 ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 21.67124 23.80755  24.86726  1.000 50.65983 ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.34176 24.01895  26.04384  1.000 52.15244 ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.67721 22.85759  28.14665  1.000 51.80129 ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.12143 25.10532  26.45734  1.000 53.46790 ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.45122 23.92591  28.55049  1.000 53.39066 ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.66327 25.04285  27.71030  1.000 53.75963 ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 21.74127 17.77829  27.70662  1.000 41.85004 ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.17855 16.66587  28.44206  1.000 42.32285 ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.13474 17.18357  29.41171  1.000 40.73193 ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.13421 18.36434  29.76939  1.000 40.79368 ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.27685 15.91655  29.19544  1.000 45.51630 ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 23.33393 15.29179  28.29123  1.000 48.72054 ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 24.20660 14.30173  29.05287  0.800 50.45613 ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.29169 14.64753  30.46742  0.700 52.41932 ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 25.09136 15.58111  30.96709  0.700 53.83315 ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 25.89611 16.29177  30.18837  0.700 54.86903 ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 25.07451 15.81539  32.27746  0.700 53.00155 ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.19442 16.33671  29.80153  1.000 40.91524 ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.13143 16.77830  30.73037  1.000 41.67748 ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 18.63888 17.41168  32.00988  1.000 44.64678 ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.00353 18.33225  32.53686  1.000 44.53795 ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.38048 15.47817  31.04923  1.000 41.56832 ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 17.63700 14.58412  29.89968  1.000 41.37629 ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.03835 14.93413  29.39372  1.000 40.72920 ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 19.76436 16.93207  32.53003  1.000 46.80534 ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.28144 17.43329  33.79893  1.000 47.97354 ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 20.61933 18.91724  33.72671  1.000 48.51393 ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 20.56946 19.61670  34.74524  1.000 50.41970 ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.51078 16.62049  34.19251  1.000 48.56759 ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 20.94725 19.41152  32.53993  1.000 46.94775 ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.32049 20.79852  32.31474  1.000 46.85744 ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.14587 21.69554  31.97106  1.000 46.40705 ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.36934 22.84206  31.56615  1.000 47.16987 ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.31835 20.89421  31.16506  1.000 50.28958 ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 23.61255 20.10689  31.34615  1.000 54.43369 ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.43450 20.09176  30.07029  1.000 56.59687 ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 23.90725 19.65075  29.01426  1.000 55.62538 ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 25.59264 20.55868  30.11591  1.000 58.84667 ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 18.91137 21.19953  32.08172  1.000 45.46540 ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 17.75942 21.99608  31.66938  1.000 46.12024 ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 17.68863 23.31872  32.41424  1.000 46.41847 ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.38301 24.35978  31.81975  1.000 44.55653 ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.47745 21.20771  31.89093  1.000 46.76287 ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 17.94177 23.29809  33.73185  1.000 48.11818 ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 17.83579 24.52879  34.49785  1.000 49.90717 ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 18.87951 25.53810  34.06488  1.000 47.57294 ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.59866 26.74366  34.02234  1.000 47.08195 ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 17.94761 24.21816  35.98233  1.000 56.47954 ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 16.72705 23.49558  36.49002  1.000 63.32226 ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 15.64801 23.73485  35.90026  1.000 65.11530 ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 16.83388 22.69338  37.45115  1.000 66.38527 ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.08187 25.06414  33.70668  1.000 45.42198 ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.12359 25.97782  33.25082  1.000 43.54351 ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.73143 26.61537  31.92208  1.000 42.68701 ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.01098 27.79611  31.68415  1.000 41.92673 ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.46511 25.24195  33.12418  1.000 42.89983 ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.06623 25.83623  31.05544  1.000 41.68501 ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.54501 26.33276  29.78836  1.000 40.51624 ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.46157 27.38760  29.99442  1.000 42.08596 ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.47913 28.44170  29.34691  1.000 43.68196 ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.00602 25.15898  28.97491  1.000 38.78521 ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.37718 25.44156  27.61370  1.000 39.12630 ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 19.33678 26.20972  26.72079  1.000 39.24731 ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.01850 24.11398  26.99220  1.000 38.68432 ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.48893 27.11334  30.87002  1.000 42.70355 ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.48160 28.12808  31.19111  1.000 43.42142 ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.15447 29.45602  31.51317  1.000 46.39498 ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.81835 30.50499  30.94595  1.000 46.51235 ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.59872 27.66184  32.36348  1.000 41.40402 ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.69928 28.80947  32.85595  1.000 39.73891 ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.76166 26.45056  31.94694  1.000 42.10900 ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.13579 29.41856  32.41850  1.000 48.59398 ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.80960 30.64145  32.84332  1.000 50.67325 ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.52381 31.31664  31.67623  1.000 51.42506 ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 19.29995 32.50198  31.40115  1.000 52.66782 ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.78281 30.32034  33.97874  1.000 52.22662 ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 20.45146 31.53791  34.59451  1.000 54.09669 ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 20.96789 31.24273  36.00924  1.000 54.86415 ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 22.22880 32.03591  36.30466  1.000 55.57719 ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 22.50181 32.17439  37.76778  1.000 56.84969 ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.37422 30.57109  30.96372  1.000 51.35625 ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 21.15367 31.17602  29.88133  1.000 51.43739 ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 20.23961 31.75761  28.81498  1.000 51.16967 ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 20.47200 32.86493  28.30989  1.000 48.45954 ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 22.09729 30.14009  29.27534  1.000 50.62258 ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 23.34394 29.85498  30.10221  1.000 51.57780 ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 24.16019 28.74276  29.46985  1.000 51.79900 ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 24.16152 31.14416  30.25659  1.000 52.05416 ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 19.16963 31.03232  28.49551  1.000 52.19266 ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 18.23197 31.47428  27.47934  1.000 52.88639 ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 17.48744 32.71001  27.93688  1.000 55.15551 ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 17.24765 33.62624  27.14280  1.000 55.00857 ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 17.26878 30.33671  27.18340  1.000 53.59748 ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 16.32641 30.31387  26.00251  1.000 54.52437 ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 17.05272 30.63544  24.69297  1.000 54.64263 ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 15.73793 28.90818  25.98613  1.000 54.17157 ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 17.12522 32.75567  29.22424  1.000 57.33100 ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 16.39239 33.90014  29.74251  1.000 60.71526 ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 17.17955 35.18275  29.54008  1.000 63.20473 ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 16.63601 36.19191  29.07292  1.000 64.27470 ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 16.06907 33.68812  31.21734  1.000 61.25478 ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 18.47151 35.15901  29.86529  1.000 64.22887 ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 19.27546 36.35963  29.68310  1.000 66.93392 ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 19.39894 36.71127  28.20886  1.000 69.33126 ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 19.18752 37.86270  27.81610  1.000 70.29077 ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 20.64818 36.17406  30.31006  1.000 68.32505 ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 21.64556 37.24837  29.90365  1.000 70.86394 ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 23.00002 36.96338  30.54013  1.000 72.47744 ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 24.12694 37.66677  29.82474  1.000 73.41527 ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 25.43487 37.20343  30.37005  1.000 74.84096 ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 19.71988 35.72500  27.37527  1.000 71.09834 ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.81593 35.93773  25.94612  1.000 72.26362 ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 21.24226 36.11342  25.48324  1.000 74.42437 ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 22.15508 35.46391  26.00328  1.000 75.01952 ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 21.44050 36.97864  24.48948  1.000 76.93002 ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 22.76011 37.33398  23.97079  1.000 79.82936 ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 23.54577 36.11902  23.46470  1.000 81.67754 ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 24.76672 36.20735  23.26040  1.000 84.83392 ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 23.57723 38.10053  25.01994  1.000 79.80295 ? 94  GLU A CB  1 
ATOM   741  N N   . TYR A 1 95  ? 22.86509 34.98653  23.25965  1.000 77.98332 ? 95  TYR A N   1 
ATOM   742  C CA  . TYR A 1 95  ? 23.46362 33.79070  22.67918  1.000 72.58847 ? 95  TYR A CA  1 
ATOM   743  C C   . TYR A 1 95  ? 23.77152 34.02226  21.20385  1.000 70.50371 ? 95  TYR A C   1 
ATOM   744  O O   . TYR A 1 95  ? 23.31256 34.98742  20.58551  1.000 72.31648 ? 95  TYR A O   1 
ATOM   745  C CB  . TYR A 1 95  ? 22.52172 32.59302  22.82005  1.000 69.16224 ? 95  TYR A CB  1 
ATOM   746  C CG  . TYR A 1 95  ? 21.11814 32.91512  22.35298  1.000 66.03931 ? 95  TYR A CG  1 
ATOM   747  C CD1 . TYR A 1 95  ? 20.75126 32.77396  21.02008  1.000 64.16006 ? 95  TYR A CD1 1 
ATOM   748  C CD2 . TYR A 1 95  ? 20.16858 33.39933  23.24413  1.000 65.54841 ? 95  TYR A CD2 1 
ATOM   749  C CE1 . TYR A 1 95  ? 19.47642 33.09144  20.59697  1.000 63.92228 ? 95  TYR A CE1 1 
ATOM   750  C CE2 . TYR A 1 95  ? 18.89174 33.70906  22.82868  1.000 65.37896 ? 95  TYR A CE2 1 
ATOM   751  C CZ  . TYR A 1 95  ? 18.55172 33.55717  21.50677  1.000 65.00120 ? 95  TYR A CZ  1 
ATOM   752  O OH  . TYR A 1 95  ? 17.27160 33.87550  21.11355  1.000 66.47975 ? 95  TYR A OH  1 
ATOM   753  N N   . GLN A 1 96  ? 24.53194 33.10155  20.62408  1.000 66.41353 ? 96  GLN A N   1 
ATOM   754  C CA  . GLN A 1 96  ? 24.92757 33.19703  19.22681  1.000 63.27508 ? 96  GLN A CA  1 
ATOM   755  C C   . GLN A 1 96  ? 24.11878 32.21059  18.39651  1.000 60.06592 ? 96  GLN A C   1 
ATOM   756  O O   . GLN A 1 96  ? 23.96251 31.04609  18.78339  1.000 61.43357 ? 96  GLN A O   1 
ATOM   757  C CB  . GLN A 1 96  ? 26.42371 32.93447  19.06384  1.000 63.14928 ? 96  GLN A CB  1 
ATOM   758  C CG  . GLN A 1 96  ? 27.30849 34.01705  19.66482  0.700 62.54158 ? 96  GLN A CG  1 
ATOM   759  C CD  . GLN A 1 96  ? 28.77028 33.64959  19.59525  0.600 62.41270 ? 96  GLN A CD  1 
ATOM   760  O OE1 . GLN A 1 96  ? 29.13031 32.61054  19.04278  0.600 62.20034 ? 96  GLN A OE1 1 
ATOM   761  N NE2 . GLN A 1 96  ? 29.62486 34.49614  20.15940  0.600 62.73953 ? 96  GLN A NE2 1 
ATOM   762  N N   . LYS A 1 97  ? 23.60191 32.68415  17.26482  1.000 55.10553 ? 97  LYS A N   1 
ATOM   763  C CA  . LYS A 1 97  ? 22.87700 31.83913  16.33246  1.000 51.47517 ? 97  LYS A CA  1 
ATOM   764  C C   . LYS A 1 97  ? 23.84984 31.26226  15.31105  1.000 48.75876 ? 97  LYS A C   1 
ATOM   765  O O   . LYS A 1 97  ? 24.75624 31.95353  14.83663  1.000 48.83435 ? 97  LYS A O   1 
ATOM   766  C CB  . LYS A 1 97  ? 21.76663 32.62903  15.63616  1.000 51.94933 ? 97  LYS A CB  1 
ATOM   767  C CG  . LYS A 1 97  ? 20.69127 33.14842  16.59683  1.000 53.24991 ? 97  LYS A CG  1 
ATOM   768  C CD  . LYS A 1 97  ? 19.56156 33.87496  15.86853  1.000 55.00725 ? 97  LYS A CD  1 
ATOM   769  C CE  . LYS A 1 97  ? 19.53655 35.36503  16.20925  1.000 56.22188 ? 97  LYS A CE  1 
ATOM   770  N NZ  . LYS A 1 97  ? 18.37590 36.09462  15.62094  1.000 57.12726 ? 97  LYS A NZ  1 
ATOM   771  N N   . VAL A 1 98  ? 23.69253 29.96711  15.04298  1.000 45.50216 ? 98  VAL A N   1 
ATOM   772  C CA  . VAL A 1 98  ? 24.41738 29.23012  14.01733  1.000 42.69096 ? 98  VAL A CA  1 
ATOM   773  C C   . VAL A 1 98  ? 23.37874 28.73974  13.01659  1.000 39.18425 ? 98  VAL A C   1 
ATOM   774  O O   . VAL A 1 98  ? 22.26208 28.38845  13.40938  1.000 38.13862 ? 98  VAL A O   1 
ATOM   775  C CB  . VAL A 1 98  ? 25.19378 28.06259  14.66362  1.000 44.15430 ? 98  VAL A CB  1 
ATOM   776  C CG1 . VAL A 1 98  ? 25.81231 27.18956  13.65106  1.000 46.32597 ? 98  VAL A CG1 1 
ATOM   777  C CG2 . VAL A 1 98  ? 26.27127 28.62102  15.57593  1.000 45.17778 ? 98  VAL A CG2 1 
ATOM   778  N N   . SER A 1 99  ? 23.71803 28.74316  11.72423  1.000 36.60121 ? 99  SER A N   1 
ATOM   779  C CA  . SER A 1 99  ? 22.77694 28.35140  10.68178  1.000 35.46778 ? 99  SER A CA  1 
ATOM   780  C C   . SER A 1 99  ? 23.28539 27.12941  9.92553   1.000 32.79080 ? 99  SER A C   1 
ATOM   781  O O   . SER A 1 99  ? 24.46694 27.06033  9.57005   1.000 33.66502 ? 99  SER A O   1 
ATOM   782  C CB  . SER A 1 99  ? 22.53004 29.51073  9.69980   1.000 39.54657 ? 99  SER A CB  1 
ATOM   783  O OG  . SER A 1 99  ? 22.08577 30.64965  10.42117  1.000 44.01613 ? 99  SER A OG  1 
ATOM   784  N N   . TYR A 1 100 ? 22.39263 26.15390  9.68420   1.000 31.53883 ? 100 TYR A N   1 
ATOM   785  C CA  . TYR A 1 100 ? 22.70949 25.03205  8.79028   1.000 31.01401 ? 100 TYR A CA  1 
ATOM   786  C C   . TYR A 1 100 ? 21.92241 25.13151  7.49113   1.000 29.80612 ? 100 TYR A C   1 
ATOM   787  O O   . TYR A 1 100 ? 20.78123 25.59603  7.48926   1.000 27.92415 ? 100 TYR A O   1 
ATOM   788  C CB  . TYR A 1 100 ? 22.39060 23.65744  9.38887   1.000 32.63730 ? 100 TYR A CB  1 
ATOM   789  C CG  . TYR A 1 100 ? 23.28152 23.20676  10.52086  1.000 35.14426 ? 100 TYR A CG  1 
ATOM   790  C CD1 . TYR A 1 100 ? 24.36222 23.97259  10.93088  1.000 38.10533 ? 100 TYR A CD1 1 
ATOM   791  C CD2 . TYR A 1 100 ? 23.06063 21.97914  11.14627  1.000 36.58854 ? 100 TYR A CD2 1 
ATOM   792  C CE1 . TYR A 1 100 ? 25.18666 23.54649  11.99717  1.000 39.86401 ? 100 TYR A CE1 1 
ATOM   793  C CE2 . TYR A 1 100 ? 23.86130 21.54804  12.18370  1.000 39.63269 ? 100 TYR A CE2 1 
ATOM   794  C CZ  . TYR A 1 100 ? 24.92590 22.31968  12.59398  1.000 42.02582 ? 100 TYR A CZ  1 
ATOM   795  O OH  . TYR A 1 100 ? 25.69140 21.84494  13.62845  1.000 45.40043 ? 100 TYR A OH  1 
ATOM   796  N N   . PRO A 1 101 ? 22.49672 24.64461  6.38699   1.000 29.92458 ? 101 PRO A N   1 
ATOM   797  C CA  . PRO A 1 101 ? 21.79461 24.66188  5.09765   1.000 28.36322 ? 101 PRO A CA  1 
ATOM   798  C C   . PRO A 1 101 ? 20.65047 23.66284  5.06794   1.000 27.18746 ? 101 PRO A C   1 
ATOM   799  O O   . PRO A 1 101 ? 20.63086 22.66777  5.80472   1.000 27.98017 ? 101 PRO A O   1 
ATOM   800  C CB  . PRO A 1 101 ? 22.88860 24.27079  4.09447   1.000 28.58347 ? 101 PRO A CB  1 
ATOM   801  C CG  . PRO A 1 101 ? 24.19950 24.50745  4.79960   1.000 28.37066 ? 101 PRO A CG  1 
ATOM   802  C CD  . PRO A 1 101 ? 23.89433 24.18658  6.24165   1.000 28.98735 ? 101 PRO A CD  1 
ATOM   803  N N   . LEU A 1 102 ? 19.68750 23.93450  4.18209   1.000 26.30866 ? 102 LEU A N   1 
ATOM   804  C CA  . LEU A 1 102 ? 18.51776 23.09257  3.99426   1.000 26.27851 ? 102 LEU A CA  1 
ATOM   805  C C   . LEU A 1 102 ? 18.39935 22.70790  2.52901   1.000 26.72294 ? 102 LEU A C   1 
ATOM   806  O O   . LEU A 1 102 ? 19.03969 23.30133  1.66044   1.000 27.90056 ? 102 LEU A O   1 
ATOM   807  C CB  . LEU A 1 102 ? 17.22722 23.78737  4.40948   1.000 25.81037 ? 102 LEU A CB  1 
ATOM   808  C CG  . LEU A 1 102 ? 17.22837 24.24633  5.87673   1.000 25.79639 ? 102 LEU A CG  1 
ATOM   809  C CD1 . LEU A 1 102 ? 16.01044 25.10983  6.18721   1.000 25.76651 ? 102 LEU A CD1 1 
ATOM   810  C CD2 . LEU A 1 102 ? 17.31934 23.02545  6.80413   1.000 26.27913 ? 102 LEU A CD2 1 
ATOM   811  N N   . LEU A 1 103 ? 17.55423 21.71413  2.27860   1.000 25.44286 ? 103 LEU A N   1 
ATOM   812  C CA  . LEU A 1 103 ? 17.36266 21.16292  0.93508   1.000 25.73768 ? 103 LEU A CA  1 
ATOM   813  C C   . LEU A 1 103 ? 15.95210 21.44865  0.46231   1.000 28.65324 ? 103 LEU A C   1 
ATOM   814  O O   . LEU A 1 103 ? 14.98212 21.15409  1.16740   1.000 29.77192 ? 103 LEU A O   1 
ATOM   815  C CB  . LEU A 1 103 ? 17.59436 19.65786  0.94318   1.000 25.38476 ? 103 LEU A CB  1 
ATOM   816  C CG  . LEU A 1 103 ? 17.24180 18.91213  -0.34526  1.000 25.20141 ? 103 LEU A CG  1 
ATOM   817  C CD1 . LEU A 1 103 ? 18.20505 19.32554  -1.48355  1.000 25.51064 ? 103 LEU A CD1 1 
ATOM   818  C CD2 . LEU A 1 103 ? 17.28176 17.40871  -0.10111  1.000 24.76482 ? 103 LEU A CD2 1 
ATOM   819  N N   . LYS A 1 104 ? 15.82233 21.95903  -0.75837  1.000 29.19437 ? 104 LYS A N   1 
ATOM   820  C CA  . LYS A 1 104 ? 14.51242 22.19473  -1.34777  1.000 29.11627 ? 104 LYS A CA  1 
ATOM   821  C C   . LYS A 1 104 ? 14.21277 21.08223  -2.34676  1.000 29.53757 ? 104 LYS A C   1 
ATOM   822  O O   . LYS A 1 104 ? 15.03250 20.80576  -3.23023  1.000 30.15120 ? 104 LYS A O   1 
ATOM   823  C CB  . LYS A 1 104 ? 14.48012 23.54770  -2.04946  1.000 29.83313 ? 104 LYS A CB  1 
ATOM   824  C CG  . LYS A 1 104 ? 13.11137 23.90440  -2.66393  1.000 30.97285 ? 104 LYS A CG  1 
ATOM   825  C CD  . LYS A 1 104 ? 13.24260 25.14947  -3.56145  0.900 32.28313 ? 104 LYS A CD  1 
ATOM   826  C CE  . LYS A 1 104 ? 11.92095 25.64606  -4.05062  0.800 35.74807 ? 104 LYS A CE  1 
ATOM   827  N NZ  . LYS A 1 104 ? 12.14476 26.72111  -5.06469  0.800 39.74700 ? 104 LYS A NZ  1 
ATOM   828  N N   . THR A 1 105 ? 13.05238 20.43875  -2.21025  1.000 29.58968 ? 105 THR A N   1 
ATOM   829  C CA  . THR A 1 105 ? 12.58434 19.45599  -3.19210  1.000 30.76239 ? 105 THR A CA  1 
ATOM   830  C C   . THR A 1 105 ? 11.34526 20.01159  -3.86931  1.000 31.58636 ? 105 THR A C   1 
ATOM   831  O O   . THR A 1 105 ? 10.41700 20.46149  -3.18936  1.000 33.17990 ? 105 THR A O   1 
ATOM   832  C CB  . THR A 1 105 ? 12.23955 18.11137  -2.53720  1.000 32.13114 ? 105 THR A CB  1 
ATOM   833  O OG1 . THR A 1 105 ? 13.35870 17.64499  -1.78381  1.000 34.02185 ? 105 THR A OG1 1 
ATOM   834  C CG2 . THR A 1 105 ? 11.85019 17.07233  -3.56738  1.000 32.04758 ? 105 THR A CG2 1 
ATOM   835  N N   . THR A 1 106 ? 11.32022 19.97640  -5.20292  1.000 31.03546 ? 106 THR A N   1 
ATOM   836  C CA  . THR A 1 106 ? 10.15006 20.37387  -5.95627  1.000 31.57509 ? 106 THR A CA  1 
ATOM   837  C C   . THR A 1 106 ? 9.66085  19.16383  -6.71660  1.000 32.82232 ? 106 THR A C   1 
ATOM   838  O O   . THR A 1 106 ? 10.44522 18.49629  -7.39687  1.000 33.38152 ? 106 THR A O   1 
ATOM   839  C CB  . THR A 1 106 ? 10.45090 21.51361  -6.91977  1.000 32.86344 ? 106 THR A CB  1 
ATOM   840  O OG1 . THR A 1 106 ? 10.99822 22.60167  -6.16522  1.000 35.89490 ? 106 THR A OG1 1 
ATOM   841  C CG2 . THR A 1 106 ? 9.15197  21.95721  -7.58962  1.000 32.09514 ? 106 THR A CG2 1 
ATOM   842  N N   . VAL A 1 107 ? 8.37573  18.88440  -6.60389  1.000 33.91884 ? 107 VAL A N   1 
ATOM   843  C CA  . VAL A 1 107 ? 7.74563  17.79534  -7.33484  1.000 35.84584 ? 107 VAL A CA  1 
ATOM   844  C C   . VAL A 1 107 ? 6.73559  18.41754  -8.28069  1.000 36.51254 ? 107 VAL A C   1 
ATOM   845  O O   . VAL A 1 107 ? 5.80231  19.10569  -7.84100  1.000 36.65045 ? 107 VAL A O   1 
ATOM   846  C CB  . VAL A 1 107 ? 7.07116  16.78285  -6.39201  1.000 35.90969 ? 107 VAL A CB  1 
ATOM   847  C CG1 . VAL A 1 107 ? 6.55629  15.60454  -7.19721  1.000 35.15783 ? 107 VAL A CG1 1 
ATOM   848  C CG2 . VAL A 1 107 ? 8.05184  16.32119  -5.29696  1.000 36.94276 ? 107 VAL A CG2 1 
ATOM   849  N N   . LYS A 1 108 ? 6.93819  18.19761  -9.57904  1.000 36.87958 ? 108 LYS A N   1 
ATOM   850  C CA  . LYS A 1 108 ? 6.05965  18.68787  -10.61886 1.000 40.67690 ? 108 LYS A CA  1 
ATOM   851  C C   . LYS A 1 108 ? 5.19962  17.53532  -11.12406 1.000 46.97857 ? 108 LYS A C   1 
ATOM   852  O O   . LYS A 1 108 ? 5.68048  16.40319  -11.23790 1.000 47.75784 ? 108 LYS A O   1 
ATOM   853  C CB  . LYS A 1 108 ? 6.89302  19.29475  -11.75437 1.000 39.85468 ? 108 LYS A CB  1 
ATOM   854  N N   . TYR A 1 109 ? 3.91853  17.82492  -11.39088 1.000 49.96577 ? 109 TYR A N   1 
ATOM   855  C CA  . TYR A 1 109 ? 2.94057  16.88329  -11.95455 1.000 54.90934 ? 109 TYR A CA  1 
ATOM   856  C C   . TYR A 1 109 ? 2.38425  17.30878  -13.31197 1.000 60.68969 ? 109 TYR A C   1 
ATOM   857  O O   . TYR A 1 109 ? 2.92749  18.20038  -13.97304 1.000 63.99628 ? 109 TYR A O   1 
ATOM   858  C CB  . TYR A 1 109 ? 1.74020  16.71479  -11.02952 1.000 51.67515 ? 109 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 109 ? 2.11253  16.53467  -9.57536  1.000 50.28194 ? 109 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 109 ? 2.35046  17.63452  -8.76068  1.000 50.18935 ? 109 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 109 ? 2.18131  15.27539  -9.01616  1.000 49.80321 ? 109 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 109 ? 2.66329  17.49038  -7.44735  1.000 51.13948 ? 109 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 109 ? 2.49205  15.11334  -7.69635  1.000 52.06217 ? 109 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 109 ? 2.73751  16.22468  -6.91018  1.000 53.55159 ? 109 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 109 ? 3.05488  16.05345  -5.58325  1.000 56.39503 ? 109 TYR A OH  1 
ATOM   866  N N   . GLY A 1 110 ? 1.27687  16.68096  -13.71594 1.000 62.05827 ? 110 GLY A N   1 
ATOM   867  C CA  . GLY A 1 110 ? 0.54062  17.06368  -14.91052 1.000 61.12473 ? 110 GLY A CA  1 
ATOM   868  C C   . GLY A 1 110 ? -0.95445 17.25284  -14.69232 1.000 61.27066 ? 110 GLY A C   1 
ATOM   869  O O   . GLY A 1 110 ? -1.69361 17.68135  -15.60538 1.000 59.97146 ? 110 GLY A O   1 
ATOM   870  N N   . LYS A 1 114 ? 0.88603  20.74249  -12.05681 1.000 62.68885 ? 114 LYS A N   1 
ATOM   871  C CA  . LYS A 1 114 ? 0.86509  21.25442  -10.68909 1.000 61.68827 ? 114 LYS A CA  1 
ATOM   872  C C   . LYS A 1 114 ? 2.22387  20.99434  -10.01004 1.000 60.32684 ? 114 LYS A C   1 
ATOM   873  O O   . LYS A 1 114 ? 3.06410  20.28489  -10.58002 1.000 60.34506 ? 114 LYS A O   1 
ATOM   874  C CB  . LYS A 1 114 ? -0.28700 20.62411  -9.90208  1.000 61.14493 ? 114 LYS A CB  1 
ATOM   875  C CG  . LYS A 1 114 ? -0.73201 21.47570  -8.72162  1.000 61.91014 ? 114 LYS A CG  1 
ATOM   876  C CD  . LYS A 1 114 ? -0.45964 22.94426  -9.01763  1.000 62.58545 ? 114 LYS A CD  1 
ATOM   877  C CE  . LYS A 1 114 ? 0.24404  23.66039  -7.87323  1.000 62.92747 ? 114 LYS A CE  1 
ATOM   878  N NZ  . LYS A 1 114 ? 0.81311  24.96491  -8.33993  1.000 64.04879 ? 114 LYS A NZ  1 
ATOM   879  N N   . GLU A 1 115 ? 2.43726  21.55069  -8.80799  1.000 56.91759 ? 115 GLU A N   1 
ATOM   880  C CA  . GLU A 1 115 ? 3.78030  21.58398  -8.23104  1.000 54.41287 ? 115 GLU A CA  1 
ATOM   881  C C   . GLU A 1 115 ? 3.73222  21.69794  -6.71319  1.000 49.32055 ? 115 GLU A C   1 
ATOM   882  O O   . GLU A 1 115 ? 3.03887  22.56575  -6.17444  1.000 51.49177 ? 115 GLU A O   1 
ATOM   883  C CB  . GLU A 1 115 ? 4.54492  22.76370  -8.80867  1.000 57.84342 ? 115 GLU A CB  1 
ATOM   884  C CG  . GLU A 1 115 ? 5.97552  22.77790  -8.44816  1.000 60.94576 ? 115 GLU A CG  1 
ATOM   885  C CD  . GLU A 1 115 ? 6.71859  23.96839  -9.00653  1.000 63.39333 ? 115 GLU A CD  1 
ATOM   886  O OE1 . GLU A 1 115 ? 7.20916  23.88016  -10.16111 1.000 64.12919 ? 115 GLU A OE1 1 
ATOM   887  O OE2 . GLU A 1 115 ? 6.82117  24.98642  -8.27636  1.000 64.34836 ? 115 GLU A OE2 1 
ATOM   888  N N   . ALA A 1 116 ? 4.49800  20.85473  -6.03099  1.000 44.08133 ? 116 ALA A N   1 
ATOM   889  C CA  . ALA A 1 116 ? 4.61702  20.87885  -4.58022  1.000 41.69608 ? 116 ALA A CA  1 
ATOM   890  C C   . ALA A 1 116 ? 6.07347  21.09630  -4.21388  1.000 39.59091 ? 116 ALA A C   1 
ATOM   891  O O   . ALA A 1 116 ? 6.95715  20.50324  -4.83472  1.000 39.07512 ? 116 ALA A O   1 
ATOM   892  C CB  . ALA A 1 116 ? 4.15801  19.56269  -3.97164  1.000 42.21902 ? 116 ALA A CB  1 
ATOM   893  N N   . THR A 1 117 ? 6.32823  21.90431  -3.18947  1.000 39.29871 ? 117 THR A N   1 
ATOM   894  C CA  . THR A 1 117 ? 7.68553  22.06183  -2.67538  1.000 39.81932 ? 117 THR A CA  1 
ATOM   895  C C   . THR A 1 117 ? 7.79138  21.59562  -1.22112  1.000 37.09549 ? 117 THR A C   1 
ATOM   896  O O   . THR A 1 117 ? 6.85935  21.75472  -0.42409  1.000 36.75006 ? 117 THR A O   1 
ATOM   897  C CB  . THR A 1 117 ? 8.17291  23.52209  -2.77468  1.000 43.28539 ? 117 THR A CB  1 
ATOM   898  O OG1 . THR A 1 117 ? 7.37245  24.36640  -1.94058  1.000 47.72862 ? 117 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 117 ? 8.09039  24.02652  -4.19587  1.000 41.28993 ? 117 THR A CG2 1 
ATOM   900  N N   . TYR A 1 118 ? 8.93953  21.02701  -0.87566  1.000 35.25261 ? 118 TYR A N   1 
ATOM   901  C CA  . TYR A 1 118 ? 9.19309  20.57205  0.48166   1.000 32.26034 ? 118 TYR A CA  1 
ATOM   902  C C   . TYR A 1 118 ? 10.56520 21.03338  0.91220   1.000 33.37357 ? 118 TYR A C   1 
ATOM   903  O O   . TYR A 1 118 ? 11.47724 21.18646  0.09474   1.000 35.09185 ? 118 TYR A O   1 
ATOM   904  C CB  . TYR A 1 118 ? 9.13525  19.05902  0.59736   1.000 32.02322 ? 118 TYR A CB  1 
ATOM   905  C CG  . TYR A 1 118 ? 7.86861  18.49380  0.04018   1.000 35.36427 ? 118 TYR A CG  1 
ATOM   906  C CD1 . TYR A 1 118 ? 7.78347  18.12202  -1.30025  1.000 37.93495 ? 118 TYR A CD1 1 
ATOM   907  C CD2 . TYR A 1 118 ? 6.74101  18.32679  0.84792   1.000 37.14163 ? 118 TYR A CD2 1 
ATOM   908  C CE1 . TYR A 1 118 ? 6.60980  17.61513  -1.82034  1.000 40.27594 ? 118 TYR A CE1 1 
ATOM   909  C CE2 . TYR A 1 118 ? 5.56794  17.81244  0.33483   1.000 38.42623 ? 118 TYR A CE2 1 
ATOM   910  C CZ  . TYR A 1 118 ? 5.50256  17.46988  -1.00580  1.000 40.03854 ? 118 TYR A CZ  1 
ATOM   911  O OH  . TYR A 1 118 ? 4.35708  16.94717  -1.53612  1.000 41.31595 ? 118 TYR A OH  1 
ATOM   912  N N   . LEU A 1 119 ? 10.71946 21.19119  2.21009   1.000 31.66594 ? 119 LEU A N   1 
ATOM   913  C CA  . LEU A 1 119 ? 11.99425 21.56546  2.79302   1.000 32.55070 ? 119 LEU A CA  1 
ATOM   914  C C   . LEU A 1 119 ? 12.45554 20.42998  3.68676   1.000 29.92825 ? 119 LEU A C   1 
ATOM   915  O O   . LEU A 1 119 ? 11.64642 19.87920  4.42669   1.000 30.26689 ? 119 LEU A O   1 
ATOM   916  C CB  . LEU A 1 119 ? 11.81780 22.85833  3.55425   1.000 36.31096 ? 119 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 119 ? 12.95841 23.83386  3.69421   1.000 40.14562 ? 119 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 119 ? 13.45631 24.31102  2.35041   1.000 40.10524 ? 119 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 119 ? 12.48559 25.00260  4.55909   1.000 42.41092 ? 119 LEU A CD2 1 
ATOM   920  N N   . ALA A 1 120 ? 13.72655 20.03724  3.56760   1.000 28.08048 ? 120 ALA A N   1 
ATOM   921  C CA  . ALA A 1 120 ? 14.30390 18.96519  4.37220   1.000 26.74974 ? 120 ALA A CA  1 
ATOM   922  C C   . ALA A 1 120 ? 15.48652 19.45295  5.20285   1.000 26.97174 ? 120 ALA A C   1 
ATOM   923  O O   . ALA A 1 120 ? 16.34674 20.19948  4.70961   1.000 26.66889 ? 120 ALA A O   1 
ATOM   924  C CB  . ALA A 1 120 ? 14.78370 17.80572  3.51659   1.000 25.73186 ? 120 ALA A CB  1 
ATOM   925  N N   . LEU A 1 121 ? 15.55157 18.98062  6.44918   1.000 26.02498 ? 121 LEU A N   1 
ATOM   926  C CA  . LEU A 1 121 ? 16.70117 19.20544  7.31539   1.000 25.11751 ? 121 LEU A CA  1 
ATOM   927  C C   . LEU A 1 121 ? 17.67148 18.03655  7.25283   1.000 25.19572 ? 121 LEU A C   1 
ATOM   928  O O   . LEU A 1 121 ? 18.90386 18.23045  7.36854   1.000 25.82254 ? 121 LEU A O   1 
ATOM   929  C CB  . LEU A 1 121 ? 16.21143 19.44819  8.76000   1.000 26.15644 ? 121 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 121 ? 17.28329 19.48442  9.85773   1.000 27.88099 ? 121 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 121 ? 18.25952 20.59157  9.60480   1.000 25.62073 ? 121 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 121 ? 16.57705 19.70723  11.20411  1.000 29.00592 ? 121 LEU A CD2 1 
ATOM   933  N N   . ASN A 1 122 ? 17.15747 16.82286  7.07322   1.000 23.52974 ? 122 ASN A N   1 
ATOM   934  C CA  . ASN A 1 122 ? 18.02427 15.66281  6.91284   1.000 23.21788 ? 122 ASN A CA  1 
ATOM   935  C C   . ASN A 1 122 ? 18.16451 15.31302  5.43416   1.000 23.10605 ? 122 ASN A C   1 
ATOM   936  O O   . ASN A 1 122 ? 19.24516 15.44345  4.86810   1.000 23.35915 ? 122 ASN A O   1 
ATOM   937  C CB  . ASN A 1 122 ? 17.47702 14.45586  7.65176   1.000 23.85202 ? 122 ASN A CB  1 
ATOM   938  C CG  . ASN A 1 122 ? 18.09253 14.27574  9.03980   1.000 25.83957 ? 122 ASN A CG  1 
ATOM   939  O OD1 . ASN A 1 122 ? 18.95524 15.06516  9.50216   1.000 25.95449 ? 122 ASN A OD1 1 
ATOM   940  N ND2 . ASN A 1 122 ? 17.68979 13.20895  9.69135   1.000 26.66144 ? 122 ASN A ND2 1 
ATOM   941  N N   . GLU A 1 123 ? 17.10433 14.82441  4.81992   1.000 22.42263 ? 123 GLU A N   1 
ATOM   942  C CA  . GLU A 1 123 ? 17.25479 14.39692  3.42246   1.000 23.01028 ? 123 GLU A CA  1 
ATOM   943  C C   . GLU A 1 123 ? 15.89442 14.23373  2.77051   1.000 23.88820 ? 123 GLU A C   1 
ATOM   944  O O   . GLU A 1 123 ? 14.85303 14.19609  3.42671   1.000 25.62212 ? 123 GLU A O   1 
ATOM   945  C CB  . GLU A 1 123 ? 18.02640 13.07144  3.29918   1.000 23.80053 ? 123 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 123 ? 17.19815 11.87119  3.72420   1.000 25.06156 ? 123 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 123 ? 17.06170 11.77092  5.22645   1.000 27.01901 ? 123 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 123 ? 18.11440 11.66479  5.92242   1.000 25.87327 ? 123 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 123 ? 15.88809 11.81554  5.69573   1.000 29.27436 ? 123 GLU A OE2 1 
ATOM   950  N N   . SER A 1 124 ? 15.92560 14.11974  1.44391   1.000 23.01471 ? 124 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 14.75561 13.72939  0.65895   1.000 24.47220 ? 124 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 15.12308 12.47609  -0.11698  1.000 26.90578 ? 124 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 16.19613 12.42789  -0.72051  1.000 28.01833 ? 124 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 14.36435 14.87397  -0.26434  1.000 26.34286 ? 124 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 13.22971 14.56982  -1.07194  1.000 29.41003 ? 124 SER A OG  1 
ATOM   956  N N   . THR A 1 125 ? 14.28576 11.44722  -0.07377  1.000 26.56818 ? 125 THR A N   1 
ATOM   957  C CA  . THR A 1 125 ? 14.59467 10.22764  -0.81768  1.000 26.50399 ? 125 THR A CA  1 
ATOM   958  C C   . THR A 1 125 ? 13.48122 9.94447   -1.79806  1.000 26.50429 ? 125 THR A C   1 
ATOM   959  O O   . THR A 1 125 ? 12.36314 10.41167  -1.64170  1.000 27.16119 ? 125 THR A O   1 
ATOM   960  C CB  . THR A 1 125 ? 14.78621 8.99458   0.08062   1.000 26.49291 ? 125 THR A CB  1 
ATOM   961  O OG1 . THR A 1 125 ? 13.52012 8.54477   0.55381   1.000 28.74926 ? 125 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 125 ? 15.70752 9.33171   1.24631   1.000 27.22922 ? 125 THR A CG2 1 
ATOM   963  N N   . VAL A 1 126 ? 13.82299 9.21773   -2.85462  1.000 26.35844 ? 126 VAL A N   1 
ATOM   964  C CA  . VAL A 1 126 ? 12.83142 8.81536   -3.83286  1.000 26.92975 ? 126 VAL A CA  1 
ATOM   965  C C   . VAL A 1 126 ? 13.00630 7.32733   -4.11779  1.000 27.68527 ? 126 VAL A C   1 
ATOM   966  O O   . VAL A 1 126 ? 14.13307 6.85022   -4.26875  1.000 27.29275 ? 126 VAL A O   1 
ATOM   967  C CB  . VAL A 1 126 ? 12.94069 9.68270   -5.09691  1.000 28.92228 ? 126 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 126 ? 14.29810 9.58070   -5.66597  1.000 33.69808 ? 126 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 126 ? 11.90061 9.23027   -6.10462  1.000 28.27753 ? 126 VAL A CG2 1 
ATOM   970  N N   . LYS A 1 127 ? 11.89935 6.58868   -4.11466  1.000 29.34163 ? 127 LYS A N   1 
ATOM   971  C CA  . LYS A 1 127 ? 11.83784 5.17631   -4.47653  1.000 31.10008 ? 127 LYS A CA  1 
ATOM   972  C C   . LYS A 1 127 ? 10.64065 4.97062   -5.40953  1.000 31.65413 ? 127 LYS A C   1 
ATOM   973  O O   . LYS A 1 127 ? 9.80428  5.85568   -5.58205  1.000 29.93563 ? 127 LYS A O   1 
ATOM   974  C CB  . LYS A 1 127 ? 11.71602 4.25149   -3.24646  1.000 32.73831 ? 127 LYS A CB  1 
ATOM   975  C CG  . LYS A 1 127 ? 12.85221 4.42099   -2.19971  1.000 36.08113 ? 127 LYS A CG  1 
ATOM   976  C CD  . LYS A 1 127 ? 12.64681 3.57796   -0.90910  1.000 41.23817 ? 127 LYS A CD  1 
ATOM   977  C CE  . LYS A 1 127 ? 13.80517 3.79320   0.11097   1.000 44.81970 ? 127 LYS A CE  1 
ATOM   978  N NZ  . LYS A 1 127 ? 13.70234 3.13766   1.48569   1.000 46.09874 ? 127 LYS A NZ  1 
ATOM   979  N N   . SER A 1 128 ? 10.53389 3.77620   -5.98079  1.000 34.17016 ? 128 SER A N   1 
ATOM   980  C CA  . SER A 1 128 ? 9.37976  3.49496   -6.82376  1.000 38.52421 ? 128 SER A CA  1 
ATOM   981  C C   . SER A 1 128 ? 8.19080  3.09453   -5.96920  1.000 42.07468 ? 128 SER A C   1 
ATOM   982  O O   . SER A 1 128 ? 8.33759  2.66786   -4.82875  1.000 43.91746 ? 128 SER A O   1 
ATOM   983  C CB  . SER A 1 128 ? 9.66937  2.36904   -7.80433  1.000 43.01226 ? 128 SER A CB  1 
ATOM   984  O OG  . SER A 1 128 ? 9.47832  1.11907   -7.15459  1.000 46.93192 ? 128 SER A OG  1 
ATOM   985  N N   . SER A 1 129 ? 6.99923  3.20801   -6.54458  1.000 46.25758 ? 129 SER A N   1 
ATOM   986  C CA  . SER A 1 129 ? 5.79274  2.80560   -5.83973  1.000 52.82800 ? 129 SER A CA  1 
ATOM   987  C C   . SER A 1 129 ? 5.48350  1.32065   -6.00234  1.000 59.25947 ? 129 SER A C   1 
ATOM   988  O O   . SER A 1 129 ? 4.31255  0.93698   -5.96301  1.000 61.76495 ? 129 SER A O   1 
ATOM   989  C CB  . SER A 1 129 ? 4.61611  3.63883   -6.32934  1.000 54.92058 ? 129 SER A CB  1 
ATOM   990  O OG  . SER A 1 129 ? 4.50823  3.48119   -7.73330  1.000 57.94067 ? 129 SER A OG  1 
ATOM   991  N N   . GLY A 1 130 ? 6.48904  0.47121   -6.20558  1.000 62.73392 ? 130 GLY A N   1 
ATOM   992  C CA  . GLY A 1 130 ? 6.22319  -0.94976  -6.36935  1.000 64.85316 ? 130 GLY A CA  1 
ATOM   993  C C   . GLY A 1 130 ? 7.03967  -1.63495  -7.44934  1.000 65.79964 ? 130 GLY A C   1 
ATOM   994  O O   . GLY A 1 130 ? 7.65406  -2.67907  -7.20296  1.000 68.71741 ? 130 GLY A O   1 
ATOM   995  N N   . GLY A 1 131 ? 7.05803  -1.06526  -8.65075  1.000 62.00871 ? 131 GLY A N   1 
ATOM   996  C CA  . GLY A 1 131 ? 7.83237  -1.62495  -9.73386  1.000 57.73887 ? 131 GLY A CA  1 
ATOM   997  C C   . GLY A 1 131 ? 9.28839  -1.21763  -9.64494  1.000 53.71332 ? 131 GLY A C   1 
ATOM   998  O O   . GLY A 1 131 ? 9.73353  -0.65625  -8.64002  1.000 54.65151 ? 131 GLY A O   1 
ATOM   999  N N   . PRO A 1 132 ? 10.06782 -1.50890  -10.68378 1.000 48.68316 ? 132 PRO A N   1 
ATOM   1000 C CA  . PRO A 1 132 ? 11.46559 -1.06900  -10.68849 1.000 45.16110 ? 132 PRO A CA  1 
ATOM   1001 C C   . PRO A 1 132 ? 11.58506 0.45062   -10.74743 1.000 41.49964 ? 132 PRO A C   1 
ATOM   1002 O O   . PRO A 1 132 ? 10.77233 1.14803   -11.36408 1.000 44.00297 ? 132 PRO A O   1 
ATOM   1003 C CB  . PRO A 1 132 ? 12.04952 -1.72914  -11.94863 1.000 45.87628 ? 132 PRO A CB  1 
ATOM   1004 C CG  . PRO A 1 132 ? 10.90441 -2.10026  -12.76368 1.000 47.55936 ? 132 PRO A CG  1 
ATOM   1005 C CD  . PRO A 1 132 ? 9.75720  -2.36578  -11.83689 1.000 48.64972 ? 132 PRO A CD  1 
ATOM   1006 N N   . PHE A 1 133 ? 12.62090 0.96166   -10.09753 1.000 34.93896 ? 133 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 133 ? 12.88722 2.38911   -10.05481 1.000 31.76000 ? 133 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 133 ? 13.87669 2.73474   -11.15909 1.000 30.61483 ? 133 PHE A C   1 
ATOM   1009 O O   . PHE A 1 133 ? 15.00536 2.25381   -11.14303 1.000 31.11865 ? 133 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 133 ? 13.46453 2.77010   -8.68931  1.000 29.57794 ? 133 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 133 ? 13.82464 4.21508   -8.55280  1.000 28.67064 ? 133 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 133 ? 12.83827 5.18565   -8.45773  1.000 28.26441 ? 133 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 133 ? 15.15420 4.59658   -8.48272  1.000 28.33506 ? 133 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 133 ? 13.18112 6.52036   -8.31054  1.000 28.26856 ? 133 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 133 ? 15.51101 5.93029   -8.32841  1.000 28.40092 ? 133 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 133 ? 14.52515 6.89307   -8.22504  1.000 28.61095 ? 133 PHE A CZ  1 
ATOM   1017 N N   . VAL A 1 134 ? 13.44841 3.53382   -12.13847 1.000 29.90879 ? 134 VAL A N   1 
ATOM   1018 C CA  . VAL A 1 134 ? 14.34982 3.97345   -13.20174 1.000 29.97149 ? 134 VAL A CA  1 
ATOM   1019 C C   . VAL A 1 134 ? 14.11730 5.45519   -13.41525 1.000 30.59147 ? 134 VAL A C   1 
ATOM   1020 O O   . VAL A 1 134 ? 12.98944 5.86417   -13.70849 1.000 32.04499 ? 134 VAL A O   1 
ATOM   1021 C CB  . VAL A 1 134 ? 14.12545 3.22128   -14.52897 1.000 29.90711 ? 134 VAL A CB  1 
ATOM   1022 C CG1 . VAL A 1 134 ? 15.11295 3.69781   -15.61611 1.000 29.57479 ? 134 VAL A CG1 1 
ATOM   1023 C CG2 . VAL A 1 134 ? 14.21350 1.75102   -14.33249 1.000 29.81300 ? 134 VAL A CG2 1 
ATOM   1024 N N   . VAL A 1 135 ? 15.16446 6.26858   -13.27876 1.000 28.51343 ? 135 VAL A N   1 
ATOM   1025 C CA  . VAL A 1 135 ? 15.00999 7.69257   -13.56268 1.000 28.26301 ? 135 VAL A CA  1 
ATOM   1026 C C   . VAL A 1 135 ? 16.21145 8.20539   -14.32706 1.000 28.71442 ? 135 VAL A C   1 
ATOM   1027 O O   . VAL A 1 135 ? 17.33403 7.72935   -14.14989 1.000 29.98723 ? 135 VAL A O   1 
ATOM   1028 C CB  . VAL A 1 135 ? 14.82540 8.56496   -12.30098 1.000 27.52393 ? 135 VAL A CB  1 
ATOM   1029 C CG1 . VAL A 1 135 ? 13.50854 8.28386   -11.65262 1.000 29.98095 ? 135 VAL A CG1 1 
ATOM   1030 C CG2 . VAL A 1 135 ? 15.98253 8.37713   -11.34369 1.000 27.11516 ? 135 VAL A CG2 1 
ATOM   1031 N N   . ASP A 1 136 ? 15.98942 9.23900   -15.12830 1.000 28.04602 ? 136 ASP A N   1 
ATOM   1032 C CA  . ASP A 1 136 ? 17.10820 9.93055   -15.73870 1.000 28.89444 ? 136 ASP A CA  1 
ATOM   1033 C C   . ASP A 1 136 ? 17.53278 11.03194  -14.77820 1.000 27.00069 ? 136 ASP A C   1 
ATOM   1034 O O   . ASP A 1 136 ? 16.68892 11.76577  -14.26627 1.000 27.35666 ? 136 ASP A O   1 
ATOM   1035 C CB  . ASP A 1 136 ? 16.75131 10.48944  -17.11098 1.000 32.75003 ? 136 ASP A CB  1 
ATOM   1036 C CG  . ASP A 1 136 ? 16.78082 9.41800   -18.19486 1.000 37.23444 ? 136 ASP A CG  1 
ATOM   1037 O OD1 . ASP A 1 136 ? 17.66730 8.54279   -18.13538 1.000 40.53596 ? 136 ASP A OD1 1 
ATOM   1038 O OD2 . ASP A 1 136 ? 15.91655 9.43447   -19.11591 1.000 37.84102 ? 136 ASP A OD2 1 
ATOM   1039 N N   . VAL A 1 137 ? 18.82869 11.12901  -14.52219 1.000 25.35156 ? 137 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 137 ? 19.37054 12.12704  -13.61554 1.000 25.77831 ? 137 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 137 ? 19.94131 13.23573  -14.46697 1.000 26.77954 ? 137 VAL A C   1 
ATOM   1042 O O   . VAL A 1 137 ? 20.85237 12.99090  -15.27214 1.000 27.88783 ? 137 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 137 ? 20.45830 11.52649  -12.71440 1.000 24.96324 ? 137 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 137 ? 21.06710 12.58333  -11.81163 1.000 24.70498 ? 137 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 137 ? 19.89110 10.37849  -11.90450 1.000 26.33244 ? 137 VAL A CG2 1 
ATOM   1046 N N   . VAL A 1 138 ? 19.42303 14.44581  -14.29942 1.000 26.40454 ? 138 VAL A N   1 
ATOM   1047 C CA  . VAL A 1 138 ? 19.79414 15.59018  -15.13384 1.000 26.98005 ? 138 VAL A CA  1 
ATOM   1048 C C   . VAL A 1 138 ? 20.36034 16.67065  -14.21547 1.000 27.86055 ? 138 VAL A C   1 
ATOM   1049 O O   . VAL A 1 138 ? 19.68360 17.12567  -13.28522 1.000 30.67101 ? 138 VAL A O   1 
ATOM   1050 C CB  . VAL A 1 138 ? 18.58496 16.11380  -15.92165 1.000 28.17664 ? 138 VAL A CB  1 
ATOM   1051 C CG1 . VAL A 1 138 ? 18.96195 17.31988  -16.70669 1.000 28.14433 ? 138 VAL A CG1 1 
ATOM   1052 C CG2 . VAL A 1 138 ? 18.04764 15.01985  -16.84180 1.000 28.07700 ? 138 VAL A CG2 1 
ATOM   1053 N N   . ILE A 1 139 ? 21.59167 17.07936  -14.46496 1.000 25.42274 ? 139 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 139 ? 22.26167 18.04687  -13.61598 1.000 25.47399 ? 139 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 139 ? 22.41853 19.32508  -14.40377 1.000 27.55557 ? 139 ILE A C   1 
ATOM   1056 O O   . ILE A 1 139 ? 23.11526 19.33895  -15.42828 1.000 29.31372 ? 139 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 139 ? 23.62837 17.52944  -13.14916 1.000 25.74733 ? 139 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 139 ? 23.45959 16.18072  -12.44653 1.000 26.51854 ? 139 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 139 ? 24.28986 18.56838  -12.23705 1.000 25.37412 ? 139 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 139 ? 24.80516 15.46726  -12.14944 1.000 27.81030 ? 139 ILE A CD1 1 
ATOM   1061 N N   . ASN A 1 140 ? 21.79400 20.40398  -13.94220 1.000 27.94836 ? 140 ASN A N   1 
ATOM   1062 C CA  . ASN A 1 140 ? 21.87788 21.67681  -14.67345 1.000 30.64572 ? 140 ASN A CA  1 
ATOM   1063 C C   . ASN A 1 140 ? 21.57290 21.48103  -16.15708 1.000 32.73856 ? 140 ASN A C   1 
ATOM   1064 O O   . ASN A 1 140 ? 22.29190 21.97258  -17.02688 1.000 34.01855 ? 140 ASN A O   1 
ATOM   1065 C CB  . ASN A 1 140 ? 23.24806 22.32706  -14.50511 1.000 30.29364 ? 140 ASN A CB  1 
ATOM   1066 C CG  . ASN A 1 140 ? 23.57180 22.59700  -13.06558 1.000 31.91260 ? 140 ASN A CG  1 
ATOM   1067 O OD1 . ASN A 1 140 ? 22.68756 22.95433  -12.30168 1.000 32.49009 ? 140 ASN A OD1 1 
ATOM   1068 N ND2 . ASN A 1 140 ? 24.83785 22.43495  -12.68429 1.000 31.57048 ? 140 ASN A ND2 1 
ATOM   1069 N N   . ASP A 1 141 ? 20.52178 20.72447  -16.44888 1.000 34.59059 ? 141 ASP A N   1 
ATOM   1070 C CA  . ASP A 1 141 ? 20.05598 20.43095  -17.82017 1.000 38.15840 ? 141 ASP A CA  1 
ATOM   1071 C C   . ASP A 1 141 ? 20.95831 19.47657  -18.60523 1.000 38.75494 ? 141 ASP A C   1 
ATOM   1072 O O   . ASP A 1 141 ? 20.72038 19.27386  -19.82736 1.000 42.10375 ? 141 ASP A O   1 
ATOM   1073 C CB  . ASP A 1 141 ? 19.86675 21.70411  -18.65626 1.000 41.84078 ? 141 ASP A CB  1 
ATOM   1074 C CG  . ASP A 1 141 ? 18.85323 22.66936  -18.05192 0.700 44.51447 ? 141 ASP A CG  1 
ATOM   1075 O OD1 . ASP A 1 141 ? 18.01509 22.24922  -17.22224 0.700 45.53302 ? 141 ASP A OD1 1 
ATOM   1076 O OD2 . ASP A 1 141 ? 18.88404 23.85655  -18.43581 0.700 45.56595 ? 141 ASP A OD2 1 
ATOM   1077 N N   . ILE A 1 142 ? 21.98541 18.91716  -17.99389 1.000 37.02078 ? 142 ILE A N   1 
ATOM   1078 C CA  . ILE A 1 142 ? 22.90930 17.96723  -18.60532 1.000 37.22717 ? 142 ILE A CA  1 
ATOM   1079 C C   . ILE A 1 142 ? 22.45971 16.56964  -18.19750 1.000 32.33240 ? 142 ILE A C   1 
ATOM   1080 O O   . ILE A 1 142 ? 22.37276 16.26853  -16.99385 1.000 31.83042 ? 142 ILE A O   1 
ATOM   1081 C CB  . ILE A 1 142 ? 24.35319 18.22839  -18.13500 1.000 44.43866 ? 142 ILE A CB  1 
ATOM   1082 C CG1 . ILE A 1 142 ? 25.01069 19.41278  -18.87192 1.000 51.08449 ? 142 ILE A CG1 1 
ATOM   1083 C CG2 . ILE A 1 142 ? 25.19903 16.95888  -18.23881 1.000 44.53758 ? 142 ILE A CG2 1 
ATOM   1084 C CD1 . ILE A 1 142 ? 24.08497 20.34681  -19.62770 1.000 55.74858 ? 142 ILE A CD1 1 
ATOM   1085 N N   . HIS A 1 143 ? 22.15061 15.71827  -19.18140 1.000 30.01752 ? 143 HIS A N   1 
ATOM   1086 C CA  . HIS A 1 143 ? 21.76962 14.32651  -18.93777 1.000 28.60282 ? 143 HIS A CA  1 
ATOM   1087 C C   . HIS A 1 143 ? 22.99592 13.56143  -18.45788 1.000 28.98270 ? 143 HIS A C   1 
ATOM   1088 O O   . HIS A 1 143 ? 23.92871 13.30706  -19.23231 1.000 31.87484 ? 143 HIS A O   1 
ATOM   1089 C CB  . HIS A 1 143 ? 21.17690 13.68615  -20.20331 1.000 29.16420 ? 143 HIS A CB  1 
ATOM   1090 C CG  . HIS A 1 143 ? 19.74630 14.04837  -20.43805 0.700 33.57868 ? 143 HIS A CG  1 
ATOM   1091 N ND1 . HIS A 1 143 ? 19.29288 15.35278  -20.42580 0.700 34.61412 ? 143 HIS A ND1 1 
ATOM   1092 C CD2 . HIS A 1 143 ? 18.65841 13.27844  -20.67254 0.700 34.07251 ? 143 HIS A CD2 1 
ATOM   1093 C CE1 . HIS A 1 143 ? 17.99145 15.36878  -20.65535 0.700 31.89830 ? 143 HIS A CE1 1 
ATOM   1094 N NE2 . HIS A 1 143 ? 17.58576 14.12480  -20.82066 0.700 33.15717 ? 143 HIS A NE2 1 
ATOM   1095 N N   . PHE A 1 144 ? 22.99189 13.17992  -17.18660 1.000 25.46654 ? 144 PHE A N   1 
ATOM   1096 C CA  . PHE A 1 144 ? 24.17228 12.63659  -16.52696 1.000 25.07592 ? 144 PHE A CA  1 
ATOM   1097 C C   . PHE A 1 144 ? 24.17309 11.11368  -16.43300 1.000 25.80564 ? 144 PHE A C   1 
ATOM   1098 O O   . PHE A 1 144 ? 25.19997 10.48819  -16.71584 1.000 26.96506 ? 144 PHE A O   1 
ATOM   1099 C CB  . PHE A 1 144 ? 24.29639 13.23920  -15.11802 1.000 24.39990 ? 144 PHE A CB  1 
ATOM   1100 C CG  . PHE A 1 144 ? 25.46028 12.72673  -14.36317 1.000 24.68074 ? 144 PHE A CG  1 
ATOM   1101 C CD1 . PHE A 1 144 ? 26.73306 13.22863  -14.61924 1.000 26.00801 ? 144 PHE A CD1 1 
ATOM   1102 C CD2 . PHE A 1 144 ? 25.29252 11.75430  -13.38643 1.000 24.03889 ? 144 PHE A CD2 1 
ATOM   1103 C CE1 . PHE A 1 144 ? 27.82067 12.75614  -13.94648 1.000 27.91525 ? 144 PHE A CE1 1 
ATOM   1104 C CE2 . PHE A 1 144 ? 26.38001 11.27113  -12.65789 1.000 25.37440 ? 144 PHE A CE2 1 
ATOM   1105 C CZ  . PHE A 1 144 ? 27.65430 11.76620  -12.93810 1.000 28.41676 ? 144 PHE A CZ  1 
ATOM   1106 N N   . GLU A 1 145 ? 23.04712 10.49080  -16.06168 1.000 25.16092 ? 145 GLU A N   1 
ATOM   1107 C CA  . GLU A 1 145 ? 23.01643 9.03836   -16.00405 1.000 25.18467 ? 145 GLU A CA  1 
ATOM   1108 C C   . GLU A 1 145 ? 21.56458 8.61669   -16.00111 1.000 25.95475 ? 145 GLU A C   1 
ATOM   1109 O O   . GLU A 1 145 ? 20.68477 9.40905   -15.66206 1.000 28.26778 ? 145 GLU A O   1 
ATOM   1110 C CB  . GLU A 1 145 ? 23.74365 8.50298   -14.76087 1.000 26.64852 ? 145 GLU A CB  1 
ATOM   1111 C CG  . GLU A 1 145 ? 22.98640 8.84936   -13.46849 1.000 27.90599 ? 145 GLU A CG  1 
ATOM   1112 C CD  . GLU A 1 145 ? 23.69968 8.39293   -12.21296 1.000 30.73803 ? 145 GLU A CD  1 
ATOM   1113 O OE1 . GLU A 1 145 ? 24.79009 7.80752   -12.33190 1.000 32.25484 ? 145 GLU A OE1 1 
ATOM   1114 O OE2 . GLU A 1 145 ? 23.15158 8.63837   -11.11902 1.000 30.68819 ? 145 GLU A OE2 1 
ATOM   1115 N N   . ARG A 1 146 ? 21.32256 7.36137   -16.39768 1.000 26.04722 ? 146 ARG A N   1 
ATOM   1116 C CA  . ARG A 1 146 ? 20.04754 6.69140   -16.15033 1.000 26.48581 ? 146 ARG A CA  1 
ATOM   1117 C C   . ARG A 1 146 ? 20.24614 5.78922   -14.94595 1.000 28.62776 ? 146 ARG A C   1 
ATOM   1118 O O   . ARG A 1 146 ? 21.02331 4.82576   -14.99975 1.000 32.02764 ? 146 ARG A O   1 
ATOM   1119 C CB  . ARG A 1 146 ? 19.57096 5.87622   -17.34243 1.000 28.17526 ? 146 ARG A CB  1 
ATOM   1120 C CG  . ARG A 1 146 ? 18.20730 5.23603   -17.07665 1.000 28.52858 ? 146 ARG A CG  1 
ATOM   1121 C CD  . ARG A 1 146 ? 17.51315 4.76769   -18.32667 1.000 30.90960 ? 146 ARG A CD  1 
ATOM   1122 N NE  . ARG A 1 146 ? 17.05293 5.92365   -19.06644 1.000 33.60105 ? 146 ARG A NE  1 
ATOM   1123 C CZ  . ARG A 1 146 ? 16.38693 5.83501   -20.21172 1.000 37.62372 ? 146 ARG A CZ  1 
ATOM   1124 N NH1 . ARG A 1 146 ? 16.10440 4.65868   -20.75317 1.000 39.12459 ? 146 ARG A NH1 1 
ATOM   1125 N NH2 . ARG A 1 146 ? 15.96969 6.94993   -20.81147 1.000 39.00125 ? 146 ARG A NH2 1 
ATOM   1126 N N   . PHE A 1 147 ? 19.57655 6.11837   -13.85185 1.000 26.23349 ? 147 PHE A N   1 
ATOM   1127 C CA  . PHE A 1 147 ? 19.72925 5.36922   -12.61829 1.000 26.48171 ? 147 PHE A CA  1 
ATOM   1128 C C   . PHE A 1 147 ? 18.70894 4.24351   -12.55339 1.000 26.59633 ? 147 PHE A C   1 
ATOM   1129 O O   . PHE A 1 147 ? 17.51053 4.48273   -12.69765 1.000 25.94025 ? 147 PHE A O   1 
ATOM   1130 C CB  . PHE A 1 147 ? 19.54680 6.27241   -11.40196 1.000 25.48394 ? 147 PHE A CB  1 
ATOM   1131 C CG  . PHE A 1 147 ? 19.72814 5.52782   -10.11372 1.000 25.22469 ? 147 PHE A CG  1 
ATOM   1132 C CD1 . PHE A 1 147 ? 20.99238 5.33650   -9.58234  1.000 25.98595 ? 147 PHE A CD1 1 
ATOM   1133 C CD2 . PHE A 1 147 ? 18.64983 4.95633   -9.46772  1.000 25.42593 ? 147 PHE A CD2 1 
ATOM   1134 C CE1 . PHE A 1 147 ? 21.18148 4.62057   -8.42892  1.000 25.98950 ? 147 PHE A CE1 1 
ATOM   1135 C CE2 . PHE A 1 147 ? 18.84482 4.21594   -8.25721  1.000 25.28582 ? 147 PHE A CE2 1 
ATOM   1136 C CZ  . PHE A 1 147 ? 20.11054 4.05902   -7.76062  1.000 25.78170 ? 147 PHE A CZ  1 
ATOM   1137 N N   . ARG A 1 148 ? 19.18417 3.03228   -12.30933 1.000 27.24917 ? 148 ARG A N   1 
ATOM   1138 C CA  . ARG A 1 148 ? 18.33283 1.89326   -12.03839 1.000 28.52205 ? 148 ARG A CA  1 
ATOM   1139 C C   . ARG A 1 148 ? 18.76998 1.31341   -10.71279 1.000 27.13285 ? 148 ARG A C   1 
ATOM   1140 O O   . ARG A 1 148 ? 19.95797 1.06785   -10.51894 1.000 27.96365 ? 148 ARG A O   1 
ATOM   1141 C CB  . ARG A 1 148 ? 18.43756 0.81466   -13.11049 1.000 31.65724 ? 148 ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 148 ? 18.05072 1.27747   -14.42745 1.000 34.88396 ? 148 ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 148 ? 17.98371 0.06829   -15.34731 0.800 37.85771 ? 148 ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 148 ? 17.45160 0.42754   -16.65742 0.700 41.54586 ? 148 ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 148 ? 18.09331 1.18696   -17.53171 0.700 45.58505 ? 148 ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 148 ? 19.29229 1.68973   -17.26503 0.700 46.51563 ? 148 ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 148 ? 17.53173 1.43087   -18.71120 0.700 48.21085 ? 148 ARG A NH2 1 
ATOM   1148 N N   . GLY A 1 149 ? 17.82687 1.10834   -9.80597  1.000 27.05154 ? 149 GLY A N   1 
ATOM   1149 C CA  . GLY A 1 149 ? 18.18959 0.54837   -8.51010  1.000 27.72926 ? 149 GLY A CA  1 
ATOM   1150 C C   . GLY A 1 149 ? 17.02578 0.68801   -7.56506  1.000 26.40816 ? 149 GLY A C   1 
ATOM   1151 O O   . GLY A 1 149 ? 15.87574 0.76215   -7.99416  1.000 29.45180 ? 149 GLY A O   1 
ATOM   1152 N N   . ASP A 1 150 ? 17.33586 0.73567   -6.26345  1.000 24.76649 ? 150 ASP A N   1 
ATOM   1153 C CA  . ASP A 1 150 ? 16.24612 0.84542   -5.30044  1.000 25.42973 ? 150 ASP A CA  1 
ATOM   1154 C C   . ASP A 1 150 ? 15.77125 2.28053   -5.10489  1.000 26.35876 ? 150 ASP A C   1 
ATOM   1155 O O   . ASP A 1 150 ? 14.60422 2.48932   -4.76922  1.000 28.62715 ? 150 ASP A O   1 
ATOM   1156 C CB  . ASP A 1 150 ? 16.66093 0.29114   -3.93019  1.000 27.10776 ? 150 ASP A CB  1 
ATOM   1157 C CG  . ASP A 1 150 ? 16.72328 -1.20506  -3.89523  1.000 29.92360 ? 150 ASP A CG  1 
ATOM   1158 O OD1 . ASP A 1 150 ? 16.33799 -1.83792  -4.90110  1.000 31.38530 ? 150 ASP A OD1 1 
ATOM   1159 O OD2 . ASP A 1 150 ? 17.13040 -1.75050  -2.83403  1.000 31.73169 ? 150 ASP A OD2 1 
ATOM   1160 N N   . GLY A 1 151 ? 16.63905 3.26934   -5.24042  1.000 24.03018 ? 151 GLY A N   1 
ATOM   1161 C CA  . GLY A 1 151 ? 16.22657 4.63849   -4.98527  1.000 21.95159 ? 151 GLY A CA  1 
ATOM   1162 C C   . GLY A 1 151 ? 17.41982 5.55903   -4.87376  1.000 21.87803 ? 151 GLY A C   1 
ATOM   1163 O O   . GLY A 1 151 ? 18.56375 5.15429   -5.06937  1.000 24.00869 ? 151 GLY A O   1 
ATOM   1164 N N   . LEU A 1 152 ? 17.13013 6.81906   -4.59386  1.000 21.71183 ? 152 LEU A N   1 
ATOM   1165 C CA  . LEU A 1 152 ? 18.14601 7.85933   -4.48059  1.000 21.96080 ? 152 LEU A CA  1 
ATOM   1166 C C   . LEU A 1 152 ? 17.88098 8.65446   -3.20114  1.000 21.54886 ? 152 LEU A C   1 
ATOM   1167 O O   . LEU A 1 152 ? 16.74294 8.75661   -2.74692  1.000 23.17328 ? 152 LEU A O   1 
ATOM   1168 C CB  . LEU A 1 152 ? 18.13796 8.78544   -5.70135  1.000 23.26521 ? 152 LEU A CB  1 
ATOM   1169 C CG  . LEU A 1 152 ? 18.66346 8.14112   -6.99359  1.000 24.78218 ? 152 LEU A CG  1 
ATOM   1170 C CD1 . LEU A 1 152 ? 18.28809 9.03421   -8.19168  1.000 26.70574 ? 152 LEU A CD1 1 
ATOM   1171 C CD2 . LEU A 1 152 ? 20.17387 7.91745   -6.94224  1.000 24.53579 ? 152 LEU A CD2 1 
ATOM   1172 N N   . CYS A 1 153 ? 18.92953 9.18120   -2.59321  1.000 21.30066 ? 153 CYS A N   1 
ATOM   1173 C CA  . CYS A 1 153 ? 18.83562 9.98691   -1.37889  1.000 22.50987 ? 153 CYS A CA  1 
ATOM   1174 C C   . CYS A 1 153 ? 19.59699 11.28354  -1.59359  1.000 22.57181 ? 153 CYS A C   1 
ATOM   1175 O O   . CYS A 1 153 ? 20.77220 11.25379  -1.99279  1.000 22.55442 ? 153 CYS A O   1 
ATOM   1176 C CB  . CYS A 1 153 ? 19.45958 9.20812   -0.21729  1.000 22.83771 ? 153 CYS A CB  1 
ATOM   1177 S SG  . CYS A 1 153 ? 19.58715 10.16603  1.32248   1.000 24.44816 ? 153 CYS A SG  1 
ATOM   1178 N N   . MET A 1 154 ? 18.94484 12.40972  -1.36207  1.000 21.53176 ? 154 MET A N   1 
ATOM   1179 C CA  . MET A 1 154 ? 19.61721 13.70107  -1.42729  1.000 21.93653 ? 154 MET A CA  1 
ATOM   1180 C C   . MET A 1 154 ? 19.66175 14.29694  -0.03446  1.000 21.92270 ? 154 MET A C   1 
ATOM   1181 O O   . MET A 1 154 ? 18.60128 14.52847  0.55061   1.000 22.82813 ? 154 MET A O   1 
ATOM   1182 C CB  . MET A 1 154 ? 18.88769 14.67313  -2.34156  1.000 22.22509 ? 154 MET A CB  1 
ATOM   1183 C CG  . MET A 1 154 ? 19.71608 15.94465  -2.56252  1.000 23.50636 ? 154 MET A CG  1 
ATOM   1184 S SD  . MET A 1 154 ? 21.23016 15.71750  -3.53491  1.000 24.39427 ? 154 MET A SD  1 
ATOM   1185 C CE  . MET A 1 154 ? 20.60208 15.95720  -5.23004  1.000 25.10188 ? 154 MET A CE  1 
ATOM   1186 N N   . SER A 1 155 ? 20.86027 14.60286  0.45058   1.000 21.83425 ? 155 SER A N   1 
ATOM   1187 C CA  . SER A 1 155 ? 21.05698 14.94877  1.86193   1.000 22.18375 ? 155 SER A CA  1 
ATOM   1188 C C   . SER A 1 155 ? 21.55624 16.38331  2.01589   1.000 22.62841 ? 155 SER A C   1 
ATOM   1189 O O   . SER A 1 155 ? 22.29031 16.90591  1.17255   1.000 23.54008 ? 155 SER A O   1 
ATOM   1190 C CB  . SER A 1 155 ? 22.04813 13.97535  2.48676   1.000 23.45741 ? 155 SER A CB  1 
ATOM   1191 O OG  . SER A 1 155 ? 22.34301 14.31476  3.84395   1.000 27.09837 ? 155 SER A OG  1 
ATOM   1192 N N   . THR A 1 156 ? 21.15715 17.03195  3.10020   1.000 22.03388 ? 156 THR A N   1 
ATOM   1193 C CA  . THR A 1 156 ? 21.80343 18.26009  3.55175   1.000 22.10177 ? 156 THR A CA  1 
ATOM   1194 C C   . THR A 1 156 ? 23.12550 17.93433  4.25482   1.000 23.07962 ? 156 THR A C   1 
ATOM   1195 O O   . THR A 1 156 ? 23.42718 16.77611  4.53907   1.000 24.21780 ? 156 THR A O   1 
ATOM   1196 C CB  . THR A 1 156 ? 20.91359 18.97536  4.56956   1.000 22.03746 ? 156 THR A CB  1 
ATOM   1197 O OG1 . THR A 1 156 ? 20.89512 18.14502  5.71912   1.000 23.74612 ? 156 THR A OG1 1 
ATOM   1198 C CG2 . THR A 1 156 ? 19.49395 19.17482  4.10387   1.000 21.11663 ? 156 THR A CG2 1 
ATOM   1199 N N   . PRO A 1 157 ? 23.94818 18.93850  4.54683   1.000 22.73497 ? 157 PRO A N   1 
ATOM   1200 C CA  . PRO A 1 157 ? 25.17578 18.67114  5.33890   1.000 22.12489 ? 157 PRO A CA  1 
ATOM   1201 C C   . PRO A 1 157 ? 24.87720 18.02288  6.67571   1.000 22.70011 ? 157 PRO A C   1 
ATOM   1202 O O   . PRO A 1 157 ? 25.48139 16.99167  7.00612   1.000 24.09155 ? 157 PRO A O   1 
ATOM   1203 C CB  . PRO A 1 157 ? 25.79070 20.06712  5.47241   1.000 22.89776 ? 157 PRO A CB  1 
ATOM   1204 C CG  . PRO A 1 157 ? 25.31250 20.78409  4.23977   1.000 24.80816 ? 157 PRO A CG  1 
ATOM   1205 C CD  . PRO A 1 157 ? 23.89832 20.33651  4.08186   1.000 24.27577 ? 157 PRO A CD  1 
ATOM   1206 N N   . SER A 1 158 ? 23.91218 18.54738  7.42878   1.000 24.24151 ? 158 SER A N   1 
ATOM   1207 C CA  . SER A 1 158 ? 23.63279 17.94441  8.73634   1.000 23.71482 ? 158 SER A CA  1 
ATOM   1208 C C   . SER A 1 158 ? 22.98146 16.57751  8.56461   1.000 21.70101 ? 158 SER A C   1 
ATOM   1209 O O   . SER A 1 158 ? 23.06558 15.72602  9.46546   1.000 23.50977 ? 158 SER A O   1 
ATOM   1210 C CB  . SER A 1 158 ? 22.81507 18.89313  9.62649   1.000 25.81476 ? 158 SER A CB  1 
ATOM   1211 O OG  . SER A 1 158 ? 21.54284 19.23300  9.10095   1.000 26.65865 ? 158 SER A OG  1 
ATOM   1212 N N   . GLY A 1 159 ? 22.31433 16.34737  7.43237   1.000 20.55289 ? 159 GLY A N   1 
ATOM   1213 C CA  . GLY A 1 159 ? 21.77865 15.01941  7.16410   1.000 20.46578 ? 159 GLY A CA  1 
ATOM   1214 C C   . GLY A 1 159 ? 22.81747 14.01912  6.72958   1.000 21.43037 ? 159 GLY A C   1 
ATOM   1215 O O   . GLY A 1 159 ? 22.51067 12.82495  6.65872   1.000 22.87560 ? 159 GLY A O   1 
ATOM   1216 N N   . THR A 1 160 ? 24.05925 14.44974  6.50549   1.000 22.01201 ? 160 THR A N   1 
ATOM   1217 C CA  . THR A 1 160 ? 25.01664 13.49544  5.96718   1.000 22.40240 ? 160 THR A CA  1 
ATOM   1218 C C   . THR A 1 160 ? 25.38301 12.43943  6.98999   1.000 21.32065 ? 160 THR A C   1 
ATOM   1219 O O   . THR A 1 160 ? 25.81877 11.35873  6.60909   1.000 21.37311 ? 160 THR A O   1 
ATOM   1220 C CB  . THR A 1 160 ? 26.30840 14.16400  5.43400   1.000 23.17731 ? 160 THR A CB  1 
ATOM   1221 O OG1 . THR A 1 160 ? 26.95318 14.93872  6.44712   1.000 23.36149 ? 160 THR A OG1 1 
ATOM   1222 C CG2 . THR A 1 160 ? 26.02830 15.04171  4.20221   1.000 23.04897 ? 160 THR A CG2 1 
ATOM   1223 N N   . THR A 1 161 ? 25.14104 12.69195  8.27094   1.000 20.81559 ? 161 THR A N   1 
ATOM   1224 C CA  . THR A 1 161 ? 25.38461 11.66839  9.27629   1.000 22.67187 ? 161 THR A CA  1 
ATOM   1225 C C   . THR A 1 161 ? 24.18786 10.74056  9.47547   1.000 23.29147 ? 161 THR A C   1 
ATOM   1226 O O   . THR A 1 161 ? 24.23500 9.86237   10.35959  1.000 25.52462 ? 161 THR A O   1 
ATOM   1227 C CB  . THR A 1 161 ? 25.73194 12.34071  10.62177  1.000 25.00992 ? 161 THR A CB  1 
ATOM   1228 O OG1 . THR A 1 161 ? 24.86943 13.47008  10.79813  1.000 26.93473 ? 161 THR A OG1 1 
ATOM   1229 C CG2 . THR A 1 161 ? 27.13922 12.85140  10.61391  1.000 25.04160 ? 161 THR A CG2 1 
ATOM   1230 N N   . ALA A 1 162 ? 23.11085 10.92834  8.72256   1.000 22.91136 ? 162 ALA A N   1 
ATOM   1231 C CA  . ALA A 1 162 ? 21.87764 10.16871  8.88472   1.000 24.49558 ? 162 ALA A CA  1 
ATOM   1232 C C   . ALA A 1 162 ? 21.80856 9.09114   7.79143   1.000 25.45432 ? 162 ALA A C   1 
ATOM   1233 O O   . ALA A 1 162 ? 22.79244 8.33980   7.63543   1.000 25.11128 ? 162 ALA A O   1 
ATOM   1234 C CB  . ALA A 1 162 ? 20.68333 11.14257  8.88408   1.000 23.18930 ? 162 ALA A CB  1 
ATOM   1235 N N   . TYR A 1 163 ? 20.71984 8.99094   7.04435   1.000 23.32553 ? 163 TYR A N   1 
ATOM   1236 C CA  . TYR A 1 163 ? 20.55194 7.97179   6.01521   1.000 21.61435 ? 163 TYR A CA  1 
ATOM   1237 C C   . TYR A 1 163 ? 21.71076 8.00148   5.03286   1.000 20.17018 ? 163 TYR A C   1 
ATOM   1238 O O   . TYR A 1 163 ? 22.24384 6.96483   4.65978   1.000 20.05003 ? 163 TYR A O   1 
ATOM   1239 C CB  . TYR A 1 163 ? 19.23568 8.23400   5.29694   1.000 21.58282 ? 163 TYR A CB  1 
ATOM   1240 C CG  . TYR A 1 163 ? 18.56609 7.09877   4.56988   1.000 23.58823 ? 163 TYR A CG  1 
ATOM   1241 C CD1 . TYR A 1 163 ? 19.13481 5.84416   4.45348   1.000 24.08493 ? 163 TYR A CD1 1 
ATOM   1242 C CD2 . TYR A 1 163 ? 17.28433 7.27793   4.05705   1.000 27.57259 ? 163 TYR A CD2 1 
ATOM   1243 C CE1 . TYR A 1 163 ? 18.45815 4.80287   3.79268   1.000 24.76558 ? 163 TYR A CE1 1 
ATOM   1244 C CE2 . TYR A 1 163 ? 16.62195 6.26622   3.35669   1.000 30.13383 ? 163 TYR A CE2 1 
ATOM   1245 C CZ  . TYR A 1 163 ? 17.20751 5.03435   3.24223   1.000 31.22007 ? 163 TYR A CZ  1 
ATOM   1246 O OH  . TYR A 1 163 ? 16.52841 4.04600   2.56668   1.000 36.75878 ? 163 TYR A OH  1 
ATOM   1247 N N   . ASN A 1 164 ? 22.15405 9.19460   4.67004   1.000 19.12779 ? 164 ASN A N   1 
ATOM   1248 C CA  . ASN A 1 164 ? 23.30051 9.35479   3.77374   1.000 19.75160 ? 164 ASN A CA  1 
ATOM   1249 C C   . ASN A 1 164 ? 24.47780 8.50491   4.21152   1.000 21.73612 ? 164 ASN A C   1 
ATOM   1250 O O   . ASN A 1 164 ? 25.14325 7.85438   3.38371   1.000 22.85233 ? 164 ASN A O   1 
ATOM   1251 C CB  . ASN A 1 164 ? 23.69443 10.83418  3.75575   1.000 21.39667 ? 164 ASN A CB  1 
ATOM   1252 C CG  . ASN A 1 164 ? 24.99912 11.09979  3.03176   1.000 23.45504 ? 164 ASN A CG  1 
ATOM   1253 O OD1 . ASN A 1 164 ? 24.99353 11.27650  1.80852   1.000 25.60580 ? 164 ASN A OD1 1 
ATOM   1254 N ND2 . ASN A 1 164 ? 26.12175 11.20170  3.77041   1.000 23.28181 ? 164 ASN A ND2 1 
ATOM   1255 N N   . LYS A 1 165 ? 24.74973 8.47738   5.52132   1.000 21.39562 ? 165 LYS A N   1 
ATOM   1256 C CA  . LYS A 1 165 ? 25.92659 7.76600   5.99551   1.000 20.79196 ? 165 LYS A CA  1 
ATOM   1257 C C   . LYS A 1 165 ? 25.77126 6.27237   5.74986   1.000 21.21262 ? 165 LYS A C   1 
ATOM   1258 O O   . LYS A 1 165 ? 26.72719 5.60177   5.36311   1.000 19.65259 ? 165 LYS A O   1 
ATOM   1259 C CB  . LYS A 1 165 ? 26.12762 8.05916   7.49736   1.000 21.32786 ? 165 LYS A CB  1 
ATOM   1260 C CG  . LYS A 1 165 ? 27.32034 7.35444   8.06116   1.000 21.45975 ? 165 LYS A CG  1 
ATOM   1261 C CD  . LYS A 1 165 ? 27.58294 7.88417   9.46235   1.000 22.08462 ? 165 LYS A CD  1 
ATOM   1262 C CE  . LYS A 1 165 ? 28.94396 7.45113   9.96536   1.000 26.78020 ? 165 LYS A CE  1 
ATOM   1263 N NZ  . LYS A 1 165 ? 29.07517 5.94952   10.09970  1.000 31.74484 ? 165 LYS A NZ  1 
ATOM   1264 N N   . SER A 1 166 ? 24.55912 5.73977   5.98324   1.000 21.87026 ? 166 SER A N   1 
ATOM   1265 C CA  . SER A 1 166 ? 24.30158 4.30743   5.80895   1.000 22.41404 ? 166 SER A CA  1 
ATOM   1266 C C   . SER A 1 166 ? 24.45362 3.87605   4.36615   1.000 23.44075 ? 166 SER A C   1 
ATOM   1267 O O   . SER A 1 166 ? 24.72384 2.70342   4.09565   1.000 23.61387 ? 166 SER A O   1 
ATOM   1268 C CB  . SER A 1 166 ? 22.87822 3.98523   6.28518   1.000 22.95570 ? 166 SER A CB  1 
ATOM   1269 O OG  . SER A 1 166 ? 22.77878 4.29335   7.67144   1.000 26.20749 ? 166 SER A OG  1 
ATOM   1270 N N   . LEU A 1 167 ? 24.25308 4.80223   3.44218   1.000 23.66838 ? 167 LEU A N   1 
ATOM   1271 C CA  . LEU A 1 167 ? 24.36619 4.55799   1.99885   1.000 23.99762 ? 167 LEU A CA  1 
ATOM   1272 C C   . LEU A 1 167 ? 25.76203 4.81015   1.47083   1.000 25.05570 ? 167 LEU A C   1 
ATOM   1273 O O   . LEU A 1 167 ? 25.98288 4.76530   0.23769   1.000 26.88061 ? 167 LEU A O   1 
ATOM   1274 C CB  . LEU A 1 167 ? 23.35401 5.43329   1.24557   1.000 23.49755 ? 167 LEU A CB  1 
ATOM   1275 C CG  . LEU A 1 167 ? 21.88220 5.13177   1.58245   1.000 22.74568 ? 167 LEU A CG  1 
ATOM   1276 C CD1 . LEU A 1 167 ? 20.97745 6.21343   1.01255   1.000 22.08874 ? 167 LEU A CD1 1 
ATOM   1277 C CD2 . LEU A 1 167 ? 21.44382 3.74168   1.11439   1.000 22.50838 ? 167 LEU A CD2 1 
ATOM   1278 N N   . GLY A 1 168 ? 26.72067 5.04116   2.35415   1.000 24.43880 ? 168 GLY A N   1 
ATOM   1279 C CA  . GLY A 1 168 ? 28.09336 5.24045   1.93148   1.000 23.85215 ? 168 GLY A CA  1 
ATOM   1280 C C   . GLY A 1 168 ? 28.48213 6.66268   1.59647   1.000 25.63534 ? 168 GLY A C   1 
ATOM   1281 O O   . GLY A 1 168 ? 29.60543 6.87125   1.09588   1.000 27.13680 ? 168 GLY A O   1 
ATOM   1282 N N   . GLY A 1 169 ? 27.63878 7.64829   1.91296   1.000 23.12394 ? 169 GLY A N   1 
ATOM   1283 C CA  . GLY A 1 169 ? 27.96827 9.02474   1.61903   1.000 21.85823 ? 169 GLY A CA  1 
ATOM   1284 C C   . GLY A 1 169 ? 29.04993 9.59913   2.52632   1.000 22.62368 ? 169 GLY A C   1 
ATOM   1285 O O   . GLY A 1 169 ? 29.37231 9.08026   3.62041   1.000 24.54967 ? 169 GLY A O   1 
ATOM   1286 N N   . ALA A 1 170 ? 29.58652 10.73788  2.08631   1.000 20.29058 ? 170 ALA A N   1 
ATOM   1287 C CA  . ALA A 1 170 ? 30.58621 11.45587  2.87030   1.000 21.29461 ? 170 ALA A CA  1 
ATOM   1288 C C   . ALA A 1 170 ? 29.91295 12.27220  3.96516   1.000 24.02045 ? 170 ALA A C   1 
ATOM   1289 O O   . ALA A 1 170 ? 28.76018 12.68942  3.82755   1.000 26.27608 ? 170 ALA A O   1 
ATOM   1290 C CB  . ALA A 1 170 ? 31.40413 12.37270  1.97488   1.000 22.02535 ? 170 ALA A CB  1 
ATOM   1291 N N   . LEU A 1 171 ? 30.61206 12.46444  5.08960   1.000 23.58276 ? 171 LEU A N   1 
ATOM   1292 C CA  . LEU A 1 171 ? 30.08768 13.38107  6.11166   1.000 23.12372 ? 171 LEU A CA  1 
ATOM   1293 C C   . LEU A 1 171 ? 30.62212 14.76896  5.78576   1.000 25.02011 ? 171 LEU A C   1 
ATOM   1294 O O   . LEU A 1 171 ? 31.83944 14.93191  5.62643   1.000 26.88666 ? 171 LEU A O   1 
ATOM   1295 C CB  . LEU A 1 171 ? 30.55430 12.96524  7.51215   1.000 22.77970 ? 171 LEU A CB  1 
ATOM   1296 C CG  . LEU A 1 171 ? 30.36197 11.47357  7.84189   1.000 24.72151 ? 171 LEU A CG  1 
ATOM   1297 C CD1 . LEU A 1 171 ? 30.71767 11.14047  9.33329   1.000 24.99090 ? 171 LEU A CD1 1 
ATOM   1298 C CD2 . LEU A 1 171 ? 28.93933 11.03350  7.54568   1.000 26.24259 ? 171 LEU A CD2 1 
ATOM   1299 N N   . MET A 1 172 ? 29.74807 15.75715  5.69094   1.000 25.57488 ? 172 MET A N   1 
ATOM   1300 C CA  . MET A 1 172 ? 30.11610 17.10512  5.27360   1.000 28.41919 ? 172 MET A CA  1 
ATOM   1301 C C   . MET A 1 172 ? 29.87124 18.08975  6.40323   1.000 27.03929 ? 172 MET A C   1 
ATOM   1302 O O   . MET A 1 172 ? 28.79532 18.10211  7.00861   1.000 27.71353 ? 172 MET A O   1 
ATOM   1303 C CB  . MET A 1 172 ? 29.32096 17.57264  4.03566   1.000 33.26819 ? 172 MET A CB  1 
ATOM   1304 C CG  . MET A 1 172 ? 29.32515 16.64889  2.92309   1.000 39.80587 ? 172 MET A CG  1 
ATOM   1305 S SD  . MET A 1 172 ? 28.29831 17.43540  1.66289   1.000 44.65972 ? 172 MET A SD  1 
ATOM   1306 C CE  . MET A 1 172 ? 29.05521 19.04888  1.67535   1.000 45.46134 ? 172 MET A CE  1 
ATOM   1307 N N   . HIS A 1 173 ? 30.84945 18.93491  6.65721   1.000 25.64245 ? 173 HIS A N   1 
ATOM   1308 C CA  . HIS A 1 173 ? 30.67879 19.98432  7.64605   1.000 26.55314 ? 173 HIS A CA  1 
ATOM   1309 C C   . HIS A 1 173 ? 29.58509 20.96797  7.21955   1.000 29.22764 ? 173 HIS A C   1 
ATOM   1310 O O   . HIS A 1 173 ? 29.53259 21.37629  6.04580   1.000 31.18912 ? 173 HIS A O   1 
ATOM   1311 C CB  . HIS A 1 173 ? 31.99481 20.70564  7.86149   1.000 26.96597 ? 173 HIS A CB  1 
ATOM   1312 C CG  . HIS A 1 173 ? 31.94879 21.63962  9.01902   1.000 28.48514 ? 173 HIS A CG  1 
ATOM   1313 N ND1 . HIS A 1 173 ? 31.51706 22.94178  8.89495   1.000 30.42721 ? 173 HIS A ND1 1 
ATOM   1314 C CD2 . HIS A 1 173 ? 32.20414 21.44681  10.33543  1.000 28.56477 ? 173 HIS A CD2 1 
ATOM   1315 C CE1 . HIS A 1 173 ? 31.54873 23.52760  10.07796  1.000 30.34766 ? 173 HIS A CE1 1 
ATOM   1316 N NE2 . HIS A 1 173 ? 31.96451 22.64320  10.97154  1.000 30.57565 ? 173 HIS A NE2 1 
ATOM   1317 N N   . PRO A 1 174 ? 28.67434 21.33901  8.11993   1.000 29.08784 ? 174 PRO A N   1 
ATOM   1318 C CA  . PRO A 1 174 ? 27.50049 22.11621  7.71305   1.000 30.68026 ? 174 PRO A CA  1 
ATOM   1319 C C   . PRO A 1 174 ? 27.78141 23.57007  7.38173   1.000 33.54712 ? 174 PRO A C   1 
ATOM   1320 O O   . PRO A 1 174 ? 26.85189 24.27152  6.95943   1.000 35.49928 ? 174 PRO A O   1 
ATOM   1321 C CB  . PRO A 1 174 ? 26.55430 21.97027  8.91778   1.000 31.87174 ? 174 PRO A CB  1 
ATOM   1322 C CG  . PRO A 1 174 ? 27.43382 21.64715  10.04670  1.000 30.80499 ? 174 PRO A CG  1 
ATOM   1323 C CD  . PRO A 1 174 ? 28.60695 20.92300  9.53620   1.000 29.75690 ? 174 PRO A CD  1 
ATOM   1324 N N   . SER A 1 175 ? 29.01796 24.05429  7.49606   1.000 33.33013 ? 175 SER A N   1 
ATOM   1325 C CA  . SER A 1 175 ? 29.33980 25.35769  6.93065   1.000 33.45095 ? 175 SER A CA  1 
ATOM   1326 C C   . SER A 1 175 ? 29.38931 25.31785  5.40318   1.000 34.94518 ? 175 SER A C   1 
ATOM   1327 O O   . SER A 1 175 ? 29.43965 26.37663  4.76113   1.000 37.08809 ? 175 SER A O   1 
ATOM   1328 C CB  . SER A 1 175 ? 30.67874 25.86046  7.48762   1.000 34.78303 ? 175 SER A CB  1 
ATOM   1329 O OG  . SER A 1 175 ? 31.73492 25.03246  7.04214   1.000 36.97393 ? 175 SER A OG  1 
ATOM   1330 N N   . ILE A 1 176 ? 29.36849 24.13322  4.81580   1.000 32.01525 ? 176 ILE A N   1 
ATOM   1331 C CA  . ILE A 1 176 ? 29.44365 23.98999  3.36722   1.000 30.63724 ? 176 ILE A CA  1 
ATOM   1332 C C   . ILE A 1 176 ? 28.02055 23.99652  2.83204   1.000 30.77298 ? 176 ILE A C   1 
ATOM   1333 O O   . ILE A 1 176 ? 27.21310 23.13839  3.20169   1.000 31.24477 ? 176 ILE A O   1 
ATOM   1334 C CB  . ILE A 1 176 ? 30.16376 22.69973  2.96941   1.000 30.15593 ? 176 ILE A CB  1 
ATOM   1335 C CG1 . ILE A 1 176 ? 31.56627 22.68334  3.55712   1.000 29.87911 ? 176 ILE A CG1 1 
ATOM   1336 C CG2 . ILE A 1 176 ? 30.14963 22.54950  1.41775   1.000 30.53947 ? 176 ILE A CG2 1 
ATOM   1337 C CD1 . ILE A 1 176 ? 32.24837 21.32982  3.38843   1.000 30.34159 ? 176 ILE A CD1 1 
ATOM   1338 N N   . GLU A 1 177 ? 27.71073 24.95962  1.96440   1.000 29.44114 ? 177 GLU A N   1 
ATOM   1339 C CA  . GLU A 1 177 ? 26.36138 25.08899  1.41898   1.000 29.14573 ? 177 GLU A CA  1 
ATOM   1340 C C   . GLU A 1 177 ? 26.25891 24.14303  0.22600   1.000 28.83643 ? 177 GLU A C   1 
ATOM   1341 O O   . GLU A 1 177 ? 26.57239 24.50658  -0.91658  1.000 29.94498 ? 177 GLU A O   1 
ATOM   1342 C CB  . GLU A 1 177 ? 26.07578 26.53754  1.06349   1.000 32.13251 ? 177 GLU A CB  1 
ATOM   1343 C CG  . GLU A 1 177 ? 26.04522 27.47639  2.27846   1.000 36.04943 ? 177 GLU A CG  1 
ATOM   1344 C CD  . GLU A 1 177 ? 25.53455 28.87488  1.93568   0.700 40.72553 ? 177 GLU A CD  1 
ATOM   1345 O OE1 . GLU A 1 177 ? 26.06371 29.51194  1.00098   0.700 41.48612 ? 177 GLU A OE1 1 
ATOM   1346 O OE2 . GLU A 1 177 ? 24.57512 29.33251  2.57972   0.700 43.67601 ? 177 GLU A OE2 1 
ATOM   1347 N N   . ALA A 1 178 ? 25.83165 22.90071  0.49060   1.000 27.98398 ? 178 ALA A N   1 
ATOM   1348 C CA  . ALA A 1 178 ? 25.81301 21.84756  -0.52355  1.000 24.96750 ? 178 ALA A CA  1 
ATOM   1349 C C   . ALA A 1 178 ? 24.71747 20.83227  -0.21836  1.000 24.47170 ? 178 ALA A C   1 
ATOM   1350 O O   . ALA A 1 178 ? 24.11851 20.82209  0.86914   1.000 25.36657 ? 178 ALA A O   1 
ATOM   1351 C CB  . ALA A 1 178 ? 27.15788 21.12100  -0.58939  1.000 22.99386 ? 178 ALA A CB  1 
ATOM   1352 N N   . MET A 1 179 ? 24.49546 19.93551  -1.17806  1.000 23.12042 ? 179 MET A N   1 
ATOM   1353 C CA  . MET A 1 179 ? 23.64275 18.76771  -1.00967  1.000 22.99706 ? 179 MET A CA  1 
ATOM   1354 C C   . MET A 1 179 ? 24.37483 17.57725  -1.60245  1.000 21.83067 ? 179 MET A C   1 
ATOM   1355 O O   . MET A 1 179 ? 25.18078 17.73532  -2.52849  1.000 22.83499 ? 179 MET A O   1 
ATOM   1356 C CB  . MET A 1 179 ? 22.26974 18.95870  -1.69751  1.000 23.25288 ? 179 MET A CB  1 
ATOM   1357 C CG  . MET A 1 179 ? 22.40523 19.24719  -3.23098  1.000 23.72056 ? 179 MET A CG  1 
ATOM   1358 S SD  . MET A 1 179 ? 20.78179 19.57933  -3.96455  1.000 24.63678 ? 179 MET A SD  1 
ATOM   1359 C CE  . MET A 1 179 ? 21.36582 19.68779  -5.71415  1.000 22.54277 ? 179 MET A CE  1 
ATOM   1360 N N   . GLN A 1 180 ? 24.08381 16.37892  -1.08370  1.000 21.14663 ? 180 GLN A N   1 
ATOM   1361 C CA  . GLN A 1 180 ? 24.80589 15.17853  -1.48540  1.000 21.24042 ? 180 GLN A CA  1 
ATOM   1362 C C   . GLN A 1 180 ? 23.83681 14.10129  -1.95425  1.000 21.38594 ? 180 GLN A C   1 
ATOM   1363 O O   . GLN A 1 180 ? 22.91465 13.72301  -1.22142  1.000 23.01524 ? 180 GLN A O   1 
ATOM   1364 C CB  . GLN A 1 180 ? 25.71050 14.65052  -0.34923  1.000 19.21984 ? 180 GLN A CB  1 
ATOM   1365 C CG  . GLN A 1 180 ? 26.53053 13.44268  -0.77467  1.000 18.62174 ? 180 GLN A CG  1 
ATOM   1366 C CD  . GLN A 1 180 ? 27.51290 12.97438  0.28709   1.000 21.53159 ? 180 GLN A CD  1 
ATOM   1367 O OE1 . GLN A 1 180 ? 28.14213 11.93566  0.13890   1.000 22.86335 ? 180 GLN A OE1 1 
ATOM   1368 N NE2 . GLN A 1 180 ? 27.58718 13.70793  1.39674   1.000 22.52727 ? 180 GLN A NE2 1 
ATOM   1369 N N   . LEU A 1 181 ? 24.06858 13.57914  -3.17905  1.000 20.91901 ? 181 LEU A N   1 
ATOM   1370 C CA  . LEU A 1 181 ? 23.23099 12.53860  -3.75721  1.000 20.92951 ? 181 LEU A CA  1 
ATOM   1371 C C   . LEU A 1 181 ? 23.90099 11.17815  -3.58959  1.000 23.01756 ? 181 LEU A C   1 
ATOM   1372 O O   . LEU A 1 181 ? 25.04220 10.97801  -4.05536  1.000 24.16072 ? 181 LEU A O   1 
ATOM   1373 C CB  . LEU A 1 181 ? 22.98181 12.83605  -5.24202  1.000 22.38328 ? 181 LEU A CB  1 
ATOM   1374 C CG  . LEU A 1 181 ? 22.10370 11.81409  -5.93808  1.000 22.29481 ? 181 LEU A CG  1 
ATOM   1375 C CD1 . LEU A 1 181 ? 20.61005 11.94642  -5.48819  1.000 22.14014 ? 181 LEU A CD1 1 
ATOM   1376 C CD2 . LEU A 1 181 ? 22.19431 12.05233  -7.45137  1.000 23.22810 ? 181 LEU A CD2 1 
ATOM   1377 N N   . THR A 1 182 ? 23.19278 10.23452  -2.95710  1.000 22.22078 ? 182 THR A N   1 
ATOM   1378 C CA  . THR A 1 182 ? 23.69762 8.86969   -2.81334  1.000 22.99987 ? 182 THR A CA  1 
ATOM   1379 C C   . THR A 1 182 ? 22.72417 7.88258   -3.41914  1.000 22.75984 ? 182 THR A C   1 
ATOM   1380 O O   . THR A 1 182 ? 21.50911 8.11525   -3.46148  1.000 21.69215 ? 182 THR A O   1 
ATOM   1381 C CB  . THR A 1 182 ? 23.94399 8.48310   -1.32158  1.000 23.84818 ? 182 THR A CB  1 
ATOM   1382 O OG1 . THR A 1 182 ? 22.76966 8.76731   -0.56837  1.000 26.99727 ? 182 THR A OG1 1 
ATOM   1383 C CG2 . THR A 1 182 ? 25.09308 9.24042   -0.78308  1.000 23.16209 ? 182 THR A CG2 1 
ATOM   1384 N N   . GLU A 1 183 ? 23.29146 6.77632   -3.90524  1.000 22.67247 ? 183 GLU A N   1 
ATOM   1385 C CA  . GLU A 1 183 ? 22.54619 5.68741   -4.53916  1.000 21.90083 ? 183 GLU A CA  1 
ATOM   1386 C C   . GLU A 1 183 ? 22.11016 4.64451   -3.52380  1.000 21.46832 ? 183 GLU A C   1 
ATOM   1387 O O   . GLU A 1 183 ? 22.86517 4.31085   -2.59973  1.000 23.27553 ? 183 GLU A O   1 
ATOM   1388 C CB  . GLU A 1 183 ? 23.42534 4.99417   -5.56547  1.000 24.74316 ? 183 GLU A CB  1 
ATOM   1389 C CG  . GLU A 1 183 ? 24.01887 5.90334   -6.64436  1.000 29.52139 ? 183 GLU A CG  1 
ATOM   1390 C CD  . GLU A 1 183 ? 24.84507 5.10499   -7.63677  1.000 34.35446 ? 183 GLU A CD  1 
ATOM   1391 O OE1 . GLU A 1 183 ? 25.13001 3.90930   -7.35145  1.000 38.05120 ? 183 GLU A OE1 1 
ATOM   1392 O OE2 . GLU A 1 183 ? 25.19742 5.66233   -8.69267  1.000 33.68423 ? 183 GLU A OE2 1 
ATOM   1393 N N   . MET A 1 184 ? 20.93157 4.08432   -3.74040  1.000 22.00807 ? 184 MET A N   1 
ATOM   1394 C CA  . MET A 1 184 ? 20.47536 2.89528   -3.02937  1.000 24.24919 ? 184 MET A CA  1 
ATOM   1395 C C   . MET A 1 184 ? 20.50647 1.73872   -4.00966  1.000 24.89387 ? 184 MET A C   1 
ATOM   1396 O O   . MET A 1 184 ? 19.62376 1.65250   -4.86377  1.000 27.08159 ? 184 MET A O   1 
ATOM   1397 C CB  . MET A 1 184 ? 19.06182 3.06853   -2.49375  1.000 27.17282 ? 184 MET A CB  1 
ATOM   1398 C CG  . MET A 1 184 ? 18.84140 4.30306   -1.66725  1.000 32.06844 ? 184 MET A CG  1 
ATOM   1399 S SD  . MET A 1 184 ? 17.07728 4.41288   -1.26475  1.000 38.82860 ? 184 MET A SD  1 
ATOM   1400 C CE  . MET A 1 184 ? 17.02486 5.89324   -0.26327  1.000 41.34782 ? 184 MET A CE  1 
ATOM   1401 N N   . ALA A 1 185 ? 21.45243 0.82963   -3.82638  1.000 25.53171 ? 185 ALA A N   1 
ATOM   1402 C CA  . ALA A 1 185 ? 21.51652 -0.46694  -4.49921  1.000 25.85191 ? 185 ALA A CA  1 
ATOM   1403 C C   . ALA A 1 185 ? 21.38351 -0.30984  -6.01635  1.000 26.35511 ? 185 ALA A C   1 
ATOM   1404 O O   . ALA A 1 185 ? 20.47395 -0.82775  -6.62532  1.000 27.47596 ? 185 ALA A O   1 
ATOM   1405 C CB  . ALA A 1 185 ? 20.44633 -1.42453  -3.96353  1.000 25.08579 ? 185 ALA A CB  1 
ATOM   1406 N N   . SER A 1 186 ? 22.29933 0.44003   -6.60136  1.000 28.18409 ? 186 SER A N   1 
ATOM   1407 C CA  . SER A 1 186 ? 22.28332 0.60794   -8.05907  1.000 29.85329 ? 186 SER A CA  1 
ATOM   1408 C C   . SER A 1 186 ? 22.71603 -0.66726  -8.76067  1.000 30.68435 ? 186 SER A C   1 
ATOM   1409 O O   . SER A 1 186 ? 23.61346 -1.38386  -8.30387  1.000 30.74076 ? 186 SER A O   1 
ATOM   1410 C CB  . SER A 1 186 ? 23.20725 1.73949   -8.48990  1.000 31.17675 ? 186 SER A CB  1 
ATOM   1411 O OG  . SER A 1 186 ? 24.53208 1.49014   -8.05111  1.000 34.48166 ? 186 SER A OG  1 
ATOM   1412 N N   . ILE A 1 187 ? 22.11046 -0.92913  -9.92404  1.000 29.63203 ? 187 ILE A N   1 
ATOM   1413 C CA  . ILE A 1 187 ? 22.54969 -2.08645  -10.69470 1.000 31.71317 ? 187 ILE A CA  1 
ATOM   1414 C C   . ILE A 1 187 ? 23.64778 -1.64170  -11.63864 1.000 31.87567 ? 187 ILE A C   1 
ATOM   1415 O O   . ILE A 1 187 ? 23.57593 -0.56881  -12.24672 1.000 33.34328 ? 187 ILE A O   1 
ATOM   1416 C CB  . ILE A 1 187 ? 21.40121 -2.74853  -11.45635 1.000 35.17111 ? 187 ILE A CB  1 
ATOM   1417 C CG1 . ILE A 1 187 ? 21.93168 -4.00725  -12.14860 1.000 36.33455 ? 187 ILE A CG1 1 
ATOM   1418 C CG2 . ILE A 1 187 ? 20.83001 -1.80374  -12.49924 1.000 37.31257 ? 187 ILE A CG2 1 
ATOM   1419 C CD1 . ILE A 1 187 ? 20.86368 -5.06597  -12.43088 1.000 38.74002 ? 187 ILE A CD1 1 
ATOM   1420 N N   . ASN A 1 188 ? 24.68219 -2.44886  -11.73975 1.000 31.08478 ? 188 ASN A N   1 
ATOM   1421 C CA  . ASN A 1 188 ? 25.74640 -2.16487  -12.69372 1.000 33.78717 ? 188 ASN A CA  1 
ATOM   1422 C C   . ASN A 1 188 ? 26.16129 -3.45677  -13.37469 1.000 34.64357 ? 188 ASN A C   1 
ATOM   1423 O O   . ASN A 1 188 ? 26.59316 -4.40621  -12.71377 1.000 35.14955 ? 188 ASN A O   1 
ATOM   1424 C CB  . ASN A 1 188 ? 26.92380 -1.48174  -12.00282 1.000 37.86256 ? 188 ASN A CB  1 
ATOM   1425 C CG  . ASN A 1 188 ? 26.70319 0.01390   -11.86314 1.000 42.99933 ? 188 ASN A CG  1 
ATOM   1426 O OD1 . ASN A 1 188 ? 27.11994 0.79450   -12.72211 1.000 46.57361 ? 188 ASN A OD1 1 
ATOM   1427 N ND2 . ASN A 1 188 ? 26.02087 0.41841   -10.80571 1.000 43.54448 ? 188 ASN A ND2 1 
ATOM   1428 N N   . ASN A 1 189 ? 26.00450 -3.49221  -14.69307 1.000 34.29172 ? 189 ASN A N   1 
ATOM   1429 C CA  . ASN A 1 189 ? 26.42377 -4.62685  -15.50863 1.000 33.98456 ? 189 ASN A CA  1 
ATOM   1430 C C   . ASN A 1 189 ? 26.82860 -4.09405  -16.87256 1.000 36.83224 ? 189 ASN A C   1 
ATOM   1431 O O   . ASN A 1 189 ? 27.01770 -2.89164  -17.05634 1.000 39.00111 ? 189 ASN A O   1 
ATOM   1432 C CB  . ASN A 1 189 ? 25.32487 -5.70527  -15.56652 1.000 33.94994 ? 189 ASN A CB  1 
ATOM   1433 C CG  . ASN A 1 189 ? 24.01464 -5.17922  -16.07268 1.000 34.18009 ? 189 ASN A CG  1 
ATOM   1434 O OD1 . ASN A 1 189 ? 23.99593 -4.31102  -16.95117 1.000 35.12526 ? 189 ASN A OD1 1 
ATOM   1435 N ND2 . ASN A 1 189 ? 22.89282 -5.71728  -15.54829 1.000 32.96579 ? 189 ASN A ND2 1 
ATOM   1436 N N   . ARG A 1 190 ? 26.96686 -4.99940  -17.83447 1.000 39.91621 ? 190 ARG A N   1 
ATOM   1437 C CA  . ARG A 1 190 ? 27.35564 -4.59601  -19.18538 1.000 44.57678 ? 190 ARG A CA  1 
ATOM   1438 C C   . ARG A 1 190 ? 26.38030 -3.57680  -19.78250 1.000 45.31477 ? 190 ARG A C   1 
ATOM   1439 O O   . ARG A 1 190 ? 26.79847 -2.68570  -20.52659 1.000 45.97274 ? 190 ARG A O   1 
ATOM   1440 C CB  . ARG A 1 190 ? 27.46510 -5.84443  -20.06353 1.000 48.22362 ? 190 ARG A CB  1 
ATOM   1441 C CG  . ARG A 1 190 ? 27.89591 -5.59863  -21.48087 1.000 51.97682 ? 190 ARG A CG  1 
ATOM   1442 C CD  . ARG A 1 190 ? 27.88614 -6.88789  -22.28878 1.000 54.30545 ? 190 ARG A CD  1 
ATOM   1443 N NE  . ARG A 1 190 ? 26.54309 -7.22966  -22.73966 1.000 56.88532 ? 190 ARG A NE  1 
ATOM   1444 C CZ  . ARG A 1 190 ? 25.88878 -8.31772  -22.36598 1.000 59.02201 ? 190 ARG A CZ  1 
ATOM   1445 N NH1 . ARG A 1 190 ? 26.45981 -9.23731  -21.60649 1.000 59.14497 ? 190 ARG A NH1 1 
ATOM   1446 N NH2 . ARG A 1 190 ? 24.63128 -8.49033  -22.77008 1.000 60.26444 ? 190 ARG A NH2 1 
ATOM   1447 N N   . VAL A 1 191 ? 25.07929 -3.68622  -19.48431 1.000 44.63235 ? 191 VAL A N   1 
ATOM   1448 C CA  . VAL A 1 191 ? 24.10087 -2.77959  -20.09447 1.000 46.18495 ? 191 VAL A CA  1 
ATOM   1449 C C   . VAL A 1 191 ? 23.66223 -1.60026  -19.21951 1.000 45.65296 ? 191 VAL A C   1 
ATOM   1450 O O   . VAL A 1 191 ? 23.22332 -0.57494  -19.76433 1.000 51.70056 ? 191 VAL A O   1 
ATOM   1451 C CB  . VAL A 1 191 ? 22.84793 -3.53708  -20.60135 1.000 48.47866 ? 191 VAL A CB  1 
ATOM   1452 C CG1 . VAL A 1 191 ? 23.22464 -4.50587  -21.72561 1.000 48.22873 ? 191 VAL A CG1 1 
ATOM   1453 C CG2 . VAL A 1 191 ? 22.10718 -4.23104  -19.48178 1.000 50.28830 ? 191 VAL A CG2 1 
ATOM   1454 N N   . TYR A 1 192 ? 23.76401 -1.70041  -17.89937 1.000 40.26566 ? 192 TYR A N   1 
ATOM   1455 C CA  . TYR A 1 192 ? 23.32446 -0.62716  -17.00967 1.000 37.38696 ? 192 TYR A CA  1 
ATOM   1456 C C   . TYR A 1 192 ? 24.52474 -0.07011  -16.25728 1.000 36.54355 ? 192 TYR A C   1 
ATOM   1457 O O   . TYR A 1 192 ? 25.30722 -0.84854  -15.71737 1.000 37.60414 ? 192 TYR A O   1 
ATOM   1458 C CB  . TYR A 1 192 ? 22.30106 -1.14755  -16.01556 1.000 38.70014 ? 192 TYR A CB  1 
ATOM   1459 C CG  . TYR A 1 192 ? 21.07221 -1.79456  -16.62405 1.000 43.70652 ? 192 TYR A CG  1 
ATOM   1460 C CD1 . TYR A 1 192 ? 20.36799 -1.17600  -17.65741 1.000 45.80277 ? 192 TYR A CD1 1 
ATOM   1461 C CD2 . TYR A 1 192 ? 20.59582 -3.00358  -16.14573 1.000 48.37329 ? 192 TYR A CD2 1 
ATOM   1462 C CE1 . TYR A 1 192 ? 19.21399 -1.75964  -18.19438 1.000 47.86034 ? 192 TYR A CE1 1 
ATOM   1463 C CE2 . TYR A 1 192 ? 19.44730 -3.59604  -16.67658 1.000 49.98297 ? 192 TYR A CE2 1 
ATOM   1464 C CZ  . TYR A 1 192 ? 18.76320 -2.96353  -17.69733 1.000 50.25478 ? 192 TYR A CZ  1 
ATOM   1465 O OH  . TYR A 1 192 ? 17.63877 -3.55361  -18.22376 1.000 52.31432 ? 192 TYR A OH  1 
ATOM   1466 N N   . ARG A 1 193 ? 24.64471 1.26653   -16.20891 1.000 36.08515 ? 193 ARG A N   1 
ATOM   1467 C CA  . ARG A 1 193 ? 25.79899 1.98790   -15.67743 1.000 36.52081 ? 193 ARG A CA  1 
ATOM   1468 C C   . ARG A 1 193 ? 25.34812 3.20297   -14.87463 1.000 34.05403 ? 193 ARG A C   1 
ATOM   1469 O O   . ARG A 1 193 ? 24.57847 4.02864   -15.37836 1.000 36.09512 ? 193 ARG A O   1 
ATOM   1470 C CB  . ARG A 1 193 ? 26.71118 2.47446   -16.80693 1.000 40.80203 ? 193 ARG A CB  1 
ATOM   1471 C CG  . ARG A 1 193 ? 28.09442 2.88475   -16.36133 0.900 46.06475 ? 193 ARG A CG  1 
ATOM   1472 C CD  . ARG A 1 193 ? 29.09348 1.75635   -16.64918 0.800 49.81940 ? 193 ARG A CD  1 
ATOM   1473 N NE  . ARG A 1 193 ? 30.43085 2.26551   -16.93026 0.700 52.43010 ? 193 ARG A NE  1 
ATOM   1474 C CZ  . ARG A 1 193 ? 30.94843 2.37744   -18.14853 0.700 53.86978 ? 193 ARG A CZ  1 
ATOM   1475 N NH1 . ARG A 1 193 ? 30.26430 2.02552   -19.22931 0.700 54.31673 ? 193 ARG A NH1 1 
ATOM   1476 N NH2 . ARG A 1 193 ? 32.18266 2.85193   -18.28731 0.700 53.90879 ? 193 ARG A NH2 1 
ATOM   1477 N N   . THR A 1 194 ? 25.83314 3.32693   -13.63980 1.000 28.95693 ? 194 THR A N   1 
ATOM   1478 C CA  . THR A 1 194 ? 25.69081 4.56621   -12.89087 1.000 28.25923 ? 194 THR A CA  1 
ATOM   1479 C C   . THR A 1 194 ? 27.06303 4.98620   -12.38754 1.000 26.71627 ? 194 THR A C   1 
ATOM   1480 O O   . THR A 1 194 ? 28.04973 4.27429   -12.54384 1.000 26.27605 ? 194 THR A O   1 
ATOM   1481 C CB  . THR A 1 194 ? 24.71079 4.43817   -11.70506 1.000 31.23361 ? 194 THR A CB  1 
ATOM   1482 O OG1 . THR A 1 194 ? 25.35672 3.71996   -10.64719 1.000 33.21661 ? 194 THR A OG1 1 
ATOM   1483 C CG2 . THR A 1 194 ? 23.44633 3.71826   -12.12744 1.000 32.61986 ? 194 THR A CG2 1 
ATOM   1484 N N   . ILE A 1 195 ? 27.13386 6.18201   -11.80677 1.000 26.51442 ? 195 ILE A N   1 
ATOM   1485 C CA  . ILE A 1 195 ? 28.41979 6.69132   -11.35702 1.000 25.22381 ? 195 ILE A CA  1 
ATOM   1486 C C   . ILE A 1 195 ? 28.93911 5.89809   -10.14656 1.000 25.71447 ? 195 ILE A C   1 
ATOM   1487 O O   . ILE A 1 195 ? 30.15027 5.74920   -9.98050  1.000 27.47116 ? 195 ILE A O   1 
ATOM   1488 C CB  . ILE A 1 195 ? 28.30601 8.21232   -11.05861 1.000 26.52845 ? 195 ILE A CB  1 
ATOM   1489 C CG1 . ILE A 1 195 ? 29.66416 8.85682   -10.82965 1.000 25.81807 ? 195 ILE A CG1 1 
ATOM   1490 C CG2 . ILE A 1 195 ? 27.32989 8.48638   -9.90889  1.000 28.28830 ? 195 ILE A CG2 1 
ATOM   1491 C CD1 . ILE A 1 195 ? 30.66293 8.78964   -12.02070 1.000 26.93318 ? 195 ILE A CD1 1 
ATOM   1492 N N   A GLY A 1 196 ? 28.07157 5.37071   -9.28838  0.500 26.05704 ? 196 GLY A N   1 
ATOM   1493 N N   B GLY A 1 196 ? 28.02418 5.37857   -9.31979  0.500 25.50868 ? 196 GLY A N   1 
ATOM   1494 C CA  A GLY A 1 196 ? 28.61405 4.51555   -8.22864  0.500 26.75244 ? 196 GLY A CA  1 
ATOM   1495 C CA  B GLY A 1 196 ? 28.27806 4.65961   -8.04382  0.500 25.05684 ? 196 GLY A CA  1 
ATOM   1496 C C   A GLY A 1 196 ? 29.43429 5.20950   -7.15695  0.500 27.11155 ? 196 GLY A C   1 
ATOM   1497 C C   B GLY A 1 196 ? 28.58334 5.60189   -6.89817  0.500 23.01548 ? 196 GLY A C   1 
ATOM   1498 O O   A GLY A 1 196 ? 30.07588 4.52365   -6.34484  0.500 29.31259 ? 196 GLY A O   1 
ATOM   1499 O O   B GLY A 1 196 ? 27.99170 5.50465   -5.81719  0.500 20.99857 ? 196 GLY A O   1 
ATOM   1500 N N   . SER A 1 197 ? 29.44876 6.54288   -7.13286  1.000 24.32858 ? 197 SER A N   1 
ATOM   1501 C CA  . SER A 1 197 ? 29.97636 7.37182   -6.06822  1.000 23.22525 ? 197 SER A CA  1 
ATOM   1502 C C   . SER A 1 197 ? 28.91918 8.38044   -5.64565  1.000 23.12530 ? 197 SER A C   1 
ATOM   1503 O O   . SER A 1 197 ? 28.12356 8.81496   -6.47149  1.000 23.12430 ? 197 SER A O   1 
ATOM   1504 C CB  . SER A 1 197 ? 31.20974 8.12620   -6.55186  1.000 21.82463 ? 197 SER A CB  1 
ATOM   1505 O OG  . SER A 1 197 ? 32.17967 7.23218   -7.05557  1.000 23.24690 ? 197 SER A OG  1 
ATOM   1506 N N   . PRO A 1 198 ? 28.89563 8.76939   -4.37080  1.000 21.77089 ? 198 PRO A N   1 
ATOM   1507 C CA  . PRO A 1 198 ? 28.10741 9.93554   -3.96599  1.000 22.73140 ? 198 PRO A CA  1 
ATOM   1508 C C   . PRO A 1 198 ? 28.53759 11.17644  -4.73850  1.000 23.05862 ? 198 PRO A C   1 
ATOM   1509 O O   . PRO A 1 198 ? 29.71387 11.34476  -5.08558  1.000 23.49927 ? 198 PRO A O   1 
ATOM   1510 C CB  . PRO A 1 198 ? 28.44113 10.08713  -2.46953  1.000 23.85811 ? 198 PRO A CB  1 
ATOM   1511 C CG  . PRO A 1 198 ? 29.00882 8.76413   -2.07125  1.000 22.47313 ? 198 PRO A CG  1 
ATOM   1512 C CD  . PRO A 1 198 ? 29.70183 8.21248   -3.28022  1.000 20.59574 ? 198 PRO A CD  1 
ATOM   1513 N N   . LEU A 1 199 ? 27.59481 12.07506  -4.97429  1.000 21.05998 ? 199 LEU A N   1 
ATOM   1514 C CA  . LEU A 1 199 ? 27.88831 13.32861  -5.65193  1.000 22.01502 ? 199 LEU A CA  1 
ATOM   1515 C C   . LEU A 1 199 ? 27.54153 14.46880  -4.72905  1.000 23.33357 ? 199 LEU A C   1 
ATOM   1516 O O   . LEU A 1 199 ? 26.45103 14.46838  -4.12230  1.000 23.44044 ? 199 LEU A O   1 
ATOM   1517 C CB  . LEU A 1 199 ? 27.05818 13.47616  -6.94202  1.000 20.53462 ? 199 LEU A CB  1 
ATOM   1518 C CG  . LEU A 1 199 ? 27.22101 12.29354  -7.89971  1.000 21.69414 ? 199 LEU A CG  1 
ATOM   1519 C CD1 . LEU A 1 199 ? 26.34307 12.47991  -9.18061  1.000 23.46512 ? 199 LEU A CD1 1 
ATOM   1520 C CD2 . LEU A 1 199 ? 28.67688 12.03274  -8.30456  1.000 23.43177 ? 199 LEU A CD2 1 
ATOM   1521 N N   . VAL A 1 200 ? 28.43662 15.45012  -4.64046  1.000 22.96325 ? 200 VAL A N   1 
ATOM   1522 C CA  . VAL A 1 200 ? 28.24172 16.64232  -3.81118  1.000 22.73742 ? 200 VAL A CA  1 
ATOM   1523 C C   . VAL A 1 200 ? 28.08655 17.84779  -4.72228  1.000 24.00821 ? 200 VAL A C   1 
ATOM   1524 O O   . VAL A 1 200 ? 28.97432 18.12117  -5.55662  1.000 23.76126 ? 200 VAL A O   1 
ATOM   1525 C CB  . VAL A 1 200 ? 29.41890 16.85656  -2.85010  1.000 21.00679 ? 200 VAL A CB  1 
ATOM   1526 C CG1 . VAL A 1 200 ? 29.20628 18.12506  -2.03829  1.000 21.67002 ? 200 VAL A CG1 1 
ATOM   1527 C CG2 . VAL A 1 200 ? 29.48567 15.70836  -1.87627  1.000 21.94667 ? 200 VAL A CG2 1 
ATOM   1528 N N   . PHE A 1 201 ? 26.94351 18.56595  -4.57358  1.000 24.65861 ? 201 PHE A N   1 
ATOM   1529 C CA  . PHE A 1 201 ? 26.52983 19.68996  -5.40489  1.000 24.96692 ? 201 PHE A CA  1 
ATOM   1530 C C   . PHE A 1 201 ? 26.56493 20.98875  -4.62480  1.000 26.76458 ? 201 PHE A C   1 
ATOM   1531 O O   . PHE A 1 201 ? 26.08223 21.03571  -3.48401  1.000 27.03047 ? 201 PHE A O   1 
ATOM   1532 C CB  . PHE A 1 201 ? 25.11648 19.47674  -5.94337  1.000 23.70588 ? 201 PHE A CB  1 
ATOM   1533 C CG  . PHE A 1 201 ? 24.99490 18.25978  -6.78963  1.000 23.53816 ? 201 PHE A CG  1 
ATOM   1534 C CD1 . PHE A 1 201 ? 25.32426 18.29381  -8.15624  1.000 23.65677 ? 201 PHE A CD1 1 
ATOM   1535 C CD2 . PHE A 1 201 ? 24.56103 17.08335  -6.24165  1.000 23.68284 ? 201 PHE A CD2 1 
ATOM   1536 C CE1 . PHE A 1 201 ? 25.25394 17.13233  -8.91897  1.000 25.34600 ? 201 PHE A CE1 1 
ATOM   1537 C CE2 . PHE A 1 201 ? 24.48490 15.92806  -6.98470  1.000 24.69894 ? 201 PHE A CE2 1 
ATOM   1538 C CZ  . PHE A 1 201 ? 24.83900 15.94502  -8.35189  1.000 24.58944 ? 201 PHE A CZ  1 
ATOM   1539 N N   . PRO A 1 202 ? 27.07990 22.05822  -5.20977  1.000 27.71982 ? 202 PRO A N   1 
ATOM   1540 C CA  . PRO A 1 202 ? 27.00264 23.36814  -4.55414  1.000 27.87537 ? 202 PRO A CA  1 
ATOM   1541 C C   . PRO A 1 202 ? 25.62950 24.00288  -4.68588  1.000 28.93987 ? 202 PRO A C   1 
ATOM   1542 O O   . PRO A 1 202 ? 24.72385 23.52321  -5.38482  1.000 27.35201 ? 202 PRO A O   1 
ATOM   1543 C CB  . PRO A 1 202 ? 28.04885 24.20460  -5.28806  1.000 27.91641 ? 202 PRO A CB  1 
ATOM   1544 C CG  . PRO A 1 202 ? 28.05344 23.61559  -6.69214  1.000 29.10114 ? 202 PRO A CG  1 
ATOM   1545 C CD  . PRO A 1 202 ? 27.68781 22.13798  -6.55927  1.000 28.16972 ? 202 PRO A CD  1 
ATOM   1546 N N   . LYS A 1 203 ? 25.49089 25.10352  -3.95801  1.000 31.19006 ? 203 LYS A N   1 
ATOM   1547 C CA  . LYS A 1 203 ? 24.33866 25.97520  -4.09326  1.000 34.61136 ? 203 LYS A CA  1 
ATOM   1548 C C   . LYS A 1 203 ? 24.21034 26.39857  -5.54745  1.000 33.63963 ? 203 LYS A C   1 
ATOM   1549 O O   . LYS A 1 203 ? 25.21480 26.58707  -6.24180  1.000 33.49267 ? 203 LYS A O   1 
ATOM   1550 C CB  . LYS A 1 203 ? 24.52338 27.18838  -3.17463  1.000 38.46123 ? 203 LYS A CB  1 
ATOM   1551 C CG  . LYS A 1 203 ? 23.28408 27.92521  -2.78048  0.800 42.79899 ? 203 LYS A CG  1 
ATOM   1552 C CD  . LYS A 1 203 ? 23.68357 29.17335  -2.01510  0.700 45.32105 ? 203 LYS A CD  1 
ATOM   1553 C CE  . LYS A 1 203 ? 22.46723 29.91173  -1.53920  0.700 46.04859 ? 203 LYS A CE  1 
ATOM   1554 N NZ  . LYS A 1 203 ? 21.53435 28.93984  -0.92840  0.700 45.33164 ? 203 LYS A NZ  1 
ATOM   1555 N N   . HIS A 1 204 ? 22.97351 26.47937  -6.02163  1.000 32.61553 ? 204 HIS A N   1 
ATOM   1556 C CA  . HIS A 1 204 ? 22.58784 26.91600  -7.35946  1.000 33.98210 ? 204 HIS A CA  1 
ATOM   1557 C C   . HIS A 1 204 ? 22.69264 25.81682  -8.40600  1.000 34.06140 ? 204 HIS A C   1 
ATOM   1558 O O   . HIS A 1 204 ? 22.25540 26.03511  -9.52322  1.000 38.48502 ? 204 HIS A O   1 
ATOM   1559 C CB  . HIS A 1 204 ? 23.38308 28.13938  -7.85585  1.000 36.82707 ? 204 HIS A CB  1 
ATOM   1560 C CG  . HIS A 1 204 ? 23.33601 29.30964  -6.92310  1.000 41.03615 ? 204 HIS A CG  1 
ATOM   1561 N ND1 . HIS A 1 204 ? 22.15212 29.86962  -6.49268  1.000 43.22599 ? 204 HIS A ND1 1 
ATOM   1562 C CD2 . HIS A 1 204 ? 24.32361 30.03853  -6.35217  1.000 42.47200 ? 204 HIS A CD2 1 
ATOM   1563 C CE1 . HIS A 1 204 ? 22.41167 30.88665  -5.69334  1.000 43.51830 ? 204 HIS A CE1 1 
ATOM   1564 N NE2 . HIS A 1 204 ? 23.72158 31.01714  -5.60156  1.000 43.45524 ? 204 HIS A NE2 1 
ATOM   1565 N N   . HIS A 1 205 ? 23.25071 24.65410  -8.10964  1.000 30.94475 ? 205 HIS A N   1 
ATOM   1566 C CA  . HIS A 1 205 ? 23.09227 23.53350  -9.02473  1.000 28.52699 ? 205 HIS A CA  1 
ATOM   1567 C C   . HIS A 1 205 ? 21.73465 22.89201  -8.79355  1.000 28.64419 ? 205 HIS A C   1 
ATOM   1568 O O   . HIS A 1 205 ? 21.26826 22.78447  -7.66334  1.000 30.04182 ? 205 HIS A O   1 
ATOM   1569 C CB  . HIS A 1 205 ? 24.18223 22.48810  -8.82536  1.000 28.23134 ? 205 HIS A CB  1 
ATOM   1570 C CG  . HIS A 1 205 ? 25.50131 22.90095  -9.36656  1.000 27.94632 ? 205 HIS A CG  1 
ATOM   1571 N ND1 . HIS A 1 205 ? 26.43988 21.99945  -9.80603  1.000 29.06450 ? 205 HIS A ND1 1 
ATOM   1572 C CD2 . HIS A 1 205 ? 26.01022 24.13023  -9.61142  1.000 28.78385 ? 205 HIS A CD2 1 
ATOM   1573 C CE1 . HIS A 1 205 ? 27.48848 22.65694  -10.27319 1.000 30.27651 ? 205 HIS A CE1 1 
ATOM   1574 N NE2 . HIS A 1 205 ? 27.25164 23.95272  -10.16801 1.000 29.65149 ? 205 HIS A NE2 1 
ATOM   1575 N N   . VAL A 1 206 ? 21.11106 22.44282  -9.86730  1.000 28.28290 ? 206 VAL A N   1 
ATOM   1576 C CA  . VAL A 1 206 ? 19.80272 21.81056  -9.81370  1.000 28.87334 ? 206 VAL A CA  1 
ATOM   1577 C C   . VAL A 1 206 ? 19.94049 20.39080  -10.33082 1.000 27.64762 ? 206 VAL A C   1 
ATOM   1578 O O   . VAL A 1 206 ? 20.47814 20.16381  -11.42325 1.000 30.08193 ? 206 VAL A O   1 
ATOM   1579 C CB  . VAL A 1 206 ? 18.75624 22.58350  -10.63890 1.000 30.93841 ? 206 VAL A CB  1 
ATOM   1580 C CG1 . VAL A 1 206 ? 17.42000 21.89397  -10.59901 1.000 32.35162 ? 206 VAL A CG1 1 
ATOM   1581 C CG2 . VAL A 1 206 ? 18.61835 24.00763  -10.13432 1.000 31.25668 ? 206 VAL A CG2 1 
ATOM   1582 N N   . VAL A 1 207 ? 19.46726 19.43831  -9.54826  1.000 25.63467 ? 207 VAL A N   1 
ATOM   1583 C CA  . VAL A 1 207 ? 19.45353 18.03795  -9.92697  1.000 25.26830 ? 207 VAL A CA  1 
ATOM   1584 C C   . VAL A 1 207 ? 18.00241 17.68023  -10.13126 1.000 25.78950 ? 207 VAL A C   1 
ATOM   1585 O O   . VAL A 1 207 ? 17.16858 17.87443  -9.23693  1.000 26.53810 ? 207 VAL A O   1 
ATOM   1586 C CB  . VAL A 1 207 ? 20.09613 17.14642  -8.85307  1.000 27.44304 ? 207 VAL A CB  1 
ATOM   1587 C CG1 . VAL A 1 207 ? 19.97791 15.66723  -9.23977  1.000 29.20906 ? 207 VAL A CG1 1 
ATOM   1588 C CG2 . VAL A 1 207 ? 21.52549 17.51897  -8.67149  1.000 28.46196 ? 207 VAL A CG2 1 
ATOM   1589 N N   . SER A 1 208 ? 17.69198 17.20432  -11.32839 1.000 27.05669 ? 208 SER A N   1 
ATOM   1590 C CA  . SER A 1 208 ? 16.34008 16.85547  -11.70588 1.000 28.87348 ? 208 SER A CA  1 
ATOM   1591 C C   . SER A 1 208 ? 16.27494 15.35693  -11.96602 1.000 29.45778 ? 208 SER A C   1 
ATOM   1592 O O   . SER A 1 208 ? 17.12599 14.82181  -12.68550 1.000 30.94288 ? 208 SER A O   1 
ATOM   1593 C CB  . SER A 1 208 ? 15.96491 17.63508  -12.96708 1.000 32.49409 ? 208 SER A CB  1 
ATOM   1594 O OG  . SER A 1 208 ? 14.75085 17.17635  -13.48466 1.000 39.33485 ? 208 SER A OG  1 
ATOM   1595 N N   . LEU A 1 209 ? 15.27581 14.68103  -11.39892 1.000 28.11464 ? 209 LEU A N   1 
ATOM   1596 C CA  . LEU A 1 209 ? 15.01898 13.28262  -11.70322 1.000 27.38206 ? 209 LEU A CA  1 
ATOM   1597 C C   . LEU A 1 209 ? 13.80978 13.21366  -12.62197 1.000 29.51423 ? 209 LEU A C   1 
ATOM   1598 O O   . LEU A 1 209 ? 12.76930 13.82215  -12.34087 1.000 31.19897 ? 209 LEU A O   1 
ATOM   1599 C CB  . LEU A 1 209 ? 14.75969 12.45314  -10.43968 1.000 25.32170 ? 209 LEU A CB  1 
ATOM   1600 C CG  . LEU A 1 209 ? 15.83206 12.58978  -9.39074  1.000 26.71299 ? 209 LEU A CG  1 
ATOM   1601 C CD1 . LEU A 1 209 ? 15.45111 11.66092  -8.24143  1.000 28.61791 ? 209 LEU A CD1 1 
ATOM   1602 C CD2 . LEU A 1 209 ? 17.20094 12.23294  -9.91368  1.000 28.36961 ? 209 LEU A CD2 1 
ATOM   1603 N N   . GLN A 1 210 ? 13.94617 12.49659  -13.72928 1.000 31.33672 ? 210 GLN A N   1 
ATOM   1604 C CA  . GLN A 1 210 ? 12.88876 12.47019  -14.72838 1.000 33.70218 ? 210 GLN A CA  1 
ATOM   1605 C C   . GLN A 1 210 ? 12.48975 11.02464  -14.99340 1.000 33.57603 ? 210 GLN A C   1 
ATOM   1606 O O   . GLN A 1 210 ? 13.35605 10.19701  -15.31236 1.000 33.67709 ? 210 GLN A O   1 
ATOM   1607 C CB  . GLN A 1 210 ? 13.37068 13.16285  -16.02968 1.000 36.38784 ? 210 GLN A CB  1 
ATOM   1608 C CG  . GLN A 1 210 ? 13.66640 14.65073  -15.82650 0.800 37.75461 ? 210 GLN A CG  1 
ATOM   1609 C CD  . GLN A 1 210 ? 14.35134 15.31317  -16.99422 0.700 40.66130 ? 210 GLN A CD  1 
ATOM   1610 O OE1 . GLN A 1 210 ? 14.46602 14.74001  -18.07546 0.700 42.03026 ? 210 GLN A OE1 1 
ATOM   1611 N NE2 . GLN A 1 210 ? 14.82002 16.54300  -16.77828 0.700 41.73038 ? 210 GLN A NE2 1 
ATOM   1612 N N   . PRO A 1 211 ? 11.20565 10.68849  -14.88982 1.000 34.52373 ? 211 PRO A N   1 
ATOM   1613 C CA  . PRO A 1 211 ? 10.78994 9.29125   -15.01733 1.000 35.17702 ? 211 PRO A CA  1 
ATOM   1614 C C   . PRO A 1 211 ? 11.02357 8.78012   -16.42317 1.000 37.21948 ? 211 PRO A C   1 
ATOM   1615 O O   . PRO A 1 211 ? 10.97846 9.53698   -17.39442 1.000 37.63311 ? 211 PRO A O   1 
ATOM   1616 C CB  . PRO A 1 211 ? 9.29689  9.34132   -14.71103 1.000 35.02298 ? 211 PRO A CB  1 
ATOM   1617 C CG  . PRO A 1 211 ? 9.08920  10.62143  -13.97830 1.000 36.45272 ? 211 PRO A CG  1 
ATOM   1618 C CD  . PRO A 1 211 ? 10.06121 11.56844  -14.60078 1.000 35.80438 ? 211 PRO A CD  1 
ATOM   1619 N N   . VAL A 1 212 ? 11.25798 7.47489   -16.51331 1.000 38.51543 ? 212 VAL A N   1 
ATOM   1620 C CA  . VAL A 1 212 ? 11.55319 6.80740   -17.76930 1.000 39.87223 ? 212 VAL A CA  1 
ATOM   1621 C C   . VAL A 1 212 ? 10.39574 5.92819   -18.21469 1.000 42.96104 ? 212 VAL A C   1 
ATOM   1622 O O   . VAL A 1 212 ? 10.01771 5.93627   -19.39060 1.000 44.03892 ? 212 VAL A O   1 
ATOM   1623 C CB  . VAL A 1 212 ? 12.85873 5.99199   -17.65351 1.000 37.35804 ? 212 VAL A CB  1 
ATOM   1624 C CG1 . VAL A 1 212 ? 13.05227 5.09865   -18.88366 1.000 37.59107 ? 212 VAL A CG1 1 
ATOM   1625 C CG2 . VAL A 1 212 ? 14.03160 6.92416   -17.48500 1.000 34.32417 ? 212 VAL A CG2 1 
ATOM   1626 N N   . ASN A 1 213 ? 9.79873  5.19575   -17.28072 1.000 44.92820 ? 213 ASN A N   1 
ATOM   1627 C CA  . ASN A 1 213 ? 8.60541  4.40766   -17.56164 1.000 46.85225 ? 213 ASN A CA  1 
ATOM   1628 C C   . ASN A 1 213 ? 7.51745  4.73593   -16.54670 1.000 47.40128 ? 213 ASN A C   1 
ATOM   1629 O O   . ASN A 1 213 ? 6.68629  5.62211   -16.76940 1.000 50.15353 ? 213 ASN A O   1 
ATOM   1630 C CB  . ASN A 1 213 ? 8.93264  2.91379   -17.53405 0.700 47.84968 ? 213 ASN A CB  1 
ATOM   1631 C CG  . ASN A 1 213 ? 7.88929  2.08099   -18.24207 0.600 50.19616 ? 213 ASN A CG  1 
ATOM   1632 O OD1 . ASN A 1 213 ? 6.78796  2.55775   -18.53741 0.600 50.64343 ? 213 ASN A OD1 1 
ATOM   1633 N ND2 . ASN A 1 213 ? 8.22381  0.82595   -18.51764 0.600 51.44734 ? 213 ASN A ND2 1 
ATOM   1634 N N   . ASP A 1 214 ? 7.51680  4.01967   -15.43195 1.000 46.55973 ? 214 ASP A N   1 
ATOM   1635 C CA  . ASP A 1 214 ? 6.59793  4.31144   -14.33961 1.000 46.20680 ? 214 ASP A CA  1 
ATOM   1636 C C   . ASP A 1 214 ? 6.73427  5.76312   -13.89951 1.000 42.68258 ? 214 ASP A C   1 
ATOM   1637 O O   . ASP A 1 214 ? 7.83544  6.31442   -13.83664 1.000 42.48527 ? 214 ASP A O   1 
ATOM   1638 C CB  . ASP A 1 214 ? 6.88466  3.35888   -13.16906 0.800 48.87684 ? 214 ASP A CB  1 
ATOM   1639 C CG  . ASP A 1 214 ? 5.88806  3.48332   -12.03496 0.700 52.38757 ? 214 ASP A CG  1 
ATOM   1640 O OD1 . ASP A 1 214 ? 5.04406  4.40145   -12.05591 0.700 53.92638 ? 214 ASP A OD1 1 
ATOM   1641 O OD2 . ASP A 1 214 ? 5.95188  2.64971   -11.10458 0.700 53.78199 ? 214 ASP A OD2 1 
ATOM   1642 N N   . LYS A 1 215 ? 5.60692  6.38411   -13.57741 1.000 41.36581 ? 215 LYS A N   1 
ATOM   1643 C CA  . LYS A 1 215 ? 5.60375  7.77256   -13.14439 1.000 41.51733 ? 215 LYS A CA  1 
ATOM   1644 C C   . LYS A 1 215 ? 5.17555  7.94454   -11.68486 1.000 39.95001 ? 215 LYS A C   1 
ATOM   1645 O O   . LYS A 1 215 ? 5.01746  9.07723   -11.23684 1.000 40.41359 ? 215 LYS A O   1 
ATOM   1646 C CB  . LYS A 1 215 ? 4.69870  8.60848   -14.04803 1.000 43.56020 ? 215 LYS A CB  1 
ATOM   1647 C CG  . LYS A 1 215 ? 5.02939  8.52254   -15.51917 0.800 45.96869 ? 215 LYS A CG  1 
ATOM   1648 C CD  . LYS A 1 215 ? 5.31221  9.91067   -16.08824 0.700 48.24619 ? 215 LYS A CD  1 
ATOM   1649 C CE  . LYS A 1 215 ? 4.03870  10.69002  -16.34855 0.700 50.05759 ? 215 LYS A CE  1 
ATOM   1650 N NZ  . LYS A 1 215 ? 3.36640  10.26359  -17.61341 0.600 51.53440 ? 215 LYS A NZ  1 
ATOM   1651 N N   . ASP A 1 216 ? 4.95901  6.86072   -10.94898 1.000 38.55253 ? 216 ASP A N   1 
ATOM   1652 C CA  . ASP A 1 216 ? 4.56705  6.94433   -9.54760  1.000 37.72856 ? 216 ASP A CA  1 
ATOM   1653 C C   . ASP A 1 216 ? 5.75840  6.67665   -8.63468  1.000 38.04298 ? 216 ASP A C   1 
ATOM   1654 O O   . ASP A 1 216 ? 6.48187  5.68714   -8.80611  1.000 39.23045 ? 216 ASP A O   1 
ATOM   1655 C CB  . ASP A 1 216 ? 3.46085  5.95582   -9.23325  0.900 36.88783 ? 216 ASP A CB  1 
ATOM   1656 C CG  . ASP A 1 216 ? 2.22376  6.18317   -10.07164 0.800 38.44180 ? 216 ASP A CG  1 
ATOM   1657 O OD1 . ASP A 1 216 ? 2.05574  7.27582   -10.65464 0.700 38.60805 ? 216 ASP A OD1 1 
ATOM   1658 O OD2 . ASP A 1 216 ? 1.41702  5.25395   -10.13188 0.700 39.56779 ? 216 ASP A OD2 1 
ATOM   1659 N N   . PHE A 1 217 ? 5.93436  7.53641   -7.64352  1.000 36.24984 ? 217 PHE A N   1 
ATOM   1660 C CA  . PHE A 1 217 ? 7.09926  7.44682   -6.77030  1.000 33.48020 ? 217 PHE A CA  1 
ATOM   1661 C C   . PHE A 1 217 ? 6.70348  7.66021   -5.32268  1.000 32.61053 ? 217 PHE A C   1 
ATOM   1662 O O   . PHE A 1 217 ? 5.80705  8.44266   -5.01746  1.000 33.89006 ? 217 PHE A O   1 
ATOM   1663 C CB  . PHE A 1 217 ? 8.14619  8.48406   -7.14039  1.000 33.23933 ? 217 PHE A CB  1 
ATOM   1664 C CG  . PHE A 1 217 ? 8.63138  8.35241   -8.55795  1.000 34.42884 ? 217 PHE A CG  1 
ATOM   1665 C CD1 . PHE A 1 217 ? 9.71026  7.51021   -8.85856  1.000 34.44866 ? 217 PHE A CD1 1 
ATOM   1666 C CD2 . PHE A 1 217 ? 8.03558  9.06707   -9.57222  1.000 34.38568 ? 217 PHE A CD2 1 
ATOM   1667 C CE1 . PHE A 1 217 ? 10.18978 7.37738   -10.14696 1.000 34.39271 ? 217 PHE A CE1 1 
ATOM   1668 C CE2 . PHE A 1 217 ? 8.49474  8.93785   -10.87657 1.000 35.48107 ? 217 PHE A CE2 1 
ATOM   1669 C CZ  . PHE A 1 217 ? 9.57177  8.08844   -11.16379 1.000 34.69595 ? 217 PHE A CZ  1 
ATOM   1670 N N   . GLN A 1 218 ? 7.44811  7.02188   -4.43336  1.000 30.51931 ? 218 GLN A N   1 
ATOM   1671 C CA  . GLN A 1 218 ? 7.32471  7.26364   -3.00611  1.000 30.40205 ? 218 GLN A CA  1 
ATOM   1672 C C   . GLN A 1 218 ? 8.43516  8.23594   -2.63451  1.000 30.81736 ? 218 GLN A C   1 
ATOM   1673 O O   . GLN A 1 218 ? 9.61351  7.93135   -2.83199  1.000 32.13304 ? 218 GLN A O   1 
ATOM   1674 C CB  . GLN A 1 218 ? 7.42400  5.94627   -2.24152  1.000 32.78783 ? 218 GLN A CB  1 
ATOM   1675 C CG  . GLN A 1 218 ? 7.16451  6.06807   -0.73946  1.000 35.95996 ? 218 GLN A CG  1 
ATOM   1676 C CD  . GLN A 1 218 ? 5.69629  5.87925   -0.38333  0.700 37.28564 ? 218 GLN A CD  1 
ATOM   1677 O OE1 . GLN A 1 218 ? 4.96022  5.19959   -1.09147  0.700 37.96010 ? 218 GLN A OE1 1 
ATOM   1678 N NE2 . GLN A 1 218 ? 5.26215  6.49587   0.70870   0.700 38.69708 ? 218 GLN A NE2 1 
ATOM   1679 N N   . ILE A 1 219 ? 8.06873  9.44016   -2.21023  1.000 29.97751 ? 219 ILE A N   1 
ATOM   1680 C CA  . ILE A 1 219 ? 9.04239  10.48989  -1.92000  1.000 31.07625 ? 219 ILE A CA  1 
ATOM   1681 C C   . ILE A 1 219 ? 9.03192  10.76596  -0.43037  1.000 32.16364 ? 219 ILE A C   1 
ATOM   1682 O O   . ILE A 1 219 ? 7.97598  11.05692  0.13979   1.000 33.21653 ? 219 ILE A O   1 
ATOM   1683 C CB  . ILE A 1 219 ? 8.74374  11.76584  -2.70882  1.000 32.63389 ? 219 ILE A CB  1 
ATOM   1684 C CG1 . ILE A 1 219 ? 8.83743  11.45033  -4.21720  1.000 31.43231 ? 219 ILE A CG1 1 
ATOM   1685 C CG2 . ILE A 1 219 ? 9.71946  12.85245  -2.31544  1.000 35.36806 ? 219 ILE A CG2 1 
ATOM   1686 C CD1 . ILE A 1 219 ? 8.28236  12.53953  -5.14731  1.000 32.59112 ? 219 ILE A CD1 1 
ATOM   1687 N N   . SER A 1 220 ? 10.18945 10.68327  0.20451   1.000 31.89721 ? 220 SER A N   1 
ATOM   1688 C CA  . SER A 1 220 ? 10.22979 10.99994  1.62194   1.000 34.37033 ? 220 SER A CA  1 
ATOM   1689 C C   . SER A 1 220 ? 10.95585 12.32869  1.78345   1.000 33.59376 ? 220 SER A C   1 
ATOM   1690 O O   . SER A 1 220 ? 11.84887 12.67452  0.98651   1.000 36.05221 ? 220 SER A O   1 
ATOM   1691 C CB  . SER A 1 220 ? 10.93331 9.90929   2.39858   1.000 41.04491 ? 220 SER A CB  1 
ATOM   1692 O OG  . SER A 1 220 ? 12.33149 10.02501  2.15123   1.000 46.87499 ? 220 SER A OG  1 
ATOM   1693 N N   . VAL A 1 221 ? 10.54628 13.08638  2.78825   1.000 29.82024 ? 221 VAL A N   1 
ATOM   1694 C CA  . VAL A 1 221 ? 11.20554 14.31002  3.19073   1.000 30.63861 ? 221 VAL A CA  1 
ATOM   1695 C C   . VAL A 1 221 ? 11.37365 14.18303  4.70867   1.000 31.25072 ? 221 VAL A C   1 
ATOM   1696 O O   . VAL A 1 221 ? 10.37993 14.20628  5.43458   1.000 30.85935 ? 221 VAL A O   1 
ATOM   1697 C CB  . VAL A 1 221 ? 10.36934 15.54177  2.84496   1.000 33.68358 ? 221 VAL A CB  1 
ATOM   1698 C CG1 . VAL A 1 221 ? 10.99800 16.79028  3.41352   1.000 33.99132 ? 221 VAL A CG1 1 
ATOM   1699 C CG2 . VAL A 1 221 ? 10.13930 15.64772  1.32175   1.000 35.07133 ? 221 VAL A CG2 1 
ATOM   1700 N N   . ASP A 1 222 ? 12.60190 13.98284  5.17911   1.000 30.31353 ? 222 ASP A N   1 
ATOM   1701 C CA  . ASP A 1 222 ? 12.80155 13.68216  6.62600   1.000 31.29862 ? 222 ASP A CA  1 
ATOM   1702 C C   . ASP A 1 222 ? 11.92364 12.45678  6.94683   1.000 34.17121 ? 222 ASP A C   1 
ATOM   1703 O O   . ASP A 1 222 ? 11.88152 11.47921  6.18604   1.000 36.74854 ? 222 ASP A O   1 
ATOM   1704 C CB  . ASP A 1 222 ? 12.57034 14.97190  7.41716   1.000 29.59522 ? 222 ASP A CB  1 
ATOM   1705 C CG  . ASP A 1 222 ? 13.62288 16.03725  7.08076   1.000 28.40948 ? 222 ASP A CG  1 
ATOM   1706 O OD1 . ASP A 1 222 ? 14.69600 15.63892  6.63040   1.000 28.18477 ? 222 ASP A OD1 1 
ATOM   1707 O OD2 . ASP A 1 222 ? 13.38421 17.25055  7.24256   1.000 29.03203 ? 222 ASP A OD2 1 
ATOM   1708 N N   . HIS A 1 223 ? 11.16620 12.37285  8.03717   1.000 36.24140 ? 223 HIS A N   1 
ATOM   1709 C CA  A HIS A 1 223 ? 10.37817 11.19806  8.39108   0.500 39.85180 ? 223 HIS A CA  1 
ATOM   1710 C CA  B HIS A 1 223 ? 10.56522 11.03916  8.08800   0.500 39.93880 ? 223 HIS A CA  1 
ATOM   1711 C C   . HIS A 1 223 ? 9.16211  10.96965  7.49170   1.000 41.33399 ? 223 HIS A C   1 
ATOM   1712 O O   . HIS A 1 223 ? 8.49580  9.93828   7.63607   1.000 46.13340 ? 223 HIS A O   1 
ATOM   1713 C CB  A HIS A 1 223 ? 9.91183  11.33457  9.85393   0.500 41.70115 ? 223 HIS A CB  1 
ATOM   1714 C CB  B HIS A 1 223 ? 10.57655 10.40849  9.47193   0.500 42.80355 ? 223 HIS A CB  1 
ATOM   1715 C CG  A HIS A 1 223 ? 9.43923  12.71391  10.21570  0.500 43.76615 ? 223 HIS A CG  1 
ATOM   1716 C CG  B HIS A 1 223 ? 10.74985 8.91899   9.40086   0.500 43.40080 ? 223 HIS A CG  1 
ATOM   1717 N ND1 A HIS A 1 223 ? 10.26648 13.81935  10.20162  0.500 43.60360 ? 223 HIS A ND1 1 
ATOM   1718 N ND1 B HIS A 1 223 ? 11.57148 8.32528   8.46211   0.500 42.42006 ? 223 HIS A ND1 1 
ATOM   1719 C CD2 A HIS A 1 223 ? 8.22589  13.16164  10.61803  0.500 44.84577 ? 223 HIS A CD2 1 
ATOM   1720 C CD2 B HIS A 1 223 ? 10.19151 7.90665   10.10771  0.500 43.68351 ? 223 HIS A CD2 1 
ATOM   1721 C CE1 A HIS A 1 223 ? 9.58147  14.88841  10.56204  0.500 44.18122 ? 223 HIS A CE1 1 
ATOM   1722 C CE1 B HIS A 1 223 ? 11.53094 7.01302   8.61218   0.500 42.81249 ? 223 HIS A CE1 1 
ATOM   1723 N NE2 A HIS A 1 223 ? 8.34017  14.51691  10.82698  0.500 45.20926 ? 223 HIS A NE2 1 
ATOM   1724 N NE2 B HIS A 1 223 ? 10.70013 6.73251   9.60266   0.500 43.86969 ? 223 HIS A NE2 1 
ATOM   1725 N N   . LEU A 1 224 ? 8.78881  11.92810  6.65820   1.000 39.41779 ? 224 LEU A N   1 
ATOM   1726 C CA  . LEU A 1 224 ? 7.45812  11.95241  6.05121   1.000 39.15970 ? 224 LEU A CA  1 
ATOM   1727 C C   . LEU A 1 224 ? 7.52198  11.33473  4.65851   1.000 42.05952 ? 224 LEU A C   1 
ATOM   1728 O O   . LEU A 1 224 ? 8.21281  11.87102  3.78605   1.000 44.29467 ? 224 LEU A O   1 
ATOM   1729 C CB  . LEU A 1 224 ? 6.96705  13.38740  5.95305   1.000 40.62002 ? 224 LEU A CB  1 
ATOM   1730 C CG  . LEU A 1 224 ? 5.69279  13.51704  5.11233   1.000 46.90265 ? 224 LEU A CG  1 
ATOM   1731 C CD1 . LEU A 1 224 ? 4.50311  12.91042  5.86663   1.000 49.68674 ? 224 LEU A CD1 1 
ATOM   1732 C CD2 . LEU A 1 224 ? 5.42324  14.97540  4.72009   1.000 48.34197 ? 224 LEU A CD2 1 
ATOM   1733 N N   . SER A 1 225 ? 6.80355  10.22797  4.45308   1.000 41.95669 ? 225 SER A N   1 
ATOM   1734 C CA  . SER A 1 225 ? 6.80170  9.49204   3.19471   1.000 43.69939 ? 225 SER A CA  1 
ATOM   1735 C C   . SER A 1 225 ? 5.43704  9.62807   2.52718   1.000 43.55147 ? 225 SER A C   1 
ATOM   1736 O O   . SER A 1 225 ? 4.40560  9.40499   3.16927   1.000 46.29178 ? 225 SER A O   1 
ATOM   1737 C CB  . SER A 1 225 ? 7.12797  8.02017   3.44923   1.000 47.13930 ? 225 SER A CB  1 
ATOM   1738 O OG  . SER A 1 225 ? 7.33540  7.28900   2.25880   1.000 48.86714 ? 225 SER A OG  1 
ATOM   1739 N N   . ILE A 1 226 ? 5.43461  9.96485   1.23727   1.000 43.01575 ? 226 ILE A N   1 
ATOM   1740 C CA  . ILE A 1 226 ? 4.21832  10.30171  0.50817   1.000 44.08612 ? 226 ILE A CA  1 
ATOM   1741 C C   . ILE A 1 226 ? 4.26365  9.63931   -0.85645  1.000 41.01283 ? 226 ILE A C   1 
ATOM   1742 O O   . ILE A 1 226 ? 5.29248  9.66619   -1.54065  1.000 40.73863 ? 226 ILE A O   1 
ATOM   1743 C CB  . ILE A 1 226 ? 4.06475  11.82945  0.34811   1.000 49.86480 ? 226 ILE A CB  1 
ATOM   1744 C CG1 . ILE A 1 226 ? 3.93487  12.50085  1.71685   1.000 53.10570 ? 226 ILE A CG1 1 
ATOM   1745 C CG2 . ILE A 1 226 ? 2.88030  12.17935  -0.57070  1.000 51.13481 ? 226 ILE A CG2 1 
ATOM   1746 C CD1 . ILE A 1 226 ? 4.06766  14.00181  1.65917   1.000 54.34440 ? 226 ILE A CD1 1 
ATOM   1747 N N   . LEU A 1 227 ? 3.14825  9.05173   -1.26326  1.000 40.28828 ? 227 LEU A N   1 
ATOM   1748 C CA  . LEU A 1 227 ? 3.05391  8.52081   -2.61675  1.000 42.66103 ? 227 LEU A CA  1 
ATOM   1749 C C   . LEU A 1 227 ? 2.68405  9.64973   -3.56851  1.000 45.10136 ? 227 LEU A C   1 
ATOM   1750 O O   . LEU A 1 227 ? 1.66914  10.32050  -3.37417  1.000 46.64122 ? 227 LEU A O   1 
ATOM   1751 C CB  . LEU A 1 227 ? 2.01582  7.40632   -2.68142  1.000 42.99051 ? 227 LEU A CB  1 
ATOM   1752 C CG  . LEU A 1 227 ? 1.77347  6.81167   -4.07093  1.000 43.46049 ? 227 LEU A CG  1 
ATOM   1753 C CD1 . LEU A 1 227 ? 3.04688  6.29006   -4.64469  1.000 43.88952 ? 227 LEU A CD1 1 
ATOM   1754 C CD2 . LEU A 1 227 ? 0.74007  5.71415   -3.96113  1.000 44.12072 ? 227 LEU A CD2 1 
ATOM   1755 N N   . HIS A 1 228 ? 3.49357  9.86836   -4.59780  1.000 45.62116 ? 228 HIS A N   1 
ATOM   1756 C CA  . HIS A 1 228 ? 3.17354  10.85676  -5.61937  1.000 46.60637 ? 228 HIS A CA  1 
ATOM   1757 C C   . HIS A 1 228 ? 2.87634  10.14079  -6.92667  1.000 44.01556 ? 228 HIS A C   1 
ATOM   1758 O O   . HIS A 1 228 ? 3.63760  9.27452   -7.35878  1.000 43.43984 ? 228 HIS A O   1 
ATOM   1759 C CB  . HIS A 1 228 ? 4.31518  11.85429  -5.80605  1.000 51.24947 ? 228 HIS A CB  1 
ATOM   1760 C CG  . HIS A 1 228 ? 4.53815  12.74663  -4.62734  1.000 55.49614 ? 228 HIS A CG  1 
ATOM   1761 N ND1 . HIS A 1 228 ? 4.15150  14.06981  -4.61105  1.000 57.63539 ? 228 HIS A ND1 1 
ATOM   1762 C CD2 . HIS A 1 228 ? 5.11583  12.50758  -3.42539  1.000 57.79045 ? 228 HIS A CD2 1 
ATOM   1763 C CE1 . HIS A 1 228 ? 4.47990  14.60672  -3.44832  1.000 59.08313 ? 228 HIS A CE1 1 
ATOM   1764 N NE2 . HIS A 1 228 ? 5.06697  13.68052  -2.71037  1.000 58.88042 ? 228 HIS A NE2 1 
ATOM   1765 N N   . ARG A 1 229 ? 1.77190  10.49719  -7.54512  1.000 44.55690 ? 229 ARG A N   1 
ATOM   1766 C CA  . ARG A 1 229 ? 1.34552  9.86800   -8.77497  1.000 45.49540 ? 229 ARG A CA  1 
ATOM   1767 C C   . ARG A 1 229 ? 1.47327  10.87090  -9.90635  1.000 45.76135 ? 229 ARG A C   1 
ATOM   1768 O O   . ARG A 1 229 ? 1.28785  12.07496  -9.70582  1.000 44.96137 ? 229 ARG A O   1 
ATOM   1769 C CB  . ARG A 1 229 ? -0.09662 9.36691   -8.65015  1.000 45.64933 ? 229 ARG A CB  1 
ATOM   1770 C CG  . ARG A 1 229 ? -0.23894 8.16565   -7.70897  1.000 46.17400 ? 229 ARG A CG  1 
ATOM   1771 C CD  . ARG A 1 229 ? -1.68479 7.70393   -7.61234  0.800 47.87746 ? 229 ARG A CD  1 
ATOM   1772 N NE  . ARG A 1 229 ? -1.75106 6.29273   -7.25179  0.700 51.51450 ? 229 ARG A NE  1 
ATOM   1773 C CZ  . ARG A 1 229 ? -2.15453 5.83187   -6.07763  0.700 54.19495 ? 229 ARG A CZ  1 
ATOM   1774 N NH1 . ARG A 1 229 ? -2.58188 6.64524   -5.12683  0.700 55.01378 ? 229 ARG A NH1 1 
ATOM   1775 N NH2 . ARG A 1 229 ? -2.13710 4.52005   -5.85499  0.700 55.35911 ? 229 ARG A NH2 1 
ATOM   1776 N N   . ASP A 1 230 ? 1.80475  10.36465  -11.09634 1.000 46.98778 ? 230 ASP A N   1 
ATOM   1777 C CA  . ASP A 1 230 ? 1.81059  11.18942  -12.30339 1.000 51.17875 ? 230 ASP A CA  1 
ATOM   1778 C C   . ASP A 1 230 ? 2.89900  12.26465  -12.22526 1.000 48.24645 ? 230 ASP A C   1 
ATOM   1779 O O   . ASP A 1 230 ? 2.67873  13.42751  -12.56338 1.000 48.80485 ? 230 ASP A O   1 
ATOM   1780 C CB  . ASP A 1 230 ? 0.42013  11.80515  -12.53713 1.000 56.74144 ? 230 ASP A CB  1 
ATOM   1781 C CG  . ASP A 1 230 ? 0.29592  12.51022  -13.87324 1.000 63.20586 ? 230 ASP A CG  1 
ATOM   1782 O OD1 . ASP A 1 230 ? 0.77526  11.95169  -14.89204 1.000 65.14814 ? 230 ASP A OD1 1 
ATOM   1783 O OD2 . ASP A 1 230 ? -0.29624 13.62090  -13.90352 1.000 65.88456 ? 230 ASP A OD2 1 
ATOM   1784 N N   . VAL A 1 231 ? 4.08769  11.87035  -11.76683 1.000 44.80632 ? 231 VAL A N   1 
ATOM   1785 C CA  . VAL A 1 231 ? 5.18207  12.81293  -11.58118 1.000 40.31758 ? 231 VAL A CA  1 
ATOM   1786 C C   . VAL A 1 231 ? 5.87524  13.05108  -12.91199 1.000 40.69320 ? 231 VAL A C   1 
ATOM   1787 O O   . VAL A 1 231 ? 6.16664  12.10118  -13.64865 1.000 42.62543 ? 231 VAL A O   1 
ATOM   1788 C CB  . VAL A 1 231 ? 6.17511  12.28106  -10.54015 1.000 39.85865 ? 231 VAL A CB  1 
ATOM   1789 C CG1 . VAL A 1 231 ? 7.48092  12.99691  -10.66628 1.000 38.26543 ? 231 VAL A CG1 1 
ATOM   1790 C CG2 . VAL A 1 231 ? 5.58925  12.43181  -9.12553  1.000 41.31633 ? 231 VAL A CG2 1 
ATOM   1791 N N   . GLN A 1 232 ? 6.14011  14.31744  -13.22675 1.000 39.16765 ? 232 GLN A N   1 
ATOM   1792 C CA  . GLN A 1 232 ? 6.93909  14.65913  -14.39625 1.000 39.93223 ? 232 GLN A CA  1 
ATOM   1793 C C   . GLN A 1 232 ? 8.39938  14.89417  -14.06160 1.000 40.40390 ? 232 GLN A C   1 
ATOM   1794 O O   . GLN A 1 232 ? 9.27076  14.65797  -14.90801 1.000 42.74220 ? 232 GLN A O   1 
ATOM   1795 C CB  . GLN A 1 232 ? 6.37924  15.91027  -15.08278 1.000 40.42433 ? 232 GLN A CB  1 
ATOM   1796 N N   . GLU A 1 233 ? 8.69047  15.33696  -12.84351 1.000 38.51029 ? 233 GLU A N   1 
ATOM   1797 C CA  . GLU A 1 233 ? 10.04306 15.76318  -12.49640 1.000 37.00184 ? 233 GLU A CA  1 
ATOM   1798 C C   . GLU A 1 233 ? 10.12682 15.92983  -10.98985 1.000 33.26748 ? 233 GLU A C   1 
ATOM   1799 O O   . GLU A 1 233 ? 9.17990  16.42093  -10.37180 1.000 33.38637 ? 233 GLU A O   1 
ATOM   1800 C CB  . GLU A 1 233 ? 10.36650 17.09739  -13.18156 1.000 39.01554 ? 233 GLU A CB  1 
ATOM   1801 C CG  . GLU A 1 233 ? 11.76533 17.61265  -12.95702 0.800 40.43255 ? 233 GLU A CG  1 
ATOM   1802 C CD  . GLU A 1 233 ? 11.94569 19.01265  -13.51317 0.700 41.50636 ? 233 GLU A CD  1 
ATOM   1803 O OE1 . GLU A 1 233 ? 10.93527 19.69489  -13.68010 0.700 41.77827 ? 233 GLU A OE1 1 
ATOM   1804 O OE2 . GLU A 1 233 ? 13.08979 19.44119  -13.77437 0.700 42.01361 ? 233 GLU A OE2 1 
ATOM   1805 N N   . ILE A 1 234 ? 11.25442 15.52527  -10.40482 1.000 31.59382 ? 234 ILE A N   1 
ATOM   1806 C CA  . ILE A 1 234 ? 11.60519 15.86474  -9.02984  1.000 30.72166 ? 234 ILE A CA  1 
ATOM   1807 C C   . ILE A 1 234 ? 12.88529 16.67774  -9.10537  1.000 30.70081 ? 234 ILE A C   1 
ATOM   1808 O O   . ILE A 1 234 ? 13.84166 16.24362  -9.75356  1.000 31.98089 ? 234 ILE A O   1 
ATOM   1809 C CB  . ILE A 1 234 ? 11.81320 14.61491  -8.15287  1.000 31.47931 ? 234 ILE A CB  1 
ATOM   1810 C CG1 . ILE A 1 234 ? 10.56935 13.72182  -8.14013  1.000 32.95760 ? 234 ILE A CG1 1 
ATOM   1811 C CG2 . ILE A 1 234 ? 12.25009 15.03451  -6.74336  1.000 32.56843 ? 234 ILE A CG2 1 
ATOM   1812 C CD1 . ILE A 1 234 ? 10.88030 12.22806  -7.97570  1.000 33.97993 ? 234 ILE A CD1 1 
ATOM   1813 N N   . ARG A 1 235 ? 12.88625 17.87281  -8.50991  1.000 28.61652 ? 235 ARG A N   1 
ATOM   1814 C CA  . ARG A 1 235 ? 14.01992 18.78494  -8.61786  1.000 29.22054 ? 235 ARG A CA  1 
ATOM   1815 C C   . ARG A 1 235 ? 14.58664 19.04104  -7.23274  1.000 28.76345 ? 235 ARG A C   1 
ATOM   1816 O O   . ARG A 1 235 ? 13.83508 19.36290  -6.31159  1.000 29.83028 ? 235 ARG A O   1 
ATOM   1817 C CB  . ARG A 1 235 ? 13.62165 20.13817  -9.21699  1.000 33.30525 ? 235 ARG A CB  1 
ATOM   1818 C CG  . ARG A 1 235 ? 13.17984 20.04820  -10.65177 1.000 39.06675 ? 235 ARG A CG  1 
ATOM   1819 C CD  . ARG A 1 235 ? 12.57151 21.34961  -11.19286 0.800 42.61314 ? 235 ARG A CD  1 
ATOM   1820 N NE  . ARG A 1 235 ? 13.50074 22.46540  -11.25908 0.700 44.63143 ? 235 ARG A NE  1 
ATOM   1821 C CZ  . ARG A 1 235 ? 14.20960 22.78849  -12.33350 0.700 48.40031 ? 235 ARG A CZ  1 
ATOM   1822 N NH1 . ARG A 1 235 ? 14.19379 22.03703  -13.42716 0.700 48.34165 ? 235 ARG A NH1 1 
ATOM   1823 N NH2 . ARG A 1 235 ? 14.96137 23.88959  -12.30891 0.700 50.22641 ? 235 ARG A NH2 1 
ATOM   1824 N N   . TYR A 1 236 ? 15.89847 18.98387  -7.13003  1.000 27.49720 ? 236 TYR A N   1 
ATOM   1825 C CA  . TYR A 1 236 ? 16.61894 19.24252  -5.88300  1.000 27.23677 ? 236 TYR A CA  1 
ATOM   1826 C C   . TYR A 1 236 ? 17.55807 20.43021  -6.01815  1.000 27.71018 ? 236 TYR A C   1 
ATOM   1827 O O   . TYR A 1 236 ? 18.28072 20.55413  -7.01642  1.000 28.34904 ? 236 TYR A O   1 
ATOM   1828 C CB  . TYR A 1 236 ? 17.46804 18.04128  -5.48041  1.000 28.07875 ? 236 TYR A CB  1 
ATOM   1829 C CG  . TYR A 1 236 ? 16.66943 16.81018  -5.16812  1.000 31.38459 ? 236 TYR A CG  1 
ATOM   1830 C CD1 . TYR A 1 236 ? 15.85646 16.74802  -4.01553  1.000 32.40839 ? 236 TYR A CD1 1 
ATOM   1831 C CD2 . TYR A 1 236 ? 16.74346 15.69007  -5.97534  1.000 33.52854 ? 236 TYR A CD2 1 
ATOM   1832 C CE1 . TYR A 1 236 ? 15.14081 15.61536  -3.70491  1.000 34.29722 ? 236 TYR A CE1 1 
ATOM   1833 C CE2 . TYR A 1 236 ? 16.02780 14.54766  -5.65228  1.000 36.68047 ? 236 TYR A CE2 1 
ATOM   1834 C CZ  . TYR A 1 236 ? 15.21814 14.52774  -4.53103  1.000 37.74165 ? 236 TYR A CZ  1 
ATOM   1835 O OH  . TYR A 1 236 ? 14.51428 13.38795  -4.21070  1.000 43.36840 ? 236 TYR A OH  1 
ATOM   1836 N N   . GLU A 1 237 ? 17.62562 21.26058  -4.98127  1.000 27.96625 ? 237 GLU A N   1 
ATOM   1837 C CA  . GLU A 1 237 ? 18.58406 22.35556  -4.95055  1.000 27.74837 ? 237 GLU A CA  1 
ATOM   1838 C C   . GLU A 1 237 ? 18.76148 22.73521  -3.49653  1.000 27.60426 ? 237 GLU A C   1 
ATOM   1839 O O   . GLU A 1 237 ? 17.85039 22.53985  -2.69532  1.000 26.49609 ? 237 GLU A O   1 
ATOM   1840 C CB  . GLU A 1 237 ? 18.13320 23.58101  -5.75548  1.000 30.86892 ? 237 GLU A CB  1 
ATOM   1841 C CG  . GLU A 1 237 ? 16.76540 24.10569  -5.46890  0.800 33.90960 ? 237 GLU A CG  1 
ATOM   1842 C CD  . GLU A 1 237 ? 16.13724 24.76904  -6.72364  0.700 37.39258 ? 237 GLU A CD  1 
ATOM   1843 O OE1 . GLU A 1 237 ? 16.79171 25.62328  -7.35005  0.700 37.81445 ? 237 GLU A OE1 1 
ATOM   1844 O OE2 . GLU A 1 237 ? 14.99717 24.42590  -7.11551  0.700 39.05488 ? 237 GLU A OE2 1 
ATOM   1845 N N   . VAL A 1 238 ? 19.91883 23.30627  -3.18249  1.000 26.13283 ? 238 VAL A N   1 
ATOM   1846 C CA  . VAL A 1 238 ? 20.09464 23.89323  -1.85119  1.000 25.06525 ? 238 VAL A CA  1 
ATOM   1847 C C   . VAL A 1 238 ? 19.11072 25.04746  -1.65526  1.000 28.32518 ? 238 VAL A C   1 
ATOM   1848 O O   . VAL A 1 238 ? 18.97687 25.94389  -2.50035  1.000 28.75791 ? 238 VAL A O   1 
ATOM   1849 C CB  . VAL A 1 238 ? 21.55884 24.30818  -1.66316  1.000 23.47599 ? 238 VAL A CB  1 
ATOM   1850 C CG1 . VAL A 1 238 ? 21.75801 24.92753  -0.23455  1.000 24.62863 ? 238 VAL A CG1 1 
ATOM   1851 C CG2 . VAL A 1 238 ? 22.38834 23.06284  -1.81722  1.000 23.64538 ? 238 VAL A CG2 1 
ATOM   1852 N N   . SER A 1 239 ? 18.36487 25.00483  -0.55980  1.000 30.07522 ? 239 SER A N   1 
ATOM   1853 C CA  . SER A 1 239 ? 17.37396 26.03926  -0.29308  1.000 31.79766 ? 239 SER A CA  1 
ATOM   1854 C C   . SER A 1 239 ? 18.06457 27.36303  0.00411   1.000 34.37353 ? 239 SER A C   1 
ATOM   1855 O O   . SER A 1 239 ? 19.21312 27.40122  0.45818   1.000 35.65875 ? 239 SER A O   1 
ATOM   1856 C CB  . SER A 1 239 ? 16.48913 25.62697  0.89245   1.000 33.27977 ? 239 SER A CB  1 
ATOM   1857 O OG  . SER A 1 239 ? 15.62823 26.69387  1.28924   1.000 34.58941 ? 239 SER A OG  1 
ATOM   1858 N N   . ALA A 1 240 ? 17.36813 28.46369  -0.27189  1.000 35.61465 ? 240 ALA A N   1 
ATOM   1859 C CA  . ALA A 1 240 ? 17.80269 29.75441  0.25410   1.000 36.23209 ? 240 ALA A CA  1 
ATOM   1860 C C   . ALA A 1 240 ? 17.51295 29.89190  1.73617   1.000 36.79476 ? 240 ALA A C   1 
ATOM   1861 O O   . ALA A 1 240 ? 18.11565 30.74384  2.40347   1.000 38.92850 ? 240 ALA A O   1 
ATOM   1862 C CB  . ALA A 1 240 ? 17.11664 30.88891  -0.48300  1.000 37.30122 ? 240 ALA A CB  1 
ATOM   1863 N N   . LYS A 1 241 ? 16.60344 29.08300  2.26564   1.000 35.96434 ? 241 LYS A N   1 
ATOM   1864 C CA  . LYS A 1 241 ? 16.25801 29.13644  3.68253   1.000 35.09965 ? 241 LYS A CA  1 
ATOM   1865 C C   . LYS A 1 241 ? 17.28466 28.36743  4.49302   1.000 35.27592 ? 241 LYS A C   1 
ATOM   1866 O O   . LYS A 1 241 ? 17.89510 27.41420  4.00747   1.000 36.31101 ? 241 LYS A O   1 
ATOM   1867 C CB  . LYS A 1 241 ? 14.85756 28.56432  3.90049   1.000 35.32119 ? 241 LYS A CB  1 
ATOM   1868 C CG  . LYS A 1 241 ? 13.76536 29.35236  3.15581   0.800 35.13717 ? 241 LYS A CG  1 
ATOM   1869 C CD  . LYS A 1 241 ? 12.47677 28.53885  3.01917   0.700 37.25175 ? 241 LYS A CD  1 
ATOM   1870 C CE  . LYS A 1 241 ? 11.39319 29.29546  2.23726   0.700 39.02620 ? 241 LYS A CE  1 
ATOM   1871 N NZ  . LYS A 1 241 ? 10.06745 28.58149  2.27600   0.700 40.64410 ? 241 LYS A NZ  1 
ATOM   1872 N N   . LYS A 1 242 ? 17.45333 28.77093  5.75692   1.000 34.90999 ? 242 LYS A N   1 
ATOM   1873 C CA  . LYS A 1 242 ? 18.39500 28.13717  6.66763   1.000 34.28373 ? 242 LYS A CA  1 
ATOM   1874 C C   . LYS A 1 242 ? 17.68840 27.89186  7.97871   1.000 33.11294 ? 242 LYS A C   1 
ATOM   1875 O O   . LYS A 1 242 ? 16.72498 28.58984  8.30401   1.000 34.79406 ? 242 LYS A O   1 
ATOM   1876 C CB  . LYS A 1 242 ? 19.60901 29.01109  6.93018   1.000 37.95780 ? 242 LYS A CB  1 
ATOM   1877 C CG  . LYS A 1 242 ? 20.37365 29.41222  5.67507   1.000 41.22089 ? 242 LYS A CG  1 
ATOM   1878 C CD  . LYS A 1 242 ? 21.83497 29.70326  5.97652   1.000 46.32975 ? 242 LYS A CD  1 
ATOM   1879 C CE  . LYS A 1 242 ? 22.71393 28.49395  5.65264   1.000 49.22148 ? 242 LYS A CE  1 
ATOM   1880 N NZ  . LYS A 1 242 ? 23.91316 28.35146  6.55203   1.000 50.00180 ? 242 LYS A NZ  1 
ATOM   1881 N N   . ILE A 1 243 ? 18.14973 26.88652  8.72360   1.000 31.33535 ? 243 ILE A N   1 
ATOM   1882 C CA  . ILE A 1 243 ? 17.67664 26.68349  10.09025  1.000 30.09755 ? 243 ILE A CA  1 
ATOM   1883 C C   . ILE A 1 243 ? 18.69774 27.30139  11.02643  1.000 30.87332 ? 243 ILE A C   1 
ATOM   1884 O O   . ILE A 1 243 ? 19.90675 27.20247  10.80708  1.000 31.64624 ? 243 ILE A O   1 
ATOM   1885 C CB  . ILE A 1 243 ? 17.45077 25.19370  10.42504  1.000 29.79652 ? 243 ILE A CB  1 
ATOM   1886 C CG1 . ILE A 1 243 ? 16.87083 25.01501  11.84503  1.000 31.00955 ? 243 ILE A CG1 1 
ATOM   1887 C CG2 . ILE A 1 243 ? 18.73416 24.37904  10.24569  1.000 29.94298 ? 243 ILE A CG2 1 
ATOM   1888 C CD1 . ILE A 1 243 ? 16.77770 23.56440  12.26374  1.000 31.23939 ? 243 ILE A CD1 1 
ATOM   1889 N N   . HIS A 1 244 ? 18.20972 27.94038  12.07527  1.000 32.16603 ? 244 HIS A N   1 
ATOM   1890 C CA  . HIS A 1 244 ? 19.05632 28.62813  13.03948  1.000 32.92670 ? 244 HIS A CA  1 
ATOM   1891 C C   . HIS A 1 244 ? 18.98362 27.90455  14.36722  1.000 32.39405 ? 244 HIS A C   1 
ATOM   1892 O O   . HIS A 1 244 ? 17.88766 27.55211  14.82271  1.000 32.83723 ? 244 HIS A O   1 
ATOM   1893 C CB  . HIS A 1 244 ? 18.61860 30.08485  13.18232  1.000 35.78849 ? 244 HIS A CB  1 
ATOM   1894 C CG  . HIS A 1 244 ? 18.58137 30.82073  11.87414  1.000 39.68813 ? 244 HIS A CG  1 
ATOM   1895 N ND1 . HIS A 1 244 ? 19.68805 31.44060  11.32910  1.000 40.21538 ? 244 HIS A ND1 1 
ATOM   1896 C CD2 . HIS A 1 244 ? 17.57241 31.01405  10.99170  1.000 41.46254 ? 244 HIS A CD2 1 
ATOM   1897 C CE1 . HIS A 1 244 ? 19.35942 31.99391  10.17384  1.000 41.22703 ? 244 HIS A CE1 1 
ATOM   1898 N NE2 . HIS A 1 244 ? 18.08152 31.74763  9.94433   1.000 41.93165 ? 244 HIS A NE2 1 
ATOM   1899 N N   . PHE A 1 245 ? 20.14529 27.66902  14.97007  1.000 32.41935 ? 245 PHE A N   1 
ATOM   1900 C CA  . PHE A 1 245 ? 20.23911 27.08273  16.30558  1.000 35.42020 ? 245 PHE A CA  1 
ATOM   1901 C C   . PHE A 1 245 ? 20.71165 28.13174  17.30110  1.000 37.52063 ? 245 PHE A C   1 
ATOM   1902 O O   . PHE A 1 245 ? 21.56004 28.96891  16.98392  1.000 37.72194 ? 245 PHE A O   1 
ATOM   1903 C CB  . PHE A 1 245 ? 21.20524 25.90214  16.31969  1.000 36.09385 ? 245 PHE A CB  1 
ATOM   1904 C CG  . PHE A 1 245 ? 20.80147 24.77405  15.43782  1.000 37.51897 ? 245 PHE A CG  1 
ATOM   1905 C CD1 . PHE A 1 245 ? 21.13540 24.77429  14.09222  1.000 38.82314 ? 245 PHE A CD1 1 
ATOM   1906 C CD2 . PHE A 1 245 ? 20.09654 23.70224  15.94875  1.000 39.05405 ? 245 PHE A CD2 1 
ATOM   1907 C CE1 . PHE A 1 245 ? 20.75292 23.71955  13.27269  1.000 39.47734 ? 245 PHE A CE1 1 
ATOM   1908 C CE2 . PHE A 1 245 ? 19.71899 22.65631  15.15007  1.000 40.53011 ? 245 PHE A CE2 1 
ATOM   1909 C CZ  . PHE A 1 245 ? 20.04703 22.65329  13.80514  1.000 39.91020 ? 245 PHE A CZ  1 
ATOM   1910 N N   . ALA A 1 246 ? 20.18148 28.08262  18.52189  1.000 37.52785 ? 246 ALA A N   1 
ATOM   1911 C CA  . ALA A 1 246 ? 20.74750 28.88849  19.59035  1.000 37.48337 ? 246 ALA A CA  1 
ATOM   1912 C C   . ALA A 1 246 ? 21.89592 28.09680  20.20207  1.000 38.65383 ? 246 ALA A C   1 
ATOM   1913 O O   . ALA A 1 246 ? 21.71166 26.94113  20.59905  1.000 38.71817 ? 246 ALA A O   1 
ATOM   1914 C CB  . ALA A 1 246 ? 19.68599 29.22266  20.63867  1.000 37.60211 ? 246 ALA A CB  1 
ATOM   1915 N N   . ARG A 1 247 ? 23.08351 28.69057  20.24309  1.000 38.66041 ? 247 ARG A N   1 
ATOM   1916 C CA  . ARG A 1 247 ? 24.24849 28.02332  20.81239  1.000 43.10513 ? 247 ARG A CA  1 
ATOM   1917 C C   . ARG A 1 247 ? 24.72912 28.81324  22.01631  1.000 44.56503 ? 247 ARG A C   1 
ATOM   1918 O O   . ARG A 1 247 ? 24.86415 30.03548  21.94583  1.000 45.76630 ? 247 ARG A O   1 
ATOM   1919 C CB  . ARG A 1 247 ? 25.37598 27.88288  19.79658  1.000 46.32377 ? 247 ARG A CB  1 
ATOM   1920 C CG  . ARG A 1 247 ? 25.01492 27.03225  18.60935  1.000 50.16337 ? 247 ARG A CG  1 
ATOM   1921 C CD  . ARG A 1 247 ? 25.02159 25.52654  18.87820  1.000 53.27471 ? 247 ARG A CD  1 
ATOM   1922 N NE  . ARG A 1 247 ? 25.16379 24.79932  17.61526  1.000 55.76220 ? 247 ARG A NE  1 
ATOM   1923 C CZ  . ARG A 1 247 ? 24.43808 23.74452  17.26555  1.000 56.65558 ? 247 ARG A CZ  1 
ATOM   1924 N NH1 . ARG A 1 247 ? 23.50408 23.25407  18.06431  1.000 57.38220 ? 247 ARG A NH1 1 
ATOM   1925 N NH2 . ARG A 1 247 ? 24.64017 23.18131  16.07585  1.000 56.30923 ? 247 ARG A NH2 1 
ATOM   1926 N N   . PHE A 1 248 ? 24.96747 28.12067  23.12042  1.000 45.47024 ? 248 PHE A N   1 
ATOM   1927 C CA  . PHE A 1 248 ? 25.39233 28.76947  24.35124  1.000 46.69623 ? 248 PHE A CA  1 
ATOM   1928 C C   . PHE A 1 248 ? 26.81825 28.44002  24.71578  1.000 46.53183 ? 248 PHE A C   1 
ATOM   1929 O O   . PHE A 1 248 ? 27.36351 29.04708  25.64646  1.000 46.53245 ? 248 PHE A O   1 
ATOM   1930 C CB  . PHE A 1 248 ? 24.47672 28.36318  25.50484  1.000 49.50739 ? 248 PHE A CB  1 
ATOM   1931 C CG  . PHE A 1 248 ? 23.07912 28.80531  25.30280  1.000 51.89029 ? 248 PHE A CG  1 
ATOM   1932 C CD1 . PHE A 1 248 ? 22.20575 28.03297  24.55040  1.000 53.59358 ? 248 PHE A CD1 1 
ATOM   1933 C CD2 . PHE A 1 248 ? 22.65558 30.02675  25.78425  1.000 52.18191 ? 248 PHE A CD2 1 
ATOM   1934 C CE1 . PHE A 1 248 ? 20.91109 28.45599  24.33259  1.000 54.35333 ? 248 PHE A CE1 1 
ATOM   1935 C CE2 . PHE A 1 248 ? 21.36781 30.45006  25.57518  1.000 52.55398 ? 248 PHE A CE2 1 
ATOM   1936 C CZ  . PHE A 1 248 ? 20.49705 29.66904  24.84882  1.000 54.48187 ? 248 PHE A CZ  1 
ATOM   1937 N N   . ARG A 1 249 ? 27.42079 27.49651  24.00800  1.000 46.07235 ? 249 ARG A N   1 
ATOM   1938 C CA  . ARG A 1 249 ? 28.75807 27.01969  24.29118  1.000 48.26439 ? 249 ARG A CA  1 
ATOM   1939 C C   . ARG A 1 249 ? 29.25700 26.33203  23.03217  1.000 48.70178 ? 249 ARG A C   1 
ATOM   1940 O O   . ARG A 1 249 ? 28.48493 26.03360  22.12064  1.000 47.90044 ? 249 ARG A O   1 
ATOM   1941 C CB  . ARG A 1 249 ? 28.76477 26.07430  25.49906  1.000 50.63425 ? 249 ARG A CB  1 
ATOM   1942 C CG  . ARG A 1 249 ? 27.86911 24.87002  25.32960  1.000 52.97754 ? 249 ARG A CG  1 
ATOM   1943 C CD  . ARG A 1 249 ? 27.51178 24.21805  26.66222  1.000 55.93499 ? 249 ARG A CD  1 
ATOM   1944 N NE  . ARG A 1 249 ? 26.74040 22.99503  26.46213  1.000 57.89641 ? 249 ARG A NE  1 
ATOM   1945 C CZ  . ARG A 1 249 ? 26.29417 22.21064  27.43361  1.000 58.92474 ? 249 ARG A CZ  1 
ATOM   1946 N NH1 . ARG A 1 249 ? 26.50681 22.49817  28.70631  1.000 58.71768 ? 249 ARG A NH1 1 
ATOM   1947 N NH2 . ARG A 1 249 ? 25.61733 21.10747  27.11925  1.000 59.49737 ? 249 ARG A NH2 1 
ATOM   1948 N N   . SER A 1 250 ? 30.56172 26.08502  22.99238  1.000 49.41308 ? 250 SER A N   1 
ATOM   1949 C CA  . SER A 1 250 ? 31.14420 25.37745  21.86583  1.000 49.58495 ? 250 SER A CA  1 
ATOM   1950 C C   . SER A 1 250 ? 30.77255 23.90380  21.90712  1.000 46.61622 ? 250 SER A C   1 
ATOM   1951 O O   . SER A 1 250 ? 30.93037 23.22570  22.92452  1.000 47.81004 ? 250 SER A O   1 
ATOM   1952 C CB  . SER A 1 250 ? 32.66404 25.53694  21.87301  1.000 53.47022 ? 250 SER A CB  1 
ATOM   1953 O OG  . SER A 1 250 ? 33.26954 24.81634  20.81523  1.000 55.81284 ? 250 SER A OG  1 
ATOM   1954 N N   . PHE A 1 251 ? 30.27116 23.40173  20.79263  1.000 43.14630 ? 251 PHE A N   1 
ATOM   1955 C CA  . PHE A 1 251 ? 30.09893 21.96544  20.60106  1.000 40.42338 ? 251 PHE A CA  1 
ATOM   1956 C C   . PHE A 1 251 ? 30.31107 21.74482  19.12140  1.000 37.88028 ? 251 PHE A C   1 
ATOM   1957 O O   . PHE A 1 251 ? 29.35556 21.69365  18.34699  1.000 38.59055 ? 251 PHE A O   1 
ATOM   1958 C CB  . PHE A 1 251 ? 28.70964 21.50452  21.04009  1.000 41.38159 ? 251 PHE A CB  1 
ATOM   1959 C CG  . PHE A 1 251 ? 28.53554 20.02256  21.05980  1.000 42.99858 ? 251 PHE A CG  1 
ATOM   1960 C CD1 . PHE A 1 251 ? 29.62261 19.18133  21.17871  1.000 44.52845 ? 251 PHE A CD1 1 
ATOM   1961 C CD2 . PHE A 1 251 ? 27.27774 19.46852  20.98236  1.000 44.45060 ? 251 PHE A CD2 1 
ATOM   1962 C CE1 . PHE A 1 251 ? 29.46864 17.81184  21.21928  1.000 44.79117 ? 251 PHE A CE1 1 
ATOM   1963 C CE2 . PHE A 1 251 ? 27.10884 18.10202  21.02675  1.000 45.36752 ? 251 PHE A CE2 1 
ATOM   1964 C CZ  . PHE A 1 251 ? 28.21347 17.26955  21.14932  1.000 45.45216 ? 251 PHE A CZ  1 
ATOM   1965 N N   . PRO A 1 252 ? 31.56873 21.67021  18.68671  1.000 33.61991 ? 252 PRO A N   1 
ATOM   1966 C CA  . PRO A 1 252 ? 31.86502 21.63167  17.25536  1.000 31.69799 ? 252 PRO A CA  1 
ATOM   1967 C C   . PRO A 1 252 ? 31.25740 20.41785  16.59077  1.000 32.51409 ? 252 PRO A C   1 
ATOM   1968 O O   . PRO A 1 252 ? 31.15597 19.34265  17.18461  1.000 33.48932 ? 252 PRO A O   1 
ATOM   1969 C CB  . PRO A 1 252 ? 33.39676 21.56262  17.21285  1.000 31.16475 ? 252 PRO A CB  1 
ATOM   1970 C CG  . PRO A 1 252 ? 33.83324 22.16846  18.53359  1.000 31.96763 ? 252 PRO A CG  1 
ATOM   1971 C CD  . PRO A 1 252 ? 32.79274 21.72729  19.51365  1.000 31.91956 ? 252 PRO A CD  1 
ATOM   1972 N N   . PHE A 1 253 ? 30.90328 20.59216  15.31000  1.000 32.13978 ? 253 PHE A N   1 
ATOM   1973 C CA  . PHE A 1 253 ? 30.30580 19.50088  14.54278  1.000 31.31211 ? 253 PHE A CA  1 
ATOM   1974 C C   . PHE A 1 253 ? 31.16682 18.24785  14.59621  1.000 28.58812 ? 253 PHE A C   1 
ATOM   1975 O O   . PHE A 1 253 ? 30.65583 17.14065  14.78721  1.000 27.20307 ? 253 PHE A O   1 
ATOM   1976 C CB  . PHE A 1 253 ? 30.09752 19.95923  13.10385  1.000 31.97569 ? 253 PHE A CB  1 
ATOM   1977 C CG  . PHE A 1 253 ? 29.53297 18.91252  12.19657  1.000 31.69567 ? 253 PHE A CG  1 
ATOM   1978 C CD1 . PHE A 1 253 ? 28.17104 18.65482  12.16936  1.000 33.31027 ? 253 PHE A CD1 1 
ATOM   1979 C CD2 . PHE A 1 253 ? 30.35087 18.22813  11.32677  1.000 31.79887 ? 253 PHE A CD2 1 
ATOM   1980 C CE1 . PHE A 1 253 ? 27.63765 17.71241  11.26700  1.000 33.03885 ? 253 PHE A CE1 1 
ATOM   1981 C CE2 . PHE A 1 253 ? 29.83538 17.30003  10.45366  1.000 33.63970 ? 253 PHE A CE2 1 
ATOM   1982 C CZ  . PHE A 1 253 ? 28.47863 17.03929  10.42063  1.000 33.19886 ? 253 PHE A CZ  1 
ATOM   1983 N N   . TRP A 1 254 ? 32.49234 18.39350  14.42535  1.000 27.82200 ? 254 TRP A N   1 
ATOM   1984 C CA  . TRP A 1 254 ? 33.29721 17.17722  14.39562  1.000 26.86593 ? 254 TRP A CA  1 
ATOM   1985 C C   . TRP A 1 254 ? 33.35842 16.50145  15.77597  1.000 26.83168 ? 254 TRP A C   1 
ATOM   1986 O O   . TRP A 1 254 ? 33.50770 15.27145  15.85327  1.000 27.42657 ? 254 TRP A O   1 
ATOM   1987 C CB  . TRP A 1 254 ? 34.69880 17.46883  13.85960  1.000 28.67350 ? 254 TRP A CB  1 
ATOM   1988 C CG  . TRP A 1 254 ? 34.71671 17.91676  12.42155  1.000 28.42772 ? 254 TRP A CG  1 
ATOM   1989 C CD1 . TRP A 1 254 ? 35.24659 19.08197  11.94364  1.000 27.71614 ? 254 TRP A CD1 1 
ATOM   1990 C CD2 . TRP A 1 254 ? 34.18255 17.22512  11.28103  1.000 29.30893 ? 254 TRP A CD2 1 
ATOM   1991 N NE1 . TRP A 1 254 ? 35.04961 19.17195  10.60111  1.000 27.69419 ? 254 TRP A NE1 1 
ATOM   1992 C CE2 . TRP A 1 254 ? 34.41955 18.04157  10.15770  1.000 28.67464 ? 254 TRP A CE2 1 
ATOM   1993 C CE3 . TRP A 1 254 ? 33.52664 16.00214  11.10105  1.000 29.99218 ? 254 TRP A CE3 1 
ATOM   1994 C CZ2 . TRP A 1 254 ? 34.04959 17.67007  8.86499   1.000 29.53075 ? 254 TRP A CZ2 1 
ATOM   1995 C CZ3 . TRP A 1 254 ? 33.15748 15.63494  9.81272   1.000 30.74214 ? 254 TRP A CZ3 1 
ATOM   1996 C CH2 . TRP A 1 254 ? 33.43209 16.46342  8.71579   1.000 30.90275 ? 254 TRP A CH2 1 
ATOM   1997 N N   . ARG A 1 255 ? 33.23820 17.26763  16.87331  1.000 26.19657 ? 255 ARG A N   1 
ATOM   1998 C CA  . ARG A 1 255 ? 33.09178 16.61902  18.17150  1.000 28.44461 ? 255 ARG A CA  1 
ATOM   1999 C C   . ARG A 1 255 ? 31.73350 15.93765  18.28819  1.000 29.71777 ? 255 ARG A C   1 
ATOM   2000 O O   . ARG A 1 255 ? 31.61687 14.83230  18.83868  1.000 30.59140 ? 255 ARG A O   1 
ATOM   2001 C CB  . ARG A 1 255 ? 33.30993 17.65795  19.29492  1.000 29.21357 ? 255 ARG A CB  1 
ATOM   2002 C CG  . ARG A 1 255 ? 33.11592 17.12885  20.71177  1.000 31.81089 ? 255 ARG A CG  1 
ATOM   2003 C CD  . ARG A 1 255 ? 34.05894 17.81214  21.73978  0.900 35.99274 ? 255 ARG A CD  1 
ATOM   2004 N NE  . ARG A 1 255 ? 35.33820 17.10835  21.74828  0.800 40.01972 ? 255 ARG A NE  1 
ATOM   2005 C CZ  . ARG A 1 255 ? 36.51193 17.63064  22.07902  0.700 42.25186 ? 255 ARG A CZ  1 
ATOM   2006 N NH1 . ARG A 1 255 ? 36.63424 18.90033  22.43676  0.700 43.47992 ? 255 ARG A NH1 1 
ATOM   2007 N NH2 . ARG A 1 255 ? 37.59367 16.85762  22.04707  0.700 42.96849 ? 255 ARG A NH2 1 
ATOM   2008 N N   . ARG A 1 256 ? 30.69930 16.56865  17.74252  1.000 29.65247 ? 256 ARG A N   1 
ATOM   2009 C CA  . ARG A 1 256 ? 29.37669 15.96053  17.71608  1.000 29.90504 ? 256 ARG A CA  1 
ATOM   2010 C C   . ARG A 1 256 ? 29.41631 14.63130  16.96618  1.000 28.43025 ? 256 ARG A C   1 
ATOM   2011 O O   . ARG A 1 256 ? 28.86851 13.62836  17.43374  1.000 28.70807 ? 256 ARG A O   1 
ATOM   2012 C CB  . ARG A 1 256 ? 28.41007 16.97099  17.08267  1.000 32.03643 ? 256 ARG A CB  1 
ATOM   2013 C CG  . ARG A 1 256 ? 26.93094 16.63421  17.14860  1.000 34.44773 ? 256 ARG A CG  1 
ATOM   2014 C CD  . ARG A 1 256 ? 26.05040 17.58977  16.30162  1.000 34.46981 ? 256 ARG A CD  1 
ATOM   2015 N NE  . ARG A 1 256 ? 26.15485 18.98598  16.67831  1.000 35.05109 ? 256 ARG A NE  1 
ATOM   2016 C CZ  . ARG A 1 256 ? 25.44939 19.52100  17.67237  1.000 41.11296 ? 256 ARG A CZ  1 
ATOM   2017 N NH1 . ARG A 1 256 ? 24.54864 18.81021  18.34236  1.000 43.17697 ? 256 ARG A NH1 1 
ATOM   2018 N NH2 . ARG A 1 256 ? 25.65446 20.79181  18.00995  1.000 41.96204 ? 256 ARG A NH2 1 
ATOM   2019 N N   . VAL A 1 257 ? 30.11688 14.59756  15.81744  1.000 26.58762 ? 257 VAL A N   1 
ATOM   2020 C CA  . VAL A 1 257 ? 30.30532 13.35259  15.08105  1.000 24.63149 ? 257 VAL A CA  1 
ATOM   2021 C C   . VAL A 1 257 ? 31.08803 12.33862  15.90556  1.000 25.72355 ? 257 VAL A C   1 
ATOM   2022 O O   . VAL A 1 257 ? 30.74082 11.14441  15.93979  1.000 26.25955 ? 257 VAL A O   1 
ATOM   2023 C CB  . VAL A 1 257 ? 31.01674 13.63371  13.74675  1.000 23.11544 ? 257 VAL A CB  1 
ATOM   2024 C CG1 . VAL A 1 257 ? 31.33983 12.33311  13.05707  1.000 21.79803 ? 257 VAL A CG1 1 
ATOM   2025 C CG2 . VAL A 1 257 ? 30.13174 14.50287  12.87193  1.000 25.40419 ? 257 VAL A CG2 1 
ATOM   2026 N N   . HIS A 1 258 ? 32.19486 12.77833  16.51827  1.000 26.07878 ? 258 HIS A N   1 
ATOM   2027 C CA  . HIS A 1 258 ? 32.97906 11.88814  17.37699  1.000 26.37490 ? 258 HIS A CA  1 
ATOM   2028 C C   . HIS A 1 258 ? 32.10423 11.26970  18.45532  1.000 27.06445 ? 258 HIS A C   1 
ATOM   2029 O O   . HIS A 1 258 ? 32.09099 10.05366  18.64677  1.000 27.63810 ? 258 HIS A O   1 
ATOM   2030 C CB  . HIS A 1 258 ? 34.14101 12.65731  18.01275  1.000 26.89795 ? 258 HIS A CB  1 
ATOM   2031 C CG  . HIS A 1 258 ? 34.92085 11.87615  19.03206  1.000 29.15102 ? 258 HIS A CG  1 
ATOM   2032 N ND1 . HIS A 1 258 ? 34.62312 11.91140  20.38393  1.000 32.17372 ? 258 HIS A ND1 1 
ATOM   2033 C CD2 . HIS A 1 258 ? 36.00203 11.06486  18.91352  1.000 29.47181 ? 258 HIS A CD2 1 
ATOM   2034 C CE1 . HIS A 1 258 ? 35.48995 11.16818  21.05728  1.000 31.62060 ? 258 HIS A CE1 1 
ATOM   2035 N NE2 . HIS A 1 258 ? 36.33804 10.64230  20.19177  1.000 32.32474 ? 258 HIS A NE2 1 
ATOM   2036 N N   . ASP A 1 259 ? 31.33715 12.09943  19.14252  1.000 26.64721 ? 259 ASP A N   1 
ATOM   2037 C CA  . ASP A 1 259 ? 30.53010 11.61795  20.25991  1.000 28.91248 ? 259 ASP A CA  1 
ATOM   2038 C C   . ASP A 1 259 ? 29.41358 10.67556  19.80505  1.000 31.45749 ? 259 ASP A C   1 
ATOM   2039 O O   . ASP A 1 259 ? 28.99878 9.79742   20.56746  1.000 34.07147 ? 259 ASP A O   1 
ATOM   2040 C CB  . ASP A 1 259 ? 29.95678 12.82324  21.00003  1.000 31.60254 ? 259 ASP A CB  1 
ATOM   2041 C CG  . ASP A 1 259 ? 31.01214 13.60230  21.78042  1.000 36.44530 ? 259 ASP A CG  1 
ATOM   2042 O OD1 . ASP A 1 259 ? 32.20591 13.19751  21.83837  1.000 36.57096 ? 259 ASP A OD1 1 
ATOM   2043 O OD2 . ASP A 1 259 ? 30.62863 14.63970  22.36699  1.000 39.46990 ? 259 ASP A OD2 1 
ATOM   2044 N N   . SER A 1 260 ? 28.88986 10.84985  18.58934  1.000 31.91805 ? 260 SER A N   1 
ATOM   2045 C CA  . SER A 1 260 ? 27.81066 9.98198   18.11063  1.000 32.80997 ? 260 SER A CA  1 
ATOM   2046 C C   . SER A 1 260 ? 28.30087 8.68488   17.50421  1.000 32.34456 ? 260 SER A C   1 
ATOM   2047 O O   . SER A 1 260 ? 27.53516 7.71490   17.47546  1.000 34.23860 ? 260 SER A O   1 
ATOM   2048 C CB  . SER A 1 260 ? 26.96089 10.68648  17.05608  1.000 33.85240 ? 260 SER A CB  1 
ATOM   2049 O OG  . SER A 1 260 ? 26.39154 11.81930  17.63493  1.000 36.15304 ? 260 SER A OG  1 
ATOM   2050 N N   . PHE A 1 261 ? 29.52739 8.64963   16.94107  1.000 29.19567 ? 261 PHE A N   1 
ATOM   2051 C CA  . PHE A 1 261 ? 29.97152 7.47918   16.19457  1.000 28.05029 ? 261 PHE A CA  1 
ATOM   2052 C C   . PHE A 1 261 ? 31.24032 6.82395   16.70847  1.000 29.29813 ? 261 PHE A C   1 
ATOM   2053 O O   . PHE A 1 261 ? 31.47392 5.64768   16.38351  1.000 30.39796 ? 261 PHE A O   1 
ATOM   2054 C CB  . PHE A 1 261 ? 30.19320 7.84486   14.71594  1.000 26.72701 ? 261 PHE A CB  1 
ATOM   2055 C CG  . PHE A 1 261 ? 28.93422 8.28856   14.03443  1.000 25.74920 ? 261 PHE A CG  1 
ATOM   2056 C CD1 . PHE A 1 261 ? 27.98290 7.34897   13.62791  1.000 27.43138 ? 261 PHE A CD1 1 
ATOM   2057 C CD2 . PHE A 1 261 ? 28.66019 9.62983   13.86401  1.000 26.44468 ? 261 PHE A CD2 1 
ATOM   2058 C CE1 . PHE A 1 261 ? 26.76560 7.74532   13.00907  1.000 27.61421 ? 261 PHE A CE1 1 
ATOM   2059 C CE2 . PHE A 1 261 ? 27.45330 10.04482  13.25612  1.000 28.17352 ? 261 PHE A CE2 1 
ATOM   2060 C CZ  . PHE A 1 261 ? 26.49694 9.09821   12.83158  1.000 27.43174 ? 261 PHE A CZ  1 
ATOM   2061 N N   . ILE A 1 262 ? 32.08297 7.53087   17.45836  1.000 29.40249 ? 262 ILE A N   1 
ATOM   2062 C CA  . ILE A 1 262 ? 33.36669 6.94921   17.81290  1.000 31.97738 ? 262 ILE A CA  1 
ATOM   2063 C C   . ILE A 1 262 ? 33.30335 6.46900   19.27368  1.000 38.02298 ? 262 ILE A C   1 
ATOM   2064 O O   . ILE A 1 262 ? 33.55606 5.29147   19.56053  1.000 40.75223 ? 262 ILE A O   1 
ATOM   2065 C CB  . ILE A 1 262 ? 34.50891 7.96128   17.57062  1.000 31.42341 ? 262 ILE A CB  1 
ATOM   2066 C CG1 . ILE A 1 262 ? 34.64030 8.30309   16.09110  1.000 31.04259 ? 262 ILE A CG1 1 
ATOM   2067 C CG2 . ILE A 1 262 ? 35.85275 7.40165   18.00240  1.000 32.08467 ? 262 ILE A CG2 1 
ATOM   2068 C CD1 . ILE A 1 262 ? 34.99041 7.13060   15.23094  1.000 30.92730 ? 262 ILE A CD1 1 
ATOM   2069 N N   . GLU A 1 263 ? 32.95490 7.36229   20.19514  1.000 40.60671 ? 263 GLU A N   1 
ATOM   2070 C CA  . GLU A 1 263 ? 32.79337 6.99743   21.61538  1.000 48.65950 ? 263 GLU A CA  1 
ATOM   2071 C C   . GLU A 1 263 ? 32.34883 8.18983   22.44156  1.000 56.96285 ? 263 GLU A C   1 
ATOM   2072 O O   . GLU A 1 263 ? 32.67610 9.32761   22.10770  1.000 58.93245 ? 263 GLU A O   1 
ATOM   2073 C CB  . GLU A 1 263 ? 34.09243 6.45678   22.23298  1.000 52.14362 ? 263 GLU A CB  1 
ATOM   2074 C CG  . GLU A 1 263 ? 35.38540 6.97513   21.57573  1.000 54.71102 ? 263 GLU A CG  1 
ATOM   2075 C CD  . GLU A 1 263 ? 36.45255 7.42451   22.55219  0.700 54.90799 ? 263 GLU A CD  1 
ATOM   2076 O OE1 . GLU A 1 263 ? 36.11746 7.65942   23.73605  0.700 55.79892 ? 263 GLU A OE1 1 
ATOM   2077 O OE2 . GLU A 1 263 ? 37.62407 7.55261   22.11353  0.700 53.55157 ? 263 GLU A OE2 1 
ATOM   2078 N N   . ASP A 1 264 ? 31.64219 7.94569   23.54668  1.000 64.58003 ? 264 ASP A N   1 
ATOM   2079 C CA  . ASP A 1 264 ? 31.16019 9.03057   24.41004  1.000 70.33535 ? 264 ASP A CA  1 
ATOM   2080 C C   . ASP A 1 264 ? 30.84870 8.52697   25.82633  1.000 72.22141 ? 264 ASP A C   1 
ATOM   2081 O O   . ASP A 1 264 ? 31.75056 8.19788   26.60455  1.000 73.29170 ? 264 ASP A O   1 
ATOM   2082 C CB  . ASP A 1 264 ? 29.91156 9.69996   23.80740  1.000 73.45833 ? 264 ASP A CB  1 
ATOM   2083 C CG  . ASP A 1 264 ? 29.46286 10.93698  24.59828  1.000 76.94481 ? 264 ASP A CG  1 
ATOM   2084 O OD1 . ASP A 1 264 ? 30.18173 11.34606  25.54099  1.000 78.92454 ? 264 ASP A OD1 1 
ATOM   2085 O OD2 . ASP A 1 264 ? 28.38917 11.50181  24.28452  1.000 77.33535 ? 264 ASP A OD2 1 
HETATM 2086 C C1  . CIT B 2 .   ? 31.59382 24.38361  14.19644  1.000 59.49489 ? 301 CIT A C1  1 
HETATM 2087 O O1  . CIT B 2 .   ? 31.54732 23.18414  13.86348  1.000 55.65692 ? 301 CIT A O1  1 
HETATM 2088 O O2  . CIT B 2 .   ? 32.71214 24.84358  14.49415  1.000 61.22750 ? 301 CIT A O2  1 
HETATM 2089 C C2  . CIT B 2 .   ? 30.37030 25.27529  14.27052  1.000 63.78967 ? 301 CIT A C2  1 
HETATM 2090 C C3  . CIT B 2 .   ? 29.27171 24.68781  15.16839  1.000 68.64412 ? 301 CIT A C3  1 
HETATM 2091 O O7  . CIT B 2 .   ? 29.87064 23.91078  16.24397  1.000 71.97115 ? 301 CIT A O7  1 
HETATM 2092 C C4  . CIT B 2 .   ? 28.38734 25.76795  15.80035  1.000 71.95032 ? 301 CIT A C4  1 
HETATM 2093 C C5  . CIT B 2 .   ? 28.83837 26.22850  17.19261  1.000 74.41482 ? 301 CIT A C5  1 
HETATM 2094 O O3  . CIT B 2 .   ? 29.00165 27.45616  17.43657  1.000 75.48266 ? 301 CIT A O3  1 
HETATM 2095 O O4  . CIT B 2 .   ? 29.03713 25.41210  18.13508  1.000 74.02811 ? 301 CIT A O4  1 
HETATM 2096 C C6  . CIT B 2 .   ? 28.43140 23.73503  14.32842  1.000 66.26616 ? 301 CIT A C6  1 
HETATM 2097 O O5  . CIT B 2 .   ? 28.32386 23.90265  13.09272  1.000 64.47022 ? 301 CIT A O5  1 
HETATM 2098 O O6  . CIT B 2 .   ? 27.87820 22.74517  14.86301  1.000 66.02596 ? 301 CIT A O6  1 
HETATM 2099 N N   . V0I C 3 .   ? 14.05225 -9.46799  -12.03058 1.000 34.61529 ? 302 V0I A N   1 
HETATM 2100 C C   . V0I C 3 .   ? 12.73887 -8.96201  -12.52279 1.000 38.83959 ? 302 V0I A C   1 
HETATM 2101 O O   . V0I C 3 .   ? 15.83563 -8.33866  -9.92198  1.000 30.43442 ? 302 V0I A O   1 
HETATM 2102 C C1  . V0I C 3 .   ? 14.04055 -9.80022  -10.60455 1.000 31.63487 ? 302 V0I A C1  1 
HETATM 2103 C C10 . V0I C 3 .   ? 18.66465 -4.00891  -7.48215  1.000 27.97051 ? 302 V0I A C10 1 
HETATM 2104 C C11 . V0I C 3 .   ? 14.52433 -10.56853 -12.88668 1.000 32.88669 ? 302 V0I A C11 1 
HETATM 2105 C C12 . V0I C 3 .   ? 15.97054 -10.83463 -12.84312 1.000 31.21924 ? 302 V0I A C12 1 
HETATM 2106 C C13 . V0I C 3 .   ? 17.16045 -10.96072 -12.89211 1.000 29.29034 ? 302 V0I A C13 1 
HETATM 2107 C C14 . V0I C 3 .   ? 18.53599 -11.27242 -12.83051 1.000 27.66080 ? 302 V0I A C14 1 
HETATM 2108 C C15 . V0I C 3 .   ? 20.38775 -12.19760 -12.33252 1.000 27.33091 ? 302 V0I A C15 1 
HETATM 2109 C C16 . V0I C 3 .   ? 20.72628 -11.06650 -13.04970 1.000 27.71872 ? 302 V0I A C16 1 
HETATM 2110 C C17 . V0I C 3 .   ? 19.44259 -9.21666  -14.09090 1.000 32.81028 ? 302 V0I A C17 1 
HETATM 2111 C C18 . V0I C 3 .   ? 18.32592 -7.20334  -13.97619 1.000 39.05633 ? 302 V0I A C18 1 
HETATM 2112 C C19 . V0I C 3 .   ? 18.36833 -7.67268  -15.43163 1.000 37.47068 ? 302 V0I A C19 1 
HETATM 2113 C C2  . V0I C 3 .   ? 15.40215 -9.71063  -9.94343  1.000 29.79990 ? 302 V0I A C2  1 
HETATM 2114 C C20 . V0I C 3 .   ? 18.50948 -9.18039  -15.28610 1.000 34.35845 ? 302 V0I A C20 1 
HETATM 2115 C C21 . V0I C 3 .   ? 16.96916 -7.23097  -13.30800 1.000 45.40208 ? 302 V0I A C21 1 
HETATM 2116 C C22 . V0I C 3 .   ? 13.62153 -5.02014  -13.26556 1.000 61.78121 ? 302 V0I A C22 1 
HETATM 2117 C C23 . V0I C 3 .   ? 14.01282 -5.19951  -10.82624 1.000 61.75231 ? 302 V0I A C23 1 
HETATM 2118 C C24 . V0I C 3 .   ? 22.88231 -11.46784 -12.84093 1.000 27.66330 ? 302 V0I A C24 1 
HETATM 2119 C C25 . V0I C 3 .   ? 21.44171 -12.97930 -11.84168 1.000 26.41156 ? 302 V0I A C25 1 
HETATM 2120 C C3  . V0I C 3 .   ? 16.88512 -8.27378  -8.96094  1.000 28.81122 ? 302 V0I A C3  1 
HETATM 2121 C C4  . V0I C 3 .   ? 16.65192 -9.38438  -7.92979  1.000 28.27542 ? 302 V0I A C4  1 
HETATM 2122 C C5  . V0I C 3 .   ? 15.39818 -10.09266 -8.46311  1.000 27.79380 ? 302 V0I A C5  1 
HETATM 2123 C C6  . V0I C 3 .   ? 15.97151 -6.26239  -7.70613  1.000 28.58281 ? 302 V0I A C6  1 
HETATM 2124 C C7  . V0I C 3 .   ? 17.68050 -5.00008  -7.65994  1.000 27.51350 ? 302 V0I A C7  1 
HETATM 2125 C C8  . V0I C 3 .   ? 18.05065 -6.12526  -8.37698  1.000 26.27140 ? 302 V0I A C8  1 
HETATM 2126 C C9  . V0I C 3 .   ? 20.09230 -5.36540  -8.69713  1.000 27.80570 ? 302 V0I A C9  1 
HETATM 2127 N N1  . V0I C 3 .   ? 16.94700 -6.93981  -8.39627  1.000 27.29648 ? 302 V0I A N1  1 
HETATM 2128 N N10 . V0I C 3 .   ? 21.96253 -10.64154 -13.34812 1.000 27.46878 ? 302 V0I A N10 1 
HETATM 2129 N N11 . V0I C 3 .   ? 22.69928 -12.58214 -12.12628 1.000 28.62897 ? 302 V0I A N11 1 
HETATM 2130 N N12 . V0I C 3 .   ? 21.26011 -14.06412 -11.08719 1.000 25.80484 ? 302 V0I A N12 1 
HETATM 2131 N N2  . V0I C 3 .   ? 16.35871 -5.09914  -7.23673  1.000 28.62113 ? 302 V0I A N2  1 
HETATM 2132 N N3  . V0I C 3 .   ? 19.25380 -6.37583  -8.91944  1.000 26.79139 ? 302 V0I A N3  1 
HETATM 2133 N N4  . V0I C 3 .   ? 19.87825 -4.23133  -8.02258  1.000 28.01677 ? 302 V0I A N4  1 
HETATM 2134 N N5  . V0I C 3 .   ? 18.45745 -2.84864  -6.84659  1.000 28.82820 ? 302 V0I A N5  1 
HETATM 2135 N N6  . V0I C 3 .   ? 19.00785 -12.32506 -12.21782 1.000 27.44979 ? 302 V0I A N6  1 
HETATM 2136 N N7  . V0I C 3 .   ? 19.53505 -10.46404 -13.37026 1.000 29.83773 ? 302 V0I A N7  1 
HETATM 2137 N N8  . V0I C 3 .   ? 16.28086 -5.96875  -13.57852 1.000 52.26051 ? 302 V0I A N8  1 
HETATM 2138 N N9  . V0I C 3 .   ? 14.58869 -5.00587  -12.16173 1.000 60.84269 ? 302 V0I A N9  1 
HETATM 2139 O O1  . V0I C 3 .   ? 15.50411 -11.49283 -8.27606  1.000 27.43139 ? 302 V0I A O1  1 
HETATM 2140 O O2  . V0I C 3 .   ? 17.81939 -10.20970 -7.91900  1.000 28.03279 ? 302 V0I A O2  1 
HETATM 2141 O O3  . V0I C 3 .   ? 19.00255 -8.20921  -13.21042 1.000 34.23193 ? 302 V0I A O3  1 
HETATM 2142 O O4  . V0I C 3 .   ? 19.11651 -9.76420  -16.44165 1.000 34.32783 ? 302 V0I A O4  1 
HETATM 2143 O O5  . V0I C 3 .   ? 19.54055 -7.19111  -16.07044 1.000 39.14100 ? 302 V0I A O5  1 
HETATM 2144 O O6  . V0I C 3 .   ? 16.48726 -3.63472  -13.15474 1.000 58.36698 ? 302 V0I A O6  1 
HETATM 2145 O O7  . V0I C 3 .   ? 16.86245 -5.14805  -11.23343 1.000 60.28766 ? 302 V0I A O7  1 
HETATM 2146 S S   . V0I C 3 .   ? 16.17303 -4.83178  -12.44207 1.000 57.57853 ? 302 V0I A S   1 
HETATM 2147 O O   . HOH D 4 .   ? 7.79012  31.40978  41.93233  1.000 35.86153 ? 401 HOH A O   1 
HETATM 2148 O O   . HOH D 4 .   ? 15.16089 -1.94253  -14.12947 1.000 51.23312 ? 402 HOH A O   1 
HETATM 2149 O O   . HOH D 4 .   ? 6.36731  19.34205  16.78067  1.000 51.15080 ? 403 HOH A O   1 
HETATM 2150 O O   . HOH D 4 .   ? 18.82756 26.66345  -6.71780  1.000 53.60039 ? 404 HOH A O   1 
HETATM 2151 O O   . HOH D 4 .   ? 31.96281 15.71491  24.14765  1.000 43.02943 ? 405 HOH A O   1 
HETATM 2152 O O   . HOH D 4 .   ? 13.79547 10.69538  -18.97076 1.000 52.82841 ? 406 HOH A O   1 
HETATM 2153 O O   . HOH D 4 .   ? 8.85130  12.75645  18.87869  1.000 56.28039 ? 407 HOH A O   1 
HETATM 2154 O O   . HOH D 4 .   ? 24.11202 8.15950   -8.85107  1.000 33.16476 ? 408 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 13.63309 10.85902  4.42066   1.000 33.01808 ? 409 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 35.51179 10.15530  23.76552  1.000 46.12980 ? 410 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 6.45956  30.60244  30.62778  1.000 46.39117 ? 411 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 25.19464 3.39132   -1.99379  1.000 42.50243 ? 412 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 2.72426  23.87517  22.58948  1.000 57.03303 ? 413 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 20.09191 26.53932  2.85170   1.000 30.38365 ? 414 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 30.82058 5.15597   11.92457  1.000 44.55274 ? 415 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 13.33307 18.81215  0.59264   1.000 37.01204 ? 416 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 10.42821 5.85973   -14.38724 1.000 48.03989 ? 417 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 14.58810 -4.09905  -5.53352  1.000 43.95169 ? 418 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 15.81192 30.81585  7.13841   1.000 55.10647 ? 419 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 21.99063 23.35443  -5.16165  1.000 30.62729 ? 420 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 33.58348 6.59566   -4.87971  1.000 22.80294 ? 421 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 27.93324 26.13569  -2.54342  1.000 48.75199 ? 422 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 37.33917 14.33519  21.19406  1.000 47.61015 ? 423 HOH A O   1 
HETATM 2170 O O   . HOH D 4 .   ? 17.58694 -10.48455 -18.51509 1.000 36.27778 ? 424 HOH A O   1 
HETATM 2171 O O   . HOH D 4 .   ? 33.44304 21.30681  13.65272  1.000 39.06386 ? 425 HOH A O   1 
HETATM 2172 O O   . HOH D 4 .   ? 20.42951 -7.92534  -10.78062 1.000 32.92243 ? 426 HOH A O   1 
HETATM 2173 O O   . HOH D 4 .   ? 20.38279 26.70713  -4.66580  1.000 39.41986 ? 427 HOH A O   1 
HETATM 2174 O O   . HOH D 4 .   ? 14.86063 16.88359  20.59380  1.000 40.93009 ? 428 HOH A O   1 
HETATM 2175 O O   . HOH D 4 .   ? 27.61529 5.53293   -1.76385  1.000 55.34991 ? 429 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 22.34432 21.05886  7.12796   1.000 27.12369 ? 430 HOH A O   1 
HETATM 2177 O O   . HOH D 4 .   ? 23.16960 -7.77100  -13.81924 1.000 37.70983 ? 431 HOH A O   1 
HETATM 2178 O O   . HOH D 4 .   ? 12.19852 1.45557   -5.44901  1.000 41.04205 ? 432 HOH A O   1 
HETATM 2179 O O   . HOH D 4 .   ? 22.65253 11.31080  0.44684   1.000 22.46092 ? 433 HOH A O   1 
HETATM 2180 O O   . HOH D 4 .   ? 15.36038 -0.37442  -11.69388 1.000 57.53441 ? 434 HOH A O   1 
HETATM 2181 O O   . HOH D 4 .   ? 5.16777  23.80505  0.14319   1.000 60.38397 ? 435 HOH A O   1 
HETATM 2182 O O   . HOH D 4 .   ? 13.66108 22.10445  -5.92000  1.000 39.99831 ? 436 HOH A O   1 
HETATM 2183 O O   . HOH D 4 .   ? 20.24071 21.86982  19.78522  1.000 40.88604 ? 437 HOH A O   1 
HETATM 2184 O O   . HOH D 4 .   ? 22.40267 27.68034  2.70161   1.000 59.31442 ? 438 HOH A O   1 
HETATM 2185 O O   . HOH D 4 .   ? 23.27359 7.39210   11.02576  1.000 31.38838 ? 439 HOH A O   1 
HETATM 2186 O O   . HOH D 4 .   ? 24.31935 5.22994   9.73366   1.000 35.56288 ? 440 HOH A O   1 
HETATM 2187 O O   . HOH D 4 .   ? 20.67589 11.61083  4.95324   1.000 23.34781 ? 441 HOH A O   1 
HETATM 2188 O O   . HOH D 4 .   ? 15.29211 28.55942  12.17606  1.000 35.38040 ? 442 HOH A O   1 
HETATM 2189 O O   . HOH D 4 .   ? 3.86854  32.12527  29.35907  1.000 50.26764 ? 443 HOH A O   1 
HETATM 2190 O O   . HOH D 4 .   ? 21.65170 1.27673   -12.89517 1.000 48.34353 ? 444 HOH A O   1 
HETATM 2191 O O   . HOH D 4 .   ? 8.48371  20.82826  3.76392   1.000 47.37241 ? 445 HOH A O   1 
HETATM 2192 O O   . HOH D 4 .   ? 13.12051 0.84147   2.87652   1.000 64.38250 ? 446 HOH A O   1 
HETATM 2193 O O   . HOH D 4 .   ? 12.09915 14.20223  33.40449  1.000 44.92885 ? 447 HOH A O   1 
HETATM 2194 O O   . HOH D 4 .   ? 37.06506 7.56955   26.32349  1.000 56.47760 ? 448 HOH A O   1 
HETATM 2195 O O   . HOH D 4 .   ? 31.69035 4.66849   -4.11389  1.000 35.96985 ? 449 HOH A O   1 
HETATM 2196 O O   . HOH D 4 .   ? 8.33389  4.63964   -10.56646 1.000 53.39192 ? 450 HOH A O   1 
HETATM 2197 O O   . HOH D 4 .   ? 11.20730 7.43918   -0.53302  1.000 32.59053 ? 451 HOH A O   1 
HETATM 2198 O O   . HOH D 4 .   ? 26.80021 22.02205  -14.62267 1.000 38.51800 ? 452 HOH A O   1 
HETATM 2199 O O   . HOH D 4 .   ? 8.44360  18.02385  18.27018  1.000 44.17627 ? 453 HOH A O   1 
HETATM 2200 O O   . HOH D 4 .   ? 5.65363  18.44458  12.41814  1.000 69.29282 ? 454 HOH A O   1 
HETATM 2201 O O   . HOH D 4 .   ? 6.87618  10.84855  19.97753  1.000 54.97644 ? 455 HOH A O   1 
HETATM 2202 O O   . HOH D 4 .   ? 3.04881  5.40234   -14.16414 1.000 50.80769 ? 456 HOH A O   1 
HETATM 2203 O O   . HOH D 4 .   ? 26.21213 29.91374  11.06307  1.000 47.44434 ? 457 HOH A O   1 
HETATM 2204 O O   . HOH D 4 .   ? 10.48086 3.88966   -12.09433 1.000 40.28286 ? 458 HOH A O   1 
HETATM 2205 O O   . HOH D 4 .   ? 26.14673 6.81389   -3.82798  1.000 35.55680 ? 459 HOH A O   1 
HETATM 2206 O O   . HOH D 4 .   ? 25.30600 9.28519   -6.62571  1.000 26.74039 ? 460 HOH A O   1 
HETATM 2207 O O   . HOH D 4 .   ? 7.89760  12.73510  15.80940  1.000 57.63504 ? 461 HOH A O   1 
HETATM 2208 O O   . HOH D 4 .   ? 23.39166 0.78091   -1.69327  1.000 39.06621 ? 462 HOH A O   1 
HETATM 2209 O O   . HOH D 4 .   ? 29.75121 26.77633  1.02423   1.000 43.28735 ? 463 HOH A O   1 
HETATM 2210 O O   . HOH D 4 .   ? 25.63797 -0.75119  -6.33722  1.000 53.75718 ? 464 HOH A O   1 
HETATM 2211 O O   . HOH D 4 .   ? 24.68035 35.24616  16.45809  1.000 64.28311 ? 465 HOH A O   1 
HETATM 2212 O O   . HOH D 4 .   ? 9.33780  8.29263   29.94587  1.000 65.49595 ? 466 HOH A O   1 
HETATM 2213 O O   . HOH D 4 .   ? 10.66894 32.73043  8.01242   1.000 61.03635 ? 467 HOH A O   1 
HETATM 2214 O O   . HOH D 4 .   ? 26.38046 21.78642  23.69715  1.000 48.18832 ? 468 HOH A O   1 
HETATM 2215 O O   . HOH D 4 .   ? 24.56763 1.54663   -5.11023  1.000 43.83872 ? 469 HOH A O   1 
HETATM 2216 O O   . HOH D 4 .   ? 26.68746 3.04820   -4.85155  1.000 53.22564 ? 470 HOH A O   1 
HETATM 2217 O O   . HOH D 4 .   ? 4.50782  18.46629  29.14027  1.000 41.22521 ? 471 HOH A O   1 
HETATM 2218 O O   . HOH D 4 .   ? 21.22027 21.06271  1.42297   1.000 31.55963 ? 472 HOH A O   1 
HETATM 2219 O O   . HOH D 4 .   ? 22.29466 2.63772   -17.42114 1.000 55.28807 ? 473 HOH A O   1 
HETATM 2220 O O   . HOH D 4 .   ? 24.55669 15.59933  19.94837  1.000 48.06760 ? 474 HOH A O   1 
HETATM 2221 O O   . HOH D 4 .   ? 27.56594 28.65837  5.35391   1.000 55.29476 ? 475 HOH A O   1 
HETATM 2222 O O   . HOH D 4 .   ? 20.84706 14.11015  32.16372  1.000 54.90679 ? 476 HOH A O   1 
HETATM 2223 O O   . HOH D 4 .   ? 18.54075 20.11191  -14.19821 1.000 41.26700 ? 477 HOH A O   1 
HETATM 2224 O O   . HOH D 4 .   ? 12.60779 11.28440  18.80020  1.000 39.27648 ? 478 HOH A O   1 
HETATM 2225 O O   . HOH D 4 .   ? 29.15836 1.99426   -10.70092 1.000 50.24065 ? 479 HOH A O   1 
HETATM 2226 O O   . HOH D 4 .   ? 9.87978  2.23388   -14.37496 1.000 53.72451 ? 480 HOH A O   1 
HETATM 2227 O O   . HOH D 4 .   ? 14.64796 9.56332   16.87242  1.000 45.54539 ? 481 HOH A O   1 
HETATM 2228 O O   . HOH D 4 .   ? 32.31846 26.49080  25.65275  1.000 65.26965 ? 482 HOH A O   1 
HETATM 2229 O O   . HOH D 4 .   ? 13.84642 8.28370   5.53162   1.000 47.72407 ? 483 HOH A O   1 
HETATM 2230 O O   . HOH D 4 .   ? 30.16650 4.83669   -1.98347  1.000 50.74521 ? 484 HOH A O   1 
HETATM 2231 O O   . HOH D 4 .   ? 0.56418  14.04781  -2.31227  1.000 58.72521 ? 485 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 0.85965 0.66120 0.72622 0.00505  -0.05541 0.02022  1   MET A N   
2    C CA  . MET A 1   ? 0.84528 0.64907 0.70966 0.01578  -0.02172 -0.00347 1   MET A CA  
3    C C   . MET A 1   ? 0.83151 0.60095 0.63445 0.06876  -0.00801 -0.01435 1   MET A C   
4    O O   . MET A 1   ? 0.81291 0.58291 0.61197 0.05317  -0.01069 -0.02833 1   MET A O   
5    C CB  . MET A 1   ? 0.83837 0.69371 0.75609 -0.00472 0.01793  -0.03045 1   MET A CB  
6    C CG  . MET A 1   ? 0.85342 0.73875 0.79090 -0.02214 0.04508  -0.05371 1   MET A CG  
7    S SD  . MET A 1   ? 0.88404 0.77011 0.81684 -0.01770 0.04911  -0.06547 1   MET A SD  
8    C CE  . MET A 1   ? 0.86488 0.75778 0.82539 -0.02703 0.05101  -0.06290 1   MET A CE  
9    N N   . LYS A 2   ? 0.83150 0.57173 0.57578 0.13115  0.00976  -0.01336 2   LYS A N   
10   C CA  . LYS A 2   ? 0.81267 0.53933 0.52042 0.15443  0.02021  -0.01983 2   LYS A CA  
11   C C   . LYS A 2   ? 0.79766 0.51946 0.43501 0.16270  0.04646  -0.00912 2   LYS A C   
12   O O   . LYS A 2   ? 0.83827 0.53060 0.38587 0.18804  0.06480  -0.01445 2   LYS A O   
13   C CB  . LYS A 2   ? 0.80878 0.54720 0.56057 0.16035  0.01680  -0.04182 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.84655 0.56110 0.60271 0.14714  0.02503  -0.07111 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.89229 0.58727 0.64336 0.11717  0.02997  -0.08607 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.93355 0.63276 0.67262 0.07004  0.01980  -0.08944 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.97421 0.66962 0.68776 0.03719  0.01429  -0.09155 2   LYS A NZ  
18   N N   . TYR A 3   ? 0.71994 0.50503 0.40101 0.14942  0.06552  0.00537  3   TYR A N   
19   C CA  . TYR A 3   ? 0.64520 0.50956 0.36866 0.17639  0.08106  0.00173  3   TYR A CA  
20   C C   . TYR A 3   ? 0.63305 0.54468 0.33915 0.21421  0.03705  -0.02472 3   TYR A C   
21   O O   . TYR A 3   ? 0.61551 0.59399 0.34603 0.23197  0.02874  -0.03907 3   TYR A O   
22   C CB  . TYR A 3   ? 0.58888 0.47005 0.35673 0.14602  0.11082  0.00151  3   TYR A CB  
23   C CG  . TYR A 3   ? 0.60027 0.43641 0.34713 0.10541  0.10777  0.01560  3   TYR A CG  
24   C CD1 . TYR A 3   ? 0.65277 0.44577 0.33792 0.08575  0.13123  0.00986  3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.57858 0.41084 0.34031 0.10694  0.07732  0.00587  3   TYR A CD2 
26   C CE1 . TYR A 3   ? 0.66107 0.43839 0.32371 0.10539  0.11665  0.00631  3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.59954 0.42317 0.32062 0.12680  0.06998  -0.01244 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 0.65246 0.45037 0.32189 0.12273  0.07098  -0.01113 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.68722 0.46796 0.32372 0.13756  0.04737  -0.01667 3   TYR A OH  
30   N N   . MET A 4   ? 0.61999 0.53593 0.30353 0.19068  0.01667  -0.03023 4   MET A N   
31   C CA  . MET A 4   ? 0.58010 0.53313 0.28917 0.12757  0.00882  -0.04357 4   MET A CA  
32   C C   . MET A 4   ? 0.51692 0.51964 0.28024 0.10382  0.03940  -0.06396 4   MET A C   
33   O O   . MET A 4   ? 0.50559 0.52708 0.28226 0.08173  0.05678  -0.06449 4   MET A O   
34   C CB  . MET A 4   ? 0.60420 0.56625 0.30134 0.14762  0.00217  -0.02171 4   MET A CB  
35   C CG  . MET A 4   ? 0.58779 0.58552 0.33317 0.12855  0.01988  -0.02429 4   MET A CG  
36   S SD  . MET A 4   ? 0.57334 0.61035 0.37111 0.12195  0.02812  -0.04099 4   MET A SD  
37   C CE  . MET A 4   ? 0.61845 0.60219 0.38557 0.10984  0.04812  -0.03150 4   MET A CE  
38   N N   . ILE A 5   ? 0.48648 0.51390 0.28102 0.10270  0.02911  -0.06973 5   ILE A N   
39   C CA  . ILE A 5   ? 0.47375 0.52505 0.28741 0.11048  0.04203  -0.06173 5   ILE A CA  
40   C C   . ILE A 5   ? 0.43641 0.56483 0.30680 0.11352  0.06354  -0.07521 5   ILE A C   
41   O O   . ILE A 5   ? 0.37228 0.58269 0.32565 0.07184  0.05655  -0.06946 5   ILE A O   
42   C CB  . ILE A 5   ? 0.43471 0.50319 0.26929 0.12901  0.01642  -0.04147 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.43079 0.46130 0.25715 0.12836  0.02494  -0.03486 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.44760 0.50069 0.28108 0.14168  0.02965  -0.03567 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.47521 0.45565 0.27089 0.12804  0.03941  -0.02563 5   ILE A CD1 
46   N N   . THR A 6   ? 0.44199 0.57317 0.30170 0.11050  0.06556  -0.10690 6   THR A N   
47   C CA  . THR A 6   ? 0.46516 0.60365 0.35130 0.06658  0.05992  -0.09636 6   THR A CA  
48   C C   . THR A 6   ? 0.44018 0.59140 0.39181 -0.00964 0.06480  -0.08396 6   THR A C   
49   O O   . THR A 6   ? 0.47186 0.62466 0.42076 -0.02114 0.08584  -0.07332 6   THR A O   
50   C CB  . THR A 6   ? 0.50077 0.67930 0.37649 0.16233  0.06844  -0.10325 6   THR A CB  
51   O OG1 . THR A 6   ? 0.55403 0.71544 0.39911 0.20542  0.10458  -0.13145 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.53423 0.70456 0.38159 0.16201  0.01945  -0.08547 6   THR A CG2 
53   N N   . SER A 7   ? 0.42370 0.54941 0.39691 -0.02262 0.07105  -0.09078 7   SER A N   
54   C CA  . SER A 7   ? 0.46250 0.52990 0.40068 -0.01577 0.09249  -0.08501 7   SER A CA  
55   C C   . SER A 7   ? 0.51698 0.53534 0.42000 -0.00674 0.09650  -0.06406 7   SER A C   
56   O O   . SER A 7   ? 0.55498 0.55412 0.42956 -0.03067 0.13442  -0.07776 7   SER A O   
57   C CB  . SER A 7   ? 0.46502 0.54266 0.39530 -0.01025 0.11139  -0.08276 7   SER A CB  
58   O OG  . SER A 7   ? 0.47823 0.55664 0.40874 0.00878  0.10392  -0.07445 7   SER A OG  
59   N N   . LYS A 8   ? 0.49650 0.50823 0.43274 0.01810  0.09365  -0.04287 8   LYS A N   
60   C CA  . LYS A 8   ? 0.53825 0.52746 0.45801 0.01834  0.12920  -0.02684 8   LYS A CA  
61   C C   . LYS A 8   ? 0.55912 0.55101 0.46448 0.03333  0.12342  -0.02088 8   LYS A C   
62   O O   . LYS A 8   ? 0.60549 0.56483 0.47875 0.02430  0.08920  -0.01858 8   LYS A O   
63   C CB  . LYS A 8   ? 0.55859 0.54753 0.49954 0.03214  0.15824  -0.04427 8   LYS A CB  
64   C CG  . LYS A 8   ? 0.60118 0.58024 0.55383 0.06056  0.17208  -0.06040 8   LYS A CG  
65   C CD  . LYS A 8   ? 0.68212 0.61327 0.59407 0.06618  0.14991  -0.05985 8   LYS A CD  
66   C CE  . LYS A 8   ? 0.76397 0.64483 0.62904 0.05493  0.13321  -0.05965 8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.83127 0.66742 0.65047 0.03833  0.11622  -0.06182 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.53941 0.55512 0.44886 0.02195  0.18297  -0.01355 9   GLY A N   
69   C CA  . GLY A 9   ? 0.57615 0.55564 0.48193 -0.02135 0.21156  -0.00644 9   GLY A CA  
70   C C   . GLY A 9   ? 0.63373 0.55282 0.53870 -0.04364 0.23253  -0.01315 9   GLY A C   
71   O O   . GLY A 9   ? 0.72392 0.56883 0.55036 -0.10676 0.17871  0.03146  9   GLY A O   
72   N N   . ASP A 10  ? 0.59525 0.53676 0.58323 -0.00511 0.26804  -0.04179 10  ASP A N   
73   C CA  . ASP A 10  ? 0.68262 0.58431 0.62540 -0.00617 0.29767  -0.03875 10  ASP A CA  
74   C C   . ASP A 10  ? 0.70414 0.54040 0.58723 0.02999  0.24412  -0.02343 10  ASP A C   
75   O O   . ASP A 10  ? 0.72538 0.51355 0.57846 0.08362  0.20046  -0.01351 10  ASP A O   
76   C CB  . ASP A 10  ? 0.75339 0.69634 0.71437 -0.05618 0.35528  -0.04007 10  ASP A CB  
77   C CG  . ASP A 10  ? 0.81342 0.80455 0.81284 -0.07577 0.36916  -0.05301 10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.80123 0.83277 0.83566 -0.07876 0.41220  -0.05936 10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.86842 0.86935 0.86367 -0.08095 0.35202  -0.05698 10  ASP A OD2 
80   N N   . GLU A 11  ? 0.69119 0.55457 0.57079 -0.02138 0.24276  0.00322  11  GLU A N   
81   C CA  . GLU A 11  ? 0.69743 0.58969 0.56944 0.00251  0.21330  0.05272  11  GLU A CA  
82   C C   . GLU A 11  ? 0.67208 0.59545 0.53005 0.04399  0.19989  0.05925  11  GLU A C   
83   O O   . GLU A 11  ? 0.70266 0.57538 0.52333 0.05748  0.21960  0.05432  11  GLU A O   
84   C CB  . GLU A 11  ? 0.72669 0.63277 0.61417 -0.03457 0.19154  0.08026  11  GLU A CB  
85   C CG  . GLU A 11  ? 0.77322 0.67544 0.64105 -0.03597 0.17379  0.08218  11  GLU A CG  
86   C CD  . GLU A 11  ? 0.82286 0.72444 0.65475 -0.01367 0.16800  0.05499  11  GLU A CD  
87   O OE1 . GLU A 11  ? 0.84914 0.74557 0.66188 0.00083  0.15489  0.04672  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 0.82370 0.74061 0.65529 -0.02277 0.18057  0.03818  11  GLU A OE2 
89   N N   . LYS A 12  ? 0.62729 0.62299 0.51337 0.04648  0.13126  0.07022  12  LYS A N   
90   C CA  . LYS A 12  ? 0.63172 0.62849 0.50351 0.02482  0.09637  0.06020  12  LYS A CA  
91   C C   . LYS A 12  ? 0.61959 0.58054 0.42577 0.04107  0.12648  0.03174  12  LYS A C   
92   O O   . LYS A 12  ? 0.59307 0.58308 0.38756 0.08613  0.14131  0.03352  12  LYS A O   
93   C CB  . LYS A 12  ? 0.61409 0.68368 0.57414 0.00437  0.04684  0.07771  12  LYS A CB  
94   C CG  . LYS A 12  ? 0.60049 0.72957 0.63442 0.01517  0.02740  0.11564  12  LYS A CG  
95   C CD  . LYS A 12  ? 0.62100 0.76450 0.68194 0.04627  0.00202  0.14425  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.66247 0.80897 0.71411 0.04318  -0.03158 0.16744  12  LYS A CE  
97   N NZ  . LYS A 12  ? 0.62107 0.83410 0.72950 0.03701  -0.05597 0.17224  12  LYS A NZ  
98   N N   . SER A 13  ? 0.57719 0.53333 0.39793 0.01363  0.15438  0.00091  13  SER A N   
99   C CA  . SER A 13  ? 0.53173 0.48187 0.37650 0.01767  0.17440  -0.04339 13  SER A CA  
100  C C   . SER A 13  ? 0.49689 0.50810 0.36731 -0.01151 0.14402  -0.04621 13  SER A C   
101  O O   . SER A 13  ? 0.44500 0.54327 0.35112 -0.01297 0.11540  -0.04183 13  SER A O   
102  C CB  . SER A 13  ? 0.57665 0.45513 0.37693 0.03311  0.19409  -0.08167 13  SER A CB  
103  O OG  . SER A 13  ? 0.60105 0.47408 0.40443 -0.00178 0.17682  -0.10810 13  SER A OG  
104  N N   . ASP A 14  ? 0.50885 0.52427 0.38294 -0.03393 0.14109  -0.04912 14  ASP A N   
105  C CA  . ASP A 14  ? 0.52561 0.54664 0.39137 -0.02470 0.12741  -0.04006 14  ASP A CA  
106  C C   . ASP A 14  ? 0.53393 0.53226 0.37761 0.00542  0.10845  0.01573  14  ASP A C   
107  O O   . ASP A 14  ? 0.49032 0.50058 0.35618 0.02762  0.10164  0.02347  14  ASP A O   
108  C CB  . ASP A 14  ? 0.50594 0.56784 0.41373 -0.07324 0.13354  -0.07107 14  ASP A CB  
109  C CG  . ASP A 14  ? 0.51879 0.58780 0.44514 -0.09771 0.15707  -0.09492 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.49792 0.57628 0.44674 -0.06560 0.20643  -0.12006 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.57055 0.60282 0.46036 -0.13261 0.15019  -0.09448 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.55626 0.55150 0.39709 0.02602  0.10099  0.03613  15  LEU A N   
113  C CA  . LEU A 15  ? 0.57519 0.56527 0.40431 0.05385  0.13861  0.05148  15  LEU A CA  
114  C C   . LEU A 15  ? 0.48102 0.59431 0.35533 0.06729  0.11470  0.01509  15  LEU A C   
115  O O   . LEU A 15  ? 0.46472 0.62716 0.32603 0.06750  0.09297  -0.00595 15  LEU A O   
116  C CB  . LEU A 15  ? 0.64357 0.57571 0.46430 0.04971  0.19894  0.13091  15  LEU A CB  
117  C CG  . LEU A 15  ? 0.75407 0.61703 0.53673 0.07621  0.21418  0.17812  15  LEU A CG  
118  C CD1 . LEU A 15  ? 0.80585 0.61713 0.56379 0.10769  0.19915  0.19972  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 0.75775 0.63002 0.57243 0.06807  0.23903  0.18832  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.42872 0.58728 0.33680 0.07264  0.09037  0.01537  16  LEU A N   
121  C CA  . LEU A 16  ? 0.42048 0.59754 0.31309 0.05179  0.07902  0.00438  16  LEU A CA  
122  C C   . LEU A 16  ? 0.41612 0.59680 0.31122 0.04100  0.06176  0.00117  16  LEU A C   
123  O O   . LEU A 16  ? 0.44029 0.59006 0.31161 0.04639  0.04319  0.01188  16  LEU A O   
124  C CB  . LEU A 16  ? 0.39609 0.62070 0.28727 0.06532  0.07666  -0.03809 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.39932 0.64057 0.27529 0.08212  0.06082  -0.03764 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.39703 0.64077 0.28758 0.12114  0.00560  -0.02040 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.42513 0.64987 0.27200 0.10614  0.07005  -0.05148 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.38198 0.58010 0.30108 0.05776  0.08493  -0.01394 17  ARG A N   
129  C CA  . ARG A 17  ? 0.33444 0.54924 0.29300 0.09238  0.06819  -0.03321 17  ARG A CA  
130  C C   . ARG A 17  ? 0.34831 0.55368 0.30430 0.08604  0.06699  -0.03394 17  ARG A C   
131  O O   . ARG A 17  ? 0.36165 0.56265 0.32668 0.09832  0.05051  -0.04219 17  ARG A O   
132  C CB  . ARG A 17  ? 0.32552 0.54255 0.26844 0.09254  0.03523  -0.05664 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.34514 0.56628 0.27032 0.12152  0.03384  -0.07843 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.35619 0.57214 0.28713 0.11486  0.02477  -0.09256 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.35372 0.59988 0.32418 0.09238  0.02429  -0.07311 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.38679 0.61183 0.35764 0.07371  0.03082  -0.03458 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.40458 0.65029 0.36024 0.06417  0.03307  -0.02715 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.39094 0.57080 0.37483 0.06731  0.03545  -0.01993 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.35753 0.56239 0.29249 0.06320  0.09052  -0.03795 18  LEU A N   
140  C CA  . LEU A 18  ? 0.38532 0.55236 0.30389 0.04677  0.09675  -0.05217 18  LEU A CA  
141  C C   . LEU A 18  ? 0.41127 0.53546 0.29871 0.05917  0.08558  -0.04802 18  LEU A C   
142  O O   . LEU A 18  ? 0.39297 0.55693 0.29962 0.04497  0.06927  -0.04157 18  LEU A O   
143  C CB  . LEU A 18  ? 0.40024 0.55519 0.33192 0.06312  0.09931  -0.02575 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.42699 0.55647 0.37565 0.05358  0.08310  0.02182  18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.45450 0.55266 0.38218 0.02034  0.10198  0.06336  18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.38869 0.54528 0.39956 0.08772  0.06013  0.04775  18  LEU A CD2 
147  N N   . ASN A 19  ? 0.43888 0.50236 0.30302 0.08896  0.06182  -0.05021 19  ASN A N   
148  C CA  . ASN A 19  ? 0.51390 0.48486 0.28922 0.12231  0.04619  -0.04561 19  ASN A CA  
149  C C   . ASN A 19  ? 0.44648 0.51931 0.27892 0.09361  0.01635  -0.06498 19  ASN A C   
150  O O   . ASN A 19  ? 0.49206 0.56741 0.28794 0.07255  -0.02759 -0.05826 19  ASN A O   
151  C CB  . ASN A 19  ? 0.62240 0.47198 0.30678 0.14253  0.06285  -0.02681 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.71108 0.46265 0.33818 0.14926  0.05814  -0.02664 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.74214 0.44383 0.34036 0.10480  0.06811  -0.01291 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.73351 0.45564 0.36284 0.19011  0.05358  -0.04812 19  ASN A ND2 
155  N N   . MET A 20  ? 0.37115 0.51471 0.25761 0.07192  0.02998  -0.05689 20  MET A N   
156  C CA  . MET A 20  ? 0.37745 0.52900 0.26668 0.04737  0.04943  -0.06369 20  MET A CA  
157  C C   . MET A 20  ? 0.41955 0.56713 0.27585 -0.00150 0.04249  -0.07081 20  MET A C   
158  O O   . MET A 20  ? 0.41228 0.58971 0.29262 -0.02628 0.02892  -0.05900 20  MET A O   
159  C CB  . MET A 20  ? 0.38055 0.52036 0.29761 0.03984  0.07950  -0.07082 20  MET A CB  
160  C CG  . MET A 20  ? 0.43391 0.55735 0.32607 0.06175  0.07212  -0.08903 20  MET A CG  
161  S SD  . MET A 20  ? 0.47840 0.60462 0.35325 0.06658  0.04335  -0.06717 20  MET A SD  
162  C CE  . MET A 20  ? 0.47819 0.56174 0.32634 0.06915  0.08104  -0.08235 20  MET A CE  
163  N N   . ILE A 21  ? 0.44191 0.55276 0.27020 0.03645  0.04303  -0.06951 21  ILE A N   
164  C CA  . ILE A 21  ? 0.44773 0.53543 0.27335 0.07211  0.04612  -0.05776 21  ILE A CA  
165  C C   . ILE A 21  ? 0.48853 0.53159 0.25615 0.12353  0.04380  -0.03697 21  ILE A C   
166  O O   . ILE A 21  ? 0.52222 0.53381 0.24444 0.17026  0.04904  -0.03118 21  ILE A O   
167  C CB  . ILE A 21  ? 0.39984 0.51974 0.29713 0.03785  0.02159  -0.07025 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.43584 0.50758 0.31785 0.02775  -0.04404 -0.06823 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.37163 0.51066 0.31402 0.02752  0.02918  -0.06869 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.45564 0.51289 0.33227 0.05455  -0.02459 -0.07420 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.46398 0.53378 0.27649 0.12286  0.01056  -0.02640 22  ALA A N   
172  C CA  . ALA A 22  ? 0.48448 0.53640 0.29024 0.10241  0.01914  -0.04618 22  ALA A CA  
173  C C   . ALA A 22  ? 0.49463 0.55698 0.31361 0.10765  0.02811  -0.06806 22  ALA A C   
174  O O   . ALA A 22  ? 0.50185 0.58258 0.31627 0.10220  0.02479  -0.07079 22  ALA A O   
175  C CB  . ALA A 22  ? 0.47177 0.52860 0.27252 0.07490  0.03393  -0.02199 22  ALA A CB  
176  N N   . GLY A 23  ? 0.49920 0.54890 0.33218 0.10286  0.02561  -0.06645 23  GLY A N   
177  C CA  . GLY A 23  ? 0.50282 0.56214 0.33826 0.08582  0.01420  -0.08484 23  GLY A CA  
178  C C   . GLY A 23  ? 0.52378 0.59267 0.34525 0.08491  0.02402  -0.10884 23  GLY A C   
179  O O   . GLY A 23  ? 0.53503 0.61506 0.34755 0.10676  0.00640  -0.11829 23  GLY A O   
180  N N   . PHE A 24  ? 0.51142 0.58220 0.34437 0.07370  0.02003  -0.12163 24  PHE A N   
181  C CA  . PHE A 24  ? 0.50306 0.55767 0.37552 0.08693  0.01790  -0.11437 24  PHE A CA  
182  C C   . PHE A 24  ? 0.53586 0.60307 0.41377 0.08989  -0.00651 -0.11450 24  PHE A C   
183  O O   . PHE A 24  ? 0.59194 0.63951 0.43673 0.06353  -0.03396 -0.12505 24  PHE A O   
184  C CB  . PHE A 24  ? 0.49400 0.50924 0.35867 0.07642  0.05116  -0.08931 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.53094 0.51400 0.36887 0.04056  0.11130  -0.08230 24  PHE A CG  
186  C CD1 . PHE A 24  ? 0.59152 0.54714 0.39160 0.02542  0.14360  -0.10166 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.51956 0.47045 0.36381 0.04038  0.12948  -0.09686 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.58940 0.53234 0.40347 0.02086  0.15134  -0.12727 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.55374 0.48322 0.38120 -0.00283 0.14131  -0.10965 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.56993 0.49775 0.40373 -0.00486 0.13943  -0.13062 24  PHE A CZ  
191  N N   . GLY A 25  ? 0.51492 0.61547 0.41642 0.12670  0.02716  -0.11843 25  GLY A N   
192  C CA  . GLY A 25  ? 0.53923 0.63895 0.43546 0.14411  0.06698  -0.13317 25  GLY A CA  
193  C C   . GLY A 25  ? 0.59614 0.65596 0.45380 0.14540  0.07885  -0.15375 25  GLY A C   
194  O O   . GLY A 25  ? 0.59353 0.66174 0.45656 0.14769  0.08082  -0.16068 25  GLY A O   
195  N N   . GLU A 26  ? 0.68800 0.68030 0.47592 0.11986  0.07783  -0.14583 26  GLU A N   
196  C CA  . GLU A 26  ? 0.76005 0.71664 0.49380 0.14133  0.09662  -0.12943 26  GLU A CA  
197  C C   . GLU A 26  ? 0.79363 0.69340 0.53604 0.09250  0.09096  -0.12909 26  GLU A C   
198  O O   . GLU A 26  ? 0.79368 0.73062 0.54373 0.07374  0.07592  -0.11837 26  GLU A O   
199  C CB  . GLU A 26  ? 0.79606 0.78301 0.46537 0.21421  0.11100  -0.11940 26  GLU A CB  
200  C CG  . GLU A 26  ? 0.86583 0.83363 0.44194 0.26664  0.09402  -0.10396 26  GLU A CG  
201  C CD  . GLU A 26  ? 0.98878 0.90941 0.44809 0.29869  0.03492  -0.07663 26  GLU A CD  
202  O OE1 . GLU A 26  ? 1.01388 0.93316 0.45537 0.34555  -0.01088 -0.04292 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 1.03981 0.93237 0.44725 0.27870  0.05270  -0.08729 26  GLU A OE2 
204  N N   . TYR A 27  ? 0.80717 0.64914 0.57470 0.08630  0.10504  -0.15116 27  TYR A N   
205  C CA  . TYR A 27  ? 0.79314 0.62892 0.62932 0.08990  0.10724  -0.14901 27  TYR A CA  
206  C C   . TYR A 27  ? 0.88083 0.63171 0.69905 0.07661  0.09868  -0.14864 27  TYR A C   
207  O O   . TYR A 27  ? 0.90271 0.61128 0.72232 0.10256  0.11699  -0.16820 27  TYR A O   
208  C CB  . TYR A 27  ? 0.70863 0.62703 0.61973 0.07823  0.11876  -0.13882 27  TYR A CB  
209  C CG  . TYR A 27  ? 0.66045 0.63768 0.60605 0.04695  0.14710  -0.12320 27  TYR A CG  
210  C CD1 . TYR A 27  ? 0.61894 0.65788 0.59049 0.01267  0.18151  -0.10942 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 0.65197 0.64136 0.59831 0.03984  0.14268  -0.11234 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 0.63098 0.68092 0.57175 0.00663  0.19422  -0.09194 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 0.63214 0.66800 0.58287 0.01108  0.16637  -0.09142 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 0.63990 0.70050 0.56489 0.00425  0.19266  -0.07940 27  TYR A CZ  
215  O OH  . TYR A 27  ? 0.64027 0.74109 0.54734 0.01666  0.19419  -0.06707 27  TYR A OH  
216  N N   . ASP A 28  ? 0.91853 0.66609 0.74032 0.05818  0.06890  -0.12479 28  ASP A N   
217  C CA  . ASP A 28  ? 0.94772 0.71017 0.78092 0.06257  0.02620  -0.09416 28  ASP A CA  
218  C C   . ASP A 28  ? 0.94428 0.73454 0.77436 0.01124  0.03439  -0.06650 28  ASP A C   
219  O O   . ASP A 28  ? 0.93373 0.73908 0.76559 -0.01843 0.04381  -0.03872 28  ASP A O   
220  C CB  . ASP A 28  ? 0.95917 0.75346 0.82264 0.08935  -0.00967 -0.08111 28  ASP A CB  
221  C CG  . ASP A 28  ? 0.97315 0.81135 0.85521 0.08592  -0.02891 -0.07692 28  ASP A CG  
222  O OD1 . ASP A 28  ? 0.99568 0.83431 0.87024 0.09345  -0.03250 -0.07075 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 0.96200 0.83614 0.86544 0.06872  -0.03322 -0.08716 28  ASP A OD2 
224  N N   . MET A 29  ? 0.91960 0.73795 0.76692 -0.00688 0.05328  -0.08175 29  MET A N   
225  C CA  . MET A 29  ? 0.88239 0.73558 0.75096 0.00268  0.09727  -0.09594 29  MET A CA  
226  C C   . MET A 29  ? 0.79565 0.72676 0.73099 0.06797  0.09715  -0.09501 29  MET A C   
227  O O   . MET A 29  ? 0.78524 0.74991 0.74309 0.07243  0.10580  -0.11696 29  MET A O   
228  C CB  . MET A 29  ? 0.94419 0.75100 0.75655 -0.02760 0.13311  -0.11128 29  MET A CB  
229  C CG  . MET A 29  ? 1.02096 0.76511 0.76627 -0.07099 0.15589  -0.12943 29  MET A CG  
230  S SD  . MET A 29  ? 1.05530 0.77177 0.78083 -0.09378 0.18176  -0.15454 29  MET A SD  
231  C CE  . MET A 29  ? 1.07865 0.76537 0.78691 -0.09564 0.22018  -0.14866 29  MET A CE  
232  N N   . GLU A 30  ? 0.73832 0.69847 0.69874 0.14590  0.08288  -0.07428 30  GLU A N   
233  C CA  . GLU A 30  ? 0.69046 0.68460 0.68570 0.20112  0.07312  -0.05858 30  GLU A CA  
234  C C   . GLU A 30  ? 0.63187 0.66222 0.63687 0.18165  0.07440  -0.08669 30  GLU A C   
235  O O   . GLU A 30  ? 0.60960 0.64810 0.61628 0.18507  0.09553  -0.14407 30  GLU A O   
236  C CB  . GLU A 30  ? 0.71543 0.69995 0.73298 0.25590  0.06838  -0.02239 30  GLU A CB  
237  C CG  . GLU A 30  ? 0.75094 0.70729 0.77810 0.30272  0.05618  0.00784  30  GLU A CG  
238  C CD  . GLU A 30  ? 0.79282 0.71348 0.82095 0.32054  0.03826  0.02294  30  GLU A CD  
239  O OE1 . GLU A 30  ? 0.82125 0.70552 0.83623 0.31100  0.03521  0.03401  30  GLU A OE1 
240  O OE2 . GLU A 30  ? 0.80329 0.72611 0.83507 0.33749  0.02623  0.02384  30  GLU A OE2 
241  N N   . TYR A 31  ? 0.59721 0.64971 0.60261 0.18161  0.06572  -0.06867 31  TYR A N   
242  C CA  . TYR A 31  ? 0.57504 0.64464 0.55445 0.22964  0.07168  -0.06753 31  TYR A CA  
243  C C   . TYR A 31  ? 0.57331 0.65657 0.53768 0.30476  0.05058  -0.06976 31  TYR A C   
244  O O   . TYR A 31  ? 0.55283 0.68019 0.53156 0.28197  0.03950  -0.05843 31  TYR A O   
245  C CB  . TYR A 31  ? 0.50896 0.62699 0.52249 0.19513  0.07867  -0.07718 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.44892 0.60544 0.47419 0.17090  0.06350  -0.10074 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.43143 0.60612 0.45756 0.19852  0.03108  -0.10639 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.44327 0.59763 0.44943 0.12243  0.03693  -0.09682 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.47451 0.61258 0.44149 0.17843  -0.00663 -0.10465 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.46973 0.60783 0.44053 0.09679  0.02430  -0.10293 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.50526 0.62024 0.42226 0.14576  0.00586  -0.11855 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.56842 0.62768 0.39706 0.13594  0.03310  -0.13790 31  TYR A OH  
253  N N   . ASP A 32  ? 0.60910 0.62971 0.53947 0.34218  0.03466  -0.07538 32  ASP A N   
254  C CA  . ASP A 32  ? 0.67951 0.63450 0.54243 0.32478  0.03854  -0.07434 32  ASP A CA  
255  C C   . ASP A 32  ? 0.63397 0.62722 0.53979 0.29809  0.01380  -0.05265 32  ASP A C   
256  O O   . ASP A 32  ? 0.61898 0.60656 0.55133 0.27495  -0.04877 -0.04823 32  ASP A O   
257  C CB  . ASP A 32  ? 0.78190 0.66223 0.55621 0.31139  0.04482  -0.06780 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.85101 0.68868 0.57880 0.31680  0.04423  -0.05555 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.84303 0.72182 0.58398 0.30896  0.07237  -0.05732 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 0.90104 0.67569 0.59381 0.31443  0.02486  -0.04615 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.57802 0.65582 0.53271 0.26962  0.04153  -0.04277 33  ASP A N   
262  C CA  . ASP A 33  ? 0.56941 0.70524 0.53303 0.22264  0.04181  -0.02809 33  ASP A CA  
263  C C   . ASP A 33  ? 0.58511 0.69911 0.52009 0.22154  -0.03779 -0.00424 33  ASP A C   
264  O O   . ASP A 33  ? 0.58378 0.71501 0.50787 0.19909  -0.06970 -0.00673 33  ASP A O   
265  C CB  . ASP A 33  ? 0.55548 0.74755 0.55077 0.16485  0.11946  -0.03659 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.65310 0.79023 0.57197 0.13130  0.14536  -0.03818 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.73028 0.79052 0.58468 0.14345  0.18158  -0.04518 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.65165 0.82215 0.57829 0.09048  0.10537  -0.02671 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.58087 0.65127 0.53775 0.25002  -0.04144 0.01854  34  VAL A N   
270  C CA  . VAL A 34  ? 0.58403 0.62246 0.56776 0.20482  -0.01743 0.03854  34  VAL A CA  
271  C C   . VAL A 34  ? 0.60520 0.62705 0.58078 0.19896  -0.01146 0.00928  34  VAL A C   
272  O O   . VAL A 34  ? 0.58356 0.64431 0.59018 0.20291  -0.01090 -0.00803 34  VAL A O   
273  C CB  . VAL A 34  ? 0.58105 0.61370 0.58293 0.15845  0.00827  0.06418  34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.57303 0.61037 0.59357 0.18404  -0.01724 0.08664  34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.57120 0.60850 0.58608 0.15046  0.02619  0.06078  34  VAL A CG2 
276  N N   . GLU A 35  ? 0.63511 0.60701 0.58041 0.19498  -0.00887 -0.00978 35  GLU A N   
277  C CA  . GLU A 35  ? 0.71318 0.59961 0.58902 0.19465  -0.02213 -0.00113 35  GLU A CA  
278  C C   . GLU A 35  ? 0.73573 0.56450 0.53800 0.18492  0.00028  -0.00706 35  GLU A C   
279  O O   . GLU A 35  ? 0.79703 0.59495 0.54575 0.15325  0.02441  0.00016  35  GLU A O   
280  C CB  . GLU A 35  ? 0.75463 0.63996 0.64812 0.18876  -0.04827 0.01875  35  GLU A CB  
281  C CG  . GLU A 35  ? 0.80136 0.69393 0.69948 0.17639  -0.06637 0.01514  35  GLU A CG  
282  C CD  . GLU A 35  ? 0.83186 0.72728 0.73710 0.16362  -0.07617 0.01762  35  GLU A CD  
283  O OE1 . GLU A 35  ? 0.84387 0.73646 0.76171 0.15170  -0.08347 0.01666  35  GLU A OE1 
284  O OE2 . GLU A 35  ? 0.83548 0.73598 0.73791 0.16959  -0.07167 0.02622  35  GLU A OE2 
285  N N   . PRO A 36  ? 0.68886 0.50628 0.48063 0.19122  -0.01346 -0.00528 36  PRO A N   
286  C CA  . PRO A 36  ? 0.66556 0.50279 0.45419 0.14369  0.01166  -0.02068 36  PRO A CA  
287  C C   . PRO A 36  ? 0.68057 0.51703 0.44695 0.11906  0.05104  -0.01315 36  PRO A C   
288  O O   . PRO A 36  ? 0.70806 0.54716 0.41892 0.13634  0.06887  -0.00883 36  PRO A O   
289  C CB  . PRO A 36  ? 0.64480 0.48717 0.43760 0.13452  -0.01187 -0.03301 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.66369 0.48105 0.44900 0.13793  -0.03663 -0.03465 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.67377 0.47347 0.45760 0.16668  -0.04396 -0.01863 36  PRO A CD  
292  N N   . GLU A 37  ? 0.64724 0.50257 0.47461 0.09009  0.06838  -0.01354 37  GLU A N   
293  C CA  . GLU A 37  ? 0.64849 0.50040 0.49917 0.06306  0.07282  -0.02363 37  GLU A CA  
294  C C   . GLU A 37  ? 0.57757 0.49526 0.44954 0.05918  0.09364  -0.05779 37  GLU A C   
295  O O   . GLU A 37  ? 0.56778 0.51009 0.43212 0.02404  0.11319  -0.06040 37  GLU A O   
296  C CB  . GLU A 37  ? 0.74856 0.52236 0.56849 0.05187  0.06898  -0.01328 37  GLU A CB  
297  C CG  . GLU A 37  ? 0.84186 0.55003 0.62163 0.02560  0.06414  -0.01464 37  GLU A CG  
298  C CD  . GLU A 37  ? 0.91761 0.56866 0.65506 -0.01035 0.07055  -0.01619 37  GLU A CD  
299  O OE1 . GLU A 37  ? 0.92854 0.57194 0.66907 0.00411  0.08539  -0.03499 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 0.96110 0.57792 0.66235 -0.04712 0.05495  -0.00425 37  GLU A OE2 
301  N N   . ILE A 38  ? 0.50542 0.47999 0.41943 0.08738  0.05322  -0.08002 38  ILE A N   
302  C CA  . ILE A 38  ? 0.47077 0.49214 0.40145 0.08635  0.00819  -0.08641 38  ILE A CA  
303  C C   . ILE A 38  ? 0.48907 0.48912 0.36636 0.15277  0.00171  -0.05257 38  ILE A C   
304  O O   . ILE A 38  ? 0.50961 0.51254 0.37235 0.17192  -0.01040 -0.03494 38  ILE A O   
305  C CB  . ILE A 38  ? 0.51232 0.51981 0.43266 0.02474  0.00719  -0.10938 38  ILE A CB  
306  C CG1 . ILE A 38  ? 0.57569 0.55088 0.47422 0.01487  0.02539  -0.15185 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.49764 0.53108 0.41232 0.00370  -0.02473 -0.09714 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 0.60062 0.56630 0.49427 0.02384  0.03753  -0.16451 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.47567 0.45936 0.33434 0.16450  0.02142  -0.04056 39  VAL A N   
310  C CA  . VAL A 39  ? 0.47683 0.43235 0.30776 0.12360  0.01868  -0.05356 39  VAL A CA  
311  C C   . VAL A 39  ? 0.47114 0.44313 0.29846 0.07576  0.04584  -0.07478 39  VAL A C   
312  O O   . VAL A 39  ? 0.50453 0.44236 0.29596 0.09161  0.01361  -0.08248 39  VAL A O   
313  C CB  . VAL A 39  ? 0.48763 0.41475 0.29701 0.10407  -0.00319 -0.06339 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.50730 0.40963 0.31492 0.07151  -0.01307 -0.09047 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.49693 0.42690 0.26716 0.12007  -0.00193 -0.03030 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.43624 0.44607 0.29322 0.05400  0.07618  -0.06742 40  ILE A N   
317  C CA  . ILE A 40  ? 0.41840 0.45471 0.29050 0.07795  0.07464  -0.08415 40  ILE A CA  
318  C C   . ILE A 40  ? 0.40494 0.42974 0.28746 0.08417  0.06418  -0.07547 40  ILE A C   
319  O O   . ILE A 40  ? 0.42933 0.41733 0.30017 0.07100  0.08193  -0.06228 40  ILE A O   
320  C CB  . ILE A 40  ? 0.44489 0.46725 0.28955 0.10139  0.05687  -0.10954 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.43690 0.45884 0.29232 0.06836  0.06468  -0.13146 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.45586 0.45391 0.27319 0.12940  0.03706  -0.09444 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.41756 0.45199 0.27821 0.02325  0.09220  -0.12901 40  ILE A CD1 
324  N N   . SER A 41  ? 0.41342 0.40745 0.27432 0.09363  0.05253  -0.09014 41  SER A N   
325  C CA  . SER A 41  ? 0.46618 0.44309 0.27314 0.06894  0.03908  -0.07372 41  SER A CA  
326  C C   . SER A 41  ? 0.44081 0.49585 0.26689 0.05924  0.06915  -0.03718 41  SER A C   
327  O O   . SER A 41  ? 0.46263 0.54844 0.29638 0.05428  0.02853  0.00556  41  SER A O   
328  C CB  . SER A 41  ? 0.53263 0.42226 0.30049 0.08341  0.04804  -0.09034 41  SER A CB  
329  O OG  . SER A 41  ? 0.59013 0.47425 0.31997 0.09275  0.04764  -0.07891 41  SER A OG  
330  N N   . ILE A 42  ? 0.41678 0.47041 0.25469 0.05983  0.10474  -0.04062 42  ILE A N   
331  C CA  . ILE A 42  ? 0.45415 0.45056 0.27765 0.08303  0.10096  -0.01117 42  ILE A CA  
332  C C   . ILE A 42  ? 0.51857 0.48114 0.30814 0.12545  0.12439  -0.01277 42  ILE A C   
333  O O   . ILE A 42  ? 0.56992 0.51623 0.31041 0.09406  0.15188  -0.02024 42  ILE A O   
334  C CB  . ILE A 42  ? 0.46253 0.42689 0.25683 0.10196  0.08004  0.00362  42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.43093 0.42671 0.26310 0.14652  0.07545  0.00545  42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.52506 0.44835 0.25883 0.06217  0.08277  -0.00175 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.42819 0.44186 0.27149 0.13843  0.06173  0.01021  42  ILE A CD1 
338  N N   . GLY A 43  ? 0.48935 0.46828 0.31803 0.13135  0.10556  -0.01311 43  GLY A N   
339  C CA  . GLY A 43  ? 0.49972 0.46954 0.33611 0.14713  0.11413  -0.04552 43  GLY A CA  
340  C C   . GLY A 43  ? 0.49496 0.50097 0.36774 0.11212  0.10856  -0.06580 43  GLY A C   
341  O O   . GLY A 43  ? 0.52331 0.57695 0.42460 0.06102  0.12966  -0.10715 43  GLY A O   
342  N N   . GLY A 44  ? 0.45240 0.46960 0.33162 0.09933  0.10693  -0.00176 44  GLY A N   
343  C CA  . GLY A 44  ? 0.43529 0.49205 0.32381 0.06010  0.09549  0.01043  44  GLY A CA  
344  C C   . GLY A 44  ? 0.39749 0.49765 0.31318 0.03240  0.06892  0.00176  44  GLY A C   
345  O O   . GLY A 44  ? 0.34865 0.47370 0.31363 0.04203  0.05336  -0.01551 44  GLY A O   
346  N N   . ASP A 45  ? 0.37156 0.53036 0.30324 0.01244  0.07011  -0.00551 45  ASP A N   
347  C CA  . ASP A 45  ? 0.30403 0.53687 0.28957 0.02056  0.06627  -0.00035 45  ASP A CA  
348  C C   . ASP A 45  ? 0.30461 0.55534 0.31228 0.01810  0.08779  -0.00397 45  ASP A C   
349  O O   . ASP A 45  ? 0.29501 0.57158 0.31651 0.02469  0.07800  -0.02647 45  ASP A O   
350  C CB  . ASP A 45  ? 0.32098 0.53595 0.29183 0.05709  0.03839  -0.02463 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.38191 0.56742 0.30062 0.02857  0.05254  -0.04393 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.39799 0.56045 0.30766 0.01112  0.06892  -0.02666 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.35722 0.58452 0.30514 0.04169  0.06436  -0.06462 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.31028 0.55382 0.32663 -0.00266 0.10440  -0.00723 46  GLY A N   
355  C CA  . GLY A 46  ? 0.29827 0.53066 0.31199 -0.01860 0.09276  -0.04283 46  GLY A CA  
356  C C   . GLY A 46  ? 0.31916 0.54220 0.29471 -0.00089 0.07502  -0.05007 46  GLY A C   
357  O O   . GLY A 46  ? 0.35164 0.56239 0.27799 0.00186  0.04828  -0.06450 46  GLY A O   
358  N N   . THR A 47  ? 0.30539 0.51462 0.28532 0.03344  0.07995  -0.04469 47  THR A N   
359  C CA  . THR A 47  ? 0.36496 0.47488 0.27121 0.01576  0.05016  -0.06604 47  THR A CA  
360  C C   . THR A 47  ? 0.35980 0.46753 0.25505 0.03906  0.05070  -0.05055 47  THR A C   
361  O O   . THR A 47  ? 0.34333 0.45840 0.24912 -0.00385 0.03545  -0.04289 47  THR A O   
362  C CB  . THR A 47  ? 0.41075 0.46066 0.27968 0.01125  0.03633  -0.05344 47  THR A CB  
363  O OG1 . THR A 47  ? 0.50038 0.48777 0.30943 -0.00148 0.03391  0.00074  47  THR A OG1 
364  C CG2 . THR A 47  ? 0.34735 0.42964 0.27238 0.00940  0.01697  -0.08218 47  THR A CG2 
365  N N   . PHE A 48  ? 0.35074 0.46772 0.25400 0.03620  0.07922  -0.03125 48  PHE A N   
366  C CA  . PHE A 48  ? 0.33492 0.47517 0.27749 0.00147  0.03970  -0.04624 48  PHE A CA  
367  C C   . PHE A 48  ? 0.33338 0.47608 0.28955 -0.00258 0.01143  -0.03204 48  PHE A C   
368  O O   . PHE A 48  ? 0.36635 0.47012 0.29003 -0.01215 0.05261  -0.04087 48  PHE A O   
369  C CB  . PHE A 48  ? 0.38019 0.47829 0.27590 -0.04583 0.03720  -0.07353 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.42307 0.48766 0.27309 -0.04702 0.06663  -0.09674 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.43329 0.48569 0.28054 -0.03324 0.07575  -0.07677 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.47476 0.48603 0.26654 -0.00810 0.08369  -0.10993 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.45686 0.49512 0.27295 -0.01400 0.07447  -0.06645 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.50492 0.51362 0.27025 -0.00493 0.07749  -0.10380 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.50083 0.50073 0.26379 -0.00334 0.09965  -0.09004 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.28498 0.46402 0.31859 -0.00244 -0.02152 -0.02541 49  LEU A N   
377  C CA  . LEU A 49  ? 0.28111 0.44195 0.35515 0.04859  0.00350  -0.02682 49  LEU A CA  
378  C C   . LEU A 49  ? 0.34227 0.46246 0.34862 0.04973  0.01802  -0.02459 49  LEU A C   
379  O O   . LEU A 49  ? 0.37398 0.46780 0.34642 0.07469  -0.00662 -0.01441 49  LEU A O   
380  C CB  . LEU A 49  ? 0.33869 0.41457 0.41934 0.11047  0.06075  -0.06627 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.37330 0.42485 0.49985 0.07699  0.07301  -0.05081 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.36227 0.39580 0.52988 0.03200  0.06528  -0.06300 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.41472 0.42158 0.51691 0.08787  0.10401  -0.05249 49  LEU A CD2 
384  N N   . SER A 50  ? 0.34658 0.47070 0.36344 0.00918  0.04679  -0.05929 50  SER A N   
385  C CA  . SER A 50  ? 0.34482 0.47811 0.38010 -0.00361 0.04816  -0.05737 50  SER A CA  
386  C C   . SER A 50  ? 0.32468 0.50321 0.36102 0.01522  0.04381  -0.08239 50  SER A C   
387  O O   . SER A 50  ? 0.33803 0.54964 0.38103 0.04034  0.04310  -0.10473 50  SER A O   
388  C CB  . SER A 50  ? 0.42607 0.47099 0.43304 -0.05768 0.05799  -0.06894 50  SER A CB  
389  O OG  . SER A 50  ? 0.45724 0.50524 0.47640 -0.06387 0.06837  -0.06542 50  SER A OG  
390  N N   . ALA A 51  ? 0.38894 0.49439 0.33137 -0.01381 0.06407  -0.08509 51  ALA A N   
391  C CA  . ALA A 51  ? 0.36336 0.47940 0.31709 -0.01242 0.03873  -0.05099 51  ALA A CA  
392  C C   . ALA A 51  ? 0.36482 0.48261 0.30442 0.03153  0.01078  -0.04384 51  ALA A C   
393  O O   . ALA A 51  ? 0.40627 0.47561 0.32332 0.08196  -0.00632 -0.03009 51  ALA A O   
394  C CB  . ALA A 51  ? 0.36392 0.48014 0.32195 -0.03943 0.03419  -0.03632 51  ALA A CB  
395  N N   . PHE A 52  ? 0.30293 0.49649 0.28281 0.04314  0.02287  -0.05300 52  PHE A N   
396  C CA  . PHE A 52  ? 0.34258 0.51400 0.28669 0.04757  0.01361  -0.03926 52  PHE A CA  
397  C C   . PHE A 52  ? 0.36414 0.53782 0.30576 0.05704  0.00431  -0.03927 52  PHE A C   
398  O O   . PHE A 52  ? 0.37579 0.52321 0.32807 0.05805  -0.01972 -0.02978 52  PHE A O   
399  C CB  . PHE A 52  ? 0.33182 0.48647 0.27746 0.03236  0.01737  -0.00952 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.36024 0.46197 0.27547 0.06476  0.00361  -0.00085 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.42879 0.44851 0.28742 0.09816  0.00337  0.01202  52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.35721 0.45957 0.25274 0.05107  -0.00226 -0.03007 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.45070 0.43466 0.27952 0.10424  0.02933  -0.00880 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.39021 0.44794 0.26917 0.05447  0.00720  -0.01772 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.41318 0.43784 0.27358 0.08426  0.02847  -0.01038 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.32040 0.56016 0.29624 0.07514  0.02291  -0.04980 53  HIS A N   
407  C CA  . HIS A 53  ? 0.29942 0.58785 0.28627 0.12557  0.02512  -0.05101 53  HIS A CA  
408  C C   . HIS A 53  ? 0.35437 0.66133 0.30848 0.15367  0.01411  -0.04678 53  HIS A C   
409  O O   . HIS A 53  ? 0.37888 0.71400 0.31900 0.17825  -0.00479 -0.04703 53  HIS A O   
410  C CB  . HIS A 53  ? 0.29017 0.54296 0.26977 0.11512  0.03395  -0.05054 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.33422 0.53285 0.28564 0.10075  0.03711  -0.02410 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.38096 0.53808 0.29210 0.07480  0.06959  -0.02107 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.33192 0.51283 0.29152 0.09291  0.02171  -0.00887 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.32940 0.51565 0.30193 0.04983  0.07448  0.00278  53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.32036 0.49634 0.30775 0.05980  0.03201  0.00519  53  HIS A NE2 
416  N N   . GLN A 54  ? 0.40632 0.66310 0.33738 0.15560  0.04885  -0.05247 54  GLN A N   
417  C CA  . GLN A 54  ? 0.38498 0.64463 0.37359 0.14103  0.04613  -0.05471 54  GLN A CA  
418  C C   . GLN A 54  ? 0.39662 0.64292 0.40096 0.13138  0.01620  -0.03140 54  GLN A C   
419  O O   . GLN A 54  ? 0.37448 0.67478 0.42592 0.08321  -0.01453 -0.00055 54  GLN A O   
420  C CB  . GLN A 54  ? 0.38899 0.66442 0.38994 0.09710  0.09911  -0.07901 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.40919 0.70797 0.43630 0.11803  0.10765  -0.07497 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.46749 0.74676 0.49554 0.13888  0.11861  -0.07779 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.45863 0.75386 0.49087 0.18247  0.11914  -0.04350 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.47931 0.74845 0.53122 0.12362  0.12694  -0.09960 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.44875 0.61568 0.39568 0.12348  0.01243  -0.04456 55  TYR A N   
426  C CA  . TYR A 55  ? 0.49131 0.59723 0.39301 0.11999  0.01433  -0.04726 55  TYR A CA  
427  C C   . TYR A 55  ? 0.48151 0.60581 0.41051 0.13878  -0.00068 -0.03811 55  TYR A C   
428  O O   . TYR A 55  ? 0.48740 0.62060 0.41951 0.16715  -0.00876 -0.02074 55  TYR A O   
429  C CB  . TYR A 55  ? 0.51969 0.57433 0.38461 0.11226  0.01757  -0.06417 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.59625 0.55203 0.38319 0.14735  0.00953  -0.08694 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.62392 0.55757 0.38235 0.17214  0.00605  -0.07952 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.60305 0.53428 0.37958 0.17026  0.02025  -0.08671 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.64551 0.56006 0.37816 0.18574  0.00769  -0.07218 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.61594 0.53554 0.38103 0.19510  0.02365  -0.09393 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.63388 0.55696 0.37979 0.19873  -0.00328 -0.08321 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.60956 0.55879 0.37027 0.23895  -0.03886 -0.10082 55  TYR A OH  
437  N N   . GLU A 56  ? 0.48914 0.59684 0.41974 0.11654  -0.01932 -0.03465 56  GLU A N   
438  C CA  . GLU A 56  ? 0.52959 0.60988 0.44705 0.08449  -0.03117 0.01015  56  GLU A CA  
439  C C   . GLU A 56  ? 0.53421 0.62285 0.45116 0.11566  -0.06167 0.03337  56  GLU A C   
440  O O   . GLU A 56  ? 0.53504 0.65349 0.42804 0.09294  -0.11962 0.05892  56  GLU A O   
441  C CB  . GLU A 56  ? 0.59206 0.60142 0.46290 0.04929  -0.05264 0.02354  56  GLU A CB  
442  C CG  . GLU A 56  ? 0.67014 0.59334 0.47974 0.02341  -0.06372 0.02649  56  GLU A CG  
443  C CD  . GLU A 56  ? 0.73435 0.60964 0.50541 0.04746  -0.05801 0.03272  56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.70499 0.58871 0.50592 0.06821  -0.05855 0.03823  56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.78845 0.64556 0.53053 0.03257  -0.05792 0.02811  56  GLU A OE2 
446  N N   . GLU A 57  ? 0.56207 0.59478 0.47727 0.15630  -0.04288 0.03484  57  GLU A N   
447  C CA  . GLU A 57  ? 0.61481 0.58127 0.50703 0.17227  -0.04165 0.02407  57  GLU A CA  
448  C C   . GLU A 57  ? 0.64358 0.54664 0.49993 0.19485  0.00527  0.00431  57  GLU A C   
449  O O   . GLU A 57  ? 0.68348 0.52169 0.51061 0.25314  -0.01815 0.01789  57  GLU A O   
450  C CB  . GLU A 57  ? 0.65304 0.61334 0.54602 0.15541  -0.08566 0.04023  57  GLU A CB  
451  C CG  . GLU A 57  ? 0.70140 0.64317 0.59596 0.16105  -0.09886 0.05472  57  GLU A CG  
452  C CD  . GLU A 57  ? 0.73952 0.65971 0.64295 0.17824  -0.11939 0.06093  57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.73162 0.66544 0.65750 0.19754  -0.14793 0.08377  57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.76534 0.66122 0.65942 0.17414  -0.11268 0.05093  57  GLU A OE2 
455  N N   . ARG A 58  ? 0.62591 0.53997 0.48637 0.17719  0.05016  -0.00399 58  ARG A N   
456  C CA  . ARG A 58  ? 0.62850 0.54986 0.49683 0.14031  0.07326  -0.01270 58  ARG A CA  
457  C C   . ARG A 58  ? 0.63094 0.53021 0.47426 0.13067  0.06421  -0.00115 58  ARG A C   
458  O O   . ARG A 58  ? 0.62052 0.51556 0.46542 0.10787  0.06535  0.01718  58  ARG A O   
459  C CB  . ARG A 58  ? 0.62331 0.59030 0.51730 0.11279  0.11226  -0.04374 58  ARG A CB  
460  C CG  . ARG A 58  ? 0.66620 0.66059 0.53809 0.07872  0.12064  -0.07229 58  ARG A CG  
461  C CD  . ARG A 58  ? 0.73113 0.72439 0.56189 0.03509  0.11347  -0.08358 58  ARG A CD  
462  N NE  . ARG A 58  ? 0.81334 0.78142 0.59023 0.02055  0.11221  -0.08750 58  ARG A NE  
463  C CZ  . ARG A 58  ? 0.88323 0.81271 0.62081 -0.01546 0.12843  -0.08131 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 0.89572 0.83198 0.63100 -0.04208 0.13209  -0.06717 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 0.90905 0.80360 0.63192 -0.00908 0.13390  -0.08912 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.61843 0.49668 0.44592 0.15208  0.05083  -0.02923 59  LEU A N   
467  C CA  . LEU A 59  ? 0.61290 0.49185 0.43023 0.15941  0.04367  -0.02325 59  LEU A CA  
468  C C   . LEU A 59  ? 0.70581 0.50322 0.45104 0.16076  0.07739  0.00548  59  LEU A C   
469  O O   . LEU A 59  ? 0.75085 0.52268 0.44274 0.12866  0.08190  -0.00999 59  LEU A O   
470  C CB  . LEU A 59  ? 0.55194 0.49359 0.40051 0.14159  0.00210  -0.04321 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.53492 0.52515 0.38473 0.15115  -0.00259 -0.03476 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.52141 0.53114 0.39087 0.16918  -0.01077 -0.04107 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.52804 0.53208 0.36424 0.13099  -0.01462 -0.03756 59  LEU A CD2 
474  N N   . ASP A 60  ? 0.75757 0.50235 0.48092 0.16995  0.09183  0.03729  60  ASP A N   
475  C CA  . ASP A 60  ? 0.85344 0.54580 0.50244 0.15080  0.09641  0.04992  60  ASP A CA  
476  C C   . ASP A 60  ? 0.80929 0.55196 0.49491 0.11110  0.05851  0.03767  60  ASP A C   
477  O O   . ASP A 60  ? 0.86398 0.56256 0.49393 0.09944  0.02078  0.01716  60  ASP A O   
478  C CB  . ASP A 60  ? 0.98611 0.59812 0.53549 0.12639  0.12171  0.07813  60  ASP A CB  
479  C CG  . ASP A 60  ? 1.09542 0.64888 0.56678 0.08910  0.12465  0.10583  60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.12671 0.64586 0.56371 0.08911  0.13071  0.13167  60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.14415 0.68873 0.59535 0.07379  0.11370  0.09088  60  ASP A OD2 
482  N N   . GLU A 61  ? 0.70420 0.53382 0.50016 0.10789  0.06442  0.03839  61  GLU A N   
483  C CA  . GLU A 61  ? 0.67015 0.50797 0.50713 0.09414  0.04064  0.01097  61  GLU A CA  
484  C C   . GLU A 61  ? 0.65105 0.46738 0.48072 0.08939  0.04262  -0.02650 61  GLU A C   
485  O O   . GLU A 61  ? 0.70029 0.47604 0.49336 0.08690  0.03945  -0.03710 61  GLU A O   
486  C CB  . GLU A 61  ? 0.67041 0.52740 0.54371 0.07609  0.02244  0.00320  61  GLU A CB  
487  C CG  . GLU A 61  ? 0.67096 0.56847 0.58771 0.02589  0.00051  -0.01795 61  GLU A CG  
488  C CD  . GLU A 61  ? 0.67258 0.61307 0.63672 0.01179  0.01299  -0.04065 61  GLU A CD  
489  O OE1 . GLU A 61  ? 0.68597 0.62888 0.65062 -0.00152 0.01726  -0.06181 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 0.66739 0.63334 0.65689 0.01462  0.03148  -0.03706 61  GLU A OE2 
491  N N   . ILE A 62  ? 0.60036 0.40756 0.45174 0.06059  0.06308  -0.04684 62  ILE A N   
492  C CA  . ILE A 62  ? 0.59027 0.39821 0.43404 0.03890  0.06912  -0.04296 62  ILE A CA  
493  C C   . ILE A 62  ? 0.62778 0.42559 0.40864 0.03376  0.04097  -0.04490 62  ILE A C   
494  O O   . ILE A 62  ? 0.69372 0.43080 0.41634 0.08234  0.03919  -0.04879 62  ILE A O   
495  C CB  . ILE A 62  ? 0.54922 0.38917 0.45013 0.04374  0.07957  -0.03436 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.52769 0.39876 0.46974 0.02257  0.07842  -0.02145 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.53241 0.37555 0.44936 0.08376  0.08504  -0.04069 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.55678 0.42095 0.48519 0.01190  0.08348  -0.00368 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.57839 0.43269 0.38084 -0.01584 -0.00105 -0.06292 63  ALA A N   
500  C CA  . ALA A 63  ? 0.58124 0.43047 0.38604 -0.02155 -0.01780 -0.07062 63  ALA A CA  
501  C C   . ALA A 63  ? 0.53656 0.43310 0.37940 0.00934  0.00270  -0.05724 63  ALA A C   
502  O O   . ALA A 63  ? 0.52691 0.45637 0.39816 0.02004  -0.00607 -0.03423 63  ALA A O   
503  C CB  . ALA A 63  ? 0.61695 0.44661 0.41746 -0.01880 -0.01856 -0.08290 63  ALA A CB  
504  N N   . PHE A 64  ? 0.48683 0.40191 0.34540 0.06669  0.01326  -0.05668 64  PHE A N   
505  C CA  . PHE A 64  ? 0.46953 0.40427 0.31165 0.06350  0.01504  -0.04293 64  PHE A CA  
506  C C   . PHE A 64  ? 0.55976 0.40951 0.30059 0.03243  -0.00070 -0.02801 64  PHE A C   
507  O O   . PHE A 64  ? 0.65973 0.42478 0.30808 0.03313  -0.00089 -0.00815 64  PHE A O   
508  C CB  . PHE A 64  ? 0.41339 0.39889 0.30473 0.06253  0.03648  -0.03364 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.41106 0.39413 0.30032 0.07077  0.05617  -0.01620 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.42671 0.37133 0.32636 0.06600  0.05564  -0.01342 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.45348 0.40648 0.30234 0.07586  0.05282  -0.01034 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.44665 0.39299 0.32199 0.04461  0.05571  -0.01373 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.43260 0.40307 0.30982 0.07833  0.06862  -0.00680 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.42764 0.40965 0.31023 0.06215  0.07107  -0.01824 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.50075 0.40582 0.27452 0.00183  0.00098  -0.02063 65  ILE A N   
516  C CA  . ILE A 65  ? 0.46292 0.42196 0.29050 0.04475  -0.00284 -0.02325 65  ILE A CA  
517  C C   . ILE A 65  ? 0.42467 0.46169 0.28776 0.05722  -0.00382 -0.02394 65  ILE A C   
518  O O   . ILE A 65  ? 0.42272 0.48141 0.29756 0.04248  0.01005  -0.04802 65  ILE A O   
519  C CB  . ILE A 65  ? 0.51404 0.40754 0.32368 0.05323  -0.03013 -0.04764 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.57019 0.39439 0.36390 0.01933  -0.02119 -0.11215 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.48652 0.43130 0.32298 0.09106  -0.05889 -0.02472 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.54827 0.39844 0.40148 0.00331  -0.02537 -0.13581 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.39678 0.47702 0.28696 0.11667  0.03302  -0.01447 66  GLY A N   
524  C CA  . GLY A 66  ? 0.41285 0.49194 0.29628 0.14142  0.05340  -0.02202 66  GLY A CA  
525  C C   . GLY A 66  ? 0.44414 0.52566 0.31593 0.15094  0.10561  -0.01684 66  GLY A C   
526  O O   . GLY A 66  ? 0.48859 0.55623 0.32010 0.21844  0.07918  -0.01237 66  GLY A O   
527  N N   . ILE A 67  ? 0.44492 0.51610 0.30910 0.07570  0.15229  -0.00978 67  ILE A N   
528  C CA  . ILE A 67  ? 0.44010 0.51663 0.31759 0.08410  0.13392  -0.01559 67  ILE A CA  
529  C C   . ILE A 67  ? 0.47121 0.55583 0.37711 0.09525  0.17769  -0.00780 67  ILE A C   
530  O O   . ILE A 67  ? 0.53405 0.58466 0.38199 0.11030  0.17393  -0.02927 67  ILE A O   
531  C CB  . ILE A 67  ? 0.44711 0.48338 0.29344 0.07596  0.08153  -0.04105 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.44343 0.48139 0.30098 0.10310  0.04024  -0.04592 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.44580 0.48368 0.27973 0.02637  0.09280  -0.05514 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.43557 0.53493 0.31392 0.06098  0.04102  -0.05368 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.49110 0.58540 0.44689 0.08189  0.19550  0.03219  68  HIS A N   
536  C CA  . HIS A 68  ? 0.57051 0.62534 0.54563 0.12238  0.20030  0.12633  68  HIS A CA  
537  C C   . HIS A 68  ? 0.54380 0.63250 0.58389 0.16664  0.21861  0.15753  68  HIS A C   
538  O O   . HIS A 68  ? 0.53023 0.60638 0.58095 0.14989  0.20852  0.16489  68  HIS A O   
539  C CB  . HIS A 68  ? 0.64961 0.64446 0.60940 0.12299  0.14395  0.18960  68  HIS A CB  
540  C CG  . HIS A 68  ? 0.72673 0.66106 0.66292 0.11036  0.08975  0.22584  68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.78713 0.67288 0.69670 0.06394  0.10246  0.22837  68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.77258 0.67617 0.68414 0.13034  0.09205  0.23619  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.82324 0.68258 0.71237 0.09621  0.14193  0.22590  68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.83169 0.69305 0.70756 0.12022  0.13891  0.22634  68  HIS A NE2 
545  N N   . THR A 69  ? 0.52528 0.67118 0.64217 0.19826  0.23688  0.16822  69  THR A N   
546  C CA  . THR A 69  ? 0.65976 0.73623 0.72638 0.18553  0.24170  0.15153  69  THR A CA  
547  C C   . THR A 69  ? 0.76945 0.79435 0.80965 0.15124  0.24930  0.10314  69  THR A C   
548  O O   . THR A 69  ? 0.79213 0.79916 0.84041 0.19668  0.24546  0.08886  69  THR A O   
549  C CB  . THR A 69  ? 0.65953 0.74606 0.72928 0.15796  0.24783  0.18956  69  THR A CB  
550  O OG1 . THR A 69  ? 0.70784 0.77977 0.72950 0.09613  0.25598  0.21656  69  THR A OG1 
551  C CG2 . THR A 69  ? 0.60308 0.72650 0.73275 0.18014  0.25188  0.19444  69  THR A CG2 
552  N N   . GLY A 70  ? 0.82969 0.84184 0.86554 0.06770  0.24132  0.07155  70  GLY A N   
553  C CA  . GLY A 70  ? 0.87220 0.88619 0.90400 0.02158  0.24013  0.05751  70  GLY A CA  
554  C C   . GLY A 70  ? 0.95659 0.93905 0.92390 0.00481  0.22802  0.05234  70  GLY A C   
555  O O   . GLY A 70  ? 0.98054 0.93907 0.92774 0.01023  0.21048  0.04101  70  GLY A O   
556  N N   . HIS A 71  ? 1.00793 0.99026 0.93805 -0.00175 0.23512  0.06088  71  HIS A N   
557  C CA  . HIS A 71  ? 1.06052 1.04365 0.95755 0.01036  0.17733  0.05624  71  HIS A CA  
558  C C   . HIS A 71  ? 1.03274 1.10026 0.91886 -0.00122 0.19201  0.08543  71  HIS A C   
559  O O   . HIS A 71  ? 1.01314 1.12620 0.93064 -0.04452 0.21949  0.09799  71  HIS A O   
560  C CB  . HIS A 71  ? 1.10471 1.02722 1.01321 0.05415  0.12228  0.01166  71  HIS A CB  
561  C CG  . HIS A 71  ? 1.15984 1.02509 1.06748 0.11169  0.04927  0.00084  71  HIS A CG  
562  N ND1 . HIS A 71  ? 1.18319 1.02438 1.08652 0.12569  0.02448  0.00774  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 1.18505 1.02394 1.09372 0.14114  0.02503  0.00148  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 1.18991 1.02259 1.10404 0.12641  0.01736  0.00597  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.20019 1.02335 1.10641 0.14180  0.01425  0.00350  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.98462 1.10344 0.85757 0.07669  0.15958  0.08607  72  LEU A N   
567  C CA  . LEU A 72  ? 0.93513 1.06556 0.78730 0.16432  0.10116  0.08239  72  LEU A CA  
568  C C   . LEU A 72  ? 0.92984 1.03905 0.66997 0.32410  0.09442  0.10517  72  LEU A C   
569  O O   . LEU A 72  ? 1.00544 1.05565 0.65614 0.44630  0.06830  0.13446  72  LEU A O   
570  C CB  . LEU A 72  ? 0.91029 1.04248 0.82290 0.08648  0.04956  0.06823  72  LEU A CB  
571  C CG  . LEU A 72  ? 0.88224 1.01523 0.84947 0.01529  0.04255  0.06107  72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.87352 1.00324 0.86561 -0.00170 0.03881  0.05266  72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.84963 0.99758 0.85097 -0.01773 0.05381  0.06783  72  LEU A CD2 
574  N N   . GLY A 73  ? 0.86021 0.97305 0.56884 0.28334  0.07618  0.05549  73  GLY A N   
575  C CA  . GLY A 73  ? 0.72341 0.87031 0.45227 0.21163  0.06425  -0.04380 73  GLY A CA  
576  C C   . GLY A 73  ? 0.63163 0.77503 0.38325 0.15693  0.02453  -0.11008 73  GLY A C   
577  O O   . GLY A 73  ? 0.66524 0.75044 0.39061 0.16837  0.01188  -0.11708 73  GLY A O   
578  N N   . PHE A 74  ? 0.50214 0.71083 0.34064 0.09089  0.04762  -0.13701 74  PHE A N   
579  C CA  . PHE A 74  ? 0.38564 0.63366 0.30764 0.00937  0.02850  -0.15192 74  PHE A CA  
580  C C   . PHE A 74  ? 0.36705 0.60423 0.33239 -0.06294 0.04124  -0.17857 74  PHE A C   
581  O O   . PHE A 74  ? 0.37879 0.65808 0.38322 -0.07242 0.05501  -0.19439 74  PHE A O   
582  C CB  . PHE A 74  ? 0.39934 0.60154 0.27709 0.00149  0.02067  -0.12424 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.45134 0.58841 0.25718 -0.01101 0.04649  -0.10485 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.48382 0.58991 0.24391 0.00710  0.04648  -0.06996 74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.47097 0.58990 0.29412 -0.01732 0.06996  -0.09424 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.48099 0.60118 0.27093 -0.02298 0.07580  -0.03759 74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.50217 0.60696 0.34128 -0.01266 0.09778  -0.07449 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.50395 0.61920 0.32972 -0.00839 0.08354  -0.05872 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.38215 0.53508 0.29034 -0.04865 0.05210  -0.15133 75  TYR A N   
590  C CA  . TYR A 75  ? 0.42709 0.47577 0.26012 -0.03467 0.05409  -0.09091 75  TYR A CA  
591  C C   . TYR A 75  ? 0.54006 0.49553 0.29093 0.01823  0.02015  -0.07417 75  TYR A C   
592  O O   . TYR A 75  ? 0.57552 0.49009 0.32178 0.04665  -0.02693 -0.05563 75  TYR A O   
593  C CB  . TYR A 75  ? 0.44377 0.44645 0.25008 -0.06243 0.09439  -0.06538 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.41804 0.43291 0.25533 -0.05468 0.07759  -0.06856 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.39953 0.44938 0.25859 -0.04363 0.09455  -0.06762 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.40012 0.40805 0.26291 -0.03349 0.05308  -0.04155 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.37575 0.45735 0.26817 -0.01205 0.07833  -0.07304 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.34628 0.40667 0.26591 -0.00587 0.05441  -0.02088 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.35573 0.44660 0.27074 0.01504  0.07433  -0.04408 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.35574 0.43617 0.28951 -0.00069 0.05374  -0.03007 75  TYR A OH  
601  N N   . ALA A 76  ? 0.54961 0.51797 0.27461 0.02850  0.06608  -0.08156 76  ALA A N   
602  C CA  . ALA A 76  ? 0.52463 0.53486 0.25294 0.01532  0.09006  -0.07945 76  ALA A CA  
603  C C   . ALA A 76  ? 0.60292 0.55296 0.29043 0.07724  0.04607  -0.10550 76  ALA A C   
604  O O   . ALA A 76  ? 0.62009 0.55364 0.30541 0.11109  -0.04006 -0.13082 76  ALA A O   
605  C CB  . ALA A 76  ? 0.43850 0.53416 0.22887 -0.04722 0.11878  -0.03526 76  ALA A CB  
606  N N   . ASP A 77  ? 0.62873 0.58944 0.33182 0.08452  0.07069  -0.06428 77  ASP A N   
607  C CA  . ASP A 77  ? 0.59306 0.63112 0.34060 0.04986  0.06214  -0.04632 77  ASP A CA  
608  C C   . ASP A 77  ? 0.52072 0.63280 0.38002 0.03953  0.06947  -0.02091 77  ASP A C   
609  O O   . ASP A 77  ? 0.52576 0.66210 0.39706 0.04502  0.09997  -0.03166 77  ASP A O   
610  C CB  . ASP A 77  ? 0.67825 0.66115 0.34302 0.02914  0.06672  -0.05702 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.77005 0.69708 0.36615 0.05212  0.10557  -0.06274 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.75087 0.70391 0.37845 0.10318  0.06634  -0.06992 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.85343 0.71241 0.38138 0.03105  0.15900  -0.08793 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.41701 0.58316 0.39740 0.03510  0.08200  0.00598  78  TRP A N   
615  C CA  . TRP A 78  ? 0.52087 0.57460 0.42770 0.05458  0.07681  0.00492  78  TRP A CA  
616  C C   . TRP A 78  ? 0.57109 0.56681 0.41537 0.11095  0.07420  0.01748  78  TRP A C   
617  O O   . TRP A 78  ? 0.59663 0.54006 0.39516 0.13729  0.10711  0.02089  78  TRP A O   
618  C CB  . TRP A 78  ? 0.58343 0.57054 0.47244 0.03606  0.06087  -0.01749 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.68066 0.59235 0.51926 0.03196  0.03254  -0.01849 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.70954 0.60978 0.53736 0.04348  0.01859  -0.03901 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.76926 0.61026 0.54574 0.01516  -0.00740 -0.01839 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.76463 0.61226 0.54796 0.03190  0.00771  -0.04503 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.80753 0.61818 0.55585 0.01392  -0.02196 -0.03500 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.79299 0.61719 0.55803 -0.00614 -0.03101 -0.03005 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.83241 0.63129 0.56784 -0.01281 -0.05719 -0.03606 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.82526 0.63230 0.57104 -0.01560 -0.06349 -0.03925 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.83524 0.63501 0.57238 -0.02324 -0.07805 -0.03644 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.57591 0.57968 0.43453 0.11814  0.04178  0.00663  79  ARG A N   
629  C CA  . ARG A 79  ? 0.54923 0.60081 0.45803 0.13774  0.04079  -0.01102 79  ARG A CA  
630  C C   . ARG A 79  ? 0.50143 0.61963 0.42657 0.16288  0.01877  -0.02945 79  ARG A C   
631  O O   . ARG A 79  ? 0.47756 0.63734 0.43507 0.20500  -0.02117 -0.03931 79  ARG A O   
632  C CB  . ARG A 79  ? 0.59007 0.62741 0.51194 0.12799  0.04244  -0.00642 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.63400 0.64785 0.56931 0.12920  0.03657  0.00481  79  ARG A CG  
634  C CD  . ARG A 79  ? 0.66337 0.64030 0.61344 0.13121  0.02250  0.00747  79  ARG A CD  
635  N NE  . ARG A 79  ? 0.70471 0.64280 0.64418 0.12705  0.01448  0.00124  79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.72786 0.65885 0.65870 0.14276  0.00751  -0.00719 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.74641 0.66969 0.66867 0.13252  0.01838  -0.00823 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.71002 0.65268 0.65112 0.18248  -0.00533 -0.01907 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.51827 0.64045 0.39587 0.11869  0.04472  -0.02899 80  PRO A N   
640  C CA  . PRO A 80  ? 0.50443 0.67878 0.40034 0.14050  0.03654  -0.03107 80  PRO A CA  
641  C C   . PRO A 80  ? 0.52755 0.73759 0.43123 0.16738  0.02513  -0.02833 80  PRO A C   
642  O O   . PRO A 80  ? 0.50590 0.76652 0.41982 0.19604  0.02786  -0.02126 80  PRO A O   
643  C CB  . PRO A 80  ? 0.52025 0.67201 0.38715 0.14135  0.05411  -0.02584 80  PRO A CB  
644  C CG  . PRO A 80  ? 0.52990 0.66446 0.37775 0.13911  0.07580  -0.03369 80  PRO A CG  
645  C CD  . PRO A 80  ? 0.52303 0.64809 0.37641 0.12366  0.07361  -0.03512 80  PRO A CD  
646  N N   . ALA A 81  ? 0.55184 0.75557 0.47099 0.14850  -0.00037 -0.03161 81  ALA A N   
647  C CA  . ALA A 81  ? 0.56475 0.75823 0.49980 0.11941  -0.02304 -0.03714 81  ALA A CA  
648  C C   . ALA A 81  ? 0.56333 0.76264 0.51734 0.12511  -0.01148 -0.04926 81  ALA A C   
649  O O   . ALA A 81  ? 0.58690 0.78940 0.53941 0.12744  -0.03683 -0.03941 81  ALA A O   
650  C CB  . ALA A 81  ? 0.56957 0.76778 0.50799 0.08485  -0.04443 -0.02934 81  ALA A CB  
651  N N   . GLU A 82  ? 0.53229 0.74090 0.51061 0.09533  0.04034  -0.04841 82  GLU A N   
652  C CA  . GLU A 82  ? 0.51498 0.75070 0.51469 0.04942  0.05459  -0.06668 82  GLU A CA  
653  C C   . GLU A 82  ? 0.56337 0.71445 0.48544 0.00350  0.06001  -0.10085 82  GLU A C   
654  O O   . GLU A 82  ? 0.61353 0.69744 0.48127 -0.02718 0.05141  -0.13983 82  GLU A O   
655  C CB  . GLU A 82  ? 0.52379 0.83860 0.54838 0.05027  0.06071  -0.03115 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.55958 0.92845 0.58021 0.04105  0.03977  -0.00065 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.54707 1.00404 0.59931 0.01113  0.00754  0.01567  82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.49322 1.02228 0.59801 0.00441  -0.01724 0.02950  82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.58999 1.03502 0.61089 -0.02199 -0.01790 0.02326  82  GLU A OE2 
660  N N   . ALA A 83  ? 0.54262 0.71587 0.46899 -0.00363 0.09213  -0.08314 83  ALA A N   
661  C CA  . ALA A 83  ? 0.56718 0.72127 0.46391 -0.00664 0.08261  -0.07093 83  ALA A CA  
662  C C   . ALA A 83  ? 0.58812 0.72347 0.45210 0.02103  0.09279  -0.07236 83  ALA A C   
663  O O   . ALA A 83  ? 0.52368 0.73658 0.43269 0.04522  0.10762  -0.09042 83  ALA A O   
664  C CB  . ALA A 83  ? 0.56447 0.73322 0.47909 0.00566  0.06395  -0.06895 83  ALA A CB  
665  N N   . ASP A 84  ? 0.62108 0.72770 0.47949 0.01627  0.09025  -0.06350 84  ASP A N   
666  C CA  . ASP A 84  ? 0.63215 0.74855 0.51554 -0.00107 0.07585  -0.05604 84  ASP A CA  
667  C C   . ASP A 84  ? 0.58733 0.72864 0.49158 0.01558  0.06348  -0.10998 84  ASP A C   
668  O O   . ASP A 84  ? 0.55456 0.75223 0.48212 0.03020  0.07733  -0.15493 84  ASP A O   
669  C CB  . ASP A 84  ? 0.75628 0.80241 0.58728 -0.01121 0.06218  0.00212  84  ASP A CB  
670  C CG  . ASP A 84  ? 0.87164 0.86537 0.66895 -0.00845 0.06089  0.05683  84  ASP A CG  
671  O OD1 . ASP A 84  ? 0.88428 0.89463 0.69518 -0.01515 0.08652  0.08866  84  ASP A OD1 
672  O OD2 . ASP A 84  ? 0.93857 0.87339 0.71037 0.00728  0.04639  0.08004  84  ASP A OD2 
673  N N   . LYS A 85  ? 0.56048 0.68475 0.48060 0.02016  0.04743  -0.10732 85  LYS A N   
674  C CA  . LYS A 85  ? 0.53411 0.63226 0.48809 -0.02325 0.04757  -0.11215 85  LYS A CA  
675  C C   . LYS A 85  ? 0.52001 0.59984 0.50206 -0.08480 0.07730  -0.10762 85  LYS A C   
676  O O   . LYS A 85  ? 0.51878 0.56775 0.50650 -0.16730 0.09846  -0.12922 85  LYS A O   
677  C CB  . LYS A 85  ? 0.53131 0.61163 0.48705 0.00348  0.01367  -0.11564 85  LYS A CB  
678  N N   . LEU A 86  ? 0.49061 0.59522 0.49802 -0.04922 0.07678  -0.08870 86  LEU A N   
679  C CA  . LEU A 86  ? 0.50029 0.57456 0.46459 -0.01840 0.06075  -0.08063 86  LEU A CA  
680  C C   . LEU A 86  ? 0.51445 0.60895 0.47568 0.00823  0.05955  -0.09766 86  LEU A C   
681  O O   . LEU A 86  ? 0.55518 0.62583 0.47871 0.04708  0.04128  -0.09693 86  LEU A O   
682  C CB  . LEU A 86  ? 0.52366 0.52732 0.42268 -0.01483 0.03373  -0.06715 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.57561 0.51467 0.39634 -0.04947 0.01268  -0.02771 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.55778 0.53939 0.39405 -0.07028 0.03812  -0.00518 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.60348 0.48782 0.37852 -0.04091 -0.01086 -0.02812 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.51003 0.62404 0.48846 0.00718  0.09153  -0.10663 87  VAL A N   
687  C CA  . VAL A 87  ? 0.51185 0.62957 0.50840 0.02535  0.12171  -0.10711 87  VAL A CA  
688  C C   . VAL A 87  ? 0.57853 0.63673 0.54754 0.04944  0.13857  -0.10935 87  VAL A C   
689  O O   . VAL A 87  ? 0.60096 0.61206 0.55424 0.06324  0.11151  -0.11877 87  VAL A O   
690  C CB  . VAL A 87  ? 0.45515 0.62611 0.49191 0.02907  0.12255  -0.11165 87  VAL A CB  
691  C CG1 . VAL A 87  ? 0.43294 0.60876 0.46820 0.08076  0.10946  -0.12133 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.44864 0.64471 0.50660 0.00364  0.11930  -0.10166 87  VAL A CG2 
693  N N   . LYS A 88  ? 0.60795 0.66557 0.57283 0.05644  0.17959  -0.09864 88  LYS A N   
694  C CA  . LYS A 88  ? 0.63608 0.69377 0.59550 0.06227  0.18698  -0.07623 88  LYS A CA  
695  C C   . LYS A 88  ? 0.66228 0.68899 0.60264 0.07866  0.20493  -0.09518 88  LYS A C   
696  O O   . LYS A 88  ? 0.69860 0.68205 0.62049 0.10680  0.21358  -0.13731 88  LYS A O   
697  C CB  . LYS A 88  ? 0.66038 0.71776 0.60624 0.05956  0.16999  -0.03718 88  LYS A CB  
698  C CG  . LYS A 88  ? 0.71453 0.72807 0.61282 0.07017  0.14171  0.00163  88  LYS A CG  
699  C CD  . LYS A 88  ? 0.73958 0.73588 0.60913 0.07689  0.08334  0.04785  88  LYS A CD  
700  C CE  . LYS A 88  ? 0.75071 0.75246 0.60851 0.06514  0.04491  0.08065  88  LYS A CE  
701  N NZ  . LYS A 88  ? 0.77392 0.77430 0.61181 0.05440  0.02947  0.11757  88  LYS A NZ  
702  N N   . LEU A 89  ? 0.67534 0.69358 0.58238 0.07723  0.17063  -0.08749 89  LEU A N   
703  C CA  . LEU A 89  ? 0.68788 0.69647 0.57003 0.07600  0.12288  -0.08338 89  LEU A CA  
704  C C   . LEU A 89  ? 0.70424 0.67136 0.56861 0.05501  0.13339  -0.09490 89  LEU A C   
705  O O   . LEU A 89  ? 0.68241 0.60939 0.54945 0.06049  0.13750  -0.12178 89  LEU A O   
706  C CB  . LEU A 89  ? 0.62951 0.72020 0.57372 0.08461  0.09626  -0.06568 89  LEU A CB  
707  C CG  . LEU A 89  ? 0.62394 0.74090 0.59488 0.09298  0.05653  -0.04267 89  LEU A CG  
708  C CD1 . LEU A 89  ? 0.62309 0.74417 0.60087 0.12708  0.03487  -0.03824 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 0.63606 0.73865 0.60311 0.05672  0.04002  -0.02873 89  LEU A CD2 
710  N N   . LEU A 90  ? 0.69101 0.70009 0.59199 0.01626  0.15404  -0.06673 90  LEU A N   
711  C CA  . LEU A 90  ? 0.68837 0.71149 0.60958 -0.00728 0.18190  -0.03605 90  LEU A CA  
712  C C   . LEU A 90  ? 0.74517 0.70484 0.64565 0.00174  0.20629  -0.00959 90  LEU A C   
713  O O   . LEU A 90  ? 0.74403 0.71197 0.63408 -0.01403 0.20517  0.00246  90  LEU A O   
714  C CB  . LEU A 90  ? 0.69081 0.75001 0.59563 -0.05180 0.17007  -0.02501 90  LEU A CB  
715  C CG  . LEU A 90  ? 0.70023 0.78415 0.58730 -0.09387 0.16075  -0.01820 90  LEU A CG  
716  C CD1 . LEU A 90  ? 0.68786 0.79660 0.59172 -0.10051 0.17675  -0.00999 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 0.69328 0.78837 0.57662 -0.12076 0.14206  -0.02180 90  LEU A CD2 
718  N N   . ALA A 91  ? 0.78602 0.70600 0.68630 0.02194  0.21403  -0.00901 91  ALA A N   
719  C CA  . ALA A 91  ? 0.85226 0.72443 0.73021 0.01596  0.21978  -0.02114 91  ALA A CA  
720  C C   . ALA A 91  ? 0.88081 0.75161 0.76908 0.01200  0.22312  -0.04620 91  ALA A C   
721  O O   . ALA A 91  ? 0.90676 0.75335 0.78204 -0.01194 0.21507  -0.04290 91  ALA A O   
722  C CB  . ALA A 91  ? 0.86579 0.72452 0.73709 0.02719  0.19825  -0.01502 91  ALA A CB  
723  N N   . LYS A 92  ? 0.86697 0.78178 0.79166 0.04655  0.22627  -0.07171 92  LYS A N   
724  C CA  . LYS A 92  ? 0.88683 0.82219 0.83416 0.07399  0.20004  -0.08616 92  LYS A CA  
725  C C   . LYS A 92  ? 0.94827 0.81858 0.86742 0.08078  0.17496  -0.07781 92  LYS A C   
726  O O   . LYS A 92  ? 0.97501 0.81681 0.87891 0.07665  0.18632  -0.08006 92  LYS A O   
727  C CB  . LYS A 92  ? 0.86449 0.87990 0.85166 0.07520  0.18495  -0.09339 92  LYS A CB  
728  C CG  . LYS A 92  ? 0.87778 0.94550 0.86923 0.06326  0.17822  -0.09214 92  LYS A CG  
729  C CD  . LYS A 92  ? 0.88192 0.99369 0.87820 0.06214  0.17329  -0.08960 92  LYS A CD  
730  C CE  . LYS A 92  ? 0.88091 1.02463 0.88390 0.06027  0.16356  -0.08627 92  LYS A CE  
731  N NZ  . LYS A 92  ? 0.91313 1.04270 0.88778 0.05844  0.14869  -0.08213 92  LYS A NZ  
732  N N   . GLY A 93  ? 0.96620 0.84484 0.89037 0.06363  0.14020  -0.07701 93  GLY A N   
733  C CA  . GLY A 93  ? 0.96651 0.86883 0.91035 0.02884  0.12420  -0.09502 93  GLY A CA  
734  C C   . GLY A 93  ? 0.99245 0.90286 0.93248 -0.00031 0.11737  -0.11235 93  GLY A C   
735  O O   . GLY A 93  ? 1.02125 0.90249 0.92666 -0.01595 0.09959  -0.13491 93  GLY A O   
736  N N   . GLU A 94  ? 1.00993 0.95277 0.96030 -0.01052 0.13472  -0.10315 94  GLU A N   
737  C CA  . GLU A 94  ? 1.04089 1.00503 0.98723 -0.02355 0.13063  -0.09403 94  GLU A CA  
738  C C   . GLU A 94  ? 1.05650 1.03745 1.00943 -0.05169 0.12378  -0.08689 94  GLU A C   
739  O O   . GLU A 94  ? 1.06271 1.10640 1.05419 -0.05809 0.12348  -0.08178 94  GLU A O   
740  C CB  . GLU A 94  ? 1.03251 1.00882 0.99082 -0.03548 0.12450  -0.09397 94  GLU A CB  
741  N N   . TYR A 95  ? 1.01835 0.97771 0.96696 -0.08594 0.11248  -0.08557 95  TYR A N   
742  C CA  . TYR A 95  ? 0.94877 0.89589 0.91338 -0.08065 0.08888  -0.08095 95  TYR A CA  
743  C C   . TYR A 95  ? 0.93543 0.86792 0.87547 -0.08088 0.07023  -0.07856 95  TYR A C   
744  O O   . TYR A 95  ? 0.98610 0.87798 0.88361 -0.08681 0.07788  -0.07826 95  TYR A O   
745  C CB  . TYR A 95  ? 0.88531 0.84725 0.89529 -0.07367 0.07791  -0.07453 95  TYR A CB  
746  C CG  . TYR A 95  ? 0.83267 0.80128 0.87524 -0.08018 0.04082  -0.06820 95  TYR A CG  
747  C CD1 . TYR A 95  ? 0.80517 0.77079 0.86183 -0.09349 0.00897  -0.07018 95  TYR A CD1 
748  C CD2 . TYR A 95  ? 0.82908 0.79202 0.86945 -0.05001 0.01724  -0.06459 95  TYR A CD2 
749  C CE1 . TYR A 95  ? 0.80573 0.76827 0.85475 -0.07818 -0.01894 -0.07327 95  TYR A CE1 
750  C CE2 . TYR A 95  ? 0.84034 0.78081 0.86295 -0.03293 -0.00186 -0.06999 95  TYR A CE2 
751  C CZ  . TYR A 95  ? 0.83239 0.77857 0.85879 -0.03535 -0.02085 -0.07421 95  TYR A CZ  
752  O OH  . TYR A 95  ? 0.87195 0.79132 0.86266 -0.00814 -0.01818 -0.07655 95  TYR A OH  
753  N N   . GLN A 96  ? 0.86667 0.83095 0.82579 -0.07342 0.03589  -0.07684 96  GLN A N   
754  C CA  . GLN A 96  ? 0.82920 0.79901 0.77596 -0.06542 0.01079  -0.07310 96  GLN A CA  
755  C C   . GLN A 96  ? 0.79073 0.75908 0.73242 -0.06937 0.00568  -0.10110 96  GLN A C   
756  O O   . GLN A 96  ? 0.83355 0.76451 0.73614 -0.10478 -0.02438 -0.12119 96  GLN A O   
757  C CB  . GLN A 96  ? 0.82902 0.79504 0.77532 -0.06086 -0.00723 -0.03464 96  GLN A CB  
758  C CG  . GLN A 96  ? 0.82479 0.77304 0.77847 -0.05298 -0.02023 0.00123  96  GLN A CG  
759  C CD  . GLN A 96  ? 0.83386 0.75544 0.78210 -0.03832 -0.02904 0.02623  96  GLN A CD  
760  O OE1 . GLN A 96  ? 0.83388 0.74660 0.78285 -0.02045 -0.02412 0.03274  96  GLN A OE1 
761  N NE2 . GLN A 96  ? 0.84675 0.75355 0.78351 -0.03687 -0.03813 0.03827  96  GLN A NE2 
762  N N   . LYS A 97  ? 0.70290 0.71117 0.67969 -0.03511 0.02471  -0.11309 97  LYS A N   
763  C CA  . LYS A 97  ? 0.65302 0.66730 0.63550 -0.01726 0.04148  -0.11836 97  LYS A CA  
764  C C   . LYS A 97  ? 0.64569 0.65118 0.55574 -0.06169 0.04978  -0.10572 97  LYS A C   
765  O O   . LYS A 97  ? 0.66045 0.64593 0.54910 -0.08870 0.06756  -0.08582 97  LYS A O   
766  C CB  . LYS A 97  ? 0.64396 0.64903 0.68085 0.02890  0.05432  -0.11783 97  LYS A CB  
767  C CG  . LYS A 97  ? 0.65390 0.64586 0.72349 0.05019  0.05343  -0.10655 97  LYS A CG  
768  C CD  . LYS A 97  ? 0.68055 0.64667 0.76281 0.06645  0.04954  -0.08953 97  LYS A CD  
769  C CE  . LYS A 97  ? 0.69861 0.65097 0.78660 0.09292  0.04868  -0.07124 97  LYS A CE  
770  N NZ  . LYS A 97  ? 0.71692 0.65152 0.80213 0.11856  0.04505  -0.05991 97  LYS A NZ  
771  N N   . VAL A 98  ? 0.61479 0.62064 0.49344 -0.05701 0.03708  -0.12361 98  VAL A N   
772  C CA  . VAL A 98  ? 0.57836 0.59567 0.44804 -0.03544 0.00176  -0.11611 98  VAL A CA  
773  C C   . VAL A 98  ? 0.54728 0.55191 0.38963 -0.01337 0.00411  -0.09093 98  VAL A C   
774  O O   . VAL A 98  ? 0.54105 0.56283 0.34521 -0.04095 0.01411  -0.05602 98  VAL A O   
775  C CB  . VAL A 98  ? 0.61228 0.60347 0.46191 -0.00014 -0.05288 -0.13303 98  VAL A CB  
776  C CG1 . VAL A 98  ? 0.66827 0.61175 0.48015 0.02117  -0.07311 -0.13715 98  VAL A CG1 
777  C CG2 . VAL A 98  ? 0.63455 0.61747 0.46453 0.00786  -0.07406 -0.13929 98  VAL A CG2 
778  N N   . SER A 99  ? 0.50448 0.48776 0.39843 -0.01526 0.00942  -0.08287 99  SER A N   
779  C CA  . SER A 99  ? 0.47495 0.45563 0.41703 -0.02681 -0.00140 -0.07479 99  SER A CA  
780  C C   . SER A 99  ? 0.40871 0.46691 0.37029 -0.01809 0.00631  -0.07312 99  SER A C   
781  O O   . SER A 99  ? 0.39803 0.50408 0.37701 -0.02163 0.00330  -0.07829 99  SER A O   
782  C CB  . SER A 99  ? 0.56146 0.45628 0.48485 -0.03342 -0.00608 -0.08290 99  SER A CB  
783  O OG  . SER A 99  ? 0.63812 0.48875 0.54554 -0.03288 -0.00413 -0.04527 99  SER A OG  
784  N N   . TYR A 100 ? 0.41286 0.45796 0.32751 0.02854  0.00838  -0.07543 100 TYR A N   
785  C CA  . TYR A 100 ? 0.43119 0.44829 0.29892 0.08722  0.01677  -0.05507 100 TYR A CA  
786  C C   . TYR A 100 ? 0.40479 0.43965 0.28806 0.05255  0.02716  -0.02475 100 TYR A C   
787  O O   . TYR A 100 ? 0.36870 0.41162 0.28068 0.01608  0.02315  0.01111  100 TYR A O   
788  C CB  . TYR A 100 ? 0.49633 0.45605 0.28769 0.14828  -0.01586 -0.04611 100 TYR A CB  
789  C CG  . TYR A 100 ? 0.55312 0.49733 0.28487 0.19128  -0.05715 -0.06768 100 TYR A CG  
790  C CD1 . TYR A 100 ? 0.62559 0.52638 0.29586 0.23401  -0.04126 -0.06958 100 TYR A CD1 
791  C CD2 . TYR A 100 ? 0.59822 0.50187 0.29011 0.20202  -0.09996 -0.04905 100 TYR A CD2 
792  C CE1 . TYR A 100 ? 0.66864 0.54777 0.29824 0.27048  -0.04680 -0.06205 100 TYR A CE1 
793  C CE2 . TYR A 100 ? 0.67498 0.52758 0.30330 0.21750  -0.09222 -0.04816 100 TYR A CE2 
794  C CZ  . TYR A 100 ? 0.71043 0.57246 0.31390 0.26705  -0.07329 -0.05433 100 TYR A CZ  
795  O OH  . TYR A 100 ? 0.75229 0.62041 0.35230 0.30310  -0.08532 -0.05053 100 TYR A OH  
796  N N   . PRO A 101 ? 0.38309 0.47150 0.28241 0.01764  0.02375  -0.02074 101 PRO A N   
797  C CA  . PRO A 101 ? 0.34764 0.46206 0.26797 -0.02797 0.00631  -0.02467 101 PRO A CA  
798  C C   . PRO A 101 ? 0.31818 0.45269 0.26213 0.00618  0.00926  -0.02899 101 PRO A C   
799  O O   . PRO A 101 ? 0.33693 0.44616 0.28002 -0.00789 0.00303  -0.02187 101 PRO A O   
800  C CB  . PRO A 101 ? 0.33244 0.46981 0.28379 -0.04304 0.00927  -0.04520 101 PRO A CB  
801  C CG  . PRO A 101 ? 0.31137 0.48657 0.28002 -0.02156 0.01750  -0.03472 101 PRO A CG  
802  C CD  . PRO A 101 ? 0.32374 0.49988 0.27777 0.01089  0.03993  -0.02324 101 PRO A CD  
803  N N   . LEU A 102 ? 0.30587 0.43988 0.25386 0.05954  0.02838  -0.03650 102 LEU A N   
804  C CA  . LEU A 102 ? 0.32016 0.43117 0.24713 0.06802  0.01618  -0.03679 102 LEU A CA  
805  C C   . LEU A 102 ? 0.31636 0.46338 0.23561 0.05956  -0.00488 -0.03315 102 LEU A C   
806  O O   . LEU A 102 ? 0.34434 0.47887 0.23689 0.05453  0.00774  -0.01002 102 LEU A O   
807  C CB  . LEU A 102 ? 0.31539 0.41349 0.25180 0.08283  0.05923  -0.02951 102 LEU A CB  
808  C CG  . LEU A 102 ? 0.32407 0.41465 0.24143 0.10715  0.06266  -0.00878 102 LEU A CG  
809  C CD1 . LEU A 102 ? 0.30371 0.42624 0.24905 0.13108  0.06636  0.02068  102 LEU A CD1 
810  C CD2 . LEU A 102 ? 0.33981 0.39865 0.26002 0.08988  0.01315  0.00119  102 LEU A CD2 
811  N N   . LEU A 103 ? 0.27277 0.46624 0.22770 0.08675  -0.02756 -0.04362 103 LEU A N   
812  C CA  . LEU A 103 ? 0.29718 0.45688 0.22385 0.08913  -0.02075 -0.03374 103 LEU A CA  
813  C C   . LEU A 103 ? 0.33952 0.50928 0.23990 0.09498  -0.02090 0.00318  103 LEU A C   
814  O O   . LEU A 103 ? 0.34038 0.54002 0.25080 0.06761  0.01203  0.04192  103 LEU A O   
815  C CB  . LEU A 103 ? 0.33514 0.41426 0.21510 0.07299  -0.00608 -0.02946 103 LEU A CB  
816  C CG  . LEU A 103 ? 0.36747 0.37450 0.21557 0.07434  -0.01417 -0.00246 103 LEU A CG  
817  C CD1 . LEU A 103 ? 0.38333 0.37840 0.20755 0.06978  -0.00548 0.02461  103 LEU A CD1 
818  C CD2 . LEU A 103 ? 0.35805 0.36429 0.21860 0.07295  -0.04266 -0.00483 103 LEU A CD2 
819  N N   . LYS A 104 ? 0.34760 0.50119 0.26046 0.09286  -0.02492 0.02659  104 LYS A N   
820  C CA  . LYS A 104 ? 0.32949 0.49843 0.27836 0.09778  -0.03607 0.02786  104 LYS A CA  
821  C C   . LYS A 104 ? 0.29703 0.53285 0.29241 0.04824  -0.03479 -0.01515 104 LYS A C   
822  O O   . LYS A 104 ? 0.27592 0.55812 0.31157 0.05311  -0.00523 -0.03213 104 LYS A O   
823  C CB  . LYS A 104 ? 0.37218 0.46450 0.29684 0.12715  -0.04788 0.05590  104 LYS A CB  
824  C CG  . LYS A 104 ? 0.42889 0.44321 0.30473 0.13570  -0.08255 0.06956  104 LYS A CG  
825  C CD  . LYS A 104 ? 0.47868 0.41537 0.33256 0.11964  -0.12622 0.07032  104 LYS A CD  
826  C CE  . LYS A 104 ? 0.55495 0.43713 0.36619 0.09284  -0.13004 0.06183  104 LYS A CE  
827  N NZ  . LYS A 104 ? 0.61469 0.48601 0.40951 0.07029  -0.12874 0.03392  104 LYS A NZ  
828  N N   . THR A 105 ? 0.29376 0.53719 0.29332 0.06833  -0.04444 -0.03212 105 THR A N   
829  C CA  . THR A 105 ? 0.32722 0.54183 0.29978 0.11424  -0.04877 -0.01482 105 THR A CA  
830  C C   . THR A 105 ? 0.32833 0.53756 0.33424 0.15555  -0.04271 -0.02655 105 THR A C   
831  O O   . THR A 105 ? 0.33529 0.56047 0.36492 0.17205  -0.03465 -0.01702 105 THR A O   
832  C CB  . THR A 105 ? 0.36090 0.56296 0.29697 0.08896  -0.06564 0.02540  105 THR A CB  
833  O OG1 . THR A 105 ? 0.41058 0.58365 0.29844 0.08507  -0.05788 0.07487  105 THR A OG1 
834  C CG2 . THR A 105 ? 0.34504 0.58528 0.28734 0.08031  -0.06059 0.00812  105 THR A CG2 
835  N N   . THR A 106 ? 0.32652 0.49908 0.35361 0.15953  -0.05337 -0.02108 106 THR A N   
836  C CA  . THR A 106 ? 0.34393 0.50270 0.35309 0.13677  -0.05869 -0.00609 106 THR A CA  
837  C C   . THR A 106 ? 0.33302 0.55586 0.35822 0.10378  -0.02753 0.01756  106 THR A C   
838  O O   . THR A 106 ? 0.33615 0.57479 0.35740 0.07898  -0.00999 -0.00248 106 THR A O   
839  C CB  . THR A 106 ? 0.37668 0.50765 0.36433 0.15427  -0.08363 -0.02802 106 THR A CB  
840  O OG1 . THR A 106 ? 0.41982 0.54694 0.39708 0.16786  -0.06983 -0.02906 106 THR A OG1 
841  C CG2 . THR A 106 ? 0.36336 0.50629 0.34982 0.15275  -0.08863 -0.02932 106 THR A CG2 
842  N N   . VAL A 107 ? 0.32283 0.58936 0.37658 0.09003  0.00302  0.05200  107 VAL A N   
843  C CA  . VAL A 107 ? 0.34587 0.61406 0.40205 0.11253  -0.03661 0.07033  107 VAL A CA  
844  C C   . VAL A 107 ? 0.33110 0.63184 0.42437 0.12733  -0.04173 0.07489  107 VAL A C   
845  O O   . VAL A 107 ? 0.33405 0.63471 0.42379 0.15021  -0.02024 0.05346  107 VAL A O   
846  C CB  . VAL A 107 ? 0.36539 0.59274 0.40628 0.10974  -0.08039 0.06270  107 VAL A CB  
847  C CG1 . VAL A 107 ? 0.34564 0.57328 0.41692 0.09591  -0.11670 0.02553  107 VAL A CG1 
848  C CG2 . VAL A 107 ? 0.40537 0.59740 0.40089 0.11878  -0.10489 0.07297  107 VAL A CG2 
849  N N   . LYS A 108 ? 0.32486 0.63090 0.44549 0.11753  -0.06192 0.09795  108 LYS A N   
850  C CA  . LYS A 108 ? 0.40793 0.66685 0.47076 0.15713  -0.09756 0.12650  108 LYS A CA  
851  C C   . LYS A 108 ? 0.51290 0.73445 0.53763 0.14403  -0.12862 0.12045  108 LYS A C   
852  O O   . LYS A 108 ? 0.49007 0.76721 0.55730 0.16650  -0.17517 0.13872  108 LYS A O   
853  C CB  . LYS A 108 ? 0.40050 0.66159 0.45221 0.21104  -0.06539 0.14353  108 LYS A CB  
854  N N   . TYR A 109 ? 0.54118 0.78017 0.57712 0.11194  -0.10090 0.10222  109 TYR A N   
855  C CA  . TYR A 109 ? 0.62932 0.84445 0.61254 0.02440  -0.05127 0.08385  109 TYR A CA  
856  C C   . TYR A 109 ? 0.70466 0.96421 0.63706 0.00299  -0.03493 0.09676  109 TYR A C   
857  O O   . TYR A 109 ? 0.76021 1.02892 0.64244 -0.00913 -0.01987 0.13346  109 TYR A O   
858  C CB  . TYR A 109 ? 0.55834 0.77701 0.62807 -0.02569 -0.03978 0.07185  109 TYR A CB  
859  C CG  . TYR A 109 ? 0.54104 0.71554 0.65391 -0.04037 -0.07620 0.06205  109 TYR A CG  
860  C CD1 . TYR A 109 ? 0.54016 0.69788 0.66893 -0.05059 -0.08247 0.06727  109 TYR A CD1 
861  C CD2 . TYR A 109 ? 0.53849 0.69013 0.66367 -0.02583 -0.10060 0.03875  109 TYR A CD2 
862  C CE1 . TYR A 109 ? 0.57352 0.69149 0.67806 -0.06029 -0.07887 0.04544  109 TYR A CE1 
863  C CE2 . TYR A 109 ? 0.60533 0.69293 0.67987 -0.04404 -0.07936 0.01694  109 TYR A CE2 
864  C CZ  . TYR A 109 ? 0.65277 0.69914 0.68281 -0.06244 -0.07305 0.01432  109 TYR A CZ  
865  O OH  . TYR A 109 ? 0.75331 0.70856 0.68089 -0.06275 -0.07272 -0.00253 109 TYR A OH  
866  N N   . GLY A 110 ? 0.71233 0.99853 0.64707 0.02544  -0.03026 0.06463  110 GLY A N   
867  C CA  . GLY A 110 ? 0.66053 1.01847 0.64345 0.04542  -0.06042 0.04159  110 GLY A CA  
868  C C   . GLY A 110 ? 0.64226 1.04090 0.64485 0.03738  -0.06227 0.02900  110 GLY A C   
869  O O   . GLY A 110 ? 0.58933 1.04934 0.63997 0.05565  -0.08526 0.02713  110 GLY A O   
870  N N   . LYS A 114 ? 0.77447 0.79851 0.80891 0.28272  -0.07714 0.00664  114 LYS A N   
871  C CA  . LYS A 114 ? 0.75711 0.79497 0.79180 0.31274  -0.07911 0.02567  114 LYS A CA  
872  C C   . LYS A 114 ? 0.75160 0.77780 0.76274 0.35679  -0.06235 0.04653  114 LYS A C   
873  O O   . LYS A 114 ? 0.75943 0.76554 0.76786 0.38529  -0.01056 0.06663  114 LYS A O   
874  C CB  . LYS A 114 ? 0.74334 0.77894 0.80095 0.29150  -0.08667 0.02474  114 LYS A CB  
875  C CG  . LYS A 114 ? 0.78909 0.74559 0.81762 0.27637  -0.09427 0.02236  114 LYS A CG  
876  C CD  . LYS A 114 ? 0.83143 0.71707 0.82946 0.24264  -0.09181 0.00870  114 LYS A CD  
877  C CE  . LYS A 114 ? 0.86170 0.69697 0.83228 0.21066  -0.08183 -0.02470 114 LYS A CE  
878  N NZ  . LYS A 114 ? 0.90347 0.69902 0.83108 0.18641  -0.07806 -0.04779 114 LYS A NZ  
879  N N   . GLU A 115 ? 0.70224 0.74328 0.71708 0.35235  -0.09228 0.03992  115 GLU A N   
880  C CA  . GLU A 115 ? 0.66713 0.71734 0.68297 0.27411  -0.08448 0.05960  115 GLU A CA  
881  C C   . GLU A 115 ? 0.53730 0.70030 0.63635 0.24765  -0.10192 0.05322  115 GLU A C   
882  O O   . GLU A 115 ? 0.62380 0.69164 0.64101 0.24036  -0.14702 0.04070  115 GLU A O   
883  C CB  . GLU A 115 ? 0.76214 0.71747 0.71817 0.25572  -0.06161 0.10435  115 GLU A CB  
884  C CG  . GLU A 115 ? 0.83863 0.72394 0.75309 0.29207  -0.05111 0.14628  115 GLU A CG  
885  C CD  . GLU A 115 ? 0.88737 0.73644 0.78484 0.32634  -0.04711 0.16627  115 GLU A CD  
886  O OE1 . GLU A 115 ? 0.91482 0.73809 0.78371 0.29414  -0.05528 0.16560  115 GLU A OE1 
887  O OE2 . GLU A 115 ? 0.88618 0.75063 0.80813 0.36036  -0.02522 0.17788  115 GLU A OE2 
888  N N   . ALA A 116 ? 0.38731 0.69986 0.58772 0.21665  -0.05548 0.05432  116 ALA A N   
889  C CA  . ALA A 116 ? 0.35159 0.69239 0.54028 0.16092  -0.02184 0.03357  116 ALA A CA  
890  C C   . ALA A 116 ? 0.35273 0.67555 0.47599 0.13920  -0.01706 0.01495  116 ALA A C   
891  O O   . ALA A 116 ? 0.31441 0.70279 0.46748 0.10316  -0.01868 0.03395  116 ALA A O   
892  C CB  . ALA A 116 ? 0.35605 0.69103 0.55706 0.13129  -0.01769 0.02595  116 ALA A CB  
893  N N   . THR A 117 ? 0.42095 0.63638 0.43585 0.16523  0.00624  -0.02362 117 THR A N   
894  C CA  . THR A 117 ? 0.49061 0.61814 0.40420 0.18092  -0.01070 -0.02332 117 THR A CA  
895  C C   . THR A 117 ? 0.39139 0.62776 0.39031 0.16831  -0.01081 -0.00182 117 THR A C   
896  O O   . THR A 117 ? 0.33724 0.66054 0.39855 0.15372  -0.00093 -0.01762 117 THR A O   
897  C CB  . THR A 117 ? 0.65136 0.59804 0.39525 0.18380  -0.03854 -0.02313 117 THR A CB  
898  O OG1 . THR A 117 ? 0.76894 0.62486 0.41966 0.18574  -0.04524 -0.01861 117 THR A OG1 
899  C CG2 . THR A 117 ? 0.62233 0.58287 0.36363 0.17119  -0.07759 -0.01961 117 THR A CG2 
900  N N   . TYR A 118 ? 0.36700 0.59672 0.37571 0.15240  -0.02208 0.00924  118 TYR A N   
901  C CA  . TYR A 118 ? 0.27833 0.57997 0.36745 0.09534  -0.01072 -0.00149 118 TYR A CA  
902  C C   . TYR A 118 ? 0.34587 0.56767 0.35450 0.06956  -0.00924 -0.02040 118 TYR A C   
903  O O   . TYR A 118 ? 0.39080 0.60097 0.34156 0.02951  -0.00678 -0.03192 118 TYR A O   
904  C CB  . TYR A 118 ? 0.23335 0.59061 0.39278 0.02656  -0.02135 -0.00427 118 TYR A CB  
905  C CG  . TYR A 118 ? 0.28067 0.63393 0.42908 0.02461  -0.06201 -0.02489 118 TYR A CG  
906  C CD1 . TYR A 118 ? 0.34146 0.64952 0.45037 0.01708  -0.04841 -0.04565 118 TYR A CD1 
907  C CD2 . TYR A 118 ? 0.30080 0.67135 0.43906 0.04040  -0.06528 -0.04818 118 TYR A CD2 
908  C CE1 . TYR A 118 ? 0.37013 0.68994 0.47024 0.03534  -0.03455 -0.04993 118 TYR A CE1 
909  C CE2 . TYR A 118 ? 0.30421 0.69386 0.46195 0.04334  -0.03849 -0.05116 118 TYR A CE2 
910  C CZ  . TYR A 118 ? 0.33355 0.71124 0.47649 0.01709  -0.03183 -0.05452 118 TYR A CZ  
911  O OH  . TYR A 118 ? 0.35371 0.72698 0.48913 -0.01726 -0.01485 -0.06360 118 TYR A OH  
912  N N   . LEU A 119 ? 0.32905 0.52753 0.34659 0.06819  0.02467  -0.02159 119 LEU A N   
913  C CA  . LEU A 119 ? 0.35592 0.53625 0.34461 0.07151  0.02110  -0.03967 119 LEU A CA  
914  C C   . LEU A 119 ? 0.31418 0.51697 0.30598 0.06195  0.01442  -0.02787 119 LEU A C   
915  O O   . LEU A 119 ? 0.31622 0.54642 0.28736 0.09502  0.03310  -0.00835 119 LEU A O   
916  C CB  . LEU A 119 ? 0.41862 0.57228 0.38875 0.06734  0.02962  -0.08347 119 LEU A CB  
917  C CG  . LEU A 119 ? 0.47823 0.62177 0.42535 0.06894  0.04082  -0.10503 119 LEU A CG  
918  C CD1 . LEU A 119 ? 0.49389 0.61919 0.41074 0.05979  0.05462  -0.10898 119 LEU A CD1 
919  C CD2 . LEU A 119 ? 0.52666 0.63772 0.44704 0.09417  0.02770  -0.10942 119 LEU A CD2 
920  N N   . ALA A 120 ? 0.29825 0.47733 0.29135 0.05825  -0.00545 -0.04172 120 ALA A N   
921  C CA  . ALA A 120 ? 0.29866 0.42694 0.29077 0.02905  -0.00568 -0.06241 120 ALA A CA  
922  C C   . ALA A 120 ? 0.26705 0.47053 0.28722 0.03352  0.01491  -0.05178 120 ALA A C   
923  O O   . ALA A 120 ? 0.25997 0.45684 0.29649 0.01976  0.00837  -0.06481 120 ALA A O   
924  C CB  . ALA A 120 ? 0.32455 0.35961 0.29353 -0.00484 -0.01385 -0.08803 120 ALA A CB  
925  N N   . LEU A 121 ? 0.24737 0.47870 0.26277 0.05600  0.00166  -0.01950 121 LEU A N   
926  C CA  . LEU A 121 ? 0.26496 0.44886 0.24053 0.07728  -0.00427 -0.01322 121 LEU A CA  
927  C C   . LEU A 121 ? 0.28744 0.42554 0.24434 0.02462  0.00891  -0.01159 121 LEU A C   
928  O O   . LEU A 121 ? 0.30760 0.42303 0.25052 0.01016  0.00258  -0.00033 121 LEU A O   
929  C CB  . LEU A 121 ? 0.31357 0.45373 0.22653 0.06626  -0.00063 -0.01008 121 LEU A CB  
930  C CG  . LEU A 121 ? 0.35118 0.48909 0.21908 -0.01096 0.00589  -0.03125 121 LEU A CG  
931  C CD1 . LEU A 121 ? 0.26859 0.48348 0.22140 -0.04911 -0.00034 -0.04654 121 LEU A CD1 
932  C CD2 . LEU A 121 ? 0.37038 0.52148 0.21024 -0.01792 0.00643  -0.06410 121 LEU A CD2 
933  N N   . ASN A 122 ? 0.28004 0.38308 0.23091 -0.00440 0.01705  -0.03117 122 ASN A N   
934  C CA  . ASN A 122 ? 0.30365 0.34961 0.22891 -0.00317 0.00622  -0.02108 122 ASN A CA  
935  C C   . ASN A 122 ? 0.26631 0.37920 0.23242 0.00405  -0.00524 -0.00111 122 ASN A C   
936  O O   . ASN A 122 ? 0.27900 0.37494 0.23361 0.00974  0.00936  0.02798  122 ASN A O   
937  C CB  . ASN A 122 ? 0.32997 0.33508 0.24121 0.00931  0.01693  0.00243  122 ASN A CB  
938  C CG  . ASN A 122 ? 0.38341 0.34268 0.25569 0.00509  0.04786  0.02425  122 ASN A CG  
939  O OD1 . ASN A 122 ? 0.40196 0.33863 0.24556 0.04227  0.03856  0.02300  122 ASN A OD1 
940  N ND2 . ASN A 122 ? 0.40124 0.33781 0.27397 0.01202  0.04484  0.03838  122 ASN A ND2 
941  N N   . GLU A 123 ? 0.21435 0.40993 0.22768 0.02531  -0.01957 -0.00505 123 GLU A N   
942  C CA  . GLU A 123 ? 0.20996 0.42687 0.23745 0.01945  -0.01449 -0.03236 123 GLU A CA  
943  C C   . GLU A 123 ? 0.21225 0.44974 0.24565 0.01952  0.02024  -0.03427 123 GLU A C   
944  O O   . GLU A 123 ? 0.23882 0.48664 0.24806 -0.00906 0.04159  -0.00509 123 GLU A O   
945  C CB  . GLU A 123 ? 0.23440 0.42117 0.24875 -0.04287 0.00968  -0.02718 123 GLU A CB  
946  C CG  . GLU A 123 ? 0.25362 0.44824 0.25036 -0.06717 0.00977  -0.02599 123 GLU A CG  
947  C CD  . GLU A 123 ? 0.27230 0.47667 0.27763 -0.03316 0.01089  0.00902  123 GLU A CD  
948  O OE1 . GLU A 123 ? 0.27975 0.42948 0.27383 0.00386  -0.00561 0.01325  123 GLU A OE1 
949  O OE2 . GLU A 123 ? 0.28342 0.53164 0.29724 -0.01654 0.00321  0.02258  123 GLU A OE2 
950  N N   . SER A 124 ? 0.19510 0.42738 0.25198 0.00670  -0.01693 -0.03704 124 SER A N   
951  C CA  . SER A 124 ? 0.21710 0.45338 0.25935 0.02153  -0.02483 -0.03225 124 SER A CA  
952  C C   . SER A 124 ? 0.27301 0.47482 0.27447 -0.01843 -0.01361 -0.04256 124 SER A C   
953  O O   . SER A 124 ? 0.25415 0.50158 0.30883 -0.03577 0.00546  -0.04846 124 SER A O   
954  C CB  . SER A 124 ? 0.22921 0.47346 0.29824 0.06804  -0.04840 -0.01695 124 SER A CB  
955  O OG  . SER A 124 ? 0.24822 0.52300 0.34622 0.09555  -0.03943 -0.01617 124 SER A OG  
956  N N   . THR A 125 ? 0.25207 0.48810 0.26931 0.01764  -0.02337 -0.04435 125 THR A N   
957  C CA  . THR A 125 ? 0.23751 0.50969 0.25983 0.01179  -0.01253 -0.05191 125 THR A CA  
958  C C   . THR A 125 ? 0.20350 0.53380 0.26974 0.03904  0.01313  -0.08812 125 THR A C   
959  O O   . THR A 125 ? 0.20022 0.54794 0.28384 0.04403  -0.01285 -0.09472 125 THR A O   
960  C CB  . THR A 125 ? 0.24272 0.50671 0.25718 -0.04854 0.01831  0.01723  125 THR A CB  
961  O OG1 . THR A 125 ? 0.25983 0.55250 0.28001 -0.06547 0.03405  0.03865  125 THR A OG1 
962  C CG2 . THR A 125 ? 0.30946 0.48201 0.24312 -0.03700 -0.01301 0.04175  125 THR A CG2 
963  N N   . VAL A 126 ? 0.18956 0.54141 0.27053 0.02474  -0.00497 -0.06441 126 VAL A N   
964  C CA  . VAL A 126 ? 0.21053 0.52808 0.28460 0.02245  -0.04734 -0.05949 126 VAL A CA  
965  C C   . VAL A 126 ? 0.20933 0.51909 0.32350 0.03586  -0.02220 -0.05085 126 VAL A C   
966  O O   . VAL A 126 ? 0.22700 0.49056 0.31944 -0.00664 -0.00896 -0.06071 126 VAL A O   
967  C CB  . VAL A 126 ? 0.29146 0.53341 0.27405 -0.02424 -0.06204 -0.04074 126 VAL A CB  
968  C CG1 . VAL A 126 ? 0.42766 0.57217 0.28054 -0.08487 -0.07118 -0.02415 126 VAL A CG1 
969  C CG2 . VAL A 126 ? 0.30939 0.50630 0.25873 -0.07284 -0.08612 -0.04694 126 VAL A CG2 
970  N N   . LYS A 127 ? 0.22889 0.51739 0.36856 0.01325  -0.03230 -0.03433 127 LYS A N   
971  C CA  . LYS A 127 ? 0.26692 0.49545 0.41929 0.00383  -0.06562 -0.01152 127 LYS A CA  
972  C C   . LYS A 127 ? 0.25437 0.50325 0.44510 -0.04006 -0.04864 -0.01806 127 LYS A C   
973  O O   . LYS A 127 ? 0.23561 0.46986 0.43195 -0.03160 -0.04286 -0.04357 127 LYS A O   
974  C CB  . LYS A 127 ? 0.30321 0.48955 0.45114 0.03451  -0.07193 0.05414  127 LYS A CB  
975  C CG  . LYS A 127 ? 0.35494 0.52336 0.49261 0.05165  -0.02705 0.11560  127 LYS A CG  
976  C CD  . LYS A 127 ? 0.47209 0.56541 0.52936 0.02107  0.00284  0.15678  127 LYS A CD  
977  C CE  . LYS A 127 ? 0.54668 0.60221 0.55406 0.06487  0.01324  0.18418  127 LYS A CE  
978  N NZ  . LYS A 127 ? 0.56314 0.61586 0.57254 0.07891  0.01190  0.18350  127 LYS A NZ  
979  N N   . SER A 128 ? 0.25292 0.55783 0.48756 -0.09865 -0.02089 -0.01885 128 SER A N   
980  C CA  . SER A 128 ? 0.32745 0.58165 0.55464 -0.13184 0.02468  -0.02643 128 SER A CA  
981  C C   . SER A 128 ? 0.37899 0.62993 0.58973 -0.13176 0.01008  -0.02407 128 SER A C   
982  O O   . SER A 128 ? 0.41186 0.66978 0.58702 -0.15847 0.00988  0.00744  128 SER A O   
983  C CB  . SER A 128 ? 0.45553 0.58199 0.59674 -0.12978 0.06126  -0.03774 128 SER A CB  
984  O OG  . SER A 128 ? 0.54263 0.61269 0.62788 -0.11454 0.09313  -0.05437 128 SER A OG  
985  N N   . SER A 129 ? 0.44521 0.66316 0.64920 -0.09905 -0.00833 -0.04909 129 SER A N   
986  C CA  . SER A 129 ? 0.53294 0.76211 0.71218 -0.06222 -0.02982 -0.04502 129 SER A CA  
987  C C   . SER A 129 ? 0.62923 0.87769 0.74467 -0.02808 0.01239  -0.04873 129 SER A C   
988  O O   . SER A 129 ? 0.62119 0.97629 0.74931 -0.03433 0.01808  -0.04883 129 SER A O   
989  C CB  . SER A 129 ? 0.57167 0.76922 0.74585 -0.03145 -0.06736 -0.03362 129 SER A CB  
990  O OG  . SER A 129 ? 0.61492 0.81150 0.77507 -0.04200 -0.08867 -0.02588 129 SER A OG  
991  N N   . GLY A 130 ? 0.73649 0.87944 0.76767 -0.00303 0.04421  -0.05398 130 GLY A N   
992  C CA  . GLY A 130 ? 0.81983 0.86845 0.77584 -0.00835 0.05942  -0.05851 130 GLY A CA  
993  C C   . GLY A 130 ? 0.86582 0.86182 0.77244 -0.03575 0.06432  -0.06735 130 GLY A C   
994  O O   . GLY A 130 ? 0.97120 0.85330 0.78644 -0.01140 0.07201  -0.05107 130 GLY A O   
995  N N   . GLY A 131 ? 0.76502 0.84668 0.74434 -0.10384 0.06187  -0.09436 131 GLY A N   
996  C CA  . GLY A 131 ? 0.66509 0.80897 0.71975 -0.12390 0.07020  -0.10540 131 GLY A CA  
997  C C   . GLY A 131 ? 0.59261 0.76004 0.68821 -0.13071 0.07571  -0.10765 131 GLY A C   
998  O O   . GLY A 131 ? 0.59444 0.77441 0.70766 -0.15637 0.10414  -0.10976 131 GLY A O   
999  N N   . PRO A 132 ? 0.52365 0.69275 0.63333 -0.08768 0.05415  -0.10074 132 PRO A N   
1000 C CA  . PRO A 132 ? 0.46811 0.65352 0.59429 -0.03462 0.03621  -0.08383 132 PRO A CA  
1001 C C   . PRO A 132 ? 0.41260 0.62098 0.54322 -0.03027 -0.00056 -0.07145 132 PRO A C   
1002 O O   . PRO A 132 ? 0.44793 0.63773 0.58626 -0.06073 -0.03136 -0.05444 132 PRO A O   
1003 C CB  . PRO A 132 ? 0.49774 0.64991 0.59544 -0.02580 0.03021  -0.09561 132 PRO A CB  
1004 C CG  . PRO A 132 ? 0.52560 0.67711 0.60433 -0.04748 0.03128  -0.10116 132 PRO A CG  
1005 C CD  . PRO A 132 ? 0.54316 0.68821 0.61710 -0.06517 0.04150  -0.10080 132 PRO A CD  
1006 N N   . PHE A 133 ? 0.33946 0.54890 0.43916 -0.05009 -0.00537 -0.08082 133 PHE A N   
1007 C CA  . PHE A 133 ? 0.32017 0.50881 0.37776 -0.04016 -0.00825 -0.04751 133 PHE A CA  
1008 C C   . PHE A 133 ? 0.31285 0.49546 0.35491 0.02896  0.00682  -0.03834 133 PHE A C   
1009 O O   . PHE A 133 ? 0.30213 0.52954 0.35070 0.06368  0.00849  -0.03066 133 PHE A O   
1010 C CB  . PHE A 133 ? 0.30962 0.45610 0.35811 -0.06152 -0.02632 -0.02923 133 PHE A CB  
1011 C CG  . PHE A 133 ? 0.33623 0.41763 0.33549 -0.03513 -0.00911 -0.01739 133 PHE A CG  
1012 C CD1 . PHE A 133 ? 0.33990 0.40652 0.32750 -0.02600 0.03268  -0.01138 133 PHE A CD1 
1013 C CD2 . PHE A 133 ? 0.33118 0.41769 0.32773 0.00010  -0.01929 -0.00518 133 PHE A CD2 
1014 C CE1 . PHE A 133 ? 0.32495 0.42869 0.32043 0.01556  0.03024  -0.00538 133 PHE A CE1 
1015 C CE2 . PHE A 133 ? 0.32685 0.42779 0.32447 0.04511  -0.03131 0.00700  133 PHE A CE2 
1016 C CZ  . PHE A 133 ? 0.32753 0.44233 0.31724 0.04099  -0.00560 -0.00589 133 PHE A CZ  
1017 N N   . VAL A 134 ? 0.33820 0.44674 0.35146 0.04432  0.00067  -0.02703 134 VAL A N   
1018 C CA  . VAL A 134 ? 0.38692 0.41644 0.33542 0.05467  0.00233  -0.00077 134 VAL A CA  
1019 C C   . VAL A 134 ? 0.37064 0.44636 0.34533 0.02882  -0.02650 -0.00742 134 VAL A C   
1020 O O   . VAL A 134 ? 0.36767 0.47048 0.37941 0.01893  -0.04608 -0.01350 134 VAL A O   
1021 C CB  . VAL A 134 ? 0.44060 0.37858 0.31716 0.05131  0.01893  0.02054  134 VAL A CB  
1022 C CG1 . VAL A 134 ? 0.43602 0.38118 0.30651 0.04063  0.04612  0.01345  134 VAL A CG1 
1023 C CG2 . VAL A 134 ? 0.44482 0.36910 0.31884 0.06479  -0.00306 0.02012  134 VAL A CG2 
1024 N N   . VAL A 135 ? 0.31211 0.45409 0.31718 0.01646  -0.02591 0.00237  135 VAL A N   
1025 C CA  . VAL A 135 ? 0.29885 0.46803 0.30698 0.02402  -0.03026 -0.00351 135 VAL A CA  
1026 C C   . VAL A 135 ? 0.32532 0.46701 0.29869 0.06144  -0.00976 -0.00875 135 VAL A C   
1027 O O   . VAL A 135 ? 0.34885 0.48947 0.30105 0.07315  0.01523  -0.00461 135 VAL A O   
1028 C CB  . VAL A 135 ? 0.24112 0.50114 0.30353 0.05222  -0.04362 -0.00466 135 VAL A CB  
1029 C CG1 . VAL A 135 ? 0.29381 0.53437 0.31097 0.10384  -0.04897 -0.00668 135 VAL A CG1 
1030 C CG2 . VAL A 135 ? 0.21685 0.50337 0.31003 0.03160  -0.05479 0.00852  135 VAL A CG2 
1031 N N   . ASP A 136 ? 0.32233 0.44184 0.30145 0.08004  -0.04485 0.00853  136 ASP A N   
1032 C CA  . ASP A 136 ? 0.33592 0.45497 0.30697 0.05518  -0.06145 0.01479  136 ASP A CA  
1033 C C   . ASP A 136 ? 0.29096 0.43786 0.29708 0.06553  -0.04988 0.00086  136 ASP A C   
1034 O O   . ASP A 136 ? 0.30186 0.42975 0.30782 0.07575  -0.04769 0.00416  136 ASP A O   
1035 C CB  . ASP A 136 ? 0.40492 0.49866 0.34077 0.08449  -0.08222 0.03008  136 ASP A CB  
1036 C CG  . ASP A 136 ? 0.49969 0.55277 0.36228 0.09456  -0.11229 0.02783  136 ASP A CG  
1037 O OD1 . ASP A 136 ? 0.58172 0.58061 0.37784 0.09581  -0.10416 0.02109  136 ASP A OD1 
1038 O OD2 . ASP A 136 ? 0.51168 0.56763 0.35848 0.07932  -0.13718 0.01506  136 ASP A OD2 
1039 N N   . VAL A 137 ? 0.27792 0.40181 0.28351 0.03767  -0.03977 -0.01386 137 VAL A N   
1040 C CA  . VAL A 137 ? 0.28538 0.40746 0.28662 0.03878  -0.00806 -0.02428 137 VAL A CA  
1041 C C   . VAL A 137 ? 0.30543 0.41685 0.29522 0.02068  0.00219  0.00473  137 VAL A C   
1042 O O   . VAL A 137 ? 0.30937 0.45274 0.29751 0.03305  0.02023  0.02382  137 VAL A O   
1043 C CB  . VAL A 137 ? 0.26491 0.39589 0.28769 0.01963  -0.01110 -0.03455 137 VAL A CB  
1044 C CG1 . VAL A 137 ? 0.27058 0.37500 0.29310 -0.00136 -0.02522 -0.06155 137 VAL A CG1 
1045 C CG2 . VAL A 137 ? 0.26051 0.43350 0.30651 0.02320  -0.00749 -0.02231 137 VAL A CG2 
1046 N N   . VAL A 138 ? 0.27714 0.42261 0.30351 -0.00467 -0.00999 -0.00139 138 VAL A N   
1047 C CA  . VAL A 138 ? 0.29540 0.41735 0.31237 -0.01781 -0.03204 0.00405  138 VAL A CA  
1048 C C   . VAL A 138 ? 0.30641 0.43505 0.31712 -0.00616 -0.00226 -0.00839 138 VAL A C   
1049 O O   . VAL A 138 ? 0.36719 0.47707 0.32109 -0.01526 0.00898  -0.03667 138 VAL A O   
1050 C CB  . VAL A 138 ? 0.31241 0.42469 0.33348 -0.01886 -0.04855 0.00218  138 VAL A CB  
1051 C CG1 . VAL A 138 ? 0.31564 0.38885 0.36487 0.02610  -0.05831 0.01572  138 VAL A CG1 
1052 C CG2 . VAL A 138 ? 0.28206 0.45001 0.33473 -0.02436 -0.06989 -0.02194 138 VAL A CG2 
1053 N N   . ILE A 139 ? 0.24879 0.41120 0.30596 0.00425  0.02714  0.00751  139 ILE A N   
1054 C CA  . ILE A 139 ? 0.27693 0.39278 0.29819 -0.05215 0.02457  -0.00944 139 ILE A CA  
1055 C C   . ILE A 139 ? 0.35305 0.39303 0.30090 -0.02107 0.02690  -0.01222 139 ILE A C   
1056 O O   . ILE A 139 ? 0.39718 0.40746 0.30915 -0.03260 0.05195  -0.00717 139 ILE A O   
1057 C CB  . ILE A 139 ? 0.29080 0.38875 0.29873 -0.03200 -0.00301 -0.02146 139 ILE A CB  
1058 C CG1 . ILE A 139 ? 0.29025 0.41211 0.30523 -0.03188 -0.00776 -0.03483 139 ILE A CG1 
1059 C CG2 . ILE A 139 ? 0.28962 0.38417 0.29031 -0.04973 -0.01085 -0.00824 139 ILE A CG2 
1060 C CD1 . ILE A 139 ? 0.28622 0.45942 0.31103 -0.00998 0.02196  -0.03378 139 ILE A CD1 
1061 N N   . ASN A 140 ? 0.38027 0.39477 0.28688 -0.02955 0.01520  -0.02010 140 ASN A N   
1062 C CA  . ASN A 140 ? 0.45846 0.42444 0.28150 -0.02132 0.00023  -0.00656 140 ASN A CA  
1063 C C   . ASN A 140 ? 0.52889 0.42671 0.28831 -0.02662 -0.00986 0.02542  140 ASN A C   
1064 O O   . ASN A 140 ? 0.54180 0.45376 0.29700 -0.01909 -0.00244 0.04343  140 ASN A O   
1065 C CB  . ASN A 140 ? 0.43283 0.45476 0.26343 -0.01287 0.00081  -0.01137 140 ASN A CB  
1066 C CG  . ASN A 140 ? 0.44868 0.48763 0.27623 -0.00303 0.01457  -0.00066 140 ASN A CG  
1067 O OD1 . ASN A 140 ? 0.45120 0.49836 0.28492 -0.02207 0.02463  -0.00636 140 ASN A OD1 
1068 N ND2 . ASN A 140 ? 0.42058 0.49800 0.28096 0.01605  0.01347  0.01475  140 ASN A ND2 
1069 N N   . ASP A 141 ? 0.59032 0.41927 0.30469 -0.04048 -0.05413 0.04432  141 ASP A N   
1070 C CA  . ASP A 141 ? 0.66872 0.45385 0.32727 0.01172  -0.09523 0.06635  141 ASP A CA  
1071 C C   . ASP A 141 ? 0.65801 0.48752 0.32698 0.06193  -0.09912 0.05405  141 ASP A C   
1072 O O   . ASP A 141 ? 0.75013 0.54194 0.30768 0.09018  -0.09788 0.04166  141 ASP A O   
1073 C CB  . ASP A 141 ? 0.74237 0.47276 0.37463 0.02138  -0.08303 0.10334  141 ASP A CB  
1074 C CG  . ASP A 141 ? 0.77454 0.50118 0.41563 0.03619  -0.04817 0.12761  141 ASP A CG  
1075 O OD1 . ASP A 141 ? 0.78017 0.53681 0.41307 0.07486  -0.03727 0.12911  141 ASP A OD1 
1076 O OD2 . ASP A 141 ? 0.78473 0.50055 0.44603 0.01404  -0.02833 0.14237  141 ASP A OD2 
1077 N N   . ILE A 142 ? 0.57849 0.44455 0.38358 0.08668  -0.03820 0.05480  142 ILE A N   
1078 C CA  . ILE A 142 ? 0.51972 0.43863 0.45611 0.07803  0.00697  0.03691  142 ILE A CA  
1079 C C   . ILE A 142 ? 0.41275 0.43755 0.37818 0.07437  -0.02273 0.03388  142 ILE A C   
1080 O O   . ILE A 142 ? 0.38573 0.46306 0.36062 0.04987  -0.02939 0.06166  142 ILE A O   
1081 C CB  . ILE A 142 ? 0.61505 0.45031 0.62310 0.07388  0.04344  0.02891  142 ILE A CB  
1082 C CG1 . ILE A 142 ? 0.76526 0.46062 0.71510 0.10692  0.06403  0.03696  142 ILE A CG1 
1083 C CG2 . ILE A 142 ? 0.56674 0.45434 0.67114 0.02185  0.02686  0.02393  142 ILE A CG2 
1084 C CD1 . ILE A 142 ? 0.89121 0.47317 0.75381 0.11624  0.07057  0.06036  142 ILE A CD1 
1085 N N   . HIS A 143 ? 0.39502 0.42870 0.31682 0.06811  -0.02833 0.02009  143 HIS A N   
1086 C CA  . HIS A 143 ? 0.37426 0.42467 0.28785 0.02875  -0.04393 -0.00855 143 HIS A CA  
1087 C C   . HIS A 143 ? 0.38742 0.44517 0.26862 0.03194  -0.00889 0.00974  143 HIS A C   
1088 O O   . HIS A 143 ? 0.42209 0.49981 0.28920 0.04442  -0.00969 0.03260  143 HIS A O   
1089 C CB  . HIS A 143 ? 0.37706 0.43231 0.29873 0.03318  -0.07013 -0.05457 143 HIS A CB  
1090 C CG  . HIS A 143 ? 0.46832 0.43199 0.37553 0.02404  -0.07299 -0.06355 143 HIS A CG  
1091 N ND1 . HIS A 143 ? 0.49026 0.43046 0.39446 0.01100  -0.06877 -0.04932 143 HIS A ND1 
1092 C CD2 . HIS A 143 ? 0.44831 0.42368 0.42261 0.03938  -0.10988 -0.07625 143 HIS A CD2 
1093 C CE1 . HIS A 143 ? 0.38877 0.41152 0.41170 0.01517  -0.10850 -0.05190 143 HIS A CE1 
1094 N NE2 . HIS A 143 ? 0.40603 0.42491 0.42888 0.04457  -0.11750 -0.06280 143 HIS A NE2 
1095 N N   . PHE A 144 ? 0.31190 0.41689 0.23882 0.03372  -0.03545 0.02231  144 PHE A N   
1096 C CA  . PHE A 144 ? 0.29706 0.42480 0.23091 0.06617  -0.03936 0.02255  144 PHE A CA  
1097 C C   . PHE A 144 ? 0.30460 0.43340 0.24250 0.04865  -0.03334 0.00646  144 PHE A C   
1098 O O   . PHE A 144 ? 0.33694 0.43867 0.24894 0.02328  -0.00773 -0.00418 144 PHE A O   
1099 C CB  . PHE A 144 ? 0.29429 0.42756 0.20524 0.09063  -0.01537 0.02583  144 PHE A CB  
1100 C CG  . PHE A 144 ? 0.30291 0.41975 0.21510 0.08326  -0.00147 0.00296  144 PHE A CG  
1101 C CD1 . PHE A 144 ? 0.35677 0.40868 0.22274 0.08562  0.01247  -0.01156 144 PHE A CD1 
1102 C CD2 . PHE A 144 ? 0.30080 0.40522 0.20735 0.06251  -0.01448 0.02903  144 PHE A CD2 
1103 C CE1 . PHE A 144 ? 0.39543 0.43316 0.23206 0.07130  -0.00364 0.00302  144 PHE A CE1 
1104 C CE2 . PHE A 144 ? 0.32787 0.41251 0.22372 0.02460  -0.01060 0.02682  144 PHE A CE2 
1105 C CZ  . PHE A 144 ? 0.40094 0.44197 0.23680 0.02532  0.01770  0.02118  144 PHE A CZ  
1106 N N   . GLU A 145 ? 0.31892 0.41094 0.22613 0.02055  -0.03670 0.02844  145 GLU A N   
1107 C CA  . GLU A 145 ? 0.29523 0.43357 0.22810 0.01152  -0.04762 0.02582  145 GLU A CA  
1108 C C   . GLU A 145 ? 0.29272 0.45764 0.23581 0.00578  -0.04083 0.01490  145 GLU A C   
1109 O O   . GLU A 145 ? 0.35840 0.46757 0.24808 0.03886  -0.04712 -0.00396 145 GLU A O   
1110 C CB  . GLU A 145 ? 0.34004 0.44844 0.22404 0.06911  -0.03559 0.00013  145 GLU A CB  
1111 C CG  . GLU A 145 ? 0.33896 0.48590 0.23544 0.09410  -0.02805 -0.00350 145 GLU A CG  
1112 C CD  . GLU A 145 ? 0.35295 0.52938 0.28557 0.09554  0.03010  0.00196  145 GLU A CD  
1113 O OE1 . GLU A 145 ? 0.37746 0.51636 0.33172 0.08803  0.02298  0.02120  145 GLU A OE1 
1114 O OE2 . GLU A 145 ? 0.32497 0.57168 0.26936 0.09389  0.01280  -0.00656 145 GLU A OE2 
1115 N N   . ARG A 146 ? 0.28083 0.48025 0.22859 0.00218  -0.03379 0.01538  146 ARG A N   
1116 C CA  . ARG A 146 ? 0.26928 0.49194 0.24513 -0.01658 -0.06083 0.02131  146 ARG A CA  
1117 C C   . ARG A 146 ? 0.31982 0.51091 0.25700 0.02366  -0.04034 0.02813  146 ARG A C   
1118 O O   . ARG A 146 ? 0.35861 0.57308 0.28521 0.04527  -0.05223 0.04752  146 ARG A O   
1119 C CB  . ARG A 146 ? 0.31168 0.50553 0.25332 -0.06607 -0.04477 0.00590  146 ARG A CB  
1120 C CG  . ARG A 146 ? 0.28781 0.53254 0.26361 -0.04309 -0.07149 -0.03827 146 ARG A CG  
1121 C CD  . ARG A 146 ? 0.30543 0.57750 0.29150 0.03331  -0.10018 -0.05901 146 ARG A CD  
1122 N NE  . ARG A 146 ? 0.37365 0.59562 0.30742 0.06055  -0.12339 -0.06208 146 ARG A NE  
1123 C CZ  . ARG A 146 ? 0.47004 0.61865 0.34084 0.01903  -0.09908 -0.07887 146 ARG A CZ  
1124 N NH1 . ARG A 146 ? 0.50841 0.61727 0.36088 -0.00665 -0.07665 -0.10008 146 ARG A NH1 
1125 N NH2 . ARG A 146 ? 0.48949 0.63347 0.35891 0.02811  -0.08870 -0.07051 146 ARG A NH2 
1126 N N   . PHE A 147 ? 0.30971 0.46086 0.22618 0.04095  -0.00672 0.01643  147 PHE A N   
1127 C CA  . PHE A 147 ? 0.33761 0.43514 0.23343 0.03706  -0.02837 -0.00209 147 PHE A CA  
1128 C C   . PHE A 147 ? 0.33622 0.42339 0.25094 0.04980  -0.00372 -0.02106 147 PHE A C   
1129 O O   . PHE A 147 ? 0.29752 0.40371 0.28438 0.04723  -0.01207 -0.01952 147 PHE A O   
1130 C CB  . PHE A 147 ? 0.34957 0.39068 0.22803 0.03996  -0.02895 -0.00342 147 PHE A CB  
1131 C CG  . PHE A 147 ? 0.36877 0.35227 0.23738 0.07605  -0.01579 0.00498  147 PHE A CG  
1132 C CD1 . PHE A 147 ? 0.38275 0.35950 0.24510 0.09632  -0.03337 0.00808  147 PHE A CD1 
1133 C CD2 . PHE A 147 ? 0.36665 0.35221 0.24721 0.05176  -0.02752 -0.01226 147 PHE A CD2 
1134 C CE1 . PHE A 147 ? 0.36904 0.37545 0.24299 0.10566  -0.03251 0.02054  147 PHE A CE1 
1135 C CE2 . PHE A 147 ? 0.36436 0.36674 0.22965 0.06063  -0.05128 0.00227  147 PHE A CE2 
1136 C CZ  . PHE A 147 ? 0.36605 0.37766 0.23588 0.08716  -0.02861 0.01272  147 PHE A CZ  
1137 N N   . ARG A 148 ? 0.37709 0.42737 0.23089 0.06006  -0.01010 -0.02142 148 ARG A N   
1138 C CA  . ARG A 148 ? 0.40192 0.45312 0.22867 0.03341  -0.02033 -0.01598 148 ARG A CA  
1139 C C   . ARG A 148 ? 0.35063 0.46631 0.21398 0.01844  -0.02163 0.00943  148 ARG A C   
1140 O O   . ARG A 148 ? 0.35901 0.47769 0.22579 0.02073  0.01287  0.02320  148 ARG A O   
1141 C CB  . ARG A 148 ? 0.48483 0.48197 0.23603 0.05305  -0.00038 -0.01147 148 ARG A CB  
1142 C CG  . ARG A 148 ? 0.54211 0.51738 0.26594 0.06651  -0.01624 -0.02951 148 ARG A CG  
1143 C CD  . ARG A 148 ? 0.60355 0.52891 0.30596 0.12011  -0.04190 -0.05139 148 ARG A CD  
1144 N NE  . ARG A 148 ? 0.69793 0.54301 0.33761 0.16601  -0.08879 -0.05841 148 ARG A NE  
1145 C CZ  . ARG A 148 ? 0.78222 0.58293 0.36687 0.21720  -0.12471 -0.05820 148 ARG A CZ  
1146 N NH1 . ARG A 148 ? 0.80948 0.58932 0.36858 0.22657  -0.12975 -0.05781 148 ARG A NH1 
1147 N NH2 . ARG A 148 ? 0.82023 0.61841 0.39315 0.24104  -0.14964 -0.07209 148 ARG A NH2 
1148 N N   . GLY A 149 ? 0.32421 0.47722 0.22640 -0.01422 -0.00478 0.01379  149 GLY A N   
1149 C CA  . GLY A 149 ? 0.31376 0.49056 0.24927 -0.01960 -0.01279 0.01967  149 GLY A CA  
1150 C C   . GLY A 149 ? 0.24612 0.48897 0.26831 -0.02438 0.00565  0.01826  149 GLY A C   
1151 O O   . GLY A 149 ? 0.27316 0.55984 0.28603 -0.07615 -0.00239 0.02241  149 GLY A O   
1152 N N   . ASP A 150 ? 0.25372 0.41786 0.26944 0.01610  0.00251  -0.01336 150 ASP A N   
1153 C CA  . ASP A 150 ? 0.26535 0.41223 0.28864 0.04688  0.02708  -0.03895 150 ASP A CA  
1154 C C   . ASP A 150 ? 0.26625 0.41750 0.31776 0.00360  -0.00394 -0.04618 150 ASP A C   
1155 O O   . ASP A 150 ? 0.27920 0.45443 0.35408 -0.01323 -0.01723 -0.04137 150 ASP A O   
1156 C CB  . ASP A 150 ? 0.29982 0.45877 0.27138 0.02683  0.01875  -0.01389 150 ASP A CB  
1157 C CG  . ASP A 150 ? 0.33490 0.52891 0.27314 -0.01294 0.03060  -0.02892 150 ASP A CG  
1158 O OD1 . ASP A 150 ? 0.37169 0.54547 0.27534 -0.03703 0.01989  -0.00109 150 ASP A OD1 
1159 O OD2 . ASP A 150 ? 0.34546 0.56821 0.29199 -0.00976 0.06807  -0.04967 150 ASP A OD2 
1160 N N   . GLY A 151 ? 0.24855 0.37245 0.29203 -0.01146 -0.00436 -0.03462 151 GLY A N   
1161 C CA  . GLY A 151 ? 0.22153 0.32934 0.28319 0.01571  -0.02008 -0.04907 151 GLY A CA  
1162 C C   . GLY A 151 ? 0.24204 0.32629 0.26294 0.00524  -0.02717 -0.03650 151 GLY A C   
1163 O O   . GLY A 151 ? 0.29444 0.35688 0.26090 -0.00269 -0.01032 -0.00428 151 GLY A O   
1164 N N   . LEU A 152 ? 0.24695 0.33710 0.24091 0.01319  -0.03662 -0.05256 152 LEU A N   
1165 C CA  . LEU A 152 ? 0.23189 0.37528 0.22724 0.03128  -0.01779 -0.03046 152 LEU A CA  
1166 C C   . LEU A 152 ? 0.20859 0.36946 0.24071 0.03876  -0.02727 -0.01940 152 LEU A C   
1167 O O   . LEU A 152 ? 0.21482 0.40062 0.26503 0.01580  -0.02306 -0.02234 152 LEU A O   
1168 C CB  . LEU A 152 ? 0.25851 0.41235 0.21311 0.03767  -0.01196 -0.03206 152 LEU A CB  
1169 C CG  . LEU A 152 ? 0.24584 0.46882 0.22695 0.05183  -0.04209 -0.02226 152 LEU A CG  
1170 C CD1 . LEU A 152 ? 0.31104 0.47056 0.23309 0.08509  -0.05242 -0.02585 152 LEU A CD1 
1171 C CD2 . LEU A 152 ? 0.20167 0.49395 0.23662 0.02726  -0.02989 -0.02635 152 LEU A CD2 
1172 N N   . CYS A 153 ? 0.23747 0.34528 0.22658 0.00578  -0.03137 -0.00914 153 CYS A N   
1173 C CA  . CYS A 153 ? 0.24300 0.37260 0.23967 0.00268  -0.01009 0.00143  153 CYS A CA  
1174 C C   . CYS A 153 ? 0.25882 0.35535 0.24345 0.04052  -0.03211 -0.00131 153 CYS A C   
1175 O O   . CYS A 153 ? 0.23997 0.36654 0.25046 0.03845  -0.01379 0.01195  153 CYS A O   
1176 C CB  . CYS A 153 ? 0.24168 0.38443 0.24162 0.02260  0.00495  -0.00775 153 CYS A CB  
1177 S SG  . CYS A 153 ? 0.26205 0.41867 0.24820 0.01280  -0.00816 0.00008  153 CYS A SG  
1178 N N   . MET A 154 ? 0.22603 0.36270 0.22937 0.02497  -0.01118 -0.01133 154 MET A N   
1179 C CA  . MET A 154 ? 0.22462 0.38195 0.22692 0.02375  0.00087  -0.02123 154 MET A CA  
1180 C C   . MET A 154 ? 0.23111 0.39564 0.20622 0.02898  -0.02435 -0.01515 154 MET A C   
1181 O O   . MET A 154 ? 0.21402 0.43121 0.22214 0.02250  -0.02996 -0.00669 154 MET A O   
1182 C CB  . MET A 154 ? 0.21163 0.37494 0.25788 0.04184  0.00877  0.00177  154 MET A CB  
1183 C CG  . MET A 154 ? 0.20839 0.40401 0.28073 0.00724  0.04264  -0.00380 154 MET A CG  
1184 S SD  . MET A 154 ? 0.23524 0.39258 0.29905 0.02155  -0.02156 0.01882  154 MET A SD  
1185 C CE  . MET A 154 ? 0.18131 0.42970 0.34275 0.02403  -0.03739 0.00007  154 MET A CE  
1186 N N   . SER A 155 ? 0.25394 0.38280 0.19287 0.03718  -0.05201 -0.00710 155 SER A N   
1187 C CA  . SER A 155 ? 0.29130 0.36299 0.18859 0.02993  -0.02025 -0.00592 155 SER A CA  
1188 C C   . SER A 155 ? 0.27693 0.38117 0.20169 0.02543  -0.01092 -0.00290 155 SER A C   
1189 O O   . SER A 155 ? 0.29441 0.37714 0.22286 0.01918  -0.00766 -0.01822 155 SER A O   
1190 C CB  . SER A 155 ? 0.33764 0.35812 0.19551 0.09511  -0.02176 -0.00994 155 SER A CB  
1191 O OG  . SER A 155 ? 0.37510 0.39622 0.25829 0.07384  -0.01173 -0.00728 155 SER A OG  
1192 N N   . THR A 156 ? 0.27372 0.35570 0.20777 0.04841  -0.01578 -0.01527 156 THR A N   
1193 C CA  . THR A 156 ? 0.26281 0.32366 0.25329 0.03919  0.01110  -0.02047 156 THR A CA  
1194 C C   . THR A 156 ? 0.28042 0.32866 0.26784 0.03525  0.03161  -0.02624 156 THR A C   
1195 O O   . THR A 156 ? 0.24973 0.38854 0.28189 0.00560  0.03753  -0.01514 156 THR A O   
1196 C CB  . THR A 156 ? 0.23364 0.33572 0.26796 0.02465  0.00416  -0.02350 156 THR A CB  
1197 O OG1 . THR A 156 ? 0.28240 0.37125 0.24859 0.01316  -0.00520 -0.00874 156 THR A OG1 
1198 C CG2 . THR A 156 ? 0.19059 0.31691 0.29483 0.00454  -0.01984 -0.03133 156 THR A CG2 
1199 N N   . PRO A 157 ? 0.29002 0.31192 0.26188 -0.00492 0.00847  -0.01881 157 PRO A N   
1200 C CA  . PRO A 157 ? 0.27595 0.31631 0.24839 -0.01208 -0.02868 -0.03093 157 PRO A CA  
1201 C C   . PRO A 157 ? 0.25700 0.36713 0.23837 0.02655  0.01113  -0.04588 157 PRO A C   
1202 O O   . PRO A 157 ? 0.27221 0.39959 0.24358 0.01939  0.02430  -0.03163 157 PRO A O   
1203 C CB  . PRO A 157 ? 0.28678 0.33075 0.25248 -0.01450 -0.04132 -0.04872 157 PRO A CB  
1204 C CG  . PRO A 157 ? 0.32504 0.33978 0.27778 -0.02904 -0.01677 -0.04074 157 PRO A CG  
1205 C CD  . PRO A 157 ? 0.32521 0.31804 0.27912 -0.00738 0.00463  -0.02277 157 PRO A CD  
1206 N N   . SER A 158 ? 0.32213 0.37889 0.22005 0.01013  0.03793  -0.06246 158 SER A N   
1207 C CA  . SER A 158 ? 0.29087 0.40291 0.20728 0.01712  0.04399  -0.03638 158 SER A CA  
1208 C C   . SER A 158 ? 0.25462 0.37896 0.19096 0.00111  0.03447  -0.00461 158 SER A C   
1209 O O   . SER A 158 ? 0.29768 0.39897 0.19661 0.01629  0.03838  0.01656  158 SER A O   
1210 C CB  . SER A 158 ? 0.31728 0.44194 0.22163 0.03223  0.01176  -0.04304 158 SER A CB  
1211 O OG  . SER A 158 ? 0.32534 0.44746 0.24011 0.05510  0.01206  -0.03661 158 SER A OG  
1212 N N   . GLY A 159 ? 0.27009 0.31007 0.20075 -0.00808 -0.00025 -0.03448 159 GLY A N   
1213 C CA  . GLY A 159 ? 0.26513 0.30665 0.20583 -0.01820 -0.01656 -0.03272 159 GLY A CA  
1214 C C   . GLY A 159 ? 0.25641 0.33728 0.22056 -0.04237 -0.00559 -0.02297 159 GLY A C   
1215 O O   . GLY A 159 ? 0.28361 0.33749 0.24807 -0.05259 -0.02516 -0.02581 159 GLY A O   
1216 N N   . THR A 160 ? 0.21703 0.39001 0.22932 -0.01629 -0.01017 -0.00957 160 THR A N   
1217 C CA  . THR A 160 ? 0.23508 0.37079 0.24531 -0.01616 -0.00088 -0.00428 160 THR A CA  
1218 C C   . THR A 160 ? 0.24139 0.32143 0.24726 -0.00634 -0.01471 -0.00552 160 THR A C   
1219 O O   . THR A 160 ? 0.25175 0.28212 0.27822 0.00408  -0.03602 -0.00811 160 THR A O   
1220 C CB  . THR A 160 ? 0.25365 0.37373 0.25325 -0.01886 -0.00661 -0.00253 160 THR A CB  
1221 O OG1 . THR A 160 ? 0.24375 0.36653 0.27736 -0.00496 -0.01785 -0.00783 160 THR A OG1 
1222 C CG2 . THR A 160 ? 0.27730 0.37157 0.22689 -0.00630 0.01478  0.00796  160 THR A CG2 
1223 N N   . THR A 161 ? 0.24655 0.31673 0.22761 -0.01520 -0.00681 -0.01230 161 THR A N   
1224 C CA  . THR A 161 ? 0.26786 0.36821 0.22536 -0.03785 -0.04939 -0.00386 161 THR A CA  
1225 C C   . THR A 161 ? 0.24833 0.41870 0.21794 -0.03079 -0.05448 -0.02335 161 THR A C   
1226 O O   . THR A 161 ? 0.27616 0.48677 0.20689 -0.02727 -0.02905 -0.00908 161 THR A O   
1227 C CB  . THR A 161 ? 0.28401 0.40747 0.25878 -0.04689 -0.05709 -0.00587 161 THR A CB  
1228 O OG1 . THR A 161 ? 0.32456 0.43029 0.26855 -0.02737 -0.05867 0.00342  161 THR A OG1 
1229 C CG2 . THR A 161 ? 0.26697 0.40059 0.28391 -0.08350 -0.05789 0.00479  161 THR A CG2 
1230 N N   . ALA A 162 ? 0.25822 0.37505 0.23726 -0.02838 -0.04479 -0.05330 162 ALA A N   
1231 C CA  . ALA A 162 ? 0.28959 0.38883 0.25231 0.00570  -0.00043 -0.06518 162 ALA A CA  
1232 C C   . ALA A 162 ? 0.30235 0.39674 0.26806 -0.02663 -0.04356 -0.01726 162 ALA A C   
1233 O O   . ALA A 162 ? 0.28065 0.42229 0.25118 -0.00094 -0.05878 0.00906  162 ALA A O   
1234 C CB  . ALA A 162 ? 0.25790 0.37335 0.24984 0.01007  0.03227  -0.07798 162 ALA A CB  
1235 N N   . TYR A 163 ? 0.24972 0.35959 0.27695 -0.04472 -0.05502 -0.01292 163 TYR A N   
1236 C CA  . TYR A 163 ? 0.20350 0.35464 0.26311 -0.03739 -0.01889 -0.01429 163 TYR A CA  
1237 C C   . TYR A 163 ? 0.17321 0.34703 0.24614 -0.01129 -0.01051 -0.04147 163 TYR A C   
1238 O O   . TYR A 163 ? 0.16401 0.35671 0.24109 0.02788  -0.01082 -0.04139 163 TYR A O   
1239 C CB  . TYR A 163 ? 0.16871 0.37379 0.27754 -0.02821 -0.02719 -0.00787 163 TYR A CB  
1240 C CG  . TYR A 163 ? 0.25397 0.36562 0.27665 -0.03372 -0.06997 -0.01968 163 TYR A CG  
1241 C CD1 . TYR A 163 ? 0.28716 0.37122 0.25673 -0.00874 -0.05177 -0.05421 163 TYR A CD1 
1242 C CD2 . TYR A 163 ? 0.37379 0.37593 0.29791 -0.03882 -0.11005 -0.02209 163 TYR A CD2 
1243 C CE1 . TYR A 163 ? 0.29752 0.38344 0.26002 0.00449  -0.06219 -0.05478 163 TYR A CE1 
1244 C CE2 . TYR A 163 ? 0.46104 0.36644 0.31747 -0.03113 -0.10243 -0.03569 163 TYR A CE2 
1245 C CZ  . TYR A 163 ? 0.50148 0.37948 0.30526 0.00927  -0.08755 -0.06867 163 TYR A CZ  
1246 O OH  . TYR A 163 ? 0.68128 0.39186 0.32353 0.05148  -0.13949 -0.05759 163 TYR A OH  
1247 N N   . ASN A 164 ? 0.16281 0.32401 0.23994 -0.04149 0.00521  -0.03410 164 ASN A N   
1248 C CA  . ASN A 164 ? 0.14528 0.35712 0.24807 -0.02663 -0.00383 -0.00819 164 ASN A CA  
1249 C C   . ASN A 164 ? 0.18041 0.40233 0.24313 -0.02174 -0.01442 -0.01298 164 ASN A C   
1250 O O   . ASN A 164 ? 0.21443 0.39978 0.25407 -0.02685 -0.01163 -0.00972 164 ASN A O   
1251 C CB  . ASN A 164 ? 0.20153 0.34499 0.26645 -0.01193 -0.00416 -0.01499 164 ASN A CB  
1252 C CG  . ASN A 164 ? 0.21996 0.40614 0.26509 0.01249  -0.01915 -0.02458 164 ASN A CG  
1253 O OD1 . ASN A 164 ? 0.24633 0.46642 0.26015 -0.01955 -0.00768 -0.03831 164 ASN A OD1 
1254 N ND2 . ASN A 164 ? 0.21620 0.40594 0.26246 0.03841  -0.02227 -0.02586 164 ASN A ND2 
1255 N N   . LYS A 165 ? 0.19942 0.39230 0.22122 -0.02195 -0.04898 -0.01949 165 LYS A N   
1256 C CA  . LYS A 165 ? 0.21535 0.35788 0.21677 0.00062  -0.06697 -0.02118 165 LYS A CA  
1257 C C   . LYS A 165 ? 0.22972 0.33743 0.23883 0.03420  -0.03434 -0.04272 165 LYS A C   
1258 O O   . LYS A 165 ? 0.21205 0.28182 0.25285 0.04474  -0.02165 -0.02678 165 LYS A O   
1259 C CB  . LYS A 165 ? 0.22879 0.37103 0.21054 0.01180  -0.07284 -0.00189 165 LYS A CB  
1260 C CG  . LYS A 165 ? 0.23699 0.36332 0.21506 0.00801  -0.08544 0.02071  165 LYS A CG  
1261 C CD  . LYS A 165 ? 0.25121 0.35441 0.23350 0.03087  -0.08931 0.03469  165 LYS A CD  
1262 C CE  . LYS A 165 ? 0.37703 0.36293 0.27756 0.10719  -0.13188 -0.00664 165 LYS A CE  
1263 N NZ  . LYS A 165 ? 0.51612 0.39323 0.29680 0.13178  -0.17124 -0.03433 165 LYS A NZ  
1264 N N   . SER A 166 ? 0.22774 0.36113 0.24210 0.00925  -0.02740 -0.04945 166 SER A N   
1265 C CA  . SER A 166 ? 0.22817 0.39542 0.22804 0.04214  0.02481  -0.02226 166 SER A CA  
1266 C C   . SER A 166 ? 0.26242 0.39890 0.22931 0.03837  0.01741  -0.03257 166 SER A C   
1267 O O   . SER A 166 ? 0.31862 0.34073 0.23788 0.02800  0.00193  -0.06259 166 SER A O   
1268 C CB  . SER A 166 ? 0.22179 0.42610 0.22432 0.02303  0.09023  -0.01932 166 SER A CB  
1269 O OG  . SER A 166 ? 0.29721 0.46322 0.23534 0.02443  0.07890  -0.02015 166 SER A OG  
1270 N N   . LEU A 167 ? 0.22209 0.44904 0.22816 0.02179  -0.02463 0.00808  167 LEU A N   
1271 C CA  . LEU A 167 ? 0.21666 0.47164 0.22350 0.00074  -0.02735 -0.02210 167 LEU A CA  
1272 C C   . LEU A 167 ? 0.23478 0.49633 0.22090 0.00766  -0.03127 -0.01350 167 LEU A C   
1273 O O   . LEU A 167 ? 0.28139 0.52299 0.21696 0.01078  -0.01857 -0.03047 167 LEU A O   
1274 C CB  . LEU A 167 ? 0.22838 0.42311 0.24130 -0.00742 -0.02443 -0.02699 167 LEU A CB  
1275 C CG  . LEU A 167 ? 0.21435 0.38317 0.26672 0.03811  -0.02546 -0.03261 167 LEU A CG  
1276 C CD1 . LEU A 167 ? 0.20794 0.34062 0.29071 0.06840  -0.01656 -0.02331 167 LEU A CD1 
1277 C CD2 . LEU A 167 ? 0.22174 0.36299 0.27048 0.03858  -0.05055 -0.04174 167 LEU A CD2 
1278 N N   . GLY A 168 ? 0.21912 0.47762 0.23182 0.01619  -0.01741 0.01772  168 GLY A N   
1279 C CA  . GLY A 168 ? 0.19983 0.45992 0.24652 0.02817  0.01306  0.02072  168 GLY A CA  
1280 C C   . GLY A 168 ? 0.25531 0.47869 0.24002 0.03400  0.01340  0.00192  168 GLY A C   
1281 O O   . GLY A 168 ? 0.29270 0.49030 0.24808 0.06856  0.03074  -0.01358 168 GLY A O   
1282 N N   . GLY A 169 ? 0.23717 0.42334 0.21809 0.00951  -0.02110 -0.01160 169 GLY A N   
1283 C CA  . GLY A 169 ? 0.22530 0.38832 0.21689 0.01643  -0.02432 -0.03334 169 GLY A CA  
1284 C C   . GLY A 169 ? 0.23579 0.40072 0.22308 -0.00578 -0.01049 -0.02593 169 GLY A C   
1285 O O   . GLY A 169 ? 0.24111 0.46543 0.22623 0.00601  -0.01926 -0.04070 169 GLY A O   
1286 N N   . ALA A 170 ? 0.20041 0.35335 0.21719 -0.04486 -0.00224 0.00091  170 ALA A N   
1287 C CA  . ALA A 170 ? 0.19303 0.38495 0.23111 -0.04457 0.00237  0.01259  170 ALA A CA  
1288 C C   . ALA A 170 ? 0.23040 0.44429 0.23798 -0.01362 -0.00259 0.00127  170 ALA A C   
1289 O O   . ALA A 170 ? 0.25895 0.50401 0.23541 -0.00744 -0.00554 0.01868  170 ALA A O   
1290 C CB  . ALA A 170 ? 0.22273 0.38064 0.23350 -0.02244 0.00249  0.02968  170 ALA A CB  
1291 N N   . LEU A 171 ? 0.24427 0.39980 0.25197 -0.01486 -0.01249 -0.01540 171 LEU A N   
1292 C CA  . LEU A 171 ? 0.22387 0.39440 0.26032 -0.00375 -0.01106 -0.01283 171 LEU A CA  
1293 C C   . LEU A 171 ? 0.24422 0.40440 0.30203 0.04016  -0.01657 -0.01426 171 LEU A C   
1294 O O   . LEU A 171 ? 0.26878 0.40585 0.34695 0.07948  -0.01354 0.00284  171 LEU A O   
1295 C CB  . LEU A 171 ? 0.22879 0.39465 0.24209 -0.03663 -0.00540 0.00061  171 LEU A CB  
1296 C CG  . LEU A 171 ? 0.25346 0.43174 0.25411 -0.03431 -0.02477 0.00948  171 LEU A CG  
1297 C CD1 . LEU A 171 ? 0.24979 0.43123 0.26852 -0.03140 -0.01417 -0.00123 171 LEU A CD1 
1298 C CD2 . LEU A 171 ? 0.27382 0.45421 0.26907 -0.02062 -0.03595 0.02509  171 LEU A CD2 
1299 N N   . MET A 172 ? 0.26856 0.41339 0.28978 0.00203  -0.01819 -0.02099 172 MET A N   
1300 C CA  . MET A 172 ? 0.37320 0.41140 0.29520 -0.03745 0.01145  -0.04821 172 MET A CA  
1301 C C   . MET A 172 ? 0.33563 0.38736 0.30438 -0.05057 0.04726  -0.06836 172 MET A C   
1302 O O   . MET A 172 ? 0.33275 0.39322 0.32701 -0.04445 0.07648  -0.10405 172 MET A O   
1303 C CB  . MET A 172 ? 0.50505 0.46753 0.29146 0.00237  0.01610  -0.02680 172 MET A CB  
1304 C CG  . MET A 172 ? 0.65127 0.52770 0.33347 0.05019  0.02859  0.03743  172 MET A CG  
1305 S SD  . MET A 172 ? 0.76844 0.56352 0.36490 0.07201  -0.00197 0.08742  172 MET A SD  
1306 C CE  . MET A 172 ? 0.82199 0.54290 0.36243 0.10093  -0.02285 0.09785  172 MET A CE  
1307 N N   . HIS A 173 ? 0.30805 0.37487 0.29137 -0.04325 -0.01335 -0.08099 173 HIS A N   
1308 C CA  . HIS A 173 ? 0.30506 0.41008 0.29376 -0.01640 -0.03148 -0.06909 173 HIS A CA  
1309 C C   . HIS A 173 ? 0.32657 0.47085 0.31310 -0.00130 -0.00080 -0.09250 173 HIS A C   
1310 O O   . HIS A 173 ? 0.32166 0.52183 0.34155 0.01804  -0.01848 -0.09808 173 HIS A O   
1311 C CB  . HIS A 173 ? 0.32323 0.39806 0.30330 -0.04689 -0.00972 -0.05812 173 HIS A CB  
1312 C CG  . HIS A 173 ? 0.36320 0.40302 0.31608 -0.04018 -0.02907 -0.03858 173 HIS A CG  
1313 N ND1 . HIS A 173 ? 0.40273 0.42394 0.32943 0.00066  -0.03645 -0.01740 173 HIS A ND1 
1314 C CD2 . HIS A 173 ? 0.37061 0.40907 0.30565 -0.05231 -0.03891 -0.03739 173 HIS A CD2 
1315 C CE1 . HIS A 173 ? 0.43119 0.41723 0.30465 -0.01037 -0.05084 -0.01452 173 HIS A CE1 
1316 N NE2 . HIS A 173 ? 0.42483 0.42827 0.30863 -0.04674 -0.05130 -0.02237 173 HIS A NE2 
1317 N N   . PRO A 174 ? 0.31704 0.47206 0.31611 0.02055  -0.00295 -0.12024 174 PRO A N   
1318 C CA  . PRO A 174 ? 0.34188 0.49289 0.33094 0.02463  -0.01915 -0.10849 174 PRO A CA  
1319 C C   . PRO A 174 ? 0.39416 0.52135 0.35913 -0.02135 -0.02853 -0.10591 174 PRO A C   
1320 O O   . PRO A 174 ? 0.43016 0.54789 0.37076 -0.02887 -0.03293 -0.08877 174 PRO A O   
1321 C CB  . PRO A 174 ? 0.36082 0.51759 0.33258 0.04269  -0.00065 -0.09541 174 PRO A CB  
1322 C CG  . PRO A 174 ? 0.33745 0.50319 0.32980 0.07773  0.00827  -0.07684 174 PRO A CG  
1323 C CD  . PRO A 174 ? 0.33064 0.48132 0.31867 0.04302  0.00441  -0.11023 174 PRO A CD  
1324 N N   . SER A 175 ? 0.39461 0.49917 0.37261 -0.04374 -0.03504 -0.11891 175 SER A N   
1325 C CA  . SER A 175 ? 0.41613 0.46740 0.38746 -0.03552 -0.05630 -0.10045 175 SER A CA  
1326 C C   . SER A 175 ? 0.46120 0.46489 0.40167 -0.01956 -0.04352 -0.10205 175 SER A C   
1327 O O   . SER A 175 ? 0.52244 0.46576 0.42097 -0.02743 -0.06122 -0.10701 175 SER A O   
1328 C CB  . SER A 175 ? 0.45021 0.46361 0.40778 -0.02973 -0.07942 -0.08147 175 SER A CB  
1329 O OG  . SER A 175 ? 0.49487 0.49028 0.41970 -0.05195 -0.08315 -0.08695 175 SER A OG  
1330 N N   . ILE A 176 ? 0.38685 0.44875 0.38083 0.03325  -0.03175 -0.09727 176 ILE A N   
1331 C CA  . ILE A 176 ? 0.35310 0.44612 0.36486 0.05028  -0.04015 -0.06691 176 ILE A CA  
1332 C C   . ILE A 176 ? 0.39039 0.42288 0.35597 0.02458  -0.02600 -0.02307 176 ILE A C   
1333 O O   . ILE A 176 ? 0.39684 0.41823 0.37209 -0.02572 0.00135  0.01153  176 ILE A O   
1334 C CB  . ILE A 176 ? 0.32818 0.45265 0.36495 0.05952  -0.01687 -0.06373 176 ILE A CB  
1335 C CG1 . ILE A 176 ? 0.30742 0.43496 0.39289 0.08023  -0.03332 -0.06188 176 ILE A CG1 
1336 C CG2 . ILE A 176 ? 0.32548 0.47922 0.35566 0.00224  -0.00133 -0.05306 176 ILE A CG2 
1337 C CD1 . ILE A 176 ? 0.30376 0.44400 0.40508 0.06854  -0.03927 -0.07132 176 ILE A CD1 
1338 N N   . GLU A 177 ? 0.41839 0.37947 0.32077 0.00849  -0.03447 -0.00127 177 GLU A N   
1339 C CA  . GLU A 177 ? 0.41744 0.37025 0.31971 0.01514  -0.01769 0.00773  177 GLU A CA  
1340 C C   . GLU A 177 ? 0.42005 0.37802 0.29758 0.00547  -0.00679 0.01853  177 GLU A C   
1341 O O   . GLU A 177 ? 0.44513 0.41242 0.28022 -0.00560 -0.00088 0.03244  177 GLU A O   
1342 C CB  . GLU A 177 ? 0.47693 0.39212 0.35183 0.01752  0.01327  0.00209  177 GLU A CB  
1343 C CG  . GLU A 177 ? 0.55261 0.43005 0.38706 0.06425  0.02226  -0.01663 177 GLU A CG  
1344 C CD  . GLU A 177 ? 0.61559 0.48880 0.44300 0.08379  0.07810  -0.04022 177 GLU A CD  
1345 O OE1 . GLU A 177 ? 0.61641 0.49152 0.46836 0.07339  0.08340  -0.05810 177 GLU A OE1 
1346 O OE2 . GLU A 177 ? 0.66621 0.52550 0.46778 0.10023  0.11839  -0.04110 177 GLU A OE2 
1347 N N   . ALA A 178 ? 0.41785 0.34499 0.30042 0.02388  -0.00565 0.00700  178 ALA A N   
1348 C CA  . ALA A 178 ? 0.34504 0.30962 0.29399 0.03669  0.00027  0.01033  178 ALA A CA  
1349 C C   . ALA A 178 ? 0.30975 0.34426 0.27580 0.03173  -0.00142 0.02729  178 ALA A C   
1350 O O   . ALA A 178 ? 0.31078 0.37646 0.27657 0.05503  0.01850  0.05030  178 ALA A O   
1351 C CB  . ALA A 178 ? 0.30060 0.26219 0.31086 0.06212  -0.00908 0.02325  178 ALA A CB  
1352 N N   . MET A 179 ? 0.27131 0.33517 0.27199 0.06750  -0.02137 0.03467  179 MET A N   
1353 C CA  . MET A 179 ? 0.27465 0.34534 0.25379 0.06501  -0.01797 0.02370  179 MET A CA  
1354 C C   . MET A 179 ? 0.25781 0.32691 0.24475 0.05133  -0.02472 0.02961  179 MET A C   
1355 O O   . MET A 179 ? 0.28767 0.34397 0.23599 0.00882  0.01791  0.03141  179 MET A O   
1356 C CB  . MET A 179 ? 0.29829 0.33801 0.24721 0.06213  -0.01318 0.02326  179 MET A CB  
1357 C CG  . MET A 179 ? 0.29494 0.34332 0.26301 0.04837  -0.04175 0.01825  179 MET A CG  
1358 S SD  . MET A 179 ? 0.30478 0.35232 0.27898 0.03561  -0.02521 0.00440  179 MET A SD  
1359 C CE  . MET A 179 ? 0.23190 0.37197 0.25265 0.03351  0.00227  0.02101  179 MET A CE  
1360 N N   . GLN A 180 ? 0.23636 0.32083 0.24628 0.02696  -0.03952 0.02452  180 GLN A N   
1361 C CA  . GLN A 180 ? 0.25550 0.31177 0.23977 0.06090  -0.00728 0.00851  180 GLN A CA  
1362 C C   . GLN A 180 ? 0.23917 0.34087 0.23253 0.03381  -0.02234 0.00128  180 GLN A C   
1363 O O   . GLN A 180 ? 0.24899 0.36102 0.26446 0.00596  -0.03834 0.02161  180 GLN A O   
1364 C CB  . GLN A 180 ? 0.23702 0.26823 0.22501 0.07698  -0.00990 0.02073  180 GLN A CB  
1365 C CG  . GLN A 180 ? 0.22728 0.26959 0.21067 0.06784  -0.02750 0.01195  180 GLN A CG  
1366 C CD  . GLN A 180 ? 0.28154 0.32298 0.21359 0.04487  -0.02920 -0.00380 180 GLN A CD  
1367 O OE1 . GLN A 180 ? 0.32648 0.33650 0.20573 0.04223  -0.02372 -0.04420 180 GLN A OE1 
1368 N NE2 . GLN A 180 ? 0.28444 0.33889 0.23261 0.01760  -0.04037 0.00171  180 GLN A NE2 
1369 N N   . LEU A 181 ? 0.24236 0.34948 0.20298 0.00760  -0.03821 -0.01752 181 LEU A N   
1370 C CA  . LEU A 181 ? 0.20637 0.39774 0.19111 0.02437  -0.03574 -0.00172 181 LEU A CA  
1371 C C   . LEU A 181 ? 0.22706 0.43245 0.21505 -0.00928 0.00181  0.02976  181 LEU A C   
1372 O O   . LEU A 181 ? 0.23374 0.45272 0.23154 0.01811  0.00756  0.03393  181 LEU A O   
1373 C CB  . LEU A 181 ? 0.21856 0.44077 0.19114 0.00937  -0.04998 -0.01187 181 LEU A CB  
1374 C CG  . LEU A 181 ? 0.22955 0.43098 0.18657 -0.01300 -0.03973 -0.01475 181 LEU A CG  
1375 C CD1 . LEU A 181 ? 0.23738 0.39478 0.20907 -0.00975 -0.00360 0.00244  181 LEU A CD1 
1376 C CD2 . LEU A 181 ? 0.25775 0.44899 0.17582 -0.00980 -0.04504 -0.02955 181 LEU A CD2 
1377 N N   . THR A 182 ? 0.20325 0.42329 0.21775 0.00407  0.01200  0.02468  182 THR A N   
1378 C CA  . THR A 182 ? 0.24277 0.42051 0.21061 -0.00753 -0.00474 0.01405  182 THR A CA  
1379 C C   . THR A 182 ? 0.24147 0.39358 0.22971 0.00102  -0.01375 -0.01355 182 THR A C   
1380 O O   . THR A 182 ? 0.20640 0.38673 0.23107 0.00575  0.01441  -0.02375 182 THR A O   
1381 C CB  . THR A 182 ? 0.22870 0.47478 0.20264 -0.04453 0.03705  0.00827  182 THR A CB  
1382 O OG1 . THR A 182 ? 0.30295 0.48726 0.23556 -0.00885 0.02669  0.05154  182 THR A OG1 
1383 C CG2 . THR A 182 ? 0.20938 0.47107 0.19960 -0.06605 -0.00126 -0.01643 182 THR A CG2 
1384 N N   . GLU A 183 ? 0.24395 0.38021 0.23728 -0.01153 -0.01722 -0.02608 183 GLU A N   
1385 C CA  . GLU A 183 ? 0.24997 0.34387 0.23829 -0.01445 -0.01585 -0.00086 183 GLU A CA  
1386 C C   . GLU A 183 ? 0.20269 0.35536 0.25765 -0.00362 -0.03784 0.00371  183 GLU A C   
1387 O O   . GLU A 183 ? 0.23311 0.36402 0.28723 -0.01010 -0.03898 0.02533  183 GLU A O   
1388 C CB  . GLU A 183 ? 0.34205 0.35266 0.24542 -0.00413 0.04597  -0.00010 183 GLU A CB  
1389 C CG  . GLU A 183 ? 0.46646 0.38395 0.27127 -0.01905 0.07443  -0.00544 183 GLU A CG  
1390 C CD  . GLU A 183 ? 0.52220 0.46977 0.31335 -0.05500 0.04796  -0.00212 183 GLU A CD  
1391 O OE1 . GLU A 183 ? 0.58829 0.49692 0.36057 -0.04625 0.10073  -0.02311 183 GLU A OE1 
1392 O OE2 . GLU A 183 ? 0.45354 0.53303 0.29328 -0.04261 0.02205  -0.00548 183 GLU A OE2 
1393 N N   . MET A 184 ? 0.21113 0.35787 0.26721 0.02672  -0.01018 -0.02377 184 MET A N   
1394 C CA  . MET A 184 ? 0.23446 0.41825 0.26865 0.03527  -0.01280 -0.03114 184 MET A CA  
1395 C C   . MET A 184 ? 0.27161 0.40541 0.26883 0.00223  -0.02038 -0.02657 184 MET A C   
1396 O O   . MET A 184 ? 0.28947 0.44302 0.29649 0.01517  -0.03488 0.00056  184 MET A O   
1397 C CB  . MET A 184 ? 0.25092 0.50598 0.27554 0.05941  0.03725  -0.03833 184 MET A CB  
1398 C CG  . MET A 184 ? 0.32121 0.60510 0.29215 0.04744  0.04635  -0.04813 184 MET A CG  
1399 S SD  . MET A 184 ? 0.46959 0.69616 0.30955 0.09015  0.06213  -0.03390 184 MET A SD  
1400 C CE  . MET A 184 ? 0.58196 0.69664 0.29243 0.06891  0.07644  -0.02621 184 MET A CE  
1401 N N   . ALA A 185 ? 0.32770 0.38509 0.25729 -0.02853 -0.00169 -0.01620 185 ALA A N   
1402 C CA  . ALA A 185 ? 0.35043 0.38153 0.25029 -0.04255 -0.00069 0.01499  185 ALA A CA  
1403 C C   . ALA A 185 ? 0.33917 0.41069 0.25152 -0.00652 -0.01199 0.01971  185 ALA A C   
1404 O O   . ALA A 185 ? 0.38470 0.40829 0.25097 -0.03960 -0.04649 -0.00497 185 ALA A O   
1405 C CB  . ALA A 185 ? 0.33363 0.37096 0.24856 -0.02870 -0.01270 0.03025  185 ALA A CB  
1406 N N   . SER A 186 ? 0.35238 0.44696 0.27152 0.04761  0.00811  0.04145  186 SER A N   
1407 C CA  . SER A 186 ? 0.35454 0.45285 0.32689 0.08138  0.00352  0.02658  186 SER A CA  
1408 C C   . SER A 186 ? 0.35959 0.47663 0.32965 0.04136  0.01043  0.01182  186 SER A C   
1409 O O   . SER A 186 ? 0.33069 0.49593 0.34139 0.04746  0.04076  -0.00766 186 SER A O   
1410 C CB  . SER A 186 ? 0.32719 0.46389 0.39350 0.13273  0.01490  0.02612  186 SER A CB  
1411 O OG  . SER A 186 ? 0.36415 0.48784 0.45816 0.13223  0.02565  0.02335  186 SER A OG  
1412 N N   . ILE A 187 ? 0.33632 0.44824 0.34133 0.01277  0.01520  0.01093  187 ILE A N   
1413 C CA  . ILE A 187 ? 0.39262 0.44252 0.36981 -0.00253 0.02819  0.00639  187 ILE A CA  
1414 C C   . ILE A 187 ? 0.40516 0.45398 0.35198 0.02846  0.06228  -0.02612 187 ILE A C   
1415 O O   . ILE A 187 ? 0.45493 0.46051 0.35146 0.01388  0.09023  -0.02444 187 ILE A O   
1416 C CB  . ILE A 187 ? 0.46560 0.43406 0.43669 0.01270  -0.01620 0.00827  187 ILE A CB  
1417 C CG1 . ILE A 187 ? 0.45592 0.44413 0.48049 0.00967  -0.04193 -0.02525 187 ILE A CG1 
1418 C CG2 . ILE A 187 ? 0.52149 0.43555 0.46067 0.02225  -0.00742 0.02560  187 ILE A CG2 
1419 C CD1 . ILE A 187 ? 0.50556 0.46517 0.50121 0.00510  -0.06116 -0.03975 187 ILE A CD1 
1420 N N   . ASN A 188 ? 0.36763 0.46751 0.34594 0.06155  0.02118  -0.03603 188 ASN A N   
1421 C CA  . ASN A 188 ? 0.42037 0.50616 0.35723 0.04739  0.00098  -0.03875 188 ASN A CA  
1422 C C   . ASN A 188 ? 0.42777 0.55215 0.33638 0.03857  0.00422  -0.03959 188 ASN A C   
1423 O O   . ASN A 188 ? 0.41166 0.57995 0.34392 0.01137  0.00958  -0.02091 188 ASN A O   
1424 C CB  . ASN A 188 ? 0.53802 0.51774 0.38284 0.01181  -0.00133 -0.03949 188 ASN A CB  
1425 C CG  . ASN A 188 ? 0.65649 0.56054 0.41675 0.04769  -0.00892 -0.00907 188 ASN A CG  
1426 O OD1 . ASN A 188 ? 0.73652 0.58319 0.44987 0.06918  -0.04926 -0.00829 188 ASN A OD1 
1427 N ND2 . ASN A 188 ? 0.67973 0.55677 0.41799 0.05159  0.00973  0.02156  188 ASN A ND2 
1428 N N   . ASN A 189 ? 0.43125 0.55374 0.31793 0.05755  0.02345  -0.06025 189 ASN A N   
1429 C CA  . ASN A 189 ? 0.42022 0.56233 0.30872 0.08915  -0.00104 -0.05510 189 ASN A CA  
1430 C C   . ASN A 189 ? 0.51327 0.55661 0.32957 0.10143  -0.00282 -0.02616 189 ASN A C   
1431 O O   . ASN A 189 ? 0.54597 0.58927 0.34662 0.10957  -0.00637 -0.02051 189 ASN A O   
1432 C CB  . ASN A 189 ? 0.40652 0.61051 0.27292 0.11855  -0.03995 -0.07265 189 ASN A CB  
1433 C CG  . ASN A 189 ? 0.39273 0.65374 0.25222 0.11508  -0.02549 -0.06858 189 ASN A CG  
1434 O OD1 . ASN A 189 ? 0.44856 0.62980 0.25624 0.14343  -0.03216 -0.04617 189 ASN A OD1 
1435 N ND2 . ASN A 189 ? 0.31947 0.69559 0.23749 0.06726  -0.01206 -0.07764 189 ASN A ND2 
1436 N N   . ARG A 190 ? 0.63142 0.54865 0.33656 0.08590  0.02822  -0.01351 190 ARG A N   
1437 C CA  . ARG A 190 ? 0.74282 0.57912 0.37177 0.06875  0.11490  -0.00754 190 ARG A CA  
1438 C C   . ARG A 190 ? 0.78840 0.57094 0.36242 0.07960  0.10492  -0.00954 190 ARG A C   
1439 O O   . ARG A 190 ? 0.79572 0.56676 0.38428 0.07591  0.10784  0.01355  190 ARG A O   
1440 C CB  . ARG A 190 ? 0.78856 0.60620 0.43752 0.05124  0.20688  -0.03258 190 ARG A CB  
1441 C CG  . ARG A 190 ? 0.82102 0.63195 0.52192 0.00691  0.24058  -0.05819 190 ARG A CG  
1442 C CD  . ARG A 190 ? 0.83195 0.64556 0.58585 -0.00652 0.23642  -0.08159 190 ARG A CD  
1443 N NE  . ARG A 190 ? 0.86924 0.64890 0.64324 -0.03105 0.22361  -0.09023 190 ARG A NE  
1444 C CZ  . ARG A 190 ? 0.90237 0.66007 0.68013 -0.00411 0.16964  -0.08917 190 ARG A CZ  
1445 N NH1 . ARG A 190 ? 0.87826 0.67073 0.69825 0.02202  0.10559  -0.08995 190 ARG A NH1 
1446 N NH2 . ARG A 190 ? 0.93910 0.66689 0.68378 0.00652  0.18059  -0.09120 190 ARG A NH2 
1447 N N   . VAL A 191 ? 0.77679 0.56620 0.35284 0.10036  0.05481  -0.03279 191 VAL A N   
1448 C CA  . VAL A 191 ? 0.79786 0.58377 0.37319 0.12078  -0.01568 -0.04474 191 VAL A CA  
1449 C C   . VAL A 191 ? 0.81148 0.55742 0.36571 0.13105  -0.05638 -0.05389 191 VAL A C   
1450 O O   . VAL A 191 ? 1.00963 0.60243 0.35233 0.13976  -0.04328 -0.06628 191 VAL A O   
1451 C CB  . VAL A 191 ? 0.79382 0.64151 0.40665 0.14255  -0.02521 -0.06028 191 VAL A CB  
1452 C CG1 . VAL A 191 ? 0.76714 0.65241 0.41293 0.18955  -0.00044 -0.06965 191 VAL A CG1 
1453 C CG2 . VAL A 191 ? 0.80777 0.67183 0.43112 0.13195  -0.04638 -0.06016 191 VAL A CG2 
1454 N N   . TYR A 192 ? 0.62630 0.52159 0.38202 0.12207  -0.11350 -0.07615 192 TYR A N   
1455 C CA  . TYR A 192 ? 0.48669 0.52028 0.41356 0.11739  -0.11451 -0.09867 192 TYR A CA  
1456 C C   . TYR A 192 ? 0.41946 0.57230 0.39673 0.14501  -0.10312 -0.12528 192 TYR A C   
1457 O O   . TYR A 192 ? 0.40977 0.62172 0.39730 0.16082  -0.09495 -0.09934 192 TYR A O   
1458 C CB  . TYR A 192 ? 0.48497 0.50188 0.48359 0.08676  -0.10102 -0.08134 192 TYR A CB  
1459 C CG  . TYR A 192 ? 0.57468 0.51012 0.57584 0.04014  -0.10459 -0.06594 192 TYR A CG  
1460 C CD1 . TYR A 192 ? 0.61674 0.51489 0.60867 0.00461  -0.11205 -0.05175 192 TYR A CD1 
1461 C CD2 . TYR A 192 ? 0.67430 0.53611 0.62755 0.04233  -0.10160 -0.05932 192 TYR A CD2 
1462 C CE1 . TYR A 192 ? 0.63964 0.54244 0.63640 -0.00924 -0.09534 -0.04559 192 TYR A CE1 
1463 C CE2 . TYR A 192 ? 0.68026 0.56466 0.65421 0.01253  -0.07950 -0.04877 192 TYR A CE2 
1464 C CZ  . TYR A 192 ? 0.66140 0.58664 0.66141 -0.00241 -0.07316 -0.04891 192 TYR A CZ  
1465 O OH  . TYR A 192 ? 0.67756 0.62345 0.68669 0.02497  -0.04933 -0.03989 192 TYR A OH  
1466 N N   . ARG A 193 ? 0.40285 0.57475 0.39347 0.10974  -0.08845 -0.15257 193 ARG A N   
1467 C CA  . ARG A 193 ? 0.41575 0.55772 0.41415 0.03274  -0.05497 -0.13558 193 ARG A CA  
1468 C C   . ARG A 193 ? 0.41911 0.51063 0.36416 0.01760  -0.07511 -0.09133 193 ARG A C   
1469 O O   . ARG A 193 ? 0.48947 0.52623 0.35574 0.03653  -0.08550 -0.08986 193 ARG A O   
1470 C CB  . ARG A 193 ? 0.45117 0.60045 0.49867 -0.04060 -0.01894 -0.11419 193 ARG A CB  
1471 C CG  . ARG A 193 ? 0.52256 0.64941 0.57828 -0.01968 0.03724  -0.08658 193 ARG A CG  
1472 C CD  . ARG A 193 ? 0.55533 0.69101 0.64657 -0.01438 0.07611  -0.06229 193 ARG A CD  
1473 N NE  . ARG A 193 ? 0.57900 0.72363 0.68948 -0.04256 0.07984  -0.05175 193 ARG A NE  
1474 C CZ  . ARG A 193 ? 0.59954 0.73906 0.70821 -0.07744 0.06776  -0.05003 193 ARG A CZ  
1475 N NH1 . ARG A 193 ? 0.61482 0.73184 0.71713 -0.07269 0.05426  -0.05383 193 ARG A NH1 
1476 N NH2 . ARG A 193 ? 0.58794 0.75091 0.70944 -0.11252 0.06495  -0.05278 193 ARG A NH2 
1477 N N   . THR A 194 ? 0.32153 0.45347 0.32523 -0.00530 -0.07113 -0.04916 194 THR A N   
1478 C CA  . THR A 194 ? 0.28175 0.48854 0.30343 -0.02025 -0.02147 -0.01195 194 THR A CA  
1479 C C   . THR A 194 ? 0.28922 0.44329 0.28258 0.03962  -0.01720 -0.00863 194 THR A C   
1480 O O   . THR A 194 ? 0.27508 0.42882 0.29447 0.07131  -0.00415 -0.00167 194 THR A O   
1481 C CB  . THR A 194 ? 0.28113 0.58410 0.32150 -0.06445 0.00945  -0.00899 194 THR A CB  
1482 O OG1 . THR A 194 ? 0.31734 0.62860 0.31614 -0.08506 0.00659  -0.01379 194 THR A OG1 
1483 C CG2 . THR A 194 ? 0.28196 0.62157 0.33588 -0.05144 0.03169  -0.01765 194 THR A CG2 
1484 N N   . ILE A 195 ? 0.30865 0.43685 0.26192 0.01728  -0.02726 -0.00210 195 ILE A N   
1485 C CA  . ILE A 195 ? 0.28759 0.42602 0.24478 -0.00675 -0.04396 0.01158  195 ILE A CA  
1486 C C   . ILE A 195 ? 0.32667 0.42183 0.22853 -0.04498 -0.00561 0.01237  195 ILE A C   
1487 O O   . ILE A 195 ? 0.28778 0.51134 0.24466 -0.02468 0.00533  -0.00935 195 ILE A O   
1488 C CB  . ILE A 195 ? 0.32635 0.43943 0.24217 -0.00198 -0.01482 0.00590  195 ILE A CB  
1489 C CG1 . ILE A 195 ? 0.30575 0.43267 0.24255 -0.00328 0.03520  0.00134  195 ILE A CG1 
1490 C CG2 . ILE A 195 ? 0.37633 0.46467 0.23383 -0.00485 -0.01019 -0.00919 195 ILE A CG2 
1491 C CD1 . ILE A 195 ? 0.34213 0.44295 0.23826 0.00599  0.04582  -0.00665 195 ILE A CD1 
1492 N N   A GLY A 196 ? 0.39506 0.37998 0.21501 -0.05411 0.01778  0.02126  196 GLY A N   
1493 N N   B GLY A 196 ? 0.39050 0.37343 0.20528 -0.05269 0.00457  0.02516  196 GLY A N   
1494 C CA  A GLY A 196 ? 0.42127 0.37082 0.22439 -0.07277 -0.00251 0.01980  196 GLY A CA  
1495 C CA  B GLY A 196 ? 0.39525 0.36189 0.19491 -0.05976 -0.00651 0.02147  196 GLY A CA  
1496 C C   A GLY A 196 ? 0.40215 0.39091 0.23705 -0.09588 -0.00571 0.03061  196 GLY A C   
1497 C C   B GLY A 196 ? 0.30016 0.38246 0.19187 -0.04760 0.00522  0.02770  196 GLY A C   
1498 O O   A GLY A 196 ? 0.44879 0.40992 0.25504 -0.14918 0.03170  0.02840  196 GLY A O   
1499 O O   B GLY A 196 ? 0.21965 0.39542 0.18277 -0.02590 0.00354  0.01085  196 GLY A O   
1500 N N   . SER A 197 ? 0.31283 0.38891 0.22264 -0.04585 -0.01719 0.01834  197 SER A N   
1501 C CA  . SER A 197 ? 0.26385 0.38695 0.23166 0.02929  0.01494  0.00748  197 SER A CA  
1502 C C   . SER A 197 ? 0.24282 0.40955 0.22628 0.03894  0.02491  -0.00291 197 SER A C   
1503 O O   . SER A 197 ? 0.23848 0.40572 0.23441 0.01678  0.00378  -0.00340 197 SER A O   
1504 C CB  . SER A 197 ? 0.21694 0.36524 0.24705 0.03730  0.03983  0.00603  197 SER A CB  
1505 O OG  . SER A 197 ? 0.25826 0.37367 0.25135 0.03481  0.01611  -0.00150 197 SER A OG  
1506 N N   . PRO A 198 ? 0.21347 0.39962 0.21410 0.02061  -0.00104 -0.00817 198 PRO A N   
1507 C CA  . PRO A 198 ? 0.25992 0.38321 0.22055 0.02537  -0.01199 -0.01641 198 PRO A CA  
1508 C C   . PRO A 198 ? 0.28227 0.34718 0.24667 0.02511  -0.03836 0.00112  198 PRO A C   
1509 O O   . PRO A 198 ? 0.32458 0.31504 0.25325 0.02090  -0.03367 0.01079  198 PRO A O   
1510 C CB  . PRO A 198 ? 0.28896 0.41601 0.20153 0.04324  -0.00480 -0.01390 198 PRO A CB  
1511 C CG  . PRO A 198 ? 0.24388 0.41190 0.19810 0.04059  0.01843  -0.01469 198 PRO A CG  
1512 C CD  . PRO A 198 ? 0.18677 0.40178 0.19400 0.04513  0.00347  -0.00946 198 PRO A CD  
1513 N N   . LEU A 199 ? 0.22569 0.31824 0.25625 0.05485  -0.05464 -0.01456 199 LEU A N   
1514 C CA  . LEU A 199 ? 0.25246 0.33251 0.25150 0.01534  -0.02982 -0.01190 199 LEU A CA  
1515 C C   . LEU A 199 ? 0.25616 0.34655 0.28385 -0.01909 -0.01873 -0.00298 199 LEU A C   
1516 O O   . LEU A 199 ? 0.23102 0.36026 0.29934 -0.01222 -0.00210 -0.01154 199 LEU A O   
1517 C CB  . LEU A 199 ? 0.21203 0.33494 0.23325 0.04011  -0.01837 -0.03027 199 LEU A CB  
1518 C CG  . LEU A 199 ? 0.21899 0.35644 0.24885 0.01767  -0.00916 -0.03745 199 LEU A CG  
1519 C CD1 . LEU A 199 ? 0.21966 0.40455 0.26736 0.05666  -0.03922 -0.03558 199 LEU A CD1 
1520 C CD2 . LEU A 199 ? 0.26613 0.36200 0.26217 0.01583  0.01186  -0.03789 199 LEU A CD2 
1521 N N   . VAL A 200 ? 0.23612 0.35440 0.28198 -0.00169 -0.01231 0.01921  200 VAL A N   
1522 C CA  . VAL A 200 ? 0.28062 0.32721 0.25609 0.00112  0.01026  -0.01467 200 VAL A CA  
1523 C C   . VAL A 200 ? 0.29891 0.34061 0.27268 0.00764  0.05054  0.01952  200 VAL A C   
1524 O O   . VAL A 200 ? 0.27021 0.35446 0.27815 0.00323  0.03774  0.03424  200 VAL A O   
1525 C CB  . VAL A 200 ? 0.23235 0.30178 0.26403 -0.02135 -0.01196 -0.02460 200 VAL A CB  
1526 C CG1 . VAL A 200 ? 0.26948 0.28354 0.27035 -0.03016 -0.01510 -0.06051 200 VAL A CG1 
1527 C CG2 . VAL A 200 ? 0.24347 0.31589 0.27451 -0.05070 0.00246  0.02579  200 VAL A CG2 
1528 N N   . PHE A 201 ? 0.30730 0.34817 0.28144 0.04491  0.05834  0.02578  201 PHE A N   
1529 C CA  . PHE A 201 ? 0.30094 0.36905 0.27864 0.06347  0.00430  0.02501  201 PHE A CA  
1530 C C   . PHE A 201 ? 0.31665 0.40131 0.29897 0.05873  0.00717  0.06150  201 PHE A C   
1531 O O   . PHE A 201 ? 0.32153 0.41232 0.29319 0.05489  0.02726  0.03842  201 PHE A O   
1532 C CB  . PHE A 201 ? 0.26614 0.37729 0.25729 0.04432  -0.01731 0.01920  201 PHE A CB  
1533 C CG  . PHE A 201 ? 0.25695 0.38673 0.25066 0.03384  -0.02634 0.02940  201 PHE A CG  
1534 C CD1 . PHE A 201 ? 0.28000 0.38355 0.23530 0.01657  -0.02371 0.02366  201 PHE A CD1 
1535 C CD2 . PHE A 201 ? 0.24141 0.41049 0.24794 0.05159  -0.03905 0.03609  201 PHE A CD2 
1536 C CE1 . PHE A 201 ? 0.31707 0.41007 0.23589 -0.01105 -0.01444 0.03916  201 PHE A CE1 
1537 C CE2 . PHE A 201 ? 0.25846 0.42942 0.25056 0.03828  -0.04853 0.03500  201 PHE A CE2 
1538 C CZ  . PHE A 201 ? 0.27438 0.41615 0.24375 0.02093  -0.02827 0.04738  201 PHE A CZ  
1539 N N   . PRO A 202 ? 0.33439 0.40988 0.30896 0.02631  0.01674  0.09160  202 PRO A N   
1540 C CA  . PRO A 202 ? 0.34752 0.39391 0.31771 0.02223  0.02755  0.07838  202 PRO A CA  
1541 C C   . PRO A 202 ? 0.37923 0.38287 0.33748 0.04562  -0.00350 0.01991  202 PRO A C   
1542 O O   . PRO A 202 ? 0.34156 0.37118 0.32652 0.00009  0.00001  0.00089  202 PRO A O   
1543 C CB  . PRO A 202 ? 0.35301 0.41104 0.29665 -0.00305 0.04384  0.11516  202 PRO A CB  
1544 C CG  . PRO A 202 ? 0.39114 0.43061 0.28397 0.03164  0.04423  0.13957  202 PRO A CG  
1545 C CD  . PRO A 202 ? 0.35983 0.42673 0.28376 0.02337  0.05138  0.12033  202 PRO A CD  
1546 N N   . LYS A 203 ? 0.42397 0.38360 0.37751 0.08914  -0.03004 -0.00268 203 LYS A N   
1547 C CA  . LYS A 203 ? 0.46755 0.41952 0.42800 0.08163  -0.01977 -0.02260 203 LYS A CA  
1548 C C   . LYS A 203 ? 0.42621 0.42523 0.42672 0.04961  -0.03016 -0.00056 203 LYS A C   
1549 O O   . LYS A 203 ? 0.40580 0.44062 0.42615 0.00982  0.00511  0.02728  203 LYS A O   
1550 C CB  . LYS A 203 ? 0.52466 0.43705 0.49964 0.10135  0.00364  -0.03229 203 LYS A CB  
1551 C CG  . LYS A 203 ? 0.60681 0.47398 0.54538 0.07120  0.04084  -0.04903 203 LYS A CG  
1552 C CD  . LYS A 203 ? 0.65448 0.49463 0.57289 0.04943  0.07494  -0.06151 203 LYS A CD  
1553 C CE  . LYS A 203 ? 0.65235 0.50563 0.59166 0.02022  0.09894  -0.03873 203 LYS A CE  
1554 N NZ  . LYS A 203 ? 0.62742 0.49737 0.59761 -0.01588 0.13425  -0.00433 203 LYS A NZ  
1555 N N   . HIS A 204 ? 0.39809 0.41892 0.42223 0.06260  -0.05821 0.01205  204 HIS A N   
1556 C CA  . HIS A 204 ? 0.43373 0.43933 0.41811 0.05502  -0.05783 0.03116  204 HIS A CA  
1557 C C   . HIS A 204 ? 0.45120 0.47398 0.36900 0.06310  -0.08423 0.04768  204 HIS A C   
1558 O O   . HIS A 204 ? 0.55990 0.54610 0.35625 0.08885  -0.11401 0.05870  204 HIS A O   
1559 C CB  . HIS A 204 ? 0.48756 0.44097 0.47073 0.02349  -0.01440 0.03834  204 HIS A CB  
1560 C CG  . HIS A 204 ? 0.56737 0.46689 0.52492 -0.00030 -0.00162 0.02222  204 HIS A CG  
1561 N ND1 . HIS A 204 ? 0.61713 0.46928 0.55598 0.00510  -0.01239 0.01182  204 HIS A ND1 
1562 C CD2 . HIS A 204 ? 0.60202 0.47672 0.53500 -0.00503 -0.00719 -0.00218 204 HIS A CD2 
1563 C CE1 . HIS A 204 ? 0.63258 0.46238 0.55854 -0.00065 -0.03111 -0.01076 204 HIS A CE1 
1564 N NE2 . HIS A 204 ? 0.63450 0.46765 0.54895 -0.01087 -0.03402 -0.01462 204 HIS A NE2 
1565 N N   . HIS A 205 ? 0.39120 0.44375 0.34081 0.02046  -0.05058 0.02876  205 HIS A N   
1566 C CA  . HIS A 205 ? 0.31798 0.45468 0.31124 0.00030  -0.02743 0.01248  205 HIS A CA  
1567 C C   . HIS A 205 ? 0.32125 0.48862 0.27849 0.02527  -0.02971 0.00405  205 HIS A C   
1568 O O   . HIS A 205 ? 0.33632 0.54052 0.26461 0.02637  -0.01171 0.01378  205 HIS A O   
1569 C CB  . HIS A 205 ? 0.29099 0.44692 0.33475 0.00663  -0.00290 0.01735  205 HIS A CB  
1570 C CG  . HIS A 205 ? 0.24946 0.44199 0.37039 0.00633  0.01330  0.01814  205 HIS A CG  
1571 N ND1 . HIS A 205 ? 0.27172 0.44887 0.38373 -0.00263 0.01653  0.00087  205 HIS A ND1 
1572 C CD2 . HIS A 205 ? 0.25969 0.43077 0.40319 0.02903  0.02403  0.02217  205 HIS A CD2 
1573 C CE1 . HIS A 205 ? 0.30739 0.44149 0.40150 0.00420  0.01965  0.01269  205 HIS A CE1 
1574 N NE2 . HIS A 205 ? 0.29806 0.42188 0.40668 0.04693  0.04428  0.02960  205 HIS A NE2 
1575 N N   . VAL A 206 ? 0.33426 0.46157 0.27879 0.05749  -0.02847 0.00669  206 VAL A N   
1576 C CA  . VAL A 206 ? 0.35039 0.44255 0.30412 0.01901  -0.01669 0.02054  206 VAL A CA  
1577 C C   . VAL A 206 ? 0.30278 0.44958 0.29812 0.04176  0.00138  0.02633  206 VAL A C   
1578 O O   . VAL A 206 ? 0.34877 0.48501 0.30919 0.04057  0.00249  0.00633  206 VAL A O   
1579 C CB  . VAL A 206 ? 0.41111 0.43454 0.32987 0.00738  -0.04268 0.03783  206 VAL A CB  
1580 C CG1 . VAL A 206 ? 0.43021 0.46237 0.33664 -0.03995 -0.04065 0.05148  206 VAL A CG1 
1581 C CG2 . VAL A 206 ? 0.43157 0.42369 0.33236 0.05218  -0.03363 0.02687  206 VAL A CG2 
1582 N N   . VAL A 207 ? 0.25867 0.42673 0.28860 0.04593  -0.01858 0.04481  207 VAL A N   
1583 C CA  . VAL A 207 ? 0.26040 0.42098 0.27871 0.04778  -0.04928 0.03042  207 VAL A CA  
1584 C C   . VAL A 207 ? 0.26171 0.43795 0.28023 0.05459  -0.04160 0.01134  207 VAL A C   
1585 O O   . VAL A 207 ? 0.31728 0.41096 0.28009 0.07722  -0.01579 -0.01103 207 VAL A O   
1586 C CB  . VAL A 207 ? 0.33183 0.41825 0.29263 0.04440  -0.04367 0.01616  207 VAL A CB  
1587 C CG1 . VAL A 207 ? 0.41379 0.40384 0.29218 0.07616  0.00299  0.00643  207 VAL A CG1 
1588 C CG2 . VAL A 207 ? 0.33435 0.44153 0.30555 0.01426  -0.05019 0.00261  207 VAL A CG2 
1589 N N   . SER A 208 ? 0.28277 0.44707 0.29819 0.04037  -0.06792 0.00848  208 SER A N   
1590 C CA  . SER A 208 ? 0.28609 0.46049 0.35048 -0.00462 -0.04981 0.00797  208 SER A CA  
1591 C C   . SER A 208 ? 0.30904 0.46121 0.34902 0.00351  -0.01467 0.01918  208 SER A C   
1592 O O   . SER A 208 ? 0.32228 0.49088 0.36253 -0.01039 0.00203  0.02322  208 SER A O   
1593 C CB  . SER A 208 ? 0.30351 0.50691 0.42421 -0.00509 -0.09305 0.01498  208 SER A CB  
1594 O OG  . SER A 208 ? 0.44497 0.56166 0.48792 -0.04785 -0.05648 0.00316  208 SER A OG  
1595 N N   . LEU A 209 ? 0.29597 0.42854 0.34371 0.02628  -0.01514 0.03605  209 LEU A N   
1596 C CA  . LEU A 209 ? 0.26688 0.41784 0.35568 0.04165  -0.02896 0.03758  209 LEU A CA  
1597 C C   . LEU A 209 ? 0.26700 0.44717 0.40723 0.04561  -0.05168 0.00701  209 LEU A C   
1598 O O   . LEU A 209 ? 0.28669 0.45630 0.44242 0.05458  -0.03042 0.01924  209 LEU A O   
1599 C CB  . LEU A 209 ? 0.24475 0.39721 0.32014 0.07183  -0.00547 0.05648  209 LEU A CB  
1600 C CG  . LEU A 209 ? 0.28335 0.40289 0.32874 0.05645  0.00173  0.05865  209 LEU A CG  
1601 C CD1 . LEU A 209 ? 0.33302 0.39533 0.35900 0.04472  0.00736  0.06734  209 LEU A CD1 
1602 C CD2 . LEU A 209 ? 0.33678 0.40965 0.33149 0.02359  -0.02838 0.05657  209 LEU A CD2 
1603 N N   . GLN A 210 ? 0.29531 0.46175 0.43359 0.02231  -0.10108 -0.01987 210 GLN A N   
1604 C CA  . GLN A 210 ? 0.32084 0.47969 0.48000 0.04920  -0.11454 -0.01018 210 GLN A CA  
1605 C C   . GLN A 210 ? 0.31231 0.48229 0.48114 0.05474  -0.09821 -0.02064 210 GLN A C   
1606 O O   . GLN A 210 ? 0.33681 0.45905 0.48371 0.02936  -0.12674 -0.00723 210 GLN A O   
1607 C CB  . GLN A 210 ? 0.38922 0.47732 0.51604 0.03631  -0.13336 0.00687  210 GLN A CB  
1608 C CG  . GLN A 210 ? 0.40980 0.47080 0.55390 0.03092  -0.12149 0.00387  210 GLN A CG  
1609 C CD  . GLN A 210 ? 0.46442 0.48507 0.59545 0.05256  -0.10915 -0.00269 210 GLN A CD  
1610 O OE1 . GLN A 210 ? 0.48365 0.50347 0.60983 0.05020  -0.11047 -0.00294 210 GLN A OE1 
1611 N NE2 . GLN A 210 ? 0.49740 0.47501 0.61316 0.08810  -0.09421 0.00461  210 GLN A NE2 
1612 N N   . PRO A 211 ? 0.32516 0.49880 0.48779 0.03439  -0.03460 -0.04272 211 PRO A N   
1613 C CA  . PRO A 211 ? 0.35353 0.50357 0.47947 0.03414  -0.03383 -0.05830 211 PRO A CA  
1614 C C   . PRO A 211 ? 0.41204 0.51422 0.48790 0.04779  -0.06885 -0.04625 211 PRO A C   
1615 O O   . PRO A 211 ? 0.40845 0.52547 0.49597 0.00702  -0.05371 -0.02633 211 PRO A O   
1616 C CB  . PRO A 211 ? 0.34905 0.49320 0.48846 -0.00859 -0.01905 -0.06411 211 PRO A CB  
1617 C CG  . PRO A 211 ? 0.37368 0.50092 0.51044 0.00035  -0.01464 -0.03418 211 PRO A CG  
1618 C CD  . PRO A 211 ? 0.33545 0.51760 0.50735 0.01866  -0.01179 -0.02560 211 PRO A CD  
1619 N N   . VAL A 212 ? 0.45404 0.51406 0.49531 0.04494  -0.10138 -0.05313 212 VAL A N   
1620 C CA  . VAL A 212 ? 0.48521 0.52870 0.50106 0.03958  -0.10012 -0.08638 212 VAL A CA  
1621 C C   . VAL A 212 ? 0.50374 0.59802 0.53056 0.01395  -0.08242 -0.06766 212 VAL A C   
1622 O O   . VAL A 212 ? 0.51306 0.62629 0.53392 0.03247  -0.10855 -0.05971 212 VAL A O   
1623 C CB  . VAL A 212 ? 0.46769 0.47385 0.47790 0.03970  -0.11237 -0.11688 212 VAL A CB  
1624 C CG1 . VAL A 212 ? 0.47614 0.47283 0.47932 0.02796  -0.08799 -0.12653 212 VAL A CG1 
1625 C CG2 . VAL A 212 ? 0.39417 0.44877 0.46122 0.02727  -0.13222 -0.12434 212 VAL A CG2 
1626 N N   . ASN A 213 ? 0.51839 0.63028 0.55839 -0.01926 -0.03777 -0.04270 213 ASN A N   
1627 C CA  . ASN A 213 ? 0.54928 0.63365 0.59724 -0.01711 -0.02335 -0.02505 213 ASN A CA  
1628 C C   . ASN A 213 ? 0.53178 0.63671 0.63254 -0.03078 -0.04265 -0.00713 213 ASN A C   
1629 O O   . ASN A 213 ? 0.59214 0.66529 0.64818 -0.05280 -0.04495 -0.01234 213 ASN A O   
1630 C CB  . ASN A 213 ? 0.59383 0.62041 0.60383 0.00399  0.02559  -0.02324 213 ASN A CB  
1631 C CG  . ASN A 213 ? 0.65706 0.63239 0.61778 0.03454  0.06993  -0.02963 213 ASN A CG  
1632 O OD1 . ASN A 213 ? 0.66775 0.62998 0.62649 0.05237  0.07810  -0.04057 213 ASN A OD1 
1633 N ND2 . ASN A 213 ? 0.68439 0.64851 0.62187 0.04524  0.09250  -0.02387 213 ASN A ND2 
1634 N N   . ASP A 214 ? 0.50863 0.60990 0.65053 -0.05110 -0.04827 0.00547  214 ASP A N   
1635 C CA  . ASP A 214 ? 0.50185 0.58532 0.66848 -0.06080 -0.04806 0.00101  214 ASP A CA  
1636 C C   . ASP A 214 ? 0.42597 0.56306 0.63271 -0.04992 -0.05161 -0.02415 214 ASP A C   
1637 O O   . ASP A 214 ? 0.39980 0.56993 0.64452 -0.05666 -0.06319 -0.02014 214 ASP A O   
1638 C CB  . ASP A 214 ? 0.57021 0.57740 0.70949 -0.06210 -0.06217 0.03079  214 ASP A CB  
1639 C CG  . ASP A 214 ? 0.65975 0.57532 0.75542 -0.08107 -0.07427 0.05380  214 ASP A CG  
1640 O OD1 . ASP A 214 ? 0.69213 0.58515 0.77168 -0.05694 -0.07161 0.07244  214 ASP A OD1 
1641 O OD2 . ASP A 214 ? 0.69224 0.57190 0.77933 -0.12074 -0.08256 0.04892  214 ASP A OD2 
1642 N N   . LYS A 215 ? 0.44519 0.54871 0.57782 -0.01279 -0.04749 -0.03909 215 LYS A N   
1643 C CA  . LYS A 215 ? 0.48192 0.56334 0.53221 0.02553  -0.03781 -0.04927 215 LYS A CA  
1644 C C   . LYS A 215 ? 0.46846 0.57121 0.47825 0.01774  -0.07654 -0.08047 215 LYS A C   
1645 O O   . LYS A 215 ? 0.49212 0.57618 0.46723 0.00520  -0.06558 -0.08408 215 LYS A O   
1646 C CB  . LYS A 215 ? 0.52003 0.57831 0.55675 0.04806  -0.00246 -0.04452 215 LYS A CB  
1647 C CG  . LYS A 215 ? 0.57387 0.58987 0.58287 0.04048  0.02832  -0.04922 215 LYS A CG  
1648 C CD  . LYS A 215 ? 0.61628 0.61107 0.60578 0.02032  0.06268  -0.05679 215 LYS A CD  
1649 C CE  . LYS A 215 ? 0.65653 0.62341 0.62202 -0.00057 0.07440  -0.06536 215 LYS A CE  
1650 N NZ  . LYS A 215 ? 0.70125 0.62554 0.63128 -0.00656 0.08713  -0.06668 215 LYS A NZ  
1651 N N   . ASP A 216 ? 0.41383 0.59333 0.45766 -0.00828 -0.12832 -0.08820 216 ASP A N   
1652 C CA  . ASP A 216 ? 0.35660 0.61324 0.46367 -0.03978 -0.14599 -0.08721 216 ASP A CA  
1653 C C   . ASP A 216 ? 0.34727 0.63996 0.45822 -0.02424 -0.12024 -0.08477 216 ASP A C   
1654 O O   . ASP A 216 ? 0.35212 0.66164 0.47681 -0.01986 -0.09673 -0.08600 216 ASP A O   
1655 C CB  . ASP A 216 ? 0.32932 0.58735 0.48491 -0.08449 -0.14132 -0.07480 216 ASP A CB  
1656 C CG  . ASP A 216 ? 0.36567 0.58015 0.51479 -0.05411 -0.15111 -0.06641 216 ASP A CG  
1657 O OD1 . ASP A 216 ? 0.36988 0.57395 0.52310 -0.01029 -0.16342 -0.06458 216 ASP A OD1 
1658 O OD2 . ASP A 216 ? 0.39071 0.57904 0.53364 -0.07499 -0.14790 -0.06561 216 ASP A OD2 
1659 N N   . PHE A 217 ? 0.31458 0.63526 0.42748 -0.02659 -0.09389 -0.06854 217 PHE A N   
1660 C CA  . PHE A 217 ? 0.25528 0.62662 0.39020 0.00298  -0.04225 -0.05843 217 PHE A CA  
1661 C C   . PHE A 217 ? 0.23464 0.61003 0.39438 0.01974  -0.02482 -0.05839 217 PHE A C   
1662 O O   . PHE A 217 ? 0.22768 0.64441 0.41557 0.03422  -0.01638 -0.06254 217 PHE A O   
1663 C CB  . PHE A 217 ? 0.27865 0.61764 0.36666 0.02628  -0.00544 -0.04393 217 PHE A CB  
1664 C CG  . PHE A 217 ? 0.33947 0.61836 0.35031 0.05771  -0.03335 -0.01782 217 PHE A CG  
1665 C CD1 . PHE A 217 ? 0.34589 0.61060 0.35240 0.06149  -0.04246 -0.00697 217 PHE A CD1 
1666 C CD2 . PHE A 217 ? 0.34535 0.61134 0.34981 0.07241  -0.02475 -0.00320 217 PHE A CD2 
1667 C CE1 . PHE A 217 ? 0.33677 0.61403 0.35597 0.03897  -0.03377 0.00454  217 PHE A CE1 
1668 C CE2 . PHE A 217 ? 0.37065 0.61804 0.35942 0.05819  -0.00474 0.00869  217 PHE A CE2 
1669 C CZ  . PHE A 217 ? 0.34003 0.61120 0.36706 0.06390  -0.01719 0.00297  217 PHE A CZ  
1670 N N   . GLN A 218 ? 0.23586 0.54935 0.37438 -0.00041 -0.02224 -0.05322 218 GLN A N   
1671 C CA  . GLN A 218 ? 0.25497 0.54266 0.35751 0.02306  -0.01158 -0.05892 218 GLN A CA  
1672 C C   . GLN A 218 ? 0.26020 0.56563 0.34509 0.05873  -0.00454 -0.06114 218 GLN A C   
1673 O O   . GLN A 218 ? 0.24720 0.60516 0.36855 0.08495  0.00391  -0.07885 218 GLN A O   
1674 C CB  . GLN A 218 ? 0.31920 0.52977 0.39682 0.04931  0.00485  -0.06003 218 GLN A CB  
1675 C CG  . GLN A 218 ? 0.38080 0.53562 0.44990 0.01680  0.03160  -0.06978 218 GLN A CG  
1676 C CD  . GLN A 218 ? 0.40278 0.53241 0.48149 -0.05535 0.07210  -0.07544 218 GLN A CD  
1677 O OE1 . GLN A 218 ? 0.40472 0.54543 0.49216 -0.07535 0.09351  -0.07625 218 GLN A OE1 
1678 N NE2 . GLN A 218 ? 0.43788 0.53498 0.49746 -0.07864 0.08445  -0.08172 218 GLN A NE2 
1679 N N   . ILE A 219 ? 0.28195 0.54253 0.31453 0.03595  0.00913  -0.05118 219 ILE A N   
1680 C CA  . ILE A 219 ? 0.33789 0.54073 0.30213 0.02880  -0.01538 -0.06184 219 ILE A CA  
1681 C C   . ILE A 219 ? 0.32039 0.58937 0.31231 0.02754  0.00485  -0.07716 219 ILE A C   
1682 O O   . ILE A 219 ? 0.29289 0.63275 0.33644 0.01024  0.00448  -0.08493 219 ILE A O   
1683 C CB  . ILE A 219 ? 0.41165 0.51159 0.31670 0.04497  -0.02084 -0.07474 219 ILE A CB  
1684 C CG1 . ILE A 219 ? 0.38524 0.49301 0.31604 0.07048  -0.00938 -0.04633 219 ILE A CG1 
1685 C CG2 . ILE A 219 ? 0.51130 0.50771 0.32482 0.05874  -0.02306 -0.11195 219 ILE A CG2 
1686 C CD1 . ILE A 219 ? 0.39950 0.50692 0.33189 0.07992  0.01306  -0.04833 219 ILE A CD1 
1687 N N   . SER A 220 ? 0.33622 0.58403 0.29169 0.04402  0.02082  -0.06936 220 SER A N   
1688 C CA  . SER A 220 ? 0.38123 0.62366 0.30103 0.06976  0.03347  -0.05546 220 SER A CA  
1689 C C   . SER A 220 ? 0.33679 0.62610 0.31351 0.03803  0.04231  -0.06525 220 SER A C   
1690 O O   . SER A 220 ? 0.35152 0.65733 0.36097 -0.05924 0.05636  -0.06661 220 SER A O   
1691 C CB  . SER A 220 ? 0.55600 0.69863 0.30489 0.16900  0.04341  -0.03763 220 SER A CB  
1692 O OG  . SER A 220 ? 0.71999 0.76397 0.29707 0.19412  0.02390  -0.02173 220 SER A OG  
1693 N N   . VAL A 221 ? 0.28156 0.58224 0.26923 0.08911  0.04188  -0.08899 221 VAL A N   
1694 C CA  . VAL A 221 ? 0.29594 0.58435 0.28383 0.04441  0.03463  -0.06545 221 VAL A CA  
1695 C C   . VAL A 221 ? 0.31116 0.58241 0.29382 0.01485  0.07746  -0.05753 221 VAL A C   
1696 O O   . VAL A 221 ? 0.28193 0.58967 0.30091 0.00482  0.07141  -0.09349 221 VAL A O   
1697 C CB  . VAL A 221 ? 0.34902 0.60103 0.32977 0.03459  -0.00562 -0.02961 221 VAL A CB  
1698 C CG1 . VAL A 221 ? 0.35421 0.57861 0.35869 0.00428  -0.03427 -0.01588 221 VAL A CG1 
1699 C CG2 . VAL A 221 ? 0.37698 0.61951 0.33606 0.04473  0.01351  -0.01683 221 VAL A CG2 
1700 N N   . ASP A 222 ? 0.29573 0.54674 0.30930 -0.01454 0.11361  -0.02359 222 ASP A N   
1701 C CA  . ASP A 222 ? 0.32964 0.51857 0.34099 0.06524  0.11284  -0.03780 222 ASP A CA  
1702 C C   . ASP A 222 ? 0.33528 0.55772 0.40535 0.06961  0.10971  -0.03090 222 ASP A C   
1703 O O   . ASP A 222 ? 0.40835 0.54609 0.44184 0.09703  0.04582  -0.07006 222 ASP A O   
1704 C CB  . ASP A 222 ? 0.33803 0.46500 0.32145 0.12370  0.08562  -0.03127 222 ASP A CB  
1705 C CG  . ASP A 222 ? 0.32912 0.45736 0.29294 0.14541  0.07620  -0.01555 222 ASP A CG  
1706 O OD1 . ASP A 222 ? 0.33666 0.46914 0.26510 0.10333  0.02777  -0.01150 222 ASP A OD1 
1707 O OD2 . ASP A 222 ? 0.36933 0.43686 0.29690 0.17052  0.05700  0.01227  222 ASP A OD2 
1708 N N   . HIS A 223 ? 0.29721 0.59970 0.48010 -0.00720 0.04970  0.02016  223 HIS A N   
1709 C CA  A HIS A 223 ? 0.38141 0.59177 0.54100 -0.01650 0.03057  0.00801  223 HIS A CA  
1710 C CA  B HIS A 223 ? 0.38903 0.59488 0.53357 -0.06178 -0.00210 0.02542  223 HIS A CA  
1711 C C   . HIS A 223 ? 0.41636 0.60451 0.54963 -0.05508 0.03100  0.00907  223 HIS A C   
1712 O O   . HIS A 223 ? 0.53879 0.62622 0.58785 -0.09891 0.04138  0.00326  223 HIS A O   
1713 C CB  A HIS A 223 ? 0.42937 0.56125 0.59384 0.06855  0.02413  -0.02941 223 HIS A CB  
1714 C CB  B HIS A 223 ? 0.48472 0.57170 0.56992 -0.06720 -0.07140 0.02235  223 HIS A CB  
1715 C CG  A HIS A 223 ? 0.47077 0.55722 0.63493 0.09438  0.00515  -0.06152 223 HIS A CG  
1716 C CG  B HIS A 223 ? 0.50612 0.55355 0.58936 -0.08977 -0.11341 0.00089  223 HIS A CG  
1717 N ND1 A HIS A 223 ? 0.46092 0.54862 0.64719 0.09190  -0.02315 -0.07722 223 HIS A ND1 
1718 N ND1 B HIS A 223 ? 0.47278 0.55293 0.58606 -0.11389 -0.13277 -0.01196 223 HIS A ND1 
1719 C CD2 A HIS A 223 ? 0.49817 0.55433 0.65144 0.08775  0.00306  -0.06794 223 HIS A CD2 
1720 C CD2 B HIS A 223 ? 0.51385 0.54953 0.59639 -0.08885 -0.12238 -0.00393 223 HIS A CD2 
1721 C CE1 A HIS A 223 ? 0.48177 0.54260 0.65432 0.07927  -0.03073 -0.07876 223 HIS A CE1 
1722 C CE1 B HIS A 223 ? 0.48810 0.55004 0.58854 -0.09778 -0.13880 -0.01907 223 HIS A CE1 
1723 N NE2 A HIS A 223 ? 0.51155 0.54936 0.65684 0.08274  -0.01156 -0.07535 223 HIS A NE2 
1724 N NE2 B HIS A 223 ? 0.52126 0.55006 0.59552 -0.08789 -0.13430 -0.01123 223 HIS A NE2 
1725 N N   . LEU A 224 ? 0.38264 0.60005 0.51500 -0.03712 0.04822  -0.02829 224 LEU A N   
1726 C CA  . LEU A 224 ? 0.39605 0.59270 0.49914 -0.01979 0.04550  -0.09380 224 LEU A CA  
1727 C C   . LEU A 224 ? 0.47673 0.63819 0.48315 -0.05878 0.07264  -0.12863 224 LEU A C   
1728 O O   . LEU A 224 ? 0.60268 0.62580 0.45452 -0.09239 0.10098  -0.16686 224 LEU A O   
1729 C CB  . LEU A 224 ? 0.42104 0.57413 0.54821 0.01722  0.04538  -0.10760 224 LEU A CB  
1730 C CG  . LEU A 224 ? 0.58245 0.57650 0.62314 0.04478  0.06057  -0.10328 224 LEU A CG  
1731 C CD1 . LEU A 224 ? 0.63370 0.60692 0.64724 0.04345  0.09358  -0.10232 224 LEU A CD1 
1732 C CD2 . LEU A 224 ? 0.64131 0.54645 0.64902 0.08570  0.04315  -0.10112 224 LEU A CD2 
1733 N N   . SER A 225 ? 0.41349 0.68786 0.49282 -0.01559 0.07312  -0.09899 225 SER A N   
1734 C CA  . SER A 225 ? 0.40486 0.74986 0.50566 0.05395  0.08069  -0.05541 225 SER A CA  
1735 C C   . SER A 225 ? 0.36699 0.78739 0.50038 0.04714  0.07158  -0.07207 225 SER A C   
1736 O O   . SER A 225 ? 0.42062 0.84781 0.49044 -0.01211 0.06936  -0.07957 225 SER A O   
1737 C CB  . SER A 225 ? 0.49911 0.76359 0.52837 0.14558  0.09970  -0.00483 225 SER A CB  
1738 O OG  . SER A 225 ? 0.54377 0.77934 0.53362 0.20962  0.10402  0.01970  225 SER A OG  
1739 N N   . ILE A 226 ? 0.36827 0.74781 0.51833 0.07392  0.04063  -0.10023 226 ILE A N   
1740 C CA  . ILE A 226 ? 0.43027 0.69525 0.54955 0.08050  0.00660  -0.12993 226 ILE A CA  
1741 C C   . ILE A 226 ? 0.33367 0.66770 0.55693 0.01289  -0.01876 -0.15947 226 ILE A C   
1742 O O   . ILE A 226 ? 0.35411 0.64268 0.55109 -0.00081 -0.04383 -0.17600 226 ILE A O   
1743 C CB  . ILE A 226 ? 0.63328 0.67905 0.58230 0.13508  0.01817  -0.11383 226 ILE A CB  
1744 C CG1 . ILE A 226 ? 0.76564 0.65107 0.60106 0.14894  0.00022  -0.09638 226 ILE A CG1 
1745 C CG2 . ILE A 226 ? 0.67142 0.68676 0.58471 0.12906  0.03045  -0.11405 226 ILE A CG2 
1746 C CD1 . ILE A 226 ? 0.82521 0.62587 0.61376 0.14680  -0.01694 -0.09010 226 ILE A CD1 
1747 N N   . LEU A 227 ? 0.28018 0.67449 0.57610 -0.03230 0.00268  -0.16402 227 LEU A N   
1748 C CA  . LEU A 227 ? 0.31439 0.70798 0.59856 -0.03068 0.03049  -0.15773 227 LEU A CA  
1749 C C   . LEU A 227 ? 0.31876 0.77464 0.62025 0.05392  0.02003  -0.16933 227 LEU A C   
1750 O O   . LEU A 227 ? 0.30489 0.84521 0.62206 0.12533  0.00995  -0.18052 227 LEU A O   
1751 C CB  . LEU A 227 ? 0.34030 0.68041 0.61274 -0.09149 0.05931  -0.15015 227 LEU A CB  
1752 C CG  . LEU A 227 ? 0.36867 0.64955 0.63308 -0.10398 0.07120  -0.13589 227 LEU A CG  
1753 C CD1 . LEU A 227 ? 0.37275 0.65103 0.64382 -0.08692 0.07098  -0.12266 227 LEU A CD1 
1754 C CD2 . LEU A 227 ? 0.40705 0.63033 0.63901 -0.14327 0.08305  -0.11989 227 LEU A CD2 
1755 N N   . HIS A 228 ? 0.31766 0.76917 0.64657 0.03912  0.00912  -0.15771 228 HIS A N   
1756 C CA  . HIS A 228 ? 0.34494 0.75730 0.66858 0.03947  -0.00410 -0.12737 228 HIS A CA  
1757 C C   . HIS A 228 ? 0.29841 0.72345 0.65053 0.08158  -0.05142 -0.10910 228 HIS A C   
1758 O O   . HIS A 228 ? 0.30073 0.71566 0.63413 0.12232  -0.08942 -0.11471 228 HIS A O   
1759 C CB  . HIS A 228 ? 0.43822 0.79680 0.71223 0.01156  0.01493  -0.10660 228 HIS A CB  
1760 C CG  . HIS A 228 ? 0.51543 0.83672 0.75645 0.01829  0.02786  -0.07433 228 HIS A CG  
1761 N ND1 . HIS A 228 ? 0.56385 0.84981 0.77623 0.02660  0.03058  -0.05865 228 HIS A ND1 
1762 C CD2 . HIS A 228 ? 0.56308 0.85358 0.77911 0.03071  0.03074  -0.05226 228 HIS A CD2 
1763 C CE1 . HIS A 228 ? 0.59256 0.86224 0.79009 0.04488  0.04136  -0.04843 228 HIS A CE1 
1764 N NE2 . HIS A 228 ? 0.58738 0.86095 0.78886 0.04637  0.03387  -0.04590 228 HIS A NE2 
1765 N N   . ARG A 229 ? 0.31443 0.71331 0.66522 0.06109  -0.04627 -0.08126 229 ARG A N   
1766 C CA  . ARG A 229 ? 0.34604 0.70338 0.67920 0.03149  -0.06421 -0.03261 229 ARG A CA  
1767 C C   . ARG A 229 ? 0.35525 0.68760 0.69587 0.06784  -0.10308 0.01784  229 ARG A C   
1768 O O   . ARG A 229 ? 0.35430 0.65494 0.69909 0.12226  -0.13128 0.00844  229 ARG A O   
1769 C CB  . ARG A 229 ? 0.36124 0.68957 0.68365 0.00224  -0.03422 -0.03612 229 ARG A CB  
1770 C CG  . ARG A 229 ? 0.39529 0.67130 0.68782 -0.03408 -0.02338 -0.04474 229 ARG A CG  
1771 C CD  . ARG A 229 ? 0.46076 0.65998 0.69838 -0.04111 -0.04082 -0.04532 229 ARG A CD  
1772 N NE  . ARG A 229 ? 0.57170 0.67693 0.70869 -0.01782 -0.03707 -0.04592 229 ARG A NE  
1773 C CZ  . ARG A 229 ? 0.65168 0.68750 0.71998 0.00102  -0.02969 -0.05797 229 ARG A CZ  
1774 N NH1 . ARG A 229 ? 0.67659 0.68996 0.72372 0.00117  -0.03750 -0.06775 229 ARG A NH1 
1775 N NH2 . ARG A 229 ? 0.68448 0.69257 0.72635 0.01300  -0.01618 -0.06456 229 ARG A NH2 
1776 N N   . ASP A 230 ? 0.36676 0.71182 0.70674 0.03352  -0.11490 0.06574  230 ASP A N   
1777 C CA  . ASP A 230 ? 0.48378 0.73963 0.72115 0.03489  -0.14285 0.08924  230 ASP A CA  
1778 C C   . ASP A 230 ? 0.47356 0.66640 0.69319 0.01803  -0.17890 0.08777  230 ASP A C   
1779 O O   . ASP A 230 ? 0.49892 0.65439 0.70105 -0.01981 -0.19217 0.12181  230 ASP A O   
1780 C CB  . ASP A 230 ? 0.56793 0.83139 0.75659 0.06925  -0.12150 0.10125  230 ASP A CB  
1781 C CG  . ASP A 230 ? 0.69003 0.91953 0.79198 0.05881  -0.10583 0.08284  230 ASP A CG  
1782 O OD1 . ASP A 230 ? 0.72979 0.93895 0.80659 0.04929  -0.11587 0.06229  230 ASP A OD1 
1783 O OD2 . ASP A 230 ? 0.73699 0.96517 0.80115 0.05222  -0.08075 0.08169  230 ASP A OD2 
1784 N N   . VAL A 231 ? 0.44572 0.60921 0.64751 0.03031  -0.17240 0.06251  231 VAL A N   
1785 C CA  . VAL A 231 ? 0.36791 0.54780 0.61617 0.01357  -0.13938 0.04910  231 VAL A CA  
1786 C C   . VAL A 231 ? 0.40229 0.53851 0.60536 0.03283  -0.11409 0.02618  231 VAL A C   
1787 O O   . VAL A 231 ? 0.41853 0.58200 0.61904 0.05743  -0.09490 0.04379  231 VAL A O   
1788 C CB  . VAL A 231 ? 0.36483 0.52824 0.62138 0.00684  -0.13421 0.05604  231 VAL A CB  
1789 C CG1 . VAL A 231 ? 0.33074 0.50184 0.62133 0.00449  -0.12318 0.05111  231 VAL A CG1 
1790 C CG2 . VAL A 231 ? 0.40279 0.54243 0.62461 0.01838  -0.16432 0.06892  231 VAL A CG2 
1791 N N   . GLN A 232 ? 0.40380 0.50141 0.58298 0.03063  -0.12071 -0.01076 232 GLN A N   
1792 C CA  . GLN A 232 ? 0.45524 0.49973 0.56228 0.02847  -0.13211 -0.02118 232 GLN A CA  
1793 C C   . GLN A 232 ? 0.45562 0.55396 0.52559 0.03692  -0.14309 -0.02238 232 GLN A C   
1794 O O   . GLN A 232 ? 0.51349 0.60103 0.50949 0.02168  -0.17762 -0.02832 232 GLN A O   
1795 C CB  . GLN A 232 ? 0.49751 0.46374 0.57469 0.02901  -0.11712 -0.02110 232 GLN A CB  
1796 N N   . GLU A 233 ? 0.41881 0.54128 0.50313 0.06705  -0.10466 -0.01265 233 GLU A N   
1797 C CA  . GLU A 233 ? 0.38839 0.52904 0.48847 0.05695  -0.05592 -0.00594 233 GLU A CA  
1798 C C   . GLU A 233 ? 0.29909 0.50051 0.46442 0.05055  -0.04806 0.01427  233 GLU A C   
1799 O O   . GLU A 233 ? 0.31846 0.47498 0.47509 0.06645  -0.04181 0.02351  233 GLU A O   
1800 C CB  . GLU A 233 ? 0.44939 0.53083 0.50219 0.07197  -0.02407 0.00609  233 GLU A CB  
1801 C CG  . GLU A 233 ? 0.47504 0.53310 0.52811 0.12596  -0.01380 0.02266  233 GLU A CG  
1802 C CD  . GLU A 233 ? 0.49023 0.52750 0.55933 0.15629  -0.00981 0.05268  233 GLU A CD  
1803 O OE1 . GLU A 233 ? 0.47497 0.54116 0.57125 0.15447  0.00589  0.04669  233 GLU A OE1 
1804 O OE2 . GLU A 233 ? 0.49968 0.52427 0.57238 0.15332  -0.02644 0.07212  233 GLU A OE2 
1805 N N   . ILE A 234 ? 0.27345 0.49470 0.43227 0.02014  -0.03163 0.01320  234 ILE A N   
1806 C CA  . ILE A 234 ? 0.26752 0.49016 0.40960 0.01606  -0.02556 -0.00261 234 ILE A CA  
1807 C C   . ILE A 234 ? 0.28620 0.47954 0.40074 0.02995  0.00571  0.00517  234 ILE A C   
1808 O O   . ILE A 234 ? 0.30757 0.47824 0.42932 0.05390  0.04057  0.00403  234 ILE A O   
1809 C CB  . ILE A 234 ? 0.32144 0.48245 0.39218 0.02901  -0.05470 0.01205  234 ILE A CB  
1810 C CG1 . ILE A 234 ? 0.38130 0.46211 0.40882 0.07309  -0.03870 0.04029  234 ILE A CG1 
1811 C CG2 . ILE A 234 ? 0.37111 0.49555 0.37079 0.03824  -0.07874 0.01420  234 ILE A CG2 
1812 C CD1 . ILE A 234 ? 0.41299 0.45507 0.42302 0.09532  -0.02712 0.05353  234 ILE A CD1 
1813 N N   . ARG A 235 ? 0.26392 0.46574 0.35764 0.02402  -0.03415 0.01228  235 ARG A N   
1814 C CA  . ARG A 235 ? 0.27995 0.48888 0.34142 0.04226  -0.05644 0.00119  235 ARG A CA  
1815 C C   . ARG A 235 ? 0.29876 0.49271 0.30142 0.02285  -0.02670 -0.00386 235 ARG A C   
1816 O O   . ARG A 235 ? 0.30650 0.52238 0.30454 0.07800  -0.01078 -0.01722 235 ARG A O   
1817 C CB  . ARG A 235 ? 0.34757 0.52054 0.39734 0.10765  -0.03037 -0.00326 235 ARG A CB  
1818 C CG  . ARG A 235 ? 0.44097 0.56202 0.48137 0.11193  0.01405  0.01927  235 ARG A CG  
1819 C CD  . ARG A 235 ? 0.50601 0.57222 0.54088 0.07776  0.04427  0.07998  235 ARG A CD  
1820 N NE  . ARG A 235 ? 0.53066 0.58247 0.58266 0.05136  0.05121  0.12217  235 ARG A NE  
1821 C CZ  . ARG A 235 ? 0.60797 0.62334 0.60768 0.07703  0.01739  0.14071  235 ARG A CZ  
1822 N NH1 . ARG A 235 ? 0.60093 0.62972 0.60612 0.09108  0.00489  0.14585  235 ARG A NH1 
1823 N NH2 . ARG A 235 ? 0.64740 0.64153 0.61945 0.07699  0.02329  0.15607  235 ARG A NH2 
1824 N N   . TYR A 236 ? 0.29131 0.47374 0.27971 0.01816  -0.03638 0.01603  236 TYR A N   
1825 C CA  . TYR A 236 ? 0.28323 0.47033 0.28132 0.05327  -0.02894 0.02644  236 TYR A CA  
1826 C C   . TYR A 236 ? 0.29151 0.49225 0.26910 0.04888  -0.00251 0.00560  236 TYR A C   
1827 O O   . TYR A 236 ? 0.27720 0.52638 0.27356 0.07700  0.00159  -0.00348 236 TYR A O   
1828 C CB  . TYR A 236 ? 0.29827 0.44723 0.32136 0.07350  -0.02844 0.08015  236 TYR A CB  
1829 C CG  . TYR A 236 ? 0.34563 0.44685 0.39999 0.04764  -0.06340 0.10619  236 TYR A CG  
1830 C CD1 . TYR A 236 ? 0.32814 0.46053 0.44270 0.03431  -0.08580 0.13478  236 TYR A CD1 
1831 C CD2 . TYR A 236 ? 0.39958 0.43029 0.44406 0.04156  -0.06250 0.12107  236 TYR A CD2 
1832 C CE1 . TYR A 236 ? 0.34722 0.47604 0.47988 0.03271  -0.08201 0.14408  236 TYR A CE1 
1833 C CE2 . TYR A 236 ? 0.44727 0.44941 0.49702 0.05921  -0.07651 0.12887  236 TYR A CE2 
1834 C CZ  . TYR A 236 ? 0.42770 0.48101 0.52530 0.05066  -0.07829 0.15193  236 TYR A CZ  
1835 O OH  . TYR A 236 ? 0.52096 0.54250 0.58434 0.08803  -0.11553 0.16474  236 TYR A OH  
1836 N N   . GLU A 237 ? 0.29823 0.49465 0.26971 0.04566  0.00606  0.02750  237 GLU A N   
1837 C CA  . GLU A 237 ? 0.32779 0.44797 0.27855 0.05721  -0.00761 0.03100  237 GLU A CA  
1838 C C   . GLU A 237 ? 0.37318 0.40781 0.26785 0.04453  -0.00720 -0.00426 237 GLU A C   
1839 O O   . GLU A 237 ? 0.35184 0.37072 0.28417 0.07420  -0.00566 -0.00470 237 GLU A O   
1840 C CB  . GLU A 237 ? 0.35842 0.48570 0.32876 0.04448  -0.03278 0.05449  237 GLU A CB  
1841 C CG  . GLU A 237 ? 0.40002 0.50687 0.38152 0.06493  -0.03564 0.09478  237 GLU A CG  
1842 C CD  . GLU A 237 ? 0.44214 0.55310 0.42552 0.08431  -0.01942 0.13340  237 GLU A CD  
1843 O OE1 . GLU A 237 ? 0.46003 0.55162 0.42513 0.06966  0.02701  0.14581  237 GLU A OE1 
1844 O OE2 . GLU A 237 ? 0.45418 0.59044 0.43928 0.12733  -0.02629 0.13290  237 GLU A OE2 
1845 N N   . VAL A 238 ? 0.33530 0.39584 0.26179 0.04071  -0.01384 -0.04077 238 VAL A N   
1846 C CA  . VAL A 238 ? 0.31606 0.37429 0.26202 0.06280  -0.01258 -0.04179 238 VAL A CA  
1847 C C   . VAL A 238 ? 0.39197 0.41432 0.26994 0.07936  0.00648  -0.01788 238 VAL A C   
1848 O O   . VAL A 238 ? 0.40248 0.40366 0.28654 0.08894  -0.00781 -0.01783 238 VAL A O   
1849 C CB  . VAL A 238 ? 0.29984 0.32212 0.27002 0.06726  0.03485  -0.07345 238 VAL A CB  
1850 C CG1 . VAL A 238 ? 0.35773 0.30063 0.27742 0.03511  0.04635  -0.10356 238 VAL A CG1 
1851 C CG2 . VAL A 238 ? 0.30872 0.30664 0.28306 0.06437  0.04323  -0.05696 238 VAL A CG2 
1852 N N   . SER A 239 ? 0.43859 0.43882 0.26531 0.04801  0.02058  0.01092  239 SER A N   
1853 C CA  . SER A 239 ? 0.48718 0.43976 0.28122 0.07799  0.02736  0.00188  239 SER A CA  
1854 C C   . SER A 239 ? 0.53722 0.45563 0.31319 0.10341  0.05153  0.02952  239 SER A C   
1855 O O   . SER A 239 ? 0.55537 0.46326 0.33624 0.07674  0.07729  0.02060  239 SER A O   
1856 C CB  . SER A 239 ? 0.50764 0.46342 0.29342 0.11690  0.02537  -0.02056 239 SER A CB  
1857 O OG  . SER A 239 ? 0.54496 0.45809 0.31119 0.15205  0.01772  -0.02126 239 SER A OG  
1858 N N   . ALA A 240 ? 0.57497 0.45241 0.32582 0.12494  0.05113  0.05053  240 ALA A N   
1859 C CA  . ALA A 240 ? 0.60868 0.43327 0.33470 0.10928  0.03615  0.05391  240 ALA A CA  
1860 C C   . ALA A 240 ? 0.61625 0.43625 0.34553 0.10843  0.05841  0.03602  240 ALA A C   
1861 O O   . ALA A 240 ? 0.66611 0.44235 0.37065 0.10154  0.07562  0.01306  240 ALA A O   
1862 C CB  . ALA A 240 ? 0.64582 0.43395 0.33751 0.10641  0.01370  0.06855  240 ALA A CB  
1863 N N   . LYS A 241 ? 0.59553 0.43815 0.33280 0.11312  0.05223  0.05324  241 LYS A N   
1864 C CA  . LYS A 241 ? 0.56456 0.44810 0.32097 0.15762  0.05168  0.04568  241 LYS A CA  
1865 C C   . LYS A 241 ? 0.56033 0.46616 0.31384 0.14817  0.06094  0.03704  241 LYS A C   
1866 O O   . LYS A 241 ? 0.60057 0.47808 0.30100 0.17483  0.05623  0.05253  241 LYS A O   
1867 C CB  . LYS A 241 ? 0.54894 0.45760 0.33551 0.17620  0.02991  0.04246  241 LYS A CB  
1868 C CG  . LYS A 241 ? 0.49080 0.47111 0.37314 0.16621  -0.00158 0.04808  241 LYS A CG  
1869 C CD  . LYS A 241 ? 0.48268 0.50923 0.42349 0.15080  -0.02568 0.04764  241 LYS A CD  
1870 C CE  . LYS A 241 ? 0.47040 0.54362 0.46880 0.12442  -0.02694 0.05306  241 LYS A CE  
1871 N NZ  . LYS A 241 ? 0.48460 0.56276 0.49693 0.14383  -0.02856 0.05870  241 LYS A NZ  
1872 N N   . LYS A 242 ? 0.53447 0.45993 0.33203 0.13028  0.04783  0.01375  242 LYS A N   
1873 C CA  . LYS A 242 ? 0.47716 0.49011 0.33535 0.08699  0.04546  0.00779  242 LYS A CA  
1874 C C   . LYS A 242 ? 0.45823 0.47286 0.32706 0.02908  0.03151  -0.00751 242 LYS A C   
1875 O O   . LYS A 242 ? 0.47880 0.50125 0.34197 0.04218  0.00662  -0.01391 242 LYS A O   
1876 C CB  . LYS A 242 ? 0.50921 0.56308 0.36993 0.10549  0.04626  0.01312  242 LYS A CB  
1877 C CG  . LYS A 242 ? 0.53047 0.62441 0.41132 0.10874  0.05793  0.03304  242 LYS A CG  
1878 C CD  . LYS A 242 ? 0.63983 0.65934 0.46115 0.12255  0.04341  0.03883  242 LYS A CD  
1879 C CE  . LYS A 242 ? 0.69695 0.68138 0.49186 0.14347  0.03988  0.02320  242 LYS A CE  
1880 N NZ  . LYS A 242 ? 0.69210 0.70137 0.50638 0.13458  0.02185  0.00756  242 LYS A NZ  
1881 N N   . ILE A 243 ? 0.42945 0.44614 0.31501 0.00330  0.03097  -0.01817 243 ILE A N   
1882 C CA  . ILE A 243 ? 0.43309 0.40979 0.30069 0.01960  0.07004  -0.04031 243 ILE A CA  
1883 C C   . ILE A 243 ? 0.45898 0.40969 0.30437 0.01740  0.08094  -0.04748 243 ILE A C   
1884 O O   . ILE A 243 ? 0.50194 0.39305 0.30742 0.03874  0.06346  -0.07262 243 ILE A O   
1885 C CB  . ILE A 243 ? 0.42540 0.39775 0.30899 0.03431  0.08055  -0.03825 243 ILE A CB  
1886 C CG1 . ILE A 243 ? 0.49422 0.37205 0.31196 0.03034  0.05509  -0.02810 243 ILE A CG1 
1887 C CG2 . ILE A 243 ? 0.40510 0.41223 0.32037 0.01195  0.06648  -0.04156 243 ILE A CG2 
1888 C CD1 . ILE A 243 ? 0.50588 0.36056 0.32052 0.03786  0.06552  -0.02224 243 ILE A CD1 
1889 N N   . HIS A 244 ? 0.46809 0.42108 0.33299 -0.00655 0.07274  -0.03666 244 HIS A N   
1890 C CA  . HIS A 244 ? 0.49151 0.41375 0.34580 -0.04972 0.05196  -0.03118 244 HIS A CA  
1891 C C   . HIS A 244 ? 0.45981 0.42964 0.34138 -0.04809 0.01072  -0.04871 244 HIS A C   
1892 O O   . HIS A 244 ? 0.44872 0.43885 0.36009 -0.05469 -0.00552 -0.03782 244 HIS A O   
1893 C CB  . HIS A 244 ? 0.56638 0.41381 0.37962 -0.03613 0.05879  0.00475  244 HIS A CB  
1894 C CG  . HIS A 244 ? 0.65148 0.43577 0.42071 -0.00261 0.06236  0.05974  244 HIS A CG  
1895 N ND1 . HIS A 244 ? 0.66326 0.43682 0.42792 0.00098  0.08669  0.08562  244 HIS A ND1 
1896 C CD2 . HIS A 244 ? 0.68409 0.45986 0.43144 -0.00349 0.04626  0.07609  244 HIS A CD2 
1897 C CE1 . HIS A 244 ? 0.67053 0.46643 0.42948 -0.00443 0.08573  0.07356  244 HIS A CE1 
1898 N NE2 . HIS A 244 ? 0.68934 0.47174 0.43213 -0.00491 0.07472  0.07220  244 HIS A NE2 
1899 N N   . PHE A 245 ? 0.44997 0.45382 0.32801 -0.03855 -0.00537 -0.05785 245 PHE A N   
1900 C CA  . PHE A 245 ? 0.52961 0.47859 0.33761 -0.03614 0.00202  -0.05102 245 PHE A CA  
1901 C C   . PHE A 245 ? 0.57654 0.51730 0.33178 -0.05509 0.02098  -0.04817 245 PHE A C   
1902 O O   . PHE A 245 ? 0.60320 0.51335 0.31672 -0.05117 0.03310  -0.02172 245 PHE A O   
1903 C CB  . PHE A 245 ? 0.55000 0.46813 0.35327 0.01397  -0.00710 -0.05133 245 PHE A CB  
1904 C CG  . PHE A 245 ? 0.59236 0.46043 0.37276 0.03230  0.00793  -0.05959 245 PHE A CG  
1905 C CD1 . PHE A 245 ? 0.62610 0.46348 0.38552 0.04248  0.01260  -0.04947 245 PHE A CD1 
1906 C CD2 . PHE A 245 ? 0.62542 0.47319 0.38526 0.04727  0.00920  -0.07235 245 PHE A CD2 
1907 C CE1 . PHE A 245 ? 0.63181 0.47732 0.39083 0.04565  0.01302  -0.05711 245 PHE A CE1 
1908 C CE2 . PHE A 245 ? 0.64574 0.49451 0.39970 0.03307  0.02504  -0.06611 245 PHE A CE2 
1909 C CZ  . PHE A 245 ? 0.64731 0.47584 0.39326 0.04181  0.01893  -0.06708 245 PHE A CZ  
1910 N N   . ALA A 246 ? 0.54080 0.54021 0.34488 -0.08236 0.01777  -0.05199 246 ALA A N   
1911 C CA  . ALA A 246 ? 0.49305 0.55547 0.37568 -0.06014 0.01714  -0.06622 246 ALA A CA  
1912 C C   . ALA A 246 ? 0.50131 0.55463 0.41273 -0.07622 0.03003  -0.06632 246 ALA A C   
1913 O O   . ALA A 246 ? 0.48056 0.55679 0.43377 -0.07962 -0.00863 -0.03675 246 ALA A O   
1914 C CB  . ALA A 246 ? 0.46419 0.56961 0.39492 -0.02080 -0.00655 -0.07343 246 ALA A CB  
1915 N N   . ARG A 247 ? 0.49696 0.54042 0.43154 -0.08764 0.07650  -0.08357 247 ARG A N   
1916 C CA  . ARG A 247 ? 0.59361 0.55496 0.48923 -0.05164 0.08848  -0.07350 247 ARG A CA  
1917 C C   . ARG A 247 ? 0.58830 0.58651 0.51846 -0.01425 0.06172  -0.08601 247 ARG A C   
1918 O O   . ARG A 247 ? 0.59569 0.63307 0.51015 -0.03102 0.05195  -0.08055 247 ARG A O   
1919 C CB  . ARG A 247 ? 0.69108 0.54398 0.52504 -0.03641 0.12159  -0.04234 247 ARG A CB  
1920 C CG  . ARG A 247 ? 0.78833 0.54577 0.57187 -0.00440 0.14103  0.00040  247 ARG A CG  
1921 C CD  . ARG A 247 ? 0.86097 0.54710 0.61612 0.04523  0.16655  0.04193  247 ARG A CD  
1922 N NE  . ARG A 247 ? 0.90120 0.55069 0.66682 0.11485  0.19562  0.08621  247 ARG A NE  
1923 C CZ  . ARG A 247 ? 0.91484 0.54915 0.68867 0.18592  0.20919  0.12872  247 ARG A CZ  
1924 N NH1 . ARG A 247 ? 0.92780 0.55512 0.69734 0.17887  0.23355  0.17425  247 ARG A NH1 
1925 N NH2 . ARG A 247 ? 0.90206 0.55122 0.68621 0.24222  0.19521  0.13556  247 ARG A NH2 
1926 N N   . PHE A 248 ? 0.57507 0.58649 0.56610 0.05147  0.05043  -0.09537 248 PHE A N   
1927 C CA  . PHE A 248 ? 0.53679 0.62665 0.61080 0.08822  0.04291  -0.10050 248 PHE A CA  
1928 C C   . PHE A 248 ? 0.54387 0.62983 0.59430 0.07172  0.07710  -0.12776 248 PHE A C   
1929 O O   . PHE A 248 ? 0.53860 0.64902 0.58039 0.10429  0.10565  -0.12496 248 PHE A O   
1930 C CB  . PHE A 248 ? 0.54357 0.67019 0.66730 0.08901  0.01944  -0.06799 248 PHE A CB  
1931 C CG  . PHE A 248 ? 0.56298 0.69216 0.71646 0.10875  0.00036  -0.04300 248 PHE A CG  
1932 C CD1 . PHE A 248 ? 0.59251 0.69737 0.74643 0.11694  -0.01562 -0.03171 248 PHE A CD1 
1933 C CD2 . PHE A 248 ? 0.57022 0.67719 0.73527 0.14800  0.00217  -0.04687 248 PHE A CD2 
1934 C CE1 . PHE A 248 ? 0.60593 0.69337 0.76588 0.16435  -0.01962 -0.03000 248 PHE A CE1 
1935 C CE2 . PHE A 248 ? 0.57941 0.66686 0.75054 0.14896  -0.00471 -0.04292 248 PHE A CE2 
1936 C CZ  . PHE A 248 ? 0.62035 0.68374 0.76597 0.17024  -0.00491 -0.03148 248 PHE A CZ  
1937 N N   . ARG A 249 ? 0.56318 0.59614 0.59122 0.04744  0.09466  -0.15115 249 ARG A N   
1938 C CA  . ARG A 249 ? 0.63780 0.59491 0.60112 0.04608  0.09461  -0.16031 249 ARG A CA  
1939 C C   . ARG A 249 ? 0.64699 0.60162 0.60183 0.07499  0.06352  -0.17124 249 ARG A C   
1940 O O   . ARG A 249 ? 0.60453 0.61132 0.60415 0.11214  0.01107  -0.18759 249 ARG A O   
1941 C CB  . ARG A 249 ? 0.70669 0.60554 0.61164 -0.00607 0.09348  -0.13970 249 ARG A CB  
1942 C CG  . ARG A 249 ? 0.76495 0.63241 0.61555 -0.03717 0.08172  -0.12166 249 ARG A CG  
1943 C CD  . ARG A 249 ? 0.82740 0.68649 0.61138 -0.05900 0.07404  -0.10766 249 ARG A CD  
1944 N NE  . ARG A 249 ? 0.83816 0.75372 0.60792 -0.07327 0.07713  -0.09588 249 ARG A NE  
1945 C CZ  . ARG A 249 ? 0.83224 0.80154 0.60509 -0.07655 0.06263  -0.10467 249 ARG A CZ  
1946 N NH1 . ARG A 249 ? 0.81482 0.81893 0.59725 -0.08844 0.04467  -0.11294 249 ARG A NH1 
1947 N NH2 . ARG A 249 ? 0.83471 0.81398 0.61193 -0.06465 0.06284  -0.11045 249 ARG A NH2 
1948 N N   . SER A 250 ? 0.67164 0.60443 0.60141 0.02356  0.08589  -0.15572 250 SER A N   
1949 C CA  . SER A 250 ? 0.68653 0.60233 0.59514 -0.00252 0.07612  -0.14846 250 SER A CA  
1950 C C   . SER A 250 ? 0.64151 0.58370 0.54600 -0.00462 0.06689  -0.15997 250 SER A C   
1951 O O   . SER A 250 ? 0.68458 0.58906 0.54293 0.01214  0.08502  -0.17667 250 SER A O   
1952 C CB  . SER A 250 ? 0.76626 0.63198 0.63338 -0.02573 0.05652  -0.13423 250 SER A CB  
1953 O OG  . SER A 250 ? 0.81435 0.65781 0.64848 -0.02363 0.04054  -0.11698 250 SER A OG  
1954 N N   . PHE A 251 ? 0.56238 0.56506 0.51192 -0.01949 0.05392  -0.14538 251 PHE A N   
1955 C CA  . PHE A 251 ? 0.52510 0.52979 0.48102 -0.02225 0.04312  -0.11999 251 PHE A CA  
1956 C C   . PHE A 251 ? 0.48082 0.52591 0.43254 -0.01607 0.01229  -0.12627 251 PHE A C   
1957 O O   . PHE A 251 ? 0.49730 0.53899 0.42997 0.03300  -0.00449 -0.13494 251 PHE A O   
1958 C CB  . PHE A 251 ? 0.54833 0.51563 0.50836 0.01721  0.06127  -0.08814 251 PHE A CB  
1959 C CG  . PHE A 251 ? 0.56582 0.53042 0.53751 0.04598  0.04710  -0.07679 251 PHE A CG  
1960 C CD1 . PHE A 251 ? 0.59700 0.54364 0.55124 0.04467  0.07432  -0.09401 251 PHE A CD1 
1961 C CD2 . PHE A 251 ? 0.60165 0.53498 0.55229 0.07090  -0.00074 -0.08394 251 PHE A CD2 
1962 C CE1 . PHE A 251 ? 0.60212 0.54035 0.55939 0.03977  0.05437  -0.12292 251 PHE A CE1 
1963 C CE2 . PHE A 251 ? 0.62172 0.53860 0.56344 0.09427  -0.00332 -0.11190 251 PHE A CE2 
1964 C CZ  . PHE A 251 ? 0.61378 0.54604 0.56715 0.06850  0.02394  -0.12691 251 PHE A CZ  
1965 N N   . PRO A 252 ? 0.40165 0.49388 0.38187 -0.02779 0.00315  -0.11495 252 PRO A N   
1966 C CA  . PRO A 252 ? 0.39983 0.46354 0.34101 -0.04311 0.00499  -0.10662 252 PRO A CA  
1967 C C   . PRO A 252 ? 0.44375 0.48719 0.30445 -0.05192 0.00774  -0.08637 252 PRO A C   
1968 O O   . PRO A 252 ? 0.45572 0.53133 0.28540 -0.04705 0.00523  -0.07138 252 PRO A O   
1969 C CB  . PRO A 252 ? 0.36783 0.45671 0.35958 -0.05693 0.00923  -0.12642 252 PRO A CB  
1970 C CG  . PRO A 252 ? 0.36234 0.47998 0.37230 -0.04118 0.02731  -0.12559 252 PRO A CG  
1971 C CD  . PRO A 252 ? 0.34175 0.49200 0.37905 -0.05600 0.01855  -0.11941 252 PRO A CD  
1972 N N   . PHE A 253 ? 0.45117 0.46602 0.30397 -0.02932 0.00129  -0.08578 253 PHE A N   
1973 C CA  . PHE A 253 ? 0.45458 0.44320 0.29193 0.00153  0.00709  -0.07888 253 PHE A CA  
1974 C C   . PHE A 253 ? 0.35782 0.43873 0.28966 0.02122  0.01112  -0.06993 253 PHE A C   
1975 O O   . PHE A 253 ? 0.33483 0.40763 0.29113 0.02105  0.01496  -0.08664 253 PHE A O   
1976 C CB  . PHE A 253 ? 0.51302 0.42100 0.28091 0.01686  0.01402  -0.05669 253 PHE A CB  
1977 C CG  . PHE A 253 ? 0.49309 0.42906 0.28214 0.00588  0.04314  -0.04166 253 PHE A CG  
1978 C CD1 . PHE A 253 ? 0.51718 0.46397 0.28449 -0.01084 0.06291  -0.02542 253 PHE A CD1 
1979 C CD2 . PHE A 253 ? 0.51371 0.41332 0.28118 0.01381  0.05385  -0.05378 253 PHE A CD2 
1980 C CE1 . PHE A 253 ? 0.49413 0.47790 0.28330 0.00521  0.07846  -0.03169 253 PHE A CE1 
1981 C CE2 . PHE A 253 ? 0.54450 0.45652 0.27713 0.01629  0.06107  -0.03642 253 PHE A CE2 
1982 C CZ  . PHE A 253 ? 0.51081 0.46784 0.28276 0.01122  0.08159  -0.03171 253 PHE A CZ  
1983 N N   . TRP A 254 ? 0.31892 0.46254 0.27565 0.03693  0.01535  -0.02323 254 TRP A N   
1984 C CA  . TRP A 254 ? 0.31146 0.45482 0.25450 -0.02970 0.02964  -0.01782 254 TRP A CA  
1985 C C   . TRP A 254 ? 0.31816 0.45994 0.24138 -0.06761 0.00276  -0.05609 254 TRP A C   
1986 O O   . TRP A 254 ? 0.29997 0.48796 0.25416 -0.04370 -0.00173 -0.04196 254 TRP A O   
1987 C CB  . TRP A 254 ? 0.39204 0.44279 0.25463 -0.02171 0.03926  0.00084  254 TRP A CB  
1988 C CG  . TRP A 254 ? 0.39130 0.42295 0.26587 -0.00950 0.03856  -0.02475 254 TRP A CG  
1989 C CD1 . TRP A 254 ? 0.35712 0.41816 0.27781 0.01880  0.04748  -0.03233 254 TRP A CD1 
1990 C CD2 . TRP A 254 ? 0.40782 0.43541 0.27038 0.03343  0.05695  -0.04858 254 TRP A CD2 
1991 N NE1 . TRP A 254 ? 0.35725 0.40965 0.28535 0.03602  0.04167  -0.03112 254 TRP A NE1 
1992 C CE2 . TRP A 254 ? 0.38548 0.43033 0.27370 0.04944  0.02319  -0.04989 254 TRP A CE2 
1993 C CE3 . TRP A 254 ? 0.41329 0.45719 0.26908 0.06633  0.05104  -0.04517 254 TRP A CE3 
1994 C CZ2 . TRP A 254 ? 0.40317 0.45630 0.26257 0.06076  0.01834  -0.05231 254 TRP A CZ2 
1995 C CZ3 . TRP A 254 ? 0.44237 0.46517 0.26053 0.06135  0.02613  -0.03992 254 TRP A CZ3 
1996 C CH2 . TRP A 254 ? 0.44911 0.46484 0.26021 0.06260  0.02850  -0.05740 254 TRP A CH2 
1997 N N   . ARG A 255 ? 0.33208 0.44916 0.21412 -0.09636 -0.00967 -0.09356 255 ARG A N   
1998 C CA  . ARG A 255 ? 0.38685 0.46658 0.22734 -0.11439 -0.01377 -0.07684 255 ARG A CA  
1999 C C   . ARG A 255 ? 0.39070 0.49244 0.24600 -0.03108 -0.02256 -0.08116 255 ARG A C   
2000 O O   . ARG A 255 ? 0.39187 0.51240 0.25805 -0.03047 -0.00785 -0.07164 255 ARG A O   
2001 C CB  . ARG A 255 ? 0.43056 0.45715 0.22227 -0.12824 -0.03233 -0.05846 255 ARG A CB  
2002 C CG  . ARG A 255 ? 0.45129 0.49804 0.25934 -0.10947 -0.04583 -0.05535 255 ARG A CG  
2003 C CD  . ARG A 255 ? 0.51038 0.54929 0.30789 -0.05133 -0.07051 -0.04982 255 ARG A CD  
2004 N NE  . ARG A 255 ? 0.59604 0.59177 0.33275 -0.06373 -0.10475 -0.06124 255 ARG A NE  
2005 C CZ  . ARG A 255 ? 0.65485 0.58965 0.36087 -0.04037 -0.10353 -0.05470 255 ARG A CZ  
2006 N NH1 . ARG A 255 ? 0.69398 0.58119 0.37687 -0.02513 -0.12416 -0.04036 255 ARG A NH1 
2007 N NH2 . ARG A 255 ? 0.66056 0.59415 0.37790 -0.03106 -0.07995 -0.05855 255 ARG A NH2 
2008 N N   . ARG A 256 ? 0.38083 0.49059 0.25524 0.00138  -0.02437 -0.09803 256 ARG A N   
2009 C CA  . ARG A 256 ? 0.34268 0.50165 0.29192 -0.02954 -0.00726 -0.07544 256 ARG A CA  
2010 C C   . ARG A 256 ? 0.31189 0.48909 0.27924 -0.06001 0.01235  -0.03862 256 ARG A C   
2011 O O   . ARG A 256 ? 0.30168 0.51159 0.27751 -0.08290 0.01815  -0.00778 256 ARG A O   
2012 C CB  . ARG A 256 ? 0.34267 0.53129 0.34328 0.00330  0.00277  -0.05828 256 ARG A CB  
2013 C CG  . ARG A 256 ? 0.38154 0.53712 0.39020 0.06976  0.02178  -0.05795 256 ARG A CG  
2014 C CD  . ARG A 256 ? 0.41968 0.47094 0.41908 0.13728  0.02077  -0.07585 256 ARG A CD  
2015 N NE  . ARG A 256 ? 0.47118 0.43161 0.42899 0.18200  -0.00680 -0.12246 256 ARG A NE  
2016 C CZ  . ARG A 256 ? 0.66039 0.45925 0.44246 0.10395  -0.04382 -0.07687 256 ARG A CZ  
2017 N NH1 . ARG A 256 ? 0.70748 0.49034 0.44270 0.05564  -0.05621 -0.06471 256 ARG A NH1 
2018 N NH2 . ARG A 256 ? 0.72797 0.42938 0.43702 0.07425  -0.05926 -0.06298 256 ARG A NH2 
2019 N N   . VAL A 257 ? 0.33874 0.42226 0.24920 -0.01059 0.02271  -0.05699 257 VAL A N   
2020 C CA  . VAL A 257 ? 0.32318 0.37717 0.23554 0.01048  0.03542  -0.06479 257 VAL A CA  
2021 C C   . VAL A 257 ? 0.33670 0.40552 0.23516 -0.03961 0.02373  -0.05177 257 VAL A C   
2022 O O   . VAL A 257 ? 0.31516 0.43981 0.24277 -0.05504 0.02331  -0.03799 257 VAL A O   
2023 C CB  . VAL A 257 ? 0.29478 0.33352 0.24998 0.03291  0.03546  -0.05057 257 VAL A CB  
2024 C CG1 . VAL A 257 ? 0.26909 0.29420 0.26494 0.02119  0.02711  -0.06800 257 VAL A CG1 
2025 C CG2 . VAL A 257 ? 0.32118 0.38203 0.26203 0.00598  0.02884  -0.04359 257 VAL A CG2 
2026 N N   . HIS A 258 ? 0.33973 0.41083 0.24031 -0.06106 -0.00120 -0.05354 258 HIS A N   
2027 C CA  . HIS A 258 ? 0.32820 0.42570 0.24823 -0.05285 -0.00169 -0.04620 258 HIS A CA  
2028 C C   . HIS A 258 ? 0.34352 0.42570 0.25910 -0.04850 0.01943  -0.05181 258 HIS A C   
2029 O O   . HIS A 258 ? 0.34922 0.44372 0.25718 -0.06597 0.03121  -0.02238 258 HIS A O   
2030 C CB  . HIS A 258 ? 0.31712 0.46031 0.24457 -0.04135 -0.01388 -0.03034 258 HIS A CB  
2031 C CG  . HIS A 258 ? 0.36733 0.48541 0.25486 -0.01599 -0.03493 -0.02187 258 HIS A CG  
2032 N ND1 . HIS A 258 ? 0.42186 0.50897 0.29163 -0.02476 -0.03163 -0.02724 258 HIS A ND1 
2033 C CD2 . HIS A 258 ? 0.35023 0.51352 0.25605 0.00997  -0.02110 -0.02610 258 HIS A CD2 
2034 C CE1 . HIS A 258 ? 0.41218 0.50813 0.28112 0.02951  -0.04139 -0.01605 258 HIS A CE1 
2035 N NE2 . HIS A 258 ? 0.40846 0.52559 0.29414 0.03622  -0.03719 -0.01767 258 HIS A NE2 
2036 N N   . ASP A 259 ? 0.31323 0.42500 0.27425 -0.05800 0.02936  -0.06589 259 ASP A N   
2037 C CA  . ASP A 259 ? 0.35666 0.45586 0.28602 -0.08855 0.02690  -0.06405 259 ASP A CA  
2038 C C   . ASP A 259 ? 0.41042 0.49184 0.29298 -0.11034 0.05974  -0.03910 259 ASP A C   
2039 O O   . ASP A 259 ? 0.47350 0.52984 0.29122 -0.11999 0.05724  -0.01330 259 ASP A O   
2040 C CB  . ASP A 259 ? 0.42418 0.46780 0.30877 -0.06485 0.00160  -0.10874 259 ASP A CB  
2041 C CG  . ASP A 259 ? 0.50220 0.51802 0.36453 -0.02606 0.03811  -0.12228 259 ASP A CG  
2042 O OD1 . ASP A 259 ? 0.49214 0.53187 0.36553 -0.01143 0.04656  -0.11359 259 ASP A OD1 
2043 O OD2 . ASP A 259 ? 0.53819 0.55091 0.41057 -0.03168 0.04585  -0.13825 259 ASP A OD2 
2044 N N   . SER A 260 ? 0.42381 0.47858 0.31035 -0.10101 0.06244  -0.07190 260 SER A N   
2045 C CA  . SER A 260 ? 0.42689 0.47982 0.33991 -0.05567 0.06149  -0.05963 260 SER A CA  
2046 C C   . SER A 260 ? 0.42036 0.48018 0.32840 -0.06262 0.07020  -0.04125 260 SER A C   
2047 O O   . SER A 260 ? 0.44246 0.51101 0.34745 -0.08709 0.08908  -0.03779 260 SER A O   
2048 C CB  . SER A 260 ? 0.42201 0.47723 0.38699 0.01767  0.02769  -0.07035 260 SER A CB  
2049 O OG  . SER A 260 ? 0.45917 0.50549 0.40899 0.05579  0.01395  -0.07595 260 SER A OG  
2050 N N   . PHE A 261 ? 0.35139 0.46676 0.29115 0.01269  0.07067  -0.01915 261 PHE A N   
2051 C CA  . PHE A 261 ? 0.34647 0.45177 0.26754 0.03423  0.03842  -0.00187 261 PHE A CA  
2052 C C   . PHE A 261 ? 0.39144 0.43105 0.29071 0.01992  -0.02408 -0.00001 261 PHE A C   
2053 O O   . PHE A 261 ? 0.43157 0.40121 0.32221 -0.03115 -0.05947 -0.03154 261 PHE A O   
2054 C CB  . PHE A 261 ? 0.34272 0.43428 0.23851 0.03627  0.02208  0.01159  261 PHE A CB  
2055 C CG  . PHE A 261 ? 0.35018 0.39911 0.22906 0.04025  -0.02378 0.03175  261 PHE A CG  
2056 C CD1 . PHE A 261 ? 0.38413 0.42430 0.23383 0.03556  -0.03481 0.03036  261 PHE A CD1 
2057 C CD2 . PHE A 261 ? 0.40261 0.36825 0.23391 -0.02061 -0.03367 0.04416  261 PHE A CD2 
2058 C CE1 . PHE A 261 ? 0.39166 0.41814 0.23941 -0.00050 -0.00240 0.02428  261 PHE A CE1 
2059 C CE2 . PHE A 261 ? 0.43467 0.39149 0.24430 -0.04176 -0.01933 0.01794  261 PHE A CE2 
2060 C CZ  . PHE A 261 ? 0.39481 0.40434 0.24313 -0.01672 0.00904  0.01043  261 PHE A CZ  
2061 N N   . ILE A 262 ? 0.41403 0.43636 0.26677 0.01476  -0.06659 -0.00565 262 ILE A N   
2062 C CA  . ILE A 262 ? 0.43424 0.49046 0.29030 0.03636  -0.08095 0.02029  262 ILE A CA  
2063 C C   . ILE A 262 ? 0.51972 0.57676 0.34821 0.07667  -0.04219 0.03512  262 ILE A C   
2064 O O   . ILE A 262 ? 0.60870 0.58634 0.35336 0.09091  -0.04614 0.04929  262 ILE A O   
2065 C CB  . ILE A 262 ? 0.42020 0.46774 0.30601 0.06924  -0.08026 0.05154  262 ILE A CB  
2066 C CG1 . ILE A 262 ? 0.38654 0.44977 0.34317 0.07678  -0.06983 -0.00683 262 ILE A CG1 
2067 C CG2 . ILE A 262 ? 0.41142 0.48828 0.31937 0.08392  -0.07911 0.09346  262 ILE A CG2 
2068 C CD1 . ILE A 262 ? 0.37754 0.43132 0.36623 0.06589  -0.05367 -0.03354 262 ILE A CD1 
2069 N N   . GLU A 263 ? 0.49876 0.64491 0.39920 0.13060  0.00737  0.02361  263 GLU A N   
2070 C CA  . GLU A 263 ? 0.61464 0.73739 0.49680 0.15368  0.02369  0.05040  263 GLU A CA  
2071 C C   . GLU A 263 ? 0.75996 0.85188 0.55249 0.15277  0.03921  0.06935  263 GLU A C   
2072 O O   . GLU A 263 ? 0.78029 0.89263 0.56624 0.14822  0.05496  0.09283  263 GLU A O   
2073 C CB  . GLU A 263 ? 0.68440 0.73919 0.55763 0.12051  0.01322  0.03358  263 GLU A CB  
2074 C CG  . GLU A 263 ? 0.72843 0.73638 0.61396 0.08063  -0.04193 -0.01560 263 GLU A CG  
2075 C CD  . GLU A 263 ? 0.72886 0.71147 0.64592 0.07673  -0.08313 -0.05016 263 GLU A CD  
2076 O OE1 . GLU A 263 ? 0.74801 0.71937 0.65273 0.06730  -0.08037 -0.06339 263 GLU A OE1 
2077 O OE2 . GLU A 263 ? 0.69577 0.67637 0.66257 0.09013  -0.09567 -0.06140 263 GLU A OE2 
2078 N N   . ASP A 264 ? 0.91959 0.92801 0.60615 0.16108  0.01889  0.04608  264 ASP A N   
2079 C CA  . ASP A 264 ? 1.02238 0.99219 0.65785 0.19227  0.00328  0.02422  264 ASP A CA  
2080 C C   . ASP A 264 ? 1.07930 0.98148 0.68330 0.14670  0.00025  0.00881  264 ASP A C   
2081 O O   . ASP A 264 ? 1.10495 0.97916 0.70064 0.08206  -0.01012 -0.00399 264 ASP A O   
2082 C CB  . ASP A 264 ? 1.05003 1.06561 0.67545 0.26332  -0.01323 0.03109  264 ASP A CB  
2083 C CG  . ASP A 264 ? 1.07732 1.15314 0.69309 0.25849  -0.01779 0.04438  264 ASP A CG  
2084 O OD1 . ASP A 264 ? 1.08984 1.18949 0.71944 0.24138  -0.00734 0.01201  264 ASP A OD1 
2085 O OD2 . ASP A 264 ? 1.08094 1.17847 0.67898 0.25822  -0.02478 0.08519  264 ASP A OD2 
2086 C C1  . CIT B .   ? 0.69213 0.80750 0.76090 -0.01935 -0.03074 -0.08231 301 CIT A C1  
2087 O O1  . CIT B .   ? 0.62178 0.79095 0.70198 -0.01499 -0.03250 -0.07354 301 CIT A O1  
2088 O O2  . CIT B .   ? 0.73505 0.81439 0.77692 -0.01335 0.02173  -0.08400 301 CIT A O2  
2089 C C2  . CIT B .   ? 0.78232 0.82534 0.81605 0.01753  -0.07178 -0.08487 301 CIT A C2  
2090 C C3  . CIT B .   ? 0.87540 0.86036 0.87240 0.08156  -0.09178 -0.09180 301 CIT A C3  
2091 O O7  . CIT B .   ? 0.95681 0.88086 0.89690 0.07552  -0.09250 -0.08985 301 CIT A O7  
2092 C C4  . CIT B .   ? 0.96022 0.88644 0.88713 0.10180  -0.09593 -0.08322 301 CIT A C4  
2093 C C5  . CIT B .   ? 1.02031 0.91169 0.89543 0.08081  -0.09966 -0.07973 301 CIT A C5  
2094 O O3  . CIT B .   ? 1.04522 0.92590 0.89688 0.07477  -0.10700 -0.08229 301 CIT A O3  
2095 O O4  . CIT B .   ? 1.02213 0.90130 0.88931 0.06623  -0.10285 -0.07292 301 CIT A O4  
2096 C C6  . CIT B .   ? 0.78414 0.85058 0.88310 0.11383  -0.10500 -0.10798 301 CIT A C6  
2097 O O5  . CIT B .   ? 0.74607 0.81987 0.88363 0.13571  -0.12911 -0.10726 301 CIT A O5  
2098 O O6  . CIT B .   ? 0.74172 0.87757 0.88940 0.10758  -0.08736 -0.13125 301 CIT A O6  
2099 N N   . V0I C .   ? 0.40664 0.58502 0.32356 0.06419  -0.10508 0.01042  302 V0I A N   
2100 C C   . V0I C .   ? 0.54224 0.61392 0.31957 0.13677  -0.13769 0.05572  302 V0I A C   
2101 O O   . V0I C .   ? 0.33986 0.51207 0.30445 0.02234  -0.06467 -0.00790 302 V0I A O   
2102 C C1  . V0I C .   ? 0.35508 0.52949 0.31740 0.01071  -0.09487 -0.00809 302 V0I A C1  
2103 C C10 . V0I C .   ? 0.31110 0.45193 0.29972 -0.02373 -0.04564 -0.00502 302 V0I A C10 
2104 C C11 . V0I C .   ? 0.35709 0.57992 0.31254 0.08186  -0.06374 -0.01207 302 V0I A C11 
2105 C C12 . V0I C .   ? 0.36538 0.53343 0.28739 0.09053  -0.06939 -0.02290 302 V0I A C12 
2106 C C13 . V0I C .   ? 0.37355 0.47839 0.26096 0.10096  -0.08246 -0.02394 302 V0I A C13 
2107 C C14 . V0I C .   ? 0.36985 0.43955 0.24159 0.08832  -0.05725 -0.01719 302 V0I A C14 
2108 C C15 . V0I C .   ? 0.39180 0.42174 0.22492 0.02707  -0.00898 0.00977  302 V0I A C15 
2109 C C16 . V0I C .   ? 0.38280 0.43287 0.23752 0.02882  -0.04048 -0.00398 302 V0I A C16 
2110 C C17 . V0I C .   ? 0.47307 0.46056 0.31302 0.06484  -0.04138 0.00561  302 V0I A C17 
2111 C C18 . V0I C .   ? 0.54725 0.52072 0.41600 0.10455  -0.03953 0.02395  302 V0I A C18 
2112 C C19 . V0I C .   ? 0.54800 0.49658 0.37914 0.07718  -0.03379 0.01351  302 V0I A C19 
2113 C C2  . V0I C .   ? 0.32800 0.49498 0.30928 0.00498  -0.06533 -0.00756 302 V0I A C2  
2114 C C20 . V0I C .   ? 0.47681 0.48862 0.34003 0.03496  -0.02627 0.01637  302 V0I A C20 
2115 C C21 . V0I C .   ? 0.61679 0.58729 0.52100 0.11340  -0.05986 0.03637  302 V0I A C21 
2116 C C22 . V0I C .   ? 0.82617 0.78617 0.73506 0.23322  -0.06294 -0.03510 302 V0I A C22 
2117 C C23 . V0I C .   ? 0.83354 0.78288 0.72989 0.23039  -0.07355 0.00305  302 V0I A C23 
2118 C C24 . V0I C .   ? 0.43520 0.38387 0.23201 -0.02283 -0.04721 0.03048  302 V0I A C24 
2119 C C25 . V0I C .   ? 0.37796 0.39245 0.23311 -0.00621 -0.00575 0.00458  302 V0I A C25 
2120 C C3  . V0I C .   ? 0.30541 0.49229 0.29700 0.03393  -0.03819 -0.01105 302 V0I A C3  
2121 C C4  . V0I C .   ? 0.29319 0.46839 0.31276 0.04343  -0.03427 -0.00464 302 V0I A C4  
2122 C C5  . V0I C .   ? 0.28169 0.46010 0.31425 -0.00697 -0.04049 -0.00996 302 V0I A C5  
2123 C C6  . V0I C .   ? 0.30128 0.48068 0.30405 -0.01544 0.01794  -0.03724 302 V0I A C6  
2124 C C7  . V0I C .   ? 0.27576 0.47124 0.29839 -0.03822 -0.02768 -0.01450 302 V0I A C7  
2125 C C8  . V0I C .   ? 0.23375 0.47769 0.28676 -0.00342 -0.02825 -0.01527 302 V0I A C8  
2126 C C9  . V0I C .   ? 0.28766 0.46549 0.30334 -0.00788 -0.02382 -0.00267 302 V0I A C9  
2127 N N1  . V0I C .   ? 0.27214 0.47831 0.28669 0.01369  -0.01331 -0.03116 302 V0I A N1  
2128 N N10 . V0I C .   ? 0.39586 0.41855 0.22928 -0.00879 -0.02372 0.01209  302 V0I A N10 
2129 N N11 . V0I C .   ? 0.45934 0.38765 0.24078 -0.03170 -0.01923 0.02804  302 V0I A N11 
2130 N N12 . V0I C .   ? 0.36776 0.37981 0.23289 -0.01862 0.02170  0.01532  302 V0I A N12 
2131 N N2  . V0I C .   ? 0.29793 0.48204 0.30750 -0.03542 0.00154  -0.03218 302 V0I A N2  
2132 N N3  . V0I C .   ? 0.24314 0.48104 0.29377 -0.03405 -0.03847 -0.01273 302 V0I A N3  
2133 N N4  . V0I C .   ? 0.30559 0.45431 0.30461 -0.02684 -0.04074 -0.00096 302 V0I A N4  
2134 N N5  . V0I C .   ? 0.36799 0.43194 0.29541 -0.03214 -0.05951 -0.00498 302 V0I A N5  
2135 N N6  . V0I C .   ? 0.38321 0.43411 0.22565 0.03526  -0.00858 0.01074  302 V0I A N6  
2136 N N7  . V0I C .   ? 0.43853 0.43455 0.26062 0.06188  -0.04670 -0.01312 302 V0I A N7  
2137 N N8  . V0I C .   ? 0.69833 0.67777 0.60956 0.14292  -0.08145 0.00735  302 V0I A N8  
2138 N N9  . V0I C .   ? 0.81846 0.77457 0.71872 0.21312  -0.06853 -0.01745 302 V0I A N9  
2139 O O1  . V0I C .   ? 0.27587 0.44059 0.32580 -0.05252 -0.02722 -0.01283 302 V0I A O1  
2140 O O2  . V0I C .   ? 0.27611 0.45087 0.33814 0.00876  -0.01726 -0.00242 302 V0I A O2  
2141 O O3  . V0I C .   ? 0.47124 0.47928 0.35014 0.09989  -0.02825 0.02996  302 V0I A O3  
2142 O O4  . V0I C .   ? 0.45559 0.50428 0.34443 -0.01145 0.03035  0.02336  302 V0I A O4  
2143 O O5  . V0I C .   ? 0.61606 0.48008 0.39104 0.09156  -0.03019 0.02476  302 V0I A O5  
2144 O O6  . V0I C .   ? 0.79769 0.71510 0.70489 0.12710  -0.05255 -0.04169 302 V0I A O6  
2145 O O7  . V0I C .   ? 0.81467 0.77885 0.69713 0.13210  -0.07533 0.04530  302 V0I A O7  
2146 S S   . V0I C .   ? 0.76808 0.73356 0.68608 0.16362  -0.08418 -0.00946 302 V0I A S   
2147 O O   . HOH D .   ? 0.46810 0.48933 0.40515 -0.01562 0.00702  -0.08677 401 HOH A O   
2148 O O   . HOH D .   ? 0.62753 0.71166 0.60743 0.02112  -0.01392 -0.13603 402 HOH A O   
2149 O O   . HOH D .   ? 0.67248 0.72939 0.54163 -0.01605 0.14787  0.02726  403 HOH A O   
2150 O O   . HOH D .   ? 0.68035 0.77513 0.58110 -0.06634 0.08699  0.15866  404 HOH A O   
2151 O O   . HOH D .   ? 0.60155 0.54696 0.48641 0.01689  -0.04586 -0.10558 405 HOH A O   
2152 O O   . HOH D .   ? 0.73818 0.82332 0.44575 0.29648  -0.18669 -0.00919 406 HOH A O   
2153 O O   . HOH D .   ? 0.98242 0.67897 0.47701 -0.17249 0.28205  -0.09341 407 HOH A O   
2154 O O   . HOH D .   ? 0.38868 0.65757 0.21387 -0.03742 -0.03189 0.00013  408 HOH A O   
2155 O O   . HOH D .   ? 0.25623 0.64617 0.35214 -0.01386 -0.04372 -0.12147 409 HOH A O   
2156 O O   . HOH D .   ? 0.56906 0.65313 0.53053 -0.03399 -0.10634 0.06980  410 HOH A O   
2157 O O   . HOH D .   ? 0.53754 0.62534 0.59978 -0.01071 0.24420  -0.05498 411 HOH A O   
2158 O O   . HOH D .   ? 0.37794 0.78426 0.45271 0.19504  -0.16542 -0.15451 412 HOH A O   
2159 O O   . HOH D .   ? 0.97972 0.74963 0.43765 0.03159  -0.07545 -0.08735 413 HOH A O   
2160 O O   . HOH D .   ? 0.34900 0.41885 0.38659 0.04143  0.01687  0.08658  414 HOH A O   
2161 O O   . HOH D .   ? 0.60926 0.70037 0.38317 0.22496  -0.07151 -0.11625 415 HOH A O   
2162 O O   . HOH D .   ? 0.35104 0.59624 0.45900 -0.01729 -0.03263 0.04410  416 HOH A O   
2163 O O   . HOH D .   ? 0.37347 0.93079 0.52103 -0.02680 -0.17378 0.07952  417 HOH A O   
2164 O O   . HOH D .   ? 0.39641 0.71029 0.56326 -0.10998 0.10533  -0.03583 418 HOH A O   
2165 O O   . HOH D .   ? 0.71051 0.77012 0.61316 0.40185  0.00115  0.12790  419 HOH A O   
2166 O O   . HOH D .   ? 0.40597 0.42002 0.33771 -0.02896 -0.02254 -0.02566 420 HOH A O   
2167 O O   . HOH D .   ? 0.27972 0.33053 0.25616 -0.01582 0.01096  -0.02801 421 HOH A O   
2168 O O   . HOH D .   ? 0.47423 0.55807 0.82005 0.03333  0.11716  0.09219  422 HOH A O   
2169 O O   . HOH D .   ? 0.76286 0.57632 0.46978 0.07405  0.19793  0.07267  423 HOH A O   
2170 O O   . HOH D .   ? 0.44300 0.57083 0.36456 -0.06128 -0.06789 0.02140  424 HOH A O   
2171 O O   . HOH D .   ? 0.58439 0.59017 0.30969 -0.07283 0.04817  -0.01711 425 HOH A O   
2172 O O   . HOH D .   ? 0.37800 0.55984 0.31306 -0.04672 -0.00976 0.00205  426 HOH A O   
2173 O O   . HOH D .   ? 0.45018 0.61495 0.43264 0.12851  0.09172  0.17690  427 HOH A O   
2174 O O   . HOH D .   ? 0.63965 0.55787 0.35764 -0.02324 0.06870  -0.08140 428 HOH A O   
2175 O O   . HOH D .   ? 0.87297 0.60247 0.62760 -0.15838 0.15444  0.20912  429 HOH A O   
2176 O O   . HOH D .   ? 0.33415 0.44761 0.24881 0.02351  -0.02876 -0.05345 430 HOH A O   
2177 O O   . HOH D .   ? 0.26480 0.47344 0.69456 -0.02538 0.10192  -0.19789 431 HOH A O   
2178 O O   . HOH D .   ? 0.23240 0.44823 0.87878 -0.01099 0.05545  0.01727  432 HOH A O   
2179 O O   . HOH D .   ? 0.25633 0.42759 0.16949 -0.05066 -0.01760 -0.01414 433 HOH A O   
2180 O O   . HOH D .   ? 0.42106 0.59488 1.17011 0.03353  -0.17525 -0.00245 434 HOH A O   
2181 O O   . HOH D .   ? 0.65224 0.81217 0.82991 0.34661  0.27730  0.09018  435 HOH A O   
2182 O O   . HOH D .   ? 0.34057 0.85131 0.32787 0.18216  0.07076  0.18365  436 HOH A O   
2183 O O   . HOH D .   ? 0.34671 0.79450 0.41228 0.09162  0.09255  -0.17455 437 HOH A O   
2184 O O   . HOH D .   ? 0.69965 0.51949 1.03453 0.12173  -0.00941 -0.08134 438 HOH A O   
2185 O O   . HOH D .   ? 0.41701 0.46840 0.30721 -0.11523 -0.09680 0.07382  439 HOH A O   
2186 O O   . HOH D .   ? 0.48613 0.57645 0.28865 -0.18751 0.04400  0.01439  440 HOH A O   
2187 O O   . HOH D .   ? 0.22416 0.39912 0.26382 -0.01852 -0.00081 0.02502  441 HOH A O   
2188 O O   . HOH D .   ? 0.54004 0.50663 0.29762 -0.04510 -0.04043 -0.02170 442 HOH A O   
2189 O O   . HOH D .   ? 0.73910 0.69340 0.47744 0.07408  0.18177  -0.16959 443 HOH A O   
2190 O O   . HOH D .   ? 0.66353 0.65460 0.51870 0.09293  0.18093  0.12924  444 HOH A O   
2191 O O   . HOH D .   ? 0.52317 0.89265 0.38412 -0.03603 0.17060  -0.06568 445 HOH A O   
2192 O O   . HOH D .   ? 0.63790 0.99539 0.81294 0.16297  -0.18090 -0.04137 446 HOH A O   
2193 O O   . HOH D .   ? 0.76342 0.53327 0.41040 0.03323  -0.03498 0.00948  447 HOH A O   
2194 O O   . HOH D .   ? 0.93750 0.54280 0.66560 -0.00659 -0.07986 -0.02388 448 HOH A O   
2195 O O   . HOH D .   ? 0.37977 0.40326 0.58366 -0.00175 -0.08904 0.01955  449 HOH A O   
2196 O O   . HOH D .   ? 0.63675 0.64263 0.74927 -0.09707 0.20386  -0.10977 450 HOH A O   
2197 O O   . HOH D .   ? 0.26635 0.62667 0.34528 -0.06154 -0.01207 0.00439  451 HOH A O   
2198 O O   . HOH D .   ? 0.44574 0.62968 0.38809 0.00208  -0.01207 -0.01096 452 HOH A O   
2199 O O   . HOH D .   ? 0.63082 0.58002 0.46765 0.24264  0.19237  0.03462  453 HOH A O   
2200 O O   . HOH D .   ? 0.71084 1.03267 0.88931 0.12096  0.41278  -0.06093 454 HOH A O   
2201 O O   . HOH D .   ? 0.79121 0.76384 0.53380 -0.16743 0.00930  -0.09519 455 HOH A O   
2202 O O   . HOH D .   ? 0.47158 0.70891 0.74996 0.00603  -0.10041 -0.09422 456 HOH A O   
2203 O O   . HOH D .   ? 0.58479 0.54164 0.67624 -0.19052 -0.03160 -0.15305 457 HOH A O   
2204 O O   . HOH D .   ? 0.29189 0.64077 0.59791 0.03366  0.01614  -0.14251 458 HOH A O   
2205 O O   . HOH D .   ? 0.26566 0.70592 0.37941 0.03993  -0.03380 -0.03267 459 HOH A O   
2206 O O   . HOH D .   ? 0.29213 0.43209 0.29178 -0.02924 -0.02244 -0.02797 460 HOH A O   
2207 O O   . HOH D .   ? 0.82089 0.66437 0.70460 0.06675  0.32847  0.01174  461 HOH A O   
2208 O O   . HOH D .   ? 0.49254 0.47754 0.51426 0.04903  -0.21493 -0.06448 462 HOH A O   
2209 O O   . HOH D .   ? 0.50064 0.57185 0.57223 -0.07408 -0.02086 0.11538  463 HOH A O   
2210 O O   . HOH D .   ? 0.45368 0.36416 1.22468 -0.02867 -0.19848 -0.08528 464 HOH A O   
2211 O O   . HOH D .   ? 0.97247 0.60878 0.86122 0.19127  0.14675  0.11917  465 HOH A O   
2212 O O   . HOH D .   ? 1.09247 0.62132 0.77476 -0.15754 -0.02134 0.23099  466 HOH A O   
2213 O O   . HOH D .   ? 0.71428 0.84522 0.75961 -0.03708 0.10649  0.31954  467 HOH A O   
2214 O O   . HOH D .   ? 0.63342 0.71403 0.48349 -0.05057 -0.06977 -0.08840 468 HOH A O   
2215 O O   . HOH D .   ? 0.31422 0.43003 0.92142 -0.04228 0.10697  -0.17442 469 HOH A O   
2216 O O   . HOH D .   ? 0.50065 0.58666 0.93503 0.12889  0.17992  0.20826  470 HOH A O   
2217 O O   . HOH D .   ? 0.47555 0.69089 0.39994 -0.03939 0.18133  -0.18113 471 HOH A O   
2218 O O   . HOH D .   ? 0.38219 0.43307 0.38386 0.09029  0.06202  0.12811  472 HOH A O   
2219 O O   . HOH D .   ? 0.65771 0.62077 0.82221 0.18204  -0.19537 0.05708  473 HOH A O   
2220 O O   . HOH D .   ? 0.53798 0.57231 0.71606 -0.09391 -0.15479 -0.11965 474 HOH A O   
2221 O O   . HOH D .   ? 0.83475 0.71100 0.55520 0.10696  -0.12811 -0.18401 475 HOH A O   
2222 O O   . HOH D .   ? 0.60314 0.87672 0.60634 0.26330  0.17775  0.13143  476 HOH A O   
2223 O O   . HOH D .   ? 0.43308 0.73781 0.39706 0.01413  -0.05605 0.02735  477 HOH A O   
2224 O O   . HOH D .   ? 0.41127 0.59679 0.48427 0.10049  0.08245  0.03455  478 HOH A O   
2225 O O   . HOH D .   ? 0.59237 0.70181 0.61473 -0.08286 -0.19794 -0.02658 479 HOH A O   
2226 O O   . HOH D .   ? 0.56902 0.83345 0.63882 -0.17870 0.02085  -0.03722 480 HOH A O   
2227 O O   . HOH D .   ? 0.56047 0.63563 0.53442 0.13229  0.10127  0.02360  481 HOH A O   
2228 O O   . HOH D .   ? 0.75859 0.82274 0.89862 0.22806  0.06545  0.18034  482 HOH A O   
2229 O O   . HOH D .   ? 0.69119 0.72774 0.39437 0.19399  -0.05809 0.03305  483 HOH A O   
2230 O O   . HOH D .   ? 0.56128 0.50080 0.86601 0.22250  0.29294  0.27974  484 HOH A O   
2231 O O   . HOH D .   ? 0.85835 0.69077 0.68217 0.23813  -0.15560 -0.01715 485 HOH A O   
# 
